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
|
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
O75129
|
ASTN2_HUMAN
|
MAAAGARLSPGPGSGLRGRPRLCFHPGPPPLLPLLLLFLLLLPPPPLLAGATAAASREPDSPCRLKTVTVSTLPALRESDIGWSGARAGAGAGTGAGAAAAAASPGSPGSAGTAAESRLLLFVRNELPGRIAVQDDLDNTELPFFTLEMSGTAADISLVHWRQQWLENGTLYFHVSMSSSGQLAQATAPTLQEPSEIVEEQMHILHISVMGGLIALLLLLLVFTVALYAQRRWQKRRRIPQKSASTEATHEIHYIPSVLLGPQARESFRSSRLQTHNSVIGVPIRETPILDDYDCEEDEEPPRRANHVSREDEFGSQVTHTLDSLGHPGEEKVDFEKKAAAEATQETVESLMQKFKESFRANTPIEIGQLQPPLRSTSAGKRKRRSKSRGGISFGRAKGTSGSEADDETQLTFYTEQYRSRRRSKGLLKSPVNKTALTLIAVSSCILAMVCGSQMSCPLTVKVTLHVPEHFIADGSSFVVSEGSYLDISDWLNPAKLSLYYQINATSPWVRDLCGQRTTDACEQLCDPETGECSCHEGYAPDPVHRHLCVRSDWGQSEGPWPYTTLERGYDLVTGEQAPEKILRSTFSLGQGLWLPVSKSFVVPPVELSINPLASCKTDVLVTEDPADVREEAMLSTYFETINDLLSSFGPVRDCSRNNGGCTRNFKCVSDRQVDSSGCVCPEELKPMKDGSGCYDHSKGIDCSDGFNGGCEQLCLQQTLPLPYDATSSTIFMFCGCVEEYKLAPDGKSCLMLSDVCEGPKCLKPDSKFNDTLFGEMLHGYNNRTQHVNQGQVFQMTFRENNFIKDFPQLADGLLVIPLPVEEQCRGVLSEPLPDLQLLTGDIRYDEAMGYPMVQQWRVRSNLYRVKLSTITLAAGFTNVLKILTKESSREELLSFIQHYGSHYIAEALYGSELTCIIHFPSKKVQQQLWLQYQKETTELGSKKELKSMPFITYLSGLLTAQMLSDDQLISGVEIRCEEKGRCPSTCHLCRRPGKEQLSPTPVLLEINRVVPLYTLIQDNGTKEAFKSALMSSYWCSGKGDVIDDWCRCDLSAFDANGLPNCSPLLQPVLRLSPTVEPSSTVVSLEWVDVQPAIGTKVSDYILQHKKVDEYTDTDLYTGEFLSFADDLLSGLGTSCVAAGRSHGEVPEVSIYSVIFKCLEPDGLYKFTLYAVDTRGRHSELSTVTLRTACPLVDDNKAEEIADKIYNLYNGYTSGKEQQMAYNTLMEVSASMLFRVQHHYNSHYEKFGDFVWRSEDELGPRKAHLILRRLERVSSHCSSLLRSAYIQSRVETVPYLFCRSEEVRPAGMVWYSILKDTKITCEEKMVSMARNTYGESKGR
| null | null |
establishment of body hair planar orientation [GO:0048105]; negative regulation of protein localization to cell surface [GO:2000009]; neuron cell-cell adhesion [GO:0007158]; neuron migration [GO:0001764]; protein localization to cell surface [GO:0034394]; protein transport [GO:0015031]
|
cell cortex [GO:0005938]; cell pole [GO:0060187]; clathrin-coated vesicle [GO:0030136]; early endosome [GO:0005769]; endosome [GO:0005768]; late endosome [GO:0005770]; membrane [GO:0016020]; perikaryon [GO:0043204]
|
calcium ion binding [GO:0005509]; inositol 1,3,4,5 tetrakisphosphate binding [GO:0043533]
|
PF18411;PF19743;PF19441;PF18577;PF01823;
|
2.10.25.10;
|
Astrotactin family
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q80Z10}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q80Z10}. Perikaryon {ECO:0000250|UniProtKB:Q80Z10}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q80Z10}. Early endosome {ECO:0000250|UniProtKB:Q80Z10}. Late endosome {ECO:0000250|UniProtKB:Q80Z10}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:Q80Z10}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q80Z10}. Note=Integral membrane protein not detected at the cell membrane. Detected in cytoplasmic vesicles in the cell cortex, close to the anterior pole of migrating neurons. Detected at the base of the leading process in migrating neurons. {ECO:0000250|UniProtKB:Q80Z10}.
| null | null | null | null | null |
FUNCTION: Mediates recycling of the neuronal cell adhesion molecule ASTN1 to the anterior pole of the cell membrane in migrating neurons. Promotes ASTN1 internalization and intracellular transport of endocytosed ASTN1 (By similarity). Selectively binds inositol-4,5-bisphosphate, inositol-3,4,5-trisphosphate and inositol-1,3,4,5-tetrakisphosphate, suggesting it is recruited to membranes that contain lipids with a phosphoinositide headgroup (Ref.6). {ECO:0000250|UniProtKB:Q80Z10, ECO:0000269|Ref.6}.
|
Homo sapiens (Human)
|
O75131
|
CPNE3_HUMAN
|
MAAQCVTKVALNVSCANLLDKDIGSKSDPLCVLFLNTSGQQWYEVERTERIKNCLNPQFSKTFIIDYYFEVVQKLKFGVYDIDNKTIELSDDDFLGECECTLGQIVSSKKLTRPLVMKTGRPAGKGSITISAEEIKDNRVVLFEMEARKLDNKDLFGKSDPYLEFHKQTSDGNWLMVHRTEVVKNNLNPVWRPFKISLNSLCYGDMDKTIKVECYDYDNDGSHDLIGTFQTTMTKLKEASRSSPVEFECINEKKRQKKKSYKNSGVISVKQCEITVECTFLDYIMGGCQLNFTVGVDFTGSNGDPRSPDSLHYISPNGVNEYLTALWSVGLVIQDYDADKMFPAFGFGAQIPPQWQVSHEFPMNFNPSNPYCNGIQGIVEAYRSCLPQIKLYGPTNFSPIINHVARFAAAATQQQTASQYFVLLIITDGVITDLDETRQAIVNASRLPMSIIIVGVGGADFSAMEFLDGDGGSLRSPLGEVAIRDIVQFVPFRQFQNAPKEALAQCVLAEIPQQVVGYFNTYKLLPPKNPATKQQKQ
| null |
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
|
cellular response to calcium ion [GO:0071277]; cellular response to growth factor stimulus [GO:0071363]; ERBB2 signaling pathway [GO:0038128]; positive regulation of cell migration [GO:0030335]
|
azurophil granule membrane [GO:0035577]; cell junction [GO:0030054]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
calcium-dependent phospholipid binding [GO:0005544]; calcium-dependent protein binding [GO:0048306]; metal ion binding [GO:0046872]; protein serine/threonine kinase activity [GO:0004674]; receptor tyrosine kinase binding [GO:0030971]; RNA binding [GO:0003723]
|
PF00168;PF07002;
|
2.60.40.150;
|
Copine family
|
PTM: Phosphorylated on serine and threonine residues (PubMed:11041869). {ECO:0000269|PubMed:11041869}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20010870, ECO:0000269|PubMed:21087455}. Cytoplasm {ECO:0000269|PubMed:12949241, ECO:0000269|PubMed:20010870, ECO:0000269|PubMed:21087455}. Cell membrane {ECO:0000269|PubMed:20010870, ECO:0000269|PubMed:21087455}. Cell junction {ECO:0000269|PubMed:20010870}. Cell junction, focal adhesion {ECO:0000269|PubMed:20010870}. Note=Associates to the membrane in a calcium-dependent manner (PubMed:20010870). Translocates to the cell membrane and the nucleus in a calcium- or growth factor heregulin-dependent manner (PubMed:20010870, PubMed:21087455). Colocalizes with the tyrosine phosphorylated ERBB2 form at cell membrane and focal adhesions in a calcium- or growth factor heregulin-dependent manner (PubMed:20010870). {ECO:0000269|PubMed:20010870, ECO:0000269|PubMed:21087455}.
| null | null | null | null | null |
FUNCTION: Calcium-dependent phospholipid-binding protein that plays a role in ERBB2-mediated tumor cell migration in response to growth factor heregulin stimulation (PubMed:20010870). {ECO:0000269|PubMed:20010870}.
|
Homo sapiens (Human)
|
O75132
|
ZBED4_HUMAN
|
MENNLKTCPKEDGDFVSDKIKFKIEEEDDDGIPPDSLERMDFKSEQEDMKQTDSGGERAGLGGTGCSCKPPGKYLSAESEDDYGALFSQYSSTLYDVAMEAVTQSLLSSRNMSSRKKSPAWKHFFISPRDSTKAICMYCVKEFSRGKNEKDLSTSCLMRHVRRAHPTVLIQENGSVSAVSSFPSPSLLLPPQPADAGDLSTILSPIKLVQKVASKIPSPDRITEESVSVVSSEEISSDMSVSEKCGREEALVGSSPHLPALHYDEPAENLAEKSLPLPKSTSGSRRRSAVWKHFYLSPLDNSKAVCIHCMNEFSRGKNGKDLGTSCLIRHMWRAHRAIVLQENGGTGIPPLYSTPPTLLPSLLPPEGELSSVSSSPVKPVRESPSASSSPDRLTEDLQSHLNPGDGLMEDVAAFSSSDDIGEASASSPEKQQADGLSPRLFESGAIFQQNKKVMKRLKSEVWHHFSLAPMDSLKAECRYCGCAISRGKKGDVGTSCLMRHLYRRHPEVVGSQKGFLGASLANSPYATLASAESSSSKLTDLPTVVTKNNQVMFPVNSKKTSKLWNHFSICSADSTKVVCLHCGRTISRGKKPTNLGTSCLLRHLQRFHSNVLKTEVSETARPSSPDTRVPRGTELSGASSFDDTNEKFYDSHPVAKKITSLIAEMIALDLQPYSFVDNVGFNRLLEYLKPQYSLPAPSYFSRTAIPGMYDNVKQIIMSHLKEAESGVIHFTSGIWMSNQTREYLTLTAHWVSFESPARPRCDDHHCSALLDVSQVDCDYSGNSIQKQLECWWEAWVTSTGLQVGITVTDNASIGKTLNEGEHSSVQCFSHTVNLIVSEAIKSQRMVQNLLSLARKICERVHRSPKAKEKLAELQREYALPQHHLIQDVPSKWSTSFHMLERLIEQKRAINEMSVECNFRELISCDQWEVMQSVCRALKPFEAASREMSTQMSTLSQVIPMVHILNRKVEMLFEETMGIDTMLRSLKEAMVSRLSATLHDPRYVFATLLDPRYKASLFTEEEAEQYKQDLIRELELMNSTSEDVAASHRCDAGSPSKDSAAEENLWSLVAKVKKKDPREKLPEAMVLAYLEEEVLEHSCDPLTYWNLKKASWPGLSALAVRFLGCPPSIVPSEKLFNTPTENGSLGQSRLMMEHFEKLIFLKVNLPLIYFQY
| null | null |
positive regulation of transcription by RNA polymerase II [GO:0045944]
|
chromatin [GO:0000785]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; photoreceptor inner segment [GO:0001917]
|
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; protein dimerization activity [GO:0046983]; RNA binding [GO:0003723]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; transcription cis-regulatory region binding [GO:0000976]
|
PF05699;PF02892;
| null | null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17209048, ECO:0000269|PubMed:19369242, ECO:0000269|PubMed:22693546}. Cytoplasm {ECO:0000269|PubMed:17209048, ECO:0000269|PubMed:22693546}. Photoreceptor inner segment {ECO:0000269|PubMed:19369242}.
| null | null | null | null | null |
FUNCTION: Transcriptional regulator that binds to poly-guanine tracts in gene promoters and activates transcription (By similarity). Able to bind single- and double-stranded DNA and RNA (By similarity). {ECO:0000250|UniProtKB:Q80WQ9}.
|
Homo sapiens (Human)
|
O75140
|
DEPD5_HUMAN
|
MRTTKVYKLVIHKKGFGGSDDELVVNPKVFPHIKLGDIVEIAHPNDEYSPLLLQVKSLKEDLQKETISVDQTVTQVFRLRPYQDVYVNVVDPKDVTLDLVELTFKDQYIGRGDMWRLKKSLVSTCAYITQKVEFAGIRAQAGELWVKNEKVMCGYISEDTRVVFRSTSAMVYIFIQMSCEMWDFDIYGDLYFEKAVNGFLADLFTKWKEKNCSHEVTVVLFSRTFYDAKSVDEFPEINRASIRQDHKGRFYEDFYKVVVQNERREEWTSLLVTIKKLFIQYPVLVRLEQAEGFPQGDNSTSAQGNYLEAINLSFNVFDKHYINRNFDRTGQMSVVITPGVGVFEVDRLLMILTKQRMIDNGIGVDLVCMGEQPLHAVPLFKLHNRSAPRDSRLGDDYNIPHWINHSFYTSKSQLFCNSFTPRIKLAGKKPASEKAKNGRDTSLGSPKESENALPIQVDYDAYDAQVFRLPGPSRAQCLTTCRSVRERESHSRKSASSCDVSSSPSLPSRTLPTEEVRSQASDDSSLGKSANILMIPHPHLHQYEVSSSLGYTSTRDVLENMMEPPQRDSSAPGRFHVGSAESMLHVRPGGYTPQRALINPFAPSRMPMKLTSNRRRWMHTFPVGPSGEAIQIHHQTRQNMAELQGSGQRDPTHSSAELLELAYHEAAGRHSNSRQPGDGMSFLNFSGTEELSVGLLSNSGAGMNPRTQNKDSLEDSVSTSPDPILTLSAPPVVPGFCCTVGVDWKSLTTPACLPLTTDYFPDRQGLQNDYTEGCYDLLPEADIDRRDEDGVQMTAQQVFEEFICQRLMQGYQIIVQPKTQKPNPAVPPPLSSSPLYSRGLVSRNRPEEEDQYWLSMGRTFHKVTLKDKMITVTRYLPKYPYESAQIHYTYSLCPSHSDSEFVSCWVEFSHERLEEYKWNYLDQYICSAGSEDFSLIESLKFWRTRFLLLPACVTATKRITEGEAHCDIYGDRPRADEDEWQLLDGFVRFVEGLNRIRRRHRSDRMMRKGTAMKGLQMTGPISTHSLESTAPPVGKKGTSALSALLEMEASQKCLGEQQAAVHGGKSSAQSAESSSVAMTPTYMDSPRKDGAFFMEFVRSPRTASSAFYPQVSVDQTATPMLDGTSLGICTGQSMDRGNSQTFGNSQNIGEQGYSSTNSSDSSSQQLVASSLTSSSTLTEILEAMKHPSTGVQLLSEQKGLSPYCFISAEVVHWLVNHVEGIQTQAMAIDIMQKMLEEQLITHASGEAWRTFIYGFYFYKIVTDKEPDRVAMQQPATTWHTAGVDDFASFQRKWFEVAFVAEELVHSEIPAFLLPWLPSRPASYASRHSSFSRSFGGRSQAAALLAATVPEQRTVTLDVDVNNRTDRLEWCSCYYHGNFSLNAAFEIKLHWMAVTAAVLFEMVQGWHRKATSCGFLLVPVLEGPFALPSYLYGDPLRAQLFIPLNISCLLKEGSEHLFDSFEPETYWDRMHLFQEAIAHRFGFVQDKYSASAFNFPAENKPQYIHVTGTVFLQLPYSKRKFSGQQRRRRNSTSSTNQNMFCEERVGYNWAYNTMLTKTWRSSATGDEKFADRLLKDFTDFCINRDNRLVTFWTSCLEKMHASAP
| null | null |
cellular response to amino acid starvation [GO:0034198]; intracellular signal transduction [GO:0035556]; negative regulation of TOR signaling [GO:0032007]; negative regulation of TORC1 signaling [GO:1904262]; positive regulation of autophagy [GO:0010508]
|
cytosol [GO:0005829]; GATOR1 complex [GO:1990130]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; perinuclear region of cytoplasm [GO:0048471]
|
GTPase activator activity [GO:0005096]; protein-containing complex binding [GO:0044877]; small GTPase binding [GO:0031267]
|
PF00610;PF19418;PF12257;
|
1.10.10.10;
|
IML1 family
|
PTM: Phosphorylation at Ser-1002 and Ser-1530 by AKT1 and PIM1 inhibit the activity of DEPDC5, releasing inhibition of the mTORC1 pathway. {ECO:0000269|PubMed:31548394}.; PTM: Ubiquitinated (PubMed:29769719). Amino acid-induced 'Lys-48'-linked polyubiquitination of DEPDC5 by the BCR(KLHL22) ubiquitin ligase complex leads to DEPDC5 proteasomal degradation and inhibition of the GATOR1 complex (PubMed:29769719). Ubiquitination may occur at multiple lysines (PubMed:29769719). {ECO:0000269|PubMed:29769719}.
|
SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:28199306}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P61460}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P61460}. Note=Localization to lysosomes is mediated by the KICSTOR complex and is amino acid-independent. {ECO:0000269|PubMed:28199306}.
| null | null | null | null | null |
FUNCTION: As a component of the GATOR1 complex functions as an inhibitor of the amino acid-sensing branch of the mTORC1 pathway (PubMed:23723238, PubMed:25457612, PubMed:29590090, PubMed:29769719, PubMed:31548394, PubMed:35338845). In response to amino acid depletion, the GATOR1 complex has GTPase activating protein (GAP) activity and strongly increases GTP hydrolysis by RagA/RRAGA (or RagB/RRAGB) within heterodimeric Rag complexes, thereby turning them into their inactive GDP-bound form, releasing mTORC1 from lysosomal surface and inhibiting mTORC1 signaling (PubMed:23723238, PubMed:25457612, PubMed:29590090, PubMed:29769719, PubMed:35338845). In the presence of abundant amino acids, the GATOR1 complex is negatively regulated by GATOR2, the other GATOR subcomplex, in this amino acid-sensing branch of the TORC1 pathway (PubMed:23723238, PubMed:25457612, PubMed:29769719). Within the GATOR1 complex, DEPDC5 mediates direct interaction with the nucleotide-binding pocket of small GTPases Rag (RagA/RRAGA, RagB/RRAGB, RagC/RRAGC and/or RagD/RRAGD) and coordinates their nucleotide loading states by promoting RagA/RRAGA or RagB/RRAGB into their GDP-binding state and RagC/RRAGC or RagD/RRAGD into their GTP-binding state (PubMed:29590090, PubMed:35338845). However, it does not execute the GAP activity, which is mediated by NPRL2 (PubMed:29590090). {ECO:0000269|PubMed:23723238, ECO:0000269|PubMed:25457612, ECO:0000269|PubMed:29590090, ECO:0000269|PubMed:29769719, ECO:0000269|PubMed:31548394, ECO:0000269|PubMed:35338845}.
|
Homo sapiens (Human)
|
O75143
|
ATG13_HUMAN
|
METDLNSQDRKDLDKFIKFFALKTVQVIVQARLGEKICTRSSSSPTGSDWFNLAIKDIPEVTHEAKKALAGQLPAVGRSMCVEISLKTSEGDSMELEIWCLEMNEKCDKEIKVSYTVYNRLSLLLKSLLAITRVTPAYRLSRKQGHEYVILYRIYFGEVQLSGLGEGFQTVRVGTVGTPVGTITLSCAYRINLAFMSTRQFERTPPIMGIIIDHFVDRPYPSSSPMHPCNYRTAGEDTGVIYPSVEDSQEVCTTSFSTSPPSQLSSSRLSYQPAALGVGSADLAYPVVFAAGLNATHPHQLMVPGKEGGVPLAPNQPVHGTQADQERLATCTPSDRTHCAATPSSSEDTETVSNSSEGRASPHDVLETIFVRKVGAFVNKPINQVTLTSLDIPFAMFAPKNLELEDTDPMVNPPDSPETESPLQGSLHSDGSSGGSSGNTHDDFVMIDFKPAFSKDDILPMDLGTFYREFQNPPQLSSLSIDIGAQSMAEDLDSLPEKLAVHEKNVREFDAFVETLQ
| null | null |
autophagosome assembly [GO:0000045]; mitophagy [GO:0000423]; negative regulation of cell population proliferation [GO:0008285]; piecemeal microautophagy of the nucleus [GO:0034727]; positive regulation of autophagy [GO:0010508]; positive regulation of protein targeting to mitochondrion [GO:1903955]; protein localization to phagophore assembly site [GO:0034497]; regulation of protein lipidation [GO:1903059]; response to mitochondrial depolarisation [GO:0098780]
|
Atg1/ULK1 kinase complex [GO:1990316]; autophagosome [GO:0005776]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; mitochondrion [GO:0005739]; phagophore assembly site [GO:0000407]; phagophore assembly site membrane [GO:0034045]
|
protein kinase binding [GO:0019901]; protein kinase regulator activity [GO:0019887]; protein serine/threonine kinase activator activity [GO:0043539]
|
PF10033;
|
3.30.900.10;
|
ATG13 family, Metazoan subfamily
|
PTM: Phosphorylated by ULK1, ULK2 and mTOR. Phosphorylation status depends on nutrient-rich conditions; dephosphorylated during starvation or following treatment with rapamycin. ULK1-mediated phosphorylation of ATG13 at Ser-355 is required for efficient clearance of depolarized mitochondria. {ECO:0000269|PubMed:18936157, ECO:0000269|PubMed:19211835, ECO:0000269|PubMed:19225151, ECO:0000269|PubMed:19287211, ECO:0000269|PubMed:21258367, ECO:0000269|PubMed:21855797}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:19211835}. Preautophagosomal structure {ECO:0000269|PubMed:19211835}. Note=Under starvation conditions, is localized to puncate structures primarily representing the isolation membrane; the isolation membrane sequesters a portion of the cytoplasm resulting in autophagosome formation. {ECO:0000269|PubMed:19211835}.
| null | null | null | null | null |
FUNCTION: Autophagy factor required for autophagosome formation and mitophagy. Target of the TOR kinase signaling pathway that regulates autophagy through the control of the phosphorylation status of ATG13 and ULK1, and the regulation of the ATG13-ULK1-RB1CC1 complex. Through its regulation of ULK1 activity, plays a role in the regulation of the kinase activity of mTORC1 and cell proliferation. {ECO:0000269|PubMed:18936157, ECO:0000269|PubMed:19211835, ECO:0000269|PubMed:19225151, ECO:0000269|PubMed:19287211, ECO:0000269|PubMed:21795849, ECO:0000269|PubMed:21855797}.
|
Homo sapiens (Human)
|
O75144
|
ICOSL_HUMAN
|
MRLGSPGLLFLLFSSLRADTQEKEVRAMVGSDVELSCACPEGSRFDLNDVYVYWQTSESKTVVTYHIPQNSSLENVDSRYRNRALMSPAGMLRGDFSLRLFNVTPQDEQKFHCLVLSQSLGFQEVLSVEVTLHVAANFSVPVVSAPHSPSQDELTFTCTSINGYPRPNVYWINKTDNSLLDQALQNDTVFLNMRGLYDVVSVLRIARTPSVNIGCCIENVLLQQNLTVGSQTGNDIGERDKITENPVSTGEKNAATWSILAVLCLLVVVAVAIGWVCRDRCLQHSYAGAWAVSPETELTGHV
| null | null |
adaptive immune response [GO:0002250]; B cell activation [GO:0042113]; defense response [GO:0006952]; hyperosmotic response [GO:0006972]; positive regulation of activated T cell proliferation [GO:0042104]; regulation of cytokine production [GO:0001817]; signal transduction [GO:0007165]; T cell activation [GO:0042110]; T cell receptor signaling pathway [GO:0050852]
|
external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; plasma membrane [GO:0005886]
|
identical protein binding [GO:0042802]; signaling receptor binding [GO:0005102]
|
PF07686;
|
2.60.40.10;
|
Immunoglobulin superfamily, BTN/MOG family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11007762}; Single-pass type I membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Ligand for the T-cell-specific cell surface receptor ICOS. Acts as a costimulatory signal for T-cell proliferation and cytokine secretion; induces also B-cell proliferation and differentiation into plasma cells. Could play an important role in mediating local tissue responses to inflammatory conditions, as well as in modulating the secondary immune response by co-stimulating memory T-cell function (By similarity). {ECO:0000250}.
|
Homo sapiens (Human)
|
O75145
|
LIPA3_HUMAN
|
MMCEVMPTISEDGRRGSALGPDEAGGELERLMVTMLTERERLLETLREAQDGLATAQLRLRELGHEKDSLQRQLSIALPQEFAALTKELNLCREQLLEREEEIAELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPGGVSSEVEVLKALKSLFEHHKALDEKVRERLRMALERVAVLEEELELSNQETLNLREQLSRRRSGLEEPGKDGDGQTLANGLGPGGDSNRRTAELEEALERQRAEVCQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYLSAQREATSLHDANDKLENELASKESLYRQSEEKSRQLAEWLDDAKQKLQQTLQKAETLPEIEAQLAQRVAALNKAEERHGNFEERLRQLEAQLEEKNQELQRARQREKMNDDHNKRLSETVDKLLSESNERLQLHLKERMGALEEKNSLSEEIANMKKLQDELLLNKEQLLAEMERMQMEIDQLRGRPPSSYSRSLPGSALELRYSQAPTLPSGAHLDPYVAGSGRAGKRGRWSGVKEEPSKDWERSAPAGSIPPPFPGELDGSDEEEAEGMFGAELLSPSGQADVQTLAIMLQEQLEAINKEIKLIQEEKETTEQRAEELESRVSSSGLDSLGRYRSSCSLPPSLTTSTLASPSPPSSGHSTPRLAPPSPAREGTDKANHVPKEEAGAPRGEGPAIPGDTPPPTPRSARLERMTQALALQAGSLEDGGPPRGSEGTPDSLHKAPKKKSIKSSIGRLFGKKEKGRMGPPGRDSSSLAGTPSDETLATDPLGLAKLTGPGDKDRRNKRKHELLEEACRQGLPFAAWDGPTVVSWLELWVGMPAWYVAACRANVKSGAIMANLSDTEIQREIGISNPLHRLKLRLAIQEMVSLTSPSAPASSRTSTGNVWMTHEEMESLTATTKPETKEISWEQILAYGDMNHEWVGNDWLPSLGLPQYRSYFMESLVDARMLDHLNKKELRGQLKMVDSFHRVSLHYGIMCLKRLNYDRKDLERRREESQTQIRDVMVWSNERVMGWVSGLGLKEFATNLTESGVHGALLALDETFDYSDLALLLQIPTQNAQARQLLEKEFSNLISLGTDRRLDEDSAKSFSRSPSWRKMFREKDLRGVTPDSAEMLPPNFRSAAAGALGSPGLPLRKLQPEGQTSGSSRADGVSVRTYSC
| null | null |
neurotransmitter secretion [GO:0007269]; regulation of short-term neuronal synaptic plasticity [GO:0048172]; synapse organization [GO:0050808]; synaptic vesicle docking [GO:0016081]
|
acrosomal vesicle [GO:0001669]; cytosol [GO:0005829]; epididymosome [GO:0098875]; glutamatergic synapse [GO:0098978]; presynaptic active zone [GO:0048786]; presynaptic active zone cytoplasmic component [GO:0098831]
| null |
PF00536;PF07647;
|
1.10.287.1490;1.10.150.50;
|
Liprin family, Liprin-alpha subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q91Z79}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:23124857}. Note=Also detected in epididymosome. {ECO:0000250|UniProtKB:Q91Z79}.
| null | null | null | null | null |
FUNCTION: May regulate the disassembly of focal adhesions. May localize receptor-like tyrosine phosphatases type 2A at specific sites on the plasma membrane, possibly regulating their interaction with the extracellular environment and their association with substrates. {ECO:0000269|PubMed:9624153}.
|
Homo sapiens (Human)
|
O75146
|
HIP1R_HUMAN
|
MNSIKNVPARVLSRRPGHSLEAEREQFDKTQAISISKAINTQEAPVKEKHARRIILGTHHEKGAFTFWSYAIGLPLPSSSILSWKFCHVLHKVLRDGHPNVLHDCQRYRSNIREIGDLWGHLHDRYGQLVNVYTKLLLTKISFHLKHPQFPAGLEVTDEVLEKAAGTDVNNIFQLTVEMFDYMDCELKLSESVFRQLNTAIAVSQMSSGQCRLAPLIQVIQDCSHLYHYTVKLLFKLHSCLPADTLQGHRDRFHEQFHSLRNFFRRASDMLYFKRLIQIPRLPEGPPNFLRASALAEHIKPVVVIPEEAPEDEEPENLIEISTGPPAGEPVVVADLFDQTFGPPNGSVKDDRDLQIESLKREVEMLRSELEKIKLEAQRYIAQLKSQVNALEGELEEQRKQKQKALVDNEQLRHELAQLRAAQLEGERSQGLREEAERKASATEARYNKLKEKHSELVHVHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQVEQVKRESELKLEEKSDQLEKLKRELEAKAGELARAQEALSHTEQSKSELSSRLDTLSAEKDALSGAVRQREADLLAAQSLVRETEAALSREQQRSSQEQGELQGRLAERESQEQGLRQRLLDEQFAVLRGAAAEAAGILQDAVSKLDDPLHLRCTSSPDYLVSRAQEALDAVSTLEEGHAQYLTSLADASALVAALTRFSHLAADTIINGGATSHLAPTDPADRLIDTCRECGARALELMGQLQDQQALRHMQASLVRTPLQGILQLGQELKPKSLDVRQEELGAVVDKEMAATSAAIEDAVRRIEDMMNQARHASSGVKLEVNERILNSCTDLMKAIRLLVTTSTSLQKEIVESGRGAATQQEFYAKNSRWTEGLISASKAVGWGATQLVEAADKVVLHTGKYEELIVCSHEIAASTAQLVAASKVKANKHSPHLSRLQECSRTVNERAANVVASTKSGQEQIEDRDTMDFSGLSLIKLKKQEMETQVRVLELEKTLEAERMRLGELRKQHYVLAGASGSPGEEVAIRPSTAPRSVTTKKPPLAQKPSVAPRQDHQLDKKDGIYPAQLVNY
| null | null |
actin filament organization [GO:0007015]; activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; clathrin coat assembly [GO:0048268]; digestive system development [GO:0055123]; endocytosis [GO:0006897]; negative regulation of actin filament polymerization [GO:0030837]; negative regulation of apoptotic process [GO:0043066]; negative regulation of Arp2/3 complex-mediated actin nucleation [GO:0034316]; positive regulation of apoptotic process [GO:0043065]; positive regulation of clathrin coat assembly [GO:1905445]; positive regulation of epidermal growth factor receptor signaling pathway [GO:0045742]; positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway [GO:1901030]; positive regulation of platelet-derived growth factor receptor-beta signaling pathway [GO:2000588]; positive regulation of protein binding [GO:0032092]; postsynapse organization [GO:0099173]; protein stabilization [GO:0050821]; receptor-mediated endocytosis [GO:0006898]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of clathrin-dependent endocytosis [GO:2000369]; regulation of endocytosis [GO:0030100]; regulation of gastric acid secretion [GO:0060453]
|
apical plasma membrane [GO:0016324]; cell cortex [GO:0005938]; clathrin-coated pit [GO:0005905]; clathrin-coated vesicle [GO:0030136]; clathrin-coated vesicle membrane [GO:0030665]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; dendrite cytoplasm [GO:0032839]; dendritic spine [GO:0043197]; glutamatergic synapse [GO:0098978]; intracellular membrane-bounded organelle [GO:0043231]; mitochondrion [GO:0005739]; neuronal cell body [GO:0043025]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; ruffle membrane [GO:0032587]; synaptic membrane [GO:0097060]
|
actin filament binding [GO:0051015]; clathrin adaptor activity [GO:0035615]; clathrin binding [GO:0030276]; clathrin light chain binding [GO:0032051]; identical protein binding [GO:0042802]; phosphatidylinositol binding [GO:0035091]; phosphatidylinositol-3,4,5-trisphosphate binding [GO:0005547]; phosphatidylinositol-3,4-bisphosphate binding [GO:0043325]; phosphatidylinositol-3,5-bisphosphate binding [GO:0080025]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; SH3 domain binding [GO:0017124]
|
PF07651;PF16515;PF01608;
|
1.20.5.1700;1.25.40.90;6.10.250.920;1.20.1410.10;
|
SLA2 family
| null |
SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Endomembrane system. Cytoplasmic vesicle, clathrin-coated vesicle membrane. Note=Membrane-associated protein, mainly localized at the endocytic compartments and in the perinuclear region.
| null | null | null | null | null |
FUNCTION: Component of clathrin-coated pits and vesicles, that may link the endocytic machinery to the actin cytoskeleton. Binds 3-phosphoinositides (via ENTH domain). May act through the ENTH domain to promote cell survival by stabilizing receptor tyrosine kinases following ligand-induced endocytosis. {ECO:0000269|PubMed:11889126, ECO:0000269|PubMed:14732715}.
|
Homo sapiens (Human)
|
O75147
|
OBSL1_HUMAN
|
MKASSGDQGSPPCFLRFPRPVRVVSGAEAELKCVVLGEPPPVVVWEKGGQQLAASERLSFPADGAEHGLLLTAALPTDAGVYVCRARNAAGEAYAAAAVTVLEPPASDPELQPAERPLPSPGSGEGAPVFLTGPRSQWVLRGAEVVLTCRAGGLPEPTLYWEKDGMALDEVWDSSHFALQPGRAEDGPGASLALRILAARLPDSGVYVCHARNAHGHAQAGALLQVHQPPESPPADPDEAPAPVVEPLKCAPKTFWVNEGKHAKFRCYVMGKPEPEIEWHWEGRPLLPDRRRLMYRDRDGGFVLKVLYCQAKDRGLYVCAARNSAGQTLSAVQLHVKEPRLRFTRPLQDVEGREHGIAVLECKVPNSRIPTAWFREDQRLLPCRKYEQIEEGTVRRLIIHRLKADDDGIYLCEMRGRVRTVANVTVKGPILKRLPRKLDVLEGENAVLLVETLEAGVEGRWSRDGEELPVICQSSSGHMHALVLPGVTREDAGEVTFSLGNSRTTTLLRVKCVKHSPPGPPILAEMFKGHKNTVLLTWKPPEPAPETPFIYRLERQEVGSEDWIQCFSIEKAGAVEVPGDCVPSEGDYRFRICTVSGHGRSPHVVFHGSAHLVPTARLVAGLEDVQVYDGEDAVFSLDLSTIIQGTWFLNGEELKSNEPEGQVEPGALRYRIEQKGLQHRLILHAVKHQDSGALVGFSCPGVQDSAALTIQESPVHILSPQDRVSLTFTTSERVVLTCELSRVDFPATWYKDGQKVEESELLVVKMDGRKHRLILPEAKVQDSGEFECRTEGVSAFFGVTVQDPPVHIVDPREHVFVHAITSECVMLACEVDREDAPVRWYKDGQEVEESDFVVLENEGPHRRLVLPATQPSDGGEFQCVAGDECAYFTVTITDVSSWIVYPSGKVYVAAVRLERVVLTCELCRPWAEVRWTKDGEEVVESPALLLQKEDTVRRLVLPAVQLEDSGEYLCEIDDESASFTVTVTEPPVRIIYPRDEVTLIAVTLECVVLMCELSREDAPVRWYKDGLEVEESEALVLERDGPRCRLVLPAAQPEDGGEFVCDAGDDSAFFTVTVTAPPERIVHPAARSLDLHFGAPGRVELRCEVAPAGSQVRWYKDGLEVEASDALQLGAEGPTRTLTLPHAQPEDAGEYVCETRHEAITFNVILAEPPVQFLALETTPSPLCVAPGEPVVLSCELSRAGAPVVWSHNGRPVQEGEGLELHAEGPRRVLCIQAAGPAHAGLYTCQSGAAPGAPSLSFTVQVAEPPVRVVAPEAAQTRVRSTPGGDLELVVHLSGPGGPVRWYKDGERLASQGRVQLEQAGARQVLRVQGARSGDAGEYLCDAPQDSRIFLVSVEEPLLVKLVSELTPLTVHEGDDATFRCEVSPPDADVTWLRNGAVVTPGPQVEMAQNGSSRILTLRGCQLGDAGTVTLRAGSTATSARLHVRETELLFLRRLQDVRAEEGQDVCLEVETGRVGAAGAVRWVRGGQPLPHDSRLSMAQDGHIHRLFIHGVILADQGTYGCESHHDRTLARLSVRPRQLRVLRPLEDVTISEGGSATFQLELSQEGVTGEWARGGVQLYPGPKCHIHSDGHRHRLVLNGLGLADSGCVSFTADSLRCAARLIVREVPVTIVRGPHDLEVTEGDTATFECELSQALADVTWEKDGNALTPSPRLRLQALGTRRLLQLRRCGPSDAGTYSCAVGTARAGPVRLTVRERTVAVLSELRSVSAREGDGATFECTVSEVETTGRWELGGRPLRPGARVRIRQEGKKHILVLSELRAEDAGEVRFQAGPAQSLALLEVEALPLQMCRHPPREKTVLVGRRAVLEVTVSRSGGHVCWLREGAELCPGDKYEMRSHGPTHSLVIHDVRPEDQGTYCCQAGQDSTHTRLLVEGN
| null | null |
cardiac myofibril assembly [GO:0055003]; cytoskeleton organization [GO:0007010]; Golgi organization [GO:0007030]; microtubule cytoskeleton organization [GO:0000226]; positive regulation of dendrite morphogenesis [GO:0050775]; protein localization to Golgi apparatus [GO:0034067]; regulation of mitotic nuclear division [GO:0007088]
|
3M complex [GO:1990393]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; intercalated disc [GO:0014704]; M band [GO:0031430]; perinuclear region of cytoplasm [GO:0048471]; Z disc [GO:0030018]
|
cytoskeletal anchor activity [GO:0008093]
|
PF07679;PF13927;
|
2.60.40.10;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24793695}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:24793695}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:24793695}. Golgi apparatus {ECO:0000269|PubMed:21572988}. Note=Colocalizes with CUL7 at the Golgi apparatus in neurons (PubMed:21572988).
