Entry
stringlengths 6
10
| Entry Name
stringlengths 5
11
| Sequence
stringlengths 2
35.2k
| EC number
stringlengths 7
118
⌀ | Cofactor
stringlengths 38
1.77k
⌀ | Gene Ontology (biological process)
stringlengths 18
11.3k
⌀ | Gene Ontology (cellular component)
stringlengths 17
1.75k
⌀ | Gene Ontology (molecular function)
stringlengths 24
2.09k
⌀ | Pfam
stringlengths 8
232
⌀ | Gene3D
stringlengths 10
250
⌀ | Protein families
stringlengths 9
237
⌀ | Post-translational modification
stringlengths 16
8.52k
⌀ | Subcellular location [CC]
stringlengths 29
6.18k
⌀ | Catalytic activity
stringlengths 64
35.7k
⌀ | Kinetics
stringlengths 69
11.7k
⌀ | Pathway
stringlengths 27
908
⌀ | pH dependence
stringlengths 64
955
⌀ | Temperature dependence
stringlengths 70
1.16k
⌀ | Function [CC]
stringlengths 17
15.3k
⌀ | Organism
stringlengths 8
196
|
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
O15033
|
AREL1_HUMAN
|
MFYVIGGITVSVVAFFFTIKFLFELAARVVSFLQNEDRERRGDRTIYDYVRGNYLDPRSCKVSWDWKDPYEVGHSMAFRVHLFYKNGQPFPAHRPVGLRVHISHVELAVEIPVTQEVLQEPNSNVVKVAFTVRKAGRYEITVKLGGLNVAYSPYYKIFQPGMVVPSKTKIVCHFSTLVLTCGQPHTLQIVPRDEYDNPTNNSMSLRDEHNYTLSIHELGPQEEESTGVSFEKSVTSNRQTFQVFLRLTLHSRGCFHACISYQNQPINNGEFDIIVLSEDEKNIVERNVSTSGVSIYFEAYLYNATNCSSTPWHLPPMHMTSSQRRPSTAVDEEDEDSPSECHTPEKVKKPKKVYCYVSPKQFSVKEFYLKIIPWRLYTFRVCPGTKFSYLGPDPVHKLLTLVVDDGIQPPVELSCKERNILAATFIRSLHKNIGGSETFQDKVNFFQRELRQVHMKRPHSKVTLKVSRHALLESSLKATRNFSISDWSKNFEVVFQDEEALDWGGPRREWFELICKALFDTTNQLFTRFSDNNQALVHPNPNRPAHLRLKMYEFAGRLVGKCLYESSLGGAYKQLVRARFTRSFLAQIIGLRMHYKYFETDDPEFYKSKVCFILNNDMSEMELVFAEEKYNKSGQLDKVVELMTGGAQTPVTNANKIFYLNLLAQYRLASQVKEEVEHFLKGLNELVPENLLAIFDENELELLMCGTGDISVSDFKAHAVVVGGSWHFREKVMRWFWTVVSSLTQEELARLLQFTTGSSQLPPGGFAALCPSFQIIAAPTHSTLPTAHTCFNQLCLPTYDSYEEVHRMLQLAISEGCEGFGML
|
2.3.2.26
| null |
apoptotic process [GO:0006915]; negative regulation of apoptotic process [GO:0043066]; protein K11-linked ubiquitination [GO:0070979]; protein K33-linked ubiquitination [GO:1990390]; protein polyubiquitination [GO:0000209]; protein ubiquitination [GO:0016567]; regulation of inflammatory response [GO:0050727]; ubiquitin-dependent protein catabolic process [GO:0006511]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]
|
ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]
|
PF00630;PF00632;
|
3.30.2160.10;3.30.2410.10;3.90.1750.10;2.60.40.10;
| null |
PTM: Autoubiquitinated in vitro in the presence of E2 enzyme UBE2D1/UBCH5A. {ECO:0000269|PubMed:23479728}.
| null |
CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.26; Evidence={ECO:0000269|PubMed:23479728, ECO:0000269|PubMed:25752577};
| null |
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:23479728, ECO:0000269|PubMed:25752577}.
| null | null |
FUNCTION: E3 ubiquitin-protein ligase that catalyzes 'Lys-11'- or 'Lys-33'-linked polyubiquitin chains, with some preference for 'Lys-33' linkages (PubMed:25752577). E3 ubiquitin-protein ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates (PubMed:23479728, PubMed:31578312). Ubiquitinates SEPTIN4, DIABLO/SMAC and HTRA2 in vitro (PubMed:23479728). Modulates pulmonary inflammation by targeting SOCS2 for ubiquitination and subsequent degradation by the proteasome (PubMed:31578312). {ECO:0000269|PubMed:23479728, ECO:0000269|PubMed:25752577, ECO:0000269|PubMed:31578312}.
|
Homo sapiens (Human)
|
O15040
|
TCPR2_HUMAN
|
MASISEPVTFREFCPLYYLLNAIPTKIQKGFRSIVVYLTALDTNGDYIAVGSSIGMLYLYCRHLNQMRKYNFEGKTESITVVKLLSCFDDLVAAGTASGRVAVFQLVSSLPGRNKQLRRFDVTGIHKNSITALAWSPNGMKLFSGDDKGKIVYSSLDLDQGLCNSQLVLEEPSSIVQLDYSQKVLLVSTLQRSLLFYTEEKSVRQIGTQPRKSTGKFGACFIPGLCKQSDLTLYASRPGLRLWKADVHGTVQATFILKDAFAGGVKPFELHPRLESPNSGSCSLPERHLGLVSCFFQEGWVLSWNEYSIYLLDTVNQATVAGLEGSGDIVSVSCTENEIFFLKGDRNIIRISSRPEGLTSTVRDGLEMSGCSERVHVQQAEKLPGATVSETRLRGSSMASSVASEPRSRSSSLNSTDSGSGLLPPGLQATPELGKGSQPLSQRFNAISSEDFDQELVVKPIKVKRKKKKKKTEGGSRSTCHSSLESTPCSEFPGDSPQSLNTDLLSMTSSVLGSSVDQLSAESPDQESSFNGEVNGVPQENTDPETFNVLEVSGSMPDSLAEEDDIRTEMPHCHHAHGRELLNGAREDVGGSDVTGLGDEPCPADDGPNSTQLPFQEQDSSPGAHDGEDIQPIGPQSTFCEVPLLNSLTVPSSLSWAPSAEQWLPGTRADEGSPVEPSQEQDILTSMEASGHLSTNLWHAVTDDDTGQKEIPISERVLGSVGGQLTPVSALAASTHKPWLEQPPRDQTLTSSDEEDIYAHGLPSSSSETSVTELGPSCSQQDLSRLGAEDAGLLKPDQFAESWMGYSGPGYGILSLVVSEKYIWCLDYKGGLFCSALPGAGLRWQKFEDAVQQVAVSPSGALLWKIEQKSNRAFACGKVTIKGKRHWYEALPQAVFVALSDDTAWIIRTSGDLYLQTGLSVDRPCARAVKVDCPYPLSQITARNNVVWALTEQRALLYREGVSSFCPEGEQWKCDIVSERQALEPVCITLGDQQTLWALDIHGNLWFRTGIISKKPQGDDDHWWQVSITDYVVFDQCSLFQTIIHATHSVATAAQAPVEKVADKLRMAFWSQQLQCQPSLLGVNNSGVWISSGKNEFHVAKGSLIGTYWNHVVPRGTASATKWAFVLASAAPTKEGSFLWLCQSSKDLCSVSAQSAQSRPSTVQLPPEAEMRAYAACQDALWALDSLGQVFIRTLSKSCPTGMHWTRLDLSQLGAVKLTSLACGNQHIWACDSRGGVYFRVGTQPLNPSLMLPAWIMIEPPVQPAGVSLVSVHSSPNDQMLWVLDSRWNVHVRTGITEEMPVGTAWEHVPGLQACQLALSTRTVWARCPNGDLARRYGVTDKNPAGDYWKKIPGSVSCFTVTASDELWAVGPPGYLLQRLTKTFSHSHGTQKSSQAAMPHPEDLEDEWEVI
| null | null |
autophagy [GO:0006914]; protein exit from endoplasmic reticulum [GO:0032527]
|
cytoplasm [GO:0005737]
| null |
PF06462;PF19193;
|
2.130.10.10;
|
WD repeat KIAA0329 family
| null | null | null | null | null | null | null |
FUNCTION: Probably plays a role as positive regulator of autophagy. {ECO:0000269|PubMed:23176824}.
|
Homo sapiens (Human)
|
O15041
|
SEM3E_HUMAN
|
MASAGHIITLLLWGYLLELWTGGHTADTTHPRLRLSHKELLNLNRTSIFHSPFGFLDLHTMLLDEYQERLFVGGRDLVYSLSLERISDGYKEIHWPSTALKMEECIMKGKDAGECANYVRVLHHYNRTHLLTCGTGAFDPVCAFIRVGYHLEDPLFHLESPRSERGRGRCPFDPSSSFISTLIGSELFAGLYSDYWSRDAAIFRSMGRLAHIRTEHDDERLLKEPKFVGSYMIPDNEDRDDNKVYFFFTEKALEAENNAHAIYTRVGRLCVNDVGGQRILVNKWSTFLKARLVCSVPGMNGIDTYFDELEDVFLLPTRDHKNPVIFGLFNTTSNIFRGHAICVYHMSSIRAAFNGPYAHKEGPEYHWSVYEGKVPYPRPGSCASKVNGGRYGTTKDYPDDAIRFARSHPLMYQAIKPAHKKPILVKTDGKYNLKQIAVDRVEAEDGQYDVLFIGTDNGIVLKVITIYNQEMESMEEVILEELQIFKDPVPIISMEISSKRQQLYIGSASAVAQVRFHHCDMYGSACADCCLARDPYCAWDGISCSRYYPTGTHAKRRFRRQDVRHGNAAQQCFGQQFVGDALDKTEEHLAYGIENNSTLLECTPRSLQAKVIWFVQKGRETRKEEVKTDDRVVKMDLGLLFLRLHKSDAGTYFCQTVEHSFVHTVRKITLEVVEEEKVEDMFNKDDEEDRHHRMPCPAQSSISQGAKPWYKEFLQLIGYSNFQRVEEYCEKVWCTDRKRKKLKMSPSKWKYANPQEKKLRSKPEHYRLPRHTLDS
| null | null |
axon guidance [GO:0007411]; branching involved in blood vessel morphogenesis [GO:0001569]; gonadotrophin-releasing hormone neuronal migration to the hypothalamus [GO:0021828]; negative chemotaxis [GO:0050919]; negative regulation of angiogenesis [GO:0016525]; negative regulation of axon extension involved in axon guidance [GO:0048843]; negative regulation of cell-matrix adhesion [GO:0001953]; negative regulation of neuron apoptotic process [GO:0043524]; neural crest cell migration [GO:0001755]; positive regulation of cell migration [GO:0030335]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; regulation of cell shape [GO:0008360]; semaphorin-plexin signaling pathway [GO:0071526]; sprouting angiogenesis [GO:0002040]; synapse organization [GO:0050808]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]
|
chemorepellent activity [GO:0045499]; receptor ligand activity [GO:0048018]; semaphorin receptor binding [GO:0030215]
|
PF00047;PF01403;
|
2.60.40.10;3.30.1680.10;2.130.10.10;
|
Semaphorin family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Plays an important role in signaling via the cell surface receptor PLXND1. Mediates reorganization of the actin cytoskeleton, leading to the retraction of cell projections. Promotes focal adhesion disassembly and inhibits adhesion of endothelial cells to the extracellular matrix. Regulates angiogenesis, both during embryogenesis and after birth. Can down-regulate sprouting angiogenesis. Required for normal vascular patterning during embryogenesis. Plays an important role in ensuring the specificity of synapse formation (By similarity). {ECO:0000250}.
|
Homo sapiens (Human)
|
O15042
|
SR140_HUMAN
|
MADKTPGGSQKASSKTRSSDVHSSGSSDAHMDASGPSDSDMPSRTRPKSPRKHNYRNESARESLCDSPHQNLSRPLLENKLKAFSIGKMSTAKRTLSKKEQEELKKKEDEKAAAEIYEEFLAAFEGSDGNKVKTFVRGGVVNAAKEEHETDEKRGKIYKPSSRFADQKNPPNQSSNERPPSLLVIETKKPPLKKGEKEKKKSNLELFKEELKQIQEERDERHKTKGRLSRFEPPQSDSDGQRRSMDAPSRRNRSSGVLDDYAPGSHDVGDPSTTNLYLGNINPQMNEEMLCQEFGRFGPLASVKIMWPRTDEERARERNCGFVAFMNRRDAERALKNLNGKMIMSFEMKLGWGKAVPIPPHPIYIPPSMMEHTLPPPPSGLPFNAQPRERLKNPNAPMLPPPKNKEDFEKTLSQAIVKVVIPTERNLLALIHRMIEFVVREGPMFEAMIMNREINNPMFRFLFENQTPAHVYYRWKLYSILQGDSPTKWRTEDFRMFKNGSFWRPPPLNPYLHGMSEEQETEAFVEEPSKKGALKEEQRDKLEEILRGLTPRKNDIGDAMVFCLNNAEAAEEIVDCITESLSILKTPLPKKIARLYLVSDVLYNSSAKVANASYYRKFFETKLCQIFSDLNATYRTIQGHLQSENFKQRVMTCFRAWEDWAIYPEPFLIKLQNIFLGLVNIIEEKETEDVPDDLDGAPIEEELDGAPLEDVDGIPIDATPIDDLDGVPIKSLDDDLDGVPLDATEDSKKNEPIFKVAPSKWEAVDESELEAQAVTTSKWELFDQHEESEEEENQNQEEESEDEEDTQSSKSEEHHLYSNPIKEEMTESKFSKYSEMSEEKRAKLREIELKVMKFQDELESGKRPKKPGQSFQEQVEHYRDKLLQREKEKELERERERDKKDKEKLESRSKDKKEKDECTPTRKERKRRHSTSPSPSRSSSGRRVKSPSPKSERSERSERSHKESSRSRSSHKDSPRDVSKKAKRSPSGSRTPKRSRRSRSRSPKKSGKKSRSQSRSPHRSHKKSKKNKH
| null | null |
RNA processing [GO:0006396]
|
nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
RNA binding [GO:0003723]
|
PF04818;PF08312;PF00076;PF01805;
|
1.25.40.90;3.30.70.330;6.10.140.420;1.10.10.790;
|
Splicing factor SR family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20858735}.
| null | null | null | null | null | null |
Homo sapiens (Human)
|
O15047
|
SET1A_HUMAN
|
MDQEGGGDGQKAPSFQWRNYKLIVDPALDPALRRPSQKVYRYDGVHFSVNDSKYIPVEDLQDPRCHVRSKNRDFSLPVPKFKLDEFYIGQIPLKEVTFARLNDNVRETFLKDMCRKYGEVEEVEILLHPRTRKHLGLARVLFTSTRGAKETVKNLHLTSVMGNIIHAQLDIKGQQRMKYYELIVNGSYTPQTVPTGGKALSEKFQGSGAATETAESRRRSSSDTAAYPAGTTAVGTPGNGTPCSQDTSFSSSRQDTPSSFGQFTPQSSQGTPYTSRGSTPYSQDSAYSSSTTSTSFKPRRSENSYQDAFSRRHFSASSASTTASTAIAATTAATASSSASSSSLSSSSSSSSSSSSSQFRSSDANYPAYYESWNRYQRHTSYPPRRATREEPPGAPFAENTAERFPPSYTSYLPPEPSRPTDQDYRPPASEAPPPEPPEPGGGGGGGGPSPEREEVRTSPRPASPARSGSPAPETTNESVPFAQHSSLDSRIEMLLKEQRSKFSFLASDTEEEEENSSMVLGARDTGSEVPSGSGHGPCTPPPAPANFEDVAPTGSGEPGATRESPKANGQNQASPCSSGDDMEISDDDRGGSPPPAPTPPQQPPPPPPPPPPPPPYLASLPLGYPPHQPAYLLPPRPDGPPPPEYPPPPPPPPHIYDFVNSLELMDRLGAQWGGMPMSFQMQTQMLTRLHQLRQGKGLIAASAGPPGGAFGEAFLPFPPPQEAAYGLPYALYAQGQEGRGAYSREAYHLPMPMAAEPLPSSSVSGEEARLPPREEAELAEGKTLPTAGTVGRVLAMLVQEMKSIMQRDLNRKMVENVAFGAFDQWWESKEEKAKPFQNAAKQQAKEEDKEKTKLKEPGLLSLVDWAKSGGTTGIEAFAFGSGLRGALRLPSFKVKRKEPSEISEASEEKRPRPSTPAEEDEDDPEQEKEAGEPGRPGTKPPKRDEERGKTQGKHRKSFALDSEGEEASQESSSEKDEEDDEEDEEDEDREEAVDTTKKETEVSDGEDEESDSSSKCSLYADSDGENDSTSDSESSSSSSSSSSSSSSSSSSSSSSSSESSSEDEEEEERPAALPSASPPPREVPVPTPAPVEVPVPERVAGSPVTPLPEQEASPARPAGPTEESPPSAPLRPPEPPAGPPAPAPRPDERPSSPIPLLPPPKKRRKTVSFSAIEVVPAPEPPPATPPQAKFPGPASRKAPRGVERTIRNLPLDHASLVKSWPEEVSRGGRSRAGGRGRLTEEEEAEPGTEVDLAVLADLALTPARRGLPALPAVEDSEATETSDEAERPRPLLSHILLEHNYALAVKPTPPAPALRPPEPVPAPAALFSSPADEVLEAPEVVVAEAEEPKPQQLQQQREEGEEEGEEEGEEEEEESSDSSSSSDGEGALRRRSLRSHARRRRPPPPPPPPPPRAYEPRSEFEQMTILYDIWNSGLDSEDMSYLRLTYERLLQQTSGADWLNDTHWVHHTITNLTTPKRKRRPQDGPREHQTGSARSEGYYPISKKEKDKYLDVCPVSARQLEGVDTQGTNRVLSERRSEQRRLLSAIGTSAIMDSDLLKLNQLKFRKKKLRFGRSRIHEWGLFAMEPIAADEMVIEYVGQNIRQMVADMREKRYVQEGIGSSYLFRVDHDTIIDATKCGNLARFINHCCTPNCYAKVITIESQKKIVIYSKQPIGVDEEITYDYKFPLEDNKIPCLCGTESCRGSLN
|
2.1.1.364
| null |
brain development [GO:0007420]; DNA damage response [GO:0006974]; methylation [GO:0032259]; regulation of chromatin organization [GO:1902275]; regulation of hematopoietic stem cell differentiation [GO:1902036]
|
chromatin [GO:0000785]; cytoplasm [GO:0005737]; histone methyltransferase complex [GO:0035097]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; Set1C/COMPASS complex [GO:0048188]
|
beta-catenin binding [GO:0008013]; histone H3K4 methyltransferase activity [GO:0042800]; histone H3K4 monomethyltransferase activity [GO:0140945]; histone H3K4 trimethyltransferase activity [GO:0140999]; RNA binding [GO:0003723]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]
|
PF11764;PF00076;PF00856;
|
3.30.70.330;2.170.270.10;
|
Class V-like SAM-binding methyltransferase superfamily
| null |
SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:17355966, ECO:0000269|PubMed:38003223}. Chromosome {ECO:0000269|PubMed:17355966}. Cytoplasm {ECO:0000269|PubMed:38003223}. Note=Localizes to a largely non-overlapping set of euchromatic nuclear speckles with SETD1B, suggesting that SETD1A and SETD1B each bind to a unique set of target genes (PubMed:17355966). Predominantly nuclear (PubMed:38003223). {ECO:0000269|PubMed:17355966, ECO:0000269|PubMed:38003223}.
|
CATALYTIC ACTIVITY: Reaction=L-lysyl(4)-[histone H3] + S-adenosyl-L-methionine = H(+) + N(6)-methyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60264, Rhea:RHEA-COMP:15543, Rhea:RHEA-COMP:15547, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.364; Evidence={ECO:0000269|PubMed:25561738, ECO:0000269|PubMed:29937342}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60265; Evidence={ECO:0000269|PubMed:25561738, ECO:0000269|PubMed:29937342}; CATALYTIC ACTIVITY: Reaction=N(6)-methyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-methionine = H(+) + N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60268, Rhea:RHEA-COMP:15540, Rhea:RHEA-COMP:15543, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61929, ChEBI:CHEBI:61976; Evidence={ECO:0000269|PubMed:25561738}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60269; Evidence={ECO:0000269|PubMed:25561738}; CATALYTIC ACTIVITY: Reaction=N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-methionine = H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60272, Rhea:RHEA-COMP:15537, Rhea:RHEA-COMP:15540, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961, ChEBI:CHEBI:61976; Evidence={ECO:0000269|PubMed:25561738}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60273; Evidence={ECO:0000269|PubMed:25561738};
| null | null | null | null |
FUNCTION: Histone methyltransferase that catalyzes methyl group transfer from S-adenosyl-L-methionine to the epsilon-amino group of 'Lys-4' of histone H3 (H3K4) via a non-processive mechanism (PubMed:12670868, PubMed:25561738). Part of chromatin remodeling machinery, forms H3K4me1, H3K4me2 and H3K4me3 methylation marks at active chromatin sites where transcription and DNA repair take place (PubMed:29937342, PubMed:31197650, PubMed:32346159). Responsible for H3K4me3 enriched promoters and transcriptional programming of inner mass stem cells and neuron progenitors during embryogenesis (By similarity) (PubMed:31197650). Required for H3K4me1 mark at stalled replication forks. Mediates FANCD2-dependent nucleosome remodeling and RAD51 nucleofilaments stabilization at reversed forks, protecting them from nucleolytic degradation (PubMed:29937342, PubMed:32346159). Does not methylate 'Lys-4' of histone H3 if the neighboring 'Lys-9' residue is already methylated (PubMed:12670868). Binds RNAs involved in RNA processing and the DNA damage response (PubMed:38003223). {ECO:0000250|UniProtKB:E9PYH6, ECO:0000269|PubMed:12670868, ECO:0000269|PubMed:25561738, ECO:0000269|PubMed:29937342, ECO:0000269|PubMed:31197650, ECO:0000269|PubMed:32346159, ECO:0000269|PubMed:38003223}.
|
Homo sapiens (Human)
|
O15049
|
N4BP3_HUMAN
|
MATAPGPAGIAMGSVGSLLERQDFSPEELRAALAGSRGSRQPDGLLRKGLGQREFLSYLHLPKKDSKSTKNTKRAPRNEPADYATLYYREHSRAGDFSKTSLPERGRFDKCRIRPSVFKPTAGNGKGFLSMQSLASHKGQKLWRSNGSLHTLACHPPLSPGPRASQARAQLLHALSLDEGGPEPEPSLSDSSSGGSFGRSPGTGPSPFSSSLGHLNHLGGSLDRASQGPKEAGPPAVLSCLPEPPPPYEFSCSSAEEMGAVLPETCEELKRGLGDEDGSNPFTQVLEERQRLWLAELKRLYVERLHEVTQKAERSERNLQLQLFMAQQEQRRLRKELRAQQGLAPEPRAPGTLPEADPSARPEEEARWEVCQKTAEISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELVRLREAVRSLQEQAPREEAPGSCETDDCKSRGLLGEAGGSEARDSAEQLRAELLQERLRGQEQALRFEQERRTWQEEKERVLRYQREIQGGYMDMYRRNQALEQELRALREPPTPWSPRLESSKI
| null | null |
innate immune response [GO:0045087]; nervous system development [GO:0007399]
|
axon [GO:0030424]; cytoplasmic vesicle [GO:0031410]; dendrite [GO:0030425]
| null |
PF06818;
| null |
N4BP3 family
| null |
SUBCELLULAR LOCATION: Cytoplasmic vesicle {ECO:0000269|PubMed:11717310}. Cell projection, axon {ECO:0000250|UniProtKB:Q3LUD3}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q3LUD3}. Note=In developing neurons, accumulates in early growth cones and at branching points of axons and dendrites. {ECO:0000250|UniProtKB:Q3LUD3}.
| null | null | null | null | null |
FUNCTION: Plays a positive role in the antiviral innate immune signaling pathway. Mechanistically, interacts with MAVS and functions as a positive regulator to promote 'Lys-63'-linked polyubiquitination of MAVS and thus strengthens the interaction between MAVS and TRAF2 (PubMed:34880843). Also plays a role in axon and dendrite arborization during cranial nerve development. May also be important for neural crest migration and early development of other anterior structures including eye, brain and cranial cartilage (By similarity). {ECO:0000250|UniProtKB:A0A1L8GXY6, ECO:0000269|PubMed:34880843}.
|
Homo sapiens (Human)
|
O15054
|
KDM6B_HUMAN
|
MHRAVDPPGARAAREAFALGGLSCAGAWSSCPPHPPPRSAWLPGGRCSASIGQPPLPAPLPPSHGSSSGHPSKPYYAPGAPTPRPLHGKLESLHGCVQALLREPAQPGLWEQLGQLYESEHDSEEATRCYHSALRYGGSFAELGPRIGRLQQAQLWNFHTGSCQHRAKVLPPLEQVWNLLHLEHKRNYGAKRGGPPVKRAAEPPVVQPVPPAALSGPSGEEGLSPGGKRRRGCNSEQTGLPPGLPLPPPPLPPPPPPPPPPPPPLPGLATSPPFQLTKPGLWSTLHGDAWGPERKGSAPPERQEQRHSLPHPYPYPAPAYTAHPPGHRLVPAAPPGPGPRPPGAESHGCLPATRPPGSDLRESRVQRSRMDSSVSPAATTACVPYAPSRPPGLPGTTTSSSSSSSSNTGLRGVEPNPGIPGADHYQTPALEVSHHGRLGPSAHSSRKPFLGAPAATPHLSLPPGPSSPPPPPCPRLLRPPPPPAWLKGPACRAAREDGEILEELFFGTEGPPRPAPPPLPHREGFLGPPASRFSVGTQDSHTPPTPPTPTTSSSNSNSGSHSSSPAGPVSFPPPPYLARSIDPLPRPPSPAQNPQDPPLVPLTLALPPAPPSSCHQNTSGSFRRPESPRPRVSFPKTPEVGPGPPPGPLSKAPQPVPPGVGELPARGPRLFDFPPTPLEDQFEEPAEFKILPDGLANIMKMLDESIRKEEEQQQHEAGVAPQPPLKEPFASLQSPFPTDTAPTTTAPAVAVTTTTTTTTTTTATQEEEKKPPPALPPPPPLAKFPPPSQPQPPPPPPPSPASLLKSLASVLEGQKYCYRGTGAAVSTRPGPLPTTQYSPGPPSGATALPPTSAAPSAQGSPQPSASSSSQFSTSGGPWARERRAGEEPVPGPMTPTQPPPPLSLPPARSESEVLEEISRACETLVERVGRSATDPADPVDTAEPADSGTERLLPPAQAKEEAGGVAAVSGSCKRRQKEHQKEHRRHRRACKDSVGRRPREGRAKAKAKVPKEKSRRVLGNLDLQSEEIQGREKSRPDLGGASKAKPPTAPAPPSAPAPSAQPTPPSASVPGKKAREEAPGPPGVSRADMLKLRSLSEGPPKELKIRLIKVESGDKETFIASEVEERRLRMADLTISHCAADVVRASRNAKVKGKFRESYLSPAQSVKPKINTEEKLPREKLNPPTPSIYLESKRDAFSPVLLQFCTDPRNPITVIRGLAGSLRLNLGLFSTKTLVEASGEHTVEVRTQVQQPSDENWDLTGTRQIWPCESSRSHTTIAKYAQYQASSFQESLQEEKESEDEESEEPDSTTGTPPSSAPDPKNHHIIKFGTNIDLSDAKRWKPQLQELLKLPAFMRVTSTGNMLSHVGHTILGMNTVQLYMKVPGSRTPGHQENNNFCSVNINIGPGDCEWFAVHEHYWETISAFCDRHGVDYLTGSWWPILDDLYASNIPVYRFVQRPGDLVWINAGTVHWVQATGWCNNIAWNVGPLTAYQYQLALERYEWNEVKNVKSIVPMIHVSWNVARTVKISDPDLFKMIKFCLLQSMKHCQVQRESLVRAGKKIAYQGRVKDEPAYYCNECDVEVFNILFVTSENGSRNTYLVHCEGCARRRSAGLQGVVVLEQYRTEELAQAYDAFTLAPASTSR
|
1.14.11.68
|
COFACTOR: Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000250}; COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:17825402};
|
cardiac muscle cell differentiation [GO:0055007]; cell fate commitment [GO:0045165]; cellular response to hydrogen peroxide [GO:0070301]; chromatin remodeling [GO:0006338]; endothelial cell differentiation [GO:0045446]; hippocampus development [GO:0021766]; inflammatory response to antigenic stimulus [GO:0002437]; mesodermal cell differentiation [GO:0048333]; positive regulation of cold-induced thermogenesis [GO:0120162]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of gene expression [GO:0010468]; response to activity [GO:0014823]; response to fungicide [GO:0060992]
|
MLL3/4 complex [GO:0044666]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
beta-catenin binding [GO:0008013]; chromatin DNA binding [GO:0031490]; histone demethylase activity [GO:0032452]; histone H3K27me2/H3K27me3 demethylase activity [GO:0071558]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF02373;PF21322;PF21326;
|
1.20.58.1370;2.10.110.20;2.60.120.650;
|
UTX family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:17825402}.
|
CATALYTIC ACTIVITY: Reaction=2 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(27)-[histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + N(6)-methyl-L-lysyl(27)-[histone H3] + 2 succinate; Xref=Rhea:RHEA:60224, Rhea:RHEA-COMP:15535, Rhea:RHEA-COMP:15544, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:61929, ChEBI:CHEBI:61961; EC=1.14.11.68; Evidence={ECO:0000269|PubMed:17713478, ECO:0000269|PubMed:17825402, ECO:0000269|PubMed:17851529, ECO:0000269|PubMed:18003914};
| null | null | null | null |
FUNCTION: Histone demethylase that specifically demethylates 'Lys-27' of histone H3, thereby playing a central role in histone code (PubMed:17713478, PubMed:17825402, PubMed:17851529, PubMed:18003914). Demethylates trimethylated and dimethylated H3 'Lys-27' (PubMed:17713478, PubMed:17825402, PubMed:17851529, PubMed:18003914). Plays a central role in regulation of posterior development, by regulating HOX gene expression (PubMed:17851529). Involved in inflammatory response by participating in macrophage differentiation in case of inflammation by regulating gene expression and macrophage differentiation (PubMed:17825402). Plays a demethylase-independent role in chromatin remodeling to regulate T-box family member-dependent gene expression by acting as a link between T-box factors and the SMARCA4-containing SWI/SNF remodeling complex (By similarity). {ECO:0000250|UniProtKB:Q5NCY0, ECO:0000269|PubMed:17713478, ECO:0000269|PubMed:17825402, ECO:0000269|PubMed:17851529, ECO:0000269|PubMed:18003914, ECO:0000269|PubMed:28262558}.
|
Homo sapiens (Human)
|
O15055
|
PER2_HUMAN
|
MNGYAEFPPSPSNPTKEPVEPQPSQVPLQEDVDMSSGSSGHETNENCSTGRDSQGSDCDDSGKELGMLVEPPDARQSPDTFSLMMAKSEHNPSTSGCSSDQSSKVDTHKELIKTLKELKVHLPADKKAKGKASTLATLKYALRSVKQVKANEEYYQLLMSSEGHPCGADVPSYTVEEMESVTSEHIVKNADMFAVAVSLVSGKILYISDQVASIFHCKRDAFSDAKFVEFLAPHDVGVFHSFTSPYKLPLWSMCSGADSFTQECMEEKSFFCRVSVRKSHENEIRYHPFRMTPYLVKVRDQQGAESQLCCLLLAERVHSGYEAPRIPPEKRIFTTTHTPNCLFQDVDERAVPLLGYLPQDLIETPVLVQLHPSDRPLMLAIHKKILQSGGQPFDYSPIRFRARNGEYITLDTSWSSFINPWSRKISFIIGRHKVRVGPLNEDVFAAHPCTEEKALHPSIQELTEQIHRLLLQPVPHSGSSGYGSLGSNGSHEHLMSQTSSSDSNGHEDSRRRRAEICKNGNKTKNRSHYSHESGEQKKKSVTEMQTNPPAEKKAVPAMEKDSLGVSFPEELACKNQPTCSYQQISCLDSVIRYLESCNEAATLKRKCEFPANVPALRSSDKRKATVSPGPHAGEAEPPSRVNSRTGVGTHLTSLALPGKAESVASLTSQCSYSSTIVHVGDKKPQPELEMVEDAASGPESLDCLAGPALACGLSQEKEPFKKLGLTKEVLAAHTQKEEQSFLQKFKEIRKLSIFQSHCHYYLQERSKGQPSERTAPGLRNTSGIDSPWKKTGKNRKLKSKRVKPRDSSESTGSGGPVSARPPLVGLNATAWSPSDTSQSSCPAVPFPAPVPAAYSLPVFPAPGTVAAPPAPPHASFTVPAVPVDLQHQFAVQPPPFPAPLAPVMAFMLPSYSFPSGTPNLPQAFFPSQPQFPSHPTLTSEMASASQPEFPSRTSIPRQPCACPATRATPPSAMGRASPPLFQSRSSSPLQLNLLQLEEAPEGGTGAMGTTGATETAAVGADCKPGTSRDQQPKAPLTRDEPSDTQNSDALSTSSGLLNLLLNEDLCSASGSAASESLGSGSLGCDASPSGAGSSDTSHTSKYFGSIDSSENNHKAKMNTGMEESEHFIKCVLQDPIWLLMADADSSVMMTYQLPSRNLEAVLKEDREKLKLLQKLQPRFTESQKQELREVHQWMQTGGLPAAIDVAECVYCENKEKGNICIPYEEDIPSLGLSEVSDTKEDENGSPLNHRIEEQT
| null | null |
chromatin remodeling [GO:0006338]; circadian regulation of gene expression [GO:0032922]; circadian regulation of translation [GO:0097167]; circadian rhythm [GO:0007623]; entrainment of circadian clock by photoperiod [GO:0043153]; fatty acid metabolic process [GO:0006631]; gluconeogenesis [GO:0006094]; glycogen biosynthetic process [GO:0005978]; lactate biosynthetic process [GO:0019249]; negative regulation of circadian rhythm [GO:0042754]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of fat cell proliferation [GO:0070345]; negative regulation of protein ubiquitination [GO:0031397]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of transcription regulatory region DNA binding [GO:2000678]; positive regulation of cold-induced thermogenesis [GO:0120162]; regulation of cell cycle [GO:0051726]; regulation of circadian rhythm [GO:0042752]; regulation of glutamate uptake involved in transmission of nerve impulse [GO:0051946]; regulation of insulin secretion [GO:0050796]; regulation of neurogenesis [GO:0050767]; regulation of vasoconstriction [GO:0019229]; response to ischemia [GO:0002931]; white fat cell differentiation [GO:0050872]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]
|
transcription cis-regulatory region binding [GO:0000976]; transcription coactivator activity [GO:0003713]; transcription corepressor binding [GO:0001222]
|
PF08447;PF21353;PF12114;
|
3.30.450.20;
| null |
PTM: Acetylated. Deacetylated by SIRT1, resulting in decreased protein stability. Deacetylated by SIRT6, preventing its degradation by the proteasome, resulting in increased protein stability. {ECO:0000250|UniProtKB:O54943}.; PTM: Phosphorylated by CSNK1E and CSNK1D. Phosphorylation results in PER2 protein degradation. May be dephosphorylated by PP1. {ECO:0000269|PubMed:11165242, ECO:0000269|PubMed:11232563}.; PTM: Ubiquitinated, leading to its proteasomal degradation. Ubiquitination may be inhibited by CRY1. {ECO:0000250|UniProtKB:O54943}.
|
SUBCELLULAR LOCATION: [Isoform 1]: Nucleus {ECO:0000269|PubMed:22274616}. Cytoplasm {ECO:0000250|UniProtKB:O54943}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O54943}. Note=Nucleocytoplasmic shuttling is effected by interaction with other circadian core oscillator proteins and/or by phosphorylation. Translocate to the nucleus after phosphorylation by CSNK1D or CSNK1E. Also translocated to the nucleus by CRY1 or CRY2. PML regulates its nuclear localization. {ECO:0000250|UniProtKB:O54943}.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus, nucleolus {ECO:0000269|PubMed:24202686}.
| null | null | null | null | null |
FUNCTION: Transcriptional repressor which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, BMAL1, BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndrome and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and BMAL1 or BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK|NPAS2-BMAL1|BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress BMAL1 transcription, respectively. PER1 and PER2 proteins transport CRY1 and CRY2 into the nucleus with appropriate circadian timing, but also contribute directly to repression of clock-controlled target genes through interaction with several classes of RNA-binding proteins, helicases and others transcriptional repressors. PER appears to regulate circadian control of transcription by at least three different modes. First, interacts directly with the CLOCK-BMAL1 at the tail end of the nascent transcript peak to recruit complexes containing the SIN3-HDAC that remodel chromatin to repress transcription. Second, brings H3K9 methyltransferases such as SUV39H1 and SUV39H2 to the E-box elements of the circadian target genes, like PER2 itself or PER1. The recruitment of each repressive modifier to the DNA seems to be very precisely temporally orchestrated by the large PER complex, the deacetylases acting before than the methyltransferases. Additionally, large PER complexes are also recruited to the target genes 3' termination site through interactions with RNA-binding proteins and helicases that may play a role in transcription termination to regulate transcription independently of CLOCK-BMAL1 interactions. Recruitment of large PER complexes to the elongating polymerase at PER and CRY termination sites inhibited SETX action, impeding RNA polymerase II release and thereby repressing transcriptional reinitiation. May propagate clock information to metabolic pathways via the interaction with nuclear receptors. Coactivator of PPARA and corepressor of NR1D1, binds rhythmically at the promoter of nuclear receptors target genes like BMAL1 or G6PC1. Directly and specifically represses PPARG proadipogenic activity by blocking PPARG recruitment to target promoters and thereby inhibiting transcriptional activation. Required for fatty acid and lipid metabolism, is involved as well in the regulation of circulating insulin levels. Plays an important role in the maintenance of cardiovascular functions through the regulation of NO and vasodilatatory prostaglandins production in aortas. Controls circadian glutamate uptake in synaptic vesicles through the regulation of VGLUT1 expression. May also be involved in the regulation of inflammatory processes. Represses the CLOCK-BMAL1 induced transcription of BHLHE40/DEC1 and ATF4. Negatively regulates the formation of the TIMELESS-CRY1 complex by competing with TIMELESS for binding to CRY1. {ECO:0000250|UniProtKB:O54943}.
|
Homo sapiens (Human)
|
O15056
|
SYNJ2_HUMAN
|
MALSKGLRLLGRLGAEGDCSVLLEARGRDDCLLFEAGTVATLAPEEKEVIKGQYGKLTDAYGCLGELRLKSGGTSLSFLVLVTGCTSVGRIPDAEIYKITATDFYPLQEEAKEEERLIALKKILSSGVFYFSWPNDGSRFDLTVRTQKQGDDSSEWGNSFFWNQLLHVPLRQHQVSCCDWLLKIICGVVTIRTVYASHKQAKACLVSRVSCERTGTRFHTRGVNDDGHVSNFVETEQMIYMDDGVSSFVQIRGSVPLFWEQPGLQVGSHHLRLHRGLEANAPAFDRHMVLLKEQYGQQVVVNLLGSRGGEEVLNRAFKKLLWASCHAGDTPMINFDFHQFAKGGKLEKLETLLRPQLKLHWEDFDVFTKGENVSPRFQKGTLRMNCLDCLDRTNTVQSFIALEVLHLQLKTLGLSSKPIVDRFVESFKAMWSLNGHSLSKVFTGSRALEGKAKVGKLKDGARSMSRTIQSNFFDGVKQEAIKLLLVGDVYGEEVADKGGMLLDSTALLVTPRILKAMTERQSEFTNFKRIRIAMGTWNVNGGKQFRSNVLRTAELTDWLLDSPQLSGATDSQDDSSPADIFAVGFEEMVELSAGNIVNASTTNKKMWGEQLQKAISRSHRYILLTSAQLVGVCLYIFVRPYHVPFIRDVAIDTVKTGMGGKAGNKGAVGIRFQFHSTSFCFICSHLTAGQSQVKERNEDYKEITQKLCFPMGRNVFSHDYVFWCGDFNYRIDLTYEEVFYFVKRQDWKKLLEFDQLQLQKSSGKIFKDFHEGAINFGPTYKYDVGSAAYDTSDKCRTPAWTDRVLWWRKKHPFDKTAGELNLLDSDLDVDTKVRHTWSPGALQYYGRAELQASDHRPVLAIVEVEVQEVDVGARERVFQEVSSFQGPLDATVVVNLQSPTLEEKNEFPEDLRTELMQTLGSYGTIVLVRINQGQMLVTFADSHSALSVLDVDGMKVKGRAVKIRPKTKDWLKGLREEIIRKRDSMAPVSPTANSCLLEENFDFTSLDYESEGDILEDDEDYLVDEFNQPGVSDSELGGDDLSDVPGPTALAPPSKSPALTKKKQHPTYKDDADLVELKRELEAVGEFRHRSPSRSLSVPNRPRPPQPPQRPPPPTGLMVKKSASDASISSGTHGQYSILQTARLLPGAPQQPPKARTGISKPYNVKQIKTTNAQEAEAAIRCLLEARGGASEEALSAVAPRDLEASSEPEPTPGAAKPETPQAPPLLPRRPPPRVPAIKKPTLRRTGKPLSPEEQFEQQTVHFTIGPPETSVEAPPVVTAPRVPPVPKPRTFQPGKAAERPSHRKPASDEAPPGAGASVPPPLEAPPLVPKVPPRRKKSAPAAFHLQVLQSNSQLLQGLTYNSSDSPSGHPPAAGTVFPQGDFLSTSSATSPDSDGTKAMKPEAAPLLGDYQDPFWNLLHHPKLLNNTWLSKSSDPLDSGTRSPKRDPIDPVSAGASAAKAELPPDHEHKTLGHWVTISDQEKRTALQVFDPLAKT
|
3.1.3.36
| null |
membrane organization [GO:0061024]; phosphatidylinositol biosynthetic process [GO:0006661]; phosphatidylinositol dephosphorylation [GO:0046856]; synaptic vesicle endocytosis [GO:0048488]
|
cell projection [GO:0042995]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; membrane raft [GO:0045121]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; presynapse [GO:0098793]
|
phosphatidylinositol phosphate 4-phosphatase activity [GO:0034596]; phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity [GO:0052629]; phosphatidylinositol-3,5-bisphosphate 5-phosphatase activity [GO:0043813]; phosphatidylinositol-3-phosphate phosphatase activity [GO:0004438]; phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity [GO:0004439]; RNA binding [GO:0003723]; SH3 domain binding [GO:0017124]
|
PF08952;PF02383;
|
3.30.70.330;3.60.10.10;
|
Synaptojanin family; Inositol 1,4,5-trisphosphate 5-phosphatase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11084340}. Cell membrane {ECO:0000269|PubMed:11084340}. Membrane raft {ECO:0000269|PubMed:11084340}. Presynapse {ECO:0000250|UniProtKB:O55207}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O55207}. Note=Localizes at presynapse terminals in brain and at bundles of microtubules surrounding the nucleus in the elongating spermatids corresponding to the manchette (By similarity). Translocates from the cytoplasm to membrane ruffles in a RAC1-dependent manner (PubMed:11084340). {ECO:0000269|PubMed:11084340}.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + phosphate; Xref=Rhea:RHEA:22764, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58178, ChEBI:CHEBI:58456; EC=3.1.3.36; Evidence={ECO:0000250|UniProtKB:Q9D2G5};
| null | null | null | null |
FUNCTION: Inositol 5-phosphatase which may be involved in distinct membrane trafficking and signal transduction pathways. May mediate the inhibitory effect of Rac1 on endocytosis.
|
Homo sapiens (Human)
|
O15060
|
ZBT39_HUMAN
|
MGMRIKLQSTNHPNNLLKELNKCRLSETMCDVTIVVGSRSFPAHKAVLACAAGYFQNLFLNTGLDAARTYVVDFITPANFEKVLSFVYTSELFTDLINVGVIYEVAERLGMEDLLQACHSTFPDLESTARAKPLTSTSESHSGTLSCPSAEPAHPLGELRGGGDYLGADRNYVLPSDAGGSYKEEEKNVASDANHSLHLPQPPPPPPKTEDHDTPAPFTSIPSMMTQPLLGTVSTGIQTSTSSCQPYKVQSNGDFSKNSFLTPDNAVDITTGTNSCLSNSEHSKDPGFGQMDELQLEDLGDDDLQFEDPAEDIGTTEEVIELSDDSEDELAFGENDNRENKAMPCQVCKKVLEPNIQLIRQHARDHVDLLTGNCKVCETHFQDRNSRVTHVLSHIGIFLFSCDMCETKFFTQWQLTLHRRDGIFENNIIVHPNDPLPGKLGLFSGAASPELKCAACGKVLAKDFHVVRGHILDHLNLKGQACSVCDQRHLNLCSLMWHTLSHLGISVFSCSVCANSFVDWHLLEKHMAVHQSLEDALFHCRLCSQSFKSEAAYRYHVSQHKCNSGLDARPGFGLQHPALQKRKLPAEEFLGEELALQGQPGNSKYSCKVCGKRFAHTSEFNYHRRIHTGEKPYQCKVCHKFFRGRSTIKCHLKTHSGALMYRCTVCGHYSSTLNLMSKHVGVHKGSLPPDFTIEQTFMYIIHSKEADKNPDS
| null | null |
negative regulation of transcription by RNA polymerase II [GO:0000122]; regulation of cytokine production [GO:0001817]; regulation of immune system process [GO:0002682]
|
nucleoplasm [GO:0005654]
|
DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF00651;PF00096;
|
3.30.160.60;
|
Krueppel C2H2-type zinc-finger protein family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: May be involved in transcriptional regulation.
|
Homo sapiens (Human)
|
O15061
|
SYNEM_HUMAN
|
MLSWRLQTGPEKAELQELNARLYDYVCRVRELERENLLLEEELRGRRGREGLWAEGQARCAEEARSLRQQLDELSWATALAEGERDALRRELRELQRLDAEERAARGRLDAELGAQQRELQEALGARAALEALLGRLQAERRGLDAAHERDVRELRARAASLTMHFRARATGPAAPPPRLREVHDSYALLVAESWRETVQLYEDEVRELEEALRRGQESRLQAEEETRLCAQEAEALRREALGLEQLRARLEDALLRMREEYGIQAEERQRVIDCLEDEKATLTLAMADWLRDYQDLLQVKTGLSLEVATYRALLEGESNPEIVIWAEHVENMPSEFRNKSYHYTDSLLQRENERNLFSRQKAPLASFNHSSALYSNLSGHRGSQTGTSIGGDARRGFLGSGYSSSATTQQENSYGKAVSSQTNVRTFSPTYGLLRNTEAQVKTFPDRPKAGDTREVPVYIGEDSTIARESYRDRRDKVAAGASESTRSNERTVILGKKTEVKATREQERNRPETIRTKPEEKMFDSKEKASEERNLRWEELTKLDKEARQRESQQMKEKAKEKDSPKEKSVREREVPISLEVSQDRRAEVSPKGLQTPVKDAGGGTGREAEARELRFRLGTSDATGSLQGDSMTETVAENIVTSILKQFTQSPETEASADSFPDTKVTYVDRKELPGERKTKTEIVVESKLTEDVDVSDEAGLDYLLSKDIKEVGLKGKSAEQMIGDIINLGLKGREGRAKVVNVEIVEEPVSYVSGEKPEEFSVPFKVEEVEDVSPGPWGLVKEEEGYGESDVTFSVNQHRRTKQPQENTTHVEEVTEAGDSEGEQSYFVSTPDEHPGGHDRDDGSVYGQIHIEEESTIRYSWQDEIVQGTRRRTQKDGAVGEKVVKPLDVPAPSLEGDLGSTHWKEQARSGEFHAEPTVIEKEIKIPHEFHTSMKGISSKEPRQQLVEVIGQLEETLPERMREELSALTREGQGGPGSVSVDVKKVQGAGGSSVTLVAEVNVSQTVDADRLDLEELSKDEASEMEKAVESVVRESLSRQRSPAPGSPDEEGGAEAPAAGIRFRRWATRELYIPSGESEVAGGASHSSGQRTPQGPVSATVEVSSPTGFAQSQVLEDVSQAARHIKLGPSEVWRTERMSYEGPTAEVVEVSAGGDLSQAASPTGASRSVRHVTLGPGQSPLSREVIFLGPAPACPEAWGSPEPGPAESSADMDGSGRHSTFGCRQFHAEKEIIFQGPISAAGKVGDYFATEESVGTQTSVRQLQLGPKEGFSGQIQFTAPLSDKVELGVIGDSVHMEGLPGSSTSIRHISIGPQRHQTTQQIVYHGLVPQLGESGDSESTVHGEGSADVHQATHSHTSGRQTVMTEKSTFQSVVSESPQEDSAEDTSGAEMTSGVSRSFRHIRLGPTETETSEHIAIRGPVSRTFVLAGSADSPELGKLADSSRTLRHIAPGPKETSFTFQMDVSNVEAIRSRTQEAGALGVSDRGSWRDADSRNDQAVGVSFKASAGEGDQAHREQGKEQAMFDKKVQLQRMVDQRSVISDEKKVALLYLDNEEEENDGHWF
| null | null |
fast-twitch skeletal muscle fiber contraction [GO:0031443]; intermediate filament cytoskeleton organization [GO:0045104]
|
adherens junction [GO:0005912]; costamere [GO:0043034]; intermediate filament [GO:0005882]; intermediate filament cytoskeleton [GO:0045111]; neurofilament cytoskeleton [GO:0060053]; sarcolemma [GO:0042383]
|
intermediate filament binding [GO:0019215]; structural constituent of cytoskeleton [GO:0005200]; structural constituent of muscle [GO:0008307]; vinculin binding [GO:0017166]
|
PF00038;
|
1.20.5.170;1.20.5.1160;
|
Intermediate filament family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell junction, adherens junction. Note=There are at least two distinct SYNM subpopulations, one in which SYMN interacts with DES within the Z-lines, and another in which it interacts with both DTNA and DES at the costamere.
| null | null | null | null | null |
FUNCTION: Type-VI intermediate filament (IF) which plays an important cytoskeletal role within the muscle cell cytoskeleton. It forms heteromeric IFs with desmin and/or vimentin, and via its interaction with cytoskeletal proteins alpha-dystrobrevin, dystrophin, talin-1, utrophin and vinculin, is able to link these heteromeric IFs to adherens-type junctions, such as to the costameres, neuromuscular junctions, and myotendinous junctions within striated muscle cells. {ECO:0000269|PubMed:11353857, ECO:0000269|PubMed:16777071, ECO:0000269|PubMed:18028034}.