| null | null | null | null | null |
FUNCTION: Core component of the 3M complex, a complex required to regulate microtubule dynamics and genome integrity. It is unclear how the 3M complex regulates microtubules, it could act by controlling the level of a microtubule stabilizer (PubMed:24793695, PubMed:24793696). Acts as a regulator of the Cul7-RING(FBXW8) ubiquitin-protein ligase, playing a critical role in the ubiquitin ligase pathway that regulates Golgi morphogenesis and dendrite patterning in brain. Required to localize CUL7 to the Golgi apparatus in neurons. {ECO:0000269|PubMed:21572988, ECO:0000269|PubMed:24793695, ECO:0000269|PubMed:24793696}.
|
Homo sapiens (Human)
|
O75150
|
BRE1B_HUMAN
|
MSGPGNKRAAGDGGSGPPEKKLSREEKTTTTLIEPIRLGGISSTEEMDLKVLQFKNKKLAERLEQRQACEDELRERIEKLEKRQATDDATLLIVNRYWAQLDETVEALLRCHESQGELSSAPEAPGTQEGPTCDGTPLPEPGTSELRDPLLMQLRPPLSEPALAFVVALGASSSEEVELELQGRMEFSKAAVSRVVEASDRLQRRVEELCQRVYSRGDSEPLSEAAQAHTRELGRENRRLQDLATQLQEKHHRISLEYSELQDKVTSAETKVLEMETTVEDLQWDIEKLRKREQKLNKHLAEALEQLNSGYYVSGSSSGFQGGQITLSMQKFEMLNAELEENQELANSRMAELEKLQAELQGAVRTNERLKVALRSLPEEVVRETGEYRMLQAQFSLLYNESLQVKTQLDEARGLLLATKNSHLRHIEHMESDELGLQKKLRTEVIQLEDTLAQVRKEYEMLRIEFEQNLAANEQAGPINREMRHLISSLQNHNHQLKGDAQRYKRKLREVQAEIGKLRAQASGSAHSTPNLGHPEDSGVSAPAPGKEEGGPGPVSTPDNRKEMAPVPGTTTTTTSVKKEELVPSEEDFQGITPGAQGPSSRGREPEARPKRELREREGPSLGPPPVASALSRADREKAKVEETKRKESELLKGLRAELKKAQESQKEMKLLLDMYKSAPKEQRDKVQLMAAERKAKAEVDELRSRIRELEERDRRESKKIADEDALRRIRQAEEQIEHLQRKLGATKQEEEALLSEMDVTGQAFEDMQEQNGRLLQQLREKDDANFKLMSERIKANQIHKLLREEKDELGEQVLGLKSQVDAQLLTVQKLEEKERALQGSLGGVEKELTLRSQALELNKRKAVEAAQLAEDLKVQLEHVQTRLREIQPCLAESRAAREKESFNLKRAQEDISRLRRKLEKQRKVEVYADADEILQEEIKEYKARLTCPCCNTRKKDAVLTKCFHVFCFECVRGRYEARQRKCPKCNAAFGAHDFHRIYIS
|
2.3.2.27
| null |
chromatin organization [GO:0006325]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein ubiquitination [GO:0016567]; ubiquitin-dependent protein catabolic process [GO:0006511]
|
HULC complex [GO:0033503]; membrane [GO:0016020]; neuron projection [GO:0043005]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ubiquitin ligase complex [GO:0000151]
|
metal ion binding [GO:0046872]; mRNA 3'-UTR binding [GO:0003730]; protein homodimerization activity [GO:0042803]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin protein ligase binding [GO:0031625]
|
PF00097;
|
3.30.40.10;
|
BRE1 family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10944455}.
|
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:16307923, ECO:0000269|PubMed:19410543};
| null |
PATHWAY: Protein modification; protein ubiquitination.
| null | null |
FUNCTION: Component of the RNF20/40 E3 ubiquitin-protein ligase complex that mediates monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1). H2BK120ub1 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation (H3K4me and H3K79me, respectively). It thereby plays a central role in histone code and gene regulation. The RNF20/40 complex forms a H2B ubiquitin ligase complex in cooperation with the E2 enzyme UBE2A or UBE2B; reports about the cooperation with UBE2E1/UBCH are contradictory. Required for transcriptional activation of Hox genes. {ECO:0000269|PubMed:16307923, ECO:0000269|PubMed:19410543}.; FUNCTION: (Microbial infection) Promotes the human herpesvirus 8 (KSHV) lytic cycle by inducing the expression of lytic viral genes including the latency switch gene RTA/ORF50. {ECO:0000269|PubMed:37888983}.
|
Homo sapiens (Human)
|
O75151
|
PHF2_HUMAN
|
MATVPVYCVCRLPYDVTRFMIECDACKDWFHGSCVGVEEEEAPDIDIYHCPNCEKTHGKSTLKKKRTWHKHGPGQAPDVKPVQNGSQLFIKELRSRTFPSAEDVVARVPGSQLTLGYMEEHGFTEPILVPKKDGLGLAVPAPTFYVSDVENYVGPERSVDVTDVTKQKDCKMKLKEFVDYYYSTNRKRVLNVTNLEFSDTRMSSFVEPPDIVKKLSWVENYWPDDALLAKPKVTKYCLICVKDSYTDFHIDSGGASAWYHVLKGEKTFYLIRPASANISLYERWRSASNHSEMFFADQVDKCYKCIVKQGQTLFIPSGWIYATLTPVDCLAFAGHFLHSLSVEMQMRAYEVERRLKLGSLTQFPNFETACWYMGKHLLEAFKGSHKSGKQLPPHLVQGAKILNGAFRSWTKKQALAEHEDELPEHFKPSQLIKDLAKEIRLSENASKAVRPEVNTVASSDEVCDGDREKEEPPSPIEATPPQSLLEKVSKKKTPKTVKMPKPSKIPKPPKPPKPPRPPKTLKLKDGGKKKGKKSRESASPTIPNLDLLEAHTKEALTKMEPPKKGKATKSVLSVPNKDVVHMQNDVERLEIREQTKSKSEAKWKYKNSKPDSLLKMEEEQKLEKSPLAGNKDNKFSFSFSNKKLLGSKALRPPTSPGVFGALQNFKEDKPKPVRDEYEYVSDDGELKIDEFPIRRKKNAPKRDLSFLLDKKAVLPTPVTKPKLDSAAYKSDDSSDEGSLHIDTDTKPGRNARVKKESGSSAAGILDLLQASEEVGALEYNPSSQPPASPSTQEAIQGMLSMANLQASDSCLQTTWGAGQAKGSSLAAHGARKNGGGSGKSAGKRLLKRAAKNSVDLDDYEEEQDHLDACFKDSDYVYPSLESDEDNPIFKSRSKKRKGSDDAPYSPTARVGPSVPRQDRPVREGTRVASIETGLAAAAAKLSQQEEQKSKKKKSAKRKLTPNTTSPSTSTSISAGTTSTSTTPASTTPASTTPASTSTASSQASQEGSSPEPPPESHSSSLADHEYTAAGTFTGAQAGRTSQPMAPGVFLTQRRPSASSPNNNTAAKGKRTKKGMATAKQRLGKILKIHRNGKLLL
|
1.14.11.-
| null |
liver development [GO:0001889]; negative regulation of rDNA heterochromatin formation [GO:0061188]; protein demethylation [GO:0006482]; regulation of transcription by RNA polymerase II [GO:0006357]; transcription initiation-coupled chromatin remodeling [GO:0045815]
|
kinetochore [GO:0000776]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
histone H3K9 demethylase activity [GO:0032454]; histone H4K20 demethylase activity [GO:0035575]; iron ion binding [GO:0005506]; methylated histone binding [GO:0035064]; transcription coactivator activity [GO:0003713]; transcription coregulator activity [GO:0003712]; zinc ion binding [GO:0008270]
|
PF17811;PF02373;PF00628;
|
1.20.58.1360;2.60.120.650;3.30.40.10;
|
JHDM1 histone demethylase family, JHDM1D subfamily
|
PTM: Phosphorylated by PKA on specific serine residues, leading to the formation of an active lysine demethylase complex. {ECO:0000269|PubMed:21532585}.
|
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:20129925}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:20813266}.
|
CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + N(6),N(6)-dimethyl-L-lysyl(9)-[histone H3] + O2 = CO2 + formaldehyde + N(6)-methyl-L-lysyl(9)-[histone H3] + succinate; Xref=Rhea:RHEA:60192, Rhea:RHEA-COMP:15541, Rhea:RHEA-COMP:15542, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:61929, ChEBI:CHEBI:61976; Evidence={ECO:0000269|PubMed:21532585}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60193; Evidence={ECO:0000269|PubMed:21532585};
| null | null | null | null |
FUNCTION: Lysine demethylase that demethylates both histones and non-histone proteins (PubMed:20129925, PubMed:21167174, PubMed:21532585). Enzymatically inactive by itself, and becomes active following phosphorylation by PKA: forms a complex with ARID5B and mediates demethylation of methylated ARID5B (PubMed:21532585). Demethylation of ARID5B leads to target the PHF2-ARID5B complex to target promoters, where PHF2 mediates demethylation of dimethylated 'Lys-9' of histone H3 (H3K9me2), followed by transcription activation of target genes (PubMed:21532585). The PHF2-ARID5B complex acts as a coactivator of HNF4A in liver. PHF2 is recruited to trimethylated 'Lys-4' of histone H3 (H3K4me3) at rDNA promoters and promotes expression of rDNA (PubMed:21532585). Involved in the activation of toll-like receptor 4 (TLR4)-target inflammatory genes in macrophages by catalyzing the demethylation of trimethylated histone H4 lysine 20 (H4K20me3) at the gene promoters (By similarity). {ECO:0000250|UniProtKB:Q9WTU0, ECO:0000269|PubMed:20129925, ECO:0000269|PubMed:21167174, ECO:0000269|PubMed:21532585}.
|
Homo sapiens (Human)
|
O75152
|
ZC11A_HUMAN
|
MPNQGEDCYFFFYSTCTKGDSCPFRHCEAAIGNETVCTLWQEGRCFRQVCRFRHMEIDKKRSEIPCYWENQPTGCQKLNCAFHHNRGRYVDGLFLPPSKTVLPTVPESPEEEVKASQLSVQQNKLSVQSNPSPQLRSVMKVESSENVPSPTHPPVVINAADDDEDDDDQFSEEGDETKTPTLQPTPEVHNGLRVTSVRKPAVNIKQGECLNFGIKTLEEIKSKKMKEKSKKQGEGSSGVSSLLLHPEPVPGPEKENVRTVVRTVTLSTKQGEEPLVRLSLTERLGKRKFSAGGDSDPPLKRSLAQRLGKKVEAPETNIDKTPKKAQVSKSLKERLGMSADPDNEDATDKVNKVGEIHVKTLEEILLERASQKRGELQTKLKTEGPSKTDDSTSGARSSSTIRIKTFSEVLAEKKHRQQEAERQKSKKDTTCIKLKIDSEIKKTVVLPPIVASRGQSEEPAGKTKSMQEVHIKTLEEIKLEKALRVQQSSESSTSSPSQHEATPGARRLLRITKRTGMKEEKNLQEGNEVDSQSSIRTEAKEASGETTGVDITKIQVKRCETMREKHMQKQQEREKSVLTPLRGDVASCNTQVAEKPVLTAVPGITRHLTKRLPTKSSQKVEVETSGIGDSLLNVKCAAQTLEKRGKAKPKVNVKPSVVKVVSSPKLAPKRKAVEMHAAVIAAVKPLSSSSVLQEPPAKKAAVAVVPLVSEDKSVTVPEAENPRDSLVLPPTQSSSDSSPPEVSGPSSSQMSMKTRRLSSASTGKPPLSVEDDFEKLIWEISGGKLEAEIDLDPGKDEDDLLLELSEMIDS
| null | null |
poly(A)+ mRNA export from nucleus [GO:0016973]
|
nucleoplasm [GO:0005654]
|
metal ion binding [GO:0046872]; RNA binding [GO:0003723]
|
PF15663;
|
3.30.1370.210;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:29610341}.
| null | null | null | null | null |
FUNCTION: RNA-binding protein that interacts with purine-rich sequences and is involved in nuclear mRNA export; probably mediated by association with the TREX complex. {ECO:0000269|PubMed:22928037, ECO:0000269|PubMed:29610341}.; FUNCTION: (Microbial infection) Plays a role in efficient growth of several nuclear-replicating viruses such as HIV-1, influenza virus or herpes simplex virus 1/HHV-1. Required for efficient viral mRNA Export. {ECO:0000269|PubMed:29610341}.
|
Homo sapiens (Human)
|
O75154
|
RFIP3_HUMAN
|
MASAPPASPPGSEPPGPDPEPGGPDGPGAAQLAPGPAELRLGAPVGGPDPQSPGLDEPAPGAAADGGARWSAGPAPGLEGGPRDPGPSAPPPRSGPRGQLASPDAPGPGPRSEAPLPELDPLFSWTEEPEECGPASCPESAPFRLQGSSSSHRARGEVDVFSPFPAPTAGELALEQGPGSPPQPSDLSQTHPLPSEPVGSQEDGPRLRAVFDALDGDGDGFVRIEDFIQFATVYGAEQVKDLTKYLDPSGLGVISFEDFYQGITAIRNGDPDGQCYGGVASAQDEEPLACPDEFDDFVTYEANEVTDSAYMGSESTYSECETFTDEDTSTLVHPELQPEGDADSAGGSAVPSECLDAMEEPDHGALLLLPGRPHPHGQSVITVIGGEEHFEDYGEGSEAELSPETLCNGQLGCSDPAFLTPSPTKRLSSKKVARYLHQSGALTMEALEDPSPELMEGPEEDIADKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKELLCKMEREKSIEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRGRSSSMGLQEYHSRARESELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQGAKSLFSTAFSESLAAEISSVSRDELMEAIQKQEEINFRLQDYIDRIIVAIMETNPSILEVK
| null | null |
cell cycle [GO:0007049]; cell division [GO:0051301]; early endosome to recycling endosome transport [GO:0061502]; endocytic recycling [GO:0032456]; Golgi to plasma membrane protein transport [GO:0043001]; negative regulation of adiponectin secretion [GO:0070164]; positive regulation of cilium assembly [GO:0045724]; positive regulation of mitotic cytokinetic process [GO:1903438]; protein localization to cilium [GO:0061512]; protein localization to cleavage furrow [GO:1905345]; regulation of cilium assembly [GO:1902017]; regulation of cytokinesis [GO:0032465]; regulation of early endosome to recycling endosome transport [GO:1902954]; regulation of endocytic recycling [GO:2001135]; regulation of protein localization to centrosome [GO:1904779]; regulation of vesicle-mediated transport [GO:0060627]; vesicle-mediated transport [GO:0016192]
|
centriolar satellite [GO:0034451]; centrosome [GO:0005813]; cleavage furrow [GO:0032154]; cytosol [GO:0005829]; endocytic vesicle [GO:0030139]; endocytic vesicle membrane [GO:0030666]; endosome [GO:0005768]; Golgi membrane [GO:0000139]; intercellular bridge [GO:0045171]; intracellular membrane-bounded organelle [GO:0043231]; midbody [GO:0030496]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; postsynaptic recycling endosome membrane [GO:0098944]; recycling endosome [GO:0055037]; recycling endosome membrane [GO:0055038]; trans-Golgi network membrane [GO:0032588]
|
calcium ion binding [GO:0005509]; dynein light intermediate chain binding [GO:0051959]; identical protein binding [GO:0042802]; molecular adaptor activity [GO:0060090]; protein homodimerization activity [GO:0042803]; protein-containing complex binding [GO:0044877]; protein-macromolecule adaptor activity [GO:0030674]; small GTPase binding [GO:0031267]
|
PF13499;PF09457;
|
1.20.5.2440;1.10.238.10;
| null |
PTM: Phosphorylated at Ser-102 by CDK1 during metaphase, and dephosphorylated as cells enter telophase. {ECO:0000269|PubMed:22401586}.
|
SUBCELLULAR LOCATION: Endosome membrane. Recycling endosome membrane {ECO:0000269|PubMed:11495908, ECO:0000269|PubMed:15601896, ECO:0000269|PubMed:17007872, ECO:0000269|PubMed:17394487, ECO:0000269|PubMed:20026645}; Peripheral membrane protein {ECO:0000305}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:15158446, ECO:0000269|PubMed:15601896, ECO:0000269|PubMed:17394487, ECO:0000269|PubMed:18511905}. Cleavage furrow {ECO:0000269|PubMed:15158446, ECO:0000269|PubMed:15601896}. Midbody {ECO:0000269|PubMed:15601896, ECO:0000269|PubMed:16148947, ECO:0000269|PubMed:18511905}. Golgi apparatus membrane {ECO:0000269|PubMed:25673879}; Peripheral membrane protein {ECO:0000305}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:25673879}; Peripheral membrane protein {ECO:0000305}. Note=During interphase, localized in vesicles continuously moving from peripheral sorting endosomes in the cell towards the pericentrosomal endosomal recycling compartment (ERC) (PubMed:17394487, PubMed:20026645). In early mitosis remains diffuse and distributed through the cell. The onset of anaphase sequesters these vesicles to the centrosomes at the opposite poles of the cell. During telophase these vesicles move from the centrosomes, to the furrow, and then to the midbody to aid in abscission (PubMed:15158446, PubMed:15601896, PubMed:18511905). Interaction with Rab11 mediates localization to endosomes (PubMed:11495908). Interaction with ARF6 mediates localization to the midbody (PubMed:16148947). Localized to the Golgi and TGN when interacting with RHO in photoreceptors (PubMed:25673879). Localized to rhodopsin transport carriers when interacting with RAB11A and ASAP1 in photoreceptors (PubMed:25673879). {ECO:0000269|PubMed:11495908, ECO:0000269|PubMed:15601896, ECO:0000269|PubMed:16148947, ECO:0000269|PubMed:17394487, ECO:0000269|PubMed:18511905, ECO:0000269|PubMed:20026645, ECO:0000269|PubMed:25673879}.
| null | null | null | null | null |
FUNCTION: Downstream effector molecule for Rab11 GTPase which is involved in endocytic trafficking, cytokinesis and intracellular ciliogenesis by participating in membrane delivery (PubMed:15601896, PubMed:16148947, PubMed:17394487, PubMed:17628206, PubMed:18511905, PubMed:19327867, PubMed:20026645, PubMed:25673879, PubMed:26258637, PubMed:31204173). Recruited by Rab11 to endosomes where it links Rab11 to dynein motor complex (PubMed:20026645). The functional Rab11-RAB11FIP3-dynein complex regulates the movement of peripheral sorting endosomes (SE) along microtubule tracks toward the microtubule organizing center/centrosome, generating the endocytic recycling compartment (ERC) during interphase of cell cycle (PubMed:17394487, PubMed:20026645). Facilitates the interaction between dynein and dynactin and activates dynein processivity (PubMed:25035494). Binding with ASAP1 is needed to regulate the pericentrosomal localization of recycling endosomes (By similarity). The Rab11-RAB11FIP3 complex is also implicated in the transport during telophase of vesicles derived from recycling endosomes to the cleavage furrow via centrosome-anchored microtubules, where the vesicles function to deliver membrane during late cytokinesis and abscission (PubMed:15601896, PubMed:16148947). The recruitment of Rab11-RAB11FIP3-containing endosomes to the cleavage furrow and tethering to the midbody is co-mediated by RAB11FIP3 interaction with ARF6-exocyst and RACGAP1-MKLP1 tethering complexes (PubMed:17628206, PubMed:18511905). Also involved in the Rab11-Rabin8-Rab8 ciliogenesis cascade by facilitating the orderly assembly of a ciliary targeting complex containing Rab11, ASAP1, Rabin8/RAB3IP, RAB11FIP3 and ARF4, which directs preciliary vesicle trafficking to mother centriole and ciliogenesis initiation (PubMed:26258637, PubMed:31204173). Also promotes the activity of Rab11 and ASAP1 in the ARF4-dependent Golgi-to-cilia transport of the sensory receptor rhodopsin (PubMed:25673879). Competes with WDR44 for binding to Rab11, which controls intracellular ciliogenesis pathway (PubMed:31204173). May play a role in breast cancer cell motility by regulating actin cytoskeleton (PubMed:19327867). {ECO:0000250|UniProtKB:Q8CHD8, ECO:0000269|PubMed:15601896, ECO:0000269|PubMed:16148947, ECO:0000269|PubMed:17394487, ECO:0000269|PubMed:17628206, ECO:0000269|PubMed:18511905, ECO:0000269|PubMed:19327867, ECO:0000269|PubMed:20026645, ECO:0000269|PubMed:25035494, ECO:0000269|PubMed:25673879, ECO:0000269|PubMed:26258637, ECO:0000269|PubMed:31204173}.
|
Homo sapiens (Human)
|
O75155
|
CAND2_HUMAN
|
MSTAAFHISSLLEKMTSSDKDFRFMATSDLMSELQKDSIQLDEDSERKVVKMLLRLLEDKNGEVQNLAVKCLGPLVVKVKEYQVETIVDTLCTNMRSDKEQLRDIAGIGLKTVLSELPPAATGSGLATNVCRKITGQLTSAIAQQEDVAVQLEALDILSDMLSRLGVPLGAFHASLLHCLLPQLSSPRLAVRKRAVGALGHLAAACSTDLFVELADHLLDRLPGPRVPTSPTAIRTLIQCLGSVGRQAGHRLGAHLDRLVPLVEDFCNLDDDELRESCLQAFEAFLRKCPKEMGPHVPNVTSLCLQYIKHDPNYNYDSDEDEEQMETEDSEFSEQESEDEYSDDDDMSWKVRRAAAKCIAALISSRPDLLPDFHCTLAPVLIRRFKEREENVKADVFTAYIVLLRQTQPPKGWLEAMEEPTQTGSNLHMLRGQVPLVVKALQRQLKDRSVRARQGCFSLLTELAGVLPGSLAEHMPVLVSGIIFSLADRSSSSTIRMDALAFLQGLLGTEPAEAFHPHLPILLPPVMACVADSFYKIAAEALVVLQELVRALWPLHRPRMLDPEPYVGEMSAVTLARLRATDLDQEVKERAISCMGHLVGHLGDRLGDDLEPTLLLLLDRLRNEITRLPAIKALTLVAVSPLQLDLQPILAEALHILASFLRKNQRALRLATLAALDALAQSQGLSLPPSAVQAVLAELPALVNESDMHVAQLAVDFLATVTQAQPASLVEVSGPVLSELLRLLRSPLLPAGVLAAAEGFLQALVGTRPPCVDYAKLISLLTAPVYEQAVDGGPGLHKQVFHSLARCVAALSAACPQEAASTASRLVCDARSPHSSTGVKVLAFLSLAEVGQVAGPGHQRELKAVLLEALGSPSEDVRAAASYALGRVGAGSLPDFLPFLLEQIEAEPRRQYLLLHSLREALGAAQPDSLKPYAEDIWALLFQRCEGAEEGTRGVVAECIGKLVLVNPSFLLPRLRKQLAAGRPHTRSTVITAVKFLISDQPHPIDPLLKSFIGEFMESLQDPDLNVRRATLAFFNSAVHNKPSLVRDLLDDILPLLYQETKIRRDLIREVEMGPFKHTVDDGLDVRKAAFECMYSLLESCLGQLDICEFLNHVEDGLKDHYDIRMLTFIMVARLATLCPAPVLQRVDRLIEPLRATCTAKVKAGSVKQEFEKQDELKRSAMRAVAALLTIPEVGKSPIMADFSSQIRSNPELAALFESIQKDSASAPSTDSMELS
| null | null |
positive regulation of DNA-templated transcription [GO:0045893]; protein ubiquitination [GO:0016567]; SCF complex assembly [GO:0010265]
|
cytosol [GO:0005829]; nucleus [GO:0005634]
|
TBP-class protein binding [GO:0017025]
|
PF08623;
|
1.25.10.10;
|
CAND family
|
PTM: Ubiquitinated and targeted for proteasomal degradation. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Probable assembly factor of SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complexes that promotes the exchange of the substrate-recognition F-box subunit in SCF complexes, thereby playing a key role in the cellular repertoire of SCF complexes. {ECO:0000250}.
|
Homo sapiens (Human)
|
O75159
|
SOCS5_HUMAN
|
MDKVGKMWNNFKYRCQNLFGHEGGSRSENVDMNSNRCLSVKEKNISIGDSTPQQQSSPLRENIALQLGLSPSKNSSRRNQNCATEIPQIVEISIEKDNDSCVTPGTRLARRDSYSRHAPWGGKKKHSCSTKTQSSLDADKKFGRTRSGLQRRERRYGVSSVHDMDSVSSRTVGSRSLRQRLQDTVGLCFPMRTYSKQSKPLFSNKRKIHLSELMLEKCPFPAGSDLAQKWHLIKQHTAPVSPHSTFFDTFDPSLVSTEDEEDRLRERRRLSIEEGVDPPPNAQIHTFEATAQVNPLYKLGPKLAPGMTEISGDSSAIPQANCDSEEDTTTLCLQSRRQKQRQISGDSHTHVSRQGAWKVHTQIDYIHCLVPDLLQITGNPCYWGVMDRYEAEALLEGKPEGTFLLRDSAQEDYLFSVSFRRYNRSLHARIEQWNHNFSFDAHDPCVFHSSTVTGLLEHYKDPSSCMFFEPLLTISLNRTFPFSLQYICRAVICRCTTYDGIDGLPLPSMLQDFLKEYHYKQKVRVRWLEREPVKAK
| null | null |
cellular response to low-density lipoprotein particle stimulus [GO:0071404]; cytokine-mediated signaling pathway [GO:0019221]; epidermal growth factor receptor signaling pathway [GO:0007173]; intracellular signal transduction [GO:0035556]; negative regulation of epidermal growth factor-activated receptor activity [GO:0007175]; negative regulation of inflammatory response [GO:0050728]; negative regulation of interleukin-6 production [GO:0032715]; negative regulation of monocyte chemotactic protein-1 production [GO:0071638]; negative regulation of signal transduction [GO:0009968]; negative regulation of T-helper 2 cell differentiation [GO:0045629]; phosphatidylinositol phosphate biosynthetic process [GO:0046854]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; positive regulation of T-helper 1 cell differentiation [GO:0045627]; protein ubiquitination [GO:0016567]; receptor signaling pathway via JAK-STAT [GO:0007259]; vascular endothelial cell response to fluid shear stress [GO:0097699]
|
cytosol [GO:0005829]; phosphatidylinositol 3-kinase complex [GO:0005942]
|
1-phosphatidylinositol-3-kinase regulator activity [GO:0046935]; epidermal growth factor receptor binding [GO:0005154]; receptor tyrosine kinase binding [GO:0030971]
|
PF00017;PF12610;PF07525;
|
3.30.505.10;
| null |
PTM: Phosphorylated. Phosphorylation is induced by EGF. {ECO:0000269|PubMed:15590694}.
| null | null | null |
PATHWAY: Protein modification; protein ubiquitination.
| null | null |
FUNCTION: SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. May be a substrate-recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Inhibits for instance EGF signaling by mediating the degradation of the EGF receptor/EGFR. Involved in the regulation of T-helper cell differentiation by inhibiting of the IL4 signaling pathway which promotes differentiation into the Th2 phenotype. Can also partially inhibit IL6 and LIF signaling. {ECO:0000269|PubMed:15590694}.
|
Homo sapiens (Human)
|
O75161
|
NPHP4_HUMAN
|
MNDWHRIFTQNVLVPPHPQRARQPWKESTAFQCVLKWLDGPVIRQGVLEVLSEVECHLRVSFFDVTYRHFFGRTWKTTVKPTKRPPSRIVFNEPLYFHTSLNHPHIVAVVEVVAEGKKRDGSLQTLSCGFGILRIFSNQPDSPISASQDKRLRLYHGTPRALLHPLLQDPAEQNRHMTLIENCSLQYTLKPHPALEPAFHLLPENLLVSGLQQIPGLLPAHGESGDALRKPRLQKPITGHLDDLFFTLYPSLEKFEEELLELHVQDHFQEGCGPLDGGALEILERRLRVGVHNGLGFVQRPQVVVLVPEMDVALTRSASFSRKVVSSSKTSSGSQALVLRSRLRLPEMVGHPAFAVIFQLEYVFSSPAGVDGNAASVTSLSNLACMHMVRWAVWNPLLEADSGRVTLPLQGGIQPNPSHCLVYKVPSASMSSEEVKQVESGTLRFQFSLGSEEHLDAPTEPVSGPKVERRPSRKPPTSPSSPPAPVPRVLAAPQNSPVGPGLSISQLAASPRSPTQHCLARPTSQLPHGSQASPAQAQEFPLEAGISHLEADLSQTSLVLETSIAEQLQELPFTPLHAPIVVGTQTRSSAGQPSRASMVLLQSSGFPEILDANKQPAEAVSATEPVTFNPQKEESDCLQSNEMVLQFLAFSRVAQDCRGTSWPKTVYFTFQFYRFPPATTPRLQLVQLDEAGQPSSGALTHILVPVSRDGTFDAGSPGFQLRYMVGPGFLKPGERRCFARYLAVQTLQIDVWDGDSLLLIGSAAVQMKHLLRQGRPAVQASHELEVVATEYEQDNMVVSGDMLGFGRVKPIGVHSVVKGRLHLTLANVGHPCEQKVRGCSTLPPSRSRVISNDGASRFSGGSLLTTGSSRRKHVVQAQKLADVDSELAAMLLTHARQGKGPQDVSRESDATRRRKLERMRSVRLQEAGGDLGRRGTSVLAQQSVRTQHLRDLQVIAAYRERTKAESIASLLSLAITTEHTLHATLGVAEFFEFVLKNPHNTQHTVTVEIDNPELSVIVDSQEWRDFKGAAGLHTPVEEDMFHLRGSLAPQLYLRPHETAHVPFKFQSFSAGQLAMVQASPGLSNEKGMDAVSPWKSSAVPTKHAKVLFRASGGKPIAVLCLTVELQPHVVDQVFRFYHPELSFLKKAIRLPPWHTFPGAPVGMLGEDPPVHVRCSDPNVICETQNVGPGEPRDIFLKVASGPSPEIKDFFVIIYSDRWLATPTQTWQVYLHSLQRVDVSCVAGQLTRLSLVLRGTQTVRKVRAFTSHPQELKTDPKGVFVLPPRGVQDLHVGVRPLRAGSRFVHLNLVDVDCHQLVASWLVCLCCRQPLISKAFEIMLAAGEGKGVNKRITYTNPYPSRRTFHLHSDHPELLRFREDSFQVGGGETYTIGLQFAPSQRVGEEEILIYINDHEDKNEEAFCVKVIYQ
| null | null |
actin cytoskeleton organization [GO:0030036]; cell-cell adhesion [GO:0098609]; flagellated sperm motility [GO:0030317]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; photoreceptor cell maintenance [GO:0045494]; photoreceptor cell outer segment organization [GO:0035845]; positive regulation of bicellular tight junction assembly [GO:1903348]; protein localization to ciliary transition zone [GO:1904491]; retina development in camera-type eye [GO:0060041]; signal transduction [GO:0007165]; visual behavior [GO:0007632]
|
bicellular tight junction [GO:0005923]; cell-cell junction [GO:0005911]; centriole [GO:0005814]; centrosome [GO:0005813]; ciliary basal body [GO:0036064]; ciliary base [GO:0097546]; ciliary transition zone [GO:0035869]; cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; non-motile cilium [GO:0097730]; nuclear body [GO:0016604]; nucleoplasm [GO:0005654]; photoreceptor distal connecting cilium [GO:0120206]; ribbon synapse [GO:0097470]
|
structural molecule activity [GO:0005198]
| null | null |
NPHP4 family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:17558407, ECO:0000269|PubMed:26644512}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:17558407}. Cell junction, tight junction {ECO:0000250|UniProtKB:P59240}. Nucleus {ECO:0000269|PubMed:22654112}. Note=In cultured renal cells, it localizes diffusely in the cytoplasm but, as cells approach confluence, it accumulates to basolateral tight junctions (By similarity). Localizes to the ciliary transition zone (By similarity). In the retinal photoreceptor cell layer, localizes at the connecting cilium (By similarity). {ECO:0000250|UniProtKB:P59240}.
| null | null | null | null | null |
FUNCTION: Involved in the organization of apical junctions; the function is proposed to implicate a NPHP1-4-8 module (PubMed:19755384, PubMed:21565611). Does not seem to be strictly required for ciliogenesis (PubMed:21565611). Required for building functional cilia. Involved in the organization of the subapical actin network in multiciliated epithelial cells. Seems to recruit INT to basal bodies of motile cilia which subsequently interacts with actin-modifying proteins such as DAAM1 (By similarity). In cooperation with INVS may down-regulate the canonical Wnt pathway and promote the Wnt-PCP pathway by regulating expression and subcellular location of disheveled proteins. Stabilizes protein levels of JADE1 and promotes its translocation to the nucleus leading to cooperative inhibition of canonical Wnt signaling (PubMed:21498478, PubMed:22654112). Acts as a negative regulator of the hippo pathway by association with LATS1 and modifying LATS1-dependent phosphorylation and localization of WWTR1/TAZ (PubMed:21555462). {ECO:0000250|UniProtKB:B0DOB4, ECO:0000250|UniProtKB:P59240, ECO:0000269|PubMed:21498478, ECO:0000269|PubMed:21555462, ECO:0000269|PubMed:21565611, ECO:0000269|PubMed:22654112, ECO:0000305|PubMed:19755384}.
|
Homo sapiens (Human)
|
O75164
|
KDM4A_HUMAN
|
MASESETLNPSARIMTFYPTMEEFRNFSRYIAYIESQGAHRAGLAKVVPPKEWKPRASYDDIDDLVIPAPIQQLVTGQSGLFTQYNIQKKAMTVREFRKIANSDKYCTPRYSEFEELERKYWKNLTFNPPIYGADVNGTLYEKHVDEWNIGRLRTILDLVEKESGITIEGVNTPYLYFGMWKTSFAWHTEDMDLYSINYLHFGEPKSWYSVPPEHGKRLERLAKGFFPGSAQSCEAFLRHKMTLISPLMLKKYGIPFDKVTQEAGEFMITFPYGYHAGFNHGFNCAESTNFATRRWIEYGKQAVLCSCRKDMVKISMDVFVRKFQPERYKLWKAGKDNTVIDHTLPTPEAAEFLKESELPPRAGNEEECPEEDMEGVEDGEEGDLKTSLAKHRIGTKRHRVCLEIPQEVSQSELFPKEDLSSEQYEMTECPAALAPVRPTHSSVRQVEDGLTFPDYSDSTEVKFEELKNVKLEEEDEEEEQAAAALDLSVNPASVGGRLVFSGSKKKSSSSLGSGSSRDSISSDSETSEPLSCRAQGQTGVLTVHSYAKGDGRVTVGEPCTRKKGSAARSFSERELAEVADEYMFSLEENKKSKGRRQPLSKLPRHHPLVLQECVSDDETSEQLTPEEEAEETEAWAKPLSQLWQNRPPNFEAEKEFNETMAQQAPHCAVCMIFQTYHQVEFGGFNQNCGNASDLAPQKQRTKPLIPEMCFTSTGCSTDINLSTPYLEEDGTSILVSCKKCSVRVHASCYGVPPAKASEDWMCSRCSANALEEDCCLCSLRGGALQRANDDRWVHVSCAVAILEARFVNIAERSPVDVSKIPLPRFKLKCIFCKKRRKRTAGCCVQCSHGRCPTAFHVSCAQAAGVMMQPDDWPFVVFITCFRHKIPNLERAKGALQSITAGQKVISKHKNGRFYQCEVVRLTTETFYEVNFDDGSFSDNLYPEDIVSQDCLQFGPPAEGEVVQVRWTDGQVYGAKFVASHPIQMYQVEFEDGSQLVVKRDDVYTLDEELPKRVKSRLSVASDMRFNEIFTEKEVKQEKKRQRVINSRYREDYIEPALYRAIME
|
1.14.11.66; 1.14.11.69
|
COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:16603238}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000269|PubMed:16603238};
|
apoptotic chromosome condensation [GO:0030263]; cardiac muscle hypertrophy in response to stress [GO:0014898]; chromatin remodeling [GO:0006338]; negative regulation of astrocyte differentiation [GO:0048712]; negative regulation of autophagy [GO:0010507]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of gene expression [GO:0010629]; positive regulation of gene expression [GO:0010628]; positive regulation of neuron differentiation [GO:0045666]; regulation of gene expression [GO:0010468]; response to nutrient levels [GO:0031667]
|
chromatin [GO:0000785]; cytosol [GO:0005829]; fibrillar center [GO:0001650]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; pericentric heterochromatin [GO:0005721]
|
histone demethylase activity [GO:0032452]; histone H3K36 demethylase activity [GO:0051864]; histone H3K36me2/H3K36me3 demethylase activity [GO:0140681]; histone H3K9 demethylase activity [GO:0032454]; histone H3K9me2/H3K9me3 demethylase activity [GO:0140684]; methylated histone binding [GO:0035064]; ubiquitin protein ligase binding [GO:0031625]; zinc ion binding [GO:0008270]
|
PF02373;PF02375;PF13831;PF18104;PF13832;
|
2.30.30.140;3.10.330.70;2.60.120.650;3.30.40.10;
|
JHDM3 histone demethylase family
|
PTM: (Microbial infection) SUMOylated by human herpesvirus 8 E3 SUMO-protein ligase K-bZIP/K8 at Lys-471; thereby modulating the chromatin binding and histone demethylase activity of KDM4A. {ECO:0000269|PubMed:28212444}.; PTM: Ubiquitinated by RNF8 and RNF168 following DNA damage, leading to its degradation. Degradation promotes accessibility of H4K20me2 mark for DNA repair protein TP53BP1, which is then recruited. {ECO:0000269|PubMed:22373579}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00537, ECO:0000269|PubMed:15927959, ECO:0000269|PubMed:16024779}.
|
CATALYTIC ACTIVITY: Reaction=2 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(9)-[histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + N(6)-methyl-L-lysyl(9)-[histone H3] + 2 succinate; Xref=Rhea:RHEA:60200, Rhea:RHEA-COMP:15538, Rhea:RHEA-COMP:15542, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:61929, ChEBI:CHEBI:61961; EC=1.14.11.66; Evidence={ECO:0000269|PubMed:16603238}; CATALYTIC ACTIVITY: Reaction=2 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(36)-[histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + N(6)-methyl-L-lysyl(36)-[histone H3] + 2 succinate; Xref=Rhea:RHEA:60236, Rhea:RHEA-COMP:9786, Rhea:RHEA-COMP:15536, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:61929, ChEBI:CHEBI:61961; EC=1.14.11.69; Evidence={ECO:0000269|PubMed:16603238};
| null | null | null | null |
FUNCTION: Histone demethylase that specifically demethylates 'Lys-9' and 'Lys-36' residues of histone H3, thereby playing a central role in histone code (PubMed:26741168). Does not demethylate histone H3 'Lys-4', H3 'Lys-27' nor H4 'Lys-20'. Demethylates trimethylated H3 'Lys-9' and H3 'Lys-36' residue, while it has no activity on mono- and dimethylated residues. Demethylation of Lys residue generates formaldehyde and succinate. Participates in transcriptional repression of ASCL2 and E2F-responsive promoters via the recruitment of histone deacetylases and NCOR1, respectively. {ECO:0000269|PubMed:16024779, ECO:0000269|PubMed:16603238, ECO:0000269|PubMed:26741168}.; FUNCTION: [Isoform 2]: Crucial for muscle differentiation, promotes transcriptional activation of the Myog gene by directing the removal of repressive chromatin marks at its promoter. Lacks the N-terminal demethylase domain. {ECO:0000269|PubMed:21694756}.
|
Homo sapiens (Human)
|
O75165
|
DJC13_HUMAN
|
MNIIRENKDLACFYTTKHSWRGKYKRVFSVGTHAITTYNPNTLEVTNQWPYGDICSISPVGKGQGTEFNLTFRKGSGKKSETLKFSTEHRTELLTEALRFRTDFSEGKITGRRYNCYKHHWSDSRKPVILEVTPGGFDQINPATNRVLCSYDYRNIEGFVDLSDYQGGFCILYGGFSRLHLFASEQREEIIKSAIDHAGNYIGISLRIRKEPLEFEQYLNLRFGKYSTDESITSLAEFVVQKISPRHSEPVKRVLALTETCLVERDPATYNIATLKPLGEVFALVCDSENPQLFTIEFIKGQVRKYSSTERDSLLASLLDGVRASGNRDVCVKMTPTHKGQRWGLLSMPVDEEVESLHLRFLATPPNGNFADAVFRFNANISYSGVLHAVTQDGLFSENKEKLINNAITALLSQEGDVVASNAELESQFQAVRRLVASKAGFLAFTQLPKFRERLGVKVVKALKRSNNGIIHAAVDMLCALMCPMHDDYDLRQEQLNKASLLSSKKFLENLLEKFNSHVDHGTGALVISSLLDFLTFALCAPYSETTEGQQFDMLLEMVASNGRTLFKLFQHPSMAIIKGAGLVMKAIIEEGDKEIATKMQELALSEGALPRHLHTAMFTISSDQRMLTNRQLSRHLVGLWTADNATATNLLKRILPPGLLAYLESSDLVPEKDADRMHVRDNVKIAMDQYGKFNKVPEWQRLAGKAAKEVEKFAKEKVDLVLMHWRDRMGIAQKENINQKPVVLRKRRQRIKIEANWDLFYYRFGQDHARSNLIWNFKTREELKDTLESEMRAFNIDRELGSANVISWNHHEFEVKYECLAEEIKIGDYYLRLLLEEDENEESGSIKRSYEFFNELYHRFLLTPKVNMKCLCLQALAIVYGRCHEEIGPFTDTRYIIGMLERCTDKLERDRLILFLNKLILNKKNVKDLMDSNGIRILVDLLTLAHLHVSRATVPLQSNVIEAAPDMKRESEKEWYFGNADKERSGPYGFHEMQELWTKGMLNAKTRCWAQGMDGWRPLQSIPQLKWCLLASGQAVLNETDLATLILNMLITMCGYFPSRDQDNAIIRPLPKVKRLLSDSTCLPHIIQLLLTFDPILVEKVAILLYHIMQDNPQLPRLYLSGVFFFIMMYTGSNVLPVARFLKYTHTKQAFKSEETKGQDIFQRSILGHILPEAMVCYLENYEPEKFSEIFLGEFDTPEAIWSSEMRRLMIEKIAAHLADFTPRLQSNTRALYQYCPIPIINYPQLENELFCNIYYLKQLCDTLRFPDWPIKDPVKLLKDTLDAWKKEVEKKPPMMSIDDAYEVLNLPQGQGPHDESKIRKAYFRLAQKYHPDKNPEGRDMFEKVNKAYEFLCTKSAKIVDGPDPENIILILKTQSILFNRHKEDLQPYKYAGYPMLIRTITMETSDDLLFSKESPLLPAATELAFHTVNCSALNAEELRRENGLEVLQEAFSRCVAVLTRASKPSDMSVQVCGYISKCYSVAAQFEECREKITEMPSIIKDLCRVLYFGKSIPRVAALGVECVSSFAVDFWLQTHLFQAGILWYLLGFLFNYDYTLEESGIQKSEETNQQEVANSLAKLSVHALSRLGGYLAEEQATPENPTIRKSLAGMLTPYVARKLAVASVTEILKMLNSNTESPYLIWNNSTRAELLEFLESQQENMIKKGDCDKTYGSEFVYSDHAKELIVGEIFVRVYNEVPTFQLEVPKAFAASLLDYIGSQAQYLHTFMAITHAAKVESEQHGDRLPRVEMALEALRNVIKYNPGSESECIGHFKLIFSLLRVHGAGQVQQLALEVVNIVTSNQDCVNNIAESMVLSSLLALLHSLPSSRQLVLETLYALTSSTKIIKEAMAKGALIYLLDMFCNSTHPQVRAQTAELFAKMTADKLIGPKVRITLMKFLPSVFMDAMRDNPEAAVHIFEGTHENPELIWNDNSRDKVSTTVREMMLEHFKNQQDNPEANWKLPEDFAVVFGEAEGELAVGGVFLRIFIAQPAWVLRKPREFLIALLEKLTELLEKNNPHGETLETLTMATVCLFSAQPQLADQVPPLGHLPKVIQAMNHRNNAIPKSAIRVIHALSENELCVRAMASLETIGPLMNGMKKRADTVGLACEAINRMFQKEQSELVAQALKADLVPYLLKLLEGIGLENLDSPAATKAQIVKALKAMTRSLQYGEQVNEILCRSSVWSAFKDQKHDLFISESQTAGYLTGPGVAGYLTAGTSTSVMSNLPPPVDHEAGDLGYQT
| null | null |
endosome organization [GO:0007032]; osteoblast differentiation [GO:0001649]; protein transport [GO:0015031]; receptor-mediated endocytosis [GO:0006898]; regulation of early endosome to late endosome transport [GO:2000641]; regulation of early endosome to recycling endosome transport [GO:1902954]
|
azurophil granule membrane [GO:0035577]; cytosol [GO:0005829]; early endosome membrane [GO:0031901]; endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; intracellular membrane-bounded organelle [GO:0043231]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; plasma membrane [GO:0005886]; secretory granule membrane [GO:0030667]
| null |
PF00226;PF14237;PF19432;
|
1.10.287.110;1.25.10.10;
| null | null |
SUBCELLULAR LOCATION: Early endosome {ECO:0000269|PubMed:18256511}. Early endosome membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000269|PubMed:18256511}. Endosome membrane {ECO:0000269|PubMed:24643499}.
| null | null | null | null | null |
FUNCTION: Involved in membrane trafficking through early endosomes, such as the early endosome to recycling endosome transport implicated in the recycling of transferrin and the early endosome to late endosome transport implicated in degradation of EGF and EGFR (PubMed:18256511, PubMed:18307993). Involved in the regulation of endosomal membrane tubulation and regulates the dynamics of SNX1 on the endosomal membrane; via association with WASHC2 may link the WASH complex to the retromer SNX-BAR subcomplex (PubMed:24643499). {ECO:0000269|PubMed:18256511, ECO:0000269|PubMed:18307993, ECO:0000269|PubMed:24643499}.
|
Homo sapiens (Human)
|
O75167
|
PHAR2_HUMAN
|
MDNAVDGLDKASIANSDGPTAGSQTPPFKRKGKLSTIGKIFKPWKWRKKKTSDKFRETSAVLERKISTRQSREELIRRGVLKELPDQDGDVTVNFENSNGHMIPIGEESTREENVVKSEEGNGSVSEKTPPLEEQAEDKKENTENHSETPAAPALPPSAPPKPRPKPKPKKSPVPPKGATAGASHKGDEVPPIKKNTKAPGKQAPVPPPKPASRNTTREAAGSSHSKKTTGSKASASPSTSSTSSRPKASKETVSSKAGTVGTTKGKRKTDKQPITSHLSSDTTTSGTSDLKGEPAETRVESFKLEQTVPGAEEQNTGKFKSMVPPPPVAPAPSPLAPPLPLEDQCITASDTPVVLVSVGADLPVSALDPSQLLWAEEPTNRTTLYSGTGLSVNRENAKCFTTKEELGKTVPQLLTPGLMGESSESFSASEDEGHREYQANDSDSDGPILYTDDEDEDEDEDGSGESALASKIRRRDTLAIKLGNRPSKKELEDKNILQRTSEEERQEIRQQIGTKLVRRLSQRPTTEELEQRNILKQKNEEEEQEAKMELKRRLSRKLSLRPTVAELQARRILRFNEYVEVTDSPDYDRRADKPWARLTPADKAAIRKELNEFKSTEMEVHEESRQFTRFHRP
| null | null |
actin cytoskeleton organization [GO:0030036]
|
plasma membrane [GO:0005886]; platelet alpha granule membrane [GO:0031092]
|
actin binding [GO:0003779]; protein phosphatase inhibitor activity [GO:0004864]
|
PF02755;
|
6.10.140.1750;6.10.140.2130;
|
Phosphatase and actin regulator family
| null |
SUBCELLULAR LOCATION: [Isoform 2]: Membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 4]: Membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.
| null | null | null | null | null | null |
Homo sapiens (Human)
|
O75170
|
PP6R2_HUMAN
|
MFWKFDLNTTSHVDKLLDKEHVTLQELMDEDDILQECKAQNQKLLDFLCRQQCMEELVSLITQDPPLDMEEKVRFKYPNTACELLTCDVPQISDRLGGDESLLSLLYDFLDHEPPLNPLLASFFSKTIGNLIARKTEQVITFLKKKDKFISLVLKHIGTSALMDLLLRLVSCVEPAGLRQDVLHWLNEEKVIQRLVELIHPSQDEDRQSNASQTLCDIVRLGRDQGSQLQEALEPDPLLTALESQDCVEQLLKNMFDGDRTESCLVSGTQVLLTLLETRRVGTEGLVDSFSQGLERSYAVSSSVLHGIEPRLKDFHQLLLNPPKKKAILTTIGVLEEPLGNARLHGARLMAALLHTNTPSINQELCRLNTMDLLLDLFFKYTWNNFLHFQVELCIAAILSHAAREERTEASGSESRVEPPHENGNRSLETPQPAASLPDNTMVTHLFQKCCLVQRILEAWEANDHTQAAGGMRRGNMGHLTRIANAVVQNLERGPVQTHISEVIRGLPADCRGRWESFVEETLTETNRRNTVDLVSTHHLHSSSEDEDIEGAFPNELSLQQAFSDYQIQQMTANFVDQFGFNDEEFADQDDNINAPFDRIAEINFNIDADEDSPSAALFEACCSDRIQPFDDDEDEDIWEDSDTRCAARVMARPRFGAPHASESCSKNGPERGGQDGKASLEAHRDAPGAGAPPAPGKKEAPPVEGDSEGAMWTAVFDEPANSTPTAPGVVRDVGSSVWAAGTSAPEEKGWAKFTDFQPFCCSESGPRCSSPVDTECSHAEGSRSQGPEKASQASYFAVSPASPCAWNVCVTRKAPLLASDSSSSGGSHSEDGDQKAASAMDAVSRGPGREAPPLPTVARTEEAVGRVGCADSRLLSPACPAPKEVTAAPAVAVPPEATVAITTALSKAGPAIPTPAVSSALAVAVPLGPIMAVTAAPAMVATLGTVTKDGKTDAPPEGAALNGPV
| null | null | null |
cytoplasmic ribonucleoprotein granule [GO:0036464]; cytosol [GO:0005829]; nucleus [GO:0005634]
|
protein phosphatase binding [GO:0019903]; protein phosphatase regulator activity [GO:0019888]
|
PF04499;
|
1.25.10.10;
|
SAPS family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16769727}.
| null | null | null | null | null |
FUNCTION: Regulatory subunit of protein phosphatase 6 (PP6). May function as a scaffolding PP6 subunit. Involved in the PP6-mediated dephosphorylation of NFKBIE opposing its degradation in response to TNF-alpha. {ECO:0000269|PubMed:16769727}.
|
Homo sapiens (Human)
|
O75173
|
ATS4_HUMAN
|
MSQTGSHPGRGLAGRWLWGAQPCLLLPIVPLSWLVWLLLLLLASLLPSARLASPLPREEEIVFPEKLNGSVLPGSGAPARLLCRLQAFGETLLLELEQDSGVQVEGLTVQYLGQAPELLGGAEPGTYLTGTINGDPESVASLHWDGGALLGVLQYRGAELHLQPLEGGTPNSAGGPGAHILRRKSPASGQGPMCNVKAPLGSPSPRPRRAKRFASLSRFVETLVVADDKMAAFHGAGLKRYLLTVMAAAAKAFKHPSIRNPVSLVVTRLVILGSGEEGPQVGPSAAQTLRSFCAWQRGLNTPEDSDPDHFDTAILFTRQDLCGVSTCDTLGMADVGTVCDPARSCAIVEDDGLQSAFTAAHELGHVFNMLHDNSKPCISLNGPLSTSRHVMAPVMAHVDPEEPWSPCSARFITDFLDNGYGHCLLDKPEAPLHLPVTFPGKDYDADRQCQLTFGPDSRHCPQLPPPCAALWCSGHLNGHAMCQTKHSPWADGTPCGPAQACMGGRCLHMDQLQDFNIPQAGGWGPWGPWGDCSRTCGGGVQFSSRDCTRPVPRNGGKYCEGRRTRFRSCNTEDCPTGSALTFREEQCAAYNHRTDLFKSFPGPMDWVPRYTGVAPQDQCKLTCQAQALGYYYVLEPRVVDGTPCSPDSSSVCVQGRCIHAGCDRIIGSKKKFDKCMVCGGDGSGCSKQSGSFRKFRYGYNNVVTIPAGATHILVRQQGNPGHRSIYLALKLPDGSYALNGEYTLMPSPTDVVLPGAVSLRYSGATAASETLSGHGPLAQPLTLQVLVAGNPQDTRLRYSFFVPRPTPSTPRPTPQDWLHRRAQILEILRRRPWAGRK
|
3.4.24.82
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:18042673}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:18042673};
|
extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]; proteolysis [GO:0006508]; skeletal system development [GO:0001501]
|
collagen-containing extracellular matrix [GO:0062023]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; nuclear speck [GO:0016607]
|
metalloendopeptidase activity [GO:0004222]; metallopeptidase activity [GO:0008237]; peptidase activity [GO:0008233]; protease binding [GO:0002020]; zinc ion binding [GO:0008270]
|
PF17771;PF19236;PF05986;PF01421;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.; 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, extracellular space, extracellular matrix {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=Glutamyl endopeptidase. Bonds cleaved include 370-Thr-Glu-Gly-Glu-|-Ala-Arg-Gly-Ser-377 in the interglobular domain of mammalian aggrecan.; EC=3.4.24.82;
| null | null | null | null |
FUNCTION: Cleaves aggrecan, a cartilage proteoglycan, and may be involved in its turnover. May play an important role in the destruction of aggrecan in arthritic diseases. Could also be a critical factor in the exacerbation of neurodegeneration in Alzheimer disease. Cleaves aggrecan at the '392-Glu-|-Ala-393' site.
|
Homo sapiens (Human)
|
O75175
|
CNOT3_HUMAN
|
MADKRKLQGEIDRCLKKVSEGVEQFEDIWQKLHNAANANQKEKYEADLKKEIKKLQRLRDQIKTWVASNEIKDKRQLIDNRKLIETQMERFKVVERETKTKAYSKEGLGLAQKVDPAQKEKEEVGQWLTNTIDTLNMQVDQFESEVESLSVQTRKKKGDKDKQDRIEGLKRHIEKHRYHVRMLETILRMLDNDSILVDAIRKIKDDVEYYVDSSQDPDFEENEFLYDDLDLEDIPQALVATSPPSHSHMEDEIFNQSSSTPTSTTSSSPIPPSPANCTTENSEDDKKRGRSTDSEVSQSPAKNGSKPVHSNQHPQSPAVPPTYPSGPPPAASALSTTPGNNGVPAPAAPPSALGPKASPAPSHNSGTPAPYAQAVAPPAPSGPSTTQPRPPSVQPSGGGGGGSGGGGSSSSSNSSAGGGAGKQNGATSYSSVVADSPAEVALSSSGGNNASSQALGPPSGPHNPPPSTSKEPSAAAPTGAGGVAPGSGNNSGGPSLLVPLPVNPPSSPTPSFSDAKAAGALLNGPPQFSTAPEIKAPEPLSSLKSMAERAAISSGIEDPVPTLHLTERDIILSSTSAPPASAQPPLQLSEVNIPLSLGVCPLGPVPLTKEQLYQQAMEEAAWHHMPHPSDSERIRQYLPRNPCPTPPYHHQMPPPHSDTVEFYQRLSTETLFFIFYYLEGTKAQYLAAKALKKQSWRFHTKYMMWFQRHEEPKTITDEFEQGTYIYFDYEKWGQRKKEGFTFEYRYLEDRDLQ
| null | null |
nuclear-transcribed mRNA poly(A) tail shortening [GO:0000289]; positive regulation of cold-induced thermogenesis [GO:0120162]; regulation of DNA-templated transcription [GO:0006355]; regulation of stem cell population maintenance [GO:2000036]; regulation of translation [GO:0006417]; regulatory ncRNA-mediated gene silencing [GO:0031047]; trophectodermal cell differentiation [GO:0001829]
|
CCR4-NOT complex [GO:0030014]; CCR4-NOT core complex [GO:0030015]; cytosol [GO:0005829]; nucleus [GO:0005634]; P-body [GO:0000932]
| null |
PF04153;PF04065;
|
2.30.30.1020;
|
CNOT2/3/5 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}. Cytoplasm, P-body {ECO:0000250}. Note=NANOS2 promotes its localization to P-body. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Component of the CCR4-NOT complex which is one of the major cellular mRNA deadenylases and is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation. Additional complex functions may be a consequence of its influence on mRNA expression. May be involved in metabolic regulation; may be involved in recruitment of the CCR4-NOT complex to deadenylation target mRNAs involved in energy metabolism. Involved in mitotic progression and regulation of the spindle assembly checkpoint by regulating the stability of MAD1L1 mRNA. Can repress transcription and may link the CCR4-NOT complex to transcriptional regulation; the repressive function may involve histone deacetylases. Involved in the maintenance of embryonic stem (ES) cell identity. {ECO:0000269|PubMed:14707134, ECO:0000269|PubMed:22342980, ECO:0000269|PubMed:22367759}.
|
Homo sapiens (Human)
|
O75177
|
CREST_HUMAN
|
MSVAFASARPRGKGEVTQQTIQKMLDENHHLIQCILEYQSKGKTAECTQYQQILHRNLVYLATIADSNQNMQSLLPAPPTQNMNLGPGALTQSGSSQGLHSQGSLSDAISTGLPPSSLLQGQIGNGPSHVSMQQTAPNTLPTTSMSISGPGYSHAGPASQGVPMQGQGTIGNYVSRTNINMQSNPVSMMQQQAATSHYSSAQGGSQHYQGQSSIAMMGQGSQGSSMMGQRPMAPYRPSQQGSSQQYLGQEEYYGEQYSHSQGAAEPMGQQYYPDGHGDYAYQQSSYTEQSYDRSFEESTQHYYEGGNSQYSQQQAGYQQGAAQQQTYSQQQYPSQQSYPGQQQGYGSAQGAPSQYPGYQQGQGQQYGSYRAPQTAPSAQQQRPYGYEQGQYGNYQQ
| null | null |
chromatin organization [GO:0006325]; dendrite development [GO:0016358]; positive regulation of dendrite morphogenesis [GO:0050775]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of transcription by RNA polymerase II [GO:0045944]
|
cytosol [GO:0005829]; kinetochore [GO:0000776]; nBAF complex [GO:0071565]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
transcription coactivator activity [GO:0003713]
|
PF05030;
| null |
SS18 family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}. Note=Localizes to nuclear bodies. Colocalizes with SGO1 at kinetochore (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Transcriptional activator which is required for calcium-dependent dendritic growth and branching in cortical neurons. Recruits CREB-binding protein (CREBBP) to nuclear bodies. Component of the CREST-BRG1 complex, a multiprotein complex that regulates promoter activation by orchestrating a calcium-dependent release of a repressor complex and a recruitment of an activator complex. In resting neurons, transcription of the c-FOS promoter is inhibited by BRG1-dependent recruitment of a phospho-RB1-HDAC1 repressor complex. Upon calcium influx, RB1 is dephosphorylated by calcineurin, which leads to release of the repressor complex. At the same time, there is increased recruitment of CREBBP to the promoter by a CREST-dependent mechanism, which leads to transcriptional activation. The CREST-BRG1 complex also binds to the NR2B promoter, and activity-dependent induction of NR2B expression involves a release of HDAC1 and recruitment of CREBBP (By similarity). {ECO:0000250}.
|
Homo sapiens (Human)
|
O75179
|
ANR17_HUMAN
|
MEKATVPVAAATAAEGEGSPPAVAAVAGPPAAAEVGGGVGGSSRARSASSPRGMVRVCDLLLKKKPPQQQHHKAKRNRTCRPPSSSESSSDSDNSGGGGGGGGGGGGGGGTSSNNSEEEEDDDDEEEEVSEVESFILDQDDLENPMLETASKLLLSGTADGADLRTVDPETQARLEALLEAAGIGKLSTADGKAFADPEVLRRLTSSVSCALDEAAAALTRMRAESTANAGQSDNRSLAEACSEGDVNAVRKLLIEGRSVNEHTEEGESLLCLACSAGYYELAQVLLAMHANVEDRGIKGDITPLMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAGINTHSNEFKESALTLACYKGHLEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLLGQGANINAQTEETQETALTLACCGGFLEVADFLIKAGADIELGCSTPLMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGHVCTVQFLISKGANVNRTTANNDHTVLSLACAGGHLAVVELLLAHGADPTHRLKDGSTMLIEAAKGGHTSVVCYLLDYPNNLLSAPPPDVTQLTPPSHDLNRAPRVPVQALPMVVPPQEPDKPPANVATTLPIRNKAASKQKSSSHLPANSQDVQGYITNQSPESIVEEAQGKLTELEQRIKEAIEKNAQLQSLELAHADQLTKEKIEELNKTREEQIQKKQKILEELQKVERELQLKTQQQLKKQYLEVKAQRIQLQQQQQQSCQHLGLLTPVGVGEQLSEGDYARLQQVDPVLLKDEPQQTAAQMGFAPIQPLAMPQALPLAAGPLPPGSIANLTELQGVIVGQPVLGQAQLAGLGQGILTETQQGLMVASPAQTLNDTLDDIMAAVSGRASAMSNTPTHSIAASISQPQTPTPSPIISPSAMLPIYPAIDIDAQTESNHDTALTLACAGGHEELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQSERTKDTPLSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSRTGSKLGISPLMLAAMNGHTAAVKLLLDMGSDINAQIETNRNTALTLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAPPVPSSRDTALTIAADKGHYKFCELLIGRGAHIDVRNKKGNTPLWLAANGGHLDVVQLLVQAGADVDAADNRKITPLMAAFRKGHVKVVRYLVKEVNQFPSDSECMRYIATITDKEMLKKCHLCMESIVQAKDRQAAEANKNASILLEELDLEKLREESRRLALAAKREKRKEKRRKKKEEQRRKLEEIEAKNKENFELQAAQEKEKLKVEDEPEVLTEPPSATTTTTIGISATWTTLAGSHGKRNNTITTTSSKRKNRKNKITPENVQIIFDDPLPISYSQPEKVNGESKSSSTSESGDSDNMRISSCSDESSNSNSSRKSDNHSPAVVTTTVSSKKQPSVLVTFPKEERKSVSGKASIKLSETISEGTSNSLSTCTKSGPSPLSSPNGKLTVASPKRGQKREEGWKEVVRRSKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALIKDPDKEIDELIPKNRLKSSSANSKIGSSAPTTTAANTSLMGIKMTTVALSSTSQTATALTVPAISSASTHKTIKNPVNNVRPGFPVSLPLAYPPPQFAHALLAAQTFQQIRPPRLPMTHFGGTFPPAQSTWGPFPVRPLSPARATNSPKPHMVPRHSNQNSSGSQVNSAGSLTSSPTTTTSSSASTVPGTSTNGSPSSPSVRRQLFVTVVKTSNATTTTVTTTASNNNTAPTNATYPMPTAKEHYPVSSPSSPSPPAQPGGVSRNSPLDCGSASPNKVASSSEQEAGSPPVVETTNTRPPNSSSSSGSSSAHSNQQQPPGSVSQEPRPPLQQSQVPPPEVRMTVPPLATSSAPVAVPSTAPVTYPMPQTPMGCPQPTPKMETPAIRPPPHGTTAPHKNSASVQNSSVAVLSVNHIKRPHSVPSSVQLPSTLSTQSACQNSVHPANKPIAPNFSAPLPFGPFSTLFENSPTSAHAFWGGSVVSSQSTPESMLSGKSSYLPNSDPLHQSDTSKAPGFRPPLQRPAPSPSGIVNMDSPYGSVTPSSTHLGNFASNISGGQMYGPGAPLGGAPAAANFNRQHFSPLSLLTPCSSASNDSSAQSVSSGVRAPSPAPSSVPLGSEKPSNVSQDRKVPVPIGTERSARIRQTGTSAPSVIGSNLSTSVGHSGIWSFEGIGGNQDKVDWCNPGMGNPMIHRPMSDPGVFSQHQAMERDSTGIVTPSGTFHQHVPAGYMDFPKVGGMPFSVYGNAMIPPVAPIPDGAGGPIFNGPHAADPSWNSLIKMVSSSTENNGPQTVWTGPWAPHMNSVHMNQLG
| null | null |
blood vessel maturation [GO:0001955]; defense response to bacterium [GO:0042742]; innate immune response [GO:0045087]; negative regulation of smooth muscle cell differentiation [GO:0051151]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of cell cycle [GO:0045787]; positive regulation of G1/S transition of mitotic cell cycle [GO:1900087]; positive regulation of MDA-5 signaling pathway [GO:1900245]; positive regulation of RIG-I signaling pathway [GO:1900246]; regulation of DNA replication [GO:0006275]
|
chromatin [GO:0000785]; cytoplasm [GO:0005737]; male germ cell nucleus [GO:0001673]; membrane [GO:0016020]; nuclear membrane [GO:0031965]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
chromatin binding [GO:0003682]; RNA binding [GO:0003723]
|
PF00023;PF12796;PF13637;PF00013;
|
1.25.40.20;3.30.1370.10;
| null |
PTM: Phosphorylated by CDK2. {ECO:0000269|PubMed:19150984}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17276651, ECO:0000269|PubMed:22328336}. Nucleus {ECO:0000269|PubMed:17276651, ECO:0000269|PubMed:19150984, ECO:0000269|PubMed:22328336}. Note=Detected around the nucleolus. Localized on chromatin in a cell cycle-dependent manner. {ECO:0000269|PubMed:17276651, ECO:0000269|PubMed:19150984}.
| null | null | null | null | null |
FUNCTION: Could play pivotal roles in cell cycle and DNA regulation (PubMed:19150984). Involved in innate immune defense against viruse by positively regulating the viral dsRNA receptors DDX58 and IFIH1 signaling pathways (PubMed:22328336). Involves in NOD2- and NOD1-mediated responses to bacteria suggesting a role in innate antibacterial immune pathways too (PubMed:23711367). Target of enterovirus 71 which is the major etiological agent of HFMD (hand, foot and mouth disease) (PubMed:17276651). Could play a central role for the formation and/or maintenance of the blood vessels of the circulation system (By similarity). {ECO:0000250|UniProtKB:Q99NH0, ECO:0000269|PubMed:17276651, ECO:0000269|PubMed:19150984, ECO:0000269|PubMed:22328336, ECO:0000269|PubMed:23711367}.
|
Homo sapiens (Human)
|
O75182
|
SIN3B_HUMAN
|
MAHAGGGSGGSGAGGPAGRGLSGARWGRSGSAGHEKLPVHVEDALTYLDQVKIRFGSDPATYNGFLEIMKEFKSQSIDTPGVIRRVSQLFHEHPDLIVGFNAFLPLGYRIDIPKNGKLNIQSPLTSQENSHNHGDGAEDFKQQVPYKEDKPQVPLESDSVEFNNAISYVNKIKTRFLDHPEIYRSFLEILHTYQKEQLNTRGRPFRGMSEEEVFTEVANLFRGQEDLLSEFGQFLPEAKRSLFTGNGPCEMHSVQKNEHDKTPEHSRKRSRPSLLRPVSAPAKKKMKLRGTKDLSIAAVGKYGTLQEFSFFDKVRRVLKSQEVYENFLRCIALFNQELVSGSELLQLVSPFLGKFPELFAQFKSFLGVKELSFAPPMSDRSGDGISREIDYASCKRIGSSYRALPKTYQQPKCSGRTAICKELDHWTLLQGSWTDDYCMSKFKNTCWIPGYSAGVLNDTWVSFPSWSEDSTFVSSKKTPYEEQLHRCEDERFELDVVLETNLATIRVLESVQKKLSRMAPEDQEKFRLDDSLGGTSEVIQRRAIYRIYGDKAPEIIESLKKNPVTAVPVVLKRLKAKEEEWREAQQGFNKIWREQYEKAYLKSLDHQAVNFKQNDTKALRSKSLLNEIESVYDEHQEQHSEGRSAPSSEPHLIFVYEDRQILEDAAALISYYVKRQPAIQKEDQGTIHQLLHQFVPSLFFSQQLDLGASEESADEDRDSPQGQTTDPSERKKPAPGPHSSPPEEKGAFGDAPATEQPPLPPPAPHKPLDDVYSLFFANNNWYFFLRLHQTLCSRLLKIYRQAQKQLLEYRTEKEREKLLCEGRREKGSDPAMELRLKQPSEVELEEYYPAFLDMVRSLLEGSIDPTQYEDTLREMFTIHAYVGFTMDKLVQNIARQLHHLVSDDVCLKVVELYLNEKKRGAAGGNLSSRCVRAARETSYQWKAERCMADENCFKVMFLQRKGQVIMTIELLDTEEAQTEDPVEVQHLARYVEQYVGTEGASSSPTEGFLLKPVFLQRNLKKFRRRWQSEQARALRGEARSSWKRLVGVESACDVDCRFKLSTHKMVFIVNSEDYMYRRGTLCRAKQVQPLVLLRHHQHFEEWHSRWLEDNVTVEAASLVQDWLMGEEDEDMVPCKTLCETVHVHGLPVTRYRVQYSRRPASP
| null | null |
negative regulation of cell migration [GO:0030336]; negative regulation of transcription by RNA polymerase II [GO:0000122]
|
autosome [GO:0030849]; chromatin [GO:0000785]; cytoplasm [GO:0005737]; histone deacetylase complex [GO:0000118]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; X chromosome [GO:0000805]; XY body [GO:0001741]; Y chromosome [GO:0000806]
|
chromatin binding [GO:0003682]; transcription corepressor activity [GO:0003714]
|
PF02671;PF08295;PF16879;
|
1.20.1160.11;
| null |
PTM: Ubiquitinated by RNF220 that leads to proteasomal degradation. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00810}.
| null | null | null | null | null |
FUNCTION: Acts as a transcriptional repressor. Interacts with MXI1 to repress MYC responsive genes and antagonize MYC oncogenic activities. Interacts with MAD-MAX heterodimers by binding to MAD. The heterodimer then represses transcription by tethering SIN3B to DNA. Also forms a complex with FOXK1 which represses transcription. With FOXK1, regulates cell cycle progression probably by repressing cell cycle inhibitor genes expression. As part of the SIN3B complex represses transcription and counteracts the histone acetyltransferase activity of EP300 through the recognition H3K27ac marks by PHF12 and the activity of the histone deacetylase HDAC2 (PubMed:37137925). SIN3B complex is recruited downstream of the constitutively active genes transcriptional start sites through interaction with histones and mitigates histone acetylation and RNA polymerase II progression within transcribed regions contributing to the regulation of transcription (PubMed:21041482). {ECO:0000250|UniProtKB:Q62141, ECO:0000269|PubMed:21041482, ECO:0000269|PubMed:37137925}.