|
Homo sapiens (Human)
|
O15062
|
ZBTB5_HUMAN
|
MDFPGHFEQIFQQLNYQRLHGQLCDCVIVVGNRHFKAHRSVLAACSTHFRALFSVAEGDQTMNMIQLDSEVVTAEAFAALIDMMYTSTLMLGESNVMDVLLAASHLHLNSVVKACKHYLTTRTLPMSPPSERVQEQSARMQRSFMLQQLGLSIVSSALNSSQNGEEQPAPMSSSMRSNLDQRTPFPMRRLHKRKQSAEERARQRLRPSIDESAISDVTPENGPSGVHSREEFFSPDSLKIVDNPKADGMTDNQEDSAIMFDQSFGTQEDAQVPSQSDNSAGNMAQLSMASRATQVETSFDQEAAPEKSSFQCENPEVGLGEKEHMRVVVKSEPLSSPEPQDEVSDVTSQAEGSESVEVEGVVVSAEKIDLSPESSDRSFSDPQSSTDRVGDIHILEVTNNLEHKSTFSISNFLNKSRGNNFTANQNNDDNIPNTTSDCRLESEAPYLLSPEAGPAGGPSSAPGSHVENPFSEPADSHFVRPMQEVMGLPCVQTSGYQGGEQFGMDFSRSGLGLHSSFSRVMIGSPRGGASNFPYYRRIAPKMPVVTSVRSSQIPENSTSSQLMMNGATSSFENGHPSQPGPPQLTRASADVLSKCKKALSEHNVLVVEGARKYACKICCKTFLTLTDCKKHIRVHTGEKPYACLKCGKRFSQSSHLYKHSKTTCLRWQSSNLPSTLL
| null | null |
negative regulation of transcription by RNA polymerase II [GO:0000122]; regulation of transcription by RNA polymerase II [GO:0006357]
|
chromatin [GO:0000785]; nucleus [GO:0005634]
|
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; metal ion binding [GO:0046872]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]
|
PF00651;
|
3.30.160.60;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: May be involved in transcriptional regulation.
|
Homo sapiens (Human)
|
O15066
|
KIF3B_HUMAN
|
MSKLKSSESVRVVVRCRPMNGKEKAASYDKVVDVDVKLGQVSVKNPKGTAHEMPKTFTFDAVYDWNAKQFELYDETFRPLVDSVLQGFNGTIFAYGQTGTGKTYTMEGIRGDPEKRGVIPNSFDHIFTHISRSQNQQYLVRASYLEIYQEEIRDLLSKDQTKRLELKERPDTGVYVKDLSSFVTKSVKEIEHVMNVGNQNRSVGATNMNEHSSRSHAIFVITIECSEVGLDGENHIRVGKLNLVDLAGSERQAKTGAQGERLKEATKINLSLSALGNVISALVDGKSTHIPYRDSKLTRLLQDSLGGNAKTVMVANVGPASYNVEETLTTLRYANRAKNIKNKPRVNEDPKDALLREFQEEIARLKAQLEKRSIGRRKRREKRREGGGSGGGGEEEEEEGEEGEEEGDDKDDYWREQQEKLEIEKRAIVEDHSLVAEEKMRLLKEKEKKMEDLRREKDAAEMLGAKIKAMESKLLVGGKNIVDHTNEQQKILEQKRQEIAEQKRREREIQQQMESRDEETLELKETYSSLQQEVDIKTKKLKKLFSKLQAVKAEIHDLQEEHIKERQELEQTQNELTRELKLKHLIIENFIPLEEKSKIMNRAFFDEEEDHWKLHPITRLENQQMMKRPVSAVGYKRPLSQHARMSMMIRPEARYRAENIVLLELDMPSRTTRDYEGPAIAPKVQAALDAALQDEDEIQVDASSFESTANKKSKARPKSGRKSGSSSSSSGTPASQLYPQSRGLVPK
| null | null |
anterograde axonal transport [GO:0008089]; anterograde dendritic transport of neurotransmitter receptor complex [GO:0098971]; cilium assembly [GO:0060271]; determination of left/right symmetry [GO:0007368]; intraciliary transport [GO:0042073]; microtubule-based movement [GO:0007018]; mitotic centrosome separation [GO:0007100]; mitotic spindle assembly [GO:0090307]; mitotic spindle organization [GO:0007052]; opsin transport [GO:0036372]; plus-end-directed vesicle transport along microtubule [GO:0072383]; positive regulation of cytokinesis [GO:0032467]; spindle elongation [GO:0051231]; vesicle-mediated transport [GO:0016192]
|
axon cytoplasm [GO:1904115]; centrosome [GO:0005813]; ciliary tip [GO:0097542]; cilium [GO:0005929]; cytosol [GO:0005829]; dendrite [GO:0030425]; dendrite cytoplasm [GO:0032839]; dendritic spine [GO:0043197]; extracellular exosome [GO:0070062]; kinesin complex [GO:0005871]; kinesin II complex [GO:0016939]; membrane [GO:0016020]; microtubule [GO:0005874]; microtubule cytoskeleton [GO:0015630]; midbody [GO:0030496]; plus-end kinesin complex [GO:0005873]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; intraciliary transport particle B binding [GO:0120170]; microtubule binding [GO:0008017]; microtubule motor activity [GO:0003777]; plus-end-directed microtubule motor activity [GO:0008574]; small GTPase binding [GO:0031267]
|
PF00225;
|
3.40.850.10;
|
TRAFAC class myosin-kinesin ATPase superfamily, Kinesin family, Kinesin II subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. Cell projection, cilium {ECO:0000250|UniProtKB:Q61771}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:Q61771}.
| null | null | null | null | null |
FUNCTION: Microtubule-based molecular motor that transport intracellular cargos, such as vesicles, organelles and protein complexes. Uses ATP hydrolysis to generate force to bind and move along the microtubule (By similarity). Plays a role in cilia formation (PubMed:32386558). Involved in photoreceptor integrity and opsin trafficking in rod photoreceptors (PubMed:32386558). Transports vesicles containing N-methyl-D-aspartate (NMDA) receptor subunit GRIN2A into neuronal dendrites (By similarity). {ECO:0000250|UniProtKB:Q61771, ECO:0000269|PubMed:32386558}.
|
Homo sapiens (Human)
|
O15067
|
PUR4_HUMAN
|
MSPVLHFYVRPSGHEGAAPGHTRRKLQGKLPELQGVETELCYNVNWTAEALPSAEETKKLMWLFGCPLLLDDVARESWLLPGSNDLLLEVGPRLNFSTPTSTNIVSVCRATGLGPVDRVETTRRYRLSFAHPPSAEVEAIALATLHDRMTEQHFPHPIQSFSPESMPEPLNGPINILGEGRLALEKANQELGLALDSWDLDFYTKRFQELQRNPSTVEAFDLAQSNSEHSRHWFFKGQLHVDGQKLVHSLFESIMSTQESSNPNNVLKFCDNSSAIQGKEVRFLRPEDPTRPSRFQQQQGLRHVVFTAETHNFPTGVCPFSGATTGTGGRIRDVQCTGRGAHVVAGTAGYCFGNLHIPGYNLPWEDPSFQYPGNFARPLEVAIEASNGASDYGNKFGEPVLAGFARSLGLQLPDGQRREWIKPIMFSGGIGSMEADHISKEAPEPGMEVVKVGGPVYRIGVGGGAASSVQVQGDNTSDLDFGAVQRGDPEMEQKMNRVIRACVEAPKGNPICSLHDQGAGGNGNVLKELSDPAGAIIYTSRFQLGDPTLNALEIWGAEYQESNALLLRSPNRDFLTHVSARERCPACFVGTITGDRRIVLVDDRECPVRRNGQGDAPPTPLPTPVDLELEWVLGKMPRKEFFLQRKPPMLQPLALPPGLSVHQALERVLRLPAVASKRYLTNKVDRSVGGLVAQQQCVGPLQTPLADVAVVALSHEELIGAATALGEQPVKSLLDPKVAARLAVAEALTNLVFALVTDLRDVKCSGNWMWAAKLPGEGAALADACEAMVAVMAALGVAVDGGKDSLSMAARVGTETVRAPGSLVISAYAVCPDITATVTPDLKHPEGRGHLLYVALSPGQHRLGGTALAQCFSQLGEHPPDLDLPENLVRAFSITQGLLKDRLLCSGHDVSDGGLVTCLLEMAFAGNCGLQVDVPVPRVDVLSVLFAEEPGLVLEVQEPDLAQVLKRYRDAGLHCLELGHTGEAGPHAMVRVSVNGAVVLEEPVGELRALWEETSFQLDRLQAEPRCVAEEERGLRERMGPSYCLPPTFPKASVPREPGGPSPRVAILREEGSNGDREMADAFHLAGFEVWDVTMQDLCSGAIGLDTFRGVAFVGGFSYADVLGSAKGWAAAVTFHPRAGAELRRFRKRPDTFSLGVCNGCQLLALLGWVGGDPNEDAAEMGPDSQPARPGLLLRHNLSGRYESRWASVRVGPGPALMLRGMEGAVLPVWSAHGEGYVAFSSPELQAQIEARGLAPLHWADDDGNPTEQYPLNPNGSPGGVAGICSCDGRHLAVMPHPERAVRPWQWAWRPPPFDTLTTSPWLQLFINARNWTLEGSC
|
6.3.5.3
| null |
'de novo' AMP biosynthetic process [GO:0044208]; 'de novo' IMP biosynthetic process [GO:0006189]; 'de novo' XMP biosynthetic process [GO:0097294]; anterior head development [GO:0097065]; glutamine metabolic process [GO:0006541]; GMP biosynthetic process [GO:0006177]; purine nucleotide biosynthetic process [GO:0006164]; purine ribonucleoside monophosphate biosynthetic process [GO:0009168]; response to xenobiotic stimulus [GO:0009410]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]
|
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; phosphoribosylformylglycinamidine synthase activity [GO:0004642]
|
PF02769;PF18072;PF18076;PF13507;
|
3.40.50.880;1.10.8.750;3.90.650.10;3.30.1330.10;
|
FGAMS family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate; Xref=Rhea:RHEA:17129, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, ChEBI:CHEBI:147286, ChEBI:CHEBI:147287, ChEBI:CHEBI:456216; EC=6.3.5.3; Evidence={ECO:0000305|PubMed:10548741}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17130; Evidence={ECO:0000305|PubMed:10548741};
| null |
PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 1/2. {ECO:0000305|PubMed:10548741}.
| null | null |
FUNCTION: Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. {ECO:0000305|PubMed:10548741}.
|
Homo sapiens (Human)
|
O15068
|
MCF2L_HUMAN
|
MFDCWRFILCKRPGSNSYSSPQRPNEAKKEETDHQIDVSDVIRLVQDTPEATAMATDEIMHQDIVPLCAADIQDQLKKRFAYLSGGRGQDGSPVITFPDYPAFSEIPDKEFQNVMTYLTSIPSLQDAGIGFILVIDRRRDKWTSVKASVLRIAASFPANLQLVLVLRPTGFFQRTLSDIAFKFNRDDFKMKVPVIMLSSVPDLHGYIDKSQLTEDLGGTLDYCHSRWLCQRTAIESFALMVKQTAQMLQSFGTELAETELPNDVQSTSSVLCAHTEKKDKAKEDLRLALKEGHSVLESLRELQAEGSEPSVNQDQLDNQATVQRLLAQLNETEAAFDEFWAKHQQKLEQCLQLRHFEQGFREVKAILDAASQKIATFTDIGNSLAHVEHLLRDLASFEEKSGVAVERARALSLDGEQLIGNKHYAVDSIRPKCQELRHLCDQFSAEIARRRGLLSKSLELHRRLETSMKWCDEGIYLLASQPVDKCQSQDGAEAALQEIEKFLETGAENKIQELNAIYKEYESILNQDLMEHVRKVFQKQASMEEVFHRRQASLKKLAARQTRPVQPVAPRPEALAKSPCPSPGIRRGSENSSSEGGALRRGPYRRAKSEMSESRQGRGSAGEEEESLAILRRHVMSELLDTERAYVEELLCVLEGYAAEMDNPLMAHLLSTGLHNKKDVLFGNMEEIYHFHNRIFLRELENYTDCPELVGRCFLERMEDFQIYEKYCQNKPRSESLWRQCSDCPFFQECQRKLDHKLSLDSYLLKPVQRITKYQLLLKEMLKYSRNCEGAEDLQEALSSILGILKAVNDSMHLIAITGYDGNLGDLGKLLMQGSFSVWTDHKRGHTKVKELARFKPMQRHLFLHEKAVLFCKKREENGEGYEKAPSYSYKQSLNMAAVGITENVKGDAKKFEIWYNAREEVYIVQAPTPEIKAAWVNEIRKVLTSQLQACREASQHRALEQSQSLPLPAPTSTSPSRGNSRNIKKLEERKTDPLSLEGYVSSAPLTKPPEKGKGWSKTSHSLEAPEDDGGWSSAEEQINSSDAEEDGGLGPKKLVPGKYTVVADHEKGGPDALRVRSGDVVELVQEGDEGLWYVRDPTTGKEGWVPASSLSVRLGPSGSAQCLSSSGKAHVPRAHP
| null | null |
intracellular signal transduction [GO:0035556]; positive regulation of Rho protein signal transduction [GO:0035025]; regulation of small GTPase mediated signal transduction [GO:0051056]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; endomembrane system [GO:0012505]; extracellular space [GO:0005615]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; extrinsic component of membrane [GO:0019898]; plasma membrane [GO:0005886]
|
guanyl-nucleotide exchange factor activity [GO:0005085]; phosphatidylinositol binding [GO:0035091]
|
PF13716;PF00169;PF00621;PF07653;PF00435;
|
1.20.58.60;1.20.900.10;2.30.29.30;2.30.30.40;
|
MCF2 family
| null |
SUBCELLULAR LOCATION: [Isoform 5]: Cytoplasm {ECO:0000269|PubMed:15157669}. Cell membrane {ECO:0000269|PubMed:15157669}; Peripheral membrane protein {ECO:0000269|PubMed:15157669}; Cytoplasmic side {ECO:0000269|PubMed:15157669}.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm {ECO:0000269|PubMed:15157669}. Endomembrane system {ECO:0000269|PubMed:15157669}. Note=Interaction with membranes enriched in phosphoinositides is mediated by the CRAL-TRIO domain. {ECO:0000269|PubMed:15157669}.; SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q64096}. Cell membrane {ECO:0000250|UniProtKB:Q64096}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q64096}; Cytoplasmic side {ECO:0000250|UniProtKB:Q64096}.
| null | null | null | null | null |
FUNCTION: Guanine nucleotide exchange factor that catalyzes guanine nucleotide exchange on RHOA and CDC42, and thereby contributes to the regulation of RHOA and CDC42 signaling pathways (By similarity). Seems to lack activity with RAC1. Becomes activated and highly tumorigenic by truncation of the N-terminus (By similarity). Isoform 5 activates CDC42 (PubMed:15157669). {ECO:0000250|UniProtKB:Q63406, ECO:0000269|PubMed:15157669}.; FUNCTION: [Isoform 3]: Does not catalyze guanine nucleotide exchange on CDC42 (PubMed:15157669). {ECO:0000269|PubMed:15157669}.
|
Homo sapiens (Human)
|
O15072
|
ATS3_HUMAN
|
MVLLSLWLIAAALVEVRTSADGQAGNEEMVQIDLPIKRYREYELVTPVSTNLEGRYLSHTLSASHKKRSARDVSSNPEQLFFNITAFGKDFHLRLKPNTQLVAPGAVVEWHETSLVPGNITDPINNHQPGSATYRIRRTEPLQTNCAYVGDIVDIPGTSVAISNCDGLAGMIKSDNEEYFIEPLERGKQMEEEKGRIHVVYKRSAVEQAPIDMSKDFHYRESDLEGLDDLGTVYGNIHQQLNETMRRRRHAGENDYNIEVLLGVDDSVVRFHGKEHVQNYLLTLMNIVNEIYHDESLGVHINVVLVRMIMLGYAKSISLIERGNPSRSLENVCRWASQQQRSDLNHSEHHDHAIFLTRQDFGPAGMQGYAPVTGMCHPVRSCTLNHEDGFSSAFVVAHETGHVLGMEHDGQGNRCGDETAMGSVMAPLVQAAFHRYHWSRCSGQELKRYIHSYDCLLDDPFDHDWPKLPELPGINYSMDEQCRFDFGVGYKMCTAFRTFDPCKQLWCSHPDNPYFCKTKKGPPLDGTECAAGKWCYKGHCMWKNANQQKQDGNWGSWTKFGSCSRTCGTGVRFRTRQCNNPMPINGGQDCPGVNFEYQLCNTEECQKHFEDFRAQQCQQRNSHFEYQNTKHHWLPYEHPDPKKRCHLYCQSKETGDVAYMKQLVHDGTHCSYKDPYSICVRGECVKVGCDKEIGSNKVEDKCGVCGGDNSHCRTVKGTFTRTPRKLGYLKMFDIPPGARHVLIQEDEASPHILAIKNQATGHYILNGKGEEAKSRTFIDLGVEWDYNIEDDIESLHTDGPLHDPVIVLIIPQENDTRSSLTYKYIIHEDSVPTINSNNVIQEELDTFEWALKSWSQCSKPCGGGFQYTKYGCRRKSDNKMVHRSFCEANKKPKPIRRMCNIQECTHPLWVAEEWEHCTKTCGSSGYQLRTVRCLQPLLDGTNRSVHSKYCMGDRPESRRPCNRVPCPAQWKTGPWSECSVTCGEGTEVRQVLCRAGDHCDGEKPESVRACQLPPCNDEPCLGDKSIFCQMEVLARYCSIPGYNKLCCESCSKRSSTLPPPYLLEAAETHDDVISNPSDLPRSLVMPTSLVPYHSETPAKKMSLSSISSVGGPNAYAAFRPNSKPDGANLRQRSAQQAGSKTVRLVTVPSSPPTKRVHLSSASQMAAASFFAASDSIGASSQARTSKKDGKIIDNRRPTRSSTLER
|
3.4.24.-
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250};
|
collagen biosynthetic process [GO:0032964]; collagen catabolic process [GO:0030574]; collagen fibril organization [GO:0030199]; extracellular matrix organization [GO:0030198]; in utero embryonic development [GO:0001701]; positive regulation of vascular endothelial growth factor signaling pathway [GO:1900748]; protein processing [GO:0016485]; supramolecular fiber organization [GO:0097435]; vascular endothelial growth factor production [GO:0010573]
|
extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
endopeptidase activity [GO:0004175]; heparin binding [GO:0008201]; metalloendopeptidase activity [GO:0004222]; zinc ion binding [GO:0008270]
|
PF17771;PF19236;PF05986;PF01562;PF01421;PF19030;PF00090;
|
2.60.120.830;3.40.1620.60;3.40.390.10;2.20.100.10;
| null |
PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}.; PTM: Glycosylated. Can be O-fucosylated by POFUT2 on a serine or a threonine residue found within the consensus sequence C1-X(2)-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are the first and second cysteine residue of the repeat, respectively. Fucosylated repeats can then be further glycosylated by the addition of a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL. Fucosylation mediates the efficient secretion of ADAMTS family members. Can also be C-glycosylated with one or two mannose molecules on tryptophan residues within the consensus sequence W-X-X-W of the TPRs, and N-glycosylated. These other glycosylations can also facilitate secretion (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28985353}. Secreted, extracellular space, extracellular matrix {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Cleaves the propeptides of type II collagen prior to fibril assembly. Does not act on types I and III collagens.
|
Homo sapiens (Human)
|
O15075
|
DCLK1_HUMAN
|
MSFGRDMELEHFDERDKAQRYSRGSRVNGLPSPTHSAHCSFYRTRTLQTLSSEKKAKKVRFYRNGDRYFKGIVYAISPDRFRSFEALLADLTRTLSDNVNLPQGVRTIYTIDGLKKISSLDQLVEGESYVCGSIEPFKKLEYTKNVNPNWSVNVKTTSASRAVSSLATAKGSPSEVRENKDFIRPKLVTIIRSGVKPRKAVRILLNKKTAHSFEQVLTDITDAIKLDSGVVKRLYTLDGKQVMCLQDFFGDDDIFIACGPEKFRYQDDFLLDESECRVVKSTSYTKIASSSRRSTTKSPGPSRRSKSPASTSSVNGTPGSQLSTPRSGKSPSPSPTSPGSLRKQRSSQHGGSSTSLASTKVCSSMDENDGPGEEVSEEGFQIPATITERYKVGRTIGDGNFAVVKECVERSTAREYALKIIKKSKCRGKEHMIQNEVSILRRVKHPNIVLLIEEMDVPTELYLVMELVKGGDLFDAITSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVYEHQDGSKSLKLGDFGLATIVDGPLYTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRGSGDDQEVLFDQILMGQVDFPSPYWDNVSDSAKELITMMLLVDVDQRFSAVQVLEHPWVNDDGLPENEHQLSVAGKIKKHFNTGPKPNSTAAGVSVIATTALDKERQVFRRRRNQDVRSRYKAQPAPPELNSESEDYSPSSSETVRSPNSPF
|
2.7.11.1
| null |
axon extension [GO:0048675]; central nervous system development [GO:0007417]; central nervous system projection neuron axonogenesis [GO:0021952]; dendrite morphogenesis [GO:0048813]; endosomal transport [GO:0016197]; forebrain development [GO:0030900]; intracellular signal transduction [GO:0035556]; negative regulation of protein localization to nucleus [GO:1900181]; nervous system development [GO:0007399]; neuron migration [GO:0001764]; neuron projection morphogenesis [GO:0048812]; protein localization to nucleus [GO:0034504]; protein phosphorylation [GO:0006468]; response to virus [GO:0009615]
|
plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]
|
ATP binding [GO:0005524]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF03607;PF00069;
|
3.10.20.230;1.10.510.10;
|
Protein kinase superfamily, CAMK Ser/Thr protein kinase family, CaMK subfamily
| null | null |
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
| null | null | null | null |
FUNCTION: Probable kinase that may be involved in a calcium-signaling pathway controlling neuronal migration in the developing brain. May also participate in functions of the mature nervous system.
|
Homo sapiens (Human)
|
O15078
|
CE290_HUMAN
|
MPPNINWKEIMKVDPDDLPRQEELADNLLISLSKVEVNELKSEKQENVIHLFRITQSLMKMKAQEVELALEEVEKAGEEQAKFENQLKTKVMKLENELEMAQQSAGGRDTRFLRNEICQLEKQLEQKDRELEDMEKELEKEKKVNEQLALRNEEAENENSKLRRENKRLKKKNEQLCQDIIDYQKQIDSQKETLLSRRGEDSDYRSQLSKKNYELIQYLDEIQTLTEANEKIEVQNQEMRKNLEESVQEMEKMTDEYNRMKAIVHQTDNVIDQLKKENDHYQLQVQELTDLLKSKNEEDDPIMVAVNAKVEEWKLILSSKDDEIIEYQQMLHNLREKLKNAQLDADKSNVMALQQGIQERDSQIKMLTEQVEQYTKEMEKNTCIIEDLKNELQRNKGASTLSQQTHMKIQSTLDILKEKTKEAERTAELAEADAREKDKELVEALKRLKDYESGVYGLEDAVVEIKNCKNQIKIRDREIEILTKEINKLELKISDFLDENEALRERVGLEPKTMIDLTEFRNSKHLKQQQYRAENQILLKEIESLEEERLDLKKKIRQMAQERGKRSATSGLTTEDLNLTENISQGDRISERKLDLLSLKNMSEAQSKNEFLSRELIEKERDLERSRTVIAKFQNKLKELVEENKQLEEGMKEILQAIKEMQKDPDVKGGETSLIIPSLERLVNAIESKNAEGIFDASLHLKAQVDQLTGRNEELRQELRESRKEAINYSQQLAKANLKIDHLEKETSLLRQSEGSNVVFKGIDLPDGIAPSSASIINSQNEYLIHLLQELENKEKKLKNLEDSLEDYNRKFAVIRHQQSLLYKEYLSEKETWKTESKTIKEEKRKLEDQVQQDAIKVKEYNNLLNALQMDSDEMKKILAENSRKITVLQVNEKSLIRQYTTLVELERQLRKENEKQKNELLSMEAEVCEKIGCLQRFKEMAIFKIAALQKVVDNSVSLSELELANKQYNELTAKYRDILQKDNMLVQRTSNLEHLECENISLKEQVESINKELEITKEKLHTIEQAWEQETKLGNESSMDKAKKSITNSDIVSISKKITMLEMKELNERQRAEHCQKMYEHLRTSLKQMEERNFELETKFAELTKINLDAQKVEQMLRDELADSVSKAVSDADRQRILELEKNEMELKVEVSKLREISDIARRQVEILNAQQQSRDKEVESLRMQLLDYQAQSDEKSLIAKLHQHNVSLQLSEATALGKLESITSKLQKMEAYNLRLEQKLDEKEQALYYARLEGRNRAKHLRQTIQSLRRQFSGALPLAQQEKFSKTMIQLQNDKLKIMQEMKNSQQEHRNMENKTLEMELKLKGLEELISTLKDTKGAQKVINWHMKIEELRLQELKLNRELVKDKEEIKYLNNIISEYERTISSLEEEIVQQNKFHEERQMAWDQREVDLERQLDIFDRQQNEILNAAQKFEEATGSIPDPSLPLPNQLEIALRKIKENIRIILETRATCKSLEEKLKEKESALRLAEQNILSRDKVINELRLRLPATAEREKLIAELGRKEMEPKSHHTLKIAHQTIANMQARLNQKEEVLKKYQRLLEKAREEQREIVKKHEEDLHILHHRLELQADSSLNKFKQTAWDLMKQSPTPVPTNKHFIRLAEMEQTVAEQDDSLSSLLVKLKKVSQDLERQREITELKVKEFENIKLQLQENHEDEVKKVKAEVEDLKYLLDQSQKESQCLKSELQAQKEANSRAPTTTMRNLVERLKSQLALKEKQQKALSRALLELRAEMTAAAEERIISATSQKEAHLNVQQIVDRHTRELKTQVEDLNENLLKLKEALKTSKNRENSLTDNLNDLNNELQKKQKAYNKILREKEEIDQENDELKRQIKRLTSGLQGKPLTDNKQSLIEELQRKVKKLENQLEGKVEEVDLKPMKEKNAKEELIRWEEGKKWQAKIEGIRNKLKEKEGEVFTLTKQLNTLKDLFAKADKEKLTLQRKLKTTGMTVDQVLGIRALESEKELEELKKRNLDLENDILYMRAHQALPRDSVVEDLHLQNRYLQEKLHALEKQFSKDTYSKPSISGIESDDHCQREQELQKENLKLSSENIELKFQLEQANKDLPRLKNQVRDLKEMCEFLKKEKAEVQRKLGHVRGSGRSGKTIPELEKTIGLMKKVVEKVQRENEQLKKASGILTSEKMANIEQENEKLKAELEKLKAHLGHQLSMHYESKTKGTEKIIAENERLRKELKKETDAAEKLRIAKNNLEILNEKMTVQLEETGKRLQFAESRGPQLEGADSKSWKSIVVTRMYETKLKELETDIAKKNQSITDLKQLVKEATEREQKVNKYNEDLEQQIKILKHVPEGAETEQGLKRELQVLRLANHQLDKEKAELIHQIEANKDQSGAESTIPDADQLKEKIKDLETQLKMSDLEKQHLKEEIKKLKKELENFDPSFFEEIEDLKYNYKEEVKKNILLEEKVKKLSEQLGVELTSPVAASEEFEDEEESPVNFPIY
| null | null |
camera-type eye development [GO:0043010]; ciliary basal body-plasma membrane docking [GO:0097711]; ciliary transition zone assembly [GO:1905349]; cilium assembly [GO:0060271]; eye photoreceptor cell development [GO:0042462]; hindbrain development [GO:0030902]; kidney development [GO:0001822]; non-motile cilium assembly [GO:1905515]; otic vesicle formation [GO:0030916]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of intracellular protein transport [GO:0090316]; pronephros development [GO:0048793]; protein transport [GO:0015031]; regulation of establishment of protein localization [GO:0070201]
|
centriolar satellite [GO:0034451]; centriole [GO:0005814]; centrosome [GO:0005813]; ciliary basal body [GO:0036064]; ciliary transition zone [GO:0035869]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular region [GO:0005576]; membrane [GO:0016020]; MKS complex [GO:0036038]; nucleus [GO:0005634]; photoreceptor connecting cilium [GO:0032391]; protein-containing complex [GO:0032991]; specific granule lumen [GO:0035580]
|
identical protein binding [GO:0042802]
|
PF16574;
| null | null |
PTM: Ubiquitinated. May undergo monoubiquitination; monoubiquitination is inhibited in response to cellular stress, such as ultraviolet light (UV) radiation or heat shock, but does not cause its displacement from centriolar satellites. {ECO:0000269|PubMed:24121310}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:16682973, ECO:0000269|PubMed:21493627, ECO:0000269|PubMed:21565611, ECO:0000269|PubMed:22797915}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000269|PubMed:17705300, ECO:0000269|PubMed:21493627, ECO:0000269|PubMed:22797915, ECO:0000269|PubMed:23943788, ECO:0000269|PubMed:24121310}. Nucleus {ECO:0000250|UniProtKB:Q6A078}. Cell projection, cilium {ECO:0000269|PubMed:23943788}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q6A078}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:22797915}. Cytoplasmic vesicle {ECO:0000303|PubMed:24051377}. Note=Displaced from centriolar satellites in response to cellular stress, such as ultraviolet light (UV) radiation or heat shock (PubMed:24121310). Found in the connecting cilium of photoreceptor cells, base of cilium in kidney intramedullary collecting duct cells (By similarity). Localizes at the transition zone, a region between the basal body and the ciliary axoneme (PubMed:23943788). Localization at the ciliary transition zone as well as at centriolar satellites is BBsome-dependent (PubMed:23943788). {ECO:0000250|UniProtKB:Q6A078, ECO:0000269|PubMed:23943788, ECO:0000269|PubMed:24121310}.
| null | null | null | null | null |
FUNCTION: Involved in early and late steps in cilia formation. Its association with CCP110 is required for inhibition of primary cilia formation by CCP110 (PubMed:18694559). May play a role in early ciliogenesis in the disappearance of centriolar satellites and in the transition of primary ciliar vesicles (PCVs) to capped ciliary vesicles (CCVs). Required for the centrosomal recruitment of RAB8A and for the targeting of centriole satellite proteins to centrosomes such as of PCM1 (PubMed:24421332). Required for the correct localization of ciliary and phototransduction proteins in retinal photoreceptor cells; may play a role in ciliary transport processes (By similarity). Required for efficient recruitment of RAB8A to primary cilium (PubMed:17705300). In the ciliary transition zone is part of the tectonic-like complex which is required for tissue-specific ciliogenesis and may regulate ciliary membrane composition (By similarity). Involved in regulation of the BBSome complex integrity, specifically for presence of BBS2, BBS5 and BBS8/TTC8 in the complex, and in ciliary targeting of selected BBSome cargos. May play a role in controlling entry of the BBSome complex to cilia possibly implicating IQCB1/NPHP5 (PubMed:25552655). Activates ATF4-mediated transcription (PubMed:16682973). {ECO:0000250|UniProtKB:Q6A078, ECO:0000269|PubMed:16682973, ECO:0000269|PubMed:17705300, ECO:0000269|PubMed:18694559, ECO:0000269|PubMed:24421332, ECO:0000269|PubMed:25552655}.
|
Homo sapiens (Human)
|
O15079
|
SNPH_HUMAN
|
MAMSLPGSRRTSAGSRRRTSPPVSVRDAYGTSSLSSSSNSGSYKGSDSSPTPRRSMKYTLCSDNHGIKPPTPEQYLTPLQQKEVCIRHLKARLKDTQDRLQDRDTEIDDLKTQLSRMQEDWIEEECHRVEAQLALKEARKEIKQLKQVIDTVKNNLIDKDKGLQKYFVDINIQNKKLETLLHSMEVAQNGMAKEDGTGESAGGSPARSLTRSSTYTKLSDPAVCGDRQPGDPSSGSAEDGADSGFAAADDTLSRTDALEASSLLSSGVDCGTEETSLHSSFGLGPRFPASNTYEKLLCGMEAGVQASCMQERAIQTDFVQYQPDLDTILEKVTQAQVCGTDPESGDRCPELDAHPSGPRDPNSAVVVTVGDELEAPEPITRGPTPQRPGANPNPGQSVSVVCPMEEEEEAAVAEKEPKSYWSRHYIVDLLAVVVPAVPTVAWLCRSQRRQGQPIYNISSLLRGCCTVALHSIRRISCRSLSQPSPSPAGGGSQL
| null | null |
neuron differentiation [GO:0030182]; neurotransmitter secretion [GO:0007269]; synaptic vesicle docking [GO:0016081]
|
cytoplasm [GO:0005737]; cytoplasmic microtubule [GO:0005881]; membrane [GO:0016020]; mitochondrion [GO:0005739]; neuron projection [GO:0043005]; presynapse [GO:0098793]
|
syntaxin-1 binding [GO:0017075]
|
PF15290;
| null | null | null |
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Synapse, synaptosome.
| null | null | null | null | null |
FUNCTION: Inhibits SNARE complex formation by absorbing free STX1A. {ECO:0000269|PubMed:10707983}.
|
Homo sapiens (Human)
|
O15083
|
ERC2_HUMAN
|
MYGSARTITNLEGSPSRSPRLPRSPRLGHRRTSSGGGGGTGKTLSMENIQSLNAAYATSGPMYLSDHEGVASTTYPKGTMTLGRATNRAVYGGRVTAMGSSPNIASAGLSHTDVLSYTDQHGGLTGSSHHHHHQVPSMLRQVRDSTMLDLQAQLKELQRENDLLRKELDIKDSKLGSSMNSIKTFWSPELKKERVLRKEEAARMSVLKEQMRVSHEENQHLQLTIQALQDELRTQRDLNHLLQQESGNRGAEHFTIELTEENFRRLQAEHDRQAKELFLLRKTLEEMELRIETQKQTLNARDESIKKLLEMLQSKGLPSKSLEDDNERTRRMAEAESQVSHLEVILDQKEKENIHLREELHRRSQLQPEPAKTKALQTVIEMKDTKIASLERNIRDLEDEIQMLKANGVLNTEDREEEIKQIEVYKSHSKFMKTKIDQLKQELSKKESELLALQTKLETLSNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKGTLAGEIRDMKDMLEVKERKINVLQKKIENLQEQLRDKDKQLTNLKDRVKSLQTDSSNTDTALATLEEALSEKERIIERLKEQRERDDRERLEEIESFRKENKDLKEKVNALQAELTEKESSLIDLKEHASSLASAGLKRDSKLKSLEIAIEQKKEECSKLEAQLKKAHNIEDDSRMNPEFADQIKQLDKEASYYRDECGKAQAEVDRLLEILKEVENEKNDKDKKIAELESLTLRHMKDQNKKVANLKHNQQLEKKKNAQLLEEVRRREDSMADNSQHLQIEELMNALEKTRQELDATKARLASTQQSLAEKEAHLANLRIERRKQLEEILEMKQEALLAAISEKDANIALLELSASKKKKTQEEVMALKREKDRLVHQLKQQTQNRMKLMADNYDDDHHHYHHHHHHHHHRSPGRSQHSNHRPSPDQDDEEGIWA
| null | null |
maintenance of presynaptic active zone structure [GO:0048790]; neuromuscular synaptic transmission [GO:0007274]; regulation of calcium-dependent activation of synaptic vesicle fusion [GO:0150037]; regulation of presynaptic cytosolic calcium ion concentration [GO:0099509]; regulation of synaptic plasticity [GO:0048167]; synaptic vesicle priming [GO:0016082]
|
cytoskeleton of presynaptic active zone [GO:0048788]; GABA-ergic synapse [GO:0098982]; glutamatergic synapse [GO:0098978]; growth cone [GO:0030426]; presynaptic active zone [GO:0048786]; presynaptic membrane [GO:0042734]
|
structural constituent of presynaptic active zone [GO:0098882]
|
PF10174;
|
1.10.287.1490;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12923177}. Synapse {ECO:0000269|PubMed:12923177}. Presynaptic active zone {ECO:0000269|PubMed:12923177}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12923177}. Note=In neurons, localized to synapses, and colocalizes with PCLO. Localized to the active zone of presynaptic density (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Thought to be involved in the organization of the cytomatrix at the nerve terminals active zone (CAZ) which regulates neurotransmitter release. Seems to act together with BSN. May recruit liprin-alpha proteins to the CAZ.
|
Homo sapiens (Human)
|
O15084
|
ANR28_HUMAN
|
MAFLKLRDQPSLVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGAIVNQKNEKGFTPLHFAAASTHGALCLELLVGNGADVNMKSKDGKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGHELLINTLITSGADTAKRGIHGMFPLHLAALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRSPLHYAAANCNYQCLFALVGSGASVNDLDERGCTPLHYAATSDTDGKCLEYLLRNDANPGIRDKQGYNAVHYSAAYGHRLCLQLIASETPLDVLMETSGTDMLSDSDNRATISPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPLDLAAFKGHVECVDVLINQGASILVKDYILKRTPIHAAATNGHSECLRLLIGNAEPQNAVDIQDGNGQTPLMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQHGAKCLLRDSRGRTPIHLSAACGHIGVLGALLQSAASMDANPATADNHGYTALHWACYNGHETCVELLLEQEVFQKTEGNAFSPLHCAVINDNEGAAEMLIDTLGASIVNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQTNTVEMLVSSASAELTLQDNSKNTALHLACSKGHETSALLILEKITDRNLINATNAALQTPLHVAARNGLTMVVQELLGKGASVLAVDENGYTPALACAPNKDVADCLALILATMMPVSSSSPLSSLTFNAINRYTNTSKTVSFEALPIMRNEPSSYCSFNNIGGEQEYLYTDVDELNDSDSETY
| null | null |
negative regulation of non-canonical NF-kappaB signal transduction [GO:1901223]
|
cytosol [GO:0005829]; nucleoplasm [GO:0005654]
| null |
PF00023;PF12796;PF13637;
|
1.25.40.20;
| null | null |
SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:16564677}. Note=Seems to be excluded from nucleoli.
| null | null | null | null | null |
FUNCTION: Putative regulatory subunit of protein phosphatase 6 (PP6) that may be involved in the recognition of phosphoprotein substrates. Involved in the PP6-mediated dephosphorylation of NFKBIE opposing its degradation in response to TNF-alpha. Selectively inhibits the phosphatase activity of PPP1C. Targets PPP1C to modulate HNRPK phosphorylation. {ECO:0000269|PubMed:16564677, ECO:0000269|PubMed:18186651}.
|
Homo sapiens (Human)
|
O15085
|
ARHGB_HUMAN
|
MSVRLPQSIDRLSSLSSLGDSAPERKSPSHHRQPSDASETTGLVQRCVIIQKDQHGFGFTVSGDRIVLVQSVRPGGAAMKAGVKEGDRIIKVNGTMVTNSSHLEVVKLIKSGAYVALTLLGSSPSSMGISGLQQDPSPAGAPRITSVIPSPPPPPPLPPPQRITGPKPLQDPEVQKHATQILRNMLRQEEKELQDILPLYGDTSQRPSEGRLSLDSQEGDSGLDSGTERFPSLSESLMNRNSVLSDPGLDSPRTSPVIMARVAQHHRRQGSDAAVPSTGDQGVDQSPKPLIIGPEEDYDPGYFNNESDIIFQDLEKLKSRPAHLGVFLRYIFSQADPSPLLFYLCAEVYQQASPKDSRSLGKDIWNIFLEKNAPLRVKIPEMLQAEIDSRLRNSEDARGVLCEAQEAAMPEIQEQIHDYRTKRTLGLGSLYGENDLLDLDGDPLRERQVAEKQLAALGDILSKYEEDRSAPMDFALNTYMSHAGIRLREARPSNTAEKAQSAPDKDKWLPFFPKTKKSSNSKKEKDALEDKKRNPILKYIGKPKSSSQSTFHIPLSPVEVKPGNVRNIIQHFENNQQYDAPEPGTQRLSTGSFPEDLLESDSSRSEIRLGRSESLKGREEMKRSRKAENVPRSRSDVDMDAAAEATRLHQSASSSTSSLSTRSLENPTPPFTPKMGRRSIESPSLGFCTDTLLPHLLEDDLGQLSDLEPEPDAQNWQHTVGKDVVAGLTQREIDRQEVINELFVTEASHLRTLRVLDLIFYQRMKKENLMPREELARLFPNLPELIEIHNSWCEAMKKLREEGPIIKEISDLMLARFDGPAREELQQVAAQFCSYQSIALELIKTKQRKESRFQLFMQEAESHPQCRRLQLRDLIISEMQRLTKYPLLLESIIKHTEGGTSEHEKLCRARDQCREILKYVNEAVKQTENRHRLEGYQKRLDATALERASNPLAAEFKSLDLTTRKMIHEGPLTWRISKDKTLDLHVLLLEDLLVLLQKQDEKLLLKCHSKTAVGSSDSKQTFSPVLKLNAVLIRSVATDKRAFFIICTSKLGPPQIYELVALTSSDKNTWMELLEEAVRNATRHPGAAPMPVHPPPPGPREPAQQGPTPSRVELDDSDVFHGEPEPEELPGGTGSQQRVQGKHQVLLEDPEQEGSAEEEELGVLPCPSTSLDGENRGIRTRNPIHLAFPGPLFMEGLADSALEDVENLRHLILWSLLPGHTMETQAAQEPEDDLTPTPSVISVTSHPWDPGSPGQAPPGGEGDNTQLAGLEGERPEQEDMGLCSLEHLPPRTRNSGIWESPELDRNLAEDASSTEAAGGYKVVRKAEVAGSKVVPALPESGQSEPGPPEVEGGTKATGNCFYVSMPSGPPDSSTDHSEAPMSPPQPDSLPAGQTEPQPQLQGGNDDPRRPSRSPPSLALRDVGMIFHTIEQLTLKLNRLKDMELAHRELLKSLGGESSGGTTPVGSFHTEAARWTDGSLSPPAKEPLASDSRNSHELGPCPEDGSDAPLEDSTADAAASPGP
| null | null |
actin cytoskeleton organization [GO:0030036]; establishment of cell polarity [GO:0030010]; G protein-coupled receptor signaling pathway [GO:0007186]; positive regulation of DNA-templated transcription [GO:0045893]; regulation of cell growth [GO:0001558]; regulation of small GTPase mediated signal transduction [GO:0051056]; Rho protein signal transduction [GO:0007266]; striated muscle contraction [GO:0006941]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]
|
G protein-coupled receptor binding [GO:0001664]; GTPase activator activity [GO:0005096]; guanyl-nucleotide exchange factor activity [GO:0005085]
|
PF00595;PF17838;PF09128;PF00621;
|
2.30.42.10;1.20.900.10;2.30.29.30;1.10.167.10;
| null |
PTM: Phosphorylated by MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14).; PTM: Ubiquitinated by the BCR(KLHL20) E3 ubiquitin ligase complex when previously phosphorylated by MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14), leading to its degradation, thereby restricting RhoA activity and facilitating growth cone spreading and neurite outgrowth. {ECO:0000269|PubMed:21670212}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10900204}. Membrane {ECO:0000269|PubMed:10900204}. Note=Translocated to the membrane upon stimulation.
| null | null | null | null | null |
FUNCTION: May play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13). Acts as guanine nucleotide exchange factor (GEF) for RhoA GTPase and may act as GTPase-activating protein (GAP) for GNA12 and GNA13. Involved in neurotrophin-induced neurite outgrowth. {ECO:0000269|PubMed:21670212}.
|
Homo sapiens (Human)
|
O15091
|
MRPP3_HUMAN
|
MTFYLFGIRSFPKLWKSPYLGLGPGHSYVSLFLADRCGIRNQQRLFSLKTMSPQNTKATNLIAKARYLRKDEGSNKQVYSVPHFFLAGAAKERSQMNSQTEDHALAPVRNTIQLPTQPLNSEEWDKLKEDLKENTGKTSFESWIISQMAGCHSSIDVAKSLLAWVAAKNNGIVSYDLLVKYLYLCVFHMQTSEVIDVFEIMKARYKTLEPRGYSLLIRGLIHSDRWREALLLLEDIKKVITPSKKNYNDCIQGALLHQDVNTAWNLYQELLGHDIVPMLETLKAFFDFGKDIKDDNYSNKLLDILSYLRNNQLYPGESFAHSIKTWFESVPGKQWKGQFTTVRKSGQCSGCGKTIESIQLSPEEYECLKGKIMRDVIDGGDQYRKTTPQELKRFENFIKSRPPFDVVIDGLNVAKMFPKVRESQLLLNVVSQLAKRNLRLLVLGRKHMLRRSSQWSRDEMEEVQKQASCFFADDISEDDPFLLYATLHSGNHCRFITRDLMRDHKACLPDAKTQRLFFKWQQGHQLAIVNRFPGSKLTFQRILSYDTVVQTTGDSWHIPYDEDLVERCSCEVPTKWLCLHQKT
|
3.1.26.5
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305|PubMed:25953853}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000305|PubMed:25953853}; Note=Binds 2 Mg(2+) or Mg(2+) ions per subunit. {ECO:0000305|PubMed:25953853};
|
mitochondrial tRNA 5'-end processing [GO:0097745]; tRNA 5'-leader removal [GO:0001682]
|
mitochondrial matrix [GO:0005759]; mitochondrial nucleoid [GO:0042645]; mitochondrial ribonuclease P complex [GO:0030678]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]
|
metal ion binding [GO:0046872]; ribonuclease P activity [GO:0004526]
|
PF16953;
|
3.40.50.11980;1.25.40.10;
|
PPR family, P subfamily
|
PTM: Degraded by LONP1 following mitochondrial unfolded protein response, probably leading to inhibit translation in mitochondrion. {ECO:0000269|PubMed:27350246}.
|
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:18984158}.
|
CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.; EC=3.1.26.5; Evidence={ECO:0000269|PubMed:25953853};
| null | null | null | null |
FUNCTION: Catalytic ribonuclease component of mitochondrial ribonuclease P, a complex composed of TRMT10C/MRPP1, HSD17B10/MRPP2 and PRORP/MRPP3, which cleaves tRNA molecules in their 5'-ends (PubMed:18984158, PubMed:25953853, PubMed:34715011). The presence of TRMT10C/MRPP1, HSD17B10/MRPP2 is required to catalyze tRNA molecules in their 5'-ends (PubMed:25953853). {ECO:0000269|PubMed:18984158, ECO:0000269|PubMed:25953853, ECO:0000269|PubMed:34715011}.
|
Homo sapiens (Human)
|
O15105
|
SMAD7_HUMAN
|
MFRTKRSALVRRLWRSRAPGGEDEEEGAGGGGGGGELRGEGATDSRAHGAGGGGPGRAGCCLGKAVRGAKGHHHPHPPAAGAGAAGGAEADLKALTHSVLKKLKERQLELLLQAVESRGGTRTACLLLPGRLDCRLGPGAPAGAQPAQPPSSYSLPLLLCKVFRWPDLRHSSEVKRLCCCESYGKINPELVCCNPHHLSRLCELESPPPPYSRYPMDFLKPTADCPDAVPSSAETGGTNYLAPGGLSDSQLLLEPGDRSHWCVVAYWEEKTRVGRLYCVQEPSLDIFYDLPQGNGFCLGQLNSDNKSQLVQKVRSKIGCGIQLTREVDGVWVYNRSSYPIFIKSATLDNPDSRTLLVHKVFPGFSIKAFDYEKAYSLQRPNDHEFMQQPWTGFTVQISFVKGWGQCYTRQFISSCPCWLEVIFNSR
| null | null |
adherens junction assembly [GO:0034333]; anatomical structure morphogenesis [GO:0009653]; artery morphogenesis [GO:0048844]; cell differentiation [GO:0030154]; cellular response to leukemia inhibitory factor [GO:1990830]; cellular response to transforming growth factor beta stimulus [GO:0071560]; negative regulation of activin receptor signaling pathway [GO:0032926]; negative regulation of BMP signaling pathway [GO:0030514]; negative regulation of cell migration [GO:0030336]; negative regulation of chondrocyte proliferation [GO:1902731]; negative regulation of epithelial to mesenchymal transition [GO:0010719]; negative regulation of ossification [GO:0030279]; negative regulation of peptidyl-serine phosphorylation [GO:0033137]; negative regulation of peptidyl-threonine phosphorylation [GO:0010801]; negative regulation of protein ubiquitination [GO:0031397]; negative regulation of SMAD protein signal transduction [GO:0060392]; negative regulation of T cell cytokine production [GO:0002725]; negative regulation of T-helper 17 cell differentiation [GO:2000320]; negative regulation of T-helper 17 type immune response [GO:2000317]; negative regulation of transcription by competitive promoter binding [GO:0010944]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; negative regulation of ubiquitin-protein transferase activity [GO:0051444]; positive regulation of cell-cell adhesion [GO:0022409]; positive regulation of chondrocyte hypertrophy [GO:1903043]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; protein stabilization [GO:0050821]; protein-containing complex localization [GO:0031503]; regulation of cardiac muscle contraction [GO:0055117]; regulation of epithelial to mesenchymal transition [GO:0010717]; regulation of transcription by RNA polymerase II [GO:0006357]; regulation of transforming growth factor beta receptor signaling pathway [GO:0017015]; regulation of ventricular cardiac muscle cell membrane depolarization [GO:0060373]; response to laminar fluid shear stress [GO:0034616]; SMAD protein signal transduction [GO:0060395]; transforming growth factor beta receptor signaling pathway [GO:0007179]; ureteric bud development [GO:0001657]; ventricular cardiac muscle tissue morphogenesis [GO:0055010]; ventricular septum morphogenesis [GO:0060412]
|
centrosome [GO:0005813]; chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; fibrillar center [GO:0001650]; heteromeric SMAD protein complex [GO:0071144]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]
|
activin receptor binding [GO:0070697]; beta-catenin binding [GO:0008013]; collagen binding [GO:0005518]; I-SMAD binding [GO:0070411]; metal ion binding [GO:0046872]; transcription corepressor activity [GO:0003714]; transcription regulator inhibitor activity [GO:0140416]; type I transforming growth factor beta receptor binding [GO:0034713]; ubiquitin ligase-substrate adaptor activity [GO:1990756]; ubiquitin protein ligase binding [GO:0031625]
|
PF03165;PF03166;
|
2.60.200.10;3.90.520.10;
|
Dwarfin/SMAD family
|
PTM: Phosphorylation on Ser-249 does not affect its stability, nuclear localization or inhibitory function in TGFB signaling; however it affects its ability to regulate transcription (By similarity). Phosphorylated by PDPK1. {ECO:0000250|UniProtKB:O35253, ECO:0000269|PubMed:17327236}.; PTM: Ubiquitinated by WWP1 (By similarity). Polyubiquitinated by RNF111, which is enhanced by AXIN1 and promotes proteasomal degradation (PubMed:14657019, PubMed:16601693). In response to TGF-beta, ubiquitinated by SMURF1; which promotes its degradation (PubMed:11278251). {ECO:0000250|UniProtKB:O35253, ECO:0000269|PubMed:11278251, ECO:0000269|PubMed:14657019, ECO:0000269|PubMed:16601693}.; PTM: Acetylation prevents ubiquitination and degradation mediated by SMURF1. {ECO:0000269|PubMed:12408818}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14657019, ECO:0000269|PubMed:16601693, ECO:0000269|PubMed:17327236}. Cytoplasm {ECO:0000269|PubMed:14657019, ECO:0000269|PubMed:16601693, ECO:0000269|PubMed:17327236}. Note=Interaction with NEDD4L or RNF111 induces translocation from the nucleus to the cytoplasm (PubMed:16601693). TGF-beta stimulates its translocation from the nucleus to the cytoplasm. PDPK1 inhibits its translocation from the nucleus to the cytoplasm in response to TGF-beta (PubMed:17327236). {ECO:0000269|PubMed:16601693, ECO:0000269|PubMed:17327236}.
| null | null | null | null | null |
FUNCTION: Antagonist of signaling by TGF-beta (transforming growth factor) type 1 receptor superfamily members; has been shown to inhibit TGF-beta (Transforming growth factor) and activin signaling by associating with their receptors thus preventing SMAD2 access (PubMed:21791611). Functions as an adapter to recruit SMURF2 to the TGF-beta receptor complex. Also acts by recruiting the PPP1R15A-PP1 complex to TGFBR1, which promotes its dephosphorylation. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator. {ECO:0000269|PubMed:11163210, ECO:0000269|PubMed:12023024, ECO:0000269|PubMed:14718519, ECO:0000269|PubMed:17327236, ECO:0000269|PubMed:21791611, ECO:0000269|PubMed:9892009}.