|
Homo sapiens (Human)
|
O75185
|
AT2C2_HUMAN
|
MVEGRVSEFLKKLGFSGGGRQYQALEKDEEEALIDEQSELKAIEKEKKVTALPPKEACKCQKEDLARAFCVDLHTGLSEFSVTQRRLAHGWNEFVADNSEPVWKKYLDQFKNPLILLLLGSALVSVLTKEYEDAVSIATAVLVVVTVAFIQEYRSEKSLEELTKLVPPECNCLREGKLQHLLARELVPGDVVSLSIGDRIPADIRLTEVTDLLVDESSFTGEAEPCSKTDSPLTGGGDLTTLSNIVFMGTLVQYGRGQGVVIGTGESSQFGEVFKMMQAEETPKTPLQKSMDRLGKQLTLFSFGIIGLIMLIGWSQGKQLLSMFTIGVSLAVAAIPEGLPIVVMVTLVLGVLRMAKKRVIVKKLPIVETLGCCSVLCSDKTGTLTANEMTVTQLVTSDGLRAEVSGVGYDGQGTVCLLPSKEVIKEFSNVSVGKLVEAGCVANNAVIRKNAVMGQPTEGALMALAMKMDLSDIKNSYIRKKEIPFSSEQKWMAVKCSLKTEDQEDIYFMKGALEEVIRYCTMYNNGGIPLPLTPQQRSFCLQEEKRMGSLGLRVLALASGPELGRLTFLGLVGIIDPPRVGVKEAVQVLSESGVSVKMITGDALETALAIGRNIGLCNGKLQAMSGEEVDSVEKGELADRVGKVSVFFRTSPKHKLKIIKALQESGAIVAMTGDGVNDAVALKSADIGIAMGQTGTDVSKEAANMILVDDDFSAIMNAVEEGKGIFYNIKNFVRFQLSTSISALSLITLSTVFNLPSPLNAMQILWINIIMDGPPAQSLGVEPVDKDAFRQPPRSVRDTILSRALILKILMSAAIIISGTLFIFWKEMPEDRASTPRTTTMTFTCFVFFDLFNALTCRSQTKLIFEIGFLRNHMFLYSVLGSILGQLAVIYIPPLQRVFQTENLGALDLLFLTGLASSVFILSELLKLCEKYCCSPKRVQMHPEDV
|
7.2.2.10
| null |
calcium ion transmembrane transport [GO:0070588]; intracellular calcium ion homeostasis [GO:0006874]; mammary gland epithelium development [GO:0061180]; manganese ion transport [GO:0006828]; positive regulation of calcium ion import [GO:0090280]; protein localization to plasma membrane [GO:0072659]
|
basolateral plasma membrane [GO:0016323]; cytoplasmic side of plasma membrane [GO:0009898]; cytoplasmic vesicle [GO:0031410]; endoplasmic reticulum [GO:0005783]; Golgi membrane [GO:0000139]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; trans-Golgi network membrane [GO:0032588]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; metal ion binding [GO:0046872]; P-type calcium transporter activity [GO:0005388]; P-type manganese transporter activity [GO:0140613]
|
PF13246;PF00689;PF00690;PF00122;PF00702;
|
3.40.1110.10;2.70.150.10;1.20.1110.10;3.40.50.1000;
|
Cation transport ATPase (P-type) (TC 3.A.3) family, Type IIA subfamily
| null |
SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:15831496}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:20887894}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000250|UniProtKB:A7L9Z8}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate; Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29108, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.10; Evidence={ECO:0000269|PubMed:15677451, ECO:0000269|PubMed:15831496, ECO:0000269|PubMed:16332677, ECO:0000269|PubMed:30923126}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18106; Evidence={ECO:0000305|PubMed:15677451, ECO:0000305|PubMed:15831496, ECO:0000305|PubMed:16332677, ECO:0000305|PubMed:30923126}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + Mn(2+)(in) = ADP + H(+) + Mn(2+)(out) + phosphate; Xref=Rhea:RHEA:66820, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29035, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:15831496, ECO:0000269|PubMed:30923126}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66821; Evidence={ECO:0000269|PubMed:30923126, ECO:0000305|PubMed:15831496};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.03 uM for Ca(2+) (Ca(2+)-dependent ATP hydrolysis) {ECO:0000269|PubMed:30923126}; KM=0.06 uM for Mn(2+) (Mn(2+)-dependent ATP hydrolysis) {ECO:0000269|PubMed:30923126};
| null | null | null |
FUNCTION: ATP-driven pump that supplies the Golgi apparatus with Ca(2+) and Mn(2+) ions, both essential cofactors for processing and trafficking of newly synthesized proteins in the secretory pathway (PubMed:15677451, PubMed:15831496, PubMed:16332677, PubMed:30923126). Within a catalytic cycle, acquires Ca(2+) or Mn(2+) ions on the cytoplasmic side of the membrane and delivers them to the lumenal side. The transfer of ions across the membrane is coupled to ATP hydrolysis and is associated with a transient phosphorylation that shifts the pump conformation from inward-facing to outward-facing state (PubMed:15831496, PubMed:16332677). Induces Ca(2+) influx independently of its ATP-driven pump function. At the basolateral membrane of mammary epithelial cells, interacts with Ca(2+) channel ORAI1 and mediates Ca(2+) entry independently of the Ca(2+) content of endoplasmic reticulum or Golgi stores. May facilitate transepithelial transport of large quantities of Ca(2+) for milk secretion via activation of Ca(2+) influx channels at the plasma membrane and active Ca(2+) transport at the Golgi apparatus (PubMed:20887894, PubMed:23840669). {ECO:0000269|PubMed:15677451, ECO:0000269|PubMed:15831496, ECO:0000269|PubMed:16332677, ECO:0000269|PubMed:20887894, ECO:0000269|PubMed:23840669, ECO:0000269|PubMed:30923126}.
|
Homo sapiens (Human)
|
O75190
|
DNJB6_HUMAN
|
MVDYYEVLGVQRHASPEDIKKAYRKLALKWHPDKNPENKEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGGSHFDSPFEFGFTFRNPDDVFREFFGGRDPFSFDFFEDPFEDFFGNRRGPRGSRSRGTGSFFSAFSGFPSFGSGFSSFDTGFTSFGSLGHGGLTSFSSTSFGGSGMGNFKSISTSTKMVNGRKITTKRIVENGQERVEVEEDGQLKSLTINGVADDDALAEERMRRGQNALPAQPAGLRPPKPPRPASLLRHAPHCLSEEEGEQDRPRAPGPWDPLASAAGLKEGGKRKKQKQREESKKKKSTKGNH
| null | null |
actin cytoskeleton organization [GO:0030036]; chaperone-mediated protein folding [GO:0061077]; chorio-allantoic fusion [GO:0060710]; chorion development [GO:0060717]; extracellular matrix organization [GO:0030198]; intermediate filament organization [GO:0045109]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043154]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of inclusion body assembly [GO:0090084]; protein folding [GO:0006457]; protein localization to nucleus [GO:0034504]; regulation of cellular response to heat [GO:1900034]; regulation of protein localization [GO:0032880]; syncytiotrophoblast cell differentiation involved in labyrinthine layer development [GO:0060715]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; Z disc [GO:0030018]
|
ATPase activator activity [GO:0001671]; DNA binding [GO:0003677]; heat shock protein binding [GO:0031072]; Hsp70 protein binding [GO:0030544]; identical protein binding [GO:0042802]; protein folding chaperone [GO:0044183]; protein-folding chaperone binding [GO:0051087]; unfolded protein binding [GO:0051082]
|
PF00226;
|
1.10.287.110;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:10954706}. Nucleus {ECO:0000269|PubMed:10954706}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:22366786}.
| null | null | null | null | null |
FUNCTION: Has a stimulatory effect on the ATPase activity of HSP70 in a dose-dependent and time-dependent manner and hence acts as a co-chaperone of HSP70 (PubMed:10954706, PubMed:28233300). Plays an indispensable role in the organization of KRT8/KRT18 filaments (PubMed:10954706). Acts as an endogenous molecular chaperone for neuronal proteins including huntingtin (PubMed:11896048, PubMed:22366786). Suppresses aggregation and toxicity of polyglutamine-containing, aggregation-prone proteins (PubMed:20159555, PubMed:22366786). Also reduces cellular toxicity and caspase-3 activity (PubMed:11896048). {ECO:0000269|PubMed:10954706, ECO:0000269|PubMed:11896048, ECO:0000269|PubMed:20159555, ECO:0000269|PubMed:22366786, ECO:0000269|PubMed:28233300}.; FUNCTION: [Isoform B]: Isoform B but not isoform A inhibits huntingtin aggregation. {ECO:0000269|PubMed:20159555, ECO:0000269|PubMed:22366786}.
|
Homo sapiens (Human)
|
O75191
|
XYLB_HUMAN
|
MAEHAPRRCCLGWDFSTQQVKVVAVDAELNVFYEESVHFDRDLPEFGTQGGVHVHKDGLTVTSPVLMWVQALDIILEKMKASGFDFSQVLALSGAGQQHGSIYWKAGAQQALTSLSPDLRLHQQLQDCFSISDCPVWMDSSTTAQCRQLEAAVGGAQALSCLTGSRAYERFTGNQIAKIYQQNPEAYSHTERISLVSSFAASLFLGSYSPIDYSDGSGMNLLQIQDKVWSQACLGACAPHLEEKLSPPVPSCSVVGAISSYYVQRYGFPPGCKVVAFTGDNPASLAGMRLEEGDIAVSLGTSDTLFLWLQEPMPALEGHIFCNPVDSQHYMALLCFKNGSLMREKIRNESVSRSWSDFSKALQSTEMGNGGNLGFYFDVMEITPEIIGRHRFNTENHKVAAFPGDVEVRALIEGQFMAKRIHAEGLGYRVMSKTKILATGGASHNREILQVLADVFDAPVYVIDTANSACVGSAYRAFHGLAGGTDVPFSEVVKLAPNPRLAATPSPGASQVYEALLPQYAKLEQRILSQTRGPPE
|
2.7.1.17
| null |
carbohydrate metabolic process [GO:0005975]; D-xylose metabolic process [GO:0042732]; generation of precursor metabolites and energy [GO:0006091]; glucuronate catabolic process to xylulose 5-phosphate [GO:0019640]; phosphorylation [GO:0016310]; xylulose catabolic process [GO:0005998]; xylulose metabolic process [GO:0005997]
|
cytosol [GO:0005829]
|
ATP binding [GO:0005524]; D-xylulokinase activity [GO:0004856]
|
PF02782;PF00370;
|
3.30.420.40;
|
FGGY kinase family
| null | null |
CATALYTIC ACTIVITY: Reaction=ATP + D-xylulose = ADP + D-xylulose 5-phosphate + H(+); Xref=Rhea:RHEA:10964, ChEBI:CHEBI:15378, ChEBI:CHEBI:17140, ChEBI:CHEBI:30616, ChEBI:CHEBI:57737, ChEBI:CHEBI:456216; EC=2.7.1.17; Evidence={ECO:0000269|PubMed:23179721};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=24 uM for D-xylulose {ECO:0000269|PubMed:23179721};
| null | null | null |
FUNCTION: Phosphorylates D-xylulose to produce D-xylulose 5-phosphate, a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. {ECO:0000269|PubMed:23179721}.
|
Homo sapiens (Human)
|
O75192
|
PX11A_HUMAN
|
MDAFTRFTNQTQGRDRLFRATQYTCMLLRYLLEPKAGKEKVVMKLKKLESSVSTGRKWFRLGNVVHAIQATEQSIHATDLVPRLCLTLANLNRVIYFICDTILWVRSVGLTSGINKEKWRTRAAHHYYYSLLLSLVRDLYEISLQMKRVTCDRAKKEKSASQDPLWFSVAEEETEWLQSFLLLLFRSLKQHPPLLLDTVKNLCDILNPLDQLGIYKSNPGIIGLGGLVSSIAGMITVAYPQMKLKTR
| null | null |
brown fat cell differentiation [GO:0050873]; peroxisome fission [GO:0016559]; peroxisome membrane biogenesis [GO:0016557]; peroxisome organization [GO:0007031]; regulation of peroxisome size [GO:0044375]; signal transduction [GO:0007165]
|
peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777]; protein-containing complex [GO:0032991]
|
protein homodimerization activity [GO:0042803]
|
PF05648;
| null |
Peroxin-11 family
|
PTM: Seems not to be N-glycosylated.
|
SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000269|PubMed:20826455, ECO:0000269|PubMed:9714566, ECO:0000269|PubMed:9792670}; Multi-pass membrane protein {ECO:0000269|PubMed:9714566, ECO:0000269|PubMed:9792670}.
| null | null | null | null | null |
FUNCTION: May be involved in peroxisomal proliferation and may regulate peroxisomes division (PubMed:9792670). May mediate binding of coatomer proteins to the peroxisomal membrane (By similarity). Promotes membrane protrusion and elongation on the peroxisomal surface (PubMed:20826455). {ECO:0000250|UniProtKB:O70597, ECO:0000269|PubMed:20826455, ECO:0000269|PubMed:9792670}.
|
Homo sapiens (Human)
|
O75197
|
LRP5_HUMAN
|
MEAAPPGPPWPLLLLLLLLLALCGCPAPAAASPLLLFANRRDVRLVDAGGVKLESTIVVSGLEDAAAVDFQFSKGAVYWTDVSEEAIKQTYLNQTGAAVQNVVISGLVSPDGLACDWVGKKLYWTDSETNRIEVANLNGTSRKVLFWQDLDQPRAIALDPAHGYMYWTDWGETPRIERAGMDGSTRKIIVDSDIYWPNGLTIDLEEQKLYWADAKLSFIHRANLDGSFRQKVVEGSLTHPFALTLSGDTLYWTDWQTRSIHACNKRTGGKRKEILSALYSPMDIQVLSQERQPFFHTRCEEDNGGCSHLCLLSPSEPFYTCACPTGVQLQDNGRTCKAGAEEVLLLARRTDLRRISLDTPDFTDIVLQVDDIRHAIAIDYDPLEGYVYWTDDEVRAIRRAYLDGSGAQTLVNTEINDPDGIAVDWVARNLYWTDTGTDRIEVTRLNGTSRKILVSEDLDEPRAIALHPVMGLMYWTDWGENPKIECANLDGQERRVLVNASLGWPNGLALDLQEGKLYWGDAKTDKIEVINVDGTKRRTLLEDKLPHIFGFTLLGDFIYWTDWQRRSIERVHKVKASRDVIIDQLPDLMGLKAVNVAKVVGTNPCADRNGGCSHLCFFTPHATRCGCPIGLELLSDMKTCIVPEAFLVFTSRAAIHRISLETNNNDVAIPLTGVKEASALDFDVSNNHIYWTDVSLKTISRAFMNGSSVEHVVEFGLDYPEGMAVDWMGKNLYWADTGTNRIEVARLDGQFRQVLVWRDLDNPRSLALDPTKGYIYWTEWGGKPRIVRAFMDGTNCMTLVDKVGRANDLTIDYADQRLYWTDLDTNMIESSNMLGQERVVIADDLPHPFGLTQYSDYIYWTDWNLHSIERADKTSGRNRTLIQGHLDFVMDILVFHSSRQDGLNDCMHNNGQCGQLCLAIPGGHRCGCASHYTLDPSSRNCSPPTTFLLFSQKSAISRMIPDDQHSPDLILPLHGLRNVKAIDYDPLDKFIYWVDGRQNIKRAKDDGTQPFVLTSLSQGQNPDRQPHDLSIDIYSRTLFWTCEATNTINVHRLSGEAMGVVLRGDRDKPRAIVVNAERGYLYFTNMQDRAAKIERAALDGTEREVLFTTGLIRPVALVVDNTLGKLFWVDADLKRIESCDLSGANRLTLEDANIVQPLGLTILGKHLYWIDRQQQMIERVEKTTGDKRTRIQGRVAHLTGIHAVEEVSLEEFSAHPCARDNGGCSHICIAKGDGTPRCSCPVHLVLLQNLLTCGEPPTCSPDQFACATGEIDCIPGAWRCDGFPECDDQSDEEGCPVCSAAQFPCARGQCVDLRLRCDGEADCQDRSDEADCDAICLPNQFRCASGQCVLIKQQCDSFPDCIDGSDELMCEITKPPSDDSPAHSSAIGPVIGIILSLFVMGGVYFVCQRVVCQRYAGANGPFPHEYVSGTPHVPLNFIAPGGSQHGPFTGIACGKSMMSSVSLMGGRGGVPLYDRNHVTGASSSSSSSTKATLYPPILNPPPSPATDPSLYNMDMFYSSNIPATARPYRPYIIRGMAPPTTPCSTDVCDSDYSASRWKASKYYLDLNSDSDPYPPPPTPHSQYLSAEDSCPPSPATERSYFHLFPPPPSPCTDSS
| null | null |
adipose tissue development [GO:0060612]; amino acid transport [GO:0006865]; anatomical structure regression [GO:0060033]; anterior/posterior pattern specification [GO:0009952]; apoptotic process involved in blood vessel morphogenesis [GO:1902262]; bone marrow development [GO:0048539]; bone morphogenesis [GO:0060349]; bone remodeling [GO:0046849]; branching involved in mammary gland duct morphogenesis [GO:0060444]; canonical Wnt signaling pathway [GO:0060070]; cell migration involved in gastrulation [GO:0042074]; cell-cell adhesion [GO:0098609]; cell-cell signaling involved in mammary gland development [GO:0060764]; cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; embryonic digit morphogenesis [GO:0042733]; endocytosis [GO:0006897]; establishment of blood-brain barrier [GO:0060856]; establishment of blood-retinal barrier [GO:1990963]; extracellular matrix-cell signaling [GO:0035426]; gastrulation with mouth forming second [GO:0001702]; gene expression [GO:0010467]; glucose catabolic process [GO:0006007]; mesodermal cell migration [GO:0008078]; negative regulation of osteoblast differentiation [GO:0045668]; negative regulation of protein serine/threonine kinase activity [GO:0071901]; Norrin signaling pathway [GO:0110135]; osteoblast development [GO:0002076]; osteoblast proliferation [GO:0033687]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of fat cell differentiation [GO:0045600]; positive regulation of mesenchymal cell proliferation [GO:0002053]; positive regulation of mitotic nuclear division [GO:0045840]; positive regulation of osteoblast differentiation [GO:0045669]; positive regulation of osteoblast proliferation [GO:0033690]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of apoptotic process [GO:0042981]; regulation of blood pressure [GO:0008217]; regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0061178]; response to peptide hormone [GO:0043434]; retina morphogenesis in camera-type eye [GO:0060042]; retinal blood vessel morphogenesis [GO:0061304]; somatic stem cell population maintenance [GO:0035019]
|
endoplasmic reticulum [GO:0005783]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]; Wnt signalosome [GO:1990909]; Wnt-Frizzled-LRP5/6 complex [GO:1990851]
|
coreceptor activity [GO:0015026]; Wnt receptor activity [GO:0042813]; Wnt-protein binding [GO:0017147]
|
PF14670;PF00057;PF00058;
|
2.10.25.10;4.10.400.10;2.120.10.30;
|
LDLR family
|
PTM: Phosphorylation of cytoplasmic PPPSP motifs regulates the signal transduction of the Wnt signaling pathway through acting as a docking site for AXIN1.
|
SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q91VN0}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q91VN0}. Endoplasmic reticulum {ECO:0000269|PubMed:25920554}. Note=Chaperoned to the plasma membrane by MESD. {ECO:0000250|UniProtKB:Q91VN0}.
| null | null | null | null | null |
FUNCTION: Acts as a coreceptor with members of the frizzled family of seven-transmembrane spanning receptors to transduce signal by Wnt proteins (PubMed:11336703, PubMed:11448771, PubMed:11719191, PubMed:15778503, PubMed:15908424, PubMed:16252235). Activates the canonical Wnt signaling pathway that controls cell fate determination and self-renewal during embryonic development and adult tissue regeneration (PubMed:11336703, PubMed:11719191). In particular, may play an important role in the development of the posterior patterning of the epiblast during gastrulation (By similarity). During bone development, regulates osteoblast proliferation and differentiation thus determining bone mass (PubMed:11719191). Mechanistically, the formation of the signaling complex between Wnt ligand, frizzled receptor and LRP5 coreceptor promotes the recruitment of AXIN1 to LRP5, stabilizing beta-catenin/CTNNB1 and activating TCF/LEF-mediated transcriptional programs (PubMed:11336703, PubMed:14731402, PubMed:24706814, PubMed:25920554). Acts as a coreceptor for non-Wnt proteins, such as norrin/NDP. Binding of norrin/NDP to frizzled 4/FZD4-LRP5 receptor complex triggers beta-catenin/CTNNB1-dependent signaling known to be required for retinal vascular development (PubMed:16252235, PubMed:27228167). Plays a role in controlling postnatal vascular regression in retina via macrophage-induced endothelial cell apoptosis (By similarity). {ECO:0000250|UniProtKB:Q91VN0, ECO:0000269|PubMed:11336703, ECO:0000269|PubMed:11448771, ECO:0000269|PubMed:11719191, ECO:0000269|PubMed:14731402, ECO:0000269|PubMed:15778503, ECO:0000269|PubMed:15908424, ECO:0000269|PubMed:16252235, ECO:0000269|PubMed:24706814, ECO:0000269|PubMed:25920554, ECO:0000269|PubMed:27228167}.
|
Homo sapiens (Human)
|
O75204
|
TM127_HUMAN
|
MYAPGGAGLPGGRRRRSPGGSALPKQPERSLASALPGALSITALCTALAEPAWLHIHGGTCSRQELGVSDVLGYVHPDLLKDFCMNPQTVLLLRVIAAFCFLGILCSLSAFLLDVFGPKHPALKITRRYAFAHILTVLQCATVIGFSYWASELILAQQQQHKKYHGSQVYVTFAVSFYLVAGAGGASILATAANLLRHYPTEEEEQALELLSEMEENEPYPAEYEVINQFQPPPAYTP
| null | null |
endosome organization [GO:0007032]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of TOR signaling [GO:0032007]; regulation of TOR signaling [GO:0032006]
|
cytoplasm [GO:0005737]; early endosome [GO:0005769]; membrane [GO:0016020]; plasma membrane [GO:0005886]
|
small GTPase binding [GO:0031267]
|
PF20517;
| null |
TMEM127 family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20154675, ECO:0000269|PubMed:21156949}; Multi-pass membrane protein {ECO:0000269|PubMed:20154675}. Cytoplasm {ECO:0000269|PubMed:20154675, ECO:0000269|PubMed:21156949}. Note=Association of TMEM127 with the cell membrane is enhanced by inhibition of endocytosis. In the cytoplasm, it colocalizes with markers of early endosomal structures, Golgi apparatus and lysosomes. {ECO:0000269|PubMed:20154675, ECO:0000269|PubMed:21156949}.
| null | null | null | null | null |
FUNCTION: Controls cell proliferation acting as a negative regulator of TOR signaling pathway mediated by mTORC1. May act as a tumor suppressor. {ECO:0000269|PubMed:20154675}.
|
Homo sapiens (Human)
|
O75208
|
COQ9_HUMAN
|
MAAAAVSGALGRAGWRLLQLRCLPVARCRQALVPRAFHASAVGLRSSDEQKQQPPNSFSQQHSETQGAEKPDPESSHSPPRYTDQGGEEEEDYESEEQLQHRILTAALEFVPAHGWTAEAIAEGAQSLGLSSAAASMFGKDGSELILHFVTQCNTRLTRVLEEEQKLVQLGQAEKRKTDQFLRDAVETRLRMLIPYIEHWPRALSILMLPHNIPSSLSLLTSMVDDMWHYAGDQSTDFNWYTRRAMLAAIYNTTELVMMQDSSPDFEDTWRFLENRVNDAMNMGHTAKQVKSTGEALVQGLMGAAVTLKNLTGLNQRR
| null | null |
mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; ubiquinone biosynthetic process [GO:0006744]
|
mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; ubiquinone biosynthesis complex [GO:0110142]
|
lipid binding [GO:0008289]; protein homodimerization activity [GO:0042803]
|
PF08511;PF21392;
|
1.10.357.10;
|
COQ9 family
| null |
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q8K1Z0}.
| null | null |
PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis. {ECO:0000250|UniProtKB:Q8K1Z0}.
| null | null |
FUNCTION: Lipid-binding protein involved in the biosynthesis of coenzyme Q, also named ubiquinone, an essential lipid-soluble electron transporter for aerobic cellular respiration. Binds a phospholipid of at least 10 carbons in each acyl group. May be required to present its bound-lipid to COQ7. {ECO:0000269|PubMed:25339443}.
|
Homo sapiens (Human)
|
O75223
|
GGCT_HUMAN
|
MANSGCKDVTGPDEESFLYFAYGSNLLTERIHLRNPSAAFFCVARLQDFKLDFGNSQGKTSQTWHGGIATIFQSPGDEVWGVVWKMNKSNLNSLDEQEGVKSGMYVVIEVKVATQEGKEITCRSYLMTNYESAPPSPQYKKIICMGAKENGLPLEYQEKLKAIEPNDYTGKVSEEIEDIIKKGETQTL
|
4.3.2.9
| null |
release of cytochrome c from mitochondria [GO:0001836]
|
cytosol [GO:0005829]; extracellular exosome [GO:0070062]
|
gamma-glutamylcyclotransferase activity [GO:0003839]; protein homodimerization activity [GO:0042803]
|
PF13772;
|
3.10.490.10;
|
Gamma-glutamylcyclotransferase family
| null | null |
CATALYTIC ACTIVITY: Reaction=an alpha-(gamma-L-glutamyl)-L-amino acid = 5-oxo-L-proline + an L-alpha-amino acid; Xref=Rhea:RHEA:20505, ChEBI:CHEBI:58402, ChEBI:CHEBI:59869, ChEBI:CHEBI:71304; EC=4.3.2.9; Evidence={ECO:0000269|PubMed:18515354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20506; Evidence={ECO:0000305|PubMed:18515354};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2 mM for gamma-glutamyl-L-alanine {ECO:0000269|PubMed:18515354}; Vmax=50.3 umol/min/mg enzyme {ECO:0000269|PubMed:18515354};
| null | null | null |
FUNCTION: Catalyzes the formation of 5-oxoproline from gamma-glutamyl dipeptides and may play a significant role in glutathione homeostasis (PubMed:18515354). Induces release of cytochrome c from mitochondria with resultant induction of apoptosis (PubMed:16765912). {ECO:0000269|PubMed:16765912, ECO:0000269|PubMed:18515354}.
|
Homo sapiens (Human)
|
O75251
|
NDUS7_HUMAN
|
MAVLSAPGLRGFRILGLRSSVGPAVQARGVHQSVATDGPSSTQPALPKARAVAPKPSSRGEYVVAKLDDLVNWARRSSLWPMTFGLACCAVEMMHMAAPRYDMDRFGVVFRASPRQSDVMIVAGTLTNKMAPALRKVYDQMPEPRYVVSMGSCANGGGYYHYSYSVVRGCDRIVPVDIYIPGCPPTAEALLYGILQLQRKIKRERRLQIWYRR
|
7.1.1.2
|
COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000305}; Note=Binds 1 [4Fe-4S] cluster. {ECO:0000305};
|
aerobic respiration [GO:0009060]; electron transport coupled proton transport [GO:0015990]; 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 matrix [GO:0005759]; mitochondrial respiratory chain complex I [GO:0005747]; neuronal cell body [GO:0043025]; synaptic membrane [GO:0097060]
|
4 iron, 4 sulfur cluster binding [GO:0051539]; metal ion binding [GO:0046872]; NADH dehydrogenase (ubiquinone) activity [GO:0008137]; oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor [GO:0016655]; protease binding [GO:0002020]; quinone binding [GO:0048038]
|
PF01058;
|
3.40.50.12280;
|
Complex I 20 kDa subunit family
|
PTM: Hydroxylated ar Arg-111 by NDUFAF5 early in the pathway of assembly of complex I, before the formation of the juncture between peripheral and membrane arms. {ECO:0000269|PubMed:27226634}.
|
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305|PubMed:12611891}; Peripheral membrane protein {ECO:0000250|UniProtKB:P42026}; Matrix side {ECO:0000250|UniProtKB:P42026}.
|
CATALYTIC ACTIVITY: Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2; Evidence={ECO:0000269|PubMed:17275378};
| null | null | null | null |
FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor (PubMed:17275378). Essential for the catalytic activity of complex I (PubMed:17275378). {ECO:0000269|PubMed:17275378}.
|
Homo sapiens (Human)
|
O75293
|
GA45B_HUMAN
|
MTLEELVACDNAAQKMQTVTAAVEELLVAAQRQDRLTVGVYESAKLMNVDPDSVVLCLLAIDEEEEDDIALQIHFTLIQSFCCDNDINIVRVSGMQRLAQLLGEPAETQGTTEARDLHCLLVTNPHTDAWKSHGLVEVASYCEESRGNNQWVPYISLQER
| null | null |
apoptotic process [GO:0006915]; cell differentiation [GO:0030154]; positive regulation of apoptotic process [GO:0043065]; positive regulation of JNK cascade [GO:0046330]; positive regulation of p38MAPK cascade [GO:1900745]; regulation of cell cycle [GO:0051726]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]
| null |
PF01248;
|
3.30.1330.30;
|
GADD45 family
| null | null | null | null | null | null | null |
FUNCTION: Involved in the regulation of growth and apoptosis. Mediates activation of stress-responsive MTK1/MEKK4 MAPKKK.
|
Homo sapiens (Human)
|
O75298
|
RTN2_HUMAN
|
MGQVLPVFAHCKEAPSTASSTPDSTEGGNDDSDFRELHTAREFSEEDEEETTSQDWGTPRELTFSYIAFDGVVGSGGRRDSTARRPRPQGRSVSEPRDQHPQPSLGDSLESIPSLSQSPEPGRRGDPDTAPPSERPLEDLRLRLDHLGWVARGTGSGEDSSTSSSTPLEDEEPQEPNRLETGEAGEELDLRLRLAQPSSPEVLTPQLSPGSGTPQAGTPSPSRSRDSNSGPEEPLLEEEEKQWGPLEREPVRGQCLDSTDQLEFTVEPRLLGTAMEWLKTSLLLAVYKTVPILELSPPLWTAIGWVQRGPTPPTPVLRVLLKWAKSPRSSGVPSLSLGADMGSKVADLLYWKDTRTSGVVFTGLMVSLLCLLHFSIVSVAAHLALLLLCGTISLRVYRKVLQAVHRGDGANPFQAYLDVDLTLTREQTERLSHQITSRVVSAATQLRHFFLVEDLVDSLKLALLFYILTFVGAIFNGLTLLILGVIGLFTIPLLYRQHQAQIDQYVGLVTNQLSHIKAKIRAKIPGTGALASAAAAVSGSKAKAE
| null | null |
gene expression [GO:0010467]; intracellular protein transmembrane transport [GO:0065002]; negative regulation of amyloid-beta formation [GO:1902430]; regulation of glucose import [GO:0046324]
|
cell surface [GO:0009986]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; intermediate filament [GO:0005882]; sarcoplasmic reticulum membrane [GO:0033017]; T-tubule [GO:0030315]; terminal cisterna [GO:0014802]; Z disc [GO:0030018]
| null |
PF02453;
|
1.20.5.2480;
| null | null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22232211}; Multi-pass membrane protein {ECO:0000255}. Sarcoplasmic reticulum membrane {ECO:0000250|UniProtKB:O70622}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q6WN19}; Multi-pass membrane protein {ECO:0000255}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:O70622}; Multi-pass membrane protein {ECO:0000255}. Cell membrane, sarcolemma, T-tubule {ECO:0000250|UniProtKB:O70622}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:O70622}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O70622}. Note=Localizes to intermediate filaments in mononucleated myoblasts and to Z lines in mature myotubes. {ECO:0000250|UniProtKB:O70622}.
| null | null | null | null | null |
FUNCTION: Inhibits amyloid precursor protein processing, probably by blocking BACE1 activity (PubMed:15286784). Enhances trafficking of the glutamate transporter SLC1A1/EAAC1 from the endoplasmic reticulum to the cell surface (By similarity). Plays a role in the translocation of SLC2A4/GLUT4 from intracellular membranes to the cell membrane which facilitates the uptake of glucose into the cell (By similarity). {ECO:0000250|UniProtKB:O70622, ECO:0000250|UniProtKB:Q6WN19, ECO:0000269|PubMed:15286784}.
|
Homo sapiens (Human)
|
O75306
|
NDUS2_HUMAN
|
MAALRALCGFRGVAAQVLRPGAGVRLPIQPSRGVRQWQPDVEWAQQFGGAVMYPSKETAHWKPPPWNDVDPPKDTIVKNITLNFGPQHPAAHGVLRLVMELSGEMVRKCDPHIGLLHRGTEKLIEYKTYLQALPYFDRLDYVSMMCNEQAYSLAVEKLLNIRPPPRAQWIRVLFGEITRLLNHIMAVTTHALDLGAMTPFFWLFEEREKMFEFYERVSGARMHAAYIRPGGVHQDLPLGLMDDIYQFSKNFSLRLDELEELLTNNRIWRNRTIDIGVVTAEEALNYGFSGVMLRGSGIQWDLRKTQPYDVYDQVEFDVPVGSRGDCYDRYLCRVEEMRQSLRIIAQCLNKMPPGEIKVDDAKVSPPKRAEMKTSMESLIHHFKLYTEGYQVPPGATYTAIEAPKGEFGVYLVSDGSSRPYRCKIKAPGFAHLAGLDKMSKGHMLADVVAIIGTQDIVFGEVDR
|
7.1.1.2
|
COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Note=Binds 1 [4Fe-4S] cluster.;
|
aerobic respiration [GO:0009060]; cellular response to oxygen levels [GO:0071453]; gliogenesis [GO:0042063]; mitochondrial ATP synthesis coupled electron transport [GO:0042775]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; mitochondrial respiratory chain complex I assembly [GO:0032981]; neural precursor cell proliferation [GO:0061351]; neurogenesis [GO:0022008]; proton motive force-driven mitochondrial ATP synthesis [GO:0042776]; response to oxidative stress [GO:0006979]
|
mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrial respiratory chain complex I [GO:0005747]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]
|
4 iron, 4 sulfur cluster binding [GO:0051539]; electron transfer activity [GO:0009055]; metal ion binding [GO:0046872]; NAD binding [GO:0051287]; NADH dehydrogenase (ubiquinone) activity [GO:0008137]; oxygen sensor activity [GO:0019826]; quinone binding [GO:0048038]; ubiquitin protein ligase binding [GO:0031625]
|
PF00346;
|
1.10.645.10;
|
Complex I 49 kDa subunit family
|
PTM: Dimethylation at Arg-118 by NDUFAF7 takes place after NDUFS2 assembles into the complex I, leading to stabilize the early intermediate complex (PubMed:24089531, PubMed:24838397). {ECO:0000269|PubMed:24089531, ECO:0000269|PubMed:24838397}.
|
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305|PubMed:12611891, ECO:0000305|PubMed:9585441}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q641Y2}; Matrix side {ECO:0000250|UniProtKB:Q641Y2}.
|
CATALYTIC ACTIVITY: Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2; Evidence={ECO:0000269|PubMed:22036843, ECO:0000269|PubMed:30922174};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=10.2 uM for decylubiquinone {ECO:0000269|PubMed:22036843}; KM=55 uM for ubiquinone-1 {ECO:0000269|PubMed:22036843};
| null | null | null |
FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor (PubMed:22036843, PubMed:30922174, PubMed:28031252). Essential for the catalytic activity of complex I (PubMed:22036843, PubMed:30922174). Essential for the assembly of complex I (By similarity). Redox-sensitive, critical component of the oxygen-sensing pathway in the pulmonary vasculature which plays a key role in acute pulmonary oxygen-sensing and hypoxic pulmonary vasoconstriction (PubMed:30922174). Plays an important role in carotid body sensing of hypoxia (By similarity). Essential for glia-like neural stem and progenitor cell proliferation, differentiation and subsequent oligodendrocyte or neuronal maturation (By similarity). {ECO:0000250|UniProtKB:Q91WD5, ECO:0000269|PubMed:22036843, ECO:0000269|PubMed:28031252, ECO:0000269|PubMed:30922174}.
|
Homo sapiens (Human)
|
O75309
|
CAD16_HUMAN
|
MVPAWLWLLCVSVPQALPKAQPAELSVEVPENYGGNFPLYLTKLPLPREGAEGQIVLSGDSGKATEGPFAMDPDSGFLLVTRALDREEQAEYQLQVTLEMQDGHVLWGPQPVLVHVKDENDQVPHFSQAIYRARLSRGTRPGIPFLFLEASDRDEPGTANSDLRFHILSQAPAQPSPDMFQLEPRLGALALSPKGSTSLDHALERTYQLLVQVKDMGDQASGHQATATVEVSIIESTWVSLEPIHLAENLKVLYPHHMAQVHWSGGDVHYHLESHPPGPFEVNAEGNLYVTRELDREAQAEYLLQVRAQNSHGEDYAAPLELHVLVMDENDNVPICPPRDPTVSIPELSPPGTEVTRLSAEDADAPGSPNSHVVYQLLSPEPEDGVEGRAFQVDPTSGSVTLGVLPLRAGQNILLLVLAMDLAGAEGGFSSTCEVEVAVTDINDHAPEFITSQIGPISLPEDVEPGTLVAMLTAIDADLEPAFRLMDFAIERGDTEGTFGLDWEPDSGHVRLRLCKNLSYEAAPSHEVVVVVQSVAKLVGPGPGPGATATVTVLVERVMPPPKLDQESYEASVPISAPAGSFLLTIQPSDPISRTLRFSLVNDSEGWLCIEKFSGEVHTAQSLQGAQPGDTYTVLVEAQDTDEPRLSASAPLVIHFLKAPPAPALTLAPVPSQYLCTPRQDHGLIVSGPSKDPDLASGHGPYSFTLGPNPTVQRDWRLQTLNGSHAYLTLALHWVEPREHIIPVVVSHNAQMWQLLVRVIVCRCNVEGQCMRKVGRMKGMPTKLSAVGILVGTLVAIGIFLILIFTHWTMSRKKDPDQPADSVPLKATV
| null | null |
adherens junction organization [GO:0034332]; calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0016339]; cell adhesion [GO:0007155]; cell morphogenesis [GO:0000902]; cell-cell adhesion mediated by cadherin [GO:0044331]; cell-cell junction assembly [GO:0007043]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]
|
adherens junction [GO:0005912]; basolateral plasma membrane [GO:0016323]; catenin complex [GO:0016342]; extracellular exosome [GO:0070062]
|
cadherin binding [GO:0045296]; calcium ion binding [GO:0005509]
|
PF00028;
|
2.60.40.60;
| null | null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types.
|
Homo sapiens (Human)
|
O75311
|
GLRA3_HUMAN
|
MAHVRHFRTLVSGFYFWEAALLLSLVATKETDSARSRSAPMSPSDFLDKLMGRTSGYDARIRPNFKGPPVNVTCNIFINSFGSIAETTMDYRVNIFLRQKWNDPRLAYSEYPDDSLDLDPSMLDSIWKPDLFFANEKGANFHEVTTDNKLLRIFKNGNVLYSIRLTLTLSCPMDLKNFPMDVQTCIMQLESFGYTMNDLIFEWQDEAPVQVAEGLTLPQFLLKEEKDLRYCTKHYNTGKFTCIEVRFHLERQMGYYLIQMYIPSLLIVILSWVSFWINMDAAPARVALGITTVLTMTTQSSGSRASLPKVSYVKAIDIWMAVCLLFVFSALLEYAAVNFVSRQHKELLRFRRKRKNKTEAFALEKFYRFSDMDDEVRESRFSFTAYGMGPCLQAKDGMTPKGPNHPVQVMPKSPDEMRKVFIDRAKKIDTISRACFPLAFLIFNIFYWVIYKILRHEDIHQQQD
| null | null |
chloride transmembrane transport [GO:1902476]; protein homooligomerization [GO:0051260]; response to amino acid [GO:0043200]
|
dendrite [GO:0030425]; glycine-gated chloride channel complex [GO:0016935]; intracellular membrane-bounded organelle [GO:0043231]; neuron projection [GO:0043005]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; synapse [GO:0045202]; transmembrane transporter complex [GO:1902495]
|
extracellularly glycine-gated chloride channel activity [GO:0016934]; glycine binding [GO:0016594]; glycine-gated chloride ion channel activity [GO:0022852]; metal ion binding [GO:0046872]; neurotransmitter receptor activity [GO:0030594]; transmembrane signaling receptor activity [GO:0004888]; transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential [GO:1904315]
|
PF02931;PF02932;
|
2.70.170.10;1.20.58.390;
|
Ligand-gated ion channel (TC 1.A.9) family, Glycine receptor (TC 1.A.9.3) subfamily, GLRA3 sub-subfamily
|
PTM: Phosphorylated by PKA; this causes down-regulation of channel activity. {ECO:0000250|UniProtKB:P24524}.
|
SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000250|UniProtKB:P24524}; Multi-pass membrane protein {ECO:0000305}. Perikaryon {ECO:0000250|UniProtKB:P24524}. Cell projection, dendrite {ECO:0000250|UniProtKB:P24524}. Synapse {ECO:0000250|UniProtKB:P24524}. Cell membrane {ECO:0000269|PubMed:26416729, ECO:0000269|PubMed:9677400}; Multi-pass membrane protein {ECO:0000269|PubMed:26416729}. Note=Partially colocalizes with GPHN that is known to mediate receptor clustering at postsynaptic membranes. {ECO:0000250|UniProtKB:P24524}.
|
CATALYTIC ACTIVITY: Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823, ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:26416729, ECO:0000269|PubMed:9677400};
| null | null | null | null |
FUNCTION: Glycine receptors are ligand-gated chloride channels. Channel opening is triggered by extracellular glycine (PubMed:26416729, PubMed:9677400). Channel characteristics depend on the subunit composition; heteropentameric channels display faster channel closure (By similarity). Plays an important role in the down-regulation of neuronal excitability (By similarity). Contributes to the generation of inhibitory postsynaptic currents (By similarity). Contributes to increased pain perception in response to increased prostaglandin E2 levels (By similarity). Plays a role in cellular responses to ethanol (By similarity). {ECO:0000250|UniProtKB:P24524, ECO:0000250|UniProtKB:Q91XP5, ECO:0000269|PubMed:26416729, ECO:0000269|PubMed:9677400}.
|
Homo sapiens (Human)
|
O75312
|
ZPR1_HUMAN
|
MAASGAVEPGPPGAAVAPSPAPAPPPAPDHLFRPISAEDEEQQPTEIESLCMNCYCNGMTRLLLTKIPFFREIIVSSFSCEHCGWNNTEIQSAGRIQDQGVRYTLSVRALEDMNREVVKTDSAATRIPELDFEIPAFSQKGALTTVEGLITRAISGLEQDQPARRANKDATAERIDEFIVKLKELKQVASPFTLIIDDPSGNSFVENPHAPQKDDALVITHYNRTRQQEEMLGLQEEAPAEKPEEEDLRNEVLQFSTNCPECNAPAQTNMKLVQIPHFKEVIIMATNCENCGHRTNEVKSGGAVEPLGTRITLHITDASDMTRDLLKSETCSVEIPELEFELGMAVLGGKFTTLEGLLKDIRELVTKNPFTLGDSSNPGQTERLQEFSQKMDQIIEGNMKAHFIMDDPAGNSYLQNVYAPEDDPEMKVERYKRTFDQNEELGLNDMKTEGYEAGLAPQR
| null | null |
apoptotic process involved in development [GO:1902742]; axon development [GO:0061564]; Cajal body organization [GO:0030576]; cellular response to epidermal growth factor stimulus [GO:0071364]; DNA endoreduplication [GO:0042023]; DNA replication [GO:0006260]; inner cell mass cell proliferation [GO:0001833]; microtubule cytoskeleton organization [GO:0000226]; mRNA processing [GO:0006397]; negative regulation of motor neuron apoptotic process [GO:2000672]; positive regulation of cell cycle [GO:0045787]; positive regulation of gene expression [GO:0010628]; positive regulation of growth [GO:0045927]; positive regulation of protein import into nucleus [GO:0042307]; positive regulation of RNA splicing [GO:0033120]; pre-mRNA catabolic process [GO:1990261]; protein folding [GO:0006457]; regulation of myelination [GO:0031641]; RNA splicing [GO:0008380]; signal transduction [GO:0007165]; spinal cord development [GO:0021510]; trophectodermal cell proliferation [GO:0001834]
|
axon [GO:0030424]; Cajal body [GO:0015030]; cytoplasm [GO:0005737]; Gemini of coiled bodies [GO:0097504]; growth cone [GO:0030426]; neuronal cell body [GO:0043025]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perikaryon [GO:0043204]; perinuclear region of cytoplasm [GO:0048471]
|
protein folding chaperone [GO:0044183]; receptor tyrosine kinase binding [GO:0030971]; translation initiation factor binding [GO:0031369]; zinc ion binding [GO:0008270]
|
PF03367;
|
2.60.120.1040;2.20.25.420;
|
ZPR1 family
| null |
SUBCELLULAR LOCATION: Nucleus. Nucleus, nucleolus. Nucleus, gem. Nucleus, Cajal body. Cytoplasm, perinuclear region. Cytoplasm. Cell projection, axon {ECO:0000250}. Cell projection, growth cone {ECO:0000250}. Note=Colocalized with SMN1 in Gemini of coiled bodies (gems), Cajal bodies, axon and growth cones of neurons (By similarity). Localized predominantly in the cytoplasm in serum-starved cells growth arrested in G0 of the mitotic cell cycle. Localized both in the nucleus and cytoplasm at the G1 phase of the mitotic cell cycle. Accumulates in the subnuclear bodies during progression into the S phase of the mitotic cell cycle. Diffusely localized throughout the cell during mitosis. Colocalized with NPAT and SMN1 in nuclear bodies including gems (Gemini of coiled bodies) and Cajal bodies in a cell cycle-dependent manner. Translocates together with EEF1A1 from the cytoplasm to the nucleolus after treatment with mitogens. Colocalized with EGFR in the cytoplasm of quiescent cells. Translocates from the cytoplasm to the nucleus in a epidermal growth factor (EGF)-dependent manner. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Acts as a signaling molecule that communicates proliferative growth signals from the cytoplasm to the nucleus. It is involved in the positive regulation of cell cycle progression (PubMed:29851065). Plays a role for the localization and accumulation of the survival motor neuron protein SMN1 in sub-nuclear bodies, including gems and Cajal bodies. Induces neuron differentiation and stimulates axonal growth and formation of growth cone in spinal cord motor neurons. Plays a role in the splicing of cellular pre-mRNAs. May be involved in H(2)O(2)-induced neuronal cell death. {ECO:0000269|PubMed:11283611, ECO:0000269|PubMed:17068332, ECO:0000269|PubMed:22422766, ECO:0000269|PubMed:29851065}.
|
Homo sapiens (Human)
|
O75317
|
UBP12_HUMAN
|
MEILMTVSKFASICTMGANASALEKEIGPEQFPVNEHYFGLVNFGNTCYCNSVLQALYFCRPFREKVLAYKSQPRKKESLLTCLADLFHSIATQKKKVGVIPPKKFITRLRKENELFDNYMQQDAHEFLNYLLNTIADILQEERKQEKQNGRLPNGNIDNENNNSTPDPTWVHEIFQGTLTNETRCLTCETISSKDEDFLDLSVDVEQNTSITHCLRGFSNTETLCSEYKYYCEECRSKQEAHKRMKVKKLPMILALHLKRFKYMDQLHRYTKLSYRVVFPLELRLFNTSGDATNPDRMYDLVAVVVHCGSGPNRGHYIAIVKSHDFWLLFDDDIVEKIDAQAIEEFYGLTSDISKNSESGYILFYQSRD
|
3.4.19.12
| null |
protein deubiquitination [GO:0016579]; proteolysis [GO:0006508]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
cysteine-type deubiquitinase activity [GO:0004843]; cysteine-type endopeptidase activity [GO:0004197]; metal ion binding [GO:0046872]
|
PF00443;
|
3.90.70.10;
|
Peptidase C19 family, USP12/USP46 subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26811477, ECO:0000269|PubMed:30466959}. Cytoplasm {ECO:0000269|PubMed:26811477, ECO:0000269|PubMed:30466959}. Cell membrane {ECO:0000269|PubMed:30466959}. Note=Translocates from the nucleus to the cytosol on TCR stimulation, while it translocates into the nucleus in IFN signaling. USP12/WDR20/WDR48 complex is localized mainly to the plasma membrane (PubMed:30466959). {ECO:0000269|PubMed:26811477, ECO:0000269|PubMed:30466959, ECO:0000269|PubMed:31899788}.
|
CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000269|PubMed:19075014, ECO:0000269|PubMed:36361894};
| null | null | null | null |
FUNCTION: Deubiquitinating enzyme that plays various roles in the regulation of the immune response and inflammation (PubMed:19075014, PubMed:27373336). In complex with WDR48, acts as a potential tumor suppressor by positively regulating PHLPP1 stability (PubMed:24145035). During TCR engagement and activation, translocates into the cytoplasm and deubiquitinates its substrates LAT and TRAT1 and prevents their lysosome-dependent degradation to stabilize the TCR signaling complex at the plasma membrane (PubMed:26811477). Plays an essential role in the selective LPS-induced macrophage response through the activation of NF-kappa-B pathway (PubMed:28063927). In addition, promotes that antiviral immune response through targeting DNA sensor IFI16 to inhibit its proteasome-dependent degradation (PubMed:37410794). Participates in the interferon signaling pathway and antiviral response independently of its deubiquitinase activity by maintaining nuclear phosphorylated STAT1 levels via inhibition of its CREBBP-mediated acetylation and subsequent dephosphorylation (PubMed:31899788). Plays an intrinsic role in promoting the differentiation, activation and proliferation of CD4(+) T-cell by activating the NF-kappa-B signaling pathway through deubiquitinating and stabilizing B-cell lymphoma/leukemia 10/BCL10 (By similarity). In myeloid-derived suppressor cells promotes the activation of the NF-kappa-B via deubiquitination and stabilization of RELA (By similarity). Regulates the 'Lys-63'-linked polyubiquitin chains of BAX and thereby modulates the mitochondrial apoptotic process (PubMed:36361894). {ECO:0000250|UniProtKB:Q9D9M2, ECO:0000269|PubMed:19075014, ECO:0000269|PubMed:24145035, ECO:0000269|PubMed:26811477, ECO:0000269|PubMed:27373336, ECO:0000269|PubMed:28063927, ECO:0000269|PubMed:31899788, ECO:0000269|PubMed:36361894, ECO:0000269|PubMed:37410794}.; FUNCTION: (Microbial infection) Forms a complex with Epstein-Barr virus protein EBNA3 which is an active deubiquitinase activity that may select specific substrates to promote B-lymphocyte transformation. {ECO:0000269|PubMed:25855980}.
|
Homo sapiens (Human)
|
O75319
|
DUS11_HUMAN
|
MSQWHHPRSGWGRRRDFSGRSSAKKKGGNHIPERWKDYLPVGQRMPGTRFIAFKVPLQKSFEKKLAPEECFSPLDLFNKIREQNEELGLIIDLTYTQRYYKPEDLPETVPYLKIFTVGHQVPDDETIFKFKHAVNGFLKENKDNDKLIGVHCTHGLNRTGYLICRYLIDVEGVRPDDAIELFNRCRGHCLERQNYIEDLQNGPIRKNWNSSVPRSSDFEDSAHLMQPVHNKPVKQGPRYNLHQIQGHSAPRHFHTQTQSLQQSVRKFSENPHVYQRHHLPPPGPPGEDYSHRRYSWNVKPNASRAAQDRRRWYPYNYSRLSYPACWEWTQ
|
3.1.3.-
| null |
protein dephosphorylation [GO:0006470]; RNA processing [GO:0006396]
|
fibrillar center [GO:0001650]; intercellular bridge [GO:0045171]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
phosphatase activity [GO:0016791]; polynucleotide 5'-phosphatase activity [GO:0004651]; protein tyrosine phosphatase activity [GO:0004725]; protein tyrosine/serine/threonine phosphatase activity [GO:0008138]; RNA binding [GO:0003723]
|
PF00782;
|
3.90.190.10;
|
Protein-tyrosine phosphatase family, Non-receptor class dual specificity subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9685386}. Nucleus speckle {ECO:0000269|PubMed:9685386}.
| null | null | null | null | null |
FUNCTION: Possesses RNA 5'-triphosphatase and diphosphatase activities, but displays a poor protein-tyrosine phosphatase activity. In addition, has phosphatase activity with ATP, ADP and O-methylfluorescein phosphate (in vitro). Binds to RNA. May participate in nuclear mRNA metabolism. {ECO:0000269|PubMed:10347225, ECO:0000269|PubMed:24447265, ECO:0000269|PubMed:9685386}.
|
Homo sapiens (Human)
|
O75323
|
NIPS2_HUMAN
|
MAARVLRARGAAWAGGLLQRAAPCSLLPRLRTWTSSSNRSREDSWLKSLFVRKVDPRKDAHSNLLAKKETSNLYKLQFHNVKPECLEAYNKICQEVLPKIHEDKHYPCTLVGTWNTWYGEQDQAVHLWRYEGGYPALTEVMNKLRENKEFLEFRKARSDMLLSRKNQLLLEFSFWNEPVPRSGPNIYELRSYQLRPGTMIEWGNYWARAIRFRQDGNEAVGGFFSQIGQLYMVHHLWAYRDLQTREDIRNAAWHKHGWEELVYYTVPLIQEMESRIMIPLKTSPLQ
| null | null |
mitochondrion organization [GO:0007005]; oxidative phosphorylation [GO:0006119]; positive regulation of high voltage-gated calcium channel activity [GO:1901843]
|
mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]
| null |
PF07978;
|
3.30.70.100;
|
NipSnap family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O55126}. Mitochondrion outer membrane {ECO:0000269|PubMed:26387735}.
| null | null | null | null | null |
FUNCTION: May act as a positive regulator of L-type calcium channels. {ECO:0000250|UniProtKB:O55126}.
|
Homo sapiens (Human)
|
O75324
|
SNN_HUMAN
|
MSIMDHSPTTGVVTVIVILIAIAALGALILGCWCYLRLQRISQSEDEESIVGDGETKEPFLLVQYSAKGPCVERKAKLMTPNGPEVHG
| null | null |
response to toxic substance [GO:0009636]
|
cytoplasm [GO:0005737]; membrane [GO:0016020]; mitochondrial outer membrane [GO:0005741]
|
metal ion binding [GO:0046872]
|
PF09051;PF09050;PF09049;
|
4.10.280.20;
|
Stannin family
| null |
SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:15269288, ECO:0000269|PubMed:16246365}; Single-pass membrane protein {ECO:0000269|PubMed:16246365}.
| null | null | null | null | null |
FUNCTION: Plays a role in the toxic effects of organotins (PubMed:15269288). Plays a role in endosomal maturation (PubMed:27015288). {ECO:0000269|PubMed:15269288, ECO:0000269|PubMed:27015288}.
|
Homo sapiens (Human)
|
O75326
|
SEM7A_HUMAN
|
MTPPPPGRAAPSAPRARVPGPPARLGLPLRLRLLLLLWAAAASAQGHLRSGPRIFAVWKGHVGQDRVDFGQTEPHTVLFHEPGSSSVWVGGRGKVYLFDFPEGKNASVRTVNIGSTKGSCLDKRDCENYITLLERRSEGLLACGTNARHPSCWNLVNGTVVPLGEMRGYAPFSPDENSLVLFEGDEVYSTIRKQEYNGKIPRFRRIRGESELYTSDTVMQNPQFIKATIVHQDQAYDDKIYYFFREDNPDKNPEAPLNVSRVAQLCRGDQGGESSLSVSKWNTFLKAMLVCSDAATNKNFNRLQDVFLLPDPSGQWRDTRVYGVFSNPWNYSAVCVYSLGDIDKVFRTSSLKGYHSSLPNPRPGKCLPDQQPIPTETFQVADRHPEVAQRVEPMGPLKTPLFHSKYHYQKVAVHRMQASHGETFHVLYLTTDRGTIHKVVEPGEQEHSFAFNIMEIQPFRRAAAIQTMSLDAERRKLYVSSQWEVSQVPLDLCEVYGGGCHGCLMSRDPYCGWDQGRCISIYSSERSVLQSINPAEPHKECPNPKPDKAPLQKVSLAPNSRYYLSCPMESRHATYSWRHKENVEQSCEPGHQSPNCILFIENLTAQQYGHYFCEAQEGSYFREAQHWQLLPEDGIMAEHLLGHACALAASLWLGVLPTLTLGLLVH
| null | null |
axon extension [GO:0048675]; axon guidance [GO:0007411]; immune response [GO:0006955]; inflammatory response [GO:0006954]; integrin-mediated signaling pathway [GO:0007229]; negative chemotaxis [GO:0050919]; negative regulation of axon extension involved in axon guidance [GO:0048843]; neural crest cell migration [GO:0001755]; olfactory lobe development [GO:0021988]; osteoblast differentiation [GO:0001649]; positive regulation of axon extension [GO:0045773]; positive regulation of cell migration [GO:0030335]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of macrophage cytokine production [GO:0060907]; positive regulation of protein phosphorylation [GO:0001934]; regulation of inflammatory response [GO:0050727]; semaphorin-plexin signaling pathway [GO:0071526]
|
external side of plasma membrane [GO:0009897]; membrane [GO:0016020]; plasma membrane [GO:0005886]
|
chemorepellent activity [GO:0045499]; integrin binding [GO:0005178]; semaphorin receptor binding [GO:0030215]
|
PF13895;PF01437;PF01403;
|
2.60.40.10;3.30.1680.10;2.130.10.10;
|
Semaphorin family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10201933, ECO:0000269|PubMed:17671519, ECO:0000269|PubMed:9712866}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:10201933, ECO:0000269|PubMed:17671519, ECO:0000269|PubMed:9712866}; Extracellular side {ECO:0000269|PubMed:10201933, ECO:0000269|PubMed:17671519, ECO:0000269|PubMed:9712866}. Note=Detected in a punctate pattern on the cell membrane of basal and supra-basal skin keratinocytes.
| null | null | null | null | null |
FUNCTION: Plays an important role in integrin-mediated signaling and functions both in regulating cell migration and immune responses. Promotes formation of focal adhesion complexes, activation of the protein kinase PTK2/FAK1 and subsequent phosphorylation of MAPK1 and MAPK3. Promotes production of pro-inflammatory cytokines by monocytes and macrophages. Plays an important role in modulating inflammation and T-cell-mediated immune responses. Promotes axon growth in the embryonic olfactory bulb. Promotes attachment, spreading and dendrite outgrowth in melanocytes. {ECO:0000269|PubMed:12879062, ECO:0000269|PubMed:17377534, ECO:0000269|PubMed:17671519}.
|
Homo sapiens (Human)
|
O75330
|
HMMR_HUMAN
|
MSFPKAPLKRFNDPSGCAPSPGAYDVKTLEVLKGPVSFQKSQRFKQQKESKQNLNVDKDTTLPASARKVKSSESKESQKNDKDLKILEKEIRVLLQERGAQDRRIQDLETELEKMEARLNAALREKTSLSANNATLEKQLIELTRTNELLKSKFSENGNQKNLRILSLELMKLRNKRETKMRGMMAKQEGMEMKLQVTQRSLEESQGKIAQLEGKLVSIEKEKIDEKSETEKLLEYIEEISCASDQVEKYKLDIAQLEENLKEKNDEILSLKQSLEENIVILSKQVEDLNVKCQLLEKEKEDHVNRNREHNENLNAEMQNLKQKFILEQQEREKLQQKELQIDSLLQQEKELSSSLHQKLCSFQEEMVKEKNLFEEELKQTLDELDKLQQKEEQAERLVKQLEEEAKSRAEELKLLEEKLKGKEAELEKSSAAHTQATLLLQEKYDSMVQSLEDVTAQFESYKALTASEIEDLKLENSSLQEKAAKAGKNAEDVQHQILATESSNQEYVRMLLDLQTKSALKETEIKEITVSFLQKITDLQNQLKQQEEDFRKQLEDEEGRKAEKENTTAELTEEINKWRLLYEELYNKTKPFQLQLDAFEVEKQALLNEHGAAQEQLNKIRDSYAKLLGHQNLKQKIKHVVKLKDENSQLKSEVSKLRCQLAKKKQSETKLQEELNKVLGIKHFDPSKAFHHESKENFALKTPLKEGNTNCYRAPMECQESWK
| null | null |
hyaluronan catabolic process [GO:0030214]; receptor-mediated endocytosis [GO:0006898]
|
cell surface [GO:0009986]; centrosome [GO:0005813]; cytosol [GO:0005829]; membrane [GO:0016020]; microtubule cytoskeleton [GO:0015630]; plasma membrane [GO:0005886]; spindle [GO:0005819]
|
cargo receptor activity [GO:0038024]; hyaluronic acid binding [GO:0005540]
|
PF15908;PF15905;
| null | null | null |
SUBCELLULAR LOCATION: Cell surface {ECO:0000250|UniProtKB:Q00547}. Cytoplasm {ECO:0000250|UniProtKB:Q00547}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q00547}.
| null | null | null | null | null |
FUNCTION: Receptor for hyaluronic acid (HA) (By similarity). Involved in cell motility (By similarity). When hyaluronan binds to HMMR, the phosphorylation of a number of proteins, including PTK2/FAK1 occurs. May also be involved in cellular transformation and metastasis formation, and in regulating extracellular-regulated kinase (ERK) activity. May act as a regulator of adipogenisis (By similarity). {ECO:0000250|UniProtKB:Q00547}.
|
Homo sapiens (Human)
|
O75334
|
LIPA2_HUMAN
|
MMCEVMPTINEDTPMSQRGSQSSGSDSDSHFEQLMVNMLDERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSALPQDIESLTGGLAGSKGADPPEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGMEPGQKVHEKRLSNGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLKMRTGSLIEPTIPRTHLDTSAELRYSVGSLVDSQSDYRTTKVIRRPRRGRMGVRRDEPKVKSLGDHEWNRTQQIGVLSSHPFESDTEMSDIDDDDRETIFSSMDLLSPSGHSDAQTLAMMLQEQLDAINKEIRLIQEEKESTELRAEEIENRVASVSLEGLNLARVHPGTSITASVTASSLASSSPPSGHSTPKLTPRSPAREMDRMGVMTLPSDLRKHRRKIAVVEEDGREDKATIKCETSPPPTPRALRMTHTLPSSYHNDARSSLSVSLEPESLGLGSANSSQDSLHKAPKKKGIKSSIGRLFGKKEKARLGQLRGFMETEAAAQESLGLGKLGTQAEKDRRLKKKHELLEEARRKGLPFAQWDGPTVVAWLELWLGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLTSPSAPPTSRTPSGNVWVTHEEMENLAAPAKTKESEEGSWAQCPVFLQTLAYGDMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLKRLNYDRKELERRREASQHEIKDVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLLALGTERRLDESDDKNFRRGSTWRRQFPPREVHGISMMPGSSETLPAGFRLTTTSGQSRKMTTDVASSRLQRLDNSTVRTYSC
| null | null |
cell-matrix adhesion [GO:0007160]; dense core granule cytoskeletal transport [GO:0099519]; regulation of dendritic spine development [GO:0060998]; regulation of dendritic spine morphogenesis [GO:0061001]; regulation of synaptic vesicle exocytosis [GO:2000300]; synapse organization [GO:0050808]
|
axon [GO:0030424]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendritic spine [GO:0043197]; extracellular exosome [GO:0070062]; glutamatergic synapse [GO:0098978]; postsynaptic specialization [GO:0099572]; presynaptic active zone [GO:0048786]; presynaptic membrane [GO:0042734]; synaptic vesicle [GO:0008021]
|
structural constituent of presynapse [GO:0099181]
|
PF00536;PF07647;
|
1.10.150.50;
|
Liprin family, Liprin-alpha subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9624153}. Cell surface {ECO:0000269|PubMed:9624153}. Cell projection, dendritic spine {ECO:0000269|PubMed:30021165}. Note=Colocalizes with PTPRF at the cell surface.
| null | null | null | null | null |
FUNCTION: Alters PTPRF cellular localization and induces PTPRF clustering. May regulate the disassembly of focal adhesions. May localize receptor-like tyrosine phosphatases type 2A at specific sites on the plasma membrane, possibly regulating their interaction with the extracellular environment and their association with substrates. In neuronal cells, is a scaffolding protein in the dendritic spines which acts as immobile postsynaptic post able to recruit KIF1A-driven dense core vesicles to dendritic spines (PubMed:30021165). {ECO:0000269|PubMed:30021165, ECO:0000269|PubMed:9624153}.
|
Homo sapiens (Human)
|
O75339
|
CILP1_HUMAN
|
MVGTKAWVFSFLVLEVTSVLGRQTMLTQSVRRVQPGKKNPSIFAKPADTLESPGEWTTWFNIDYPGGKGDYERLDAIRFYYGDRVCARPLRLEARTTDWTPAGSTGQVVHGSPREGFWCLNREQRPGQNCSNYTVRFLCPPGSLRRDTERIWSPWSPWSKCSAACGQTGVQTRTRICLAEMVSLCSEASEEGQHCMGQDCTACDLTCPMGQVNADCDACMCQDFMLHGAVSLPGGAPASGAAIYLLTKTPKLLTQTDSDGRFRIPGLCPDGKSILKITKVKFAPIVLTMPKTSLKAATIKAEFVRAETPYMVMNPETKARRAGQSVSLCCKATGKPRPDKYFWYHNDTLLDPSLYKHESKLVLRKLQQHQAGEYFCKAQSDAGAVKSKVAQLIVIASDETPCNPVPESYLIRLPHDCFQNATNSFYYDVGRCPVKTCAGQQDNGIRCRDAVQNCCGISKTEEREIQCSGYTLPTKVAKECSCQRCTETRSIVRGRVSAADNGEPMRFGHVYMGNSRVSMTGYKGTFTLHVPQDTERLVLTFVDRLQKFVNTTKVLPFNKKGSAVFHEIKMLRRKKPITLEAMETNIIPLGEVVGEDPMAELEIPSRSFYRQNGEPYIGKVKASVTFLDPRNISTATAAQTDLNFINDEGDTFPLRTYGMFSVDFRDEVTSEPLNAGKVKVHLDSTQVKMPEHISTVKLWSLNPDTGLWEEEGDFKFENQRRNKREDRTFLVGNLEIRERRLFNLDVPESRRCFVKVRAYRSERFLPSEQIQGVVISVINLEPRTGFLSNPRAWGRFDSVITGPNGACVPAFCDDQSPDAYSAYVLASLAGEELQAVESSPKFNPNAIGVPQPYLNKLNYRRTDHEDPRVKKTAFQISMAKPRPNSAEESNGPIYAFENLRACEEAPPSAAHFRFYQIEGDRYDYNTVPFNEDDPMSWTEDYLAWWPKPMEFRACYIKVKIVGPLEVNVRSRNMGGTHRQTVGKLYGIRDVRSTRDRDQPNVSAACLEFKCSGMLYDQDRVDRTLVKVIPQGSCRRASVNPMLHEYLVNHLPLAVNNDTSEYTMLAPLDPLGHNYGIYTVTDQDPRTAKEIALGRCFDGTSDGSSRIMKSNVGVALTFNCVERQVGRQSAFQYLQSTPAQSPAAGTVQGRVPSRRQQRASRGGQRQGGVVASLRFPRVAQQPLIN
| null | null |
negative regulation of gene expression [GO:0010629]; negative regulation of insulin-like growth factor receptor signaling pathway [GO:0043569]; negative regulation of SMAD protein signal transduction [GO:0060392]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]
|
collagen-containing extracellular matrix [GO:0062023]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]
| null |
PF13927;PF13330;PF00090;
|
2.60.40.10;2.20.100.10;
| null |
PTM: Cleaved into 2 chains possibly by a furin-like protease upon or preceding secretion.
|
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:15864306}.
| null | null | null | null | null |
FUNCTION: Probably plays a role in cartilage scaffolding. May act by antagonizing TGF-beta1 (TGFB1) and IGF1 functions. Has the ability to suppress IGF1-induced proliferation and sulfated proteoglycan synthesis, and inhibits ligand-induced IGF1R autophosphorylation. May inhibit TGFB1-mediated induction of cartilage matrix genes via its interaction with TGFB1. Overexpression may lead to impair chondrocyte growth and matrix repair and indirectly promote inorganic pyrophosphate (PPi) supersaturation in aging and osteoarthritis cartilage. {ECO:0000269|PubMed:12746903, ECO:0000269|PubMed:15864306}.
|
Homo sapiens (Human)
|
O75340
|
PDCD6_HUMAN
|
MAAYSYRPGPGAGPGPAAGAALPDQSFLWNVFQRVDKDRSGVISDTELQQALSNGTWTPFNPVTVRSIISMFDRENKAGVNFSEFTGVWKYITDWQNVFRTYDRDNSGMIDKNELKQALSGFGYRLSDQFHDILIRKFDRQGRGQIAFDDFIQGCIVLQRLTDIFRRYDTDQDGWIQVSYEQYLSMVFSIV
| null | null |
angiogenesis [GO:0001525]; apoptotic signaling pathway [GO:0097190]; cellular response to heat [GO:0034605]; COPII vesicle coating [GO:0048208]; endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; intracellular protein transport [GO:0006886]; negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051898]; negative regulation of TOR signaling [GO:0032007]; negative regulation of vascular endothelial growth factor receptor signaling pathway [GO:0030948]; neural crest cell development [GO:0014032]; neural crest formation [GO:0014029]; positive regulation of angiogenesis [GO:0045766]; positive regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043280]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of endothelial cell proliferation [GO:0001938]; positive regulation of protein monoubiquitination [GO:1902527]; response to calcium ion [GO:0051592]; vascular endothelial growth factor receptor-2 signaling pathway [GO:0036324]
|
COPII vesicle coat [GO:0030127]; Cul3-RING ubiquitin ligase complex [GO:0031463]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum exit site [GO:0070971]; endoplasmic reticulum membrane [GO:0005789]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
calcium ion binding [GO:0005509]; calcium-dependent protein binding [GO:0048306]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; protein dimerization activity [GO:0046983]; protein homodimerization activity [GO:0042803]; protein-macromolecule adaptor activity [GO:0030674]; protein-membrane adaptor activity [GO:0043495]; ubiquitin ligase-substrate adaptor activity [GO:1990756]
|
PF13499;
|
1.10.238.10;
| null | null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16957052, ECO:0000269|PubMed:27813252}; Peripheral membrane protein {ECO:0000269|PubMed:16957052}. Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000269|PubMed:27716508}. Cytoplasm {ECO:0000269|PubMed:27716508, ECO:0000269|PubMed:27784779}. Nucleus {ECO:0000269|PubMed:17045351, ECO:0000269|PubMed:21122810, ECO:0000269|PubMed:27784779}. Endosome {ECO:0000269|PubMed:19864416}. Note=Interaction with RBM22 induces relocalization from the cytoplasm to the nucleus (PubMed:17045351). Translocated from the cytoplasm to the nucleus after heat shock cell treatment. Accumulates in cytoplasmic vesicle-like organelles after heat shock treatment, which may represent stress granules (PubMed:21122810). In response to calcium increase, relocates from cytoplasm to COPII vesicle coat (PubMed:27716508). Localizes to endoplasmic reticulum exit site (ERES) (PubMed:27813252). {ECO:0000269|PubMed:17045351, ECO:0000269|PubMed:21122810, ECO:0000269|PubMed:27716508, ECO:0000269|PubMed:27813252}.
| null | null | null | null | null |
FUNCTION: Calcium sensor that plays a key role in processes such as endoplasmic reticulum (ER)-Golgi vesicular transport, endosomal biogenesis or membrane repair. Acts as an adapter that bridges unrelated proteins or stabilizes weak protein-protein complexes in response to calcium: calcium-binding triggers exposure of apolar surface, promoting interaction with different sets of proteins thanks to 3 different hydrophobic pockets, leading to translocation to membranes (PubMed:20691033, PubMed:25667979). Involved in ER-Golgi transport by promoting the association between PDCD6IP and TSG101, thereby bridging together the ESCRT-III and ESCRT-I complexes (PubMed:19520058). Together with PEF1, acts as a calcium-dependent adapter for the BCR(KLHL12) complex, a complex involved in ER-Golgi transport by regulating the size of COPII coats (PubMed:27716508). In response to cytosolic calcium increase, the heterodimer formed with PEF1 interacts with, and bridges together the BCR(KLHL12) complex and SEC31 (SEC31A or SEC31B), promoting monoubiquitination of SEC31 and subsequent collagen export, which is required for neural crest specification (PubMed:27716508). Involved in the regulation of the distribution and function of MCOLN1 in the endosomal pathway (PubMed:19864416). Promotes localization and polymerization of TFG at endoplasmic reticulum exit site (PubMed:27813252). Required for T-cell receptor-, Fas-, and glucocorticoid-induced apoptosis (By similarity). May mediate Ca(2+)-regulated signals along the death pathway: interaction with DAPK1 can accelerate apoptotic cell death by increasing caspase-3 activity (PubMed:16132846). Its role in apoptosis may however be indirect, as suggested by knockout experiments (By similarity). May inhibit KDR/VEGFR2-dependent angiogenesis; the function involves inhibition of VEGF-induced phosphorylation of the Akt signaling pathway (PubMed:21893193). In case of infection by HIV-1 virus, indirectly inhibits HIV-1 production by affecting viral Gag expression and distribution (PubMed:27784779). {ECO:0000250|UniProtKB:P12815, ECO:0000269|PubMed:16132846, ECO:0000269|PubMed:19520058, ECO:0000269|PubMed:19864416, ECO:0000269|PubMed:20691033, ECO:0000269|PubMed:21893193, ECO:0000269|PubMed:25667979, ECO:0000269|PubMed:27716508, ECO:0000269|PubMed:27784779, ECO:0000269|PubMed:27813252}.; FUNCTION: [Isoform 2]: Has a lower Ca(2+) affinity than isoform 1 (By similarity). {ECO:0000250|UniProtKB:P12815}.