|
Homo sapiens (Human)
|
O15111
|
IKKA_HUMAN
|
MERPPGLRPGAGGPWEMRERLGTGGFGNVCLYQHRELDLKIAIKSCRLELSTKNRERWCHEIQIMKKLNHANVVKACDVPEELNILIHDVPLLAMEYCSGGDLRKLLNKPENCCGLKESQILSLLSDIGSGIRYLHENKIIHRDLKPENIVLQDVGGKIIHKIIDLGYAKDVDQGSLCTSFVGTLQYLAPELFENKPYTATVDYWSFGTMVFECIAGYRPFLHHLQPFTWHEKIKKKDPKCIFACEEMSGEVRFSSHLPQPNSLCSLVVEPMENWLQLMLNWDPQQRGGPVDLTLKQPRCFVLMDHILNLKIVHILNMTSAKIISFLLPPDESLHSLQSRIERETGINTGSQELLSETGISLDPRKPASQCVLDGVRGCDSYMVYLFDKSKTVYEGPFASRSLSDCVNYIVQDSKIQLPIIQLRKVWAEAVHYVSGLKEDYSRLFQGQRAAMLSLLRYNANLTKMKNTLISASQQLKAKLEFFHKSIQLDLERYSEQMTYGISSEKMLKAWKEMEEKAIHYAEVGVIGYLEDQIMSLHAEIMELQKSPYGRRQGDLMESLEQRAIDLYKQLKHRPSDHSYSDSTEMVKIIVHTVQSQDRVLKELFGHLSKLLGCKQKIIDLLPKVEVALSNIKEADNTVMFMQGKRQKEIWHLLKIACTQSSARSLVGSSLEGAVTPQTSAWLPPTSAEHDHSLSCVVTPQDGETSAQMIEENLNCLGHLSTIIHEANEEQGNSMMNLDWSWLTE
|
2.7.11.10
| null |
anatomical structure morphogenesis [GO:0009653]; canonical NF-kappaB signal transduction [GO:0007249]; cellular response to cadmium ion [GO:0071276]; cellular response to reactive oxygen species [GO:0034614]; cellular response to tumor necrosis factor [GO:0071356]; cellular response to virus [GO:0098586]; I-kappaB phosphorylation [GO:0007252]; immune response [GO:0006955]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; negative regulation of NF-kappaB transcription factor activity [GO:0032088]; non-canonical NF-kappaB signal transduction [GO:0038061]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of interferon-alpha production [GO:0032727]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein phosphorylation [GO:0006468]; response to acetate [GO:0010034]; response to amino acid [GO:0043200]; response to cholecystokinin [GO:0061847]; response to hydroperoxide [GO:0033194]; response to lipopolysaccharide [GO:0032496]; response to toxic substance [GO:0009636]; response to virus [GO:0009615]; response to xenobiotic stimulus [GO:0009410]; Rho protein signal transduction [GO:0007266]; skeletal muscle contraction [GO:0003009]; striated muscle cell differentiation [GO:0051146]; toll-like receptor 4 signaling pathway [GO:0034142]; tumor necrosis factor-mediated signaling pathway [GO:0033209]
|
CD40 receptor complex [GO:0035631]; cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; IkappaB kinase complex [GO:0008385]; nucleoplasm [GO:0005654]
|
ATP binding [GO:0005524]; IkappaB kinase activity [GO:0008384]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; protein kinase activity [GO:0004672]; protein serine/threonine kinase activity [GO:0004674]; protein-containing complex binding [GO:0044877]; scaffold protein binding [GO:0097110]; transferrin receptor binding [GO:1990459]
|
PF18397;PF12179;PF00069;
|
1.20.1270.250;6.10.250.2110;1.10.510.10;
|
Protein kinase superfamily, Ser/Thr protein kinase family, I-kappa-B kinase subfamily
|
PTM: Phosphorylated by MAP3K14/NIK, AKT and to a lesser extent by MEKK1, and dephosphorylated by PP2A. Autophosphorylated.; PTM: Ubiquitinated by TRIM56 via 'Lys-63'-linked ubiquitination, promoting activation of CHUK/IKKA. {ECO:0000269|PubMed:35952808}.; PTM: (Microbial infection) Acetylation of Thr-179 by Yersinia YopJ prevents phosphorylation and activation, thus blocking the I-kappa-B signaling pathway. {ECO:0000269|PubMed:17116858}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12789342, ECO:0000269|PubMed:30341167}. Nucleus {ECO:0000269|PubMed:12789342}. Note=Shuttles between the cytoplasm and the nucleus.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[I-kappa-B protein] = ADP + H(+) + O-phospho-L-seryl-[I-kappa-B protein]; Xref=Rhea:RHEA:19073, Rhea:RHEA-COMP:13698, Rhea:RHEA-COMP:13699, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.10; Evidence={ECO:0000269|PubMed:9244310, ECO:0000269|PubMed:9252186, ECO:0000269|PubMed:9346484};
| null | null | null | null |
FUNCTION: Serine kinase that plays an essential role in the NF-kappa-B signaling pathway which is activated by multiple stimuli such as inflammatory cytokines, bacterial or viral products, DNA damages or other cellular stresses (PubMed:18626576, PubMed:9244310, PubMed:9252186, PubMed:9346484). Acts as a part of the canonical IKK complex in the conventional pathway of NF-kappa-B activation and phosphorylates inhibitors of NF-kappa-B on serine residues (PubMed:18626576, PubMed:35952808, PubMed:9244310, PubMed:9252186, PubMed:9346484). These modifications allow polyubiquitination of the inhibitors and subsequent degradation by the proteasome (PubMed:18626576, PubMed:9244310, PubMed:9252186, PubMed:9346484). In turn, free NF-kappa-B is translocated into the nucleus and activates the transcription of hundreds of genes involved in immune response, growth control, or protection against apoptosis (PubMed:18626576, PubMed:9244310, PubMed:9252186, PubMed:9346484). Negatively regulates the pathway by phosphorylating the scaffold protein TAXBP1 and thus promoting the assembly of the A20/TNFAIP3 ubiquitin-editing complex (composed of A20/TNFAIP3, TAX1BP1, and the E3 ligases ITCH and RNF11) (PubMed:21765415). Therefore, CHUK plays a key role in the negative feedback of NF-kappa-B canonical signaling to limit inflammatory gene activation. As part of the non-canonical pathway of NF-kappa-B activation, the MAP3K14-activated CHUK/IKKA homodimer phosphorylates NFKB2/p100 associated with RelB, inducing its proteolytic processing to NFKB2/p52 and the formation of NF-kappa-B RelB-p52 complexes (PubMed:20501937). In turn, these complexes regulate genes encoding molecules involved in B-cell survival and lymphoid organogenesis. Participates also in the negative feedback of the non-canonical NF-kappa-B signaling pathway by phosphorylating and destabilizing MAP3K14/NIK. Within the nucleus, phosphorylates CREBBP and consequently increases both its transcriptional and histone acetyltransferase activities (PubMed:17434128). Modulates chromatin accessibility at NF-kappa-B-responsive promoters by phosphorylating histones H3 at 'Ser-10' that are subsequently acetylated at 'Lys-14' by CREBBP (PubMed:12789342). Additionally, phosphorylates the CREBBP-interacting protein NCOA3. Also phosphorylates FOXO3 and may regulate this pro-apoptotic transcription factor (PubMed:15084260). Phosphorylates RIPK1 at 'Ser-25' which represses its kinase activity and consequently prevents TNF-mediated RIPK1-dependent cell death (By similarity). Phosphorylates AMBRA1 following mitophagy induction, promoting AMBRA1 interaction with ATG8 family proteins and its mitophagic activity (PubMed:30217973). {ECO:0000250|UniProtKB:Q60680, ECO:0000269|PubMed:12789342, ECO:0000269|PubMed:15084260, ECO:0000269|PubMed:17434128, ECO:0000269|PubMed:20434986, ECO:0000269|PubMed:20501937, ECO:0000269|PubMed:21765415, ECO:0000269|PubMed:30217973, ECO:0000269|PubMed:35952808, ECO:0000269|PubMed:9244310, ECO:0000269|PubMed:9252186, ECO:0000269|PubMed:9346484, ECO:0000303|PubMed:18626576}.
|
Homo sapiens (Human)
|
O15116
|
LSM1_HUMAN
|
MNYMPGTASLIEDIDKKHLVLLRDGRTLIGFLRSIDQFANLVLHQTVERIHVGKKYGDIPRGIFVVRGENVVLLGEIDLEKESDTPLQQVSIEEILEEQRVEQQTKLEAEKLKVQALKDRGLSIPRADTLDEY
| null | null |
deadenylation-dependent decapping of nuclear-transcribed mRNA [GO:0000290]; histone mRNA catabolic process [GO:0071044]; mRNA processing [GO:0006397]; negative regulation of neuron differentiation [GO:0045665]; neuron differentiation [GO:0030182]; RNA splicing [GO:0008380]; RNA splicing, via transesterification reactions [GO:0000375]; stem cell population maintenance [GO:0019827]
|
axon [GO:0030424]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; Lsm1-7-Pat1 complex [GO:1990726]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; P-body [GO:0000932]; ribonucleoprotein complex [GO:1990904]
|
mRNA binding [GO:0003729]; pre-mRNA binding [GO:0036002]; RNA binding [GO:0003723]; RNA cap binding [GO:0000339]
|
PF01423;
|
2.30.30.100;
|
SnRNP Sm proteins family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:18172165}. Cytoplasm, P-body {ECO:0000305|PubMed:18172165}.
| null | null | null | null | null |
FUNCTION: Plays a role in the degradation of histone mRNAs, the only eukaryotic mRNAs that are not polyadenylated (PubMed:18172165). Probably also part of an LSm subunits-containing complex involved in the general process of mRNA degradation (By similarity). {ECO:0000250|UniProtKB:P47017, ECO:0000269|PubMed:18172165}.
|
Homo sapiens (Human)
|
O15117
|
FYB1_HUMAN
|
MAKYNTGGNPTEDVSVNSRPFRVTGPNSSSGIQARKNLFNNQGNASPPAGPSNVPKFGSPKPPVAVKPSSEEKPDKEPKPPFLKPTGAGQRFGTPASLTTRDPEAKVGFLKPVGPKPINLPKEDSKPTFPWPPGNKPSLHSVNQDHDLKPLGPKSGPTPPTSENEQKQAFPKLTGVKGKFMSASQDLEPKPLFPKPAFGQKPPLSTENSHEDESPMKNVSSSKGSPAPLGVRSKSGPLKPAREDSENKDHAGEISSLPFPGVVLKPAASRGGPGLSKNGEEKKEDRKIDAAKNTFQSKINQEELASGTPPARFPKAPSKLTVGGPWGQSQEKEKGDKNSATPKQKPLPPLFTLGPPPPKPNRPPNVDLTKFHKTSSGNSTSKGQTSYSTTSLPPPPPSHPASQPPLPASHPSQPPVPSLPPRNIKPPFDLKSPVNEDNQDGVTHSDGAGNLDEEQDSEGETYEDIEASKEREKKREKEEKKRLELEKKEQKEKEKKEQEIKKKFKLTGPIQVIHLAKACCDVKGGKNELSFKQGEQIEIIRITDNPEGKWLGRTARGSYGYIKTTAVEIDYDSLKLKKDSLGAPSRPIEDDQEVYDDVAEQDDISSHSQSGSGGIFPPPPDDDIYDGIEEEDADDGFPAPPKQLDMGDEVYDDVDTSDFPVSSAEMSQGTNVGKAKTEEKDLKKLKKQEKEEKDFRKKFKYDGEIRVLYSTKVTTSITSKKWGTRDLQVKPGESLEVIQTTDDTKVLCRNEEGKYGYVLRSYLADNDGEIYDDIADGCIYDND
| null | null |
immune response [GO:0006955]; integrin-mediated signaling pathway [GO:0007229]; protein localization to plasma membrane [GO:0072659]; T cell receptor signaling pathway [GO:0050852]
|
actin cytoskeleton [GO:0015629]; anchoring junction [GO:0070161]; cytosol [GO:0005829]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]
|
lipid binding [GO:0008289]; protein-containing complex binding [GO:0044877]; signaling receptor binding [GO:0005102]
|
PF14603;PF07653;
|
2.30.30.40;
| null |
PTM: T-cell receptor ligation leads to increased tyrosine phosphorylation.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9671755}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}. Cell junction {ECO:0000250|UniProtKB:O35601}. Note=Colocalizes with TMEM47 at cell-cell contacts in podocytes. {ECO:0000250|UniProtKB:O35601}.
| null | null | null | null | null |
FUNCTION: Acts as an adapter protein of the FYN and LCP2 signaling cascades in T-cells (By similarity). May play a role in linking T-cell signaling to remodeling of the actin cytoskeleton (PubMed:10747096, PubMed:16980616). Modulates the expression of IL2 (By similarity). Involved in platelet activation (By similarity). Prevents the degradation of SKAP1 and SKAP2 (PubMed:15849195). May be involved in high affinity immunoglobulin epsilon receptor signaling in mast cells (By similarity). {ECO:0000250|UniProtKB:D3ZIE4, ECO:0000250|UniProtKB:O35601, ECO:0000269|PubMed:10747096, ECO:0000269|PubMed:15849195, ECO:0000269|PubMed:16980616}.
|
Homo sapiens (Human)
|
O15118
|
NPC1_HUMAN
|
MTARGLALGLLLLLLCPAQVFSQSCVWYGECGIAYGDKRYNCEYSGPPKPLPKDGYDLVQELCPGFFFGNVSLCCDVRQLQTLKDNLQLPLQFLSRCPSCFYNLLNLFCELTCSPRQSQFLNVTATEDYVDPVTNQTKTNVKELQYYVGQSFANAMYNACRDVEAPSSNDKALGLLCGKDADACNATNWIEYMFNKDNGQAPFTITPVFSDFPVHGMEPMNNATKGCDESVDEVTAPCSCQDCSIVCGPKPQPPPPPAPWTILGLDAMYVIMWITYMAFLLVFFGAFFAVWCYRKRYFVSEYTPIDSNIAFSVNASDKGEASCCDPVSAAFEGCLRRLFTRWGSFCVRNPGCVIFFSLVFITACSSGLVFVRVTTNPVDLWSAPSSQARLEKEYFDQHFGPFFRTEQLIIRAPLTDKHIYQPYPSGADVPFGPPLDIQILHQVLDLQIAIENITASYDNETVTLQDICLAPLSPYNTNCTILSVLNYFQNSHSVLDHKKGDDFFVYADYHTHFLYCVRAPASLNDTSLLHDPCLGTFGGPVFPWLVLGGYDDQNYNNATALVITFPVNNYYNDTEKLQRAQAWEKEFINFVKNYKNPNLTISFTAERSIEDELNRESDSDVFTVVISYAIMFLYISLALGHMKSCRRLLVDSKVSLGIAGILIVLSSVACSLGVFSYIGLPLTLIVIEVIPFLVLAVGVDNIFILVQAYQRDERLQGETLDQQLGRVLGEVAPSMFLSSFSETVAFFLGALSVMPAVHTFSLFAGLAVFIDFLLQITCFVSLLGLDIKRQEKNRLDIFCCVRGAEDGTSVQASESCLFRFFKNSYSPLLLKDWMRPIVIAIFVGVLSFSIAVLNKVDIGLDQSLSMPDDSYMVDYFKSISQYLHAGPPVYFVLEEGHDYTSSKGQNMVCGGMGCNNDSLVQQIFNAAQLDNYTRIGFAPSSWIDDYFDWVKPQSSCCRVDNITDQFCNASVVDPACVRCRPLTPEGKQRPQGGDFMRFLPMFLSDNPNPKCGKGGHAAYSSAVNILLGHGTRVGATYFMTYHTVLQTSADFIDALKKARLIASNVTETMGINGSAYRVFPYSVFYVFYEQYLTIIDDTIFNLGVSLGAIFLVTMVLLGCELWSAVIMCATIAMVLVNMFGVMWLWGISLNAVSLVNLVMSCGISVEFCSHITRAFTVSMKGSRVERAEEALAHMGSSVFSGITLTKFGGIVVLAFAKSQIFQIFYFRMYLAMVLLGATHGLIFLPVLLSYIGPSVNKAKSCATEERYKGTERERLLNF
| null | null |
adult walking behavior [GO:0007628]; autophagy [GO:0006914]; bile acid metabolic process [GO:0008206]; cellular response to low-density lipoprotein particle stimulus [GO:0071404]; cellular response to steroid hormone stimulus [GO:0071383]; cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; cholesterol storage [GO:0010878]; cholesterol transport [GO:0030301]; cyclodextrin metabolic process [GO:2000900]; endocytosis [GO:0006897]; establishment of protein localization to membrane [GO:0090150]; gene expression [GO:0010467]; intestinal cholesterol absorption [GO:0030299]; intracellular cholesterol transport [GO:0032367]; intracellular lipid transport [GO:0032365]; liver development [GO:0001889]; lysosomal transport [GO:0007041]; macroautophagy [GO:0016236]; membrane raft organization [GO:0031579]; negative regulation of epithelial cell apoptotic process [GO:1904036]; negative regulation of macroautophagy [GO:0016242]; negative regulation of TORC1 signaling [GO:1904262]; neurogenesis [GO:0022008]; programmed cell death [GO:0012501]; protein glycosylation [GO:0006486]; response to cadmium ion [GO:0046686]; response to xenobiotic stimulus [GO:0009410]; symbiont entry into host cell [GO:0046718]
|
endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; Golgi apparatus [GO:0005794]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; membrane [GO:0016020]; membrane raft [GO:0045121]; nuclear envelope [GO:0005635]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]
|
cholesterol binding [GO:0015485]; signaling receptor activity [GO:0038023]; sterol transporter activity [GO:0015248]; transmembrane signaling receptor activity [GO:0004888]; virus receptor activity [GO:0001618]
|
PF16414;PF02460;PF12349;
|
1.20.1640.10;
|
Patched family
|
PTM: N-glycosylated. {ECO:0000269|PubMed:10821832, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19563754}.
|
SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000269|PubMed:12554680, ECO:0000269|PubMed:27378690}; Multi-pass membrane protein {ECO:0000269|PubMed:10821832, ECO:0000269|PubMed:27238017, ECO:0000269|PubMed:28784760}. Lysosome membrane {ECO:0000269|PubMed:17897319, ECO:0000269|PubMed:27378690, ECO:0000269|PubMed:9927649}; Multi-pass membrane protein {ECO:0000269|PubMed:10821832, ECO:0000269|PubMed:27238017, ECO:0000269|PubMed:28784760}.
|
CATALYTIC ACTIVITY: Reaction=cholesterol(in) = cholesterol(out); Xref=Rhea:RHEA:39747, ChEBI:CHEBI:16113; Evidence={ECO:0000269|PubMed:18772377};
| null | null | null | null |
FUNCTION: Intracellular cholesterol transporter which acts in concert with NPC2 and plays an important role in the egress of cholesterol from the endosomal/lysosomal compartment (PubMed:10821832, PubMed:12554680, PubMed:18772377, PubMed:27238017, PubMed:9211849, PubMed:9927649). Unesterified cholesterol that has been released from LDLs in the lumen of the late endosomes/lysosomes is transferred by NPC2 to the cholesterol-binding pocket in the N-terminal domain of NPC1 (PubMed:18772377, PubMed:19563754, PubMed:27238017, PubMed:27378690, PubMed:28784760, PubMed:9211849, PubMed:9927649). Cholesterol binds to NPC1 with the hydroxyl group buried in the binding pocket (PubMed:19563754). Binds oxysterol with higher affinity than cholesterol. May play a role in vesicular trafficking in glia, a process that may be crucial for maintaining the structural and functional integrity of nerve terminals (Probable). Inhibits cholesterol-mediated mTORC1 activation throught its interaction with SLC38A9 (PubMed:28336668). {ECO:0000269|PubMed:10821832, ECO:0000269|PubMed:12554680, ECO:0000269|PubMed:18772377, ECO:0000269|PubMed:19563754, ECO:0000269|PubMed:27238017, ECO:0000269|PubMed:27378690, ECO:0000269|PubMed:28336668, ECO:0000269|PubMed:28784760, ECO:0000269|PubMed:9211849, ECO:0000269|PubMed:9927649, ECO:0000305}.; FUNCTION: (Microbial infection) Acts as an endosomal entry receptor for ebolavirus. {ECO:0000269|PubMed:21866103, ECO:0000269|PubMed:25855742, ECO:0000269|PubMed:32855215}.
|
Homo sapiens (Human)
|
O15119
|
TBX3_HUMAN
|
MSLSMRDPVIPGTSMAYHPFLPHRAPDFAMSAVLGHQPPFFPALTLPPNGAAALSLPGALAKPIMDQLVGAAETGIPFSSLGPQAHLRPLKTMEPEEEVEDDPKVHLEAKELWDQFHKRGTEMVITKSGRRMFPPFKVRCSGLDKKAKYILLMDIIAADDCRYKFHNSRWMVAGKADPEMPKRMYIHPDSPATGEQWMSKVVTFHKLKLTNNISDKHGFTLAFPSDHATWQGNYSFGTQTILNSMHKYQPRFHIVRANDILKLPYSTFRTYLFPETEFIAVTAYQNDKITQLKIDNNPFAKGFRDTGNGRREKRKQLTLQSMRVFDERHKKENGTSDESSSEQAAFNCFAQASSPAASTVGTSNLKDLCPSEGESDAEAESKEEHGPEACDAAKISTTTSEEPCRDKGSPAVKAHLFAAERPRDSGRLDKASPDSRHSPATISSSTRGLGAEERRSPVREGTAPAKVEEARALPGKEAFAPLTVQTDAAAAHLAQGPLPGLGFAPGLAGQQFFNGHPLFLHPSQFAMGGAFSSMAAAGMGPLLATVSGASTGVSGLDSTAMASAAAAQGLSGASAATLPFHLQQHVLASQGLAMSPFGSLFPYPYTYMAAAAAASSAAASSSVHRHPFLNLNTMRPRLRYSPYSIPVPVPDGSSLLTTALPSMAAAAGPLDGKVAALAASPASVAVDSGSELNSRSSTLSSSSMSLSPKLCAEKEAATSELQSIQRLVSGLEAKPDRSRSASP
| null | null |
animal organ morphogenesis [GO:0009887]; anterior/posterior axis specification, embryo [GO:0008595]; atrioventricular bundle cell differentiation [GO:0003167]; atrioventricular canal development [GO:0036302]; atrioventricular canal morphogenesis [GO:1905222]; blood vessel development [GO:0001568]; branching involved in mammary gland duct morphogenesis [GO:0060444]; cardiac epithelial to mesenchymal transition [GO:0060317]; cardiac jelly development [GO:1905072]; cardiac muscle cell fate commitment [GO:0060923]; cell fate specification [GO:0001708]; cellular senescence [GO:0090398]; DNA-templated transcription [GO:0006351]; embryonic digit morphogenesis [GO:0042733]; embryonic forelimb morphogenesis [GO:0035115]; embryonic hindlimb morphogenesis [GO:0035116]; endocardial cushion formation [GO:0003272]; female genitalia development [GO:0030540]; follicle-stimulating hormone secretion [GO:0046884]; forelimb morphogenesis [GO:0035136]; heart looping [GO:0001947]; hepatoblast differentiation [GO:0061017]; in utero embryonic development [GO:0001701]; limbic system development [GO:0021761]; luteinizing hormone secretion [GO:0032275]; male genitalia development [GO:0030539]; mammary gland development [GO:0030879]; mammary placode formation [GO:0060596]; mesoderm morphogenesis [GO:0048332]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell proliferation involved in heart morphogenesis [GO:2000137]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of epithelial cell differentiation [GO:0030857]; negative regulation of myoblast differentiation [GO:0045662]; negative regulation of stem cell differentiation [GO:2000737]; negative regulation of transcription by RNA polymerase II [GO:0000122]; outflow tract morphogenesis [GO:0003151]; positive regulation of cell cycle [GO:0045787]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of stem cell proliferation [GO:2000648]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of protein complex stability [GO:0061635]; regulation of protein stability [GO:0031647]; regulation of transcription by RNA polymerase II [GO:0006357]; roof of mouth development [GO:0060021]; semicircular canal morphogenesis [GO:0048752]; sinoatrial node cell development [GO:0060931]; skeletal system development [GO:0001501]; smooth muscle cell differentiation [GO:0051145]; specification of animal organ position [GO:0010159]; stem cell population maintenance [GO:0019827]; stem cell proliferation [GO:0072089]; ureteric peristalsis [GO:0072105]; ventricular septum morphogenesis [GO:0060412]
|
chromatin [GO:0000785]; cilium [GO:0005929]; nucleus [GO:0005634]
|
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; sequence-specific DNA binding [GO:0043565]; sequence-specific double-stranded DNA binding [GO:1990837]
|
PF00907;PF12598;PF20627;
|
2.60.40.820;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00201}.
| null | null | null | null | null |
FUNCTION: Transcriptional repressor involved in developmental processes (PubMed:10468588). Binds to the palindromic T site 5'-TTCACACCTAGGTGTGAA-3' DNA sequence, or a half-site, which are present in the regulatory region of several genes (PubMed:12000749). Probably plays a role in limb pattern formation (PubMed:10468588). Required for mammary placode induction, and maintenance of the mammary buds during development (By similarity). Involved in branching morphogenesis in both developing lungs and adult mammary glands, via negative modulation of target genes; acting redundantly with TBX2 (By similarity). Required, together with TBX2, to maintain cell proliferation in the embryonic lung mesenchyme; perhaps acting downstream of SHH, BMP and TGFbeta signaling (By similarity). Involved in modulating early inner ear development, acting independently of, and also redundantly with, TBX2 in different subregions of the developing ear (By similarity). Acts as a negative regulator of PML function in cellular senescence (PubMed:22002537). {ECO:0000250|UniProtKB:P70324, ECO:0000269|PubMed:10468588, ECO:0000269|PubMed:12000749, ECO:0000269|PubMed:22002537}.
|
Homo sapiens (Human)
|
O15120
|
PLCB_HUMAN
|
MELWPCLAAALLLLLLLVQLSRAAEFYAKVALYCALCFTVSAVASLVCLLRHGGRTVENMSIIGWFVRSFKYFYGLRFEVRDPRRLQEARPCVIVSNHQSILDMMGLMEVLPERCVQIAKRELLFLGPVGLIMYLGGVFFINRQRSSTAMTVMADLGERMVRENLKVWIYPEGTRNDNGDLLPFKKGAFYLAVQAQVPIVPVVYSSFSSFYNTKKKFFTSGTVTVQVLEAIPTSGLTAADVPALVDTCHRAMRTTFLHISKTPQENGATAGSGVQPAQ
|
2.3.1.51
| null |
CDP-diacylglycerol biosynthetic process [GO:0016024]; epidermis development [GO:0008544]; phosphatidic acid biosynthetic process [GO:0006654]; phospholipid metabolic process [GO:0006644]; positive regulation of cytokine production [GO:0001819]; positive regulation of cytokine-mediated signaling pathway [GO:0001961]; response to xenobiotic stimulus [GO:0009410]; triglyceride biosynthetic process [GO:0019432]
|
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; plasma membrane [GO:0005886]; specific granule membrane [GO:0035579]
|
1-acylglycerol-3-phosphate O-acyltransferase activity [GO:0003841]
|
PF01553;
| null |
1-acyl-sn-glycerol-3-phosphate acyltransferase family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21873652}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:19709, ChEBI:CHEBI:57287, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342, ChEBI:CHEBI:58608; EC=2.3.1.51; Evidence={ECO:0000269|PubMed:15629135, ECO:0000269|PubMed:19075029, ECO:0000269|PubMed:21873652, ECO:0000269|PubMed:9242711}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19710; Evidence={ECO:0000305|PubMed:15629135, ECO:0000305|PubMed:19075029, ECO:0000305|PubMed:21873652, ECO:0000305|PubMed:9242711}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37131, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:74544, ChEBI:CHEBI:74546; Evidence={ECO:0000269|PubMed:15629135, ECO:0000269|PubMed:21873652}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37132; Evidence={ECO:0000305|PubMed:15629135, ECO:0000305|PubMed:21873652}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + hexadecanoyl-CoA = 1-(9Z)-octadecenoyl-2-hexadecanoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37143, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:74544, ChEBI:CHEBI:74551; Evidence={ECO:0000269|PubMed:21873652}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37144; Evidence={ECO:0000305|PubMed:21873652}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + heptadecanoyl-CoA = 1-(9Z)-octadecenoyl-2-heptadecanoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37155, ChEBI:CHEBI:57287, ChEBI:CHEBI:74307, ChEBI:CHEBI:74544, ChEBI:CHEBI:74558; Evidence={ECO:0000269|PubMed:21873652}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37156; Evidence={ECO:0000305|PubMed:21873652}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate = 1-(9Z)-octadecenoyl-2-(9Z,12Z)-octadecadienoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37159, ChEBI:CHEBI:57287, ChEBI:CHEBI:57383, ChEBI:CHEBI:74544, ChEBI:CHEBI:74563; Evidence={ECO:0000269|PubMed:21873652}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37160; Evidence={ECO:0000305|PubMed:21873652}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + tetradecanoyl-CoA = 1-(9Z)-octadecenoyl-2-tetradecanoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37171, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:74544, ChEBI:CHEBI:74579; Evidence={ECO:0000269|PubMed:21873652}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37172; Evidence={ECO:0000305|PubMed:21873652}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + pentadecanoyl-CoA = 1-(9Z)-octadecenoyl-2-pentadecanoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37175, ChEBI:CHEBI:57287, ChEBI:CHEBI:74309, ChEBI:CHEBI:74544, ChEBI:CHEBI:74578; Evidence={ECO:0000269|PubMed:21873652}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37176; Evidence={ECO:0000305|PubMed:21873652}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-phosphate = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:33187, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:57518, ChEBI:CHEBI:64839; Evidence={ECO:0000269|PubMed:21873652}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33188; Evidence={ECO:0000305|PubMed:21873652}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + 1-tetradecanoyl-sn-glycerol 3-phosphate = 1-tetradecanoyl-2-(9Z)-octadecenoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37187, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:72683, ChEBI:CHEBI:74586; Evidence={ECO:0000269|PubMed:21873652}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37188; Evidence={ECO:0000305|PubMed:21873652}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z,12Z,15Z)-octadecatrienoyl-sn-glycero-3-phosphate = 1-(9Z,12Z,15Z)-octadecatrienoyl-2-(9Z)-octadecenoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37139, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:74549, ChEBI:CHEBI:74550; Evidence={ECO:0000269|PubMed:21873652}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37140; Evidence={ECO:0000305|PubMed:21873652}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + 1-(6Z,9Z,12Z-octadecatrienoyl)-sn-glycero-3-phosphate = (6Z,9Z,12Z)-octadecatrienoyl-2-(9Z)-octadecenoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37179, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:74581, ChEBI:CHEBI:74582; Evidence={ECO:0000269|PubMed:21873652}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37180; Evidence={ECO:0000305|PubMed:21873652}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + 1-eicosanoyl-sn-glycero-3-phosphate = 1-eicosanoyl-2-(9Z)-octadecenoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37183, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:74583, ChEBI:CHEBI:74584; Evidence={ECO:0000269|PubMed:21873652}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37184; Evidence={ECO:0000305|PubMed:21873652}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-sn-glycero-3-phosphate + octadecanoyl-CoA = 1-hexadecanoyl-2-octadecanoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:35907, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394, ChEBI:CHEBI:57518, ChEBI:CHEBI:72857; Evidence={ECO:0000269|PubMed:9242711}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35908; Evidence={ECO:0000305|PubMed:9242711}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-phosphate = 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:35915, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368, ChEBI:CHEBI:57518, ChEBI:CHEBI:72864; Evidence={ECO:0000269|PubMed:9242711}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35916; Evidence={ECO:0000305|PubMed:9242711}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-sn-glycero-3-phosphate + hexadecanoyl-CoA = 1,2-dihexadecanoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:35903, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:57518, ChEBI:CHEBI:72859; Evidence={ECO:0000269|PubMed:9242711}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35904; Evidence={ECO:0000305|PubMed:9242711}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-sn-glycero-3-phosphate + tetradecanoyl-CoA = 1-hexadecanoyl-2-tetradecanoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:35899, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:57518, ChEBI:CHEBI:72858; Evidence={ECO:0000269|PubMed:9242711}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35900; Evidence={ECO:0000305|PubMed:9242711}; CATALYTIC ACTIVITY: Reaction=(11Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate = 1-(9Z)-octadecenoyl-2-(11Z)-octadecenoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37603, ChEBI:CHEBI:57287, ChEBI:CHEBI:74544, ChEBI:CHEBI:75121, ChEBI:CHEBI:75122; Evidence={ECO:0000269|PubMed:21873652}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37604; Evidence={ECO:0000305|PubMed:21873652};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=11.05 uM for C15:0-CoA {ECO:0000269|PubMed:21873652}; KM=523.97 uM for C18:0-CoA {ECO:0000269|PubMed:21873652}; KM=30.21 uM for C18:1-CoA {ECO:0000269|PubMed:21873652}; KM=8.29 uM for LPA sn-1 C18:1 {ECO:0000269|PubMed:21873652}; Vmax=51.61 nmol/min/mg enzyme for C15:0-CoA {ECO:0000269|PubMed:21873652}; Vmax=95.55 nmol/min/mg enzyme for C18:0-CoA {ECO:0000269|PubMed:21873652}; Vmax=73.81 nmol/min/mg enzyme for C18:1-CoA {ECO:0000269|PubMed:21873652}; Vmax=86.05 nmol/min/mg enzyme for LPA sn-1 C18:1 {ECO:0000269|PubMed:21873652};
|
PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
| null | null |
FUNCTION: Converts 1-acyl-sn-glycerol-3-phosphate (lysophosphatidic acid or LPA) into 1,2-diacyl-sn-glycerol-3-phosphate (phosphatidic acid or PA) by incorporating an acyl moiety at the sn-2 position of the glycerol backbone. {ECO:0000269|PubMed:15629135, ECO:0000269|PubMed:19075029, ECO:0000269|PubMed:21873652, ECO:0000269|PubMed:9242711}.
|
Homo sapiens (Human)
|
O15121
|
DEGS1_HUMAN
|
MGSRVSREDFEWVYTDQPHADRRREILAKYPEIKSLMKPDPNLIWIIIMMVLTQLGAFYIVKDLDWKWVIFGAYAFGSCINHSMTLAIHEIAHNAAFGNCKAMWNRWFGMFANLPIGIPYSISFKRYHMDHHRYLGADGVDVDIPTDFEGWFFCTAFRKFIWVILQPLFYAFRPLFINPKPITYLEVINTVAQVTFDILIYYFLGIKSLVYMLAASLLGLGLHPISGHFIAEHYMFLKGHETYSYYGPLNLLTFNVGYHNEHHDFPNIPGKSLPLVRKIAAEYYDNLPHYNSWIKVLYDFVMDDTISPYSRMKRHQKGEMVLE
|
1.14.19.17; 5.2.1.-
| null |
ceramide biosynthetic process [GO:0046513]; myelin maintenance [GO:0043217]; sphingolipid biosynthetic process [GO:0030148]; unsaturated fatty acid biosynthetic process [GO:0006636]
|
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; mitochondrial membrane [GO:0031966]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]; specific granule membrane [GO:0035579]
|
electron transfer activity [GO:0009055]; retinol isomerase activity [GO:0050251]; sphingolipid delta-4 desaturase activity [GO:0042284]
|
PF00487;PF08557;
| null |
Fatty acid desaturase type 1 family, DEGS subfamily
|
PTM: Myristoylation can target the enzyme to the mitochondria leading to an increase in ceramide levels. {ECO:0000269|PubMed:19647031}.
|
SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000269|PubMed:19647031, ECO:0000269|PubMed:30620338}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:19647031, ECO:0000269|PubMed:30620338, ECO:0000269|PubMed:9188692}; Multi-pass membrane protein {ECO:0000269|PubMed:19647031, ECO:0000269|PubMed:9188692}.
|
CATALYTIC ACTIVITY: Reaction=an N-acylsphinganine + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = an N-acylsphing-4-enine + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:46544, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:31488, ChEBI:CHEBI:52639; EC=1.14.19.17; Evidence={ECO:0000269|PubMed:11937514, ECO:0000269|PubMed:30620338}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46545; Evidence={ECO:0000305|PubMed:11937514}; CATALYTIC ACTIVITY: Reaction=all-trans-retinol = 11-cis-retinol; Xref=Rhea:RHEA:19141, ChEBI:CHEBI:16302, ChEBI:CHEBI:17336; Evidence={ECO:0000269|PubMed:23143414}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19142; Evidence={ECO:0000305|PubMed:23143414}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:19143; Evidence={ECO:0000250|UniProtKB:Q5F3C1}; CATALYTIC ACTIVITY: Reaction=all-trans-retinol = 9-cis-retinol; Xref=Rhea:RHEA:55348, ChEBI:CHEBI:17336, ChEBI:CHEBI:78272; Evidence={ECO:0000250|UniProtKB:Q5F3C1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55349; Evidence={ECO:0000250|UniProtKB:Q5F3C1}; CATALYTIC ACTIVITY: Reaction=all-trans-retinol = 13-cis-retinol; Xref=Rhea:RHEA:55352, ChEBI:CHEBI:17336, ChEBI:CHEBI:45479; Evidence={ECO:0000250|UniProtKB:Q5F3C1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55353; Evidence={ECO:0000250|UniProtKB:Q5F3C1}; CATALYTIC ACTIVITY: Reaction=11-cis-retinol = 13-cis-retinol; Xref=Rhea:RHEA:55356, ChEBI:CHEBI:16302, ChEBI:CHEBI:45479; Evidence={ECO:0000250|UniProtKB:Q5F3C1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55357; Evidence={ECO:0000250|UniProtKB:Q5F3C1}; CATALYTIC ACTIVITY: Reaction=11-cis-retinol = 9-cis-retinol; Xref=Rhea:RHEA:55360, ChEBI:CHEBI:16302, ChEBI:CHEBI:78272; Evidence={ECO:0000250|UniProtKB:Q5F3C1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55361; Evidence={ECO:0000250|UniProtKB:Q5F3C1};
| null | null | null | null |
FUNCTION: Has sphingolipid-delta-4-desaturase activity. Converts D-erythro-sphinganine to D-erythro-sphingosine (E-sphing-4-enine) (PubMed:11937514, PubMed:30620337, PubMed:30620338). Catalyzes the equilibrium isomerization of retinols (By similarity). {ECO:0000250|UniProtKB:Q5F3C1, ECO:0000269|PubMed:11937514, ECO:0000269|PubMed:30620337, ECO:0000269|PubMed:30620338}.
|
Homo sapiens (Human)
|
O15123
|
ANGP2_HUMAN
|
MWQIVFFTLSCDLVLAAAYNNFRKSMDSIGKKQYQVQHGSCSYTFLLPEMDNCRSSSSPYVSNAVQRDAPLEYDDSVQRLQVLENIMENNTQWLMKLENYIQDNMKKEMVEIQQNAVQNQTAVMIEIGTNLLNQTAEQTRKLTDVEAQVLNQTTRLELQLLEHSLSTNKLEKQILDQTSEINKLQDKNSFLEKKVLAMEDKHIIQLQSIKEEKDQLQVLVSKQNSIIEELEKKIVTATVNNSVLQKQQHDLMETVNNLLTMMSTSNSAKDPTVAKEEQISFRDCAEVFKSGHTTNGIYTLTFPNSTEEIKAYCDMEAGGGGWTIIQRREDGSVDFQRTWKEYKVGFGNPSGEYWLGNEFVSQLTNQQRYVLKIHLKDWEGNEAYSLYEHFYLSSEELNYRIHLKGLTGTAGKISSISQPGNDFSTKDGDNDKCICKCSQMLTGGWWFDACGPSNLNGMYYPQRQNTNKFNGIKWYYWKGSGYSLKATTMMIRPADF
| null | null |
angiogenesis [GO:0001525]; animal organ regeneration [GO:0031100]; cellular response to growth factor stimulus [GO:0071363]; gene expression [GO:0010467]; germ cell development [GO:0007281]; glomerulus vasculature development [GO:0072012]; maternal process involved in female pregnancy [GO:0060135]; negative regulation of angiogenesis [GO:0016525]; negative regulation of blood vessel endothelial cell migration [GO:0043537]; negative regulation of cell-substrate adhesion [GO:0010812]; negative regulation of positive chemotaxis [GO:0050928]; positive regulation of angiogenesis [GO:0045766]; response to activity [GO:0014823]; response to glucose [GO:0009749]; response to hypoxia [GO:0001666]; response to mechanical stimulus [GO:0009612]; response to organic cyclic compound [GO:0014070]; signal transduction [GO:0007165]; Tie signaling pathway [GO:0048014]
|
cell projection [GO:0042995]; collagen-containing extracellular matrix [GO:0062023]; extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
metal ion binding [GO:0046872]; receptor tyrosine kinase binding [GO:0030971]; signaling receptor binding [GO:0005102]
|
PF00147;
|
3.90.215.10;4.10.530.10;
| null | null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:32908006}.
| null | null | null | null | null |
FUNCTION: Binds to TEK/TIE2, competing for the ANGPT1 binding site, and modulating ANGPT1 signaling (PubMed:15284220, PubMed:19116766, PubMed:19223473, PubMed:9204896). Can induce tyrosine phosphorylation of TEK/TIE2 in the absence of ANGPT1 (PubMed:15284220, PubMed:19116766, PubMed:19223473, PubMed:9204896). In the absence of angiogenic inducers, such as VEGF, ANGPT2-mediated loosening of cell-matrix contacts may induce endothelial cell apoptosis with consequent vascular regression. In concert with VEGF, it may facilitate endothelial cell migration and proliferation, thus serving as a permissive angiogenic signal (PubMed:15284220, PubMed:19116766, PubMed:19223473, PubMed:9204896). Involved in the regulation of lymphangiogenesis (PubMed:32908006). {ECO:0000269|PubMed:15284220, ECO:0000269|PubMed:19116766, ECO:0000269|PubMed:19223473, ECO:0000269|PubMed:32908006, ECO:0000269|PubMed:9204896}.
|
Homo sapiens (Human)
|
O15126
|
SCAM1_HUMAN
|
MSDFDSNPFADPDLNNPFKDPSVTQVTRNVPPGLDEYNPFSDSRTPPPGGVKMPNVPNTQPAIMKPTEEHPAYTQIAKEHALAQAELLKRQEELERKAAELDRREREMQNLSQHGRKNNWPPLPSNFPVGPCFYQDFSVDIPVEFQKTVKLMYYLWMFHAVTLFLNIFGCLAWFCVDSARAVDFGLSILWFLLFTPCSFVCWYRPLYGAFRSDSSFRFFVFFFVYICQFAVHVLQAAGFHNWGNCGWISSLTGLNQNIPVGIMMIIIAALFTASAVISLVMFKKVHGLYRTTGASFEKAQQEFATGVMSNKTVQTAAANAASTAASSAAQNAFKGNQI
| null | null |
endocytosis [GO:0006897]; establishment of localization in cell [GO:0051649]; exocytosis [GO:0006887]; post-Golgi vesicle-mediated transport [GO:0006892]; protein transport [GO:0015031]
|
clathrin-coated vesicle [GO:0030136]; membrane [GO:0016020]; plasma membrane [GO:0005886]; recycling endosome membrane [GO:0055038]; specific granule membrane [GO:0035579]; synaptic vesicle membrane [GO:0030672]; trans-Golgi network [GO:0005802]; trans-Golgi network membrane [GO:0032588]; zymogen granule membrane [GO:0042589]
|
protein domain specific binding [GO:0019904]
|
PF04144;
| null |
SCAMP family
| null |
SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:15840657}; Multi-pass membrane protein {ECO:0000269|PubMed:15840657}. Recycling endosome membrane {ECO:0000269|PubMed:15840657}; Multi-pass membrane protein {ECO:0000269|PubMed:15840657}.
| null | null | null | null | null |
FUNCTION: Functions in post-Golgi recycling pathways. Acts as a recycling carrier to the cell surface.
|
Homo sapiens (Human)
|
O15127
|
SCAM2_HUMAN
|
MSAFDTNPFADPVDVNPFQDPSVTQLTNAPQGGLAEFNPFSETNAATTVPVTQLPGSSQPAVLQPSVEPTQPTPQAVVSAAQAGLLRQQEELDRKAAELERKERELQNTVANLHVRQNNWPPLPSWCPVKPCFYQDFSTEIPADYQRICKMLYYLWMLHSVTLFLNLLACLAWFSGNSSKGVDFGLSILWFLIFTPCAFLCWYRPIYKAFRSDNSFSFFVFFFVFFCQIGIYIIQLVGIPGLGDSGWIAALSTLDNHSLAISVIMMVVAGFFTLCAVLSVFLLQRVHSLYRRTGASFQQAQEEFSQGIFSSRTFHRAASSAAQGAFQGN
| null | null |
post-Golgi vesicle-mediated transport [GO:0006892]; protein transport [GO:0015031]
|
extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; recycling endosome membrane [GO:0055038]; trans-Golgi network membrane [GO:0032588]
| null |
PF04144;
| null |
SCAMP family
| null |
SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:15840657}; Multi-pass membrane protein {ECO:0000269|PubMed:15840657}. Recycling endosome membrane {ECO:0000269|PubMed:15840657}; Multi-pass membrane protein {ECO:0000269|PubMed:15840657}.
| null | null | null | null | null |
FUNCTION: Functions in post-Golgi recycling pathways. Acts as a recycling carrier to the cell surface.
|
Homo sapiens (Human)
|
O15130
|
NPFF_HUMAN
|
MDSRQAAALLVLLLLIDGGCAEGPGGQQEDQLSAEEDSEPLPPQDAQTSGSLLHYLLQAMERPGRSQAFLFQPQRFGRNTQGSWRNEWLSPRAGEGLNSQFWSLAAPQRFGKK
| null | null |
chemical synaptic transmission [GO:0007268]; excitatory postsynaptic potential [GO:0060079]; neuropeptide signaling pathway [GO:0007218]
|
axon terminus [GO:0043679]; dendrite [GO:0030425]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; perikaryon [GO:0043204]; postsynapse [GO:0098794]
|
G protein-coupled receptor binding [GO:0001664]; neuropeptide hormone activity [GO:0005184]; signaling receptor binding [GO:0005102]
|
PF15085;
| null |
FARP (FMRFamide related peptide) family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Morphine modulating peptides. Have wide-ranging physiologic effects, including the modulation of morphine-induced analgesia, elevation of arterial blood pressure, and increased somatostatin secretion from the pancreas. Neuropeptide FF potentiates and sensitizes ASIC1 and ASIC3 channels. {ECO:0000269|PubMed:11587714}.
|
Homo sapiens (Human)
|
O15131
|
IMA6_HUMAN
|
MDAMASPGKDNYRMKSYKNKALNPQEMRRRREEEGIQLRKQKREEQLFKRRNVYLPRNDESMLESPIQDPDISSTVPIPEEEVVTTDMVQMIFSNNADQQLTATQKFRKLLSKEPNPPIDQVIQKPGVVQRFVKFLERNENCTLQFEAAWALTNIASGTFLHTKVVIETGAVPIFIKLLNSEHEDVQEQAVWALGNIAGDNAECRDFVLNCEILPPLLELLTNSNRLTTTRNAVWALSNLCRGKNPPPNFSKVSPCLNVLSRLLFSSDPDVLADVCWALSYLSDGPNDKIQAVIDSGVCRRLVELLMHNDYKVVSPALRAVGNIVTGDDIQTQVILNCSALPCLLHLLSSPKESIRKEACWTVSNITAGNRAQIQAVIDANIFPVLIEILQKAEFRTRKEAAWAITNATSGGTPEQIRYLVALGCIKPLCDLLTVMDSKIVQVALNGLENILRLGEQESKQNGIGINPYCALIEEAYGLDKIEFLQSHENQEIYQKAFDLIEHYFGVEEDDPSIVPQVDENQQQFIFQQQEAPMDGFQL
| null | null |
NLS-bearing protein import into nucleus [GO:0006607]; protein import into nucleus [GO:0006606]
|
cytosol [GO:0005829]; NLS-dependent protein nuclear import complex [GO:0042564]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
nuclear import signal receptor activity [GO:0061608]; nuclear localization sequence binding [GO:0008139]
|
PF00514;PF16186;PF01749;
|
1.20.5.690;1.25.10.10;
|
Importin alpha family
| null |
SUBCELLULAR LOCATION: Cytoplasm.
| null | null | null | null | null |
FUNCTION: Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Mediates nuclear import of STAT1 homodimers and STAT1/STAT2 heterodimers by recognizing non-classical NLSs of STAT1 and STAT2 through ARM repeats 8-9. Recognizes influenza A virus nucleoprotein through ARM repeat 7-9 In vitro, mediates the nuclear import of human cytomegalovirus UL84 by recognizing a non-classical NLS.
|
Homo sapiens (Human)
|
O15143
|
ARC1B_HUMAN
|
MAYHSFLVEPISCHAWNKDRTQIAICPNNHEVHIYEKSGAKWTKVHELKEHNGQVTGIDWAPESNRIVTCGTDRNAYVWTLKGRTWKPTLVILRINRAARCVRWAPNENKFAVGSGSRVISICYFEQENDWWVCKHIKKPIRSTVLSLDWHPNNVLLAAGSCDFKCRIFSAYIKEVEERPAPTPWGSKMPFGELMFESSSSCGWVHGVCFSASGSRVAWVSHDSTVCLADADKKMAVATLASETLPLLALTFITDNSLVAAGHDCFPVLFTYDAAAGMLSFGGRLDVPKQSSQRGLTARERFQNLDKKASSEGGTAAGAGLDSLHKNSVSQISVLSGGKAKCSQFCTTGMDGGMSIWDVKSLESALKDLKIK
| null | null |
Arp2/3 complex-mediated actin nucleation [GO:0034314]; response to estradiol [GO:0032355]; response to estrogen [GO:0043627]
|
actin cytoskeleton [GO:0015629]; Arp2/3 protein complex [GO:0005885]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; nucleus [GO:0005634]; tubulobulbar complex [GO:0036284]
|
actin filament binding [GO:0051015]; structural constituent of cytoskeleton [GO:0005200]
|
PF00400;
|
2.130.10.10;
|
WD repeat ARPC1 family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11741539, ECO:0000269|PubMed:9230079}. Nucleus {ECO:0000269|PubMed:29925947}.
| null | null | null | null | null |
FUNCTION: Component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF) (PubMed:11741539, PubMed:9230079). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility (PubMed:11741539, PubMed:9230079). In addition to its role in the cytoplasmic cytoskeleton, the Arp2/3 complex also promotes actin polymerization in the nucleus, thereby regulating gene transcription and repair of damaged DNA (PubMed:29925947). The Arp2/3 complex promotes homologous recombination (HR) repair in response to DNA damage by promoting nuclear actin polymerization, leading to drive motility of double-strand breaks (DSBs) (PubMed:29925947). {ECO:0000269|PubMed:11741539, ECO:0000269|PubMed:29925947, ECO:0000269|PubMed:9230079}.