|
Homo sapiens (Human)
|
O75342
|
LX12B_HUMAN
|
MATYKVRVATGTDLLSGTRDSISLTIVGTQGESHKQLLNHFGRDFATGAVGQYTVQCPQDLGELIIIRLHKERYAFFPKDPWYCNYVQICAPNGRIYHFPAYQWMDGYETLALREATGKTTADDSLPVLLEHRKEEIRAKQDFYHWRVFLPGLPSYVHIPSYRPPVRRHRNPNRPEWNGYIPGFPILINFKATKFLNLNLRYSFLKTASFFVRLGPMALAFKVRGLLDCKHSWKRLKDIRKIFPGKKSVVSEYVAEHWAEDTFFGYQYLNGVNPGLIRRCTRIPDKFPVTDDMVAPFLGEGTCLQAELEKGNIYLADYRIMEGIPTVELSGRKQHHCAPLCLLHFGPEGKMMPIAIQLSQTPGPDCPIFLPSDSEWDWLLAKTWVRYAEFYSHEAIAHLLETHLIAEAFCLALLRNLPMCHPLYKLLIPHTRYTVQINSIGRAVLLNEGGLSAKGMSLGVEGFAGVMVRALSELTYDSLYLPNDFVERGVQDLPGYYYRDDSLAVWNALEKYVTEIITYYYPSDAAVEGDPELQSWVQEIFKECLLGRESSGFPRCLRTVPELIRYVTIVIYTCSAKHAAVNTGQMEFTAWMPNFPASMRNPPIQTKGLTTLETFMDTLPDVKTTCITLLVLWTLSREPDDRRPLGHFPDIHFVEEAPRRSIEAFRQRLNQISHDIRQRNKCLPIPYYYLDPVLIENSISI
|
1.13.11.-
|
COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000255|PROSITE-ProRule:PRU00726}; Note=Binds 1 Fe cation per subunit. {ECO:0000255|PROSITE-ProRule:PRU00726};
|
arachidonic acid metabolic process [GO:0019369]; ceramide biosynthetic process [GO:0046513]; establishment of skin barrier [GO:0061436]; hepoxilin biosynthetic process [GO:0051122]; linoleic acid metabolic process [GO:0043651]; lipid oxidation [GO:0034440]; lipoxygenase pathway [GO:0019372]; positive regulation of gene expression [GO:0010628]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of mucus secretion [GO:0070257]; protein lipidation [GO:0006497]; sphingolipid metabolic process [GO:0006665]
|
cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; perinuclear region of cytoplasm [GO:0048471]
|
arachidonate 12(R)-lipoxygenase activity [GO:0106237]; arachidonate 12(S)-lipoxygenase activity [GO:0004052]; arachidonate 8(R)-lipoxygenase activity [GO:0047677]; iron ion binding [GO:0005506]; isomerase activity [GO:0016853]; linoleate 9S-lipoxygenase activity [GO:1990136]; lyase activity [GO:0016829]; oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen [GO:0016702]
|
PF00305;PF01477;
|
3.10.450.60;2.60.60.20;
|
Lipoxygenase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00726}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:9837935}.
|
CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = (12R)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate; Xref=Rhea:RHEA:41336, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:75230; Evidence={ECO:0000269|PubMed:9618483, ECO:0000269|PubMed:9837935}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41337; Evidence={ECO:0000305|PubMed:9837935}; CATALYTIC ACTIVITY: Reaction=N-[omega-(9Z,12Z)-octadecadienoyloxy]acyl-beta-D-glucosyl-(1<->1)-octadecasphing-4E-enine + O2 = N-[omega-(9R)-hydroperoxy-(10E,12Z)-octadecadienoyloxy]acyl-beta-D-glucosyl-(1<->1)-octadecasphing-4E-enine; Xref=Rhea:RHEA:40495, ChEBI:CHEBI:15379, ChEBI:CHEBI:134621, ChEBI:CHEBI:134624; Evidence={ECO:0000269|PubMed:21558561}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40496; Evidence={ECO:0000305|PubMed:21558561}; CATALYTIC ACTIVITY: Reaction=N-[omega-(9Z,12Z)-octadecadienoyloxy]-acylsphin-4-enine + O2 = N-acyl (9R)-hydroperoxy-(10E,12Z)-octadecadienoate octadecasphing-4E-enine; Xref=Rhea:RHEA:41239, ChEBI:CHEBI:15379, ChEBI:CHEBI:77888, ChEBI:CHEBI:77889; Evidence={ECO:0000269|PubMed:21558561}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41240; Evidence={ECO:0000305|PubMed:21558561}; CATALYTIC ACTIVITY: Reaction=(6Z,9Z,12Z)-octadecatrienoate + O2 = 10-hydroperoxy-(6Z,8E,12Z)-octadecatrienoate; Xref=Rhea:RHEA:43476, ChEBI:CHEBI:15379, ChEBI:CHEBI:32391, ChEBI:CHEBI:83342; Evidence={ECO:0000269|PubMed:9837935}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43477; Evidence={ECO:0000305|PubMed:9837935}; CATALYTIC ACTIVITY: Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 = 14-hydroperoxy-(4Z,7Z,10Z,12E,16Z,19Z)-docosahexaenoate; Xref=Rhea:RHEA:43472, ChEBI:CHEBI:15379, ChEBI:CHEBI:77016, ChEBI:CHEBI:83336; Evidence={ECO:0000269|PubMed:9837935}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43473; Evidence={ECO:0000305|PubMed:9837935}; CATALYTIC ACTIVITY: Reaction=(8Z,11Z,14Z)-eicosatrienoate + O2 = (8Z,10E,14Z)-12-hydroperoxyeicosatrienoate; Xref=Rhea:RHEA:43468, ChEBI:CHEBI:15379, ChEBI:CHEBI:71589, ChEBI:CHEBI:83334; Evidence={ECO:0000269|PubMed:9837935}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43469; Evidence={ECO:0000305|PubMed:9837935}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 = (5Z,7Z,8Z,10E,14Z,17Z)-12-hydroperoxyeicosapentaenoate; Xref=Rhea:RHEA:41344, ChEBI:CHEBI:15379, ChEBI:CHEBI:58562, ChEBI:CHEBI:78078; Evidence={ECO:0000269|PubMed:9837935}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41345; Evidence={ECO:0000305|PubMed:9837935}; CATALYTIC ACTIVITY: Reaction=(6Z,9Z,12Z)-octadecatrienoate + O2 = 10R-hydroperoxy-(6Z,8E,12Z)-octadecatrienoate; Xref=Rhea:RHEA:41340, ChEBI:CHEBI:15379, ChEBI:CHEBI:32391, ChEBI:CHEBI:78070; Evidence={ECO:0000269|PubMed:9837935}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41341; Evidence={ECO:0000305|PubMed:9837935}; CATALYTIC ACTIVITY: Reaction=1-O-methyl-(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = 1-O-methyl (5Z,8Z,10E,12R,14Z)-hydroperoxyiecosatetraenoate; Xref=Rhea:RHEA:41311, ChEBI:CHEBI:15379, ChEBI:CHEBI:78033, ChEBI:CHEBI:78034; Evidence={ECO:0000250|UniProtKB:O70582}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41312; Evidence={ECO:0000250|UniProtKB:O70582}; CATALYTIC ACTIVITY: Reaction=1-O-methyl-(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = 1-O-methyl-8-hydroperoxy-(5Z,9E,11Z,14Z)-eicosatetraenoate; Xref=Rhea:RHEA:43480, ChEBI:CHEBI:15379, ChEBI:CHEBI:78033, ChEBI:CHEBI:83344; Evidence={ECO:0000250|UniProtKB:O70582}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43481; Evidence={ECO:0000250|UniProtKB:O70582}; CATALYTIC ACTIVITY: Reaction=1-O-methyl-(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = 1-O-methyl-(8R)-hydroperoxy-(5Z,9E,11Z,14Z)-eicosatrienoate; Xref=Rhea:RHEA:61868, ChEBI:CHEBI:15379, ChEBI:CHEBI:78033, ChEBI:CHEBI:78180; Evidence={ECO:0000250|UniProtKB:O70582}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61869; Evidence={ECO:0000250|UniProtKB:O70582}; CATALYTIC ACTIVITY: Reaction=1-O-methyl-(9Z,12Z)-octadecadienoate + O2 = 1-O-methyl-(9R)-hydroperoxy-(10E,12Z)-octadecadienoate; Xref=Rhea:RHEA:61872, ChEBI:CHEBI:15379, ChEBI:CHEBI:69080, ChEBI:CHEBI:145036; Evidence={ECO:0000250|UniProtKB:O70582}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61873; Evidence={ECO:0000250|UniProtKB:O70582}; CATALYTIC ACTIVITY: Reaction=1-O-methyl-20-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = 1-O-methyl-8-hydroperoxy-20-hydroxy-(5Z,9E,11Z,14Z)-eicosatetraenoate; Xref=Rhea:RHEA:61876, ChEBI:CHEBI:15379, ChEBI:CHEBI:145032, ChEBI:CHEBI:145033; Evidence={ECO:0000250|UniProtKB:O70582}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61877; Evidence={ECO:0000250|UniProtKB:O70582}; CATALYTIC ACTIVITY: Reaction=1-O-methyl-20-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = 1-O-methyl-12-hydroperoxy-20-hydroxy-(5Z,8Z,10E,14Z)-eicosatetraenoate; Xref=Rhea:RHEA:61880, ChEBI:CHEBI:15379, ChEBI:CHEBI:145032, ChEBI:CHEBI:145034; Evidence={ECO:0000250|UniProtKB:O70582}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61881; Evidence={ECO:0000250|UniProtKB:O70582}; CATALYTIC ACTIVITY: Reaction=1-O-methyl-20-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = 1-O-methyl-9-hydroperoxy-20-hydroxy-(5Z,7E,11Z,14Z)-eicosatetraenoate; Xref=Rhea:RHEA:61884, ChEBI:CHEBI:15379, ChEBI:CHEBI:145032, ChEBI:CHEBI:145035; Evidence={ECO:0000250|UniProtKB:O70582}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61885; Evidence={ECO:0000250|UniProtKB:O70582}; CATALYTIC ACTIVITY: Reaction=1-O-methyl-(9Z,12Z)-octadecadienoate + O2 = 1-O-methyl-(13S)-hydroperoxy-(9Z,11E)-octadecadienoate; Xref=Rhea:RHEA:41756, ChEBI:CHEBI:15379, ChEBI:CHEBI:69080, ChEBI:CHEBI:78040; Evidence={ECO:0000250|UniProtKB:O70582}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41757; Evidence={ECO:0000250|UniProtKB:O70582};
| null |
PATHWAY: Lipid metabolism; hydroperoxy eicosatetraenoic acid biosynthesis. {ECO:0000269|PubMed:21558561}.; PATHWAY: Lipid metabolism; sphingolipid metabolism. {ECO:0000269|PubMed:21558561}.
| null | null |
FUNCTION: Catalyzes the regio and stereo-specific incorporation of a single molecule of dioxygen into free and esterified polyunsaturated fatty acids generating lipid hydroperoxides that can be further reduced to the corresponding hydroxy species (PubMed:21558561, PubMed:9618483, PubMed:9837935). In the skin, acts upstream of ALOXE3 on the lineolate moiety of esterified omega-hydroxyacyl-sphingosine (EOS) ceramides to produce an epoxy-ketone derivative, a crucial step in the conjugation of omega-hydroxyceramide to membrane proteins (PubMed:21558561). Therefore plays a crucial role in the synthesis of corneocytes lipid envelope and the establishment of the skin barrier to water loss (PubMed:21558561). May also play a role in the regulation of the expression of airway mucins (PubMed:22441738). {ECO:0000269|PubMed:21558561, ECO:0000269|PubMed:22441738, ECO:0000269|PubMed:9618483, ECO:0000269|PubMed:9837935}.
|
Homo sapiens (Human)
|
O75343
|
GCYB2_HUMAN
|
MSGYDRMLRTLGGNLMEFIENLDALHSYLALSYQEMNAPSFRVERGADGKMFLHYYSDRSGLCHIVPGIIEAVAKDFFDIDVIMDILDMNEEVERTGKKEHVVFLIVQKAHRKMRKTKPKRLQDSQGMERDQEALQAAFLKMKEKYLNVSACPVKKSHWDVVRSIVMFGKGHLMNTFEPIYPERLWIEEKTFCNAFPFHIVFDESLQVKQARVNIQKYVPGLQTQNIQLDEYFSIIHPQVTFNIFSIRRFINSQFVLKTRREMMPVAWQSRTTLKLQGQMIWMESMWCMVYLCSPKLRSLQELEELNMHLSDIAPNDTTRDLILLNQQRLAEIELSNQLERKKEELQVLSKHLAIEKKKTETLLYAMLPKHVANQLREGKKVAAGEFKSCTILFSDVVTFTNICTACEPIQIVNVLNSMYSKFDRLTSVHAVYKVETIGDAYMVVGGVPVPIGNHAQRVANFALGMRISAKEVTNPVTGEPIQLRVGIHTGPVLADVVGDKMPRYCLFGDTVNTASRMESHGLPNKVHLSPTAYRALKNQGFKIIERGEIEVKGKGRMTTYFLIQNLNATEDEIMGRSKTPVDHKGSTQKASLPTTKLQGSVQPSCPEHSSLASWLL
|
4.6.1.2
|
COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250}; Note=Binds 1 or 2 heme groups per heterodimer. {ECO:0000250};
|
cGMP-mediated signaling [GO:0019934]; response to oxygen levels [GO:0070482]
|
cytosol [GO:0005829]; guanylate cyclase complex, soluble [GO:0008074]
|
GTP binding [GO:0005525]; guanylate cyclase activity [GO:0004383]; heme binding [GO:0020037]; metal ion binding [GO:0046872]
|
PF00211;PF07700;PF07701;
|
6.10.250.780;3.90.1520.10;3.30.450.260;3.30.70.1230;
|
Adenylyl cyclase class-4/guanylyl cyclase family
| null |
SUBCELLULAR LOCATION: Cytoplasm.
|
CATALYTIC ACTIVITY: Reaction=GTP = 3',5'-cyclic GMP + diphosphate; Xref=Rhea:RHEA:13665, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57746; EC=4.6.1.2;
| null | null | null | null | null |
Homo sapiens (Human)
|
O75344
|
FKBP6_HUMAN
|
MGGSALNQGVLEGDDAPGQSLYERLSQRMLDISGDRGVLKDVIREGAGDLVAPDASVLVKYSGYLEHMDRPFDSNYFRKTPRLMKLGEDITLWGMELGLLSMRRGELARFLFKPNYAYGTLGCPPLIPPNTTVLFEIELLDFLDCAESDKFCALSAEQQDQFPLQKVLKVAATEREFGNYLFRQNRFYDAKVRYKRALLLLRRRSAPPEEQHLVEAAKLPVLLNLSFTYLKLDRPTIALCYGEQALIIDQKNAKALFRCGQACLLLTEYQKARDFLVRAQKEQPFNHDINNELKKLASCYRDYVDKEKEMWHRMFAPCGDGSTAGES
| null | null |
cell differentiation [GO:0030154]; meiotic cell cycle [GO:0051321]; piRNA processing [GO:0034587]; positive regulation of viral genome replication [GO:0045070]; protein folding [GO:0006457]; regulatory ncRNA-mediated gene silencing [GO:0031047]; siRNA-mediated retrotransposon silencing by heterochromatin formation [GO:0141007]; spermatogenesis [GO:0007283]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; synaptonemal complex [GO:0000795]
|
FK506 binding [GO:0005528]; Hsp90 protein binding [GO:0051879]; identical protein binding [GO:0042802]
|
PF00254;
|
3.10.50.40;1.25.40.10;
|
FKBP6 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:36150389}. Nucleus {ECO:0000269|PubMed:36150389}. Note=In spermatocytes, it colocalizes with PIWIL1 in large cytoplasmic granules (PubMed:36150389). Does not localize to the synaptonemal complex (PubMed:36150389). {ECO:0000269|PubMed:36150389}.
| null | null | null | null | null |
FUNCTION: Has an essential role in spermatogenesis (PubMed:36150389). It is required to repress transposable elements and prevent their mobilization, which is essential for the germline integrity (By similarity). Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and govern the methylation and subsequent repression of transposons (By similarity). Acts as a co-chaperone via its interaction with HSP90 and is required for the piRNA amplification process, the secondary piRNA biogenesis (By similarity). May be required together with HSP90 in removal of 16 nucleotide ping-pong by-products from Piwi complexes, possibly facilitating turnover of Piwi complexes (By similarity). {ECO:0000250|UniProtKB:Q91XW8, ECO:0000269|PubMed:36150389}.
|
Homo sapiens (Human)
|
O75347
|
TBCA_HUMAN
|
MADPRVRQIKIKTGVVKRLVKEKVMYEKEAKQQEEKIEKMRAEDGENYDIKKQAEILQESRMMIPDCQRRLEAAYLDLQRILENEKDLEEAEEYKEARLVLDSVKLEA
| null | null |
post-chaperonin tubulin folding pathway [GO:0007023]; protein folding [GO:0006457]; tubulin complex assembly [GO:0007021]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; microtubule [GO:0005874]; microtubule cytoskeleton [GO:0015630]; nucleolus [GO:0005730]
|
beta-tubulin binding [GO:0048487]; protein-folding chaperone binding [GO:0051087]; RNA binding [GO:0003723]; tubulin binding [GO:0015631]
|
PF02970;
|
1.20.58.90;
|
TBCA family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
| null | null | null | null | null |
FUNCTION: Tubulin-folding protein; involved in the early step of the tubulin folding pathway.
|
Homo sapiens (Human)
|
O75348
|
VATG1_HUMAN
|
MASQSQGIQQLLQAEKRAAEKVSEARKRKNRRLKQAKEEAQAEIEQYRLQREKEFKAKEAAALGSRGSCSTEVEKETQEKMTILQTYFRQNRDEVLDNLLAFVCDIRPEIHENYRING
| null | null |
cellular response to increased oxygen levels [GO:0036295]; intracellular iron ion homeostasis [GO:0006879]; regulation of macroautophagy [GO:0016241]; synaptic vesicle lumen acidification [GO:0097401]
|
apical plasma membrane [GO:0016324]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; lysosomal membrane [GO:0005765]; plasma membrane [GO:0005886]; synaptic vesicle membrane [GO:0030672]; transmembrane transporter complex [GO:1902495]; vacuolar proton-transporting V-type ATPase, V1 domain [GO:0000221]
|
ATP hydrolysis activity [GO:0016887]; ATPase binding [GO:0051117]; proton-transporting ATPase activity, rotational mechanism [GO:0046961]
|
PF03179;
|
1.20.5.2950;
|
V-ATPase G subunit family
| null |
SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:29993276}.
| null | null | null | null | null |
FUNCTION: Subunit of the V1 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:32001091, 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 (PubMed:32001091). In aerobic conditions, involved in intracellular iron homeostasis, thus triggering the activity of Fe(2+) prolyl hydroxylase (PHD) enzymes, and leading to HIF1A hydroxylation and subsequent proteasomal degradation (PubMed:28296633). {ECO:0000269|PubMed:28296633, ECO:0000269|PubMed:33065002, ECO:0000303|PubMed:32001091}.
|
Homo sapiens (Human)
|
O75351
|
VPS4B_HUMAN
|
MSSTSPNLQKAIDLASKAAQEDKAGNYEEALQLYQHAVQYFLHVVKYEAQGDKAKQSIRAKCTEYLDRAEKLKEYLKNKEKKAQKPVKEGQPSPADEKGNDSDGEGESDDPEKKKLQNQLQGAIVIERPNVKWSDVAGLEGAKEALKEAVILPIKFPHLFTGKRTPWRGILLFGPPGTGKSYLAKAVATEANNSTFFSISSSDLVSKWLGESEKLVKNLFQLARENKPSIIFIDEIDSLCGSRSENESEAARRIKTEFLVQMQGVGVDNDGILVLGATNIPWVLDSAIRRRFEKRIYIPLPEPHARAAMFKLHLGTTQNSLTEADFRELGRKTDGYSGADISIIVRDALMQPVRKVQSATHFKKVRGPSRADPNHLVDDLLTPCSPGDPGAIEMTWMDVPGDKLLEPVVSMSDMLRSLSNTKPTVNEHDLLKLKKFTEDFGQEG
|
3.6.4.6
| null |
angiogenesis [GO:0001525]; autophagosome maturation [GO:0097352]; autophagy [GO:0006914]; canonical Wnt signaling pathway [GO:0060070]; cholesterol transport [GO:0030301]; endosomal transport [GO:0016197]; endosome to lysosome transport via multivesicular body sorting pathway [GO:0032510]; ESCRT III complex disassembly [GO:1904903]; establishment of blood-brain barrier [GO:0060856]; late endosomal microautophagy [GO:0061738]; late endosome to lysosome transport via multivesicular body sorting pathway [GO:0061764]; macroautophagy [GO:0016236]; membrane fission [GO:0090148]; midbody abscission [GO:0061952]; mitotic metaphase chromosome alignment [GO:0007080]; multivesicular body assembly [GO:0036258]; multivesicular body sorting pathway [GO:0071985]; negative regulation of exosomal secretion [GO:1903542]; nuclear membrane reassembly [GO:0031468]; nucleus organization [GO:0006997]; plasma membrane repair [GO:0001778]; positive regulation of centriole elongation [GO:1903724]; positive regulation of exosomal secretion [GO:1903543]; positive regulation of G2/M transition of mitotic cell cycle [GO:0010971]; potassium ion transport [GO:0006813]; protein depolymerization [GO:0051261]; protein transport [GO:0015031]; regulation of centrosome duplication [GO:0010824]; regulation of mitotic spindle assembly [GO:1901673]; response to lipid [GO:0033993]; ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway [GO:0043162]; ubiquitin-independent protein catabolic process via the multivesicular body sorting pathway [GO:0090611]; vacuole organization [GO:0007033]; viral budding from plasma membrane [GO:0046761]; viral budding via host ESCRT complex [GO:0039702]
|
ATPase complex [GO:1904949]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endosome [GO:0005768]; endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; Flemming body [GO:0090543]; late endosome membrane [GO:0031902]; midbody [GO:0030496]; nuclear pore [GO:0005643]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; spindle pole [GO:0000922]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]; protein-containing complex binding [GO:0044877]
|
PF00004;PF17862;PF04212;PF09336;
|
1.10.8.60;3.40.50.300;1.20.58.80;
|
AAA ATPase family
| null |
SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000250|UniProtKB:P46467}; Peripheral membrane protein {ECO:0000305}. Note=Membrane-associated in the prevacuolar endosomal compartment. Localized in HIV-1 particles purified from acutely infected cells. {ECO:0000269|PubMed:14505570}.
|
CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.6; Evidence={ECO:0000269|PubMed:18687924}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066; Evidence={ECO:0000305|PubMed:18687924};
| null | null | null | null |
FUNCTION: Involved in late steps of the endosomal multivesicular bodies (MVB) pathway. Recognizes membrane-associated ESCRT-III assemblies and catalyzes their ATP-dependent disassembly, possibly in combination with membrane fission (PubMed:18687924). Redistributes the ESCRT-III components to the cytoplasm for further rounds of MVB sorting. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. VPS4A/B are required for the exosomal release of SDCBP, CD63 and syndecan (PubMed:22660413). {ECO:0000269|PubMed:11563910, ECO:0000269|PubMed:18687924, ECO:0000269|PubMed:22660413}.; FUNCTION: (Microbial infection) In conjunction with the ESCRT machinery also appears to function in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and enveloped virus budding (HIV-1 and other lentiviruses). {ECO:0000269|PubMed:14505570, ECO:0000269|PubMed:16193069, ECO:0000269|PubMed:18606141}.
|
Homo sapiens (Human)
|
O75354
|
ENTP6_HUMAN
|
MKKGIRYETSRKTSYIFQQPQHGPWQTRMRKISNHGSLRVAKVAYPLGLCVGVFIYVAYIKWHRATATQAFFSITRAAPGARWGQQAHSPLGTAADGHEVFYGIMFDAGSTGTRVHVFQFTRPPRETPTLTHETFKALKPGLSAYADDVEKSAQGIRELLDVAKQDIPFDFWKATPLVLKATAGLRLLPGEKAQKLLQKVKKVFKASPFLVGDDCVSIMNGTDEGVSAWITINFLTGSLKTPGGSSVGMLDLGGGSTQIAFLPRVEGTLQASPPGYLTALRMFNRTYKLYSYSYLGLGLMSARLAILGGVEGQPAKDGKELVSPCLSPSFKGEWEHAEVTYRVSGQKAAASLHELCAARVSEVLQNRVHRTEEVKHVDFYAFSYYYDLAAGVGLIDAEKGGSLVVGDFEIAAKYVCRTLETQPQSSPFSCMDLTYVSLLLQEFGFPRSKVLKLTRKIDNVETSWALGAIFHYIDSLNRQKSPAS
|
3.6.1.6
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:10948193, ECO:0000269|PubMed:11041856, ECO:0000269|PubMed:14529283}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:10948193, ECO:0000269|PubMed:11041856, ECO:0000269|PubMed:14529283}; Note=Strongly and equally activated by either Ca(2+) or Mg(2+). {ECO:0000269|PubMed:14529283};
|
nucleoside diphosphate catabolic process [GO:0009134]; response to calcium ion [GO:0051592]; response to magnesium ion [GO:0032026]
|
cell surface [GO:0009986]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; membrane [GO:0016020]; plasma membrane [GO:0005886]
|
CDP phosphatase activity [GO:0036384]; GDP phosphatase activity [GO:0004382]; guanosine-5'-triphosphate,3'-diphosphate diphosphatase activity [GO:0008894]; IDP phosphatase activity [GO:1990003]; nucleoside diphosphate phosphatase activity [GO:0017110]; ribonucleoside triphosphate phosphatase activity [GO:0017111]; UDP phosphatase activity [GO:0045134]
|
PF01150;
|
3.30.420.40;3.30.420.150;
|
GDA1/CD39 NTPase family
|
PTM: The secreted form may be produced by intracellular processing. {ECO:0000305|PubMed:11041856}.; PTM: N-glycosylated. {ECO:0000269|PubMed:10948193, ECO:0000269|PubMed:11041856}.
|
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9ER31}; Single-pass type II membrane protein {ECO:0000255}. Secreted {ECO:0000269|PubMed:10948193, ECO:0000269|PubMed:11041856}. Cell membrane {ECO:0000269|PubMed:10948193, ECO:0000269|PubMed:11041856}; Single-pass type II membrane protein {ECO:0000255}. Note=Exists as a secreted and membrane-bound forms in the medium of transfected cells, the secreted form is predominant. {ECO:0000269|PubMed:10948193, ECO:0000269|PubMed:11041856}.
|
CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-diphosphate + H2O = a ribonucleoside 5'-phosphate + H(+) + phosphate; Xref=Rhea:RHEA:36799, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:58043; EC=3.6.1.6; Evidence={ECO:0000269|PubMed:10948193, ECO:0000269|PubMed:11041856, ECO:0000269|PubMed:14529283}; CATALYTIC ACTIVITY: Reaction=H2O + IDP = H(+) + IMP + phosphate; Xref=Rhea:RHEA:35207, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58053, ChEBI:CHEBI:58280; EC=3.6.1.6; Evidence={ECO:0000269|PubMed:10948193, ECO:0000269|PubMed:14529283}; CATALYTIC ACTIVITY: Reaction=GDP + H2O = GMP + H(+) + phosphate; Xref=Rhea:RHEA:22156, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58115, ChEBI:CHEBI:58189; EC=3.6.1.6; Evidence={ECO:0000269|PubMed:10948193, ECO:0000269|PubMed:14529283}; CATALYTIC ACTIVITY: Reaction=H2O + UDP = H(+) + phosphate + UMP; Xref=Rhea:RHEA:64876, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57865, ChEBI:CHEBI:58223; EC=3.6.1.6; Evidence={ECO:0000269|PubMed:10948193, ECO:0000269|PubMed:14529283};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=130 uM for GDP (in the presence of Ca(2+)) {ECO:0000269|PubMed:14529283}; Vmax=60000 umol/h/mg enzyme with GDP as substrate {ECO:0000269|PubMed:14529283};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0 to 7.4. {ECO:0000269|PubMed:14529283};
| null |
FUNCTION: Catalyzes the hydrolysis of nucleoside triphosphates and diphosphates in a calcium- or magnesium-dependent manner. Has a strong preference for nucleoside diphosphates, preferentially hydrolyzes GDP, IDP, and UDP, with slower hydrolysis of CDP, ITP, GTP, CTP, ADP, and UTP and virtually no hydrolysis of ATP (PubMed:10948193, PubMed:11041856, PubMed:14529283). The membrane bound form might support glycosylation reactions in the Golgi apparatus and, when released from cells, might catalyze the hydrolysis of extracellular nucleotides (PubMed:10948193, PubMed:11041856, PubMed:14529283). {ECO:0000269|PubMed:10948193, ECO:0000269|PubMed:11041856, ECO:0000269|PubMed:14529283}.
|
Homo sapiens (Human)
|
O75355
|
ENTP3_HUMAN
|
MFTVLTRQPCEQAGLKALYRTPTIIALVVLLVSIVVLVSITVIQIHKQEVLPPGLKYGIVLDAGSSRTTVYVYQWPAEKENNTGVVSQTFKCSVKGSGISSYGNNPQDVPRAFEECMQKVKGQVPSHLHGSTPIHLGATAGMRLLRLQNETAANEVLESIQSYFKSQPFDFRGAQIISGQEEGVYGWITANYLMGNFLEKNLWHMWVHPHGVETTGALDLGGASTQISFVAGEKMDLNTSDIMQVSLYGYVYTLYTHSFQCYGRNEAEKKFLAMLLQNSPTKNHLTNPCYPRDYSISFTMGHVFDSLCTVDQRPESYNPNDVITFEGTGDPSLCKEKVASIFDFKACHDQETCSFDGVYQPKIKGPFVAFAGFYYTASALNLSGSFSLDTFNSSTWNFCSQNWSQLPLLLPKFDEVYARSYCFSANYIYHLFVNGYKFTEETWPQIHFEKEVGNSSIAWSLGYMLSLTNQIPAESPLIRLPIEPPVFVGTLAFFTAAALLCLAFLAYLCSATRRKRHSEHAFDHAVDSD
|
3.6.1.5
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:11300774}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:11300774};
|
nucleoside diphosphate catabolic process [GO:0009134]; nucleoside triphosphate catabolic process [GO:0009143]
|
plasma membrane [GO:0005886]
|
apyrase activity [GO:0004050]; ATP binding [GO:0005524]; GDP phosphatase activity [GO:0004382]; nucleoside diphosphate phosphatase activity [GO:0017110]; ribonucleoside triphosphate phosphatase activity [GO:0017111]; UDP phosphatase activity [GO:0045134]
|
PF01150;
|
3.30.420.40;3.30.420.150;
|
GDA1/CD39 NTPase family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8BFW6}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + 2 H2O = a ribonucleoside 5'-phosphate + 2 H(+) + 2 phosphate; Xref=Rhea:RHEA:36795, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58043, ChEBI:CHEBI:61557; EC=3.6.1.5; Evidence={ECO:0000269|PubMed:10231536, ECO:0000269|PubMed:11300774};
| null | null | null | null |
FUNCTION: Has a threefold preference for the hydrolysis of ATP over ADP. {ECO:0000269|PubMed:10231536, ECO:0000269|PubMed:11300774}.
|
Homo sapiens (Human)
|
O75356
|
ENTP5_HUMAN
|
MATSWGTVFFMLVVSCVCSAVSHRNQQTWFEGIFLSSMCPINVSASTLYGIMFDAGSTGTRIHVYTFVQKMPGQLPILEGEVFDSVKPGLSAFVDQPKQGAETVQGLLEVAKDSIPRSHWKKTPVVLKATAGLRLLPEHKAKALLFEVKEIFRKSPFLVPKGSVSIMDGSDEGILAWVTVNFLTGQLHGHRQETVGTLDLGGASTQITFLPQFEKTLEQTPRGYLTSFEMFNSTYKLYTHSYLGFGLKAARLATLGALETEGTDGHTFRSACLPRWLEAEWIFGGVKYQYGGNQEGEVGFEPCYAEVLRVVRGKLHQPEEVQRGSFYAFSYYYDRAVDTDMIDYEKGGILKVEDFERKAREVCDNLENFTSGSPFLCMDLSYITALLKDGFGFADSTVLQLTKKVNNIETGWALGATFHLLQSLGISH
|
3.6.1.6
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:10400613, ECO:0000269|PubMed:15698960}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:10400613, ECO:0000269|PubMed:15698960};
|
'de novo' post-translational protein folding [GO:0051084]; nucleoside diphosphate catabolic process [GO:0009134]; protein N-linked glycosylation [GO:0006487]; UDP catabolic process [GO:0006256]; UDP-glucose metabolic process [GO:0006011]
|
endoplasmic reticulum [GO:0005783]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; membrane [GO:0016020]
|
ADP phosphatase activity [GO:0043262]; CDP phosphatase activity [GO:0036384]; GDP phosphatase activity [GO:0004382]; IDP phosphatase activity [GO:1990003]; ribonucleoside triphosphate phosphatase activity [GO:0017111]; UDP phosphatase activity [GO:0045134]
|
PF01150;
|
3.30.420.40;3.30.420.150;
|
GDA1/CD39 NTPase family
|
PTM: N-glycosylated; high-mannose type (By similarity). Glycosylation is not essential for enzymatic activity. {ECO:0000250|UniProtKB:Q9WUZ9, ECO:0000269|PubMed:11041857, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218}.
|
SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9WUZ9}. Secreted {ECO:0000269|PubMed:10400613, ECO:0000269|PubMed:15698960}.
|
CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-diphosphate + H2O = a ribonucleoside 5'-phosphate + H(+) + phosphate; Xref=Rhea:RHEA:36799, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:58043; EC=3.6.1.6; Evidence={ECO:0000269|PubMed:10400613, ECO:0000269|PubMed:15698960}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36800; Evidence={ECO:0000305|PubMed:15698960}; CATALYTIC ACTIVITY: Reaction=GDP + H2O = GMP + H(+) + phosphate; Xref=Rhea:RHEA:22156, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58115, ChEBI:CHEBI:58189; EC=3.6.1.6; Evidence={ECO:0000269|PubMed:15698960}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22157; Evidence={ECO:0000305|PubMed:15698960}; CATALYTIC ACTIVITY: Reaction=H2O + UDP = H(+) + phosphate + UMP; Xref=Rhea:RHEA:64876, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57865, ChEBI:CHEBI:58223; EC=3.6.1.6; Evidence={ECO:0000269|PubMed:15698960}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64877; Evidence={ECO:0000305|PubMed:15698960}; CATALYTIC ACTIVITY: Reaction=H2O + IDP = H(+) + IMP + phosphate; Xref=Rhea:RHEA:35207, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58053, ChEBI:CHEBI:58280; EC=3.6.1.6; Evidence={ECO:0000269|PubMed:15698960}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35208; Evidence={ECO:0000305|PubMed:15698960}; CATALYTIC ACTIVITY: Reaction=CDP + H2O = CMP + H(+) + phosphate; Xref=Rhea:RHEA:64880, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377; EC=3.6.1.6; Evidence={ECO:0000269|PubMed:10400613}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64881; Evidence={ECO:0000305|PubMed:10400613}; CATALYTIC ACTIVITY: Reaction=ADP + H2O = AMP + H(+) + phosphate; Xref=Rhea:RHEA:61436, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=3.6.1.6; Evidence={ECO:0000269|PubMed:10400613}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61437; Evidence={ECO:0000305|PubMed:10400613};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.14 mM for GDP {ECO:0000269|PubMed:15698960}; Vmax=34 mmol/h/mg enzyme with GDP as substrate {ECO:0000269|PubMed:15698960};
|
PATHWAY: Protein modification; protein glycosylation. {ECO:0000250|UniProtKB:Q9WUZ9}.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5-8.0. {ECO:0000269|PubMed:15698960};
| null |
FUNCTION: Hydrolyzes nucleoside diphosphates with a preference for GDP, IDP and UDP compared to ADP and CDP (PubMed:10400613, PubMed:15698960). In the lumen of the endoplasmic reticulum, hydrolyzes UDP that acts as an end-product feedback inhibitor of the UDP-Glc:glycoprotein glucosyltransferases. UMP can be transported back by an UDP-sugar antiporter to the cytosol where it is consumed to regenerate UDP-glucose. Therefore, it positively regulates protein reglucosylation by clearing UDP from the ER lumen and by promoting the regeneration of UDP-glucose. Protein reglucosylation is essential to proper glycoprotein folding and quality control in the ER (By similarity). {ECO:0000250|UniProtKB:Q9WUZ9, ECO:0000269|PubMed:10400613, ECO:0000269|PubMed:15698960}.