|
Homo sapiens (Human)
|
O15144
|
ARPC2_HUMAN
|
MILLEVNNRIIEETLALKFENAAAGNKPEAVEVTFADFDGVLYHISNPNGDKTKVMVSISLKFYKELQAHGADELLKRVYGSFLVNPESGYNVSLLYDLENLPASKDSIVHQAGMLKRNCFASVFEKYFQFQEEGKEGENRAVIHYRDDETMYVESKKDRVTVVFSTVFKDDDDVVIGKVFMQEFKEGRRASHTAPQVLFSHREPPLELKDTDAAVGDNIGYITFVLFPRHTNASARDNTINLIHTFRDYLHYHIKCSKAYIHTRMRAKTSDFLKVLNRARPDAEKKEMKTITGKTFSSR
| null | null |
actin filament polymerization [GO:0030041]; actin polymerization-dependent cell motility [GO:0070358]; Arp2/3 complex-mediated actin nucleation [GO:0034314]; positive regulation of actin filament polymerization [GO:0030838]; positive regulation of lamellipodium assembly [GO:0010592]; positive regulation of substrate adhesion-dependent cell spreading [GO:1900026]
|
actin cytoskeleton [GO:0015629]; Arp2/3 protein complex [GO:0005885]; cytosol [GO:0005829]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; glutamatergic synapse [GO:0098978]; lamellipodium [GO:0030027]; muscle cell projection membrane [GO:0036195]; neuron projection [GO:0043005]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; site of double-strand break [GO:0035861]
|
actin filament binding [GO:0051015]; structural constituent of cytoskeleton [GO:0005200]
|
PF04045;
|
3.30.1460.20;
|
ARPC2 family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9230079}. Cell projection {ECO:0000269|PubMed:9230079}. Synapse, synaptosome {ECO:0000250|UniProtKB:Q9CVB6}. Nucleus {ECO:0000269|PubMed:29925947}.
| null | null | null | null | null |
FUNCTION: Actin-binding component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF) (PubMed:9230079). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility (PubMed:9230079). Seems to contact the mother actin filament (PubMed:9230079). In addition to its role in the cytoplasmic cytoskeleton, the Arp2/3 complex also promotes actin polymerization in the nucleus, thereby regulating gene transcription and repair of damaged DNA (PubMed:29925947). The Arp2/3 complex promotes homologous recombination (HR) repair in response to DNA damage by promoting nuclear actin polymerization, leading to drive motility of double-strand breaks (DSBs) (PubMed:29925947). {ECO:0000269|PubMed:29925947, ECO:0000269|PubMed:9230079}.
|
Homo sapiens (Human)
|
O15145
|
ARPC3_HUMAN
|
MPAYHSSLMDPDTKLIGNMALLPIRSQFKGPAPRETKDTDIVDEAIYYFKANVFFKNYEIKNEADRTLIYITLYISECLKKLQKCNSKSQGEKEMYTLGITNFPIPGEPGFPLNAIYAKPANKQEDEVMRAYLQQLRQETGLRLCEKVFDPQNDKPSKWWTCFVKRQFMNKSLSGPGQ
| null | null |
actin polymerization-dependent cell motility [GO:0070358]; Arp2/3 complex-mediated actin nucleation [GO:0034314]; cellular response to nerve growth factor stimulus [GO:1990090]; regulation of actin filament polymerization [GO:0030833]
|
actin cytoskeleton [GO:0015629]; Arp2/3 protein complex [GO:0005885]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; filamentous actin [GO:0031941]; focal adhesion [GO:0005925]; growth cone leading edge [GO:0061850]; lamellipodium [GO:0030027]; membrane [GO:0016020]; nucleus [GO:0005634]; site of double-strand break [GO:0035861]
|
actin filament binding [GO:0051015]; structural constituent of cytoskeleton [GO:0005200]
|
PF04062;
|
1.10.1760.10;
|
ARPC3 family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9230079, ECO:0000269|PubMed:9359840}. Cell projection {ECO:0000269|PubMed:9230079, ECO:0000269|PubMed:9359840}. Nucleus {ECO:0000269|PubMed:29925947}.
| null | null | null | null | null |
FUNCTION: Component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF) (PubMed:9230079). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility (PubMed:9230079). In addition to its role in the cytoplasmic cytoskeleton, the Arp2/3 complex also promotes actin polymerization in the nucleus, thereby regulating gene transcription and repair of damaged DNA (PubMed:29925947). The Arp2/3 complex promotes homologous recombination (HR) repair in response to DNA damage by promoting nuclear actin polymerization, leading to drive motility of double-strand breaks (DSBs) (PubMed:29925947). {ECO:0000269|PubMed:29925947, ECO:0000269|PubMed:9230079}.
|
Homo sapiens (Human)
|
O15146
|
MUSK_HUMAN
|
MRELVNIPLVHILTLVAFSGTEKLPKAPVITTPLETVDALVEEVATFMCAVESYPQPEISWTRNKILIKLFDTRYSIRENGQLLTILSVEDSDDGIYCCTANNGVGGAVESCGALQVKMKPKITRPPINVKIIEGLKAVLPCTTMGNPKPSVSWIKGDSPLRENSRIAVLESGSLRIHNVQKEDAGQYRCVAKNSLGTAYSKVVKLEVEVFARILRAPESHNVTFGSFVTLHCTATGIPVPTITWIENGNAVSSGSIQESVKDRVIDSRLQLFITKPGLYTCIATNKHGEKFSTAKAAATISIAEWSKPQKDNKGYCAQYRGEVCNAVLAKDALVFLNTSYADPEEAQELLVHTAWNELKVVSPVCRPAAEALLCNHIFQECSPGVVPTPIPICREYCLAVKELFCAKEWLVMEEKTHRGLYRSEMHLLSVPECSKLPSMHWDPTACARLPHLDYNKENLKTFPPMTSSKPSVDIPNLPSSSSSSFSVSPTYSMTVIISIMSSFAIFVLLTITTLYCCRRRKQWKNKKRESAAVTLTTLPSELLLDRLHPNPMYQRMPLLLNPKLLSLEYPRNNIEYVRDIGEGAFGRVFQARAPGLLPYEPFTMVAVKMLKEEASADMQADFQREAALMAEFDNPNIVKLLGVCAVGKPMCLLFEYMAYGDLNEFLRSMSPHTVCSLSHSDLSMRAQVSSPGPPPLSCAEQLCIARQVAAGMAYLSERKFVHRDLATRNCLVGENMVVKIADFGLSRNIYSADYYKANENDAIPIRWMPPESIFYNRYTTESDVWAYGVVLWEIFSYGLQPYYGMAHEEVIYYVRDGNILSCPENCPVELYNLMRLCWSKLPADRPSFTSIHRILERMCERAEGTVSV
|
2.7.10.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:25029443};
|
cell differentiation [GO:0030154]; memory [GO:0007613]; neuromuscular junction development [GO:0007528]; positive regulation of gene expression [GO:0010628]; positive regulation of neuron projection development [GO:0010976]; positive regulation of protein geranylgeranylation [GO:2000541]; positive regulation of protein phosphorylation [GO:0001934]; protein autophosphorylation [GO:0046777]; regulation of synaptic assembly at neuromuscular junction [GO:0008582]; skeletal muscle acetylcholine-gated channel clustering [GO:0071340]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]
|
neuromuscular junction [GO:0031594]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; receptor complex [GO:0043235]
|
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein tyrosine kinase activity [GO:0004713]; transmembrane receptor protein tyrosine kinase activity [GO:0004714]; Wnt-protein binding [GO:0017147]
|
PF01392;PF07679;PF13927;PF07714;
|
1.10.2000.10;2.60.40.10;1.10.510.10;
|
Protein kinase superfamily, Tyr protein kinase family
|
PTM: Ubiquitinated by PDZRN3. Ubiquitination promotes endocytosis and lysosomal degradation (By similarity). {ECO:0000250}.; PTM: Phosphorylated (By similarity). Phosphorylation is induced by AGRIN in a LRP4-dependent manner (By similarity). Autophosphorylated (PubMed:25029443). Autophosphorylation at Tyr-554 is required for interaction with DOK7 which in turn stimulates the phosphorylation and the activation of MUSK (By similarity). {ECO:0000250|UniProtKB:Q61006, ECO:0000269|PubMed:25029443}.; PTM: Neddylated. {ECO:0000269|PubMed:20596523}.
|
SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000269|PubMed:23326516}; Single-pass type I membrane protein {ECO:0000305}. Note=Colocalizes with acetylcholine receptors (AChR) to the postsynaptic cell membrane of the neuromuscular junction. {ECO:0000269|PubMed:23326516}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10028, ECO:0000269|PubMed:25029443};
| null | null | null | null |
FUNCTION: Receptor tyrosine kinase which plays a central role in the formation and the maintenance of the neuromuscular junction (NMJ), the synapse between the motor neuron and the skeletal muscle (PubMed:25537362). Recruitment of AGRIN by LRP4 to the MUSK signaling complex induces phosphorylation and activation of MUSK, the kinase of the complex. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. May regulate AChR phosphorylation and clustering through activation of ABL1 and Src family kinases which in turn regulate MUSK. DVL1 and PAK1 that form a ternary complex with MUSK are also important for MUSK-dependent regulation of AChR clustering. May positively regulate Rho family GTPases through FNTA. Mediates the phosphorylation of FNTA which promotes prenylation, recruitment to membranes and activation of RAC1 a regulator of the actin cytoskeleton and of gene expression. Other effectors of the MUSK signaling include DNAJA3 which functions downstream of MUSK. May also play a role within the central nervous system by mediating cholinergic responses, synaptic plasticity and memory formation (By similarity). {ECO:0000250, ECO:0000269|PubMed:25537362}.
|
Homo sapiens (Human)
|
O15151
|
MDM4_HUMAN
|
MTSFSTSAQCSTSDSACRISPGQINQVRPKLPLLKILHAAGAQGEMFTVKEVMHYLGQYIMVKQLYDQQEQHMVYCGGDLLGELLGRQSFSVKDPSPLYDMLRKNLVTLATATTDAAQTLALAQDHSMDIPSQDQLKQSAEESSTSRKRTTEDDIPTLPTSEHKCIHSREDEDLIENLAQDETSRLDLGFEEWDVAGLPWWFLGNLRSNYTPRSNGSTDLQTNQDVGTAIVSDTTDDLWFLNESVSEQLGVGIKVEAADTEQTSEEVGKVSDKKVIEVGKNDDLEDSKSLSDDTDVEVTSEDEWQCTECKKFNSPSKRYCFRCWALRKDWYSDCSKLTHSLSTSDITAIPEKENEGNDVPDCRRTISAPVVRPKDAYIKKENSKLFDPCNSVEFLDLAHSSESQETISSMGEQLDNLSEQRTDTENMEDCQNLLKPCSLCEKRPRDGNIIHGRTGHLVTCFHCARRLKKAGASCPICKKEIQLVIKVFIA
| null | null |
atrial septum development [GO:0003283]; atrioventricular valve morphogenesis [GO:0003181]; cellular response to hypoxia [GO:0071456]; DNA damage response, signal transduction by p53 class mediator [GO:0030330]; endocardial cushion morphogenesis [GO:0003203]; heart valve development [GO:0003170]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of protein catabolic process [GO:0042177]; negative regulation of transcription by RNA polymerase II [GO:0000122]; protein stabilization [GO:0050821]; protein ubiquitination [GO:0016567]; protein-containing complex assembly [GO:0065003]; regulation of cell cycle [GO:0051726]; ventricular septum development [GO:0003281]
|
nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription repressor complex [GO:0017053]
|
enzyme binding [GO:0019899]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270]
|
PF13920;PF00641;
|
1.10.245.10;3.30.40.10;2.30.30.380;
|
MDM2/MDM4 family
|
PTM: Phosphorylated. Phosphorylation at Ser-367 promotes interaction with YWHAG and subsequent ubiquitination and degradation. Phosphorylation at Ser-342 also induces ubiquitination and degradation but to a lower extent. {ECO:0000269|PubMed:16163388, ECO:0000269|PubMed:16511572, ECO:0000269|PubMed:19838211}.; PTM: Ubiquitinated and degraded by MDM2. Deubiquitination by USP2 on the other hand stabilizes the MDM4 protein. {ECO:0000269|PubMed:19838211}.
|
SUBCELLULAR LOCATION: Nucleus.
| null | null | null | null | null |
FUNCTION: Along with MDM2, contributes to TP53 regulation (PubMed:32300648). Inhibits p53/TP53- and TP73/p73-mediated cell cycle arrest and apoptosis by binding its transcriptional activation domain. Inhibits degradation of MDM2. Can reverse MDM2-targeted degradation of TP53 while maintaining suppression of TP53 transactivation and apoptotic functions. {ECO:0000269|PubMed:16163388, ECO:0000269|PubMed:16511572, ECO:0000269|PubMed:32300648}.
|
Homo sapiens (Human)
|
O15155
|
BET1_HUMAN
|
MRRAGLGEGVPPGNYGNYGYANSGYSACEEENERLTESLRSKVTAIKSLSIEIGHEVKTQNKLLAEMDSQFDSTTGFLGKTMGKLKILSRGSQTKLLCYMMLFSLFVFFIIYWIIKLR
| null | null |
endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; protein transport [GO:0015031]; vesicle fusion with Golgi apparatus [GO:0048280]
|
endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; Golgi membrane [GO:0000139]; membrane [GO:0016020]; SNARE complex [GO:0031201]; transport vesicle [GO:0030133]
|
SNAP receptor activity [GO:0005484]
| null |
1.20.5.110;
|
BET1 family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Golgi apparatus, cis-Golgi network membrane {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}. Note=Concentrated most in the intermediate compartment/cis-Golgi network and the cis-Golgi cisternae 1 and 2. Greatly reduced in concentration at the trans end of the Golgi apparatus (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Required for vesicular transport from the ER to the Golgi complex. Functions as a SNARE involved in the docking process of ER-derived vesicles with the cis-Golgi membrane (By similarity). {ECO:0000250}.
|
Homo sapiens (Human)
|
O15156
|
ZBT7B_HUMAN
|
MGSPEDDLIGIPFPDHSSELLSCLNEQRQLGHLCDLTIRTQGLEYRTHRAVLAACSHYFKKLFTEGGGGAVMGAGGSGTATGGAGAGVCELDFVGPEALGALLEFAYTATLTTSSANMPAVLQAARLLEIPCVIAACMEILQGSGLEAPSPDEDDCERARQYLEAFATATASGVPNGEDSPPQVPLPPPPPPPPRPVARRSRKPRKAFLQTKGARANHLVPEVPTVPAHPLTYEEEEVAGRVGSSGGSGPGDSYSPPTGTASPPEGPQSYEPYEGEEEEEELVYPPAYGLAQGGGPPLSPEELGSDEDAIDPDLMAYLSSLHQDNLAPGLDSQDKLVRKRRSQMPQECPVCHKIIHGAGKLPRHMRTHTGEKPFACEVCGVRFTRNDKLKIHMRKHTGERPYSCPHCPARFLHSYDLKNHMHLHTGDRPYECHLCHKAFAKEDHLQRHLKGQNCLEVRTRRRRKDDAPPHYPPPSTAAASPAGLDLSNGHLDTFRLSLARFWEQSAPTGPPVSTPGPPDDDEEEGAPTTPQAEGAMESS
| null | null |
adaptive thermogenesis [GO:1990845]; ectoderm development [GO:0007398]; lactation [GO:0007595]; negative regulation of CD8-positive, alpha-beta T cell differentiation [GO:0043377]; negative regulation of gene expression [GO:0010629]; negative regulation of NK T cell proliferation [GO:0051141]; negative regulation of T-helper 17 cell differentiation [GO:2000320]; negative regulation of transcription by RNA polymerase II [GO:0000122]; NK T cell differentiation [GO:0001865]; positive regulation of brown fat cell differentiation [GO:0090336]; positive regulation of CD4-positive, alpha-beta T cell differentiation [GO:0043372]; positive regulation of cold-induced thermogenesis [GO:0120162]; positive regulation of gene expression [GO:0010628]; positive regulation of insulin receptor signaling pathway [GO:0046628]; positive regulation of interleukin-17 production [GO:0032740]; positive regulation of SREBP signaling pathway [GO:2000640]; regulation of transcription by RNA polymerase II [GO:0006357]; response to insulin [GO:0032868]; transcription by RNA polymerase II [GO:0006366]
|
nucleoplasm [GO:0005654]
|
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity [GO:0001217]; histone deacetylase binding [GO:0042826]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific double-stranded DNA binding [GO:1990837]
|
PF00651;PF00096;
|
3.30.160.60;
| null |
PTM: Acetylated directly and specifically by EP300 (PubMed:20810990). EP300-mediated acetylation of Lys-206, Lys-212 and Lys-335 stabilizes the protein by antagonizing ubiquitin conjugation (By similarity). {ECO:0000250|UniProtKB:Q64321, ECO:0000269|PubMed:20810990}.; PTM: Ubiquitinated, leading to proteasomal degradation (PubMed:20810990). Competes with acetylation on Lys-206, Lys-212 and Lys-335 (By similarity). {ECO:0000250|UniProtKB:Q64321, ECO:0000269|PubMed:20810990}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q64321}.
| null | null | null | null | null |
FUNCTION: Transcription regulator that acts as a key regulator of lineage commitment of immature T-cell precursors. Exerts distinct biological functions in the mammary epithelial cells and T cells in a tissue-specific manner. Necessary and sufficient for commitment of CD4 lineage, while its absence causes CD8 commitment. Development of immature T-cell precursors (thymocytes) to either the CD4 helper or CD8 killer T-cell lineages correlates precisely with their T-cell receptor specificity for major histocompatibility complex class II or class I molecules, respectively. Cross-antagonism between ZBTB7B and CBF complexes are determinative to CD4 versus CD8 cell fate decision. Suppresses RUNX3 expression and imposes CD4+ lineage fate by inducing the SOCS suppressors of cytokine signaling. induces, as a transcriptional activator, SOCS genes expression which represses RUNX3 expression and promotes the CD4+ lineage fate. During CD4 lineage commitment, associates with multiple sites at the CD8 locus, acting as a negative regulator of the CD8 promoter and enhancers by epigenetic silencing through the recruitment of class II histone deacetylases, such as HDAC4 and HDAC5, to these loci. Regulates the development of IL17-producing CD1d-restricted naural killer (NK) T cells. Also functions as an important metabolic regulator in the lactating mammary glands. Critical feed-forward regulator of insulin signaling in mammary gland lactation, directly regulates expression of insulin receptor substrate-1 (IRS-1) and insulin-induced Akt-mTOR-SREBP signaling (By similarity). Transcriptional repressor of the collagen COL1A1 and COL1A2 genes. May also function as a repressor of fibronectin and possibly other extracellular matrix genes (PubMed:9370309). Potent driver of brown fat development, thermogenesis and cold-induced beige fat formation. Recruits the brown fat lncRNA 1 (Blnc1):HNRNPU ribonucleoprotein complex to activate thermogenic gene expression in brown and beige adipocytes (By similarity). {ECO:0000250|UniProtKB:Q64321, ECO:0000269|PubMed:9370309}.
|
Homo sapiens (Human)
|
O15160
|
RPAC1_HUMAN
|
MAASQAVEEMRSRVVLGEFGVRNVHTTDFPGNYSGYDDAWDQDRFEKNFRVDVVHMDENSLEFDMVGIDAAIANAFRRILLAEVPTMAVEKVLVYNNTSIVQDEILAHRLGLIPIHADPRLFEYRNQGDEEGTEIDTLQFRLQVRCTRNPHAAKDSSDPNELYVNHKVYTRHMTWIPLGNQADLFPEGTIRPVHDDILIAQLRPGQEIDLLMHCVKGIGKDHAKFSPVATASYRLLPDITLLEPVEGEAAEELSRCFSPGVIEVQEVQGKKVARVANPRLDTFSREIFRNEKLKKVVRLARVRDHYIFSVESTGVLPPDVLVSEAIKVLMGKCRRFLDELDAVQMD
| null | null |
transcription by RNA polymerase I [GO:0006360]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; fibrillar center [GO:0001650]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA polymerase I complex [GO:0005736]; RNA polymerase III complex [GO:0005666]
|
DNA binding [GO:0003677]; DNA-directed 5'-3' RNA polymerase activity [GO:0003899]; protein dimerization activity [GO:0046983]; RNA polymerase I activity [GO:0001054]; RNA polymerase III activity [GO:0001056]
|
PF01000;PF01193;
|
2.170.120.12;3.30.1360.10;
|
Archaeal Rpo3/eukaryotic RPB3 RNA polymerase subunit family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26151409, ECO:0000269|PubMed:33335104}. Nucleus, nucleolus {ECO:0000269|PubMed:34887565}. Cytoplasm, cytosol {ECO:0000269|PubMed:33335104}.
| null | null | null | null | null |
FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I and III which synthesize ribosomal RNA precursors and short non-coding RNAs including 5S rRNA, snRNAs, tRNAs and miRNAs, respectively. POLR1C/RPAC1 is part of the polymerase core and may function as a clamp element that moves to open and close the cleft. {ECO:0000250|UniProtKB:P07703, ECO:0000269|PubMed:20413673, ECO:0000269|PubMed:34671025, ECO:0000269|PubMed:34887565, ECO:0000269|PubMed:36271492, ECO:0000305|PubMed:26151409}.
|
Homo sapiens (Human)
|
O15162
|
PLS1_HUMAN
|
MDKQNSQMNASHPETNLPVGYPPQYPPTAFQGPPGYSGYPGPQVSYPPPPAGHSGPGPAGFPVPNQPVYNQPVYNQPVGAAGVPWMPAPQPPLNCPPGLEYLSQIDQILIHQQIELLEVLTGFETNNKYEIKNSFGQRVYFAAEDTDCCTRNCCGPSRPFTLRIIDNMGQEVITLERPLRCSSCCCPCCLQEIEIQAPPGVPIGYVIQTWHPCLPKFTIQNEKREDVLKISGPCVVCSCCGDVDFEIKSLDEQCVVGKISKHWTGILREAFTDADNFGIQFPLDLDVKMKAVMIGACFLIDFMFFESTGSQEQKSGVW
|
3.1.-.-
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:23590222, ECO:0000269|PubMed:23659204, ECO:0000269|PubMed:24343571, ECO:0000269|PubMed:24648509, ECO:0000269|PubMed:8663431}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:27206388}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:27206388}; Note=Magnesium. Can also use zinc with lower efficiency. {ECO:0000269|PubMed:27206388};
|
acute-phase response [GO:0006953]; apoptotic process [GO:0006915]; defense response to virus [GO:0051607]; negative regulation of phagocytosis [GO:0050765]; negative regulation of viral genome replication [GO:0045071]; phosphatidylserine biosynthetic process [GO:0006659]; phosphatidylserine exposure on apoptotic cell surface [GO:0070782]; plasma membrane phospholipid scrambling [GO:0017121]; platelet activation [GO:0030168]; positive regulation of chromosome separation [GO:1905820]; positive regulation of DNA topoisomerase (ATP-hydrolyzing) activity [GO:2000373]; positive regulation of gene expression [GO:0010628]; positive regulation of innate immune response [GO:0045089]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of Fc receptor mediated stimulatory signaling pathway [GO:0060368]; regulation of mast cell activation [GO:0033003]; response to interferon-beta [GO:0035456]; response to lead ion [GO:0010288]
|
collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; membrane raft [GO:0045121]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]
|
calcium ion binding [GO:0005509]; CD4 receptor binding [GO:0042609]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; enzyme binding [GO:0019899]; epidermal growth factor receptor binding [GO:0005154]; lead ion binding [GO:0032791]; magnesium ion binding [GO:0000287]; mercury ion binding [GO:0045340]; nuclease activity [GO:0004518]; phospholipid scramblase activity [GO:0017128]; SH3 domain binding [GO:0017124]; virus receptor activity [GO:0001618]; zinc ion binding [GO:0008270]
|
PF03803;
| null |
Phospholipid scramblase family
|
PTM: Phosphorylation at Thr-161 by PKC/PKCD increases its phospholipid scramblase activity during both cell stimulation and apoptosis (PubMed:10770950). Phosphorylated by OXSR1 in the presence of RELT. {ECO:0000269|PubMed:10770950, ECO:0000269|PubMed:22052202}.; PTM: Palmitoylation is required for its phospholipid scramblase activity (PubMed:9572851). Palmitoylation regulates its localization to the cell membrane or the nucleus; trafficking to the cell membrane is dependent upon palmitoylation whereas in the absence of palmitoylation, localizes to the nucleus (PubMed:12564925). {ECO:0000269|PubMed:12564925, ECO:0000269|PubMed:9572851}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12564925, ECO:0000269|PubMed:22052202, ECO:0000269|PubMed:23590222, ECO:0000269|PubMed:24648509, ECO:0000269|PubMed:26745724, ECO:0000269|PubMed:37438530}; Single-pass type II membrane protein {ECO:0000269|PubMed:26745724}. Cell membrane {ECO:0000269|PubMed:12564925}; Lipid-anchor {ECO:0000305|PubMed:12564925}; Cytoplasmic side. Nucleus {ECO:0000269|PubMed:12564925, ECO:0000269|PubMed:16091359, ECO:0000269|PubMed:22789739, ECO:0000269|PubMed:23501106, ECO:0000269|PubMed:24648509, ECO:0000269|PubMed:35595813}. Cytoplasm {ECO:0000269|PubMed:22052202, ECO:0000269|PubMed:22789739, ECO:0000269|PubMed:23501106, ECO:0000269|PubMed:29352288, ECO:0000269|PubMed:35595813}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:22052202, ECO:0000269|PubMed:26745724}. Note=Localizes to the perinuclear region in the presence of RELT (PubMed:22052202). Palmitoylation regulates its localization to the cell membrane or the nucleus; trafficking to the cell membrane is dependent upon palmitoylation whereas in the absence of palmitoylation, localizes to the nucleus (PubMed:12564925). {ECO:0000269|PubMed:12564925, ECO:0000269|PubMed:22052202}.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(in) = a 1,2-diacyl-sn-glycero-3-phosphocholine(out); Xref=Rhea:RHEA:38571, ChEBI:CHEBI:57643; Evidence={ECO:0000269|PubMed:10770950, ECO:0000269|PubMed:18629440, ECO:0000269|PubMed:23590222, ECO:0000269|PubMed:23659204, ECO:0000269|PubMed:24343571, ECO:0000269|PubMed:24648509, ECO:0000269|PubMed:8663431, ECO:0000269|PubMed:9218461, ECO:0000269|PubMed:9485382, ECO:0000269|PubMed:9572851}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38572; Evidence={ECO:0000305|PubMed:18629440}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:38573; Evidence={ECO:0000305|PubMed:23659204}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out); Xref=Rhea:RHEA:38895, ChEBI:CHEBI:64612; Evidence={ECO:0000269|PubMed:18629440}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38896; Evidence={ECO:0000305|PubMed:18629440}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) = a 1,2-diacyl-sn-glycero-3-phospho-L-serine(out); Xref=Rhea:RHEA:38663, ChEBI:CHEBI:57262; Evidence={ECO:0000269|PubMed:23659204, ECO:0000269|PubMed:29748552, ECO:0000305|PubMed:32110987}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38664; Evidence={ECO:0000305|PubMed:29748552}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:38665; Evidence={ECO:0000305|PubMed:23659204};
| null | null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0-9.0 for nuclease activity. {ECO:0000269|PubMed:27206388};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius for nuclease activity (PubMed:27206388). Activity reduced significantly beyond 45 degrees Celsius (PubMed:27206388). {ECO:0000269|PubMed:27206388};
|
FUNCTION: Catalyzes calcium-induced ATP-independent rapid bidirectional and non-specific movement of phospholipids (lipid scrambling or lipid flip-flop) between the inner and outer leaflet of the plasma membrane resulting in collapse of the phospholipid asymmetry which leads to phosphatidylserine externalization on the cell surface (PubMed:10770950, PubMed:18629440, PubMed:23590222, PubMed:23659204, PubMed:24343571, PubMed:24648509, PubMed:29748552, PubMed:32110987, PubMed:8663431, PubMed:9218461, PubMed:9485382, PubMed:9572851). Mediates calcium-dependent phosphatidylserine externalization and apoptosis in neurons via its association with TRPC5 (By similarity). Also exhibits magnesium-dependent nuclease activity against double-stranded DNA and RNA but not single-stranded DNA and can enhance DNA decatenation mediated by TOP2A (PubMed:17567603, PubMed:27206388). Negatively regulates FcR-mediated phagocytosis in differentiated macrophages (PubMed:26745724). May contribute to cytokine-regulated cell proliferation and differentiation (By similarity). May play a role in the antiviral response of interferon (IFN) by amplifying and enhancing the IFN response through increased expression of select subset of potent antiviral genes (PubMed:15308695). Inhibits the functions of viral transactivators, including human T-cell leukemia virus (HTLV)-1 protein Tax, human immunodeficiency virus (HIV)-1 Tat, human hepatitis B virus (HBV) HBx, Epstein-Barr virus (EBV) BZLF1 and human cytomegalovirus IE1 and IE2 proteins through direct interactions (PubMed:22789739, PubMed:23501106, PubMed:25365352, PubMed:31434743, PubMed:35138119). Mediates also the inhibition of influenza virus infection by preventing nuclear import of the viral nucleoprotein/NP (PubMed:29352288, PubMed:35595813). Plays a crucial role as a defense factor against SARS-CoV-2 independently of its scramblase activity by directly targeting nascent viral vesicles to prevent virus-membrane fusion and the release of viral RNA into the host-cell cytosol (PubMed:37438530). {ECO:0000250|UniProtKB:Q9JJ00, ECO:0000269|PubMed:10770950, ECO:0000269|PubMed:15308695, ECO:0000269|PubMed:17567603, ECO:0000269|PubMed:18629440, ECO:0000269|PubMed:21806988, ECO:0000269|PubMed:22789739, ECO:0000269|PubMed:23501106, ECO:0000269|PubMed:23590222, ECO:0000269|PubMed:23659204, ECO:0000269|PubMed:24343571, ECO:0000269|PubMed:24648509, ECO:0000269|PubMed:25365352, ECO:0000269|PubMed:26745724, ECO:0000269|PubMed:27206388, ECO:0000269|PubMed:29748552, ECO:0000269|PubMed:31434743, ECO:0000269|PubMed:32110987, ECO:0000269|PubMed:35138119, ECO:0000269|PubMed:37438530, ECO:0000269|PubMed:8663431, ECO:0000269|PubMed:9218461, ECO:0000269|PubMed:9485382, ECO:0000269|PubMed:9572851}.; FUNCTION: (Microbial infection) Acts as an attachment receptor for HCV. {ECO:0000269|PubMed:21806988}.
|
Homo sapiens (Human)
|
O15164
|
TIF1A_HUMAN
|
MEVAVEKAVAAAAAASAAASGGPSAAPSGENEAESRQGPDSERGGEAARLNLLDTCAVCHQNIQSRAPKLLPCLHSFCQRCLPAPQRYLMLPAPMLGSAETPPPVPAPGSPVSGSSPFATQVGVIRCPVCSQECAERHIIDNFFVKDTTEVPSSTVEKSNQVCTSCEDNAEANGFCVECVEWLCKTCIRAHQRVKFTKDHTVRQKEEVSPEAVGVTSQRPVFCPFHKKEQLKLYCETCDKLTCRDCQLLEHKEHRYQFIEEAFQNQKVIIDTLITKLMEKTKYIKFTGNQIQNRIIEVNQNQKQVEQDIKVAIFTLMVEINKKGKALLHQLESLAKDHRMKLMQQQQEVAGLSKQLEHVMHFSKWAVSSGSSTALLYSKRLITYRLRHLLRARCDASPVTNNTIQFHCDPSFWAQNIINLGSLVIEDKESQPQMPKQNPVVEQNSQPPSGLSSNQLSKFPTQISLAQLRLQHMQQQVMAQRQQVQRRPAPVGLPNPRMQGPIQQPSISHQQPPPRLINFQNHSPKPNGPVLPPHPQQLRYPPNQNIPRQAIKPNPLQMAFLAQQAIKQWQISSGQGTPSTTNSTSSTPSSPTITSAAGYDGKAFGSPMIDLSSPVGGSYNLPSLPDIDCSSTIMLDNIVRKDTNIDHGQPRPPSNRTVQSPNSSVPSPGLAGPVTMTSVHPPIRSPSASSVGSRGSSGSSSKPAGADSTHKVPVVMLEPIRIKQENSGPPENYDFPVVIVKQESDEESRPQNANYPRSILTSLLLNSSQSSTSEETVLRSDAPDSTGDQPGLHQDNSSNGKSEWLDPSQKSPLHVGETRKEDDPNEDWCAVCQNGGELLCCEKCPKVFHLSCHVPTLTNFPSGEWICTFCRDLSKPEVEYDCDAPSHNSEKKKTEGLVKLTPIDKRKCERLLLFLYCHEMSLAFQDPVPLTVPDYYKIIKNPMDLSTIKKRLQEDYSMYSKPEDFVADFRLIFQNCAEFNEPDSEVANAGIKLENYFEELLKNLYPEKRFPKPEFRNESEDNKFSDDSDDDFVQPRKKRLKSIEERQLLK
|
2.3.2.27
| null |
calcium ion homeostasis [GO:0055074]; cellular response to estrogen stimulus [GO:0071391]; epithelial cell proliferation [GO:0050673]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of epithelial cell proliferation [GO:0050680]; positive regulation of gene expression [GO:0010628]; protein catabolic process [GO:0030163]; protein ubiquitination [GO:0016567]; regulation of apoptotic process [GO:0042981]; regulation of protein stability [GO:0031647]; regulation of signal transduction by p53 class mediator [GO:1901796]; regulation of vitamin D receptor signaling pathway [GO:0070562]; response to peptide hormone [GO:0043434]; transcription by RNA polymerase II [GO:0006366]
|
cytosol [GO:0005829]; euchromatin [GO:0000791]; male germ cell nucleus [GO:0001673]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perichromatin fibrils [GO:0005726]
|
chromatin binding [GO:0003682]; estrogen response element binding [GO:0034056]; lysine-acetylated histone binding [GO:0070577]; nuclear receptor binding [GO:0016922]; p53 binding [GO:0002039]; protein kinase activity [GO:0004672]; signaling receptor binding [GO:0005102]; transcription coactivator activity [GO:0003713]; ubiquitin protein ligase activity [GO:0061630]; zinc ion binding [GO:0008270]
|
PF00439;PF00628;PF00643;
|
1.20.920.10;3.30.160.60;3.30.40.10;
| null |
PTM: Phosphorylated at Ser-768 by ATM kinase induces ubiquitination and degradation during DNA damage. {ECO:0000269|PubMed:24820418}.; PTM: Sumoylated. {ECO:0000250|UniProtKB:Q64127}.; PTM: Undergoes ubiquitination-mediated degradation in response to DNA damage. {ECO:0000269|PubMed:24820418}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21164480, ECO:0000269|PubMed:25593309, ECO:0000269|PubMed:32324863}. Cytoplasm {ECO:0000269|PubMed:21164480}. Mitochondrion {ECO:0000269|PubMed:32324863}. Note=Colocalizes with sites of active transcription. Predominantly nuclear. Translocated from nucleus to mitochondria to mediate antiviral immunity (PubMed:32324863). Localizes to sites of DNA damage (PubMed:25593309). {ECO:0000269|PubMed:25593309, ECO:0000269|PubMed:32324863}.
|
CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000269|PubMed:24820418, ECO:0000269|PubMed:32324863};
| null |
PATHWAY: Protein modification; protein ubiquitination.
| null | null |
FUNCTION: Transcriptional coactivator that interacts with numerous nuclear receptors and coactivators and modulates the transcription of target genes. Interacts with chromatin depending on histone H3 modifications, having the highest affinity for histone H3 that is both unmodified at 'Lys-4' (H3K4me0) and acetylated at 'Lys-23' (H3K23ac). Has E3 protein-ubiquitin ligase activity. During the DNA damage response, participates in an autoregulatory feedback loop with TP53. Early in response to DNA damage, ATM kinase phosphorylates TRIM24 leading to its ubiquitination and degradation. After sufficient DNA repair has occurred, TP53 activates TRIM24 transcription, ultimately leading to TRIM24-mediated TP53 ubiquitination and degradation (PubMed:24820418). Plays a role in the regulation of cell proliferation and apoptosis, at least in part via its effects on p53/TP53 levels. Up-regulates ligand-dependent transcription activation by AR, GCR/NR3C1, thyroid hormone receptor (TR) and ESR1. Modulates transcription activation by retinoic acid (RA) receptors, including RARA. Plays a role in regulating retinoic acid-dependent proliferation of hepatocytes (By similarity). Participates also in innate immunity by mediating the specific 'Lys-63'-linked ubiquitination of TRAF3 leading to activation of downstream signal transduction of the type I IFN pathway (PubMed:32324863). Additionally, negatively regulates NLRP3/CASP1/IL-1beta-mediated pyroptosis and cell migration probably by ubiquitinating NLRP3 (PubMed:33724611). {ECO:0000250, ECO:0000269|PubMed:16322096, ECO:0000269|PubMed:19556538, ECO:0000269|PubMed:21164480, ECO:0000269|PubMed:24820418, ECO:0000269|PubMed:32324863, ECO:0000269|PubMed:33724611}.
|
Homo sapiens (Human)
|
O15165
|
LRAD4_HUMAN
|
MPEAGFQATNAFTECKFTCTSGKCLYLGSLVCNQQNDCGDNSDEENCLLVTEHPPPGIFNSELEFAQIIIIVVVVTVMVVVIVCLLNHYKVSTRSFINRPNQSRRREDGLPQEGCLWPSDSAAPRLGASEIMHAPRSRDRFTAPSFIQRDRFSRFQPTYPYVQHEIDLPPTISLSDGEEPPPYQGPCTLQLRDPEQQMELNRESVRAPPNRTIFDSDLIDIAMYSGGPCPPSSNSGISASTCSSNGRMEGPPPTYSEVMGHHPGASFLHHQRSNAHRGSRLQFQQNNAESTIVPIKGKDRKPGNLV
| null | null |
negative regulation of cell migration [GO:0030336]; negative regulation of epithelial to mesenchymal transition [GO:0010719]; negative regulation of SMAD protein signal transduction [GO:0060392]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]
|
early endosome membrane [GO:0031901]; Golgi membrane [GO:0000139]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]
|
R-SMAD binding [GO:0070412]
|
PF00057;
|
4.10.400.10;
|
PMEPA1 family
| null |
SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000269|PubMed:24627487}; Single-pass membrane protein {ECO:0000269|PubMed:24627487}.
| null | null | null | null | null |
FUNCTION: Functions as a negative regulator of TGF-beta signaling and thereby probably plays a role in cell proliferation, differentiation, apoptosis, motility, extracellular matrix production and immunosuppression. In the canonical TGF-beta pathway, ZFYVE9/SARA recruits the intracellular signal transducer and transcriptional modulators SMAD2 and SMAD3 to the TGF-beta receptor. Phosphorylated by the receptor, SMAD2 and SMAD3 then form a heteromeric complex with SMAD4 that translocates to the nucleus to regulate transcription. Through interaction with SMAD2 and SMAD3, LDLRAD4 may compete with ZFYVE9 and SMAD4 and prevent propagation of the intracellular signal. {ECO:0000269|PubMed:24627487}.
|
Homo sapiens (Human)
|
O15169
|
AXIN1_HUMAN
|
MNIQEQGFPLDLGASFTEDAPRPPVPGEEGELVSTDPRPASYSFCSGKGVGIKGETSTATPRRSDLDLGYEPEGSASPTPPYLKWAESLHSLLDDQDGISLFRTFLKQEGCADLLDFWFACTGFRKLEPCDSNEEKRLKLARAIYRKYILDNNGIVSRQTKPATKSFIKGCIMKQLIDPAMFDQAQTEIQATMEENTYPSFLKSDIYLEYTRTGSESPKVCSDQSSGSGTGKGISGYLPTLNEDEEWKCDQDMDEDDGRDAAPPGRLPQKLLLETAAPRVSSSRRYSEGREFRYGSWREPVNPYYVNAGYALAPATSANDSEQQSLSSDADTLSLTDSSVDGIPPYRIRKQHRREMQESVQVNGRVPLPHIPRTYRVPKEVRVEPQKFAEELIHRLEAVQRTREAEEKLEERLKRVRMEEEGEDGDPSSGPPGPCHKLPPAPAWHHFPPRCVDMGCAGLRDAHEENPESILDEHVQRVLRTPGRQSPGPGHRSPDSGHVAKMPVALGGAASGHGKHVPKSGAKLDAAGLHHHRHVHHHVHHSTARPKEQVEAEATRRAQSSFAWGLEPHSHGARSRGYSESVGAAPNASDGLAHSGKVGVACKRNAKKAESGKSASTEVPGASEDAEKNQKIMQWIIEGEKEISRHRRTGHGSSGTRKPQPHENSRPLSLEHPWAGPQLRTSVQPSHLFIQDPTMPPHPAPNPLTQLEEARRRLEEEEKRASRAPSKQRYVQEVMRRGRACVRPACAPVLHVVPAVSDMELSETETRSQRKVGGGSAQPCDSIVVAYYFCGEPIPYRTLVRGRAVTLGQFKELLTKKGSYRYYFKKVSDEFDCGVVFEEVREDEAVLPVFEEKIIGKVEKVD
| null | null |
activation of protein kinase activity [GO:0032147]; apoptotic process [GO:0006915]; axial mesoderm formation [GO:0048320]; canonical Wnt signaling pathway [GO:0060070]; cell development [GO:0048468]; cytoplasmic microtubule organization [GO:0031122]; dorsal/ventral axis specification [GO:0009950]; epigenetic programming in the zygotic pronuclei [GO:0044725]; head development [GO:0060322]; in utero embryonic development [GO:0001701]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of fat cell differentiation [GO:0045599]; negative regulation of gene expression [GO:0010629]; negative regulation of protein metabolic process [GO:0051248]; negative regulation of transcription elongation by RNA polymerase II [GO:0034244]; nucleocytoplasmic transport [GO:0006913]; positive regulation of JNK cascade [GO:0046330]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of peptidyl-threonine phosphorylation [GO:0010800]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; positive regulation of protein catabolic process [GO:0045732]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of protein ubiquitination [GO:0031398]; positive regulation of transforming growth factor beta receptor signaling pathway [GO:0030511]; positive regulation of ubiquitin-dependent protein catabolic process [GO:2000060]; post-anal tail morphogenesis [GO:0036342]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein polyubiquitination [GO:0000209]; protein-containing complex assembly [GO:0065003]; sensory perception of sound [GO:0007605]
|
beta-catenin destruction complex [GO:0030877]; cell cortex [GO:0005938]; cell periphery [GO:0071944]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; lateral plasma membrane [GO:0016328]; microtubule cytoskeleton [GO:0015630]; nucleolus [GO:0005730]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; Wnt signalosome [GO:1990909]
|
armadillo repeat domain binding [GO:0070016]; beta-catenin binding [GO:0008013]; enzyme binding [GO:0019899]; I-SMAD binding [GO:0070411]; identical protein binding [GO:0042802]; molecular adaptor activity [GO:0060090]; p53 binding [GO:0002039]; protein homodimerization activity [GO:0042803]; protein kinase binding [GO:0019901]; protein self-association [GO:0043621]; R-SMAD binding [GO:0070412]; signaling adaptor activity [GO:0035591]; SMAD binding [GO:0046332]; ubiquitin ligase-substrate adaptor activity [GO:1990756]; ubiquitin protein ligase binding [GO:0031625]
|
PF16646;PF08833;PF00778;PF00615;
|
1.10.196.10;2.40.240.130;1.10.167.10;
| null |
PTM: Phosphorylation and dephosphorylation of AXIN1 regulates assembly and function of the beta-catenin complex. Phosphorylated by CK1 and GSK3B. Dephosphorylated by PPP1CA and PPP2CA. Phosphorylation by CK1 enhances binding of GSK3B to AXIN1. {ECO:0000269|PubMed:17318175, ECO:0000269|PubMed:9920888}.; PTM: ADP-ribosylated by tankyrase TNKS and TNKS2. Poly-ADP-ribosylated protein is recognized by RNF146, followed by ubiquitination at 'Lys-48' and subsequent activation of the Wnt signaling pathway. {ECO:0000269|PubMed:21383061}.; PTM: Ubiquitinated by RNF146 when poly-ADP-ribosylated, leading to its degradation and subsequent activation of the Wnt signaling pathway. Sumoylation at Lys-857 and Lys-860 prevents ubiquitination and degradation. Sumoylation is required for AXIN1-mediated JNK activation. Deubiquitinated by USP34, deubiquitinated downstream of beta-catenin stabilization step: deubiquitination is important for nuclear accumulation during Wnt signaling to positively regulate beta-catenin (CTNBB1)-mediated transcription. Ubiquitination by SIAH1 and SIAH2 induces its proteasomal degradation as part of the activation of the Wnt signaling pathway (PubMed:28546513). {ECO:0000269|PubMed:18632848, ECO:0000269|PubMed:21383061, ECO:0000269|PubMed:28546513}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16601693}. Nucleus {ECO:0000269|PubMed:17210684}. Membrane {ECO:0000250|UniProtKB:O35625}. Cell membrane {ECO:0000250|UniProtKB:O35625}. Note=MACF1 is required for its translocation to cell membrane (By similarity). On UV irradiation, translocates to the nucleus and colocalizes with DAAX (PubMed:17210684). {ECO:0000250|UniProtKB:O35625, ECO:0000269|PubMed:17210684}.
| null | null | null | null | null |
FUNCTION: Component of the beta-catenin destruction complex required for regulating CTNNB1 levels through phosphorylation and ubiquitination, and modulating Wnt-signaling (PubMed:12192039, PubMed:27098453, PubMed:28829046). Controls dorsoventral patterning via two opposing effects; down-regulates CTNNB1 to inhibit the Wnt signaling pathway and ventralize embryos, but also dorsalizes embryos by activating a Wnt-independent JNK signaling pathway (PubMed:12192039). In Wnt signaling, probably facilitates the phosphorylation of CTNNB1 and APC by GSK3B (PubMed:12192039). Likely to function as a tumor suppressor. Enhances TGF-beta signaling by recruiting the RNF111 E3 ubiquitin ligase and promoting the degradation of inhibitory SMAD7 (PubMed:16601693). Also a component of the AXIN1-HIPK2-TP53 complex which controls cell growth, apoptosis and development (PubMed:17210684). Facilitates the phosphorylation of TP53 by HIPK2 upon ultraviolet irradiation (PubMed:17210684). {ECO:0000269|PubMed:12192039, ECO:0000269|PubMed:16601693, ECO:0000269|PubMed:17210684, ECO:0000269|PubMed:27098453, ECO:0000269|PubMed:28546513}.
|
Homo sapiens (Human)
|
O15173
|
PGRC2_HUMAN
|
MAAGDGDVKLGTLGSGSESSNDGGSESPGDAGAAAEGGGWAAAALALLTGGGEMLLNVALVALVLLGAYRLWVRWGRRGLGAGAGAGEESPATSLPRMKKRDFSLEQLRQYDGSRNPRILLAVNGKVFDVTKGSKFYGPAGPYGIFAGRDASRGLATFCLDKDALRDEYDDLSDLNAVQMESVREWEMQFKEKYDYVGRLLKPGEEPSEYTDEEDTKDHNKQD
| null | null |
adipose tissue development [GO:0060612]
|
endomembrane system [GO:0012505]; endoplasmic reticulum [GO:0005783]; extracellular region [GO:0005576]; membrane [GO:0016020]; nuclear envelope [GO:0005635]; nucleoplasm [GO:0005654]
|
heme binding [GO:0020037]; heme transmembrane transporter activity [GO:0015232]; nuclear steroid receptor activity [GO:0003707]; steroid binding [GO:0005496]
|
PF00173;
|
3.10.120.10;
|
Cytochrome b5 family, MAPR subfamily
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000305|PubMed:23793472}; Single-pass membrane protein {ECO:0000305}. Nucleus envelope {ECO:0000269|PubMed:27754849, ECO:0000269|PubMed:28111073}. Endoplasmic reticulum {ECO:0000269|PubMed:27754849}. Secreted {ECO:0000269|PubMed:37453717}.
| null | null | null | null | null |
FUNCTION: Required for the maintenance of uterine histoarchitecture and normal female reproductive lifespan (By similarity). May serve as a universal non-classical progesterone receptor in the uterus (Probable). Intracellular heme chaperone required for delivery of labile, or signaling heme, to the nucleus (By similarity). Plays a role in adipocyte function and systemic glucose homeostasis (PubMed:28111073). In brown fat, which has a high demand for heme, delivery of labile heme in the nucleus regulates the activity of heme-responsive transcriptional repressors such as NR1D1 and BACH1 (By similarity). {ECO:0000250|UniProtKB:Q80UU9, ECO:0000269|PubMed:28111073, ECO:0000305|PubMed:28396637}.
|
Homo sapiens (Human)
|
O15178
|
TBXT_HUMAN
|
MSSPGTESAGKSLQYRVDHLLSAVENELQAGSEKGDPTERELRVGLEESELWLRFKELTNEMIVTKNGRRMFPVLKVNVSGLDPNAMYSFLLDFVAADNHRWKYVNGEWVPGGKPEPQAPSCVYIHPDSPNFGAHWMKAPVSFSKVKLTNKLNGGGQIMLNSLHKYEPRIHIVRVGGPQRMITSHCFPETQFIAVTAYQNEEITALKIKYNPFAKAFLDAKERSDHKEMMEEPGDSQQPGYSQWGWLLPGTSTLCPPANPHPQFGGALSLPSTHSCDRYPTLRSHRSSPYPSPYAHRNNSPTYSDNSPACLSMLQSHDNWSSLGMPAHPSMLPVSHNASPPTSSSQYPSLWSVSNGAVTPGSQAAAVSNGLGAQFFRGSPAHYTPLTHPVSAPSSSGSPLYEGAAAATDIVDSQYDAAAQGRLIASWTPVSPPSM
| null | null |
anterior/posterior axis specification, embryo [GO:0008595]; cardiac muscle cell myoblast differentiation [GO:0060379]; cell fate specification [GO:0001708]; heart morphogenesis [GO:0003007]; mesoderm development [GO:0007498]; mesoderm formation [GO:0001707]; negative regulation of DNA-binding transcription factor activity [GO:0043433]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of transcription by RNA polymerase II [GO:0045944]; primitive streak formation [GO:0090009]; regulation of transcription by RNA polymerase II [GO:0006357]; signal transduction [GO:0007165]; somitogenesis [GO:0001756]
|
chromatin [GO:0000785]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; sequence-specific double-stranded DNA binding [GO:1990837]
|
PF00907;
|
2.60.40.820;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22611028, ECO:0000269|PubMed:24253444}.
| null | null | null | null | null |
FUNCTION: Involved in the transcriptional regulation of genes required for mesoderm formation and differentiation. Binds to a palindromic T site 5'-TTCACACCTAGGTGTGAA-3' DNA sequence and activates gene transcription when bound to such a site. {ECO:0000250|UniProtKB:P20293}.
|
Homo sapiens (Human)
|
O15182
|
CETN3_HUMAN
|
MSLALRSELVVDKTKRKKRRELSEEQKQEIKDAFELFDTDKDEAIDYHELKVAMRALGFDVKKADVLKILKDYDREATGKITFEDFNEVVTDWILERDPHEEILKAFKLFDDDDSGKISLRNLRRVARELGENMSDEELRAMIEEFDKDGDGEINQEEFIAIMTGDI
| null | null |
cell division [GO:0051301]; centrosome cycle [GO:0007098]; mRNA transport [GO:0051028]; protein transport [GO:0015031]
|
centriole [GO:0005814]; centrosome [GO:0005813]; ciliary basal body [GO:0036064]; cytoplasm [GO:0005737]; microtubule organizing center [GO:0005815]; nuclear pore nuclear basket [GO:0044615]; nucleolus [GO:0005730]; photoreceptor connecting cilium [GO:0032391]; transcription export complex 2 [GO:0070390]
|
calcium ion binding [GO:0005509]; G-protein beta/gamma-subunit complex binding [GO:0031683]; microtubule binding [GO:0008017]
|
PF13499;
|
1.10.238.10;
|
Centrin family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:9256449}. Nucleus, nucleolus {ECO:0000303|PubMed:22307388}. Nucleus envelope {ECO:0000269|PubMed:23591820}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:23591820}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:23591820, ECO:0000269|PubMed:26337392}. Note=Centrosome of interphase and mitotic cells (PubMed:9256449). Localizes to centriole distal lumen (PubMed:26337392). Localization at the nuclear pore complex requires NUP153 and TPR (PubMed:23591820). {ECO:0000269|PubMed:23591820, ECO:0000269|PubMed:26337392, ECO:0000269|PubMed:9256449}.
| null | null | null | null | null |
FUNCTION: Plays a fundamental role in microtubule-organizing center structure and function.; FUNCTION: As a component of the TREX-2 complex, involved in the export of mRNAs to the cytoplasm through the nuclear pores. {ECO:0000269|PubMed:22307388, ECO:0000305|PubMed:23591820}.
|
Homo sapiens (Human)
|
O15194
|
CTDSL_HUMAN
|
MDGPAIITQVTNPKEDEGRLPGAGEKASQCNVSLKKQRSRSILSSFFCCFRDYNVEAPPPSSPSVLPPLVEENGGLQKGDQRQVIPIPSPPAKYLLPEVTVLDYGKKCVVIDLDETLVHSSFKPISNADFIVPVEIDGTIHQVYVLKRPHVDEFLQRMGQLFECVLFTASLAKYADPVADLLDRWGVFRARLFRESCVFHRGNYVKDLSRLGRELSKVIIVDNSPASYIFHPENAVPVQSWFDDMTDTELLDLIPFFEGLSREDDVYSMLHRLCNR
|
3.1.3.16
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 1 Mg(2+) ion per monomer. {ECO:0000250};
|
negative regulation of G1/S transition of mitotic cell cycle [GO:2000134]; negative regulation of protein phosphorylation [GO:0001933]
|
extracellular exosome [GO:0070062]; nucleus [GO:0005634]
|
metal ion binding [GO:0046872]; myosin phosphatase activity [GO:0017018]; RNA polymerase II CTD heptapeptide repeat phosphatase activity [GO:0008420]
|
PF03031;
|
3.40.50.1000;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16;
| null | null | null | null |
FUNCTION: Recruited by REST to neuronal genes that contain RE-1 elements, leading to neuronal gene silencing in non-neuronal cells (By similarity). Preferentially catalyzes the dephosphorylation of 'Ser-5' within the tandem 7 residue repeats in the C-terminal domain (CTD) of the largest RNA polymerase II subunit POLR2A. Negatively regulates RNA polymerase II transcription, possibly by controlling the transition from initiation/capping to processive transcript elongation. {ECO:0000250, ECO:0000269|PubMed:12721286}.
|
Homo sapiens (Human)
|
O15195
|
VILL_HUMAN
|
MDISKGLPGMQGGLHIWISENRKMVPVPEGAYGNFFEEHCYVILHVPQSPKATQGASSDLHYWVGKQAGAEAQGAAEAFQQRLQDELGGQTVLHREAQGHESDCFCSYFRPGIIYRKGGLASDLKHVETNLFNIQRLLHIKGRKHVSATEVELSWNSFNKGDIFLLDLGKMMIQWNGPKTSISEKARGLALTYSLRDRERGGGRAQIGVVDDEAKAPDLMQIMEAVLGRRVGSLRAATPSKDINQLQKANVRLYHVYEKGKDLVVLELATPPLTQDLLQEEDFYILDQGGFKIYVWQGRMSSLQERKAAFSRAVGFIQAKGYPTYTNVEVVNDGAESAAFKQLFRTWSEKRRRNQKLGGRDKSIHVKLDVGKLHTQPKLAAQLRMVDDGSGKVEVWCIQDLHRQPVDPKRHGQLCAGNCYLVLYTYQRLGRVQYILYLWQGHQATADEIEALNSNAEELDVMYGGVLVQEHVTMGSEPPHFLAIFQGQLVIFQERAGHHGKGQSASTTRLFQVQGTDSHNTRTMEVPARASSLNSSDIFLLVTASVCYLWFGKGCNGDQREMARVVVTVISRKNEETVLEGQEPPHFWEALGGRAPYPSNKRLPEEVPSFQPRLFECSSHMGCLVLAEVGFFSQEDLDKYDIMLLDTWQEIFLWLGEAASEWKEAVAWGQEYLKTHPAGRSPATPIVLVKQGHEPPTFIGWFFTWDPYKWTSHPSHKEVVDGSPAAASTISEITAEVNNLRLSRWPGNGRAGAVALQALKGSQDSSENDLVRSPKSAGSRTSSSVSSTSATINGGLRREQLMHQAVEDLPEGVDPARREFYLSDSDFQDIFGKSKEEFYSMATWRQRQEKKQLGFF
| null | null |
actin filament severing [GO:0051014]; actin polymerization or depolymerization [GO:0008154]; barbed-end actin filament capping [GO:0051016]
|
actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]
|
actin filament binding [GO:0051015]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; structural constituent of cytoskeleton [GO:0005200]
|
PF00626;PF02209;
|
3.40.20.10;1.10.950.10;
|
Villin/gelsolin family
| null | null | null | null | null | null | null |
FUNCTION: Possible tumor suppressor.
|
Homo sapiens (Human)
|
O15197
|
EPHB6_HUMAN
|
MATEGAAQLGNRVAGMVCSLWVLLLVSSVLALEEVLLDTTGETSEIGWLTYPPGGWDEVSVLDDQRRLTRTFEACHVAGAPPGTGQDNWLQTHFVERRGAQRAHIRLHFSVRACSSLGVSGGTCRETFTLYYRQAEEPDSPDSVSSWHLKRWTKVDTIAADESFPSSSSSSSSSSSAAWAVGPHGAGQRAGLQLNVKERSFGPLTQRGFYVAFQDTGACLALVAVRLFSYTCPAVLRSFASFPETQASGAGGASLVAAVGTCVAHAEPEEDGVGGQAGGSPPRLHCNGEGKWMVAVGGCRCQPGYQPARGDKACQACPRGLYKSSAGNAPCSPCPARSHAPNPAAPVCPCLEGFYRASSDPPEAPCTGPPSAPQELWFEVQGSALMLHWRLPRELGGRGDLLFNVVCKECEGRQEPASGGGGTCHRCRDEVHFDPRQRGLTESRVLVGGLRAHVPYILEVQAVNGVSELSPDPPQAAAINVSTSHEVPSAVPVVHQVSRASNSITVSWPQPDQTNGNILDYQLRYYDQAEDESHSFTLTSETNTATVTQLSPGHIYGFQVRARTAAGHGPYGGKVYFQTLPQGELSSQLPERLSLVIGSILGALAFLLLAAITVLAVVFQRKRRGTGYTEQLQQYSSPGLGVKYYIDPSTYEDPCQAIRELAREVDPAYIKIEEVIGTGSFGEVRQGRLQPRGRREQTVAIQALWAGGAESLQMTFLGRAAVLGQFQHPNILRLEGVVTKSRPLMVLTEFMELGPLDSFLRQREGQFSSLQLVAMQRGVAAAMQYLSSFAFVHRSLSAHSVLVNSHLVCKVARLGHSPQGPSCLLRWAAPEVIAHGKHTTSSDVWSFGILMWEVMSYGERPYWDMSEQEVLNAIEQEFRLPPPPGCPPGLHLLMLDTWQKDRARRPHFDQLVAAFDKMIRKPDTLQAGGDPGERPSQALLTPVALDFPCLDSPQAWLSAIGLECYQDNFSKFGLCTFSDVAQLSLEDLPALGITLAGHQKKLLHHIQLLQQHLRQQGSVEV
| null | null |
axon guidance [GO:0007411]; ephrin receptor signaling pathway [GO:0048013]
|
cytosol [GO:0005829]; dendrite [GO:0030425]; extracellular region [GO:0005576]; plasma membrane [GO:0005886]
|
ATP binding [GO:0005524]; ephrin receptor activity [GO:0005003]; signaling receptor activity [GO:0038023]; transmembrane-ephrin receptor activity [GO:0005005]
|
PF14575;PF01404;PF07699;PF00041;PF07714;PF07647;
|
2.60.40.1770;2.60.120.260;2.60.40.10;1.10.150.50;1.10.510.10;2.10.50.10;
|
Protein kinase superfamily, Tyr protein kinase family, Ephrin receptor subfamily
|
PTM: Ligand-binding increases phosphorylation on tyrosine residues. Phosphorylation on tyrosine residues is mediated by transphosphorylation by the catalytically active EPHB1 in a ligand-independent manner. Tyrosine phosphorylation of the receptor may act as a switch on the functional transition from cell adhesion/attraction to de-adhesion/repulsion. {ECO:0000269|PubMed:11713248, ECO:0000269|PubMed:15955811}.
|
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 3]: Secreted {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Kinase-defective receptor for members of the ephrin-B family. Binds to ephrin-B1 and ephrin-B2. Modulates cell adhesion and migration by exerting both positive and negative effects upon stimulation with ephrin-B2. Inhibits JNK activation, T-cell receptor-induced IL-2 secretion and CD25 expression upon stimulation with ephrin-B2. {ECO:0000269|PubMed:12517763, ECO:0000269|PubMed:15955811}.
|
Homo sapiens (Human)
|
O15198
|
SMAD9_HUMAN
|
MHSTTPISSLFSFTSPAVKRLLGWKQGDEEEKWAEKAVDSLVKKLKKKKGAMDELERALSCPGQPSKCVTIPRSLDGRLQVSHRKGLPHVIYCRVWRWPDLQSHHELKPLECCEFPFGSKQKEVCINPYHYRRVETPVLPPVLVPRHSEYNPQLSLLAKFRSASLHSEPLMPHNATYPDSFQQPPCSALPPSPSHAFSQSPCTASYPHSPGSPSEPESPYQHSVDTPPLPYHATEASETQSGQPVDATADRHVVLSIPNGDFRPVCYEEPQHWCSVAYYELNNRVGETFQASSRSVLIDGFTDPSNNRNRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVYAECVSDSSIFVQSRNCNYQHGFHPATVCKIPSGCSLKVFNNQLFAQLLAQSVHHGFEVVYELTKMCTIRMSFVKGWGAEYHRQDVTSTPCWIEIHLHGPLQWLDKVLTQMGSPHNPISSVS
| null | null |
anatomical structure morphogenesis [GO:0009653]; BMP signaling pathway [GO:0030509]; cell differentiation [GO:0030154]; cellular response to BMP stimulus [GO:0071773]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]; SMAD protein signal transduction [GO:0060395]; transforming growth factor beta receptor signaling pathway [GO:0007179]
|
chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; heteromeric SMAD protein complex [GO:0071144]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; SMAD protein complex [GO:0071141]
|
DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; I-SMAD binding [GO:0070411]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF03165;PF03166;
|
2.60.200.10;3.90.520.10;
|
Dwarfin/SMAD family
|
PTM: Phosphorylated on serine by BMP (bone morphogenetic proteins) type 1 receptor kinase.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=In the cytoplasm in the absence of ligand. Migration to the nucleus when complexed with SMAD4 (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Transcriptional modulator activated by BMP (bone morphogenetic proteins) type 1 receptor kinase. SMAD9 is a receptor-regulated SMAD (R-SMAD).
|
Homo sapiens (Human)
|
O15204
|
ADEC1_HUMAN
|
MLRGISQLPAVATMSWVLLPVLWLIVQTQAIAIKQTPELTLHEIVCPKKLHILHKREIKNNQTEKHGKEERYEPEVQYQMILNGEEIILSLQKTKHLLGPDYTETLYSPRGEEITTKPENMEHCYYKGNILNEKNSVASISTCDGLRGYFTHHHQRYQIKPLKSTDEKEHAVFTSNQEEQDPANHTCGVKSTDGKQGPIRISRSLKSPEKEDFLRAQKYIDLYLVLDNAFYKNYNENLTLIRSFVFDVMNLLNVIYNTIDVQVALVGMEIWSDGDKIKVVPSASTTFDNFLRWHSSNLGKKIHDHAQLLSGISFNNRRVGLAASNSLCSPSSVAVIEAKKKNNVALVGVMSHELGHVLGMPDVPFNTKCPSGSCVMNQYLSSKFPKDFSTSCRAHFERYLLSQKPKCLLQAPIPTNIMTTPVCGNHLLEVGEDCDCGSPKECTNLCCEALTCKLKPGTDCGGDAPNHTTE
|
3.4.24.-
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250};
|
immune response [GO:0006955]; negative regulation of cell adhesion [GO:0007162]; proteolysis [GO:0006508]
|
collagen-containing extracellular matrix [GO:0062023]; extracellular region [GO:0005576]
|
metalloendopeptidase activity [GO:0004222]; zinc ion binding [GO:0008270]
|
PF01562;PF01421;
|
3.40.390.10;4.10.70.10;
| null | null |
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: May play an important role in the control of the immune response and during pregnancy. {ECO:0000250}.
|
Homo sapiens (Human)
|
O15205
|
UBD_HUMAN
|
MAPNASCLCVHVRSEEWDLMTFDANPYDSVKKIKEHVRSKTKVPVQDQVLLLGSKILKPRRSLSSYGIDKEKTIHLTLKVVKPSDEELPLFLVESGDEAKRHLLQVRRSSSVAQVKAMIETKTGIIPETQIVTCNGKRLEDGKMMADYGIRKGNLLFLACYCIGG
| null | null |
aggresome assembly [GO:0070842]; myeloid dendritic cell differentiation [GO:0043011]; positive regulation of apoptotic process [GO:0043065]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; protein modification by small protein conjugation [GO:0032446]; protein ubiquitination [GO:0016567]; proteolysis [GO:0006508]; regulation of mitotic cell cycle phase transition [GO:1901990]; response to tumor necrosis factor [GO:0034612]; response to type II interferon [GO:0034341]; ubiquitin-dependent protein catabolic process [GO:0006511]
|
aggresome [GO:0016235]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; fibrillar center [GO:0001650]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
proteasome binding [GO:0070628]
|
PF00240;
| null | null |
PTM: Can be acetylated. {ECO:0000269|PubMed:19033385}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12730673, ECO:0000269|PubMed:19033385}. Cytoplasm {ECO:0000250}. Note=Accumulates in aggresomes under proteasome inhibition conditions.
| null | null | null | null | null |
FUNCTION: Ubiquitin-like protein modifier which can be covalently attached to target protein and subsequently leads to their degradation by the 26S proteasome, in a NUB1-dependent manner. Probably functions as a survival factor. Conjugation ability activated by UBA6. Promotes the expression of the proteasome subunit beta type-9 (PSMB9/LMP2). Regulates TNF-alpha-induced and LPS-mediated activation of the central mediator of innate immunity NF-kappa-B by promoting TNF-alpha-mediated proteasomal degradation of ubiquitinated-I-kappa-B-alpha. Required for TNF-alpha-induced p65 nuclear translocation in renal tubular epithelial cells (RTECs). May be involved in dendritic cell (DC) maturation, the process by which immature dendritic cells differentiate into fully competent antigen-presenting cells that initiate T-cell responses. Mediates mitotic non-disjunction and chromosome instability, in long-term in vitro culture and cancers, by abbreviating mitotic phase and impairing the kinetochore localization of MAD2L1 during the prometaphase stage of the cell cycle. May be involved in the formation of aggresomes when proteasome is saturated or impaired. Mediates apoptosis in a caspase-dependent manner, especially in renal epithelium and tubular cells during renal diseases such as polycystic kidney disease and Human immunodeficiency virus (HIV)-associated nephropathy (HIVAN). {ECO:0000269|PubMed:15831455, ECO:0000269|PubMed:16495226, ECO:0000269|PubMed:16495380, ECO:0000269|PubMed:17889673, ECO:0000269|PubMed:18574467, ECO:0000269|PubMed:19028597, ECO:0000269|PubMed:19033385, ECO:0000269|PubMed:19166848, ECO:0000269|PubMed:19726511, ECO:0000269|PubMed:19959714}.
|
Homo sapiens (Human)
|
O15209
|
ZBT22_HUMAN
|
MEPSPLSPSGAALPLPLSLAPPPLPLPAAAVVHVSFPEVTSALLESLNQQRLQGQLCDVSIRVQGREFRAHRAVLAASSPYFHDQVLLKGMTSISLPSVMDPGAFETVLASAYTGRLSMAAADIVNFLTVGSVLQMWHIVDKCTELLREGRASATTTITTAAATSVTVPGAGVPSGSGGTVAPATMGSARSHASSRASENQSPSSSNYFSPRESTDFSSSSQEAFAASAVGSGERRGGGPVFPAPVVGSGGATSGKLLLEADELCDDGGDGRGAVVPGAGLRRPTYTPPSIMPQKHWVYVKRGGNCPAPTPLVPQDPDLEEEEEEEDLVLTCEDDEDEELGGSSRVPVGGGPEATLSISDVRTLSEPPDKGEEQVNFCESSNDFGPYEGGGPVAGLDDSGGPTPSSYAPSHPPRPLLPLDMQGNQILVFPSSSSSSSSQAPGQPPGNQAEHGAVTVGGTSVGSLGVPGSVGGVPGGTGSGDGNKIFLCHCGKAFSHKSMRDRHVNMHLNLRPFDCPVCNKKFKMKHHLTEHMKTHTGLKPYECGVCAKKFMWRDSFMRHRGHCERRHRLGGVGAVPGPGTPTGPSLPSKRESPGVGGGSGDEASAATPPSSRRVWSPPRVHKVEMGFGGGGGAN
| null | null |
regulation of transcription by RNA polymerase II [GO:0006357]
|
chromatin [GO:0000785]; nucleus [GO:0005634]
|
DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific double-stranded DNA binding [GO:1990837]
|
PF00651;
|
3.30.160.60;
|
Krueppel C2H2-type zinc-finger protein family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: May be involved in transcriptional regulation.
|
Homo sapiens (Human)
|
O15211
|
RGL2_HUMAN
|
MLPRPLRLLLDTSPPGGVVLSSFRSRDPEEGGGPGGLVVGGGQEEEEEEEEEAPVSVWDEEEDGAVFTVTSRQYRPLDPLVPMPPPRSSRRLRAGTLEALVRHLLDTRTSGTDVSFMSAFLATHRAFTSTPALLGLMADRLEALESHPTDELERTTEVAISVLSTWLASHPEDFGSEAKGQLDRLESFLLQTGYAAGKGVGGGSADLIRNLRSRVDPQAPDLPKPLALPGDPPADPTDVLVFLADHLAEQLTLLDAELFLNLIPSQCLGGLWGHRDRPGHSHLCPSVRATVTQFNKVAGAVVSSVLGATSTGEGPGEVTIRPLRPPQRARLLEKWIRVAEECRLLRNFSSVYAVVSALQSSPIHRLRAAWGEATRDSLRVFSSLCQIFSEEDNYSQSRELLVQEVKLQSPLEPHSKKAPRSGSRGGGVVPYLGTFLKDLVMLDAASKDELENGYINFDKRRKEFAVLSELRRLQNECRGYNLQPDHDIQRWLQGLRPLTEAQSHRVSCEVEPPGSSDPPAPRVLRPTLVISQWTEVLGSVGVPTPLVSCDRPSTGGDEAPTTPAPLLTRLAQHMKWPSVSSLDSALESSPSLHSPADPSHLSPPASSPRPSRGHRRSASCGSPLSGGAEEASGGTGYGGEGSGPGASDCRIIRVQMELGEDGSVYKSILVTSQDKAPSVISRVLKKNNRDSAVASEYELVQLLPGERELTIPASANVFYAMDGASHDFLLRQRRRSSTATPGVTSGPSASGTPPSEGGGGSFPRIKATGRKIARALF
| null | null |
negative regulation of cardiac muscle cell apoptotic process [GO:0010667]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; Ras protein signal transduction [GO:0007265]; regulation of Ral protein signal transduction [GO:0032485]
|
cytosol [GO:0005829]; plasma membrane [GO:0005886]
|
guanyl-nucleotide exchange factor activity [GO:0005085]
|
PF00788;PF00617;PF00618;
|
1.10.840.10;1.20.870.10;
| null | null | null | null | null | null | null | null |
FUNCTION: Probable guanine nucleotide exchange factor. Putative effector of Ras and/or Rap. Associates with the GTP-bound form of Rap 1A and H-Ras in vitro (By similarity). {ECO:0000250}.
|
Homo sapiens (Human)
|
O15212
|
PFD6_HUMAN
|
MAELIQKKLQGEVEKYQQLQKDLSKSMSGRQKLEAQLTENNIVKEELALLDGSNVVFKLLGPVLVKQELGEARATVGKRLDYITAEIKRYESQLRDLERQSEQQRETLAQLQQEFQRAQAAKAGAPGKA
| null | null |
chaperone-mediated protein complex assembly [GO:0051131]; chaperone-mediated protein folding [GO:0061077]; negative regulation of amyloid fibril formation [GO:1905907]; protein folding [GO:0006457]; protein stabilization [GO:0050821]
|
cytoplasm [GO:0005737]; prefoldin complex [GO:0016272]; protein folding chaperone complex [GO:0101031]; RPAP3/R2TP/prefoldin-like complex [GO:1990062]
|
amyloid-beta binding [GO:0001540]; protein-folding chaperone binding [GO:0051087]; unfolded protein binding [GO:0051082]
|
PF01920;
|
1.10.287.370;
|
Prefoldin subunit beta family
| null | null | null | null | null | null | null |
FUNCTION: Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins. {ECO:0000269|PubMed:9630229}.
|
Homo sapiens (Human)
|
O15213
|
WDR46_HUMAN
|
METAPKPGKDVPPKKDKLQTKRKKPRRYWEEETVPTTAGASPGPPRNKKNRELRPQRPKNAYILKKSRISKKPQVPKKPREWKNPESQRGLSGTQDPFPGPAPVPVEVVQKFCRIDKSRKLPHSKAKTRSRLEVAEAEEEETSIKAARSELLLAEEPGFLEGEDGEDTAKICQADIVEAVDIASAAKHFDLNLRQFGPYRLNYSRTGRHLAFGGRRGHVAALDWVTKKLMCEINVMEAVRDIRFLHSEALLAVAQNRWLHIYDNQGIELHCIRRCDRVTRLEFLPFHFLLATASETGFLTYLDVSVGKIVAALNARAGRLDVMSQNPYNAVIHLGHSNGTVSLWSPAMKEPLAKILCHRGGVRAVAVDSTGTYMATSGLDHQLKIFDLRGTYQPLSTRTLPHGAGHLAFSQRGLLVAGMGDVVNIWAGQGKASPPSLEQPYLTHRLSGPVHGLQFCPFEDVLGVGHTGGITSMLVPGAGEPNFDGLESNPYRSRKQRQEWEVKALLEKVPAELICLDPRALAEVDVISLEQGKKEQIERLGYDPQAKAPFQPKPKQKGRSSTASLVKRKRKVMDEEHRDKVRQSLQQQHHKEAKAKPTGARPSALDRFVR
| null | null |
maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000462]; ribosomal small subunit biogenesis [GO:0042274]
|
90S preribosome [GO:0030686]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; small-subunit processome [GO:0032040]
|
RNA binding [GO:0003723]
|
PF08149;PF00400;
|
2.130.10.10;
| null | null |
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:23848194, ECO:0000269|PubMed:34516797}.
| null | null | null | null | null |
FUNCTION: Scaffold component of the nucleolar structure. Required for localization of DDX21 and NCL to the granular compartment of the nucleolus (PubMed:23848194). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (PubMed:34516797). {ECO:0000269|PubMed:23848194, ECO:0000269|PubMed:34516797}.
|
Homo sapiens (Human)
|
O15217
|
GSTA4_HUMAN
|
MAARPKLHYPNGRGRMESVRWVLAAAGVEFDEEFLETKEQLYKLQDGNHLLFQQVPMVEIDGMKLVQTRSILHYIADKHNLFGKNLKERTLIDMYVEGTLDLLELLIMHPFLKPDDQQKEVVNMAQKAIIRYFPVFEKILRGHGQSFLVGNQLSLADVILLQTILALEEKIPNILSAFPFLQEYTVKLSNIPTIKRFLEPGSKKKPPPDEIYVRTVYNIFRP
|
2.5.1.18
| null |
glutathione metabolic process [GO:0006749]; xenobiotic metabolic process [GO:0006805]
|
cytosol [GO:0005829]
|
glutathione transferase activity [GO:0004364]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]
|
PF14497;PF02798;
|
1.20.1050.10;3.40.30.10;
|
GST superfamily, Alpha family
| null |
SUBCELLULAR LOCATION: Cytoplasm.
|
CATALYTIC ACTIVITY: Reaction=glutathione + RX = a halide anion + an S-substituted glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378, ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925, ChEBI:CHEBI:90779; EC=2.5.1.18; Evidence={ECO:0000269|PubMed:10329152, ECO:0000269|PubMed:20085333};
| null | null | null | null |
FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. This isozyme has a high catalytic efficiency with 4-hydroxyalkenals such as 4-hydroxynonenal (4-HNE). {ECO:0000269|PubMed:10329152, ECO:0000269|PubMed:20085333}.
|
Homo sapiens (Human)
|
O15226
|
NKRF_HUMAN
|
MEKILQMAEGIDIGEMPSYDLVLSKPSKGQKRHLSTCDGQNPPKKQAGSKFHARPRFEPVHFVASSSKDERQEDPYGPQTKEVNEQTHFASMPRDIYQDYTQDSFSIQDGNSQYCDSSGFILTKDQPVTANMYFDSGNPAPSTTSQQANSQSTPEPSPSQTFPESVVAEKQYFIEKLTATIWKNLSNPEMTSGSDKINYTYMLTRCIQACKTNPEYIYAPLKEIPPADIPKNKKLLTDGYACEVRCQNIYLTTGYAGSKNGSRDRATELAVKLLQKRIEVRVVRRKFKHTFGEDLVVCQIGMSSYEFPPALKPPEDLVVLGKDASGQPIFNASAKHWTNFVITENANDAIGILNNSASFNKMSIEYKYEMMPNRTWRCRVFLQDHCLAEGYGTKKTSKHAAADEALKILQKTQPTYPSVKSSQCHTGSSPRGSGKKKDIKDLVVYENSSNPVCTLNDTAQFNRMTVEYVYERMTGLRWKCKVILESEVIAEAVGVKKTVKYEAAGEAVKTLKKTQPTVINNLKKGAVEDVISRNEIQGRSAEEAYKQQIKEDNIGNQLLRKMGWTGGGLGKSGEGIREPISVKEQHKREGLGLDVERVNKIAKRDIEQIIRNYARSESHTDLTFSRELTNDERKQIHQIAQKYGLKSKSHGVGHDRYLVVGRKRRKEDLLDQLKQEGQVGHYELVMPQAN
| null | null |
negative regulation of DNA-templated transcription [GO:0045892]; positive regulation of transcription by RNA polymerase II [GO:0045944]
|
nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
ATPase activator activity [GO:0001671]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; RNA binding [GO:0003723]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF01585;PF01424;
|
3.30.160.20;3.30.1370.50;
| null | null |
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849}.
| null | null | null | null | null |
FUNCTION: Enhances the ATPase activity of DHX15 by acting like a brace that tethers mobile sections of DHX15 together, stabilizing a functional conformation with high RNA affinity of DHX15 (PubMed:12381793). Involved in the constitutive silencing of the interferon beta promoter, independently of the virus-induced signals, and in the inhibition of the basal and cytokine-induced iNOS promoter activity (PubMed:12381793). Also involved in the regulation of IL-8 transcription (PubMed:12381793). May also act as a DNA-binding transcription regulator: interacts with a specific negative regulatory element (NRE) 5'-AATTCCTCTGA-3' to mediate transcriptional repression of certain NK-kappa-B responsive genes (PubMed:10562553). {ECO:0000269|PubMed:10562553, ECO:0000269|PubMed:12381793}.
|
Homo sapiens (Human)
|
O15228
|
GNPAT_HUMAN
|
MESSSSSNSYFSVGPTSPSAVVLLYSKELKKWDEFEDILEERRHVSDLKFAMKCYTPLVYKGITPCKPIDIKCSVLNSEEIHYVIKQLSKESLQSVDVLREEVSEILDEMSHKLRLGAIRFCAFTLSKVFKQIFSKVCVNEEGIQKLQRAIQEHPVVLLPSHRSYIDFLMLSFLLYNYDLPVPVIAAGMDFLGMKMVGELLRMSGAFFMRRTFGGNKLYWAVFSEYVKTMLRNGYAPVEFFLEGTRSRSAKTLTPKFGLLNIVMEPFFKREVFDTYLVPISISYDKILEETLYVYELLGVPKPKESTTGLLKARKILSENFGSIHVYFGDPVSLRSLAAGRMSRSSYNLVPRYIPQKQSEDMHAFVTEVAYKMELLQIENMVLSPWTLIVAVLLQNRPSMDFDALVEKTLWLKGLTQAFGGFLIWPDNKPAEEVVPASILLHSNIASLVKDQVILKVDSGDSEVVDGLMLQHITLLMCSAYRNQLLNIFVRPSLVAVALQMTPGFRKEDVYSCFRFLRDVFADEFIFLPGNTLKDFEEGCYLLCKSEAIQVTTKDILVTEKGNTVLEFLVGLFKPFVESYQIICKYLLSEEEDHFSEEQYLAAVRKFTSQLLDQGTSQCYDVLSSDVQKNALAACVRLGVVEKKKINNNCIFNVNEPATTKLEEMLGCKTPIGKPATAKL
|
2.3.1.42
| null |
cerebellum morphogenesis [GO:0021587]; ether lipid biosynthetic process [GO:0008611]; fatty acid metabolic process [GO:0006631]; glycerol-3-phosphate metabolic process [GO:0006072]; membrane organization [GO:0061024]; paranodal junction assembly [GO:0030913]; phosphatidic acid biosynthetic process [GO:0006654]; phospholipid biosynthetic process [GO:0008654]; response to fatty acid [GO:0070542]; response to nutrient [GO:0007584]; response to starvation [GO:0042594]; response to xenobiotic stimulus [GO:0009410]; synapse assembly [GO:0007416]; triglyceride biosynthetic process [GO:0019432]
|
cytosol [GO:0005829]; membrane [GO:0016020]; mitochondrial membrane [GO:0031966]; peroxisomal matrix [GO:0005782]; peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777]; plasma membrane [GO:0005886]
|
glycerol-3-phosphate O-acyltransferase activity [GO:0004366]; glycerone-phosphate O-acyltransferase activity [GO:0016287]
|
PF01553;PF19277;
| null |
GPAT/DAPAT family
| null |
SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000269|PubMed:15687349}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9ES71}; Matrix side {ECO:0000250|UniProtKB:Q9ES71}. Note=Exclusively localized to the lumenal side of the peroxisomal membrane. {ECO:0000250|UniProtKB:Q9ES71}.
|
CATALYTIC ACTIVITY: Reaction=an acyl-CoA + dihydroxyacetone phosphate = a 1-acylglycerone 3-phosphate + CoA; Xref=Rhea:RHEA:17657, ChEBI:CHEBI:57287, ChEBI:CHEBI:57534, ChEBI:CHEBI:57642, ChEBI:CHEBI:58342; EC=2.3.1.42; Evidence={ECO:0000269|PubMed:10395968, ECO:0000269|PubMed:11152660, ECO:0000269|PubMed:15687349}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17658; Evidence={ECO:0000269|PubMed:11152660}; CATALYTIC ACTIVITY: Reaction=dihydroxyacetone phosphate + hexadecanoyl-CoA = 1-hexadecanoylglycerone 3-phosphate + CoA; Xref=Rhea:RHEA:40715, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:57642, ChEBI:CHEBI:58303; Evidence={ECO:0000269|PubMed:10395968, ECO:0000269|PubMed:11152660, ECO:0000269|PubMed:15687349}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40716; Evidence={ECO:0000269|PubMed:11152660};
| null |
PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism. {ECO:0000269|PubMed:11152660, ECO:0000269|PubMed:15687349}.
| null | null |
FUNCTION: Dihydroxyacetonephosphate acyltransferase catalyzing the first step in the biosynthesis of plasmalogens, a subset of phospholipids that differ from other glycerolipids by having an alkyl chain attached through a vinyl ether linkage at the sn-1 position of the glycerol backbone, and which unique physical properties have an impact on various aspects of cell signaling and membrane biology. {ECO:0000269|PubMed:11152660, ECO:0000269|PubMed:15687349}.
|
Homo sapiens (Human)
|
O15229
|
KMO_HUMAN
|
MDSSVIQRKKVAVIGGGLVGSLQACFLAKRNFQIDVYEAREDTRVATFTRGRSINLALSHRGRQALKAVGLEDQIVSQGIPMRARMIHSLSGKKSAIPYGTKSQYILSVSRENLNKDLLTAAEKYPNVKMHFNHRLLKCNPEEGMITVLGSDKVPKDVTCDLIVGCDGAYSTVRSHLMKKPRFDYSQQYIPHGYMELTIPPKNGDYAMEPNYLHIWPRNTFMMIALPNMNKSFTCTLFMPFEEFEKLLTSNDVVDFFQKYFPDAIPLIGEKLLVQDFFLLPAQPMISVKCSSFHFKSHCVLLGDAAHAIVPFFGQGMNAGFEDCLVFDELMDKFSNDLSLCLPVFSRLRIPDDHAISDLSMYNYIEMRAHVNSSWFIFQKNMERFLHAIMPSTFIPLYTMVTFSRIRYHEAVQRWHWQKKVINKGLFFLGSLIAISSTYLLIHYMSPRSFLRLRRPWNWIAHFRNTTCFPAKAVDSLEQISNLISR
|
1.14.13.9
|
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000255|HAMAP-Rule:MF_03018, ECO:0000269|PubMed:10672018, ECO:0000269|PubMed:29429898};
|
'de novo' NAD biosynthetic process from tryptophan [GO:0034354]; anthranilate metabolic process [GO:0043420]; cellular response to interleukin-1 [GO:0071347]; cellular response to lipopolysaccharide [GO:0071222]; kynurenic acid biosynthetic process [GO:0034276]; kynurenine metabolic process [GO:0070189]; L-kynurenine metabolic process [GO:0097052]; NAD metabolic process [GO:0019674]; positive regulation of glutamate secretion, neurotransmission [GO:1903296]; quinolinate biosynthetic process [GO:0019805]; response to salt stress [GO:0009651]; tryptophan catabolic process [GO:0006569]
|
cytosol [GO:0005829]; extracellular space [GO:0005615]; mitochondrial outer membrane [GO:0005741]
|
FAD binding [GO:0071949]; flavin adenine dinucleotide binding [GO:0050660]; kynurenine 3-monooxygenase activity [GO:0004502]; NAD(P)H oxidase H2O2-forming activity [GO:0016174]
|
PF01494;
|
3.50.50.60;
|
Aromatic-ring hydroxylase family, KMO subfamily
| null |
SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000255|HAMAP-Rule:MF_03018, ECO:0000269|PubMed:9237672}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03018, ECO:0000269|PubMed:9237672}.
|
CATALYTIC ACTIVITY: Reaction=H(+) + L-kynurenine + NADPH + O2 = 3-hydroxy-L-kynurenine + H2O + NADP(+); Xref=Rhea:RHEA:20545, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57783, ChEBI:CHEBI:57959, ChEBI:CHEBI:58125, ChEBI:CHEBI:58349; EC=1.14.13.9; Evidence={ECO:0000255|HAMAP-Rule:MF_03018, ECO:0000269|PubMed:10672018, ECO:0000269|PubMed:29429898, ECO:0000269|PubMed:9237672};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=24.1 uM for L-kynurenine {ECO:0000269|PubMed:10672018, ECO:0000269|PubMed:23575632, ECO:0000269|PubMed:9237672}; KM=2 uM for L-kynurenine {ECO:0000269|PubMed:26752518}; KM=78 uM for L-kynurenine {ECO:0000269|PubMed:26752518}; Vmax=8.5 umol/min/mg enzyme {ECO:0000269|PubMed:10672018, ECO:0000269|PubMed:9237672}; Note=kcat is 0.24 sec(-1) for L-kynurenine. {ECO:0000269|PubMed:28604669};
|
PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 1/3. {ECO:0000255|HAMAP-Rule:MF_03018}.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:10672018, ECO:0000269|PubMed:9237672};
| null |
FUNCTION: Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form 3-hydroxy-L-kynurenine (L-3OHKyn) (PubMed:23575632, PubMed:26752518, PubMed:28604669, PubMed:29208702, PubMed:29429898). Required for synthesis of quinolinic acid, a neurotoxic NMDA receptor antagonist and potential endogenous inhibitor of NMDA receptor signaling in axonal targeting, synaptogenesis and apoptosis during brain development. Quinolinic acid may also affect NMDA receptor signaling in pancreatic beta cells, osteoblasts, myocardial cells, and the gastrointestinal tract (Probable). {ECO:0000269|PubMed:23575632, ECO:0000269|PubMed:26752518, ECO:0000269|PubMed:28604669, ECO:0000269|PubMed:29208702, ECO:0000269|PubMed:29429898, ECO:0000305|PubMed:12402501}.
|
Homo sapiens (Human)
|
O15230
|
LAMA5_HUMAN
|
MAKRLCAGSALCVRGPRGPAPLLLVGLALLGAARAREEAGGGFSLHPPYFNLAEGARIAASATCGEEAPARGSPRPTEDLYCKLVGGPVAGGDPNQTIRGQYCDICTAANSNKAHPASNAIDGTERWWQSPPLSRGLEYNEVNVTLDLGQVFHVAYVLIKFANSPRPDLWVLERSMDFGRTYQPWQFFASSKRDCLERFGPQTLERITRDDAAICTTEYSRIVPLENGEIVVSLVNGRPGAMNFSYSPLLREFTKATNVRLRFLRTNTLLGHLMGKALRDPTVTRRYYYSIKDISIGGRCVCHGHADACDAKDPTDPFRLQCTCQHNTCGGTCDRCCPGFNQQPWKPATANSANECQSCNCYGHATDCYYDPEVDRRRASQSLDGTYQGGGVCIDCQHHTTGVNCERCLPGFYRSPNHPLDSPHVCRRCNCESDFTDGTCEDLTGRCYCRPNFSGERCDVCAEGFTGFPSCYPTPSSSNDTREQVLPAGQIVNCDCSAAGTQGNACRKDPRVGRCLCKPNFQGTHCELCAPGFYGPGCQPCQCSSPGVADDRCDPDTGQCRCRVGFEGATCDRCAPGYFHFPLCQLCGCSPAGTLPEGCDEAGRCLCQPEFAGPHCDRCRPGYHGFPNCQACTCDPRGALDQLCGAGGLCRCRPGYTGTACQECSPGFHGFPSCVPCHCSAEGSLHAACDPRSGQCSCRPRVTGLRCDTCVPGAYNFPYCEAGSCHPAGLAPVDPALPEAQVPCMCRAHVEGPSCDRCKPGFWGLSPSNPEGCTRCSCDLRGTLGGVAECQPGTGQCFCKPHVCGQACASCKDGFFGLDQADYFGCRSCRCDIGGALGQSCEPRTGVCRCRPNTQGPTCSEPARDHYLPDLHHLRLELEEAATPEGHAVRFGFNPLEFENFSWRGYAQMAPVQPRIVARLNLTSPDLFWLVFRYVNRGAMSVSGRVSVREEGRSATCANCTAQSQPVAFPPSTEPAFITVPQRGFGEPFVLNPGTWALRVEAEGVLLDYVVLLPSAYYEAALLQLRVTEACTYRPSAQQSGDNCLLYTHLPLDGFPSAAGLEALCRQDNSLPRPCPTEQLSPSHPPLITCTGSDVDVQLQVAVPQPGRYALVVEYANEDARQEVGVAVHTPQRAPQQGLLSLHPCLYSTLCRGTARDTQDHLAVFHLDSEASVRLTAEQARFFLHGVTLVPIEEFSPEFVEPRVSCISSHGAFGPNSAACLPSRFPKPPQPIILRDCQVIPLPPGLPLTHAQDLTPAMSPAGPRPRPPTAVDPDAEPTLLREPQATVVFTTHVPTLGRYAFLLHGYQPAHPTFPVEVLINAGRVWQGHANASFCPHGYGCRTLVVCEGQALLDVTHSELTVTVRVPKGRWLWLDYVLVVPENVYSFGYLREEPLDKSYDFISHCAAQGYHISPSSSSLFCRNAAASLSLFYNNGARPCGCHEVGATGPTCEPFGGQCPCHAHVIGRDCSRCATGYWGFPNCRPCDCGARLCDELTGQCICPPRTIPPDCLLCQPQTFGCHPLVGCEECNCSGPGIQELTDPTCDTDSGQCKCRPNVTGRRCDTCSPGFHGYPRCRPCDCHEAGTAPGVCDPLTGQCYCKENVQGPKCDQCSLGTFSLDAANPKGCTRCFCFGATERCRSSSYTRQEFVDMEGWVLLSTDRQVVPHERQPGTEMLRADLRHVPEAVPEAFPELYWQAPPSYLGDRVSSYGGTLRYELHSETQRGDVFVPMESRPDVVLQGNQMSITFLEPAYPTPGHVHRGQLQLVEGNFRHTETRNTVSREELMMVLASLEQLQIRALFSQISSAVFLRRVALEVASPAGQGALASNVELCLCPASYRGDSCQECAPGFYRDVKGLFLGRCVPCQCHGHSDRCLPGSGVCVDCQHNTEGAHCERCQAGFVSSRDDPSAPCVSCPCPLSVPSNNFAEGCVLRGGRTQCLCKPGYAGASCERCAPGFFGNPLVLGSSCQPCDCSGNGDPNLLFSDCDPLTGACRGCLRHTTGPRCEICAPGFYGNALLPGNCTRCDCTPCGTEACDPHSGHCLCKAGVTGRRCDRCQEGHFGFDGCGGCRPCACGPAAEGSECHPQSGQCHCRPGTMGPQCRECAPGYWGLPEQGCRRCQCPGGRCDPHTGRCNCPPGLSGERCDTCSQQHQVPVPGGPVGHSIHCEVCDHCVVLLLDDLERAGALLPAIHEQLRGINASSMAWARLHRLNASIADLQSQLRSPLGPRHETAQQLEVLEQQSTSLGQDARRLGGQAVGTRDQASQLLAGTEATLGHAKTLLAAIRAVDRTLSELMSQTGHLGLANASAPSGEQLLRTLAEVERLLWEMRARDLGAPQAAAEAELAAAQRLLARVQEQLSSLWEENQALATQTRDRLAQHEAGLMDLREALNRAVDATREAQELNSRNQERLEEALQRKQELSRDNATLQATLHAARDTLASVFRLLHSLDQAKEELERLAASLDGARTPLLQRMQTFSPAGSKLRLVEAAEAHAQQLGQLALNLSSIILDVNQDRLTQRAIEASNAYSRILQAVQAAEDAAGQALQQADHTWATVVRQGLVDRAQQLLANSTALEEAMLQEQQRLGLVWAALQGARTQLRDVRAKKDQLEAHIQAAQAMLAMDTDETSKKIAHAKAVAAEAQDTATRVQSQLQAMQENVERWQGQYEGLRGQDLGQAVLDAGHSVSTLEKTLPQLLAKLSILENRGVHNASLALSASIGRVRELIAQARGAASKVKVPMKFNGRSGVQLRTPRDLADLAAYTALKFYLQGPEPEPGQGTEDRFVMYMGSRQATGDYMGVSLRDKKVHWVYQLGEAGPAVLSIDEDIGEQFAAVSLDRTLQFGHMSVTVERQMIQETKGDTVAPGAEGLLNLRPDDFVFYVGGYPSTFTPPPLLRFPGYRGCIEMDTLNEEVVSLYNFERTFQLDTAVDRPCARSKSTGDPWLTDGSYLDGTGFARISFDSQISTTKRFEQELRLVSYSGVLFFLKQQSQFLCLAVQEGSLVLLYDFGAGLKKAVPLQPPPPLTSASKAIQVFLLGGSRKRVLVRVERATVYSVEQDNDLELADAYYLGGVPPDQLPPSLRRLFPTGGSVRGCVKGIKALGKYVDLKRLNTTGVSAGCTADLLVGRAMTFHGHGFLRLALSNVAPLTGNVYSGFGFHSAQDSALLYYRASPDGLCQVSLQQGRVSLQLLRTEVKTQAGFADGAPHYVAFYSNATGVWLYVDDQLQQMKPHRGPPPELQPQPEGPPRLLLGGLPESGTIYNFSGCISNVFVQRLLGPQRVFDLQQNLGSVNVSTGCAPALQAQTPGLGPRGLQATARKASRRSRQPARHPACMLPPHLRTTRDSYQFGGSLSSHLEFVGILARHRNWPSLSMHVLPRSSRGLLLFTARLRPGSPSLALFLSNGHFVAQMEGLGTRLRAQSRQRSRPGRWHKVSVRWEKNRILLVTDGARAWSQEGPHRQHQGAEHPQPHTLFVGGLPASSHSSKLPVTVGFSGCVKRLRLHGRPLGAPTRMAGVTPCILGPLEAGLFFPGSGGVITLDLPGATLPDVGLELEVRPLAVTGLIFHLGQARTPPYLQLQVTEKQVLLRADDGAGEFSTSVTRPSVLCDGQWHRLAVMKSGNVLRLEVDAQSNHTVGPLLAAAAGAPAPLYLGGLPEPMAVQPWPPAYCGCMRRLAVNRSPVAMTRSVEVHGAVGASGCPAA
| null | null |
branching involved in salivary gland morphogenesis [GO:0060445]; branching involved in ureteric bud morphogenesis [GO:0001658]; cell migration [GO:0016477]; cilium assembly [GO:0060271]; hair follicle development [GO:0001942]; integrin-mediated signaling pathway [GO:0007229]; lung development [GO:0030324]; morphogenesis of a polarized epithelium [GO:0001738]; morphogenesis of embryonic epithelium [GO:0016331]; muscle organ development [GO:0007517]; odontogenesis of dentin-containing tooth [GO:0042475]; postsynapse organization [GO:0099173]; protein localization to plasma membrane [GO:0072659]; regulation of cell adhesion [GO:0030155]; regulation of cell migration [GO:0030334]; regulation of embryonic development [GO:0045995]; regulation of epithelial cell proliferation [GO:0050678]; skeletal system morphogenesis [GO:0048705]; substrate adhesion-dependent cell spreading [GO:0034446]; trunk neural crest cell migration [GO:0036484]
|
basement membrane [GO:0005604]; collagen-containing extracellular matrix [GO:0062023]; extracellular exosome [GO:0070062]; extracellular matrix of synaptic cleft [GO:0098965]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; glutamatergic synapse [GO:0098978]; laminin-10 complex [GO:0043259]; laminin-11 complex [GO:0043260]; laminin-5 complex [GO:0005610]; neuromuscular junction [GO:0031594]; nucleus [GO:0005634]; synaptic cleft [GO:0043083]
|
integrin binding [GO:0005178]
|
PF00052;PF00053;PF00054;PF02210;PF06008;PF06009;PF00055;
|
2.60.120.200;2.60.120.260;2.10.25.10;2.170.300.10;
| null | null |
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane. Note=Major component.
| null | null | null | null | null |
FUNCTION: Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Plays a role in the regulation of skeletogenesis, through a mechanism that involves integrin-mediated signaling and PTK2B/PYK2 (PubMed:33242826). {ECO:0000269|PubMed:33242826}.
|
Homo sapiens (Human)
|
O15231
|
ZN185_HUMAN
|
MSISALGGRTKGKPLPPGEEERNNVLKQMKVRTTLKGDKSWITKQDESEGRTIELPSGRSRATSFSSAGEVPKPRPPSTRAPTGYIIRGVFTKPIDSSSQPQQQFPKANGTPKSAASLVRTANAGPPRPSSSGYKMTTEDYKKLAPYNIRRSSTSGDTEEEEEEEVVPFSSDEQKRRSEAASGVLRRTAPREHSYVLSAAKKSTGPTQETQAPFIAKRVEVVEEDGPSEKSQDPPALARSTPGSNSADGGRTKASRAIWIECLPSMPSPAGSQELSSRGEEIVRLQILTPRAGLRLVAPDVEGMRSSPGNKDKEAPCSRELQRDLAGEEAFRAPNTDAARSSAQLSDGNVGSGATGSRPEGLAAVDIGSERGSSSATSVSAVPADRKSNSTAAQEDAKADPKGALADYEGKDVATRVGEAWQERPGAPRGGQGDPAVPAQQPADPSTPERQSSPSGSEQLVRRESCGSSVLTDFEGKDVATKVGEAWQDRPGAPRGGQGDPAVPTQQPADPSTPEQQNSPSGSEQFVRRESCTSRVRSPSSCMVTVTVTATSEQPHIYIPAPASELDSSSTTKGILFVKEYVNASEVSSGKPVSARYSNVSSIEDSFAMEKKPPCGSTPYSERTTGGICTYCNREIRDCPKITLEHLGICCHEYCFKCGICSKPMGDLLDQIFIHRDTIHCGKCYEKLF
| null | null | null |
cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; focal adhesion [GO:0005925]
|
zinc ion binding [GO:0008270]
| null |
2.10.110.10;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16799630}. Cell junction, focal adhesion {ECO:0000269|PubMed:16799630}.
| null | null | null | null | null |
FUNCTION: May be involved in the regulation of cellular proliferation and/or differentiation.
|
Homo sapiens (Human)
|
O15232
|
MATN3_HUMAN
|
MPRPAPARRLPGLLLLLWPLLLLPSAAPDPVARPGFRRLETRGPGGSPGRRPSPAAPDGAPASGTSEPGRARGAGVCKSRPLDLVFIIDSSRSVRPLEFTKVKTFVSRIIDTLDIGPADTRVAVVNYASTVKIEFQLQAYTDKQSLKQAVGRITPLSTGTMSGLAIQTAMDEAFTVEAGAREPSSNIPKVAIIVTDGRPQDQVNEVAARAQASGIELYAVGVDRADMASLKMMASEPLEEHVFYVETYGVIEKLSSRFQETFCALDPCVLGTHQCQHVCISDGEGKHHCECSQGYTLNADKKTCSALDRCALNTHGCEHICVNDRSGSYHCECYEGYTLNEDRKTCSAQDKCALGTHGCQHICVNDRTGSHHCECYEGYTLNADKKTCSVRDKCALGSHGCQHICVSDGAASYHCDCYPGYTLNEDKKTCSATEEARRLVSTEDACGCEATLAFQDKVSSYLQRLNTKLDDILEKLKINEYGQIHR
| null | null |
cartilage development [GO:0051216]; extracellular matrix organization [GO:0030198]; skeletal system development [GO:0001501]
|
collagen-containing extracellular matrix [GO:0062023]; endoplasmic reticulum lumen [GO:0005788]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; matrilin complex [GO:0120216]
|
calcium ion binding [GO:0005509]; extracellular matrix structural constituent [GO:0005201]
|
PF12662;PF07645;PF14670;PF10393;PF00092;
|
1.20.5.30;2.10.25.10;3.40.50.410;
| null | null |
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O35701}.
| null | null | null | null | null |
FUNCTION: Major component of the extracellular matrix of cartilage and may play a role in the formation of extracellular filamentous networks.