|
Homo sapiens (Human)
|
O75360
|
PROP1_HUMAN
|
MEAERRRQAEKPKKGRVGSNLLPERHPATGTPTTTVDSSAPPCRRLPGAGGGRSRFSPQGGQRGRPHSRRRHRTTFSPVQLEQLESAFGRNQYPDIWARESLARDTGLSEARIQVWFQNRRAKQRKQERSLLQPLAHLSPAAFSSFLPESTACPYSYAAPPPPVTCFPHPYSHALPSQPSTGGAFALSHQSEDWYPTLHPAPAGHLPCPPPPPMLPLSLEPSKSWN
| null | null |
apoptotic process [GO:0006915]; blood vessel development [GO:0001568]; cell migration [GO:0016477]; central nervous system development [GO:0007417]; dorsal/ventral pattern formation [GO:0009953]; hypophysis morphogenesis [GO:0048850]; hypothalamus cell differentiation [GO:0021979]; negative regulation of apoptotic process [GO:0043066]; regulation of transcription by RNA polymerase II [GO:0006357]; somatotropin secreting cell differentiation [GO:0060126]
|
chromatin [GO:0000785]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667]
|
beta-catenin binding [GO:0008013]; chromatin binding [GO:0003682]; 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]; sequence-specific double-stranded DNA binding [GO:1990837]
|
PF00046;
|
1.10.10.60;
|
Paired homeobox family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
| null | null | null | null | null |
FUNCTION: Possibly involved in the ontogenesis of pituitary gonadotropes, as well as somatotropes, lactotropes and caudomedial thyrotropes.
|
Homo sapiens (Human)
|
O75362
|
ZN217_HUMAN
|
MQSKVTGNMPTQSLLMYMDGPEVIGSSLGSPMEMEDALSMKGTAVVPFRATQEKNVIQIEGYMPLDCMFCSQTFTHSEDLNKHVLMQHRPTLCEPAVLRVEAEYLSPLDKSQVRTEPPKEKNCKENEFSCEVCGQTFRVAFDVEIHMRTHKDSFTYGCNMCGRRFKEPWFLKNHMRTHNGKSGARSKLQQGLESSPATINEVVQVHAAESISSPYKICMVCGFLFPNKESLIEHRKVHTKKTAFGTSSAQTDSPQGGMPSSREDFLQLFNLRPKSHPETGKKPVRCIPQLDPFTTFQAWQLATKGKVAICQEVKESGQEGSTDNDDSSSEKELGETNKGSCAGLSQEKEKCKHSHGEAPSVDADPKLPSSKEKPTHCSECGKAFRTYHQLVLHSRVHKKDRRAGAESPTMSVDGRQPGTCSPDLAAPLDENGAVDRGEGGSEDGSEDGLPEGIHLDKNDDGGKIKHLTSSRECSYCGKFFRSNYYLNIHLRTHTGEKPYKCEFCEYAAAQKTSLRYHLERHHKEKQTDVAAEVKNDGKNQDTEDALLTADSAQTKNLKRFFDGAKDVTGSPPAKQLKEMPSVFQNVLGSAVLSPAHKDTQDFHKNAADDSADKVNKNPTPAYLDLLKKRSAVETQANNLICRTKADVTPPPDGSTTHNLEVSPKEKQTETAADCRYRPSVDCHEKPLNLSVGALHNCPAISLSKSLIPSITCPFCTFKTFYPEVLMMHQRLEHKYNPDVHKNCRNKSLLRSRRTGCPPALLGKDVPPLSSFCKPKPKSAFPAQSKSLPSAKGKQSPPGPGKAPLTSGIDSSTLAPSNLKSHRPQQNVGVQGAATRQQQSEMFPKTSVSPAPDKTKRPETKLKPLPVAPSQPTLGSSNINGSIDYPAKNDSPWAPPGRDYFCNRSASNTAAEFGEPLPKRLKSSVVALDVDQPGANYRRGYDLPKYHMVRGITSLLPQDCVYPSQALPPKPRFLSSSEVDSPNVLTVQKPYGGSGPLYTCVPAGSPASSSTLEGKRPVSYQHLSNSMAQKRNYENFIGNAHYRPNDKKT
| null | null |
negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of transcription by RNA polymerase II [GO:0000122]; regulation of DNA-templated transcription [GO:0006355]
|
histone deacetylase complex [GO:0000118]; mitochondrion [GO:0005739]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
DNA-binding transcription factor activity [GO:0003700]; 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 cis-regulatory region sequence-specific DNA binding [GO:0000978]; transcription cis-regulatory region binding [GO:0000976]
|
PF00096;
|
3.30.160.60;
|
Krueppel C2H2-type zinc-finger protein family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Binds to the promoters of target genes and functions as repressor. Promotes cell proliferation and antagonizes cell death. Promotes phosphorylation of AKT1 at 'Ser-473'. {ECO:0000269|PubMed:16203743, ECO:0000269|PubMed:16940172, ECO:0000269|PubMed:17259635, ECO:0000269|PubMed:18625718}.
|
Homo sapiens (Human)
|
O75364
|
PITX3_HUMAN
|
MEFGLLSEAEARSPALSLSDAGTPHPQLPEHGCKGQEHSDSEKASASLPGGSPEDGSLKKKQRRQRTHFTSQQLQELEATFQRNRYPDMSTREEIAVWTNLTEARVRVWFKNRRAKWRKRERSQQAELCKGSFAAPLGGLVPPYEEVYPGYSYGNWPPKALAPPLAAKTFPFAFNSVNVGPLASQPVFSPPSSIAASMVPSAAAAPGTVPGPGALQGLGGGPPGLAPAAVSSGAVSCPYASAAAAAAAAASSPYVYRDPCNSSLASLRLKAKQHASFSYPAVHGPPPAANLSPCQYAVERPV
| null | null |
anatomical structure morphogenesis [GO:0009653]; animal organ morphogenesis [GO:0009887]; cellular response to glial cell derived neurotrophic factor [GO:1990792]; dopaminergic neuron differentiation [GO:0071542]; lens development in camera-type eye [GO:0002088]; lens morphogenesis in camera-type eye [GO:0002089]; midbrain development [GO:0030901]; negative regulation of gliogenesis [GO:0014014]; positive regulation of cell proliferation in midbrain [GO:1904935]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of neuron apoptotic process [GO:0043525]; regulation of DNA-templated transcription [GO:0006355]; regulation of transcription by RNA polymerase II [GO:0006357]; response to cocaine [GO:0042220]; response to immobilization stress [GO:0035902]; response to methamphetamine hydrochloride [GO:1904313]
|
chromatin [GO:0000785]; nucleus [GO:0005634]
|
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; 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: Transcriptional regulator which is important for the differentiation and maintenance of meso-diencephalic dopaminergic (mdDA) neurons during development. In addition to its importance during development, it also has roles in the long-term survival and maintenance of the mdDA neurons. Activates NR4A2/NURR1-mediated transcription of genes such as SLC6A3, SLC18A2, TH and DRD2 which are essential for development of mdDA neurons. Acts by decreasing the interaction of NR4A2/NURR1 with the corepressor NCOR2/SMRT which acts through histone deacetylases (HDACs) to keep promoters of NR4A2/NURR1 target genes in a repressed deacetylated state. Essential for the normal lens development and differentiation. Plays a critical role in the maintenance of mitotic activity of lens epithelial cells, fiber cell differentiation and in the control of the temporal and spatial activation of fiber cell-specific crystallins. Positively regulates FOXE3 expression and negatively regulates PROX1 in the anterior lens epithelium, preventing activation of CDKN1B/P27Kip1 and CDKN1C/P57Kip2 and thus maintains lens epithelial cells in cell cycle (By similarity). {ECO:0000250}.
|
Homo sapiens (Human)
|
O75365
|
TP4A3_HUMAN
|
MARMNRPAPVEVSYKHMRFLITHNPTNATLSTFIEDLKKYGATTVVRVCEVTYDKTPLEKDGITVVDWPFDDGAPPPGKVVEDWLSLVKAKFCEAPGSCVAVHCVAGLGRAPVLVALALIESGMKYEDAIQFIRQKRRGAINSKQLTYLEKYRPKQRLRFKDPHTHKTRCCVM
|
3.1.3.48
| null |
cellular response to leukemia inhibitory factor [GO:1990830]; dephosphorylation [GO:0016311]; endothelial cell migration [GO:0043542]; Notch signaling pathway [GO:0007219]; positive regulation of establishment of protein localization [GO:1904951]; positive regulation of non-canonical NF-kappaB signal transduction [GO:1901224]; positive regulation of vascular permeability [GO:0043117]; regulation of DNA-templated transcription [GO:0006355]; regulation of vascular endothelial growth factor signaling pathway [GO:1900746]
|
cytoplasm [GO:0005737]; early endosome [GO:0005769]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
prenylated protein tyrosine phosphatase activity [GO:0004727]; protein tyrosine phosphatase activity [GO:0004725]
|
PF00102;
|
3.90.190.10;
|
Protein-tyrosine phosphatase family
|
PTM: Farnesylated. Farnesylation is required for membrane targeting (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12782572}. Early endosome {ECO:0000269|PubMed:12782572}.
|
CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48;
| null | null | null | null |
FUNCTION: Protein tyrosine phosphatase which stimulates progression from G1 into S phase during mitosis. Enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. May be involved in the progression of cardiac hypertrophy by inhibiting intracellular calcium mobilization in response to angiotensin II. {ECO:0000269|PubMed:11355880, ECO:0000269|PubMed:12782572}.
|
Homo sapiens (Human)
|
O75366
|
AVIL_HUMAN
|
MPLTSAFRAVDNDPGIIVWRIEKMELALVPVSAHGNFYEGDCYVILSTRRVASLLSQDIHFWIGKDSSQDEQSCAAIYTTQLDDYLGGSPVQHREVQYHESDTFRGYFKQGIIYKQGGVASGMKHVETNTYDVKRLLHVKGKRNIRATEVEMSWDSFNRGDVFLLDLGKVIIQWNGPESNSGERLKAMLLAKDIRDRERGGRAKIGVIEGDKEAASPELMKVLQDTLGRRSIIKPTVPDEIIDQKQKSTIMLYHISDSAGQLAVTEVATRPLVQDLLNHDDCYILDQSGTKIYVWKGKGATKAEKQAAMSKALGFIKMKSYPSSTNVETVNDGAESAMFKQLFQKWSVKDQTMGLGKTFSIGKIAKVFQDKFDVTLLHTKPEVAAQERMVDDGNGKVEVWRIENLELVPVEYQWYGFFYGGDCYLVLYTYEVNGKPHHILYIWQGRHASQDELAASAYQAVEVDRQFDGAAVQVRVRMGTEPRHFMAIFKGKLVIFEGGTSRKGNAEPDPPVRLFQIHGNDKSNTKAVEVPAFASSLNSNDVFLLRTQAEHYLWYGKGSSGDERAMAKELASLLCDGSENTVAEGQEPAEFWDLLGGKTPYANDKRLQQEILDVQSRLFECSNKTGQFVVTEITDFTQDDLNPTDVMLLDTWDQVFLWIGAEANATEKESALATAQQYLHTHPSGRDPDTPILIIKQGFEPPIFTGWFLAWDPNIWSAGKTYEQLKEELGDAAAIMRITADMKNATLSLNSNDSEPKYYPIAVLLKNQNQELPEDVNPAKKENYLSEQDFVSVFGITRGQFAALPGWKQLQMKKEKGLF
| null | null |
actin filament organization [GO:0007015]; actin filament severing [GO:0051014]; actin polymerization or depolymerization [GO:0008154]; barbed-end actin filament capping [GO:0051016]; cilium assembly [GO:0060271]; nervous system development [GO:0007399]; positive regulation of lamellipodium assembly [GO:0010592]; positive regulation of neuron projection development [GO:0010976]; regulation of diacylglycerol biosynthetic process [GO:1900480]
|
actin cytoskeleton [GO:0015629]; actin filament [GO:0005884]; axon [GO:0030424]; cell projection [GO:0042995]; cytoplasm [GO:0005737]; focal adhesion [GO:0005925]; lamellipodium [GO:0030027]; neuron projection [GO:0043005]
|
actin binding [GO:0003779]; actin filament binding [GO:0051015]; Arp2/3 complex binding [GO:0071933]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]
|
PF00626;PF02209;
|
3.40.20.10;1.10.950.10;
|
Villin/gelsolin family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:29058690}. Cell projection, lamellipodium {ECO:0000269|PubMed:29058690}. Cell junction, focal adhesion {ECO:0000269|PubMed:29058690}. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q9WU06}. Cell projection, axon {ECO:0000250|UniProtKB:Q9WU06}. Note=In podocytes, present in the F-actin-enriched cell periphery that generates lamellipodia and focal adhesions. {ECO:0000269|PubMed:29058690}.
| null | null | null | null | null |
FUNCTION: Ca(2+)-regulated actin-binding protein which plays an important role in actin bundling (PubMed:29058690). May have a unique function in the morphogenesis of neuronal cells which form ganglia. Required for SREC1-mediated regulation of neurite-like outgrowth. Plays a role in regenerative sensory axon outgrowth and remodeling processes after peripheral injury in neonates. Involved in the formation of long fine actin-containing filopodia-like structures in fibroblast. Plays a role in ciliogenesis. In podocytes, controls lamellipodia formation through the regulation of EGF-induced diacylglycerol generation by PLCE1 and ARP2/3 complex assembly (PubMed:29058690). {ECO:0000269|PubMed:20393563, ECO:0000269|PubMed:29058690}.
|
Homo sapiens (Human)
|
O75367
|
H2AY_HUMAN
|
MSSRGGKKKSTKTSRSAKAGVIFPVGRMLRYIKKGHPKYRIGVGAPVYMAAVLEYLTAEILELAGNAARDNKKGRVTPRHILLAVANDEELNQLLKGVTIASGGVLPNIHPELLAKKRGSKGKLEAIITPPPAKKAKSPSQKKPVSKKAGGKKGARKSKKKQGEVSKAASADSTTEGTPADGFTVLSTKSLFLGQKLQVVQADIASIDSDAVVHPTNTDFYIGGEVGNTLEKKGGKEFVEAVLELRKKNGPLEVAGAAVSAGHGLPAKFVIHCNSPVWGADKCEELLEKTVKNCLALADDKKLKSIAFPSIGSGRNGFPKQTAAQLILKAISSYFVSTMSSSIKTVYFVLFDSESIGIYVQEMAKLDAN
| null | null |
DNA repair [GO:0006281]; epigenetic regulation of gene expression [GO:0040029]; establishment of protein localization to chromatin [GO:0071169]; heterochromatin organization [GO:0070828]; negative regulation of cell cycle G2/M phase transition [GO:1902750]; negative regulation of gene expression, epigenetic [GO:0045814]; negative regulation of protein localization to chromosome, telomeric region [GO:1904815]; negative regulation of protein serine/threonine kinase activity [GO:0071901]; negative regulation of response to oxidative stress [GO:1902883]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of transcription of nucleolar large rRNA by RNA polymerase I [GO:1901837]; nucleosome assembly [GO:0006334]; positive regulation of endodermal cell differentiation [GO:1903226]; positive regulation of keratinocyte differentiation [GO:0045618]; positive regulation of maintenance of mitotic sister chromatid cohesion [GO:0034184]; positive regulation of response to oxidative stress [GO:1902884]; regulation of lipid metabolic process [GO:0019216]; regulation of NAD metabolic process [GO:1902688]; regulation of oxidative phosphorylation [GO:0002082]; regulation of response to oxidative stress [GO:1902882]; sex-chromosome dosage compensation [GO:0007549]; transcription initiation-coupled chromatin remodeling [GO:0045815]
|
Barr body [GO:0001740]; chromatin [GO:0000785]; chromosome, telomeric region [GO:0000781]; condensed chromosome [GO:0000793]; extracellular exosome [GO:0070062]; nuclear chromosome [GO:0000228]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleosome [GO:0000786]; nucleus [GO:0005634]; pericentric heterochromatin [GO:0005721]; sex chromatin [GO:0001739]; site of DNA damage [GO:0090734]
|
ADP-D-ribose binding [GO:0072570]; ADP-D-ribose modification-dependent protein binding [GO:0160002]; chromatin DNA binding [GO:0031490]; DNA binding [GO:0003677]; double-stranded methylated DNA binding [GO:0010385]; enzyme binding [GO:0019899]; nucleosomal DNA binding [GO:0031492]; poly-ADP-D-ribose modification-dependent protein binding [GO:0160004]; promoter-specific chromatin binding [GO:1990841]; protein heterodimerization activity [GO:0046982]; protein kinase binding [GO:0019901]; protein serine/threonine kinase inhibitor activity [GO:0030291]; rDNA binding [GO:0000182]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; structural constituent of chromatin [GO:0030527]; transcription cis-regulatory region binding [GO:0000976]
|
PF00125;PF16211;PF01661;
|
1.10.20.10;3.40.220.10;
|
Histone H2A family
|
PTM: Monoubiquitinated at either Lys-116 or Lys-117. May also be polyubiquitinated. Ubiquitination is mediated by the CUL3/SPOP E3 complex and does not promote proteasomal degradation. Instead, it is required for enrichment in inactive X chromosome chromatin. {ECO:0000269|PubMed:15897469, ECO:0000269|PubMed:16129414, ECO:0000269|PubMed:19818708}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15621527, ECO:0000269|PubMed:15897469, ECO:0000269|PubMed:9634239}. Chromosome {ECO:0000269|PubMed:15621527, ECO:0000269|PubMed:15897469, ECO:0000269|PubMed:21211722, ECO:0000269|PubMed:29905837, ECO:0000269|PubMed:9634239}. Note=Enriched in inactive X chromosome chromatin and in senescence-associated heterochromatin (PubMed:15621527, PubMed:15897469, PubMed:9634239). Recruited to DNA damage sites in an APLF-dependent manner (PubMed:21211722, PubMed:29905837). {ECO:0000269|PubMed:15621527, ECO:0000269|PubMed:15897469, ECO:0000269|PubMed:21211722, ECO:0000269|PubMed:29905837, ECO:0000269|PubMed:9634239}.
| null | null | null | null | null |
FUNCTION: Variant histone H2A which replaces conventional H2A in a subset of nucleosomes where it represses transcription (PubMed:12718888, PubMed:15621527, PubMed:16428466). Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template (PubMed:15897469). Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability (PubMed:15897469). DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Involved in stable X chromosome inactivation (PubMed:15897469). Inhibits the binding of transcription factors, including NF-kappa-B, and interferes with the activity of remodeling SWI/SNF complexes (PubMed:12718888, PubMed:16428466). Inhibits histone acetylation by EP300 and recruits class I HDACs, which induces a hypoacetylated state of chromatin (PubMed:16107708, PubMed:16428466). {ECO:0000269|PubMed:12718888, ECO:0000269|PubMed:15621527, ECO:0000269|PubMed:15897469, ECO:0000269|PubMed:16107708, ECO:0000269|PubMed:16428466}.; FUNCTION: [Isoform 1]: Isoform that specifically binds poly-ADP-ribose and O-acetyl-ADP-ribose and plays a key role in NAD(+) metabolism (PubMed:15902274). Able to bind to the ends of poly-ADP-ribose chains created by PARP1 and cap them (By similarity). This prevents PARP1 from further addition of ADP-ribose and thus limits the consumption of nuclear NAD(+), allowing the cell to maintain proper NAD(+) levels in both the nucleus and the mitochondria to promote proper mitochondrial respiration (By similarity). Increases the expression of genes involved in redox metabolism, including SOD3 (PubMed:23022728). {ECO:0000250|UniProtKB:Q9QZQ8, ECO:0000269|PubMed:15902274, ECO:0000269|PubMed:23022728}.; FUNCTION: [Isoform 2]: In contrast to isoform 1, does not bind poly-ADP-ribose (PubMed:15902274). Represses SOD3 gene expression (PubMed:23022728). {ECO:0000269|PubMed:15902274, ECO:0000269|PubMed:23022728}.
|
Homo sapiens (Human)
|
O75368
|
SH3L1_HUMAN
|
MVIRVYIASSSGSTAIKKKQQDVLGFLEANKIGFEEKDIAANEENRKWMRENVPENSRPATGYPLPPQIFNESQYRGDYDAFFEARENNAVYAFLGLTAPPGSKEAEVQAKQQA
| null | null |
positive regulation of cytoplasmic translational initiation [GO:1904690]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
protein-RNA adaptor activity [GO:0140517]; SH3 domain binding [GO:0017124]; ubiquitin ligase-substrate adaptor activity [GO:1990756]
|
PF04908;
|
3.40.30.10;
|
SH3BGR family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:34870550, ECO:0000305|PubMed:34331014}. Cell membrane {ECO:0000269|PubMed:32381043}.
| null | null | null | null | null |
FUNCTION: Appears to function as an adapter protein that bridges proteins together or proteins with mRNAs (PubMed:34331014). May function as a ubiquitin ligase-substrate adapter (PubMed:34331014, PubMed:34870550). Additionally, associates with translating cytoplasmic ribosomes and may promote the expression of specific mRNAs (PubMed:34331014, PubMed:34870550). {ECO:0000269|PubMed:34331014, ECO:0000269|PubMed:34870550}.
|
Homo sapiens (Human)
|
O75369
|
FLNB_HUMAN
|
MPVTEKDLAEDAPWKKIQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRKYHQRPTFRQMQLENVSVALEFLDRESIKLVSIDSKAIVDGNLKLILGLVWTLILHYSISMPVWEDEGDDDAKKQTPKQRLLGWIQNKIPYLPITNFNQNWQDGKALGALVDSCAPGLCPDWESWDPQKPVDNAREAMQQADDWLGVPQVITPEEIIHPDVDEHSVMTYLSQFPKAKLKPGAPLKPKLNPKKARAYGRGIEPTGNMVKQPAKFTVDTISAGQGDVMVFVEDPEGNKEEAQVTPDSDKNKTYSVEYLPKVTGLHKVTVLFAGQHISKSPFEVSVDKAQGDASKVTAKGPGLEAVGNIANKPTYFDIYTAGAGVGDIGVEVEDPQGKNTVELLVEDKGNQVYRCVYKPMQPGPHVVKIFFAGDTIPKSPFVVQVGEACNPNACRASGRGLQPKGVRIRETTDFKVDTKAAGSGELGVTMKGPKGLEELVKQKDFLDGVYAFEYYPSTPGRYSIAITWGGHHIPKSPFEVQVGPEAGMQKVRAWGPGLHGGIVGRSADFVVESIGSEVGSLGFAIEGPSQAKIEYNDQNDGSCDVKYWPKEPGEYAVHIMCDDEDIKDSPYMAFIHPATGGYNPDLVRAYGPGLEKSGCIVNNLAEFTVDPKDAGKAPLKIFAQDGEGQRIDIQMKNRMDGTYACSYTPVKAIKHTIAVVWGGVNIPHSPYRVNIGQGSHPQKVKVFGPGVERSGLKANEPTHFTVDCTEAGEGDVSVGIKCDARVLSEDEEDVDFDIIHNANDTFTVKYVPPAAGRYTIKVLFASQEIPASPFRVKVDPSHDASKVKAEGPGLSKAGVENGKPTHFTVYTKGAGKAPLNVQFNSPLPGDAVKDLDIIDNYDYSHTVKYTPTQQGNMQVLVTYGGDPIPKSPFTVGVAAPLDLSKIKLNGLENRVEVGKDQEFTVDTRGAGGQGKLDVTILSPSRKVVPCLVTPVTGRENSTAKFIPREEGLYAVDVTYDGHPVPGSPYTVEASLPPDPSKVKAHGPGLEGGLVGKPAEFTIDTKGAGTGGLGLTVEGPCEAKIECSDNGDGTCSVSYLPTKPGEYFVNILFEEVHIPGSPFKADIEMPFDPSKVVASGPGLEHGKVGEAGLLSVDCSEAGPGALGLEAVSDSGTKAEVSIQNNKDGTYAVTYVPLTAGMYTLTMKYGGELVPHFPARVKVEPAVDTSRIKVFGPGIEGKDVFREATTDFTVDSRPLTQVGGDHIKAHIANPSGASTECFVTDNADGTYQVEYTPFEKGLHVVEVTYDDVPIPNSPFKVAVTEGCQPSRVQAQGPGLKEAFTNKPNVFTVVTRGAGIGGLGITVEGPSESKINCRDNKDGSCSAEYIPFAPGDYDVNITYGGAHIPGSPFRVPVKDVVDPSKVKIAGPGLGSGVRARVLQSFTVDSSKAGLAPLEVRVLGPRGLVEPVNVVDNGDGTHTVTYTPSQEGPYMVSVKYADEEIPRSPFKVKVLPTYDASKVTASGPGLSSYGVPASLPVDFAIDARDAGEGLLAVQITDQEGKPKRAIVHDNKDGTYAVTYIPDKTGRYMIGVTYGGDDIPLSPYRIRATQTGDASKCLATGPGIASTVKTGEEVGFVVDAKTAGKGKVTCTVLTPDGTEAEADVIENEDGTYDIFYTAAKPGTYVIYVRFGGVDIPNSPFTVMATDGEVTAVEEAPVNACPPGFRPWVTEEAYVPVSDMNGLGFKPFDLVIPFAVRKGEITGEVHMPSGKTATPEIVDNKDGTVTVRYAPTEVGLHEMHIKYMGSHIPESPLQFYVNYPNSGSVSAYGPGLVYGVANKTATFTIVTEDAGEGGLDLAIEGPSKAEISCIDNKDGTCTVTYLPTLPGDYSILVKYNDKHIPGSPFTAKITDDSRRCSQVKLGSAADFLLDISETDLSSLTASIKAPSGRDEPCLLKRLPNNHIGISFIPREVGEHLVSIKKNGNHVANSPVSIMVVQSEIGDARRAKVYGRGLSEGRTFEMSDFIVDTRDAGYGGISLAVEGPSKVDIQTEDLEDGTCKVSYFPTVPGVYIVSTKFADEHVPGSPFTVKISGEGRVKESITRTSRAPSVATVGSICDLNLKIPEINSSDMSAHVTSPSGRVTEAEIVPMGKNSHCVRFVPQEMGVHTVSVKYRGQHVTGSPFQFTVGPLGEGGAHKVRAGGPGLERGEAGVPAEFSIWTREAGAGGLSIAVEGPSKAEITFDDHKNGSCGVSYIAQEPGNYEVSIKFNDEHIPESPYLVPVIAPSDDARRLTVMSLQESGLKVNQPASFAIRLNGAKGKIDAKVHSPSGAVEECHVSELEPDKYAVRFIPHENGVHTIDVKFNGSHVVGSPFKVRVGEPGQAGNPALVSAYGTGLEGGTTGIQSEFFINTTRAGPGTLSVTIEGPSKVKMDCQETPEGYKVMYTPMAPGNYLISVKYGGPNHIVGSPFKAKVTGQRLVSPGSANETSSILVESVTRSSTETCYSAIPKASSDASKVTSKGAGLSKAFVGQKSSFLVDCSKAGSNMLLIGVHGPTTPCEEVSMKHVGNQQYNVTYVVKERGDYVLAVKWGEEHIPGSPFHVTVP
| null | null |
actin cytoskeleton organization [GO:0030036]; cellular response to type II interferon [GO:0071346]; epithelial cell morphogenesis [GO:0003382]; keratinocyte development [GO:0003334]; signal transduction [GO:0007165]; skeletal muscle tissue development [GO:0007519]
|
actin cytoskeleton [GO:0015629]; brush border [GO:0005903]; cell cortex [GO:0005938]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; membrane [GO:0016020]; phagocytic vesicle [GO:0045335]; plasma membrane [GO:0005886]; stress fiber [GO:0001725]; Z disc [GO:0030018]
|
actin binding [GO:0003779]; actin filament binding [GO:0051015]; cadherin binding [GO:0045296]; identical protein binding [GO:0042802]; RNA binding [GO:0003723]
|
PF00307;PF00630;
|
1.10.418.10;2.60.40.10;
|
Filamin family
|
PTM: ISGylation prevents ability to interact with the upstream activators of the JNK cascade and inhibits IFNA-induced JNK signaling. {ECO:0000269|PubMed:19270716}.; PTM: Ubiquitination by a SCF-like complex containing ASB2 isoform 1 leads to proteasomal degradation which promotes muscle differentiation. {ECO:0000269|PubMed:19300455}.
|
SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm, cell cortex. Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, stress fiber. Cytoplasm, myofibril, sarcomere, Z line. Note=In differentiating myotubes, isoform 1, isoform 2 and isoform 3 are localized diffusely throughout the cytoplasm with regions of enrichment at the longitudinal actin stress fiber. In differentiated tubes, isoform 1 is also detected within the Z-lines.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytoskeleton, stress fiber.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm, cytoskeleton, stress fiber.; SUBCELLULAR LOCATION: [Isoform 6]: Cytoplasm, cytoskeleton. Note=Polarized at the periphery of myotubes.
| null | null | null | null | null |
FUNCTION: Connects cell membrane constituents to the actin cytoskeleton. May promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. Anchors various transmembrane proteins to the actin cytoskeleton. Interaction with FLNA may allow neuroblast migration from the ventricular zone into the cortical plate. Various interactions and localizations of isoforms affect myotube morphology and myogenesis. Isoform 6 accelerates muscle differentiation in vitro.
|
Homo sapiens (Human)
|
O75376
|
NCOR1_HUMAN
|
MSSSGYPPNQGAFSTEQSRYPPHSVQYTFPNTRHQQEFAVPDYRSSHLEVSQASQLLQQQQQQQLRRRPSLLSEFHPGSDRPQERRTSYEPFHPGPSPVDHDSLESKRPRLEQVSDSHFQRVSAAVLPLVHPLPEGLRASADAKKDPAFGGKHEAPSSPISGQPCGDDQNASPSKLSKEELIQSMDRVDREIAKVEQQILKLKKKQQQLEEEAAKPPEPEKPVSPPPVEQKHRSIVQIIYDENRKKAEEAHKIFEGLGPKVELPLYNQPSDTKVYHENIKTNQVMRKKLILFFKRRNHARKQREQKICQRYDQLMEAWEKKVDRIENNPRRKAKESKTREYYEKQFPEIRKQREQQERFQRVGQRGAGLSATIARSEHEISEIIDGLSEQENNEKQMRQLSVIPPMMFDAEQRRVKFINMNGLMEDPMKVYKDRQFMNVWTDHEKEIFKDKFIQHPKNFGLIASYLERKSVPDCVLYYYLTKKNENYKALVRRNYGKRRGRNQQIARPSQEEKVEEKEEDKAEKTEKKEEEKKDEEEKDEKEDSKENTKEKDKIDGTAEETEEREQATPRGRKTANSQGRRKGRITRSMTNEAAAASAAAAAATEEPPPPLPPPPEPISTEPVETSRWTEEEMEVAKKGLVEHGRNWAAIAKMVGTKSEAQCKNFYFNYKRRHNLDNLLQQHKQKTSRKPREERDVSQCESVASTVSAQEDEDIEASNEEENPEDSEVEAVKPSEDSPENATSRGNTEPAVELEPTTETAPSTSPSLAVPSTKPAEDESVETQVNDSISAETAEQMDVDQQEHSAEEGSVCDPPPATKADSVDVEVRVPENHASKVEGDNTKERDLDRASEKVEPRDEDLVVAQQINAQRPEPQSDNDSSATCSADEDVDGEPERQRMFPMDSKPSLLNPTGSILVSSPLKPNPLDLPQLQHRAAVIPPMVSCTPCNIPIGTPVSGYALYQRHIKAMHESALLEEQRQRQEQIDLECRSSTSPCGTSKSPNREWEVLQPAPHQVITNLPEGVRLPTTRPTRPPPPLIPSSKTTVASEKPSFIMGGSISQGTPGTYLTSHNQASYTQETPKPSVGSISLGLPRQQESAKSATLPYIKQEEFSPRSQNSQPEGLLVRAQHEGVVRGTAGAIQEGSITRGTPTSKISVESIPSLRGSITQGTPALPQTGIPTEALVKGSISRMPIEDSSPEKGREEAASKGHVIYEGKSGHILSYDNIKNAREGTRSPRTAHEISLKRSYESVEGNIKQGMSMRESPVSAPLEGLICRALPRGSPHSDLKERTVLSGSIMQGTPRATTESFEDGLKYPKQIKRESPPIRAFEGAITKGKPYDGITTIKEMGRSIHEIPRQDILTQESRKTPEVVQSTRPIIEGSISQGTPIKFDNNSGQSAIKHNVKSLITGPSKLSRGMPPLEIVPENIKVVERGKYEDVKAGETVRSRHTSVVSSGPSVLRSTLHEAPKAQLSPGIYDDTSARRTPVSYQNTMSRGSPMMNRTSDVTISSNKSTNHERKSTLTPTQRESIPAKSPVPGVDPVVSHSPFDPHHRGSTAGEVYRSHLPTHLDPAMPFHRALDPAAAAYLFQRQLSPTPGYPSQYQLYAMENTRQTILNDYITSQQMQVNLRPDVARGLSPREQPLGLPYPATRGIIDLTNMPPTILVPHPGGTSTPPMDRITYIPGTQITFPPRPYNSASMSPGHPTHLAAAASAEREREREREKERERERIAAASSDLYLRPGSEQPGRPGSHGYVRSPSPSVRTQETMLQQRPSVFQGTNGTSVITPLDPTAQLRIMPLPAGGPSISQGLPASRYNTAADALAALVDAAASAPQMDVSKTKESKHEAARLEENLRSRSAAVSEQQQLEQKTLEVEKRSVQCLYTSSAFPSGKPQPHSSVVYSEAGKDKGPPPKSRYEEELRTRGKTTITAANFIDVIITRQIASDKDARERGSQSSDSSSSLSSHRYETPSDAIEVISPASSPAPPQEKLQTYQPEVVKANQAENDPTRQYEGPLHHYRPQQESPSPQQQLPPSSQAEGMGQVPRTHRLITLADHICQIITQDFARNQVSSQTPQQPPTSTFQNSPSALVSTPVRTKTSNRYSPESQAQSVHHQRPGSRVSPENLVDKSRGSRPGKSPERSHVSSEPYEPISPPQVPVVHEKQDSLLLLSQRGAEPAEQRNDARSPGSISYLPSFFTKLENTSPMVKSKKQEIFRKLNSSGGGDSDMAAAQPGTEIFNLPAVTTSGSVSSRGHSFADPASNLGLEDIIRKALMGSFDDKVEDHGVVMSQPMGVVPGTANTSVVTSGETRREEGDPSPHSGGVCKPKLISKSNSRKSKSPIPGQGYLGTERPSSVSSVHSEGDYHRQTPGWAWEDRPSSTGSTQFPYNPLTMRMLSSTPPTPIACAPSAVNQAAPHQQNRIWEREPAPLLSAQYETLSDSDD
| null | null |
chromatin organization [GO:0006325]; locomotor rhythm [GO:0045475]; negative regulation of androgen receptor signaling pathway [GO:0060766]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of fatty acid metabolic process [GO:0045922]; negative regulation of glycolytic process [GO:0045820]; negative regulation of JNK cascade [GO:0046329]; negative regulation of miRNA transcription [GO:1902894]; negative regulation of transcription by RNA polymerase II [GO:0000122]; spindle assembly [GO:0051225]
|
chromatin [GO:0000785]; cytosol [GO:0005829]; histone deacetylase complex [GO:0000118]; membrane [GO:0016020]; mitotic spindle [GO:0072686]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription repressor complex [GO:0017053]
|
histone deacetylase binding [GO:0042826]; nuclear receptor binding [GO:0016922]; nuclear thyroid hormone receptor binding [GO:0046966]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; transcription cis-regulatory region binding [GO:0000976]; transcription corepressor activity [GO:0003714]
|
PF15784;PF00249;
|
1.20.5.430;1.20.58.1880;1.10.10.60;
|
N-CoR nuclear receptor corepressors family
|
PTM: Ubiquitinated; mediated by SIAH2 and leading to its subsequent proteasomal degradation. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00624}.
| null | null | null | null | null |
FUNCTION: Mediates transcriptional repression by certain nuclear receptors (PubMed:20812024). Part of a complex which promotes histone deacetylation and the formation of repressive chromatin structures which may impede the access of basal transcription factors. Participates in the transcriptional repressor activity produced by BCL6. Recruited by ZBTB7A to the androgen response elements/ARE on target genes, negatively regulates androgen receptor signaling and androgen-induced cell proliferation (PubMed:20812024). Mediates the NR1D1-dependent repression and circadian regulation of TSHB expression (By similarity). The NCOR1-HDAC3 complex regulates the circadian expression of the core clock gene ARTNL/BMAL1 and the genes involved in lipid metabolism in the liver (By similarity). {ECO:0000250|UniProtKB:Q60974, ECO:0000269|PubMed:14527417, ECO:0000269|PubMed:20812024}.