|
Homo sapiens (Human)
|
O15234
|
CASC3_HUMAN
|
MADRRRQRASQDTEDEESGASGSDSGGSPLRGGGSCSGSAGGGGSGSLPSQRGGRTGALHLRRVESGGAKSAEESECESEDGIEGDAVLSDYESAEDSEGEEGEYSEEENSKVELKSEANDAVNSSTKEEKGEEKPDTKSTVTGERQSGDGQESTEPVENKVGKKGPKHLDDDEDRKNPAYIPRKGLFFEHDLRGQTQEEEVRPKGRQRKLWKDEGRWEHDKFREDEQAPKSRQELIALYGYDIRSAHNPDDIKPRRIRKPRYGSPPQRDPNWNGERLNKSHRHQGLGGTLPPRTFINRNAAGTGRMSAPRNYSRSGGFKEGRAGFRPVEAGGQHGGRSGETVKHEISYRSRRLEQTSVRDPSPEADAPVLGSPEKEEAASEPPAAAPDAAPPPPDRPIEKKSYSRARRTRTKVGDAVKLAEEVPPPPEGLIPAPPVPETTPTPPTKTGTWEAPVDSSTSGLEQDVAQLNIAEQNWSPGQPSFLQPRELRGMPNHIHMGAGPPPQFNRMEEMGVQGGRAKRYSSQRQRPVPEPPAPPVHISIMEGHYYDPLQFQGPIYTHGDSPAPLPPQGMLVQPGMNLPHPGLHPHQTPAPLPNPGLYPPPVSMSPGQPPPQQLLAPTYFSAPGVMNFGNPSYPYAPGALPPPPPPHLYPNTQAPSQVYGGVTYYNPAQQQVQPKPSPPRRTPQPVTIKPPPPEVVSRGSS
| null | null |
intracellular mRNA localization [GO:0008298]; mRNA export from nucleus [GO:0006406]; mRNA splicing, via spliceosome [GO:0000398]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:2000622]; regulation of translation [GO:0006417]
|
cytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829]; dendrite [GO:0030425]; exon-exon junction complex [GO:0035145]; nuclear membrane [GO:0031965]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; U2-type catalytic step 1 spliceosome [GO:0071006]
|
enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; mRNA binding [GO:0003729]; RNA binding [GO:0003723]; ubiquitin protein ligase binding [GO:0031625]
|
PF09405;
| null |
CASC3 family
|
PTM: ADP-ribosylated by tankyrase TNKS and TNKS2. Poly-ADP-ribosylated protein is recognized by RNF146, followed by ubiquitination. {ECO:0000269|PubMed:21478859}.; PTM: Ubiquitinated by RNF146 when poly-ADP-ribosylated, leading to its degradation. {ECO:0000269|PubMed:21478859}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12080473}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8K3W3}. Nucleus {ECO:0000269|PubMed:12080473, ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:29301961}. Nucleus speckle {ECO:0000269|PubMed:16170325}. Cytoplasm, Stress granule {ECO:0000269|PubMed:17652158}. Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000250|UniProtKB:Q8K3X0}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q8K3X0}. Note=Shuttles between the nucleus and the cytoplasm in a XPO1/CRM1-dependent manner. Transported to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA (PubMed:15166247). In nuclear speckles, colocalizes with MAGOH. Under stress conditions, colocalizes with FMR1 and TIA1, but not MAGOH and RBM8A EJC core factors, in cytoplasmic stress granules (PubMed:17652158). In the dendrites of hippocampal neurons, localizes to dendritic ribonucleoprotein granules (By similarity). {ECO:0000250|UniProtKB:Q8K3X0, ECO:0000269|PubMed:15166247, ECO:0000269|PubMed:17652158}.
| null | null | null | null | null |
FUNCTION: Required for pre-mRNA splicing as component of the spliceosome (PubMed:28502770, PubMed:29301961). Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). Stimulates the ATPase and RNA-helicase activities of EIF4A3. Plays a role in the stress response by participating in cytoplasmic stress granules assembly and by favoring cell recovery following stress. Component of the dendritic ribonucleoprotein particles (RNPs) in hippocampal neurons. May play a role in mRNA transport. Binds spliced mRNA in sequence-independent manner, 20-24 nucleotides upstream of mRNA exon-exon junctions. Binds poly(G) and poly(U) RNA homomer. {ECO:0000269|PubMed:17375189, ECO:0000269|PubMed:17652158, ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:29301961}.
|
Homo sapiens (Human)
|
O15239
|
NDUA1_HUMAN
|
MWFEILPGLSVMGVCLLIPGLATAYIHRFTNGGKEKRVAHFGYHWSLMERDRRISGVDRYYVSKGLENID
| null | null |
aerobic respiration [GO:0009060]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; mitochondrial respiratory chain complex I assembly [GO:0032981]; proton motive force-driven mitochondrial ATP synthesis [GO:0042776]
|
mitochondrial inner membrane [GO:0005743]; mitochondrial membrane [GO:0031966]; mitochondrial respiratory chain complex I [GO:0005747]; mitochondrion [GO:0005739]
|
NADH dehydrogenase (ubiquinone) activity [GO:0008137]
|
PF15879;
| null |
Complex I NDUFA1 subunit family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305|PubMed:12611891}; Single-pass membrane protein {ECO:0000255}; Matrix side {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. {ECO:0000269|PubMed:27626371}.
|
Homo sapiens (Human)
|
O15240
|
VGF_HUMAN
|
MKALRLSASALFCLLLINGLGAAPPGRPEAQPPPLSSEHKEPVAGDAVPGPKDGSAPEVRGARNSEPQDEGELFQGVDPRALAAVLLQALDRPASPPAPSGSQQGPEEEAAEALLTETVRSQTHSLPAPESPEPAAPPRPQTPENGPEASDPSEELEALASLLQELRDFSPSSAKRQQETAAAETETRTHTLTRVNLESPGPERVWRASWGEFQARVPERAPLPPPAPSQFQARMPDSGPLPETHKFGEGVSSPKTHLGEALAPLSKAYQGVAAPFPKARRPESALLGGSEAGERLLQQGLAQVEAGRRQAEATRQAAAQEERLADLASDLLLQYLLQGGARQRGLGGRGLQEAAEERESAREEEEAEQERRGGEERVGEEDEEAAEAEAEAEEAERARQNALLFAEEEDGEAGAEDKRSQEETPGHRRKEAEGTEEGGEEEDDEEMDPQTIDSLIELSTKLHLPADDVVSIIEEVEEKRKRKKNAPPEPVPPPRAAPAPTHVRSPQPPPPAPAPARDELPDWNEVLPPWDREEDEVYPPGPYHPFPNYIRPRTLQPPSALRRRHYHHALPPSRHYPGREAQARRAQEEAEAEERRLQEQEELENYIEHVLLRRP
| null | null |
carbohydrate homeostasis [GO:0033500]; defense response to bacterium [GO:0042742]; generation of precursor metabolites and energy [GO:0006091]; glucose homeostasis [GO:0042593]; insulin secretion [GO:0030073]; ovarian follicle development [GO:0001541]; regulation of neuronal synaptic plasticity [GO:0048168]; regulation of synaptic plasticity [GO:0048167]; response to cAMP [GO:0051591]; response to cold [GO:0009409]; response to dietary excess [GO:0002021]; response to insulin [GO:0032868]; sexual reproduction [GO:0019953]; synaptic signaling via neuropeptide [GO:0099538]
|
cytoplasmic vesicle [GO:0031410]; endoplasmic reticulum lumen [GO:0005788]; extracellular space [GO:0005615]; glutamatergic synapse [GO:0098978]; Golgi apparatus [GO:0005794]; intracellular membrane-bounded organelle [GO:0043231]; neuronal cell body [GO:0043025]; transport vesicle [GO:0030133]
|
growth factor activity [GO:0008083]; hormone activity [GO:0005179]; neuropeptide hormone activity [GO:0005184]
| null | null | null |
PTM: Multiple peptides are derived from VGF, with activities in synaptic plasticity, antidepression, penile erection, autonomic activation, and increases in energy expenditure. {ECO:0000250}.
|
SUBCELLULAR LOCATION: [Neurosecretory protein VGF]: Secreted {ECO:0000269|PubMed:19194657}. Cytoplasmic vesicle, secretory vesicle {ECO:0000269|PubMed:19194657}. Note=Stored in secretory vesicles and then secreted, NERP peptides colocalize with vasopressin in the storage granules of hypothalamus.
| null | null | null | null | null |
FUNCTION: [Neurosecretory protein VGF]: Secreted polyprotein that is packaged and proteolytically processed by prohormone convertases PCSK1 and PCSK2 in a cell-type-specific manner (By similarity). VGF and peptides derived from its processing play many roles in neurogenesis and neuroplasticity associated with learning, memory, depression and chronic pain (By similarity). {ECO:0000250|UniProtKB:P20156, ECO:0000250|UniProtKB:Q0VGU4}.; FUNCTION: [Neuroendocrine regulatory peptide-1]: Plays a role in the control of body fluid homeostasis by regulating vasopressin release. Suppresses presynaptic glutamatergic neurons connected to vasopressin neurons. {ECO:0000250|UniProtKB:P20156}.; FUNCTION: [Neuroendocrine regulatory peptide-2]: Plays a role in the control of body fluid homeostasis by regulating vasopressin release. Activates GABAergic interneurons which are inhibitory neurons of the nervous system and thereby suppresses presynaptic glutamatergic neurons (By similarity). Stimulates also feeding behavior in an orexin-dependent manner in the hypothalamus (By similarity). Functions as a positive regulator for the activation of orexin neurons resulting in elevated gastric acid secretion and gastric emptying (By similarity). {ECO:0000250|UniProtKB:P20156}.; FUNCTION: [VGF-derived peptide TLQP-21]: Secreted multifunctional neuropeptide that binds to different cell receptors and thereby plays multiple physiological roles including modulation of energy expenditure, pain, response to stress, gastric regulation, glucose homeostasis as well as lipolysis (By similarity). Activates the G-protein-coupled receptor C3AR1 via a folding-upon-binding mechanism leading to enhanced lipolysis in adipocytes (By similarity). Interacts with C1QBP receptor in macrophages and microglia causing increased levels of intracellular calcium and hypersensitivity (By similarity). {ECO:0000250|UniProtKB:P20156, ECO:0000250|UniProtKB:Q0VGU4}.; FUNCTION: [VGF-derived peptide TLQP-62]: Plays a role in the regulation of memory formation and depression-related behaviors potentially by influencing synaptic plasticity and neurogenesis. Induces acute and transient activation of the NTRK2/TRKB receptor and subsequent CREB phosphorylation (By similarity). Induces also insulin secretion in insulinoma cells by increasing intracellular calcium mobilization (By similarity). {ECO:0000250|UniProtKB:Q0VGU4}.; FUNCTION: [Antimicrobial peptide VGF[554-577]]: Has bactericidal activity against M. luteus, and antifungal activity against P. Pastoris. {ECO:0000269|PubMed:23250050}.
|
Homo sapiens (Human)
|
O15243
|
OBRG_HUMAN
|
MAGVKALVALSFSGAIGLTFLMLGCALEDYGVYWPLFVLIFHAISPIPHFIAKRVTYDSDATSSACRELAYFFTTGIVVSAFGFPVILARVAVIKWGACGLVLAGNAVIFLTIQGFFLIFGRGDDFSWEQW
| null | null |
late endosome to vacuole transport via multivesicular body sorting pathway [GO:0032511]; negative regulation of growth hormone receptor signaling pathway [GO:0060400]; negative regulation of protein localization to cell surface [GO:2000009]; negative regulation of receptor signaling pathway via JAK-STAT [GO:0046426]; positive regulation of protein targeting to mitochondrion [GO:1903955]
|
endosome [GO:0005768]; endosome membrane [GO:0010008]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]
|
signaling receptor binding [GO:0005102]
|
PF04133;
| null |
OB-RGRP/VPS55 family
| null |
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endosome membrane {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Negatively regulates leptin receptor (LEPR) cell surface expression, and thus decreases response to leptin. Negatively regulates growth hormone (GH) receptor cell surface expression in liver. May play a role in liver resistance to GH during periods of reduced nutrient availability. {ECO:0000269|PubMed:18042720, ECO:0000269|PubMed:19907080}.
|
Homo sapiens (Human)
|
O15244
|
S22A2_HUMAN
|
MPTTVDDVLEHGGEFHFFQKQMFFLLALLSATFAPIYVGIVFLGFTPDHRCRSPGVAELSLRCGWSPAEELNYTVPGPGPAGEASPRQCRRYEVDWNQSTFDCVDPLASLDTNRSRLPLGPCRDGWVYETPGSSIVTEFNLVCANSWMLDLFQSSVNVGFFIGSMSIGYIADRFGRKLCLLTTVLINAAAGVLMAISPTYTWMLIFRLIQGLVSKAGWLIGYILITEFVGRRYRRTVGIFYQVAYTVGLLVLAGVAYALPHWRWLQFTVSLPNFFFLLYYWCIPESPRWLISQNKNAEAMRIIKHIAKKNGKSLPASLQRLRLEEETGKKLNPSFLDLVRTPQIRKHTMILMYNWFTSSVLYQGLIMHMGLAGDNIYLDFFYSALVEFPAAFMIILTIDRIGRRYPWAASNMVAGAACLASVFIPGDLQWLKIIISCLGRMGITMAYEIVCLVNAELYPTFIRNLGVHICSSMCDIGGIITPFLVYRLTNIWLELPLMVFGVLGLVAGGLVLLLPETKGKALPETIEEAENMQRPRKNKEKMIYLQVQKLDIPLN
| null | null |
acetylcholine transport [GO:0015870]; activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; amine transport [GO:0015837]; amino acid import across plasma membrane [GO:0089718]; body fluid secretion [GO:0007589]; cellular detoxification [GO:1990748]; choline transport [GO:0015871]; dopamine transport [GO:0015872]; dopamine uptake [GO:0090494]; epinephrine transport [GO:0048241]; export across plasma membrane [GO:0140115]; histamine transport [GO:0051608]; histamine uptake [GO:0051615]; L-alpha-amino acid transmembrane transport [GO:1902475]; L-arginine import across plasma membrane [GO:0097638]; monoatomic cation transport [GO:0006812]; neurotransmitter transport [GO:0006836]; norepinephrine transport [GO:0015874]; norepinephrine uptake [GO:0051620]; organic cation transport [GO:0015695]; positive regulation of gene expression [GO:0010628]; prostaglandin transport [GO:0015732]; purine-containing compound transmembrane transport [GO:0072530]; putrescine transport [GO:0015847]; serotonin transport [GO:0006837]; serotonin uptake [GO:0051610]; spermidine transport [GO:0015848]; thiamine transmembrane transport [GO:0071934]; transport across blood-brain barrier [GO:0150104]; xenobiotic transport [GO:0042908]; xenobiotic transport across blood-brain barrier [GO:1990962]
|
apical plasma membrane [GO:0016324]; basal plasma membrane [GO:0009925]; basolateral plasma membrane [GO:0016323]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; plasma membrane [GO:0005886]; presynapse [GO:0098793]
|
acetylcholine transmembrane transporter activity [GO:0005277]; amine transmembrane transporter activity [GO:0005275]; choline transmembrane transporter activity [GO:0015220]; efflux transmembrane transporter activity [GO:0015562]; L-amino acid transmembrane transporter activity [GO:0015179]; L-arginine transmembrane transporter activity [GO:0061459]; monoamine transmembrane transporter activity [GO:0008504]; neurotransmitter transmembrane transporter activity [GO:0005326]; organic anion transmembrane transporter activity [GO:0008514]; organic cation transmembrane transporter activity [GO:0015101]; prostaglandin transmembrane transporter activity [GO:0015132]; putrescine transmembrane transporter activity [GO:0015489]; pyrimidine nucleoside transmembrane transporter activity [GO:0015214]; quaternary ammonium group transmembrane transporter activity [GO:0015651]; spermidine transmembrane transporter activity [GO:0015606]; thiamine transmembrane transporter activity [GO:0015234]; toxin transmembrane transporter activity [GO:0019534]; xenobiotic transmembrane transporter activity [GO:0042910]
|
PF00083;
|
1.20.1250.20;
|
Major facilitator (TC 2.A.1) superfamily, Organic cation transporter (TC 2.A.1.19) family
|
PTM: Tyrosine phosphorylated by tyrosine-protein kinase YES1. {ECO:0000269|PubMed:26979622}.
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SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000250|UniProtKB:Q9R0W2}; Multi-pass membrane protein {ECO:0000305}. Basal cell membrane {ECO:0000269|PubMed:35307651}; Multi-pass membrane protein {ECO:0000305}. Apical cell membrane {ECO:0000269|PubMed:15817714, ECO:0000269|PubMed:9260930}; Multi-pass membrane protein {ECO:0000305}. Note=Localized to the basal membrane of Sertoli cells (PubMed:35307651). Localized to the basolateral membrane of proximal tubule (PubMed:11912245). Localized to the luminal/apical membrane of distal tubule (PubMed:9260930). Localized to the luminal/apical membrane of ciliated epithelial cells in bronchi (PubMed:15817714). {ECO:0000269|PubMed:11912245, ECO:0000269|PubMed:15817714, ECO:0000269|PubMed:35307651, ECO:0000269|PubMed:9260930}.
|
CATALYTIC ACTIVITY: Reaction=(R)-noradrenaline(out) = (R)-noradrenaline(in); Xref=Rhea:RHEA:73871, ChEBI:CHEBI:72587; Evidence={ECO:0000269|PubMed:16581093, ECO:0000269|PubMed:9687576}; CATALYTIC ACTIVITY: Reaction=(R)-adrenaline(out) = (R)-adrenaline(in); Xref=Rhea:RHEA:73875, ChEBI:CHEBI:71406; Evidence={ECO:0000269|PubMed:16581093}; CATALYTIC ACTIVITY: Reaction=serotonin(out) = serotonin(in); Xref=Rhea:RHEA:73867, ChEBI:CHEBI:350546; Evidence={ECO:0000269|PubMed:16581093, ECO:0000269|PubMed:9687576}; CATALYTIC ACTIVITY: Reaction=dopamine(out) = dopamine(in); Xref=Rhea:RHEA:73863, ChEBI:CHEBI:59905; Evidence={ECO:0000269|PubMed:16581093, ECO:0000269|PubMed:9687576}; CATALYTIC ACTIVITY: Reaction=histamine(out) = histamine(in); Xref=Rhea:RHEA:73879, ChEBI:CHEBI:58432; Evidence={ECO:0000269|PubMed:16581093, ECO:0000269|PubMed:17460754, ECO:0000269|PubMed:9687576}; CATALYTIC ACTIVITY: Reaction=thiamine(in) = thiamine(out); Xref=Rhea:RHEA:34919, ChEBI:CHEBI:18385; Evidence={ECO:0000269|PubMed:24961373}; CATALYTIC ACTIVITY: Reaction=creatinine(in) = creatinine(out); Xref=Rhea:RHEA:74539, ChEBI:CHEBI:16737; Evidence={ECO:0000269|PubMed:15212162, ECO:0000269|PubMed:17072098}; CATALYTIC ACTIVITY: Reaction=1-methylnicotinamide(out) = 1-methylnicotinamide(in); Xref=Rhea:RHEA:73859, ChEBI:CHEBI:16797; Evidence={ECO:0000269|PubMed:9260930}; CATALYTIC ACTIVITY: Reaction=guanidine(out) = guanidine(in); Xref=Rhea:RHEA:73883, ChEBI:CHEBI:30087; Evidence={ECO:0000269|PubMed:12089365}; CATALYTIC ACTIVITY: Reaction=choline(out) = choline(in); Xref=Rhea:RHEA:32751, ChEBI:CHEBI:15354; Evidence={ECO:0000269|PubMed:9260930}; CATALYTIC ACTIVITY: Reaction=agmatine(out) = agmatine(in); Xref=Rhea:RHEA:72131, ChEBI:CHEBI:58145; Evidence={ECO:0000269|PubMed:12538837, ECO:0000269|PubMed:21128598}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72132; Evidence={ECO:0000305|PubMed:21128598}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:72133; Evidence={ECO:0000305|PubMed:21128598}; CATALYTIC ACTIVITY: Reaction=putrescine(out) = putrescine(in); Xref=Rhea:RHEA:72135, ChEBI:CHEBI:326268; Evidence={ECO:0000269|PubMed:21128598}; CATALYTIC ACTIVITY: Reaction=spermidine(in) = spermidine(out); Xref=Rhea:RHEA:35039, ChEBI:CHEBI:57834; Evidence={ECO:0000250|UniProtKB:O70577}; CATALYTIC ACTIVITY: Reaction=tyramine(in) = tyramine(out); Xref=Rhea:RHEA:74783, ChEBI:CHEBI:327995; Evidence={ECO:0000269|PubMed:17460754}; CATALYTIC ACTIVITY: Reaction=L-histidyl-L-proline diketopiperazine(in) = L-histidyl-L-proline diketopiperazine(out); Xref=Rhea:RHEA:74787, ChEBI:CHEBI:90039; Evidence={ECO:0000269|PubMed:17460754}; CATALYTIC ACTIVITY: Reaction=(R)-salsolinol(in) = (R)-salsolinol(out); Xref=Rhea:RHEA:74791, ChEBI:CHEBI:194082; Evidence={ECO:0000269|PubMed:17460754}; CATALYTIC ACTIVITY: Reaction=N-methyl-(R)-salsolinol(in) = N-methyl-(R)-salsolinol(out); Xref=Rhea:RHEA:74795, ChEBI:CHEBI:194083; Evidence={ECO:0000269|PubMed:17460754}; CATALYTIC ACTIVITY: Reaction=acetylcholine(in) = acetylcholine(out); Xref=Rhea:RHEA:74663, ChEBI:CHEBI:15355; Evidence={ECO:0000269|PubMed:15817714}; CATALYTIC ACTIVITY: Reaction=prostaglandin F2alpha(out) = prostaglandin F2alpha(in); Xref=Rhea:RHEA:50988, ChEBI:CHEBI:57404; Evidence={ECO:0000269|PubMed:11907186}; CATALYTIC ACTIVITY: Reaction=prostaglandin E2(out) = prostaglandin E2(in); Xref=Rhea:RHEA:50984, ChEBI:CHEBI:606564; Evidence={ECO:0000269|PubMed:11907186};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=74 uM for cyclo(his-pro) {ECO:0000269|PubMed:17460754}; KM=80 uM for serotonin {ECO:0000269|PubMed:9687576}; KM=290 uM for serotonin {ECO:0000269|PubMed:16581093}; KM=130 uM for salsolinol {ECO:0000269|PubMed:17460754}; KM=150 uM for acetylcholine {ECO:0000269|PubMed:15817714}; KM=210 uM for choline {ECO:0000269|PubMed:9260930}; KM=300 uM for NMN {ECO:0000269|PubMed:9260930}; KM=390 uM for dopamine {ECO:0000269|PubMed:9687576}; KM=420 uM for adrenaline {ECO:0000269|PubMed:16581093}; KM=750 uM for thiamine {ECO:0000269|PubMed:24961373}; KM=940 uM for histamine {ECO:0000269|PubMed:16581093}; KM=1300 uM for histamine {ECO:0000269|PubMed:9687576}; KM=1400 uM for dopamine {ECO:0000269|PubMed:16581093}; KM=1500 uM for noradrenaline {ECO:0000269|PubMed:16581093}; KM=1900 uM for noradrenaline {ECO:0000269|PubMed:9687576}; KM=4000 uM for creatinine {ECO:0000269|PubMed:15212162}; KM=19010 uM for agmatine (at pH 6.0) {ECO:0000269|PubMed:21128598}; KM=1400 uM for agmatine (at pH 7.4) {ECO:0000269|PubMed:12538837}; KM=1840 uM for agmatine (at pH 7.4) {ECO:0000269|PubMed:21128598}; KM=740 uM for agmatine (at pH 8.5) {ECO:0000269|PubMed:21128598}; KM=390 uM for agmatine (at pH 9.5) {ECO:0000269|PubMed:21128598}; KM=33450 uM for putrescine (at pH 6.0) {ECO:0000269|PubMed:21128598}; KM=11290 uM for putrescine (at pH 7.4) {ECO:0000269|PubMed:21128598}; KM=3600 uM for putrescine (at pH 8.5) {ECO:0000269|PubMed:21128598}; KM=1410 uM for putrescine (at pH 9.5) {ECO:0000269|PubMed:21128598}; KM=0.0289 uM for prostaglandin E2 {ECO:0000269|PubMed:11907186}; KM=0.334 uM for prostaglandin F2-alpha {ECO:0000269|PubMed:11907186}; KM=19 uM for MPP {ECO:0000269|PubMed:9260930}; KM=24 uM for ASP (at 8 degrees Celsius) {ECO:0000269|PubMed:16394027}; Vmax=3 nmol/min/mg enzyme for cyclo(his-pro) uptake {ECO:0000269|PubMed:17460754}; Vmax=2.7 nmol/min/mg enzyme for salsolinol uptake {ECO:0000269|PubMed:17460754}; Vmax=4.56 nmol/min/mg enzyme for thiamine uptake {ECO:0000269|PubMed:24961373}; Vmax=23.5 nmol/min/mg enzyme for creatinine uptake {ECO:0000269|PubMed:21128598}; Vmax=24.1 nmol/min/mg enzyme for agmatine uptake (at pH 6.0) {ECO:0000269|PubMed:21128598}; Vmax=11.5 nmol/min/mg enzyme for agmatine uptake (at pH 7.4) {ECO:0000269|PubMed:12538837}; Vmax=12.9 nmol/min/mg enzyme for agmatine uptake (at pH 7.4) {ECO:0000269|PubMed:21128598}; Vmax=13.9 nmol/min/mg enzyme for agmatine uptake (at pH 8.5) {ECO:0000269|PubMed:21128598}; Vmax=16 nmol/min/mg enzyme for agmatine uptake (at pH 9.5) {ECO:0000269|PubMed:21128598}; Vmax=24.9 nmol/min/mg enzyme for putrescine uptake (at pH 6.0) {ECO:0000269|PubMed:21128598}; Vmax=15.6 nmol/min/mg enzyme for putrescine uptake (at pH 7.4) {ECO:0000269|PubMed:21128598}; Vmax=38.9 nmol/min/mg enzyme for putrescine uptake (at pH 8.5) {ECO:0000269|PubMed:21128598}; Vmax=52.3 nmol/min/mg enzyme for putrescine uptake (at pH 9.5) {ECO:0000269|PubMed:21128598};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9 for agmatine and putrescine uptake. {ECO:0000269|PubMed:21128598};
| null |
FUNCTION: Electrogenic voltage-dependent transporter that mediates the transport of a variety of organic cations such as endogenous bioactive amines, cationic drugs and xenobiotics (PubMed:9260930, PubMed:9687576). Functions as a Na(+)-independent, bidirectional uniporter (PubMed:21128598, PubMed:9687576). Cation cellular uptake or release is driven by the electrochemical potential, i.e. membrane potential and concentration gradient (PubMed:15212162, PubMed:9260930, PubMed:9687576). However, may also engage electroneutral cation exchange when saturating concentrations of cation substrates are reached (By similarity). Predominantly expressed at the basolateral membrane of hepatocytes and proximal tubules and involved in the uptake and disposition of cationic compounds by hepatic and renal clearance from the blood flow (PubMed:15783073). Implicated in monoamine neurotransmitters uptake such as histamine, dopamine, adrenaline/epinephrine, noradrenaline/norepinephrine, serotonin and tyramine, thereby supporting a physiological role in the central nervous system by regulating interstitial concentrations of neurotransmitters (PubMed:16581093, PubMed:17460754, PubMed:9687576). Also capable of transporting dopaminergic neuromodulators cyclo(his-pro), salsolinol and N-methyl-salsolinol, thereby involved in the maintenance of dopaminergic cell integrity in the central nervous system (PubMed:17460754). Mediates the bidirectional transport of acetylcholine (ACh) at the apical membrane of ciliated cell in airway epithelium, thereby playing a role in luminal release of ACh from bronchial epithelium (PubMed:15817714). Also transports guanidine and endogenous monoamines such as vitamin B1/thiamine, creatinine and N-1-methylnicotinamide (NMN) (PubMed:12089365, PubMed:15212162, PubMed:17072098, PubMed:24961373, PubMed:9260930). Mediates the uptake and efflux of quaternary ammonium compound choline (PubMed:9260930). Mediates the bidirectional transport of polyamine agmatine and the uptake of polyamines putrescine and spermidine (PubMed:12538837, PubMed:21128598). Able to transport non-amine endogenous compounds such as prostaglandin E2 (PGE2) and prostaglandin F2-alpha (PGF2-alpha) (PubMed:11907186). Also involved in the uptake of xenobiotic 4-(4-(dimethylamino)styryl)-N-methylpyridinium (ASP) (PubMed:12395288, PubMed:16394027). May contribute to regulate the transport of organic compounds in testis across the blood-testis-barrier (Probable). {ECO:0000250|UniProtKB:Q9R0W2, ECO:0000269|PubMed:11907186, ECO:0000269|PubMed:12089365, ECO:0000269|PubMed:12395288, ECO:0000269|PubMed:12538837, ECO:0000269|PubMed:15212162, ECO:0000269|PubMed:15783073, ECO:0000269|PubMed:15817714, ECO:0000269|PubMed:16394027, ECO:0000269|PubMed:16581093, ECO:0000269|PubMed:17072098, ECO:0000269|PubMed:17460754, ECO:0000269|PubMed:21128598, ECO:0000269|PubMed:24961373, ECO:0000269|PubMed:9260930, ECO:0000269|PubMed:9687576, ECO:0000305|PubMed:35307651}.; FUNCTION: [Isoform 2]: In contrast with isoform 1, not able to transport guanidine, creatinine, cimetidine and metformin. {ECO:0000269|PubMed:12089365, ECO:0000269|PubMed:15212162, ECO:0000269|PubMed:16272756}.
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Homo sapiens (Human)
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O15245
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S22A1_HUMAN
|
MPTVDDILEQVGESGWFQKQAFLILCLLSAAFAPICVGIVFLGFTPDHHCQSPGVAELSQRCGWSPAEELNYTVPGLGPAGEAFLGQCRRYEVDWNQSALSCVDPLASLATNRSHLPLGPCQDGWVYDTPGSSIVTEFNLVCADSWKLDLFQSCLNAGFLFGSLGVGYFADRFGRKLCLLGTVLVNAVSGVLMAFSPNYMSMLLFRLLQGLVSKGNWMAGYTLITEFVGSGSRRTVAIMYQMAFTVGLVALTGLAYALPHWRWLQLAVSLPTFLFLLYYWCVPESPRWLLSQKRNTEAIKIMDHIAQKNGKLPPADLKMLSLEEDVTEKLSPSFADLFRTPRLRKRTFILMYLWFTDSVLYQGLILHMGATSGNLYLDFLYSALVEIPGAFIALITIDRVGRIYPMAMSNLLAGAACLVMIFISPDLHWLNIIIMCVGRMGITIAIQMICLVNAELYPTFVRNLGVMVCSSLCDIGGIITPFIVFRLREVWQALPLILFAVLGLLAAGVTLLLPETKGVALPETMKDAENLGRKAKPKENTIYLKVQTSEPSGT
| null | null |
acetylcholine transport [GO:0015870]; acyl carnitine transmembrane transport [GO:1902616]; cellular detoxification [GO:1990748]; dopamine transport [GO:0015872]; dopamine uptake [GO:0090494]; epinephrine transport [GO:0048241]; establishment or maintenance of transmembrane electrochemical gradient [GO:0010248]; metanephric proximal tubule development [GO:0072237]; monoamine transport [GO:0015844]; neurotransmitter transport [GO:0006836]; norepinephrine transport [GO:0015874]; organic cation transport [GO:0015695]; prostaglandin transport [GO:0015732]; purine-containing compound transmembrane transport [GO:0072530]; putrescine transport [GO:0015847]; quaternary ammonium group transport [GO:0015697]; serotonin transport [GO:0006837]; serotonin uptake [GO:0051610]; spermidine transport [GO:0015848]; thiamine transmembrane transport [GO:0071934]; thiamine transport [GO:0015888]; transport across blood-brain barrier [GO:0150104]; xenobiotic metabolic process [GO:0006805]; xenobiotic transport [GO:0042908]; xenobiotic transport across blood-brain barrier [GO:1990962]
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apical plasma membrane [GO:0016324]; basal plasma membrane [GO:0009925]; basolateral plasma membrane [GO:0016323]; lateral plasma membrane [GO:0016328]; membrane [GO:0016020]; plasma membrane [GO:0005886]; presynapse [GO:0098793]
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(R)-carnitine transmembrane transporter activity [GO:1901235]; acetylcholine transmembrane transporter activity [GO:0005277]; dopamine:sodium symporter activity [GO:0005330]; identical protein binding [GO:0042802]; monoamine transmembrane transporter activity [GO:0008504]; neurotransmitter transmembrane transporter activity [GO:0005326]; norepinephrine:sodium symporter activity [GO:0005334]; organic anion transmembrane transporter activity [GO:0008514]; organic cation transmembrane transporter activity [GO:0015101]; prostaglandin transmembrane transporter activity [GO:0015132]; putrescine transmembrane transporter activity [GO:0015489]; pyrimidine nucleoside transmembrane transporter activity [GO:0015214]; quaternary ammonium group transmembrane transporter activity [GO:0015651]; secondary active organic cation transmembrane transporter activity [GO:0008513]; spermidine transmembrane transporter activity [GO:0015606]; thiamine transmembrane transporter activity [GO:0015234]; toxin transmembrane transporter activity [GO:0019534]; xenobiotic transmembrane transporter activity [GO:0042910]
|
PF00083;
|
1.20.1250.20;
|
Major facilitator (TC 2.A.1) superfamily, Organic cation transporter (TC 2.A.1.19) family
|
PTM: Phosphorylated. {ECO:0000250|UniProtKB:Q63089}.
|
SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000269|PubMed:12719534}; Multi-pass membrane protein {ECO:0000305}. Apical cell membrane {ECO:0000269|PubMed:15817714, ECO:0000269|PubMed:19536068, ECO:0000269|PubMed:23680637}; Multi-pass membrane protein {ECO:0000305}. Lateral cell membrane {ECO:0000269|PubMed:16263091}; Multi-pass membrane protein {ECO:0000305}. Basal cell membrane {ECO:0000269|PubMed:35307651}; Multi-pass membrane protein {ECO:0000305}. Cell membrane {ECO:0000269|PubMed:35469921}; Multi-pass membrane protein {ECO:0000305}. Note=Localized to the sinusoidal/basolateral membrane of hepatocytes (By similarity). Mainly localized to the basolateral membrane of renal proximal tubular cells (By similarity). However, also identified at the apical side of proximal tubular cells (PubMed:19536068). Mainly expressed at the lateral membrane of enterocytes (PubMed:16263091). Also observed at the apical side of enterocytes (PubMed:23680637). Localized to the luminal/apical membrane of ciliated epithelial cells in bronchi (PubMed:15817714). Localized to the basal membrane of Sertoli cells (PubMed:35307651). {ECO:0000250|UniProtKB:Q63089, ECO:0000269|PubMed:15817714, ECO:0000269|PubMed:16263091, ECO:0000269|PubMed:19536068, ECO:0000269|PubMed:23680637, ECO:0000269|PubMed:35307651}.
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CATALYTIC ACTIVITY: Reaction=1-methylnicotinamide(out) = 1-methylnicotinamide(in); Xref=Rhea:RHEA:73859, ChEBI:CHEBI:16797; Evidence={ECO:0000269|PubMed:9260930}; CATALYTIC ACTIVITY: Reaction=dopamine(out) = dopamine(in); Xref=Rhea:RHEA:73863, ChEBI:CHEBI:59905; Evidence={ECO:0000269|PubMed:35469921}; CATALYTIC ACTIVITY: Reaction=serotonin(out) = serotonin(in); Xref=Rhea:RHEA:73867, ChEBI:CHEBI:350546; Evidence={ECO:0000269|PubMed:12439218, ECO:0000269|PubMed:24961373, ECO:0000269|PubMed:35469921}; CATALYTIC ACTIVITY: Reaction=(R)-adrenaline(out) = (R)-adrenaline(in); Xref=Rhea:RHEA:73875, ChEBI:CHEBI:71406; Evidence={ECO:0000269|PubMed:35469921}; CATALYTIC ACTIVITY: Reaction=histamine(out) = histamine(in); Xref=Rhea:RHEA:73879, ChEBI:CHEBI:58432; Evidence={ECO:0000269|PubMed:35469921}; CATALYTIC ACTIVITY: Reaction=guanidine(out) = guanidine(in); Xref=Rhea:RHEA:73883, ChEBI:CHEBI:30087; Evidence={ECO:0000250|UniProtKB:Q63089}; CATALYTIC ACTIVITY: Reaction=acetylcholine(in) = acetylcholine(out); Xref=Rhea:RHEA:74663, ChEBI:CHEBI:15355; Evidence={ECO:0000269|PubMed:15817714}; CATALYTIC ACTIVITY: Reaction=thiamine(in) = thiamine(out); Xref=Rhea:RHEA:34919, ChEBI:CHEBI:18385; Evidence={ECO:0000269|PubMed:24961373, ECO:0000269|PubMed:35469921}; CATALYTIC ACTIVITY: Reaction=agmatine(out) = agmatine(in); Xref=Rhea:RHEA:72131, ChEBI:CHEBI:58145; Evidence={ECO:0000269|PubMed:21128598}; CATALYTIC ACTIVITY: Reaction=putrescine(out) = putrescine(in); Xref=Rhea:RHEA:72135, ChEBI:CHEBI:326268; Evidence={ECO:0000269|PubMed:21128598}; CATALYTIC ACTIVITY: Reaction=spermidine(in) = spermidine(out); Xref=Rhea:RHEA:35039, ChEBI:CHEBI:57834; Evidence={ECO:0000250|UniProtKB:Q63089}; CATALYTIC ACTIVITY: Reaction=L-histidyl-L-proline diketopiperazine(in) = L-histidyl-L-proline diketopiperazine(out); Xref=Rhea:RHEA:74787, ChEBI:CHEBI:90039; Evidence={ECO:0000269|PubMed:17460754}; CATALYTIC ACTIVITY: Reaction=(R)-salsolinol(in) = (R)-salsolinol(out); Xref=Rhea:RHEA:74791, ChEBI:CHEBI:194082; Evidence={ECO:0000269|PubMed:17460754}; CATALYTIC ACTIVITY: Reaction=prostaglandin F2alpha(out) = prostaglandin F2alpha(in); Xref=Rhea:RHEA:50988, ChEBI:CHEBI:57404; Evidence={ECO:0000269|PubMed:11907186}; CATALYTIC ACTIVITY: Reaction=prostaglandin E2(out) = prostaglandin E2(in); Xref=Rhea:RHEA:50984, ChEBI:CHEBI:606564; Evidence={ECO:0000269|PubMed:11907186};
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BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=440 uM for salsolinol {ECO:0000269|PubMed:17460754}; KM=558 uM for adrenaline {ECO:0000269|PubMed:35469921}; KM=655 uM for cyclo(his-pro) {ECO:0000269|PubMed:17460754}; KM=663 uM for serotonin {ECO:0000269|PubMed:35469921}; KM=674 uM for dopamine {ECO:0000269|PubMed:35469921}; KM=647 nM for prostaglandin E2 {ECO:0000269|PubMed:11907186}; KM=477 nM for prostaglandin F2-alpha {ECO:0000269|PubMed:11907186}; KM=780 uM for thiamine {ECO:0000269|PubMed:24961373}; KM=1057 uM for thiamine {ECO:0000269|PubMed:35469921}; KM=4675 uM for histamine {ECO:0000269|PubMed:35469921}; KM=18730 uM for agmatine {ECO:0000269|PubMed:21128598}; KM=19.5 uM for NMQ {ECO:0000269|PubMed:11408531}; KM=11.5 uM for NMQD {ECO:0000269|PubMed:11408531}; KM=53 uM for TBuMA {ECO:0000269|PubMed:11408531}; KM=100.9 uM for APM {ECO:0000269|PubMed:11408531}; Vmax=1 nmol/min/mg enzyme for salsolinol uptake {ECO:0000269|PubMed:17460754}; Vmax=1.123 nmol/min/mg enzyme with adrenaline as substrate {ECO:0000269|PubMed:35469921}; Vmax=6.9 nmol/min/mg enzyme for cyclo(his-pro) uptake {ECO:0000269|PubMed:17460754}; Vmax=6.183 nmol/min/mg enzyme with serotonin as substrate {ECO:0000269|PubMed:35469921}; Vmax=0.718 nmol/min/mg enzyme with dopamine as substrate {ECO:0000269|PubMed:35469921}; Vmax=2.77 nmol/min/mg enzyme with thiamine as substrate {ECO:0000269|PubMed:24961373}; Vmax=8.261 nmol/min/mg enzyme with thiamine as substrate {ECO:0000269|PubMed:35469921}; Vmax=5.124 nmol/min/mg enzyme with histamine as substrate {ECO:0000269|PubMed:35469921};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5 for the transport of MPP (PubMed:11388889). While optimum pH is 6.0 for the transport of the drug quinidine, no transport activity is observed at pH 7.5, possibly due to the protonation of quininide at pH6.0 (PubMed:11408531). {ECO:0000269|PubMed:11388889, ECO:0000269|PubMed:11408531};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 22 degrees Celsius for the transport of TEA. Doesn't show any transport activity of TEA at 4 degrees Celsius. {ECO:0000269|PubMed:9655880};
|
FUNCTION: Electrogenic voltage-dependent transporter that mediates the transport of a variety of organic cations such as endogenous bioactive amines, cationic drugs and xenobiotics (PubMed:11388889, PubMed:11408531, PubMed:12439218, PubMed:12719534, PubMed:15389554, PubMed:16263091, PubMed:16272756, PubMed:16581093, PubMed:19536068, PubMed:21128598, PubMed:23680637, PubMed:24961373, PubMed:34040533, PubMed:9187257, PubMed:9260930, PubMed:9655880). Functions as a pH- and Na(+)-independent, bidirectional transporter (By similarity). Cation cellular uptake or release is driven by the electrochemical potential (i.e. membrane potential and concentration gradient) and substrate selectivity (By similarity). Hydrophobicity is a major requirement for recognition in polyvalent substrates and inhibitors (By similarity). Primarily expressed at the basolateral membrane of hepatocytes and proximal tubules and involved in the uptake and disposition of cationic compounds by hepatic and renal clearance from the blood flow (By similarity). Most likely functions as an uptake carrier in enterocytes contributing to the intestinal elimination of organic cations from the systemic circulation (PubMed:16263091). Transports endogenous monoamines such as N-1-methylnicotinamide (NMN), guanidine, histamine, neurotransmitters dopamine, serotonin and adrenaline (PubMed:12439218, PubMed:24961373, PubMed:35469921, PubMed:9260930). Also transports natural polyamines such as spermidine, agmatine and putrescine at low affinity, but relatively high turnover (PubMed:21128598). Involved in the hepatic uptake of vitamin B1/thiamine, hence regulating hepatic lipid and energy metabolism (PubMed:24961373). Mediates the bidirectional transport of acetylcholine (ACh) at the apical membrane of ciliated cell in airway epithelium, thereby playing a role in luminal release of ACh from bronchial epithelium (PubMed:15817714). Transports dopaminergic neuromodulators cyclo(his-pro) and salsolinol with lower efficency (PubMed:17460754). Also capable of transporting non-amine endogenous compounds such as prostaglandin E2 (PGE2) and prostaglandin F2-alpha (PGF2-alpha) (PubMed:11907186). May contribute to the transport of cationic compounds in testes across the blood-testis-barrier (Probable). Also involved in the uptake of xenobiotics tributylmethylammonium (TBuMA), quinidine, N-methyl-quinine (NMQ), N-methyl-quinidine (NMQD) N-(4,4-azo-n-pentyl)-quinuclidine (APQ), azidoprocainamide methoiodide (AMP), N-(4,4-azo-n-pentyl)-21-deoxyajmalinium (APDA) and 4-(4-(dimethylamino)styryl)-N-methylpyridinium (ASP) (PubMed:11408531, PubMed:15389554, PubMed:35469921, PubMed:9260930). {ECO:0000250|UniProtKB:O08966, ECO:0000250|UniProtKB:Q63089, ECO:0000269|PubMed:11388889, ECO:0000269|PubMed:11408531, ECO:0000269|PubMed:11907186, ECO:0000269|PubMed:12439218, ECO:0000269|PubMed:12719534, ECO:0000269|PubMed:15389554, ECO:0000269|PubMed:15817714, ECO:0000269|PubMed:16263091, ECO:0000269|PubMed:16272756, ECO:0000269|PubMed:16581093, ECO:0000269|PubMed:17460754, ECO:0000269|PubMed:19536068, ECO:0000269|PubMed:21128598, ECO:0000269|PubMed:23680637, ECO:0000269|PubMed:24961373, ECO:0000269|PubMed:34040533, ECO:0000269|PubMed:35469921, ECO:0000269|PubMed:9187257, ECO:0000269|PubMed:9260930, ECO:0000269|PubMed:9655880, ECO:0000305|PubMed:35307651}.; FUNCTION: [Isoform 1]: Mediates the uptake of 1-methyl-4-phenylpyridinium (MPP(+)). {ECO:0000269|PubMed:11388889}.; FUNCTION: [Isoform 2]: Not able to uptake 1-methyl-4-phenylpyridinium (MPP(+)). {ECO:0000269|PubMed:11388889}.; FUNCTION: [Isoform 3]: Not able to uptake 1-methyl-4-phenylpyridinium (MPP(+)). {ECO:0000269|PubMed:11388889}.; FUNCTION: [Isoform 4]: Not able to uptake 1-methyl-4-phenylpyridinium (MPP(+)). {ECO:0000269|PubMed:11388889}.
|
Homo sapiens (Human)
|
O15247
|
CLIC2_HUMAN
|
MSGLRPGTQVDPEIELFVKAGSDGESIGNCPFCQRLFMILWLKGVKFNVTTVDMTRKPEELKDLAPGTNPPFLVYNKELKTDFIKIEEFLEQTLAPPRYPHLSPKYKESFDVGCNLFAKFSAYIKNTQKEANKNFEKSLLKEFKRLDDYLNTPLLDEIDPDSAEEPPVSRRLFLDGDQLTLADCSLLPKLNIIKVAAKKYRDFDIPAEFSGVWRYLHNAYAREEFTHTCPEDKEIENTYANVAKQKS
| null | null |
chloride transport [GO:0006821]; negative regulation of ryanodine-sensitive calcium-release channel activity [GO:0060315]; positive regulation of binding [GO:0051099]; regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion [GO:0010881]; regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum [GO:0010880]; signal transduction [GO:0007165]
|
chloride channel complex [GO:0034707]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
chloride channel activity [GO:0005254]; glutathione peroxidase activity [GO:0004602]
|
PF13410;PF13409;
|
1.20.1050.10;3.40.30.10;
|
Chloride channel CLIC family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15916532}. Membrane {ECO:0000305|PubMed:15916532}; Single-pass membrane protein {ECO:0000305|PubMed:15916532}. Note=Exists both as soluble cytoplasmic protein and as membrane protein with probably a single transmembrane domain.
| null | null | null | null | null |
FUNCTION: Can insert into membranes and form chloride ion channels. Channel activity depends on the pH. Membrane insertion seems to be redox-regulated and may occur only under oxydizing conditions. Modulates the activity of RYR2 and inhibits calcium influx. {ECO:0000269|PubMed:15147738, ECO:0000269|PubMed:15916532, ECO:0000269|PubMed:17945253}.
|
Homo sapiens (Human)
|
O15254
|
ACOX3_HUMAN
|
MASTVEGGDTALLPEFPRGPLDAYRARASFSWKELALFTEGEGMLRFKKTIFSALENDPLFARSPGADLSLEKYRELNFLRCKRIFEYDFLSVEDMFKSPLKVPALIQCLGMYDSSLAAKYLLHSLVFGSAVYSSGSERHLTYIQKIFRMEIFGCFALTELSHGSNTKAIRTTAHYDPATEEFIIHSPDFEAAKFWVGNMGKTATHAVVFAKLCVPGDQCHGLHPFIVQIRDPKTLLPMPGVMVGDIGKKLGQNGLDNGFAMFHKVRVPRQSLLNRMGDVTPEGTYVSPFKDVRQRFGASLGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFGPTEEEEIPVLEYPMQQWRLLPYLAAVYALDHFSKSLFLDLVELQRGLASGDRSARQAELGREIHALASASKPLASWTTQQGIQECREACGGHGYLAMNRLGVLRDDNDPNCTYEGDNNILLQQTSNYLLGLLAHQVHDGACFRSPLKSVDFLDAYPGILDQKFEVSSVADCLDSAVALAAYKWLVCYLLRETYQKLNQEKRSGSSDFEARNKCQVSHGRPLALAFVELTVVQRFHEHVHQPSVPPSLRAVLGRLSALYALWSLSRHAALLYRGGYFSGEQAGEVLESAVLALCSQLKDDAVALVDVIAPPDFVLDSPIGRADGELYKNLWGAVLQESKVLERASWWPEFSVNKPVIGSLKSKL
|
1.3.3.6
|
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:P07872};
|
fatty acid beta-oxidation using acyl-CoA oxidase [GO:0033540]; lipid homeostasis [GO:0055088]
|
cytosol [GO:0005829]; membrane [GO:0016020]; peroxisomal matrix [GO:0005782]; peroxisome [GO:0005777]
|
FAD binding [GO:0071949]; fatty acid binding [GO:0005504]; flavin adenine dinucleotide binding [GO:0050660]; pristanoyl-CoA oxidase activity [GO:0016402]
|
PF01756;PF02770;
|
2.40.110.10;1.20.140.10;
|
Acyl-CoA oxidase family
| null |
SUBCELLULAR LOCATION: Peroxisome {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-CoA + O2 = a (2E)-enoyl-CoA + H2O2; Xref=Rhea:RHEA:38959, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:58856, ChEBI:CHEBI:65111; EC=1.3.3.6; Evidence={ECO:0000250|UniProtKB:Q63448}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38960; Evidence={ECO:0000250|UniProtKB:Q63448}; CATALYTIC ACTIVITY: Reaction=(2S)-pristanoyl-CoA + O2 = (2E)-pristenoyl-CoA + H2O2; Xref=Rhea:RHEA:40459, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:77099, ChEBI:CHEBI:77293; Evidence={ECO:0000250|UniProtKB:Q63448}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40460; Evidence={ECO:0000250|UniProtKB:Q63448}; CATALYTIC ACTIVITY: Reaction=O2 + tetracosanoyl-CoA = (2E)-tetracosenoyl-CoA + H2O2; Xref=Rhea:RHEA:40319, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:65052, ChEBI:CHEBI:74693; Evidence={ECO:0000250|UniProtKB:Q63448}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40320; Evidence={ECO:0000250|UniProtKB:Q63448}; CATALYTIC ACTIVITY: Reaction=hexadecanoyl-CoA + O2 = (2E)-hexadecenoyl-CoA + H2O2; Xref=Rhea:RHEA:40167, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:57379, ChEBI:CHEBI:61526; Evidence={ECO:0000250|UniProtKB:Q63448}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40168; Evidence={ECO:0000250|UniProtKB:Q63448}; CATALYTIC ACTIVITY: Reaction=hexadecanedioyl-CoA + O2 = (2E)-hexadecenedioyl-CoA + H2O2; Xref=Rhea:RHEA:40275, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:77075, ChEBI:CHEBI:77085; Evidence={ECO:0000250|UniProtKB:Q63448}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40276; Evidence={ECO:0000250|UniProtKB:Q63448};
| null |
PATHWAY: Lipid metabolism; peroxisomal fatty acid beta-oxidation.
| null | null |
FUNCTION: Oxidizes the CoA-esters of 2-methyl-branched fatty acids. {ECO:0000250|UniProtKB:Q63448}.
|
Homo sapiens (Human)
|
O15258
|
RER1_HUMAN
|
MSEGDSVGESVHGKPSVVYRFFTRLGQIYQSWLDKSTPYTAVRWVVTLGLSFVYMIRVYLLQGWYIVTYALGIYHLNLFIAFLSPKVDPSLMEDSDDGPSLPTKQNEEFRPFIRRLPEFKFWHAATKGILVAMVCTFFDAFNVPVFWPILVMYFIMLFCITMKRQIKHMIKYRYIPFTHGKRRYRGKEDAGKAFAS
| null | null |
positive regulation of protein localization to plasma membrane [GO:1903078]; protein retention in ER lumen [GO:0006621]; retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum [GO:0006890]; skeletal muscle acetylcholine-gated channel clustering [GO:0071340]
|
cell surface [GO:0009986]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; plasma membrane [GO:0005886]
|
acetylcholine receptor binding [GO:0033130]
|
PF03248;
| null |
RER1 family
| null |
SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass membrane protein.
| null | null | null | null | null |
FUNCTION: Involved in the retrieval of endoplasmic reticulum membrane proteins from the early Golgi compartment. {ECO:0000250}.
|
Homo sapiens (Human)
|
O15259
|
NPHP1_HUMAN
|
MLARRQRDPLQALRRRNQELKQQVDSLLSESQLKEALEPNKRQHIYQRCIQLKQAIDENKNALQKLSKADESAPVANYNQRKEEEHTLLDKLTQQLQGLAVTISRENITEVGAPTEEEEESESEDSEDSGGEEEDAEEEEEEKEENESHKWSTGEEYIAVGDFTAQQVGDLTFKKGEILLVIEKKPDGWWIAKDAKGNEGLVPRTYLEPYSEEEEGQESSEEGSEEDVEAVDETADGAEVKQRTDPHWSAVQKAISEAGIFCLVNHVSFCYLIVLMRNRMETVEDTNGSETGFRAWNVQSRGRIFLVSKPVLQINTVDVLTTMGAIPAGFRPSTLSQLLEEGNQFRANYFLQPELMPSQLAFRDLMWDATEGTIRSRPSRISLILTLWSCKMIPLPGMSIQVLSRHVRLCLFDGNKVLSNIHTVRATWQPKKPKTWTFSPQVTRILPCLLDGDCFIRSNSASPDLGILFELGISYIRNSTGERGELSCGWVFLKLFDASGVPIPAKTYELFLNGGTPYEKGIEVDPSISRRAHGSVFYQIMTMRRQPQLLVKLRSLNRRSRNVLSLLPETLIGNMCSIHLLIFYRQILGDVLLKDRMSLQSTDLISHPMLATFPMLLEQPDVMDALRSSWAGKESTLKRSEKRDKEFLKSTFLLVYHDCVLPLLHSTRLPPFRWAEEETETARWKVITDFLKQNQENQGALQALLSPDGVHEPFDLSEQTYDFLGEMRKNAV
| null | null |
actin cytoskeleton organization [GO:0030036]; cell projection organization [GO:0030030]; cell-cell adhesion [GO:0098609]; positive regulation of bicellular tight junction assembly [GO:1903348]; protein localization involved in establishment of planar polarity [GO:0090251]; retina development in camera-type eye [GO:0060041]; signal transduction [GO:0007165]; spermatid differentiation [GO:0048515]; visual behavior [GO:0007632]
|
adherens junction [GO:0005912]; bicellular tight junction [GO:0005923]; cell-cell junction [GO:0005911]; cilium [GO:0005929]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; membrane [GO:0016020]; motile cilium [GO:0031514]; photoreceptor connecting cilium [GO:0032391]
|
structural molecule activity [GO:0005198]
|
PF00018;
|
2.30.30.40;
|
Nephrocystin-1 family
|
PTM: Phosphorylation by CK2 is required for the interaction with PACS1 and the targeting to the base region of cilia. {ECO:0000269|PubMed:16308564, ECO:0000269|PubMed:21357692}.
|
SUBCELLULAR LOCATION: Cell junction {ECO:0000250|UniProtKB:Q9QY53}. Cell junction, adherens junction {ECO:0000250|UniProtKB:Q9QY53}. Cell projection, cilium {ECO:0000269|PubMed:16885411}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:16308564, ECO:0000269|PubMed:16885411}. Cell junction, tight junction. Note=In the retinal photoreceptor cell layer, localizes at the connecting cilium (By similarity). Colocalizes with E-cadherin and BCAR1 at or near the cell-cell adherens junctions (By similarity). Localized to respiratory cilia axoneme (PubMed:16308564, PubMed:16885411). Localized to the transition zone of respiratory cilia (PubMed:16885411). Localized to the transition zone of photoreceptor-connecting cilia and renal monocilia (By similarity). In cultured renal cells, it localizes diffusely in the cytoplasm but, as cells approach confluence, it accumulates at basolateral tight junctions (By similarity). {ECO:0000250|UniProtKB:Q9QY53, ECO:0000269|PubMed:16308564, ECO:0000269|PubMed:16885411}.
| null | null | null | null | null |
FUNCTION: Together with BCAR1 it may play a role in the control of epithelial cell polarity (By similarity). Involved in the organization of apical junctions in kidney cells together with NPHP4 and RPGRIP1L/NPHP8 (By similarity). Does not seem to be strictly required for ciliogenesis (By similarity). Seems to help to recruit PTK2B/PYK2 to cell matrix adhesions, thereby initiating phosphorylation of PTK2B/PYK2 and PTK2B/PYK2-dependent signaling (By similarity). May play a role in the regulation of intraflagellar transport (IFT) during cilia assembly. Required for normal retina development (By similarity). In connecting photoreceptor cilia influences the movement of some IFT proteins such as IFT88 and WDR19. Involved in spermatogenesis (By similarity). {ECO:0000250|UniProtKB:Q9QY53}.
|
Homo sapiens (Human)
|
O15260
|
SURF4_HUMAN
|
MGQNDLMGTAEDFADQFLRVTKQYLPHVARLCLISTFLEDGIRMWFQWSEQRDYIDTTWNCGYLLASSFVFLNLLGQLTGCVLVLSRNFVQYACFGLFGIIALQTIAYSILWDLKFLMRNLALGGGLLLLLAESRSEGKSMFAGVPTMRESSPKQYMQLGGRVLLVLMFMTLLHFDASFFSIVQNIVGTALMILVAIGFKTKLAALTLVVWLFAINVYFNAFWTIPVYKPMHDFLKYDFFQTMSVIGGLLLVVALGPGGVSMDEKKKEW
| null | null |
COPII-coated vesicle cargo loading [GO:0090110]; endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; Golgi organization [GO:0007030]; lipid export from cell [GO:0140353]; lipid homeostasis [GO:0055088]; lipoprotein transport [GO:0042953]; positive regulation of organelle organization [GO:0010638]; regulation of lipid transport [GO:0032368]
|
azurophil granule membrane [GO:0035577]; COPII-coated ER to Golgi transport vesicle [GO:0030134]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum exit site [GO:0070971]; endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; nuclear membrane [GO:0031965]; plasma membrane [GO:0005886]; transport vesicle [GO:0030133]
|
cargo receptor activity [GO:0038024]; COPII receptor activity [GO:0097020]
|
PF02077;
| null |
SURF4 family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15308636, ECO:0000269|PubMed:18287528, ECO:0000269|PubMed:30251625, ECO:0000269|PubMed:33186557}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000269|PubMed:18287528}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:18287528, ECO:0000269|PubMed:30251625, ECO:0000269|PubMed:33186557}; Multi-pass membrane protein {ECO:0000255}. Note=Active at endoplasmic reticulum exit sites (ERES) where it is incorporated together with its lipoprotein cargos into COPII-coated vesicles. From the Golgi it is recycled back to the endoplasmic reticulum. {ECO:0000269|PubMed:18287528, ECO:0000269|PubMed:33186557}.
| null | null | null | null | null |
FUNCTION: Endoplasmic reticulum cargo receptor that mediates the export of lipoproteins by recruiting cargos into COPII vesicles to facilitate their secretion (PubMed:29643117, PubMed:30251625, PubMed:33186557). Acts as a cargo receptor for lipoproteins bearing both APOB and APOA1, thereby regulating lipoprotein delivery and the maintenance of lipid homeostasis (PubMed:29643117, PubMed:33186557). Synergizes with the GTPase SAR1B to mediate transport of circulating lipoproteins (PubMed:33186557). Promotes the secretion of PCSK9 (PubMed:30251625). Also mediates the efficient secretion of erythropoietin (EPO) (PubMed:32989016). May also play a role in the maintenance of the architecture of the endoplasmic reticulum-Golgi intermediate compartment and of the Golgi (PubMed:18287528). {ECO:0000269|PubMed:18287528, ECO:0000269|PubMed:29643117, ECO:0000269|PubMed:30251625, ECO:0000269|PubMed:32989016, ECO:0000269|PubMed:33186557}.
|
Homo sapiens (Human)
|
O15263
|
DFB4A_HUMAN
|
MRVLYLLFSFLFIFLMPLPGVFGGIGDPVTCLKSGAICHPVFCPRRYKQIGTCGLPGTKCCKKP
| null | null |
antifungal innate immune response [GO:0061760]; antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; cell chemotaxis [GO:0060326]; chemotaxis [GO:0006935]; defense response to bacterium [GO:0042742]; defense response to fungus [GO:0050832]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; G protein-coupled receptor signaling pathway [GO:0007186]; immune response [GO:0006955]; killing of cells of another organism [GO:0031640]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi lumen [GO:0005796]
|
CCR6 chemokine receptor binding [GO:0031731]; chemoattractant activity [GO:0042056]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]
|
PF00711;
| null |
Beta-defensin family, LAP/TAP subfamily
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10837369}.
| null | null | null | null | null |
FUNCTION: Exhibits antimicrobial activity against Gram-negative bacteria and Gram-positive bacteria, with highest activity against Gram-negative bacteria (PubMed:10837369, PubMed:9202117). Antimicrobial activity against P.aruginosa seems to be salt-sensitive and is reduced with high salt concentrations greater than 25 mM (PubMed:10837369). Also exhibits antimicrobial activity against the yeast C.albicans (PubMed:10837369, PubMed:30050988, PubMed:9202117). Permeabilizes C.albicans cell membranes via targeting plasma membrane lipid phosphatidylinositol 4,5-bisphosphate (PIP2), thereby leading to cell fragmentation and cell death (PubMed:30050988). Acts as a ligand for C-C chemokine receptor CCR6 (PubMed:10521347, PubMed:20068036). Binds to CCR6 and induces chemotactic activity of CCR6-expressing cells, such as immature dendritic cells and memory T cells (PubMed:10521347, PubMed:20068036). {ECO:0000269|PubMed:10521347, ECO:0000269|PubMed:10837369, ECO:0000269|PubMed:20068036, ECO:0000269|PubMed:30050988, ECO:0000269|PubMed:9202117}.
|
Homo sapiens (Human)
|
O15264
|
MK13_HUMAN
|
MSLIRKKGFYKQDVNKTAWELPKTYVSPTHVGSGAYGSVCSAIDKRSGEKVAIKKLSRPFQSEIFAKRAYRELLLLKHMQHENVIGLLDVFTPASSLRNFYDFYLVMPFMQTDLQKIMGMEFSEEKIQYLVYQMLKGLKYIHSAGVVHRDLKPGNLAVNEDCELKILDFGLARHADAEMTGYVVTRWYRAPEVILSWMHYNQTVDIWSVGCIMAEMLTGKTLFKGKDYLDQLTQILKVTGVPGTEFVQKLNDKAAKSYIQSLPQTPRKDFTQLFPRASPQAADLLEKMLELDVDKRLTAAQALTHPFFEPFRDPEEETEAQQPFDDSLEHEKLTVDEWKQHIYKEIVNFSPIARKDSRRRSGMKL
|
2.7.11.24
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
|
cell cycle [GO:0007049]; cellular response to anisomycin [GO:0072740]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to interleukin-1 [GO:0071347]; cellular response to sodium arsenite [GO:1903936]; cellular response to sorbitol [GO:0072709]; cellular response to UV [GO:0034644]; intracellular signal transduction [GO:0035556]; peptidyl-serine phosphorylation [GO:0018105]; positive regulation of inflammatory response [GO:0050729]; positive regulation of interleukin-6 production [GO:0032755]; response to osmotic stress [GO:0006970]; stress-activated MAPK cascade [GO:0051403]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; MAP kinase activity [GO:0004707]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, CMGC Ser/Thr protein kinase family, MAP kinase subfamily
|
PTM: Dually phosphorylated on Thr-180 and Tyr-182 by MAP2K3/MKK3, MAP2K4/MKK4, MAP2K6/MKK6 and MAP2K7/MKK7, which activates the enzyme. Dephosphorylated by dual specificity phosphatase DUSP1. {ECO:0000269|PubMed:9374491}.
| null |
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.24; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.24;
| null | null | null | null |
FUNCTION: Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK13 is one of the four p38 MAPKs which play an important role in the cascades of cellular responses evoked by extracellular stimuli such as pro-inflammatory cytokines or physical stress leading to direct activation of transcription factors such as ELK1 and ATF2. Accordingly, p38 MAPKs phosphorylate a broad range of proteins and it has been estimated that they may have approximately 200 to 300 substrates each. MAPK13 is one of the less studied p38 MAPK isoforms. Some of the targets are downstream kinases such as MAPKAPK2, which are activated through phosphorylation and further phosphorylate additional targets. Plays a role in the regulation of protein translation by phosphorylating and inactivating EEF2K. Involved in cytoskeletal remodeling through phosphorylation of MAPT and STMN1. Mediates UV irradiation induced up-regulation of the gene expression of CXCL14. Plays an important role in the regulation of epidermal keratinocyte differentiation, apoptosis and skin tumor development. Phosphorylates the transcriptional activator MYB in response to stress which leads to rapid MYB degradation via a proteasome-dependent pathway. MAPK13 also phosphorylates and down-regulates PRKD1 during regulation of insulin secretion in pancreatic beta cells. {ECO:0000269|PubMed:11500363, ECO:0000269|PubMed:11943212, ECO:0000269|PubMed:15632108, ECO:0000269|PubMed:17256148, ECO:0000269|PubMed:18006338, ECO:0000269|PubMed:18367666, ECO:0000269|PubMed:20478268, ECO:0000269|PubMed:9731215}.
|
Homo sapiens (Human)
|
O15265
|
ATX7_HUMAN
|
MSERAADDVRGEPRRAAAAAGGAAAAAARQQQQQQQQQQPPPPQPQRQQHPPPPPRRTRPEDGGPGAASTSAAAMATVGERRPLPSPEVMLGQSWNLWVEASKLPGKDGTELDESFKEFGKNREVMGLCREDMPIFGFCPAHDDFYLVVCNDCNQVVKPQAFQSHYERRHSSSSKPPLAVPPTSVFSFFPSLSKSKGGSASGSNRSSSGGVLSASSSSSKLLKSPKEKLQLRGNTRPMHPIQQSRVPHGRIMTPSVKVEKIHPKMDGTLLKSAVGPTCPATVSSLVKPGLNCPSIPKPTLPSPGQILNGKGLPAPPTLEKKPEDNSNNRKFLNKRLSEREFDPDIHCGVIDLDTKKPCTRSLTCKTHSLTQRRAVQGRRKRFDVLLAEHKNKTREKELIRHPDSQQPPQPLRDPHPAPPRTSQEPHQNPHGVIPSESKPFVASKPKPHTPSLPRPPGCPAQQGGSAPIDPPPVHESPHPPLPATEPASRLSSEEGEGDDKEESVEKLDCHYSGHHPQPASFCTFGSRQIGRGYYVFDSRWNRLRCALNLMVEKHLNAQLWKKIPPVPSTTSPISTRIPHRTNSVPTSQCGVSYLAAATVSTSPVLLSSTCISPNSKSVPAHGTTLNAQPAASGAMDPVCSMQSRQVSSSSSSPSTPSGLSSVPSSPMSRKPQKLKSSKSLRPKESSGNSTNCQNASSSTSGGSGKKRKNSSPLLVHSSSSSSSSSSSSHSMESFRKNCVAHSGPPYPSTVTSSHSIGLNCVTNKANAVNVRHDQSGRGPPTGSPAESIKRMSVMVNSSDSTLSLGPFIHQSNELPVNSHGSFSHSHTPLDKLIGKKRKCSPSSSSINNSSSKPTKVAKVPAVNNVHMKHTGTIPGAQGLMNSSLLHQPKARP
| null | null |
microtubule cytoskeleton organization [GO:0000226]; negative regulation of microtubule depolymerization [GO:0007026]; nucleus organization [GO:0006997]; positive regulation of DNA-templated transcription [GO:0045893]; regulation of DNA repair [GO:0006282]; regulation of RNA splicing [GO:0043484]; regulation of transcription by RNA polymerase II [GO:0006357]; visual perception [GO:0007601]
|
cytosol [GO:0005829]; microtubule cytoskeleton [GO:0015630]; nuclear matrix [GO:0016363]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; SAGA complex [GO:0000124]; transcription factor TFTC complex [GO:0033276]
| null |
PF08313;
|
6.10.140.670;
|
Ataxin-7 family
|
PTM: Proteolytically cleaved by caspase-7 (CASP7) (PubMed:17646170). The cleavage may be involved in SCA7 degeneration: the isoform fragments may exert distinct toxic influences that could contribute to selective neurodegeneration (PubMed:17646170). {ECO:0000269|PubMed:17646170}.; PTM: Sumoylation decreases the aggregation propensity and cellular toxicity of forms with an expanded poly-Gln region but has no effect on subcellular location or interaction with components of the STAGA complex. {ECO:0000269|PubMed:19843541}.
|
SUBCELLULAR LOCATION: [Isoform a]: Nucleus {ECO:0000269|PubMed:12533095, ECO:0000269|PubMed:16314424, ECO:0000269|PubMed:22100762}. Nucleus, nucleolus {ECO:0000269|PubMed:10441328}. Nucleus matrix {ECO:0000269|PubMed:10441328}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:22100762}. Note=In addition to a diffuse distribution throughout the nucleus, it is associated with the nuclear matrix and the nucleolus (PubMed:10441328). It is able to shuttle between the nucleus and cytoplasm (PubMed:16314424). {ECO:0000269|PubMed:10441328, ECO:0000269|PubMed:16314424}.; SUBCELLULAR LOCATION: [Isoform b]: Cytoplasm {ECO:0000269|PubMed:12533095}.
| null | null | null | null | null |
FUNCTION: Acts as a component of the STAGA transcription coactivator-HAT complex (PubMed:15932940, PubMed:18206972). Mediates the interaction of STAGA complex with the CRX and is involved in CRX-dependent gene activation (PubMed:15932940, PubMed:18206972). Necessary for microtubule cytoskeleton stabilization (PubMed:22100762). {ECO:0000269|PubMed:15932940, ECO:0000269|PubMed:18206972, ECO:0000269|PubMed:22100762}.
|
Homo sapiens (Human)
|
O15266
|
SHOX_HUMAN
|
MEELTAFVSKSFDQKSKDGNGGGGGGGGKKDSITYREVLESGLARSRELGTSDSSLQDITEGGGHCPVHLFKDHVDNDKEKLKEFGTARVAEGIYECKEKREDVKSEDEDGQTKLKQRRSRTNFTLEQLNELERLFDETHYPDAFMREELSQRLGLSEARVQVWFQNRRAKCRKQENQMHKGVILGTANHLDACRVAPYVNMGALRMPFQQVQAQLQLEGVAHAHPHLHPHLAAHAPYLMFPPPPFGLPIASLAESASAAAVVAAAAKSNSKNSSIADLRLKARKHAEALGL
| null | null |
positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]; skeletal system development [GO:0001501]
|
chromatin [GO:0000785]; intracellular membrane-bounded organelle [GO:0043231]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; sequence-specific DNA binding [GO:0043565]; sequence-specific double-stranded DNA binding [GO:1990837]
|
PF00046;PF03826;
|
1.10.10.60;
|
Paired homeobox family, Bicoid subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|PROSITE-ProRule:PRU00138}.
| null | null | null | null | null |
FUNCTION: Controls fundamental aspects of growth and development.
|
Homo sapiens (Human)
|
O15269
|
SPTC1_HUMAN
|
MATATEQWVLVEMVQALYEAPAYHLILEGILILWIIRLLFSKTYKLQERSDLTVKEKEELIEEWQPEPLVPPVPKDHPALNYNIVSGPPSHKTVVNGKECINFASFNFLGLLDNPRVKAAALASLKKYGVGTCGPRGFYGTFDVHLDLEDRLAKFMKTEEAIIYSYGFATIASAIPAYSKRGDIVFVDRAACFAIQKGLQASRSDIKLFKHNDMADLERLLKEQEIEDQKNPRKARVTRRFIVVEGLYMNTGTICPLPELVKLKYKYKARIFLEESLSFGVLGEHGRGVTEHYGINIDDIDLISANMENALASIGGFCCGRSFVIDHQRLSGQGYCFSASLPPLLAAAAIEALNIMEENPGIFAVLKEKCGQIHKALQGISGLKVVGESLSPAFHLQLEESTGSREQDVRLLQEIVDQCMNRSIALTQARYLEKEEKCLPPPSIRVVVTVEQTEEELERAASTIKEVAQAVLL
|
2.3.1.50
|
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250};
|
ceramide biosynthetic process [GO:0046513]; positive regulation of lipophagy [GO:1904504]; regulation of fat cell apoptotic process [GO:1904649]; sphinganine biosynthetic process [GO:0046511]; sphingolipid biosynthetic process [GO:0030148]; sphingolipid metabolic process [GO:0006665]; sphingomyelin biosynthetic process [GO:0006686]; sphingosine biosynthetic process [GO:0046512]
|
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; serine C-palmitoyltransferase complex [GO:0017059]; SPOTS complex [GO:0035339]
|
pyridoxal phosphate binding [GO:0030170]; serine C-palmitoyltransferase activity [GO:0004758]
|
PF00155;
|
3.90.1150.10;3.40.640.10;
|
Class-II pyridoxal-phosphate-dependent aminotransferase family
|
PTM: Phosphorylation at Tyr-164 inhibits activity and promotes cell survival. {ECO:0000269|PubMed:23629659}.
|
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21618344}; Single-pass membrane protein {ECO:0000250|UniProtKB:O35704}.
|
CATALYTIC ACTIVITY: Reaction=H(+) + hexadecanoyl-CoA + L-serine = 3-oxosphinganine + CO2 + CoA; Xref=Rhea:RHEA:14761, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:33384, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:58299; EC=2.3.1.50; Evidence={ECO:0000269|PubMed:19416851}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14762; Evidence={ECO:0000269|PubMed:19416851}; CATALYTIC ACTIVITY: Reaction=H(+) + L-serine + octadecanoyl-CoA = 3-oxoeicosasphinganine + CO2 + CoA; Xref=Rhea:RHEA:33683, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:33384, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394, ChEBI:CHEBI:65073; Evidence={ECO:0000269|PubMed:19416851}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33684; Evidence={ECO:0000269|PubMed:19416851}; CATALYTIC ACTIVITY: Reaction=H(+) + L-serine + tetradecanoyl-CoA = 3-oxohexadecasphinganine + CO2 + CoA; Xref=Rhea:RHEA:35675, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:33384, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:71007; Evidence={ECO:0000269|PubMed:19416851}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35676; Evidence={ECO:0000269|PubMed:19416851}; CATALYTIC ACTIVITY: Reaction=dodecanoyl-CoA + H(+) + L-serine = 3-oxotetradecasphinganine + CO2 + CoA; Xref=Rhea:RHEA:35679, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:33384, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375, ChEBI:CHEBI:71008; Evidence={ECO:0000269|PubMed:19416851}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35680; Evidence={ECO:0000269|PubMed:19416851};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.75 mM for L-serine {ECO:0000269|PubMed:20504773}; KM=0.3 mM for L-serine {ECO:0000269|PubMed:33558761}; Vmax=1350 pmol/min/mg enzyme {ECO:0000269|PubMed:20504773};
|
PATHWAY: Lipid metabolism; sphingolipid metabolism. {ECO:0000269|PubMed:19416851}.
| null | null |
FUNCTION: Component of the serine palmitoyltransferase multisubunit enzyme (SPT) that catalyzes the initial and rate-limiting step in sphingolipid biosynthesis by condensing L-serine and activated acyl-CoA (most commonly palmitoyl-CoA) to form long-chain bases. The SPT complex is also composed of SPTLC2 or SPTLC3 and SPTSSA or SPTSSB. Within this complex, the heterodimer with SPTLC2 or SPTLC3 forms the catalytic core (PubMed:19416851, PubMed:36170811, PubMed:33558762). The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference (PubMed:19416851, PubMed:33558762). The SPTLC1-SPTLC2-SPTSSA complex shows a strong preference for C16-CoA substrate, while the SPTLC1-SPTLC3-SPTSSA isozyme uses both C14-CoA and C16-CoA as substrates, with a slight preference for C14-CoA (PubMed:19648650, PubMed:19416851). The SPTLC1-SPTLC2-SPTSSB complex shows a strong preference for C18-CoA substrate, while the SPTLC1-SPTLC3-SPTSSB isozyme displays an ability to use a broader range of acyl-CoAs, without apparent preference (PubMed:19648650, PubMed:19416851, PubMed:33558761, PubMed:33558762). Required for adipocyte cell viability and metabolic homeostasis (By similarity). {ECO:0000250|UniProtKB:O35704, ECO:0000269|PubMed:19416851, ECO:0000269|PubMed:19648650, ECO:0000269|PubMed:33558761, ECO:0000269|PubMed:33558762, ECO:0000269|PubMed:36170811}.
|
Homo sapiens (Human)
|
O15270
|
SPTC2_HUMAN
|
MRPEPGGCCCRRTVRANGCVANGEVRNGYVRSSAAAAAAAAAGQIHHVTQNGGLYKRPFNEAFEETPMLVAVLTYVGYGVLTLFGYLRDFLRYWRIEKCHHATEREEQKDFVSLYQDFENFYTRNLYMRIRDNWNRPICSVPGARVDIMERQSHDYNWSFKYTGNIIKGVINMGSYNYLGFARNTGSCQEAAAKVLEEYGAGVCSTRQEIGNLDKHEELEELVARFLGVEAAMAYGMGFATNSMNIPALVGKGCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKDAIVYGQPRTRRPWKKILILVEGIYSMEGSIVRLPEVIALKKKYKAYLYLDEAHSIGALGPTGRGVVEYFGLDPEDVDVMMGTFTKSFGASGGYIGGKKELIDYLRTHSHSAVYATSLSPPVVEQIITSMKCIMGQDGTSLGKECVQQLAENTRYFRRRLKEMGFIIYGNEDSPVVPLMLYMPAKIGAFGREMLKRNIGVVVVGFPATPIIESRARFCLSAAHTKEILDTALKEIDEVGDLLQLKYSRHRLVPLLDRPFDETTYEETED
|
2.3.1.50
|
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250};
|
adipose tissue development [GO:0060612]; ceramide biosynthetic process [GO:0046513]; positive regulation of lipophagy [GO:1904504]; sphinganine biosynthetic process [GO:0046511]; sphingolipid biosynthetic process [GO:0030148]; sphingomyelin biosynthetic process [GO:0006686]; sphingosine biosynthetic process [GO:0046512]
|
endoplasmic reticulum membrane [GO:0005789]; serine C-palmitoyltransferase complex [GO:0017059]
|
pyridoxal phosphate binding [GO:0030170]; serine C-palmitoyltransferase activity [GO:0004758]
|
PF00155;
|
3.90.1150.10;3.40.640.10;
|
Class-II pyridoxal-phosphate-dependent aminotransferase family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P97363}; Single-pass membrane protein {ECO:0000250|UniProtKB:P97363}.
|
CATALYTIC ACTIVITY: Reaction=H(+) + hexadecanoyl-CoA + L-serine = 3-oxosphinganine + CO2 + CoA; Xref=Rhea:RHEA:14761, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:33384, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:58299; EC=2.3.1.50; Evidence={ECO:0000269|PubMed:19416851}; CATALYTIC ACTIVITY: Reaction=H(+) + L-serine + octadecanoyl-CoA = 3-oxoeicosasphinganine + CO2 + CoA; Xref=Rhea:RHEA:33683, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:33384, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394, ChEBI:CHEBI:65073; Evidence={ECO:0000269|PubMed:19416851}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33684; Evidence={ECO:0000269|PubMed:19416851};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.75 mM for L-serine {ECO:0000269|PubMed:20504773}; KM=0.3 mM for L-serine {ECO:0000269|PubMed:33558761}; Vmax=1350 pmol/min/mg enzyme {ECO:0000269|PubMed:20504773};
|
PATHWAY: Lipid metabolism; sphingolipid metabolism.
| null | null |
FUNCTION: Component of the serine palmitoyltransferase multisubunit enzyme (SPT) that catalyzes the initial and rate-limiting step in sphingolipid biosynthesis by condensing L-serine and activated acyl-CoA (most commonly palmitoyl-CoA) to form long-chain bases (PubMed:19416851, PubMed:19648650, PubMed:20504773, PubMed:20920666). The SPT complex is composed of SPTLC1, SPTLC2 or SPTLC3 and SPTSSA or SPTSSB. Within this complex, the heterodimer consisting of SPTLC1 and SPTLC2/SPTLC3 forms the catalytic core (PubMed:19416851). The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference (PubMed:19416851). The SPTLC1-SPTLC2-SPTSSA complex shows a strong preference for C16-CoA substrate, while the SPTLC1-SPTLC3-SPTSSA isozyme uses both C14-CoA and C16-CoA as substrates, with a slight preference for C14-CoA (PubMed:19416851, PubMed:19648650). The SPTLC1-SPTLC2-SPTSSB complex shows a strong preference for C18-CoA substrate, while the SPTLC1-SPTLC3-SPTSSB isozyme displays an ability to use a broader range of acyl-CoAs, without apparent preference (PubMed:19416851, PubMed:19648650). Crucial for adipogenesis (By similarity). {ECO:0000250|UniProtKB:P97363, ECO:0000269|PubMed:19416851, ECO:0000269|PubMed:19648650, ECO:0000269|PubMed:20504773, ECO:0000269|PubMed:20920666}.
|
Homo sapiens (Human)
|
O15273
|
TELT_HUMAN
|
MATSELSCEVSEENCERREAFWAEWKDLTLSTRPEEGCSLHEEDTQRHETYHQQGQCQVLVQRSPWLMMRMGILGRGLQEYQLPYQRVLPLPIFTPAKMGATKEEREDTPIQLQELLALETALGGQCVDRQEVAEITKQLPPVVPVSKPGALRRSLSRSMSQEAQRG
| null | null |
adult heart development [GO:0007512]; cardiac muscle cell development [GO:0055013]; cardiac muscle contraction [GO:0060048]; cardiac muscle hypertrophy [GO:0003300]; cardiac muscle hypertrophy in response to stress [GO:0014898]; cardiac muscle tissue morphogenesis [GO:0055008]; cardiac myofibril assembly [GO:0055003]; detection of mechanical stimulus [GO:0050982]; detection of muscle stretch [GO:0035995]; otic vesicle formation [GO:0030916]; protein-containing complex assembly [GO:0065003]; response to muscle stretch [GO:0035994]; sarcomere organization [GO:0045214]; sarcomerogenesis [GO:0048769]; skeletal muscle contraction [GO:0003009]; skeletal muscle myosin thick filament assembly [GO:0030241]; skeletal muscle thin filament assembly [GO:0030240]; somitogenesis [GO:0001756]
|
cytosol [GO:0005829]; I band [GO:0031674]; Z disc [GO:0030018]
|
BMP binding [GO:0036122]; FATZ binding [GO:0051373]; molecular adaptor activity [GO:0060090]; protein-macromolecule adaptor activity [GO:0030674]; structural constituent of muscle [GO:0008307]; titin binding [GO:0031432]; titin Z domain binding [GO:0070080]; transmembrane transporter binding [GO:0044325]
|
PF09470;
|
2.20.160.10;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere {ECO:0000269|PubMed:16713295}.
| null | null | null | null | null |
FUNCTION: Muscle assembly regulating factor. Mediates the antiparallel assembly of titin (TTN) molecules at the sarcomeric Z-disk.
|
Homo sapiens (Human)
|
O15287
|
FANCG_HUMAN
|
MSRQTTSVGSSCLDLWREKNDRLVRQAKVAQNSGLTLRRQQLAQDALEGLRGLLHSLQGLPAAVPVLPLELTVTCNFIILRASLAQGFTEDQAQDIQRSLERVLETQEQQGPRLEQGLRELWDSVLRASCLLPELLSALHRLVGLQAALWLSADRLGDLALLLETLNGSQSGASKDLLLLLKTWSPPAEELDAPLTLQDAQGLKDVLLTAFAYRQGLQELITGNPDKALSSLHEAASGLCPRPVLVQVYTALGSCHRKMGNPQRALLYLVAALKEGSAWGPPLLEASRLYQQLGDTTAELESLELLVEALNVPCSSKAPQFLIEVELLLPPPDLASPLHCGTQSQTKHILASRCLQTGRAGDAAEHYLDLLALLLDSSEPRFSPPPSPPGPCMPEVFLEAAVALIQAGRAQDALTLCEELLSRTSSLLPKMSRLWEDARKGTKELPYCPLWVSATHLLQGQAWVQLGAQKVAISEFSRCLELLFRATPEEKEQGAAFNCEQGCKSDAALQQLRAAALISRGLEWVASGQDTKALQDFLLSVQMCPGNRDTYFHLLQTLKRLDRRDEATALWWRLEAQTKGSHEDALWSLPLYLESYLSWIRPSDRDAFLEEFRTSLPKSCDL
| null | null |
DNA damage response [GO:0006974]; DNA repair [GO:0006281]; interstrand cross-link repair [GO:0036297]; mitochondrion organization [GO:0007005]; ovarian follicle development [GO:0001541]; response to radiation [GO:0009314]; spermatid development [GO:0007286]
|
chromatin [GO:0000785]; cytosol [GO:0005829]; Fanconi anaemia nuclear complex [GO:0043240]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]
|
damaged DNA binding [GO:0003684]
| null |
1.25.40.10;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18550849}. Cytoplasm {ECO:0000269|PubMed:18550849}. Note=The major form is nuclear. The minor form is cytoplasmic.
| null | null | null | null | null |
FUNCTION: DNA repair protein that may operate in a postreplication repair or a cell cycle checkpoint function. May be implicated in interstrand DNA cross-link repair and in the maintenance of normal chromosome stability. Candidate tumor suppressor gene.
|
Homo sapiens (Human)
|
O15294
|
OGT1_HUMAN
|
MASSVGNVADSTEPTKRMLSFQGLAELAHREYQAGDFEAAERHCMQLWRQEPDNTGVLLLLSSIHFQCRRLDRSAHFSTLAIKQNPLLAEAYSNLGNVYKERGQLQEAIEHYRHALRLKPDFIDGYINLAAALVAAGDMEGAVQAYVSALQYNPDLYCVRSDLGNLLKALGRLEEAKACYLKAIETQPNFAVAWSNLGCVFNAQGEIWLAIHHFEKAVTLDPNFLDAYINLGNVLKEARIFDRAVAAYLRALSLSPNHAVVHGNLACVYYEQGLIDLAIDTYRRAIELQPHFPDAYCNLANALKEKGSVAEAEDCYNTALRLCPTHADSLNNLANIKREQGNIEEAVRLYRKALEVFPEFAAAHSNLASVLQQQGKLQEALMHYKEAIRISPTFADAYSNMGNTLKEMQDVQGALQCYTRAIQINPAFADAHSNLASIHKDSGNIPEAIASYRTALKLKPDFPDAYCNLAHCLQIVCDWTDYDERMKKLVSIVADQLEKNRLPSVHPHHSMLYPLSHGFRKAIAERHGNLCLDKINVLHKPPYEHPKDLKLSDGRLRVGYVSSDFGNHPTSHLMQSIPGMHNPDKFEVFCYALSPDDGTNFRVKVMAEANHFIDLSQIPCNGKAADRIHQDGIHILVNMNGYTKGARNELFALRPAPIQAMWLGYPGTSGALFMDYIITDQETSPAEVAEQYSEKLAYMPHTFFIGDHANMFPHLKKKAVIDFKSNGHIYDNRIVLNGIDLKAFLDSLPDVKIVKMKCPDGGDNADSSNTALNMPVIPMNTIAEAVIEMINRGQIQITINGFSISNGLATTQINNKAATGEEVPRTIIVTTRSQYGLPEDAIVYCNFNQLYKIDPSTLQMWANILKRVPNSVLWLLRFPAVGEPNIQQYAQNMGLPQNRIIFSPVAPKEEHVRRGQLADVCLDTPLCNGHTTGMDVLWAGTPMVTMPGETLASRVAASQLTCLGCLELIAKNRQEYEDIAVKLGTDLEYLKKVRGKVWKQRISSPLFNTKQYTMELERLYLQMWEHYAAGNKPDHMIKPVEVTESA
|
2.4.1.255
| null |
apoptotic process [GO:0006915]; cellular response to glucose stimulus [GO:0071333]; chromatin organization [GO:0006325]; circadian regulation of gene expression [GO:0032922]; hemopoiesis [GO:0030097]; mitophagy [GO:0000423]; negative regulation of cell migration [GO:0030336]; negative regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032435]; negative regulation of protein ubiquitination [GO:0031397]; negative regulation of stem cell population maintenance [GO:1902455]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; positive regulation of cold-induced thermogenesis [GO:0120162]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of lipid biosynthetic process [GO:0046889]; positive regulation of proteolysis [GO:0045862]; positive regulation of stem cell population maintenance [GO:1902459]; positive regulation of TORC1 signaling [GO:1904263]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of transcription from RNA polymerase II promoter by glucose [GO:0000432]; positive regulation of translation [GO:0045727]; protein O-linked glycosylation [GO:0006493]; protein processing [GO:0016485]; regulation of gluconeogenesis [GO:0006111]; regulation of glycolytic process [GO:0006110]; regulation of insulin receptor signaling pathway [GO:0046626]; regulation of necroptotic process [GO:0060544]; regulation of neurotransmitter receptor localization to postsynaptic specialization membrane [GO:0098696]; regulation of Rac protein signal transduction [GO:0035020]; regulation of synapse assembly [GO:0051963]; regulation of transcription by RNA polymerase II [GO:0006357]; response to insulin [GO:0032868]; response to nutrient [GO:0007584]; signal transduction [GO:0007165]
|
cell projection [GO:0042995]; cytosol [GO:0005829]; glutamatergic synapse [GO:0098978]; histone acetyltransferase complex [GO:0000123]; mitochondrial membrane [GO:0031966]; NSL complex [GO:0044545]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein N-acetylglucosaminyltransferase complex [GO:0017122]; protein-containing complex [GO:0032991]
|
acetylglucosaminyltransferase activity [GO:0008375]; chromatin DNA binding [GO:0031490]; phosphatidylinositol-3,4,5-trisphosphate binding [GO:0005547]; protein O-acetylglucosaminyltransferase activity [GO:0097363]
|
PF13844;PF00515;PF13414;PF13424;PF13181;
|
3.30.720.150;3.40.50.11380;3.40.50.2000;1.25.40.10;
|
Glycosyltransferase 41 family, O-GlcNAc transferase subfamily
|
PTM: Ubiquitinated, leading to its proteasomal degradation. {ECO:0000269|PubMed:21285374}.; PTM: Phosphorylation on Ser-3 or Ser-4 by GSK3-beta positively regulates its activity (By similarity). Phosphorylation at Thr-454 by AMPK promotes nuclear localization (PubMed:24563466). {ECO:0000250|UniProtKB:Q8CGY8, ECO:0000269|PubMed:24563466}.; PTM: Glycosylated via autocatalysis; O-GlcNAcylation at Ser-399 promotes nuclear localization. {ECO:0000269|PubMed:27713473}.; PTM: [Isoform 4]: Glycosylated via autocatalysis; does not affect the enzyme activity but regulates substrate selectivity. {ECO:0000269|PubMed:31527085}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26678539, ECO:0000269|PubMed:27713473}. Cytoplasm {ECO:0000269|PubMed:26678539, ECO:0000269|PubMed:27713473}. Note=Predominantly localizes to the nucleus (PubMed:26678539). Translocates into the nucleus via association with importin KPNA1 (PubMed:27713473). {ECO:0000269|PubMed:26678539, ECO:0000269|PubMed:27713473}.; SUBCELLULAR LOCATION: [Isoform 2]: Mitochondrion {ECO:0000269|PubMed:20824293}. Membrane {ECO:0000269|PubMed:20824293}. Note=Associates with the mitochondrial inner membrane. {ECO:0000269|PubMed:20824293}.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm {ECO:0000269|PubMed:21285374}. Nucleus {ECO:0000269|PubMed:20018852, ECO:0000269|PubMed:21285374}. Cell membrane {ECO:0000250|UniProtKB:P56558}. Mitochondrion membrane {ECO:0000250|UniProtKB:P56558}. Cell projection {ECO:0000250|UniProtKB:P56558}. Note=Mostly in the nucleus. Retained in the nucleus via interaction with HCFC1 (PubMed:21285374). After insulin induction, translocated from the nucleus to the cell membrane via phosphatidylinositide binding. Colocalizes with AKT1 at the plasma membrane. TRAK1 recruits this protein to mitochondria. In the absence of TRAK1, localizes in cytosol and nucleus (By similarity). {ECO:0000250|UniProtKB:P56558, ECO:0000269|PubMed:21285374}.; SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm {ECO:0000303|PubMed:31527085}. Nucleus {ECO:0000303|PubMed:31527085}.
|
CATALYTIC ACTIVITY: Reaction=L-seryl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-(N-acetyl-beta-D-glucosaminyl)-L-seryl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:48904, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:12251, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:90838; EC=2.4.1.255; Evidence={ECO:0000269|PubMed:15361863, ECO:0000269|PubMed:21240259, ECO:0000269|PubMed:21285374, ECO:0000269|PubMed:23103939, ECO:0000269|PubMed:24563466, ECO:0000269|PubMed:26237509, ECO:0000269|PubMed:27713473, ECO:0000269|PubMed:30699359, ECO:0000269|PubMed:34074792, ECO:0000305|PubMed:26369908, ECO:0000305|PubMed:26678539}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48905; Evidence={ECO:0000269|PubMed:24563466, ECO:0000269|PubMed:26237509, ECO:0000269|PubMed:27713473, ECO:0000269|PubMed:30699359, ECO:0000269|PubMed:34074792}; CATALYTIC ACTIVITY: Reaction=L-threonyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-(N-acetyl-beta-D-glucosaminyl)-L-threonyl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:48908, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:12252, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:90840; EC=2.4.1.255; Evidence={ECO:0000269|PubMed:15361863, ECO:0000269|PubMed:21240259, ECO:0000269|PubMed:21285374, ECO:0000269|PubMed:24563466, ECO:0000269|PubMed:26237509, ECO:0000269|PubMed:37541260, ECO:0000305|PubMed:26678539}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48909; Evidence={ECO:0000269|PubMed:24563466, ECO:0000269|PubMed:26237509, ECO:0000269|PubMed:27713473, ECO:0000269|PubMed:37541260}; CATALYTIC ACTIVITY: [Isoform 4]: Reaction=L-seryl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-(N-acetyl-beta-D-glucosaminyl)-L-seryl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:48904, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:12251, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:90838; EC=2.4.1.255; Evidence={ECO:0000269|PubMed:31527085}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48905; Evidence={ECO:0000269|PubMed:31527085}; CATALYTIC ACTIVITY: [Isoform 4]: Reaction=L-threonyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-(N-acetyl-beta-D-glucosaminyl)-L-threonyl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:48908, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:12252, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:90840; EC=2.4.1.255; Evidence={ECO:0000269|PubMed:31527085}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48909; Evidence={ECO:0000269|PubMed:31527085};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.8 uM for UDP-N-acetyl-D-glucosamine {ECO:0000269|PubMed:21240259};
|
PATHWAY: Protein modification; protein glycosylation. {ECO:0000269|PubMed:15361863, ECO:0000269|PubMed:21240259, ECO:0000269|PubMed:21285374, ECO:0000269|PubMed:23103939, ECO:0000269|PubMed:26678539, ECO:0000269|PubMed:27713473, ECO:0000269|PubMed:31527085, ECO:0000269|PubMed:37541260}.
| null | null |
FUNCTION: Catalyzes the transfer of a single N-acetylglucosamine from UDP-GlcNAc to a serine or threonine residue in cytoplasmic and nuclear proteins resulting in their modification with a beta-linked N-acetylglucosamine (O-GlcNAc) (PubMed:12150998, PubMed:15361863, PubMed:19451179, PubMed:20018868, PubMed:21240259, PubMed:21285374, PubMed:23103939, PubMed:26237509, PubMed:26369908, PubMed:26678539, PubMed:27713473, PubMed:37541260). Glycosylates a large and diverse number of proteins including histone H2B, AKT1, AMPK, ATG4B, CAPRIN1, EZH2, FNIP1, KRT7, LMNA, LMNB1, LMNB2, RPTOR, HOXA1, PFKL, KMT2E/MLL5, MAPT/TAU, TET2, RBL2, RET, NOD2 and HCFC1 (PubMed:19451179, PubMed:20200153, PubMed:21285374, PubMed:22923583, PubMed:23353889, PubMed:24474760, PubMed:26237509, PubMed:26369908, PubMed:26678539, PubMed:27527864, PubMed:30699359, PubMed:34074792, PubMed:34667079, PubMed:37541260). Can regulate their cellular processes via cross-talk between glycosylation and phosphorylation or by affecting proteolytic processing (PubMed:21285374). Involved in insulin resistance in muscle and adipocyte cells via glycosylating insulin signaling components and inhibiting the 'Thr-308' phosphorylation of AKT1, enhancing IRS1 phosphorylation and attenuating insulin signaling (By similarity). Involved in glycolysis regulation by mediating glycosylation of 6-phosphofructokinase PFKL, inhibiting its activity (PubMed:22923583). Plays a key role in chromatin structure by mediating O-GlcNAcylation of 'Ser-112' of histone H2B: recruited to CpG-rich transcription start sites of active genes via its interaction with TET proteins (TET1, TET2 or TET3) (PubMed:22121020, PubMed:23353889). As part of the NSL complex indirectly involved in acetylation of nucleosomal histone H4 on several lysine residues (PubMed:20018852). O-GlcNAcylation of 'Ser-75' of EZH2 increases its stability, and facilitating the formation of H3K27me3 by the PRC2/EED-EZH2 complex (PubMed:24474760). Stabilizes KMT2E/MLL5 by mediating its glycosylation, thereby preventing KMT2E/MLL5 ubiquitination (PubMed:26678539). Regulates circadian oscillation of the clock genes and glucose homeostasis in the liver (By similarity). Stabilizes clock proteins BMAL1 and CLOCK through O-glycosylation, which prevents their ubiquitination and subsequent degradation (By similarity). Promotes the CLOCK-BMAL1-mediated transcription of genes in the negative loop of the circadian clock such as PER1/2 and CRY1/2. O-glycosylates HCFC1 and regulates its proteolytic processing and transcriptional activity (PubMed:21285374, PubMed:28302723, PubMed:28584052). Component of a THAP1/THAP3-HCFC1-OGT complex that is required for the regulation of the transcriptional activity of RRM1 (PubMed:20200153). Regulates mitochondrial motility in neurons by mediating glycosylation of TRAK1 (By similarity). Promotes autophagy by mediating O-glycosylation of ATG4B (PubMed:27527864). Acts as a regulator of mTORC1 signaling by mediating O-glycosylation of RPTOR and FNIP1: O-GlcNAcylation of RPTOR in response to glucose sufficiency promotes activation of the mTORC1 complex (PubMed:30699359, PubMed:37541260). {ECO:0000250|UniProtKB:P56558, ECO:0000250|UniProtKB:Q8CGY8, ECO:0000269|PubMed:12150998, ECO:0000269|PubMed:15361863, ECO:0000269|PubMed:19451179, ECO:0000269|PubMed:20018852, ECO:0000269|PubMed:20018868, ECO:0000269|PubMed:20200153, ECO:0000269|PubMed:21240259, ECO:0000269|PubMed:21285374, ECO:0000269|PubMed:22121020, ECO:0000269|PubMed:22923583, ECO:0000269|PubMed:23103939, ECO:0000269|PubMed:23353889, ECO:0000269|PubMed:24474760, ECO:0000269|PubMed:24563466, ECO:0000269|PubMed:26237509, ECO:0000269|PubMed:26369908, ECO:0000269|PubMed:26678539, ECO:0000269|PubMed:27527864, ECO:0000269|PubMed:28302723, ECO:0000269|PubMed:28584052, ECO:0000269|PubMed:30699359, ECO:0000269|PubMed:34074792, ECO:0000269|PubMed:34667079, ECO:0000269|PubMed:37541260}.; FUNCTION: [Isoform 2]: The mitochondrial isoform (mOGT) is cytotoxic and triggers apoptosis in several cell types including INS1, an insulinoma cell line. {ECO:0000269|PubMed:20824293}.; FUNCTION: [Isoform 4]: Has N-acetylglucosaminyltransferase activity: glycosylates proteins, such as HNRNPU, NEUROD1, NUP62 and PDCD6IP (PubMed:31527085). Displays specific substrate selectivity compared to other isoforms (PubMed:31527085). {ECO:0000269|PubMed:31527085}.
|
Homo sapiens (Human)
|
O15296
|
LX15B_HUMAN
|
MAEFRVRVSTGEAFGAGTWDKVSVSIVGTRGESPPLPLDNLGKEFTAGAEEDFQVTLPEDVGRVLLLRVHKAPPVLPLLGPLAPDAWFCRWFQLTPPRGGHLLFPCYQWLEGAGTLVLQEGTAKVSWADHHPVLQQQRQEELQARQEMYQWKAYNPGWPHCLDEKTVEDLELNIKYSTAKNANFYLQAGSAFAEMKIKGLLDRKGLWRSLNEMKRIFNFRRTPAAEHAFEHWQEDAFFASQFLNGLNPVLIRRCHYLPKNFPVTDAMVASVLGPGTSLQAELEKGSLFLVDHGILSGIQTNVINGKPQFSAAPMTLLYQSPGCGPLLPLAIQLSQTPGPNSPIFLPTDDKWDWLLAKTWVRNAEFSFHEALTHLLHSHLLPEVFTLATLRQLPHCHPLFKLLIPHTRYTLHINTLARELLIVPGQVVDRSTGIGIEGFSELIQRNMKQLNYSLLCLPEDIRTRGVEDIPGYYYRDDGMQIWGAVERFVSEIIGIYYPSDESVQDDRELQAWVREIFSKGFLNQESSGIPSSLETREALVQYVTMVIFTCSAKHAAVSAGQFDSCAWMPNLPPSMQLPPPTSKGLATCEGFIATLPPVNATCDVILALWLLSKEPGDQRPLGTYPDEHFTEEAPRRSIATFQSRLAQISRGIQERNQGLVLPYTYLDPPLIENSVSI
|
1.13.11.-; 1.13.11.33
|
COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000255|PROSITE-ProRule:PRU00726, ECO:0000269|PubMed:24497644}; Note=Binds 1 Fe cation per subunit. {ECO:0000255|PROSITE-ProRule:PRU00726, ECO:0000269|PubMed:24497644};
|
apoptotic process [GO:0006915]; arachidonic acid metabolic process [GO:0019369]; cannabinoid biosynthetic process [GO:1901696]; endocannabinoid signaling pathway [GO:0071926]; hepoxilin biosynthetic process [GO:0051122]; linoleic acid metabolic process [GO:0043651]; lipid metabolic process [GO:0006629]; lipid oxidation [GO:0034440]; lipoxin A4 biosynthetic process [GO:2001303]; lipoxygenase pathway [GO:0019372]; negative regulation of cell cycle [GO:0045786]; negative regulation of cell migration [GO:0030336]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of growth [GO:0045926]; phospholipid metabolic process [GO:0006644]; positive regulation of chemokine production [GO:0032722]; positive regulation of keratinocyte differentiation [GO:0045618]; positive regulation of macrophage derived foam cell differentiation [GO:0010744]; positive regulation of peroxisome proliferator activated receptor signaling pathway [GO:0035360]; prostate gland development [GO:0030850]; regulation of epithelial cell differentiation [GO:0030856]
|
adherens junction [GO:0005912]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; membrane [GO:0016020]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
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arachidonate 15-lipoxygenase activity [GO:0050473]; arachidonate 8(S)-lipoxygenase activity [GO:0036403]; calcium ion binding [GO:0005509]; iron ion binding [GO:0005506]; linoleate 13S-lipoxygenase activity [GO:0016165]; linoleate 9S-lipoxygenase activity [GO:1990136]; lipid binding [GO:0008289]
|
PF00305;PF01477;
|
3.10.450.60;2.60.60.20;
|
Lipoxygenase family
| null |
SUBCELLULAR LOCATION: [Isoform A]: Nucleus {ECO:0000269|PubMed:12704195}. Note=Other isoforms are excluded from the nucleus. {ECO:0000269|PubMed:12704195}.; SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12704195}. Cell membrane {ECO:0000269|PubMed:12704195, ECO:0000269|PubMed:27435673}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12704195}. Membrane {ECO:0000269|PubMed:10542053, ECO:0000269|PubMed:24497644}; Peripheral membrane protein {ECO:0000269|PubMed:24497644}. Cell junction, adherens junction {ECO:0000269|PubMed:12704195}. Cell junction, focal adhesion {ECO:0000269|PubMed:12704195}. Note=Predominantly cytosolic; becomes enriched at membranes upon calcium binding. {ECO:0000269|PubMed:10542053, ECO:0000269|PubMed:12704195, ECO:0000269|PubMed:24497644, ECO:0000269|PubMed:27435673}.
|
CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = (15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate; Xref=Rhea:RHEA:16869, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:57446; EC=1.13.11.33; Evidence={ECO:0000269|PubMed:10625675, ECO:0000269|PubMed:11956198, ECO:0000269|PubMed:12704195, ECO:0000269|PubMed:17493578, ECO:0000269|PubMed:24282679, ECO:0000269|PubMed:24497644, ECO:0000269|PubMed:9177185, ECO:0000305|PubMed:10542053, ECO:0000305|PubMed:27145229, ECO:0000305|PubMed:27435673}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16870; Evidence={ECO:0000269|PubMed:12704195}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + O2 = 13-hydroperoxy-(9Z,11E)-octadecadienoate; Xref=Rhea:RHEA:48848, ChEBI:CHEBI:15379, ChEBI:CHEBI:30245, ChEBI:CHEBI:90823; Evidence={ECO:0000269|PubMed:27435673, ECO:0000305|PubMed:10542053}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48849; Evidence={ECO:0000269|PubMed:27435673}; CATALYTIC ACTIVITY: Reaction=(5S)-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + O2 = (5S)-hydroxy-(15S)-hydroperoxy-(6E,8Z,11Z,13E)-eicosatetraenoate; Xref=Rhea:RHEA:53660, ChEBI:CHEBI:15379, ChEBI:CHEBI:90632, ChEBI:CHEBI:137546; Evidence={ECO:0000269|PubMed:27145229}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53661; Evidence={ECO:0000305|PubMed:27145229}; CATALYTIC ACTIVITY: [Isoform D]: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = 5-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate; Xref=Rhea:RHEA:48844, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:90822; Evidence={ECO:0000269|PubMed:10542053}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48845; Evidence={ECO:0000305|PubMed:10542053}; CATALYTIC ACTIVITY: Reaction=(5S,6R)-dihydroxy-(7E,9E,11Z,14Z)-eicosatetraenoate + O2 = (5S,6R)-dihydroxy-(15S)-hydroperoxy-(7E,9E,11Z,13E)-eicosatetraenoate; Xref=Rhea:RHEA:53656, ChEBI:CHEBI:15379, ChEBI:CHEBI:137542, ChEBI:CHEBI:137547; Evidence={ECO:0000269|PubMed:27145229}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53657; Evidence={ECO:0000305|PubMed:27145229}; CATALYTIC ACTIVITY: Reaction=(5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + O2 = (5S,15S)-dihydroperoxy-(6E,8Z,11Z,13E)-eicosatetraenoate; Xref=Rhea:RHEA:53652, ChEBI:CHEBI:15379, ChEBI:CHEBI:57450, ChEBI:CHEBI:137543; Evidence={ECO:0000269|PubMed:27145229}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53653; Evidence={ECO:0000305|PubMed:27145229}; CATALYTIC ACTIVITY: Reaction=2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + O2 = 2-[15(S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl]-glycerol; Xref=Rhea:RHEA:53332, ChEBI:CHEBI:15379, ChEBI:CHEBI:52392, ChEBI:CHEBI:137187; Evidence={ECO:0000269|PubMed:11956198}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53333; Evidence={ECO:0000269|PubMed:11956198}; CATALYTIC ACTIVITY: Reaction=(8S)-hydroperoxy-(5Z,9E,11Z,14Z)-eicosatetraenoate + O2 = (8S,15S)-dihydroperoxy-(5Z,9E,11Z,13E)-eicosatetraenoate; Xref=Rhea:RHEA:50932, ChEBI:CHEBI:15379, ChEBI:CHEBI:75322, ChEBI:CHEBI:133899; Evidence={ECO:0000305|PubMed:16112079}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50933; Evidence={ECO:0000305|PubMed:16112079}; CATALYTIC ACTIVITY: Reaction=N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-alanine + O2 = N-(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl-alanine; Xref=Rhea:RHEA:50184, ChEBI:CHEBI:15379, ChEBI:CHEBI:132071, ChEBI:CHEBI:132077; Evidence={ECO:0000269|PubMed:17493578}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50185; Evidence={ECO:0000305|PubMed:17493578}; CATALYTIC ACTIVITY: Reaction=N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-gamma-aminobutanoate + O2 = N-(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl-gamma-aminobutanoate; Xref=Rhea:RHEA:50180, ChEBI:CHEBI:15379, ChEBI:CHEBI:132072, ChEBI:CHEBI:132078; Evidence={ECO:0000269|PubMed:17493578}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50181; Evidence={ECO:0000269|PubMed:17493578}; CATALYTIC ACTIVITY: Reaction=N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-glycine + O2 = N-(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl-glycine; Xref=Rhea:RHEA:50188, ChEBI:CHEBI:15379, ChEBI:CHEBI:59002, ChEBI:CHEBI:132076; Evidence={ECO:0000269|PubMed:17493578}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50189; Evidence={ECO:0000269|PubMed:17493578}; CATALYTIC ACTIVITY: Reaction=N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-taurine + O2 = N-(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl-taurine; Xref=Rhea:RHEA:50156, ChEBI:CHEBI:15379, ChEBI:CHEBI:132060, ChEBI:CHEBI:132062; Evidence={ECO:0000269|PubMed:18311922}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50157; Evidence={ECO:0000305|PubMed:18311922}; CATALYTIC ACTIVITY: Reaction=2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + O2 = 2-[12-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoyl]-glycerol; Xref=Rhea:RHEA:63224, ChEBI:CHEBI:15379, ChEBI:CHEBI:52392, ChEBI:CHEBI:146254; Evidence={ECO:0000269|PubMed:11956198}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63225; Evidence={ECO:0000269|PubMed:11956198}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + O2 = 1-octadecanoyl-2-(15-hydroperoxy-5Z,8Z,11Z,13E-eicosatetraenoyl)-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:63264, ChEBI:CHEBI:15379, ChEBI:CHEBI:74965, ChEBI:CHEBI:146283; Evidence={ECO:0000269|PubMed:27435673}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63265; Evidence={ECO:0000305|PubMed:27435673}; CATALYTIC ACTIVITY: Reaction=a 1-acyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phospho-(1D-myo-inositol) + O2 = a 1-acyl-2-(15-hydroperoxy-5Z,8Z,11Z,13E-eicosatetraenoyl)-sn-glycero-3-phospho-(1D-myo-inositol); Xref=Rhea:RHEA:63276, ChEBI:CHEBI:15379, ChEBI:CHEBI:75243, ChEBI:CHEBI:146285; Evidence={ECO:0000269|PubMed:27435673}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63277; Evidence={ECO:0000305|PubMed:27435673}; CATALYTIC ACTIVITY: Reaction=a 1-acyl-2-(8Z,11Z,14Z-eicosatrienoyl)-sn-glycero-3-phospho-(1D-myo-inositol) + O2 = a 1-acyl-2-(15-hydroperoxy-8Z,11Z,13E-eicosatrienoyl)-sn-glycero-3-phospho-(1D-myo-inositol); Xref=Rhea:RHEA:63280, ChEBI:CHEBI:15379, ChEBI:CHEBI:146286, ChEBI:CHEBI:146287; Evidence={ECO:0000269|PubMed:27435673}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63281; Evidence={ECO:0000305|PubMed:27435673}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphoethanolamine + O2 = 1-octadecanoyl-2-(15-hydroperoxy-5Z,8Z,11Z,13E-eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:63268, ChEBI:CHEBI:15379, ChEBI:CHEBI:78268, ChEBI:CHEBI:146282; Evidence={ECO:0000269|PubMed:27435673}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63269; Evidence={ECO:0000305|PubMed:27435673}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phospho-(1D-myo-inositol) + O2 = 1-octadecanoyl-2-(15-hydroperoxy-5Z,8Z,11Z,13E-eicosatetraenoyl)-sn-glycero-3-phospho-(1D-myo-inositol); Xref=Rhea:RHEA:63272, ChEBI:CHEBI:15379, ChEBI:CHEBI:133606, ChEBI:CHEBI:146284; Evidence={ECO:0000269|PubMed:27435673}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63273; Evidence={ECO:0000305|PubMed:27435673}; CATALYTIC ACTIVITY: Reaction=(8Z,11Z,14Z)-eicosatrienoate + O2 = 15-hydroperoxy-(8Z,11Z,13E)-eicosatrienoate; Xref=Rhea:RHEA:63312, ChEBI:CHEBI:15379, ChEBI:CHEBI:71589, ChEBI:CHEBI:146292; Evidence={ECO:0000269|PubMed:27435673}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63313; Evidence={ECO:0000269|PubMed:27435673}; CATALYTIC ACTIVITY: Reaction=(7S)-hydroperoxy-(4Z,8E,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 = (7S,17S)-dihydroperoxy-(4Z,8E,10Z,13Z,15E,19Z)-docosahexaenoate; Xref=Rhea:RHEA:64728, ChEBI:CHEBI:15379, ChEBI:CHEBI:140349, ChEBI:CHEBI:156049; Evidence={ECO:0000269|PubMed:32404334}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64729; Evidence={ECO:0000305|PubMed:32404334}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = 15-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate; Xref=Rhea:RHEA:48832, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:90821; Evidence={ECO:0000269|PubMed:10542053}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48833; Evidence={ECO:0000305|PubMed:10542053};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1100 uM for arachidonate (isoform D at pH 7.4 and 20 degrees Celsius) {ECO:0000269|PubMed:10542053}; KM=10 uM for linoleate (isoform A at pH 7.4 and 20 degrees Celsius) {ECO:0000269|PubMed:10542053}; KM=25 uM for (5Z,8Z,11Z,14Z)-eicosatetraenoate (isoform A at pH 7.4 and 20 degrees Celsius) {ECO:0000269|PubMed:10542053}; KM=23 uM for (5Z,8Z,11Z,14Z)-eicosatetraenoate (Sf9-expressed enzyme) {ECO:0000269|PubMed:11956198}; KM=15 uM for (5Z,8Z,11Z,14Z)-eicosatetraenoate (E.coli-expressed enzyme) {ECO:0000269|PubMed:11956198}; KM=9 uM for 2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol (Sf9-expressed enzyme) {ECO:0000269|PubMed:11956198}; KM=8 uM for 2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol (E.coli-expressed enzyme) {ECO:0000269|PubMed:11956198}; KM=14 uM for anandamide (Sf9-expressed enzyme) {ECO:0000269|PubMed:11956198}; KM=11 uM for anandamide (E. Coli-expressed enzyme) {ECO:0000269|PubMed:11956198}; KM=8 uM for (5Z,8Z,11Z,14Z)-eicosatetraenoate {ECO:0000269|PubMed:17493578}; KM=11 uM for N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-glycine {ECO:0000269|PubMed:17493578}; KM=6 uM for N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-alanine {ECO:0000269|PubMed:17493578}; KM=8 uM for N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-gamma-aminobutanoate {ECO:0000269|PubMed:17493578}; KM=1.2 uM for (5Z,8Z,11Z,14Z)-eicosatetraenoate {ECO:0000269|PubMed:24282679}; KM=4 uM for (5Z,8Z,11Z,14Z)-eicosatetraenoate {ECO:0000269|PubMed:27145229}; KM=3.3 uM for (5S)-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate {ECO:0000269|PubMed:27145229}; KM=19 uM for (5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate {ECO:0000269|PubMed:27145229}; KM=1.74 uM for (5Z,8Z,11Z,14Z)-eicosatetraenoate {ECO:0000269|PubMed:27435673}; KM=3.46 uM for (8Z,11Z,14Z)-eicosatrienoate {ECO:0000269|PubMed:27435673}; Vmax=4 umol/min/mg enzyme with arachidonate as substrate (isoform A at pH 7.4 and 20 degrees Celsius) {ECO:0000269|PubMed:10542053}; Vmax=2 umol/min/mg enzyme with arachidonate as substrate (isoform D at pH 7.4 and 20 degrees Celsius) {ECO:0000269|PubMed:10542053}; Vmax=4 umol/min/mg enzyme with linoleate as substrate (isoform A at pH 7.4 and 20 degrees Celsius) {ECO:0000269|PubMed:10542053}; Vmax=0.82 nmol/sec/mg enzyme with (5Z,8Z,11Z,14Z)-eicosatetraenoate (Sf9-expressed enzyme) {ECO:0000269|PubMed:11956198}; Vmax=4.3 nmol/sec/mg enzyme with (5Z,8Z,11Z,14Z)-eicosatetraenoate (E.coli-expressed enzyme) {ECO:0000269|PubMed:11956198}; Vmax=9 nmol/sec/mg enzyme with 2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol (Sf9-expressed enzyme) {ECO:0000269|PubMed:11956198}; Vmax=8 nmol/sec/mg enzyme with 2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol (E.coli-expressed enzyme) {ECO:0000269|PubMed:11956198}; Vmax=14 nmol/sec/mg enzyme with anandamide (Sf9-expressed enzyme) {ECO:0000269|PubMed:11956198}; Vmax=11 nmol/sec/mg enzyme with anandamide (E.coli-expressed enzyme) {ECO:0000269|PubMed:11956198}; Note=kcat is 2 sec(-1) for (5Z,8Z,11Z,14Z)-eicosatetraenoate. kcat is 2.1 sec(-1) for N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-glycine. kcat is 2 sec(-1) for N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-alanine. kcat is 2 sec(-1) for N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-gamma-aminobutanoate (PubMed:17493578). kcat is 0.18 sec(-1) for (5Z,8Z,11Z,14Z)-eicosatetraenoate (PubMed:24282679). kcat is 1 sec(-1) for (5Z,8Z,11Z,14Z)-eicosatetraenoate. kcat is 2.1 sec(-1) for (5S)-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate. kcat is 1.5 sec(-1) for (5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate (PubMed:27145229). kcat is 0.46 sec(-1) for (5Z,8Z,11Z,14Z)-eicosatetraenoate. kcat is 0.31 sec(-1) for (8Z,11Z,14Z)-eicosatrienoate (PubMed:27435673). {ECO:0000269|PubMed:17493578, ECO:0000269|PubMed:24282679, ECO:0000269|PubMed:27145229, ECO:0000269|PubMed:27435673};
|
PATHWAY: Lipid metabolism; hydroperoxy eicosatetraenoic acid biosynthesis. {ECO:0000269|PubMed:10542053}.
| null | null |
FUNCTION: [Isoform A]: Non-heme iron-containing dioxygenase that catalyzes the stereo-specific peroxidation of free and esterified polyunsaturated fatty acids (PUFAs) generating a spectrum of bioactive lipid mediators (Probable) (PubMed:10542053, PubMed:10625675, PubMed:12704195, PubMed:17493578, PubMed:18311922, PubMed:24282679, PubMed:24497644, PubMed:32404334, PubMed:9177185). It inserts peroxyl groups at C15 of arachidonate ((5Z,8Z,11Z,14Z)-eicosatetraenoate) producing (15S)-hydroperoxyeicosatetraenoate/(15S)-HPETE (Probable) (PubMed:10625675, PubMed:11956198, PubMed:12704195, PubMed:17493578, PubMed:24282679, PubMed:24497644, PubMed:9177185). Also peroxidizes linoleate ((9Z,12Z)-octadecadienoate) to 13-hydroperoxyoctadecadienoate/13-HPODE (Probable) (PubMed:10542053, PubMed:27435673). Oxygenates arachidonyl derivatives such as 2-arachidonoylglycerol (2-AG) leading to the production and extracellular release of 15-hydroxyeicosatetraenoyl glycerol (15-HETE-G) that acts as a peroxisome proliferator-activated receptor alpha agonist (PubMed:11956198, PubMed:17493578, PubMed:18311922). Has the ability to efficiently class-switch ALOX5 pro-inflammatory mediators into anti-inflammatory intermediates (PubMed:27145229). Participates in the sequential oxidations of DHA ((4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate) to generate specialized pro-resolving mediators (SPMs) resolvin D5 ((7S,17S)-diHPDHA), which can actively down-regulate the immune response and have anti-aggregation properties with platelets (PubMed:32404334). In addition to free PUFAs hydrolyzed from phospholipids, it directly oxidizes PUFAs esterified to membrane-bound phospholipids (PubMed:27435673). Has no detectable 8S-lipoxygenase activity on arachidonate but reacts with (8S)-HPETE to produce (8S,15S)-diHPETE (Probable). May regulate progression through the cell cycle and cell proliferation (PubMed:11839751, PubMed:12704195). May also regulate cytokine secretion by macrophages and therefore play a role in the immune response (PubMed:18067895). May also regulate macrophage differentiation into proatherogenic foam cells (PubMed:22912809). {ECO:0000269|PubMed:10542053, ECO:0000269|PubMed:10625675, ECO:0000269|PubMed:11839751, ECO:0000269|PubMed:11956198, ECO:0000269|PubMed:12704195, ECO:0000269|PubMed:17493578, ECO:0000269|PubMed:18067895, ECO:0000269|PubMed:18311922, ECO:0000269|PubMed:22912809, ECO:0000269|PubMed:24282679, ECO:0000269|PubMed:24497644, ECO:0000269|PubMed:27145229, ECO:0000269|PubMed:27435673, ECO:0000269|PubMed:32404334, ECO:0000269|PubMed:9177185, ECO:0000305|PubMed:10542053, ECO:0000305|PubMed:16112079, ECO:0000305|PubMed:27145229, ECO:0000305|PubMed:27435673}.; FUNCTION: [Isoform B]: Does not convert arachidonic acid to 15S-hydroperoxyeicosatetraenoic acid/(15S)-HPETE. {ECO:0000269|PubMed:12704195}.
|
Homo sapiens (Human)
|
O15297
|
PPM1D_HUMAN
|
MAGLYSLGVSVFSDQGGRKYMEDVTQIVVEPEPTAEEKPSPRRSLSQPLPPRPSPAALPGGEVSGKGPAVAAREARDPLPDAGASPAPSRCCRRRSSVAFFAVCDGHGGREAAQFAREHLWGFIKKQKGFTSSEPAKVCAAIRKGFLACHLAMWKKLAEWPKTMTGLPSTSGTTASVVIIRGMKMYVAHVGDSGVVLGIQDDPKDDFVRAVEVTQDHKPELPKERERIEGLGGSVMNKSGVNRVVWKRPRLTHNGPVRRSTVIDQIPFLAVARALGDLWSYDFFSGEFVVSPEPDTSVHTLDPQKHKYIILGSDGLWNMIPPQDAISMCQDQEEKKYLMGEHGQSCAKMLVNRALGRWRQRMLRADNTSAIVICISPEVDNQGNFTNEDELYLNLTDSPSYNSQETCVMTPSPCSTPPVKSLEEDPWPRVNSKDHIPALVRSNAFSENFLEVSAEIARENVQGVVIPSKDPEPLEENCAKALTLRIHDSLNNSLPIGLVPTNSTNTVMDQKNLKMSTPGQMKAQEIERTPPTNFKRTLEESNSGPLMKKHRRNGLSRSSGAQPASLPTTSQRKNSVKLTMRRRLRGQKKIGNPLLHQHRKTVCVC
|
3.1.3.16
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000250};
|
cellular response to starvation [GO:0009267]; DNA damage response, signal transduction by p53 class mediator [GO:0030330]; DNA methylation-dependent heterochromatin formation [GO:0006346]; G2/M transition of mitotic cell cycle [GO:0000086]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of gene expression, epigenetic [GO:0045814]; peptidyl-threonine dephosphorylation [GO:0035970]; protein dephosphorylation [GO:0006470]; regulation of transcription initiation by RNA polymerase II [GO:0060260]; response to bacterium [GO:0009617]; response to radiation [GO:0009314]
|
cytosol [GO:0005829]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
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metal ion binding [GO:0046872]; mitogen-activated protein kinase binding [GO:0051019]; myosin phosphatase activity [GO:0017018]; protein serine/threonine kinase activity [GO:0004674]; protein serine/threonine phosphatase activity [GO:0004722]
|
PF00481;
|
3.60.40.10;
|
PP2C family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28343630, ECO:0000269|PubMed:9177166}. Cytoplasm, cytosol {ECO:0000269|PubMed:28343630}.
|
CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16;
| null | null | null | null |
FUNCTION: Involved in the negative regulation of p53 expression (PubMed:23242139). Required for the relief of p53-dependent checkpoint mediated cell cycle arrest. Binds to and dephosphorylates 'Ser-15' of TP53 and 'Ser-345' of CHEK1 which contributes to the functional inactivation of these proteins (PubMed:15870257, PubMed:16311512). Mediates MAPK14 dephosphorylation and inactivation (PubMed:21283629). Is also an important regulator of global heterochromatin silencing and critical in maintaining genome integrity (By similarity). {ECO:0000250|UniProtKB:Q9QZ67, ECO:0000269|PubMed:15870257, ECO:0000269|PubMed:16311512, ECO:0000269|PubMed:21283629, ECO:0000269|PubMed:23242139}.
|
Homo sapiens (Human)
|
O15303
|
GRM6_HUMAN
|
MARPRRAREPLLVALLPLAWLAQAGLARAAGSVRLAGGLTLGGLFPVHARGAAGRACGQLKKEQGVHRLEAMLYALDRVNADPELLPGVRLGARLLDTCSRDTYALEQALSFVQALIRGRGDGDEVGVRCPGGVPPLRPAPPERVVAVVGASASSVSIMVANVLRLFAIPQISYASTAPELSDSTRYDFFSRVVPPDSYQAQAMVDIVRALGWNYVSTLASEGNYGESGVEAFVQISREAGGVCIAQSIKIPREPKPGEFSKVIRRLMETPNARGIIIFANEDDIRRVLEAARQANLTGHFLWVGSDSWGAKTSPILSLEDVAVGAITILPKRASIDGFDQYFMTRSLENNRRNIWFAEFWEENFNCKLTSSGTQSDDSTRKCTGEERIGRDSTYEQEGKVQFVIDAVYAIAHALHSMHQALCPGHTGLCPAMEPTDGRMLLQYIRAVRFNGSAGTPVMFNENGDAPGRYDIFQYQATNGSASSGGYQAVGQWAETLRLDVEALQWSGDPHEVPSSLCSLPCGPGERKKMVKGVPCCWHCEACDGYRFQVDEFTCEACPGDMRPTPNHTGCRPTPVVRLSWSSPWAAPPLLLAVLGIVATTTVVATFVRYNNTPIVRASGRELSYVLLTGIFLIYAITFLMVAEPGAAVCAARRLFLGLGTTLSYSALLTKTNRIYRIFEQGKRSVTPPPFISPTSQLVITFSLTSLQVVGMIAWLGARPPHSVIDYEEQRTVDPEQARGVLKCDMSDLSLIGCLGYSLLLMVTCTVYAIKARGVPETFNEAKPIGFTMYTTCIIWLAFVPIFFGTAQSAEKIYIQTTTLTVSLSLSASVSLGMLYVPKTYVILFHPEQNVQKRKRSLKATSTVAAPPKGEDAEAHK
| null | null |
chemical synaptic transmission [GO:0007268]; detection of light stimulus involved in visual perception [GO:0050908]; detection of visible light [GO:0009584]; G protein-coupled glutamate receptor signaling pathway [GO:0007216]; locomotory behavior [GO:0007626]; positive regulation of calcium ion import across plasma membrane [GO:1905665]; regulation of synaptic transmission, glutamatergic [GO:0051966]; retina development in camera-type eye [GO:0060041]
|
dendrite [GO:0030425]; endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; new growing cell tip [GO:0035841]; plasma membrane [GO:0005886]; synapse [GO:0045202]
|
adenylate cyclase inhibiting G protein-coupled glutamate receptor activity [GO:0001640]; G protein-coupled receptor activity [GO:0004930]; glutamate receptor activity [GO:0008066]; protein homodimerization activity [GO:0042803]
|
PF00003;PF01094;PF07562;
|
3.40.50.2300;2.10.50.30;
|
G-protein coupled receptor 3 family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17405131}; Multi-pass membrane protein {ECO:0000269|PubMed:17405131}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:17405131}; Multi-pass membrane protein {ECO:0000269|PubMed:17405131}. Golgi apparatus membrane {ECO:0000269|PubMed:17405131}; Multi-pass membrane protein {ECO:0000269|PubMed:17405131}. Cell projection, dendrite {ECO:0000250}. Note=Subject to trafficking from the endoplasmic reticulum to the Golgi apparatus and then to the cell membrane.
| null | null | null | null | null |
FUNCTION: G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity (By similarity). Signaling stimulates TRPM1 channel activity and Ca(2+) uptake. Required for normal vision. {ECO:0000250, ECO:0000269|PubMed:23452348}.
|
Homo sapiens (Human)
|
O15304
|
SIVA_HUMAN
|
MPKRSCPFADVAPLQLKVRVSQRELSRGVCAERYSQEVFEKTKRLLFLGAQAYLDHVWDEGCAVVHLPESPKPGPTGAPRAARGQMLIGPDGRLIRSLGQASEADPSGVASIACSSCVRAVDGKAVCGQCERALCGQCVRTCWGCGSVACTLCGLVDCSDMYEKVLCTSCAMFET
| null |
COFACTOR: [Isoform 1]: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:16683188}; Note=Isoform 1 binds 3 Zn(2+) ions. {ECO:0000269|PubMed:16683188}; COFACTOR: [Isoform 2]: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:16683188}; Note=Isoform 2 binds 2 Zn(2+) ions. {ECO:0000269|PubMed:16683188};
|
activation-induced cell death of T cells [GO:0006924]; extrinsic apoptotic signaling pathway [GO:0097191]; intrinsic apoptotic signaling pathway [GO:0097193]; negative regulation of NF-kappaB transcription factor activity [GO:0032088]; positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway [GO:1901030]
|
cytoplasm [GO:0005737]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]
|
CD27 receptor binding [GO:0005175]; metal ion binding [GO:0046872]; tumor necrosis factor receptor binding [GO:0005164]; virus receptor activity [GO:0001618]; zinc ion binding [GO:0008270]
|
PF05458;
| null | null |
PTM: Phosphorylated by ABL2/ARG in response to oxidative stress. {ECO:0000269|PubMed:11278261}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15034012}. Nucleus {ECO:0000269|PubMed:15034012}. Note=In the nucleus, accumulates in dot-like structures.
| null | null | null | null | null |
FUNCTION: Induces CD27-mediated apoptosis. Inhibits BCL2L1 isoform Bcl-x(L) anti-apoptotic activity. Inhibits activation of NF-kappa-B and promotes T-cell receptor-mediated apoptosis. {ECO:0000269|PubMed:12011449, ECO:0000269|PubMed:14739602, ECO:0000269|PubMed:15034012, ECO:0000269|PubMed:15958577, ECO:0000269|PubMed:16491128}.
|
Homo sapiens (Human)
|
O15305
|
PMM2_HUMAN
|
MAAPGPALCLFDVDGTLTAPRQKITKEMDDFLQKLRQKIKIGVVGGSDFEKVQEQLGNDVVEKYDYVFPENGLVAYKDGKLLCRQNIQSHLGEALIQDLINYCLSYIAKIKLPKKRGTFIEFRNGMLNVSPIGRSCSQEERIEFYELDKKENIRQKFVADLRKEFAGKGLTFSIGGQISFDVFPDGWDKRYCLRHVENDGYKTIYFFGDKTMPGGNDHEIFTDPRTMGYSVTAPEDTRRICELLFS
|
5.4.2.8
| null |
GDP-mannose biosynthetic process [GO:0009298]; mannose metabolic process [GO:0006013]; protein glycosylation [GO:0006486]; protein N-linked glycosylation [GO:0006487]
|
cytosol [GO:0005829]; neuronal cell body [GO:0043025]; nucleoplasm [GO:0005654]
|
metal ion binding [GO:0046872]; phosphomannomutase activity [GO:0004615]
|
PF03332;
|
3.30.1240.20;3.40.50.1000;
|
Eukaryotic PMM family
| null |
SUBCELLULAR LOCATION: Cytoplasm.
|
CATALYTIC ACTIVITY: Reaction=alpha-D-mannose 1-phosphate = D-mannose 6-phosphate; Xref=Rhea:RHEA:11140, ChEBI:CHEBI:58409, ChEBI:CHEBI:58735; EC=5.4.2.8; Evidence={ECO:0000269|PubMed:16540464};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=16 uM for alpha-D-mannose 1-phosphate {ECO:0000269|PubMed:16540464}; KM=13.5 uM for alpha-D-glucose 1-phosphate {ECO:0000269|PubMed:16540464};
|
PATHWAY: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2.
| null | null |
FUNCTION: Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions. {ECO:0000250|UniProtKB:Q92871}.
|
Homo sapiens (Human)
|
O15315
|
RA51B_HUMAN
|
MGSKKLKRVGLSQELCDRLSRHQILTCQDFLCLSPLELMKVTGLSYRGVHELLCMVSRACAPKMQTAYGIKAQRSADFSPAFLSTTLSALDEALHGGVACGSLTEITGPPGCGKTQFCIMMSILATLPTNMGGLEGAVVYIDTESAFSAERLVEIAESRFPRYFNTEEKLLLTSSKVHLYRELTCDEVLQRIESLEEEIISKGIKLVILDSVASVVRKEFDAQLQGNLKERNKFLAREASSLKYLAEEFSIPVILTNQITTHLSGALASQADLVSPADDLSLSEGTSGSSCVIAALGNTWSHSVNTRLILQYLDSERRQILIAKSPLAPFTSFVYTIKEEGLVLQETTFCSVTQAELNWAPEILPPQPPEQLGLQMCHHTQLIF
| null | null |
blastocyst growth [GO:0001832]; DNA recombination [GO:0006310]; DNA repair [GO:0006281]; double-strand break repair via homologous recombination [GO:0000724]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of G2/M transition of mitotic cell cycle [GO:0010971]; reciprocal meiotic recombination [GO:0007131]; somite development [GO:0061053]
|
nucleoplasm [GO:0005654]; nucleus [GO:0005634]; Rad51B-Rad51C-Rad51D-XRCC2 complex [GO:0033063]; replication fork [GO:0005657]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent activity, acting on DNA [GO:0008094]; ATP-dependent DNA damage sensor activity [GO:0140664]; DNA binding [GO:0003677]; double-stranded DNA binding [GO:0003690]; four-way junction DNA binding [GO:0000400]; single-stranded DNA binding [GO:0003697]
|
PF08423;
|
3.40.50.300;
|
RecA family, RAD51 subfamily
|
PTM: Phosphorylated on tyrosine residues by BCR-ABL. {ECO:0000269|PubMed:19657362}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Involved in the homologous recombination repair (HRR) pathway of double-stranded DNA breaks arising during DNA replication or induced by DNA-damaging agents. May promote the assembly of presynaptic RAD51 nucleoprotein filaments. Binds single-stranded DNA and double-stranded DNA and has DNA-dependent ATPase activity. Part of the RAD51 paralog protein complex BCDX2 which acts in the BRCA1-BRCA2-dependent HR pathway. Upon DNA damage, BCDX2 acts downstream of BRCA2 recruitment and upstream of RAD51 recruitment. BCDX2 binds predominantly to the intersection of the four duplex arms of the Holliday junction and to junction of replication forks. The BCDX2 complex was originally reported to bind single-stranded DNA, single-stranded gaps in duplex DNA and specifically to nicks in duplex DNA. The BCDX2 subcomplex RAD51B:RAD51C exhibits single-stranded DNA-dependent ATPase activity suggesting an involvement in early stages of the HR pathway. {ECO:0000269|PubMed:11751635, ECO:0000269|PubMed:11751636, ECO:0000269|PubMed:11842113, ECO:0000269|PubMed:12441335, ECO:0000269|PubMed:23108668, ECO:0000269|PubMed:23149936}.
|
Homo sapiens (Human)
|
O15318
|
RPC7_HUMAN
|
MAGNKGRGRAAYTFNIEAVGFSKGEKLPDVVLKPPPLFPDTDYKPVPLKTGEGEEYMLALKQELRETMKRMPYFIETPEERQDIERYSKRYMKVYKEEWIPDWRRLPREMMPRNKCKKAGPKPKKAKDAGKGTPLTNTEDVLKKMEELEKRGDGEKSDEENEEKEGSKEKSKEGDDDDDDDAAEQEEYDEEEQEEENDYINSYFEDGDDFGADSDDNMDEATY
| null | null |
cell population proliferation [GO:0008283]; defense response to virus [GO:0051607]; innate immune response [GO:0045087]; positive regulation of innate immune response [GO:0045089]; positive regulation of interferon-beta production [GO:0032728]; regulation of transcription by RNA polymerase III [GO:0006359]; transcription by RNA polymerase III [GO:0006383]
|
cytosol [GO:0005829]; nuclear body [GO:0016604]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA polymerase III complex [GO:0005666]
|
chromatin binding [GO:0003682]; DNA-directed 5'-3' RNA polymerase activity [GO:0003899]
|
PF11705;
| null |
Eukaryotic RPC7 RNA polymerase subunit family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20154270, ECO:0000269|PubMed:21898682, ECO:0000269|PubMed:33335104}. Cytoplasm {ECO:0000250|UniProtKB:Q6NXY9}. Note=Excluded from nucleoli (PubMed:21898682). In zygotes and the 2-cell stage embryos, mainly in the cytoplasm. Starts to localize to the nucleus in the 8-16 cell stage embryo and early blastocysts (By similarity). {ECO:0000250|UniProtKB:Q6NXY9, ECO:0000269|PubMed:21898682}.
| null | null | null | null | null |
FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates (PubMed:20413673, PubMed:33558764, PubMed:34675218, PubMed:35637192). Specific peripheric component of RNA polymerase III (Pol III) which synthesizes small non-coding RNAs including 5S rRNA, snRNAs, tRNAs and miRNAs from at least 500 distinct genomic loci (PubMed:20154270, PubMed:20413673, PubMed:35637192). Acts as a long tether that bridges POLR3C/RPC3-POLR3F/RPC6-POLR3G/RPC7 heterotrimer and the mobile stalk of Pol III, coordinating the dynamics of Pol III stalk and clamp modules during the transition from apo to elongation state. Pol III exists as two alternative complexes defined by the mutually exclusive incorporation of subunit POLR3G/RPC7alpha or POLR3GL/RPC7beta. POLR3G/RPC7alpha modulates Pol III transcriptome by specifically enhancing the transcription of snaR-A non-coding RNAs. At resting state, occupies the active site of apo Pol III and keeps Pol III in an autoinhibitory mode, preventing non-specific transcription (PubMed:33558764, PubMed:33558766, PubMed:35637192). Pol III plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as a nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts, such as Epstein-Barr virus-encoded RNAs (EBERs), induce type I interferon and NF-kappa-B through the RIG-I pathway (PubMed:19609254, PubMed:19631370). {ECO:0000269|PubMed:19609254, ECO:0000269|PubMed:19631370, ECO:0000269|PubMed:20154270, ECO:0000269|PubMed:20413673, ECO:0000269|PubMed:33558764, ECO:0000269|PubMed:33558766, ECO:0000269|PubMed:34675218, ECO:0000269|PubMed:35637192}.
|
Homo sapiens (Human)
|
O15327
|
INP4B_HUMAN
|
MEIKEEGASEEGQHFLPTAQANDPGDCQFTSIQKTPNEPQLEFILACKDLVAPVRDRKLNTLVQISVIHPVEQSLTRYSSTEIVEGTRDPLFLTGVTFPSEYPIYEETKIKLTVYDVKDKSHDTVRTSVLPEHKDPPPEVGRSFLGYASFKVGELLKSKEQLLVLSLRTSDGGKVVGTIEVSVVKMGEIEDGEADHITTDVQGQKCALVCECTAPESVSGKDNLPFLNSVLKNPVCKLYRFPTSDNKWMRIREQMSESILSFHIPKELISLHIKEDLCRNQEIKELGELSPHWDNLRKNVLTHCDQMVNMYQDILTELSKETGSSFKSSSSKGEKTLEFVPINLHLQRMQVHSPHLKDALYDVITVGAPAAHFQGFKNGGLRKLLHRFETERRNTGYQFIYYSPENTAKAKEVLSNINQLQPLIATHADLLLNSASQHSPDSLKNSLKMLSEKTELFVHAFKDQLVRSALLALYTARPGGILKKPPSPKSSTEESSPQDQPPVMRGQDSIPHHSDYDEEEWDRVWANVGKSLNCIIAMVDKLIERDGGSEGSGGNNDGEKEPSLTDAIPSHPREDWYEQLYPLILTLKDCMGEVVNRAKQSLTFVLLQELAYSLPQCLMLTLRRDIVFSQALAGLVCGFIIKLQTSLYDPGFLQQLHTVGLIVQYEGLLSTYSDEIGMLEDMAVGISDLKKVAFKIIEAKSNDVLPVITGRREHYVVEVKLPARMFESLPLQIKEGQLLHVYPVLFNVGINEQQTLAERFGDVSLQESINQENFELLQEYYKIFMEKMPPDYISHFQEQNDLKALLENLLQNIQSKKRKNVEIMWLAATICRKLNGIRFTCCKSAKDRTSMSVTLEQCSILRDEHQLHKDFFIRALDCMRREGCRIENVLKNIKCRKYAFNMLQLMAFPKYYRPPEGTYGKADT
|
3.1.3.66
| null |
inositol phosphate metabolic process [GO:0043647]; phosphatidylinositol biosynthetic process [GO:0006661]; phosphatidylinositol dephosphorylation [GO:0046856]; signal transduction [GO:0007165]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]
|
inositol-1,3,4-trisphosphate 4-phosphatase activity [GO:0017161]; inositol-3,4-bisphosphate 4-phosphatase activity [GO:0052828]; phosphatidylinositol-3,4-bisphosphate 4-phosphatase activity [GO:0016316]
| null |
6.10.250.230;2.60.40.150;
|
Inositol 3,4-bisphosphate 4-phosphatase family
| null | null |
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4-bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + phosphate; Xref=Rhea:RHEA:17193, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57658, ChEBI:CHEBI:58088; EC=3.1.3.66; Evidence={ECO:0000269|PubMed:19647222, ECO:0000269|PubMed:24070612, ECO:0000305|PubMed:24591580}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17194; Evidence={ECO:0000305|PubMed:24070612}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,3,4-trisphosphate + H2O = 1D-myo-inositol 1,3-bisphosphate + phosphate; Xref=Rhea:RHEA:43392, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58414, ChEBI:CHEBI:83242; Evidence={ECO:0000269|PubMed:24070612}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43393; Evidence={ECO:0000305|PubMed:24070612}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 3,4-bisphosphate + H2O = 1D-myo-inositol 3-phosphate + phosphate; Xref=Rhea:RHEA:43388, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58401, ChEBI:CHEBI:83241; Evidence={ECO:0000250|UniProtKB:Q9QWG5};
| null |
PATHWAY: Signal transduction; phosphatidylinositol signaling pathway. {ECO:0000250|UniProtKB:Q9QWG5}.
| null | null |
FUNCTION: Catalyzes the hydrolysis of the 4-position phosphate of phosphatidylinositol 3,4-bisphosphate, inositol 1,3,4-trisphosphate and inositol 3,4-trisphosphate (PubMed:24070612, PubMed:24591580). Plays a role in the late stages of macropinocytosis by dephosphorylating phosphatidylinositol 3,4-bisphosphate in membrane ruffles (PubMed:24591580). The lipid phosphatase activity is critical for tumor suppressor function. Antagonizes the PI3K-AKT/PKB signaling pathway by dephosphorylating phosphoinositides and thereby modulating cell cycle progression and cell survival (PubMed:19647222, PubMed:24070612). {ECO:0000269|PubMed:19647222, ECO:0000269|PubMed:24070612, ECO:0000269|PubMed:24591580}.
|
Homo sapiens (Human)
|
O15342
|
VA0E1_HUMAN
|
MAYHGLTVPLIVMSVFWGFVGFLVPWFIPKGPNRGVIITMLVTCSVCCYLFWLIAILAQLNPLFGPQLKNETIWYLKYHWP
| null | null |
proton transmembrane transport [GO:1902600]; regulation of macroautophagy [GO:0016241]; transmembrane transport [GO:0055085]; vacuolar acidification [GO:0007035]
|
endosome membrane [GO:0010008]; lysosomal membrane [GO:0005765]; phagocytic vesicle membrane [GO:0030670]; proton-transporting V-type ATPase, V0 domain [GO:0033179]
|
ATPase-coupled ion transmembrane transporter activity [GO:0042625]; proton-transporting ATPase activity, rotational mechanism [GO:0046961]
|
PF05493;
| null |
V-ATPase e1/e2 subunit family
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (PubMed:33065002). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity). {ECO:0000250|UniProtKB:Q2KIB5, ECO:0000269|PubMed:33065002}.
|
Homo sapiens (Human)
|
O15344
|
TRI18_HUMAN
|
METLESELTCPICLELFEDPLLLPCAHSLCFNCAHRILVSHCATNESVESITAFQCPTCRHVITLSQRGLDGLKRNVTLQNIIDRFQKASVSGPNSPSETRRERAFDANTMTSAEKVLCQFCDQDPAQDAVKTCVTCEVSYCDECLKATHPNKKPFTGHRLIEPIPDSHIRGLMCLEHEDEKVNMYCVTDDQLICALCKLVGRHRDHQVAALSERYDKLKQNLESNLTNLIKRNTELETLLAKLIQTCQHVEVNASRQEAKLTEECDLLIEIIQQRRQIIGTKIKEGKVMRLRKLAQQIANCKQCIERSASLISQAEHSLKENDHARFLQTAKNITERVSMATASSQVLIPEINLNDTFDTFALDFSREKKLLECLDYLTAPNPPTIREELCTASYDTITVHWTSDDEFSVVSYELQYTIFTGQANVVSLCNSADSWMIVPNIKQNHYTVHGLQSGTKYIFMVKAINQAGSRSSEPGKLKTNSQPFKLDPKSAHRKLKVSHDNLTVERDESSSKKSHTPERFTSQGSYGVAGNVFIDSGRHYWEVVISGSTWYAIGLAYKSAPKHEWIGKNSASWALCRCNNNWVVRHNSKEIPIEPAPHLRRVGILLDYDNGSIAFYDALNSIHLYTFDVAFAQPVCPTFTVWNKCLTIITGLPIPDHLDCTEQLP
|
2.3.2.27
| null |
microtubule cytoskeleton organization [GO:0000226]; negative regulation of microtubule depolymerization [GO:0007026]; pattern specification process [GO:0007389]; positive regulation of stress-activated MAPK cascade [GO:0032874]; protein localization to microtubule [GO:0035372]; regulation of microtubule cytoskeleton organization [GO:0070507]
|
centriolar satellite [GO:0034451]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; microtubule [GO:0005874]; microtubule associated complex [GO:0005875]; spindle [GO:0005819]
|
enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; microtubule binding [GO:0008017]; phosphoprotein binding [GO:0051219]; protein homodimerization activity [GO:0042803]; transferase activity [GO:0016740]; ubiquitin protein ligase binding [GO:0031625]; zinc ion binding [GO:0008270]
|
PF18568;PF00041;PF00622;PF00643;PF13445;
|
2.60.120.920;4.10.830.40;3.30.160.60;2.60.40.10;3.30.40.10;
|
TRIM/RBCC family
|
PTM: Phosphorylated on serine and threonine residues. {ECO:0000269|PubMed:11806752}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10077590}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10077590}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:10077590}. Note=Microtubule-associated. It is associated with microtubules throughout the cell cycle, co-localizing with cytoplasmic fibers in interphase and with the mitotic spindle and midbodies during mitosis and cytokinesis.
|
CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27;
| null | null | null | null |
FUNCTION: Has E3 ubiquitin ligase activity towards IGBP1, promoting its monoubiquitination, which results in deprotection of the catalytic subunit of protein phosphatase PP2A, and its subsequent degradation by polyubiquitination. {ECO:0000269|PubMed:10400985, ECO:0000269|PubMed:11685209, ECO:0000269|PubMed:22613722}.
|
Homo sapiens (Human)
|
O15347
|
HMGB3_HUMAN
|
MAKGDPKKPKGKMSAYAFFVQTCREEHKKKNPEVPVNFAEFSKKCSERWKTMSGKEKSKFDEMAKADKVRYDREMKDYGPAKGGKKKKDPNAPKRPPSGFFLFCSEFRPKIKSTNPGISIGDVAKKLGEMWNNLNDSEKQPYITKAAKLKEKYEKDVADYKSKGKFDGAKGPAKVARKKVEEEDEEEEEEEEEEEEEEDE
| null | null |
DNA geometric change [GO:0032392]; DNA recombination [GO:0006310]; innate immune response [GO:0045087]; regulation of transcription by RNA polymerase II [GO:0006357]
|
chromosome [GO:0005694]; cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
DNA binding, bending [GO:0008301]; double-stranded DNA binding [GO:0003690]; four-way junction DNA binding [GO:0000400]; RNA binding [GO:0003723]
|
PF00505;PF09011;
|
1.10.30.10;
|
HMGB family
|
PTM: Reduction/oxidation of cysteine residues Cys-23, Cys-45 and Cys-104 and a possible intramolecular disulfide bond involving Cys-23 and Cys-45 give rise to different redox forms with specific functional activities in various cellular compartments: 1- fully reduced HMGB3 (HMGB3C23hC45hC104h), 2- disulfide HMGB3 (HMGB3C23-C45C104h) and 3- sulfonyl HMGB3 (HMGB3C23soC45soC104so). {ECO:0000250|UniProtKB:P09429, ECO:0000305|PubMed:24531895}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P40618, ECO:0000255|PROSITE-ProRule:PRU00267}. Chromosome {ECO:0000305}. Cytoplasm {ECO:0000250|UniProtKB:O54879}.
| null | null | null | null | null |
FUNCTION: Multifunctional protein with various roles in different cellular compartments. May act in a redox sensitive manner. Associates with chromatin and binds DNA with a preference for non-canonical DNA structures such as single-stranded DNA. Can bend DNA and enhance DNA flexibility by looping thus providing a mechanism to promote activities on various gene promoters (By similarity). Proposed to be involved in the innate immune response to nucleic acids by acting as a cytoplasmic promiscuous immunogenic DNA/RNA sensor (By similarity). Negatively regulates B-cell and myeloid cell differentiation. In hematopoietic stem cells may regulate the balance between self-renewal and differentiation. Involved in negative regulation of canonical Wnt signaling (By similarity). {ECO:0000250|UniProtKB:O54879, ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P40618}.
|
Homo sapiens (Human)
|
O15350
|
P73_HUMAN
|
MAQSTATSPDGGTTFEHLWSSLEPDSTYFDLPQSSRGNNEVVGGTDSSMDVFHLEGMTTSVMAQFNLLSSTMDQMSSRAASASPYTPEHAASVPTHSPYAQPSSTFDTMSPAPVIPSNTDYPGPHHFEVTFQQSSTAKSATWTYSPLLKKLYCQIAKTCPIQIKVSTPPPPGTAIRAMPVYKKAEHVTDVVKRCPNHELGRDFNEGQSAPASHLIRVEGNNLSQYVDDPVTGRQSVVVPYEPPQVGTEFTTILYNFMCNSSCVGGMNRRPILIIITLEMRDGQVLGRRSFEGRICACPGRDRKADEDHYREQQALNESSAKNGAASKRAFKQSPPAVPALGAGVKKRRHGDEDTYYLQVRGRENFEILMKLKESLELMELVPQPLVDSYRQQQQLLQRPSHLQPPSYGPVLSPMNKVHGGMNKLPSVNQLVGQPPPHSSAATPNLGPVGPGMLNNHGHAVPANGEMSSSHSAQSMVSGSHCTPPPPYHADPSLVSFLTGLGCPNCIEYFTSQGLQSIYHLQNLTIEDLGALKIPEQYRMTIWRGLQDLKQGHDYSTAQQLLRSSNAATISIGGSGELQRQRVMEAVHFRVRHTITIPNRGGPGGGPDEWADFGFDLPDCKARKQPIKEEFTEAEIH
| null |
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250};
|
cell cycle [GO:0007049]; DNA damage response [GO:0006974]; intrinsic apoptotic signaling pathway in response to DNA damage [GO:0008630]; intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator [GO:0042771]; kidney development [GO:0001822]; mismatch repair [GO:0006298]; negative regulation of cardiac muscle cell proliferation [GO:0060044]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of neuron differentiation [GO:0045665]; positive regulation of apoptotic process [GO:0043065]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of lung ciliated cell differentiation [GO:1901248]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of oligodendrocyte differentiation [GO:0048714]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein tetramerization [GO:0051262]; regulation of cell cycle [GO:0051726]; regulation of gene expression [GO:0010468]; regulation of mitotic cell cycle [GO:0007346]; regulation of transcription by RNA polymerase II [GO:0006357]; response to organonitrogen compound [GO:0010243]; response to xenobiotic stimulus [GO:0009410]
|
cell junction [GO:0030054]; chromatin [GO:0000785]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; intracellular membrane-bounded organelle [GO:0043231]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription factor binding [GO:0140297]; identical protein binding [GO:0042802]; MDM2/MDM4 family protein binding [GO:0097371]; metal ion binding [GO:0046872]; p53 binding [GO:0002039]; protein kinase binding [GO:0019901]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; transcription cis-regulatory region binding [GO:0000976]; transcription corepressor binding [GO:0001222]
|
PF00870;PF07710;PF07647;
|
2.60.40.720;4.10.170.10;1.10.150.50;
|
P53 family
|
PTM: Isoform alpha (but not isoform beta) is sumoylated on Lys-627, which potentiates proteasomal degradation but does not affect transcriptional activity. Phosphorylation by PLK1 and PLK3 inhibits the transcription regulator activity and pro-apoptotic function. {ECO:0000269|PubMed:10961991}.; PTM: Higher levels of phosphorylation seen in the brain from patients with Huntington disease.; PTM: Polyubiquitinated by RCHY1/PIRH2; leading to its degradation by the proteasome. {ECO:0000269|PubMed:19581926, ECO:0000269|PubMed:21994467}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24314664}. Cytoplasm. Note=Accumulates in the nucleus in response to DNA damage.
| null | null | null | null | null |
FUNCTION: Participates in the apoptotic response to DNA damage. Isoforms containing the transactivation domain are pro-apoptotic, isoforms lacking the domain are anti-apoptotic and block the function of p53 and transactivating p73 isoforms. May be a tumor suppressor protein. Is an activator of FOXJ1 expression (By similarity). It is an essential factor for the positive regulation of lung ciliated cell differentiation (PubMed:34077761). {ECO:0000250|UniProtKB:Q9JJP2, ECO:0000269|PubMed:10203277, ECO:0000269|PubMed:11753569, ECO:0000269|PubMed:18174154, ECO:0000269|PubMed:34077761}.
|
Homo sapiens (Human)
|
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