|
Homo sapiens (Human)
|
O75379
|
VAMP4_HUMAN
|
MPPKFKRHLNDDDVTGSVKSERRNLLEDDSDEEEDFFLRGPSGPRFGPRNDKIKHVQNQVDEVIDVMQENITKVIERGERLDELQDKSESLSDNATAFSNRSKQLRRQMWWRGCKIKAIMALVAAILLLVIIILIVMKYRT
| null | null |
endocytic recycling [GO:0032456]; Golgi ribbon formation [GO:0090161]; regulation of synaptic vesicle endocytosis [GO:1900242]; SNARE complex assembly [GO:0035493]; synaptic vesicle to endosome fusion [GO:0016189]
|
cell surface [GO:0009986]; clathrin-coated endocytic vesicle membrane [GO:0030669]; endosome [GO:0005768]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; lysosome [GO:0005764]; plasma membrane [GO:0005886]; SNARE complex [GO:0031201]; trans-Golgi network [GO:0005802]; trans-Golgi network membrane [GO:0032588]; transport vesicle [GO:0030133]
| null |
PF00957;
|
1.20.5.110;
|
Synaptobrevin family
| null |
SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}. Note=Associated with trans Golgi network (TGN) and newly formed immature secretory granules (ISG). Not found on the mature secretory organelles.
| null | null | null | null | null |
FUNCTION: Involved in the pathway that functions to remove an inhibitor (probably synaptotagmin-4) of calcium-triggered exocytosis during the maturation of secretory granules. May be a marker for this sorting pathway that is critical for remodeling the secretory response of granule.
|
Homo sapiens (Human)
|
O75381
|
PEX14_HUMAN
|
MASSEQAEQPSQPSSTPGSENVLPREPLIATAVKFLQNSRVRQSPLATRRAFLKKKGLTDEEIDMAFQQSGTAADEPSSLGPATQVVPVQPPHLISQPYSPAGSRWRDYGALAIIMAGIAFGFHQLYKKYLLPLILGGREDRKQLERMEAGLSELSGSVAQTVTQLQTTLASVQELLIQQQQKIQELAHELAAAKATTSTNWILESQNINELKSEINSLKGLLLNRRQFPPSPSAPKIPSWQIPVKSPSPSSPAAVNHHSSSDISPVSNESTSSSPGKEGHSPEGSTVTYHLLGPQEEGEGVVDVKGQVRMEVQGEEEKREDKEDEEDEEDDDVSHVDEEDCLGVQREDRRGGDGQINEQVEKLRRPEGASNESERD
| null | null |
cellular response to reactive oxygen species [GO:0034614]; microtubule anchoring [GO:0034453]; negative regulation of DNA-binding transcription factor activity [GO:0043433]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of protein binding [GO:0032091]; peroxisome organization [GO:0007031]; peroxisome transport along microtubule [GO:0036250]; protein import into peroxisome matrix [GO:0016558]; protein import into peroxisome matrix, docking [GO:0016560]; protein import into peroxisome matrix, substrate release [GO:0044721]; protein import into peroxisome matrix, translocation [GO:0016561]; protein-containing complex assembly [GO:0065003]
|
cytosol [GO:0005829]; fibrillar center [GO:0001650]; membrane [GO:0016020]; nucleus [GO:0005634]; peroxisomal importomer complex [GO:1990429]; peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777]; protein-containing complex [GO:0032991]
|
beta-tubulin binding [GO:0048487]; identical protein binding [GO:0042802]; microtubule binding [GO:0008017]; protein transmembrane transporter activity [GO:0008320]; protein-macromolecule adaptor activity [GO:0030674]; signaling receptor binding [GO:0005102]; transcription corepressor activity [GO:0003714]
|
PF04695;
|
1.10.10.10;
|
Peroxin-14 family
| null |
SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000269|PubMed:19197237}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q642G4}.
| null | null | null | null | null |
FUNCTION: Component of the PEX13-PEX14 docking complex, a translocon channel that specifically mediates the import of peroxisomal cargo proteins bound to PEX5 receptor (PubMed:24235149, PubMed:28765278, PubMed:9653144). The PEX13-PEX14 docking complex forms a large import pore which can be opened to a diameter of about 9 nm (By similarity). Mechanistically, PEX5 receptor along with cargo proteins associates with the PEX14 subunit of the PEX13-PEX14 docking complex in the cytosol, leading to the insertion of the receptor into the organelle membrane with the concomitant translocation of the cargo into the peroxisome matrix (PubMed:24235149, PubMed:28765278). Plays a key role for peroxisome movement through a direct interaction with tubulin (PubMed:21525035). {ECO:0000250|UniProtKB:P53112, ECO:0000269|PubMed:21525035, ECO:0000269|PubMed:24235149, ECO:0000269|PubMed:28765278, ECO:0000269|PubMed:9653144}.
|
Homo sapiens (Human)
|
O75382
|
TRIM3_HUMAN
|
MAKREDSPGPEVQPMDKQFLVCSICLDRYQCPKVLPCLHTFCERCLQNYIPAQSLTLSCPVCRQTSILPEQGVSALQNNFFISSLMEAMQQAPDGAHDPEDPHPLSVVAGRPLSCPNHEGKTMEFYCEACETAMCGECRAGEHREHGTVLLRDVVEQHKAALQRQLEAVRGRLPQLSAAIALVGGISQQLQERKAEALAQISAAFEDLEQALQQRKQALVSDLETICGAKQKVLQSQLDTLRQGQEHIGSSCSFAEQALRLGSAPEVLLVRKHMRERLAALAAQAFPERPHENAQLELVLEVDGLRRSVLNLGALLTTSATAHETVATGEGLRQALVGQPASLTVTTKDKDGRLVRTGSAELRAEITGPDGTRLPVPVVDHKNGTYELVYTARTEGELLLSVLLYGQPVRGSPFRVRALRPGDLPPSPDDVKRRVKSPGGPGSHVRQKAVRRPSSMYSTGGKRKDNPIEDELVFRVGSRGREKGEFTNLQGVSAASSGRIVVADSNNQCIQVFSNEGQFKFRFGVRGRSPGQLQRPTGVAVDTNGDIIVADYDNRWVSIFSPEGKFKTKIGAGRLMGPKGVAVDRNGHIIVVDNKSCCVFTFQPNGKLVGRFGGRGATDRHFAGPHFVAVNNKNEIVVTDFHNHSVKVYSADGEFLFKFGSHGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSFLSYINTSAEPLYGPQGLALTSDGHVVVADAGNHCFKAYRYLQ
|
2.3.2.27
| null |
negative regulation of translation [GO:0017148]; nervous system development [GO:0007399]; positive regulation of toll-like receptor 3 signaling pathway [GO:0034141]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein K63-linked ubiquitination [GO:0070534]; protein polyubiquitination [GO:0000209]; protein transport [GO:0015031]
|
cytoplasm [GO:0005737]; dendrite [GO:0030425]; early endosome [GO:0005769]; Golgi apparatus [GO:0005794]
|
identical protein binding [GO:0042802]; translation repressor activity [GO:0030371]; ubiquitin protein ligase activity [GO:0061630]; zinc ion binding [GO:0008270]
|
PF00630;PF01436;PF00643;PF00097;
|
3.30.160.60;2.60.40.10;2.120.10.30;3.30.40.10;
|
TRIM/RBCC family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:36481767}. Early endosome {ECO:0000269|PubMed:15772161, ECO:0000269|PubMed:32878999}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:32878999}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q9R1R2}. Note=Mainly located in the Golgi apparatus and transported to the early endosomes upon stimulation with dsRNA. {ECO:0000269|PubMed:32878999}.
|
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:24393003, ECO:0000269|PubMed:36481767};
| null | null | null | null |
FUNCTION: E3 ubiquitin ligase that plays essential roles in neuronal functions such as regulation of neuronal plasticity, learning, and memory (By similarity). In addition to its neuronal functions, participates in other biological processes such as innate immunity or cell cycle regulation. Component of the cytoskeleton-associated recycling or transport complex in neurons, polyubiquitinates gamma-actin, thus regulating neuronal plasticity, learning, and memory (By similarity). Ubiquitinates postsynaptic scaffold GKAP, a neuronal substrate involved in synaptic remodeling and thereby modulates dendritic spine morphology (By similarity). Positively regulates motility of microtubule-dependent motor protein KIF21B (By similarity). Induces growth arrest via its RING-dependent E3 ligase activity and ubiquinates CDKN1A (PubMed:24393003). Positively regulates TLR3-mediated signaling by mediating 'Lys-63'-linked polyubiquitination of TLR3 (PubMed:32878999). In turn, promotes the recognition and sorting of polyubiquitinated TLR3 by the ESCRT complexes (PubMed:32878999). {ECO:0000250|UniProtKB:Q9R1R2, ECO:0000269|PubMed:15772161, ECO:0000269|PubMed:24393003, ECO:0000269|PubMed:32878999}.
|
Homo sapiens (Human)
|
O75385
|
ULK1_HUMAN
|
MEPGRGGTETVGKFEFSRKDLIGHGAFAVVFKGRHREKHDLEVAVKCINKKNLAKSQTLLGKEIKILKELKHENIVALYDFQEMANSVYLVMEYCNGGDLADYLHAMRTLSEDTIRLFLQQIAGAMRLLHSKGIIHRDLKPQNILLSNPAGRRANPNSIRVKIADFGFARYLQSNMMAATLCGSPMYMAPEVIMSQHYDGKADLWSIGTIVYQCLTGKAPFQASSPQDLRLFYEKNKTLVPTIPRETSAPLRQLLLALLQRNHKDRMDFDEFFHHPFLDASPSVRKSPPVPVPSYPSSGSGSSSSSSSTSHLASPPSLGEMQQLQKTLASPADTAGFLHSSRDSGGSKDSSCDTDDFVMVPAQFPGDLVAEAPSAKPPPDSLMCSGSSLVASAGLESHGRTPSPSPPCSSSPSPSGRAGPFSSSRCGASVPIPVPTQVQNYQRIERNLQSPTQFQTPRSSAIRRSGSTSPLGFARASPSPPAHAEHGGVLARKMSLGGGRPYTPSPQVGTIPERPGWSGTPSPQGAEMRGGRSPRPGSSAPEHSPRTSGLGCRLHSAPNLSDLHVVRPKLPKPPTDPLGAVFSPPQASPPQPSHGLQSCRNLRGSPKLPDFLQRNPLPPILGSPTKAVPSFDFPKTPSSQNLLALLARQGVVMTPPRNRTLPDLSEVGPFHGQPLGPGLRPGEDPKGPFGRSFSTSRLTDLLLKAAFGTQAPDPGSTESLQEKPMEIAPSAGFGGSLHPGARAGGTSSPSPVVFTVGSPPSGSTPPQGPRTRMFSAGPTGSASSSARHLVPGPCSEAPAPELPAPGHGCSFADPITANLEGAVTFEAPDLPEETLMEQEHTEILRGLRFTLLFVQHVLEIAALKGSASEAAGGPEYQLQESVVADQISLLSREWGFAEQLVLYLKVAELLSSGLQSAIDQIRAGKLCLSSTVKQVVRRLNELYKASVVSCQGLSLRLQRFFLDKQRLLDRIHSITAERLIFSHAVQMVQSAALDEMFQHREGCVPRYHKALLLLEGLQHMLSDQADIENVTKCKLCIERRLSALLTGICA
|
2.7.11.1
| null |
autophagosome assembly [GO:0000045]; autophagy [GO:0006914]; axon extension [GO:0048675]; cellular response to nutrient levels [GO:0031669]; macroautophagy [GO:0016236]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of collateral sprouting [GO:0048671]; negative regulation of protein-containing complex assembly [GO:0031333]; neuron projection development [GO:0031175]; neuron projection regeneration [GO:0031102]; peptidyl-serine phosphorylation [GO:0018105]; peptidyl-threonine phosphorylation [GO:0018107]; piecemeal microautophagy of the nucleus [GO:0034727]; positive regulation of autophagosome assembly [GO:2000786]; positive regulation of autophagy [GO:0010508]; protein autophosphorylation [GO:0046777]; protein localization [GO:0008104]; protein phosphorylation [GO:0006468]; regulation of macroautophagy [GO:0016241]; regulation of protein lipidation [GO:1903059]; regulation of tumor necrosis factor-mediated signaling pathway [GO:0010803]; response to starvation [GO:0042594]; reticulophagy [GO:0061709]; signal transduction [GO:0007165]
|
Atg1/ULK1 kinase complex [GO:1990316]; autophagosome [GO:0005776]; autophagosome membrane [GO:0000421]; axon [GO:0030424]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; mitochondrial outer membrane [GO:0005741]; omegasome membrane [GO:1903349]; phagophore assembly site [GO:0000407]; phagophore assembly site membrane [GO:0034045]; recycling endosome [GO:0055037]
|
ATP binding [GO:0005524]; GTPase binding [GO:0051020]; identical protein binding [GO:0042802]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein-containing complex binding [GO:0044877]; small GTPase binding [GO:0031267]
|
PF12063;PF21127;PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, Ser/Thr protein kinase family, APG1/unc-51/ULK1 subfamily
|
PTM: Autophosphorylated. Phosphorylated under nutrient-rich conditions; dephosphorylated during starvation or following treatment with rapamycin. Under nutrient sufficiency, phosphorylated by MTOR/mTOR, disrupting the interaction with AMPK and preventing activation of ULK1 (By similarity). In response to nutrient limitation, phosphorylated and activated by AMPK, leading to activate autophagy (PubMed:21205641, PubMed:25891078). {ECO:0000250|UniProtKB:O70405, ECO:0000269|PubMed:21205641, ECO:0000269|PubMed:25891078}.; PTM: Ubiquitinated via 'Lys-63'-linkage by a complex composed of AMBRA1 and TRAF6 following autophagy induction, promoting ULK1 stability and kinase activity. Deubiquitinated by USP20; leading to ULK1 stability and autophagy initiation (PubMed:29487085). {ECO:0000269|PubMed:23524951, ECO:0000269|PubMed:29487085}.; PTM: Acetylated by KAT5/TIP60 under autophagy induction, promoting protein kinase activity. {ECO:0000250|UniProtKB:O70405}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Preautophagosomal structure {ECO:0000250}. Note=Under starvation conditions, is localized to puncate structures primarily representing the isolation membrane that sequesters a portion of the cytoplasm resulting in the formation of an autophagosome. {ECO:0000250}.
|
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; Evidence={ECO:0000269|PubMed:18936157, ECO:0000269|PubMed:25126726, ECO:0000269|PubMed:28821708, ECO:0000269|PubMed:31123703, ECO:0000269|PubMed:37306101}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; Evidence={ECO:0000269|PubMed:18936157, ECO:0000269|PubMed:25126726, ECO:0000269|PubMed:31123703, ECO:0000269|PubMed:37306101}; 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; Evidence={ECO:0000269|PubMed:18936157}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609; Evidence={ECO:0000269|PubMed:18936157};
| null | null | null | null |
FUNCTION: Serine/threonine-protein kinase involved in autophagy in response to starvation (PubMed:18936157, PubMed:21460634, PubMed:21795849, PubMed:23524951, PubMed:25040165, PubMed:29487085, PubMed:31123703). Acts upstream of phosphatidylinositol 3-kinase PIK3C3 to regulate the formation of autophagophores, the precursors of autophagosomes (PubMed:18936157, PubMed:21460634, PubMed:21795849, PubMed:25040165). Part of regulatory feedback loops in autophagy: acts both as a downstream effector and negative regulator of mammalian target of rapamycin complex 1 (mTORC1) via interaction with RPTOR (PubMed:21795849). Activated via phosphorylation by AMPK and also acts as a regulator of AMPK by mediating phosphorylation of AMPK subunits PRKAA1, PRKAB2 and PRKAG1, leading to negatively regulate AMPK activity (PubMed:21460634). May phosphorylate ATG13/KIAA0652 and RPTOR; however such data need additional evidences (PubMed:18936157). Plays a role early in neuronal differentiation and is required for granule cell axon formation (PubMed:11146101). Also phosphorylates SESN2 and SQSTM1 to regulate autophagy (PubMed:25040165, PubMed:37306101). Phosphorylates FLCN, promoting autophagy (PubMed:25126726). Phosphorylates AMBRA1 in response to autophagy induction, releasing AMBRA1 from the cytoskeletal docking site to induce autophagosome nucleation (PubMed:20921139). Phosphorylates ATG4B, leading to inhibit autophagy by decreasing both proteolytic activation and delipidation activities of ATG4B (PubMed:28821708). {ECO:0000269|PubMed:11146101, ECO:0000269|PubMed:18936157, ECO:0000269|PubMed:20921139, ECO:0000269|PubMed:21460634, ECO:0000269|PubMed:21795849, ECO:0000269|PubMed:23524951, ECO:0000269|PubMed:25040165, ECO:0000269|PubMed:25126726, ECO:0000269|PubMed:28821708, ECO:0000269|PubMed:29487085, ECO:0000269|PubMed:31123703, ECO:0000269|PubMed:37306101}.
|
Homo sapiens (Human)
|
O75386
|
TULP3_HUMAN
|
MEASRCRLSPSGDSVFHEEMMKMRQAKLDYQRLLLEKRQRKKRLEPFMVQPNPEARLRRAKPRASDEQTPLVNCHTPHSNVILHGIDGPAAVLKPDEVHAPSVSSSVVEEDAENTVDTASKPGLQERLQKHDISESVNFDEETDGISQSACLERPNSASSQNSTDTGTSGSATAAQPADNLLGDIDDLEDFVYSPAPQGVTVRCRIIRDKRGMDRGLFPTYYMYLEKEENQKIFLLAARKRKKSKTANYLISIDPVDLSREGESYVGKLRSNLMGTKFTVYDRGICPMKGRGLVGAAHTRQELAAISYETNVLGFKGPRKMSVIIPGMTLNHKQIPYQPQNNHDSLLSRWQNRTMENLVELHNKAPVWNSDTQSYVLNFRGRVTQASVKNFQIVHKNDPDYIVMQFGRVADDVFTLDYNYPLCAVQAFGIGLSSFDSKLACE
| null | null |
anterior/posterior pattern specification [GO:0009952]; bone development [GO:0060348]; brain development [GO:0007420]; bronchus morphogenesis [GO:0060434]; central nervous system neuron differentiation [GO:0021953]; embryonic camera-type eye development [GO:0031076]; embryonic digit morphogenesis [GO:0042733]; embryonic neurocranium morphogenesis [GO:0048702]; G protein-coupled receptor signaling pathway [GO:0007186]; ganglion development [GO:0061548]; negative regulation of smoothened signaling pathway [GO:0045879]; neural tube closure [GO:0001843]; protein localization to cilium [GO:0061512]; regulation of DNA-templated transcription [GO:0006355]; regulation of G protein-coupled receptor signaling pathway [GO:0008277]; smoothened signaling pathway involved in dorsal/ventral neural tube patterning [GO:0060831]
|
9+0 non-motile cilium [GO:0097731]; axoneme [GO:0005930]; ciliary base [GO:0097546]; cilium [GO:0005929]; extracellular region [GO:0005576]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
enzyme binding [GO:0019899]; G protein-coupled receptor binding [GO:0001664]; intraciliary transport particle A binding [GO:0120160]; phosphatidylinositol binding [GO:0035091]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; protein-containing complex binding [GO:0044877]
|
PF01167;PF16322;
| null |
TUB family
| null |
SUBCELLULAR LOCATION: Nucleus. Cell membrane. Cell projection, cilium {ECO:0000269|PubMed:27932497, ECO:0000269|PubMed:35397207}. Cytoplasm {ECO:0000250}. Secreted {ECO:0000250}. Note=Does not have a cleavable signal peptide and is secreted by a non-conventional pathway (By similarity). Translocates from the plasma membrane to the nucleus upon activation of guanine nucleotide-binding protein G(q) subunit alpha. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Negative regulator of the Shh signaling transduction pathway: recruited to primary cilia via association with the IFT complex A (IFT-A) and is required for recruitment of G protein-coupled receptor GPR161 to cilia, a promoter of PKA-dependent basal repression machinery in Shh signaling. Binds to phosphorylated inositide (phosphoinositide) lipids. Both IFT-A- and phosphoinositide-binding properties are required to regulate ciliary G protein-coupled receptor trafficking. During adipogenesis, regulates ciliary trafficking of FFAR4 in preadipocytes. {ECO:0000269|PubMed:11375483, ECO:0000269|PubMed:20889716, ECO:0000269|PubMed:31761534}.
|
Homo sapiens (Human)
|
O75387
|
LAT3_HUMAN
|
MAPTLQQAYRRRWWMACTAVLENLFFSAVLLGWGSLLIILKNEGFYSSTCPAESSTNTTQDEQRRWPGCDQQDEMLNLGFTIGSFVLSATTLPLGILMDRFGPRPVRLVGSACFTASCTLMALASRDVEALSPLIFLALSLNGFGGICLTFTSLTLPNMFGNLRSTLMALMIGSYASSAITFPGIKLIYDAGVAFVVIMFTWSGLACLIFLNCTLNWPIEAFPAPEEVNYTKKIKLSGLALDHKVTGDLFYTHVTTMGQRLSQKAPSLEDGSDAFMSPQDVRGTSENLPERSVPLRKSLCSPTFLWSLLTMGMTQLRIIFYMAAVNKMLEYLVTGGQEHETNEQQQKVAETVGFYSSVFGAMQLLCLLTCPLIGYIMDWRIKDCVDAPTQGTVLGDARDGVATKSIRPRYCKIQKLTNAISAFTLTNLLLVGFGITCLINNLHLQFVTFVLHTIVRGFFHSACGSLYAAVFPSNHFGTLTGLQSLISAVFALLQQPLFMAMVGPLKGEPFWVNLGLLLFSLLGFLLPSYLFYYRARLQQEYAANGMGPLKVLSGSEVTA
| null | null |
amino acid transport [GO:0006865]; isoleucine transport [GO:0015818]; L-valine transmembrane transport [GO:1903785]; leucine transport [GO:0015820]; negative regulation of amino acid transport [GO:0051956]; negative regulation of leucine import [GO:0060358]; neutral amino acid transport [GO:0015804]
|
apical plasma membrane [GO:0016324]; endoplasmic reticulum membrane [GO:0005789]; plasma membrane [GO:0005886]; podocyte foot [GO:0098846]
|
amino acid transmembrane transporter activity [GO:0015171]; L-amino acid transmembrane transporter activity [GO:0015179]; L-isoleucine transmembrane transporter activity [GO:0015188]; L-leucine transmembrane transporter activity [GO:0015190]; L-valine transmembrane transporter activity [GO:0005304]; neutral L-amino acid transmembrane transporter activity [GO:0015175]
|
PF07690;
|
1.20.1250.20;
|
SLC43A transporter (TC 2.A.1.44) family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8BSM7}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000269|PubMed:19443642}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8BSM7}; Multi-pass membrane protein {ECO:0000255}. Note=Located in the apical plasma membrane of the podocyte foot processes (PubMed:19443642). Located in the plasma membrane of liver and skeletal muscle, and in the endoplasmic reticulum and in crystalline inclusions in pancreatic acinar cells (By similarity). {ECO:0000250|UniProtKB:Q8BSM7, ECO:0000269|PubMed:19443642}.
|
CATALYTIC ACTIVITY: Reaction=D-leucine(in) = D-leucine(out); Xref=Rhea:RHEA:73015, ChEBI:CHEBI:143079; Evidence={ECO:0000269|PubMed:12930836}; CATALYTIC ACTIVITY: Reaction=L-leucine(in) = L-leucine(out); Xref=Rhea:RHEA:73011, ChEBI:CHEBI:57427; Evidence={ECO:0000269|PubMed:12930836}; CATALYTIC ACTIVITY: Reaction=L-isoleucine(in) = L-isoleucine(out); Xref=Rhea:RHEA:70943, ChEBI:CHEBI:58045; Evidence={ECO:0000269|PubMed:12930836}; CATALYTIC ACTIVITY: Reaction=L-methionine(in) = L-methionine(out); Xref=Rhea:RHEA:70939, ChEBI:CHEBI:57844; Evidence={ECO:0000269|PubMed:12930836}; CATALYTIC ACTIVITY: Reaction=L-phenylalanine(in) = L-phenylalanine(out); Xref=Rhea:RHEA:27950, ChEBI:CHEBI:58095; Evidence={ECO:0000269|PubMed:12930836}; CATALYTIC ACTIVITY: Reaction=L-valine(in) = L-valine(out); Xref=Rhea:RHEA:29703, ChEBI:CHEBI:57762; Evidence={ECO:0000269|PubMed:12930836};
| null | null | null | null |
FUNCTION: Uniport that mediates the transport of neutral amino acids such as L-leucine, L-isoleucine, L-valine, and L-phenylalanine (PubMed:12930836). The transport activity is sodium ions-independent, electroneutral and mediated by a facilitated diffusion (PubMed:12930836). {ECO:0000269|PubMed:12930836}.
|
Homo sapiens (Human)
|
O75390
|
CISY_HUMAN
|
MALLTAAARLLGTKNASCLVLAARHASASSTNLKDILADLIPKEQARIKTFRQQHGKTVVGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGFSIPECQKLLPKAKGGEEPLPEGLFWLLVTGHIPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAVTALNSESNFARAYAQGISRTKYWELIYEDSMDLIAKLPCVAAKIYRNLYREGSGIGAIDSNLDWSHNFTNMLGYTDHQFTELTRLYLTIHSDHEGGNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTQLQKEVGKDVSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFALKHLPNDPMFKLVAQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRALGVLAQLIWSRALGFPLERPKSMSTEGLMKFVDSKSG
|
2.3.3.1
| null |
carbohydrate metabolic process [GO:0005975]; citrate metabolic process [GO:0006101]; tricarboxylic acid cycle [GO:0006099]
|
extracellular exosome [GO:0070062]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; nucleus [GO:0005634]
|
citrate (Si)-synthase activity [GO:0004108]; RNA binding [GO:0003723]
|
PF00285;
|
1.10.580.10;1.10.230.10;
|
Citrate synthase family
|
PTM: Methylated (PubMed:28391595, PubMed:28887308). Trimethylation at Lys-395 by CSKMT decreases citrate synthase activity (PubMed:28887308). {ECO:0000269|PubMed:28391595, ECO:0000269|PubMed:28887308}.
|
SUBCELLULAR LOCATION: Mitochondrion matrix.
|
CATALYTIC ACTIVITY: Reaction=acetyl-CoA + H2O + oxaloacetate = citrate + CoA + H(+); Xref=Rhea:RHEA:16845, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, ChEBI:CHEBI:16947, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.3.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10117};
| null |
PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 1/2.
| null | null | null |
Homo sapiens (Human)
|
O75396
|
SC22B_HUMAN
|
MVLLTMIARVADGLPLAASMQEDEQSGRDLQQYQSQAKQLFRKLNEQSPTRCTLEAGAMTFHYIIEQGVCYLVLCEAAFPKKLAFAYLEDLHSEFDEQHGKKVPTVSRPYSFIEFDTFIQKTKKLYIDSRARRNLGSINTELQDVQRIMVANIEEVLQRGEALSALDSKANNLSSLSKKYRQDAKYLNMRSTYAKLAAVAVFFIMLIVYVRFWWL
| null | null |
endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; negative regulation of autophagosome assembly [GO:1902902]; positive regulation of protein catabolic process [GO:0045732]; protein transport [GO:0015031]; retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum [GO:0006890]; vesicle fusion with Golgi apparatus [GO:0048280]
|
endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; ER to Golgi transport vesicle membrane [GO:0012507]; Golgi membrane [GO:0000139]; melanosome [GO:0042470]; phagocytic vesicle membrane [GO:0030670]; SNARE complex [GO:0031201]; transport vesicle [GO:0030133]
|
SNAP receptor activity [GO:0005484]
|
PF13774;PF00957;
|
1.20.5.110;3.30.450.50;
|
Synaptobrevin family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q4KM74}; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:Q4KM74}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q4KM74}. Golgi apparatus, cis-Golgi network membrane {ECO:0000250|UniProtKB:Q4KM74}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q4KM74}. Melanosome {ECO:0000269|PubMed:17081065}. 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). Identified by mass spectrometry in melanosome fractions from stage I to stage IV (PubMed:17081065). {ECO:0000250|UniProtKB:Q4KM74, ECO:0000269|PubMed:17081065}.
| null | null | null | null | null |
FUNCTION: SNARE involved in targeting and fusion of ER-derived transport vesicles with the Golgi complex as well as Golgi-derived retrograde transport vesicles with the ER. {ECO:0000269|PubMed:15272311}.
|
Homo sapiens (Human)
|
O75398
|
DEAF1_HUMAN
|
MEDSDSAAKQLGLAEAAAVAAAAAVAAAAAAAAGGEAEEPVLSRDEDSEEDADSEAERETPRVTAVAVMAAEPGHMDMGAEALPGPDEAAAAAAFAEVTTVTVANVGAAADNVFTTSVANAASISGHVLSGRTALQIGDSLNTEKATLIVVHTDGSIVETTGLKGPAAPLTPGPQSPPTPLAPGQEKGGTKYNWDPSVYDSELPVRCRNISGTLYKNRLGSGGRGRCIKQGENWYSPTEFEAMAGRASSKDWKRSIRYAGRPLQCLIQDGILNPHAASCTCAACCDDMTLSGPVRLFVPYKRRKKENELPTTPVKKDSPKNITLLPATAATTFTVTPSGQITTSGALTFDRASTVEATAVISESPAQGDVFAGATVQEASVQPPCRASHPEPHYPGYQDSCQIAPFPEAALPTSHPKIVLTSLPALAVPPPTPTKAAPPALVNGLELSEPRSWLYLEEMVNSLLNTAQQLKTLFEQAKHASTYREAATNQAKIHADAERKEQSCVNCGREAMSECTGCHKVNYCSTFCQRKDWKDHQHICGQSAAVTVQADEVHVAESVMEKVTV
| null | null |
anatomical structure morphogenesis [GO:0009653]; embryonic skeletal system development [GO:0048706]; germ cell development [GO:0007281]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neural tube closure [GO:0001843]; positive regulation of DNA-templated transcription [GO:0045893]; regulation of mammary gland epithelial cell proliferation [GO:0033599]; regulation of transcription by RNA polymerase II [GO:0006357]; transcription by RNA polymerase II [GO:0006366]
|
chromatin [GO:0000785]; cytoplasm [GO:0005737]; extracellular region [GO:0005576]; fibrillar center [GO:0001650]; nucleoplasm [GO:0005654]; 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]
|
PF01342;PF01753;
|
6.10.140.2220;3.10.390.10;
| null |
PTM: May be phosphorylated by DNA-PK complex in a DNA independent manner (in vitro). {ECO:0000269|PubMed:22442688}.
|
SUBCELLULAR LOCATION: [Isoform 1]: Nucleus. Cytoplasm. Note=Cytoplasmic in non-mucinous colorectal carcinoma. When expressed alone, localized almost exclusively in the nucleus but, when expressed with isoform 4, nuclear expression decreases to 32% and cytoplasmic expression increases by 270%.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted. Note=Secreted in some cell types.; SUBCELLULAR LOCATION: [Isoform 3]: Secreted. Note=Secreted in some cell types.; SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm. Nucleus. Note=When expressed alone, localizes mainly in the cytoplasm but, when expressed with isoform 1, nuclear localization is enhanced.
| null | null | null | null | null |
FUNCTION: Transcription factor that binds to sequence with multiple copies of 5'-TTC[CG]G-3' present in its own promoter and that of the HNRPA2B1 gene. Down-regulates transcription of these genes. Binds to the retinoic acid response element (RARE) 5'-AGGGTTCACCGAAAGTTCA-3'. Activates the proenkephalin gene independently of promoter binding, probably through protein-protein interaction. When secreted, behaves as an inhibitor of cell proliferation, by arresting cells in the G0 or G1 phase. Required for neural tube closure and skeletal patterning. Regulates epithelial cell proliferation and side-branching in the mammary gland. Controls the expression of peripheral tissue antigens in pancreatic lymph nodes. Isoform 1 displays greater transcriptional activity than isoform 4. Isoform 4 may inhibit transcriptional activity of isoform 1 by interacting with isoform 1 and retaining it in the cytoplasm. Transcriptional activator of EIF4G3. {ECO:0000269|PubMed:10521432, ECO:0000269|PubMed:11427895, ECO:0000269|PubMed:11705868, ECO:0000269|PubMed:18826651, ECO:0000269|PubMed:19668219, ECO:0000269|PubMed:24726472}.
|
Homo sapiens (Human)
|
O75400
|
PR40A_HUMAN
|
MRPGTGAERGGLMVSEMESHPPSQGPGDGERRLSGSSLCSGSWVSADGFLRRRPSMGHPGMHYAPMGMHPMGQRANMPPVPHGMMPQMMPPMGGPPMGQMPGMMSSVMPGMMMSHMSQASMQPALPPGVNSMDVAAGTASGAKSMWTEHKSPDGRTYYYNTETKQSTWEKPDDLKTPAEQLLSKCPWKEYKSDSGKPYYYNSQTKESRWAKPKELEDLEGYQNTIVAGSLITKSNLHAMIKAEESSKQEECTTTSTAPVPTTEIPTTMSTMAAAEAAAAVVAAAAAAAAAAAAANANASTSASNTVSGTVPVVPEPEVTSIVATVVDNENTVTISTEEQAQLTSTPAIQDQSVEVSSNTGEETSKQETVADFTPKKEEEESQPAKKTYTWNTKEEAKQAFKELLKEKRVPSNASWEQAMKMIINDPRYSALAKLSEKKQAFNAYKVQTEKEEKEEARSKYKEAKESFQRFLENHEKMTSTTRYKKAEQMFGEMEVWNAISERDRLEIYEDVLFFLSKKEKEQAKQLRKRNWEALKNILDNMANVTYSTTWSEAQQYLMDNPTFAEDEELQNMDKEDALICFEEHIRALEKEEEEEKQKSLLRERRRQRKNRESFQIFLDELHEHGQLHSMSSWMELYPTISSDIRFTNMLGQPGSTALDLFKFYVEDLKARYHDEKKIIKDILKDKGFVVEVNTTFEDFVAIISSTKRSTTLDAGNIKLAFNSLLEKAEAREREREKEEARKMKRKESAFKSMLKQAAPPIELDAVWEDIRERFVKEPAFEDITLESERKRIFKDFMHVLEHECQHHHSKNKKHSKKSKKHHRKRSRSRSGSDSDDDDSHSKKKRQRSESRSASEHSSSAESERSYKKSKKHKKKSKKRRHKSDSPESDAEREKDKKEKDRESEKDRTRQRSESKHKSPKKKTGKDSGNWDTSGSELSEGELEKRRRTLLEQLDDDQ
| null | null |
cell cycle [GO:0007049]; cell division [GO:0051301]; cell migration [GO:0016477]; cytoskeleton organization [GO:0007010]; mRNA cis splicing, via spliceosome [GO:0045292]; mRNA splicing, via spliceosome [GO:0000398]; regulation of cell shape [GO:0008360]; regulation of cytokinesis [GO:0032465]
|
membrane [GO:0016020]; nuclear matrix [GO:0016363]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; U1 snRNP [GO:0005685]; U2-type prespliceosome [GO:0071004]
|
RNA binding [GO:0003723]
|
PF01846;PF00397;
|
2.20.70.10;1.10.10.440;
|
PRPF40 family
| null |
SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}. Nucleus matrix {ECO:0000269|PubMed:16391387}. Note=Colocalizes with AKAP8L in the nuclear matrix. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Binds to WASL/N-WASP and suppresses its translocation from the nucleus to the cytoplasm, thereby inhibiting its cytoplasmic function (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration. May play a role in cytokinesis. May be involved in pre-mRNA splicing. {ECO:0000250, ECO:0000269|PubMed:21834987}.
|
Homo sapiens (Human)
|
O75409
|
HYPM_HUMAN
|
MSEKKNCKNSSTNNNQTQDPSRNELQVPRSFVDRVVQDERDVQSQSSSTINTLLTLLDCLADYIMERVGLEASNNGSMRNTSQDREREVDNNREPHSAESDVTRFLFDEMPKSRKND
| null | null |
heterochromatin organization [GO:0070828]
|
nucleosome [GO:0000786]; nucleus [GO:0005634]
|
nucleosomal DNA binding [GO:0031492]; protein heterodimerization activity [GO:0046982]
| null |
1.10.20.10;
| null | null | null | null | null | null | null | null | null |
Homo sapiens (Human)
|
O75410
|
TACC1_HUMAN
|
MAFSPWQILSPVQWAKWTWSAVRGGAAGEDEAGGPEGDPEEEDSQAETKSLSFSSDSEGNFETPEAETPIRSPFKESCDPSLGLAGPGAKSQESQEADEQLVAEVVEKCSSKTCSKPSENEVPQQAIDSHSVKNFREEPEHDFSKISIVRPFSIETKDSTDISAVLGTKAAHGCVTAVSGKALPSSPPDALQDEAMTEGSMGVTLEASAEADLKAGNSCPELVPSRRSKLRKPKPVPLRKKAIGGEFSDTNAAVEGTPLPKASYHFSPEELDENTSPLLGDARFQKSPPDLKETPGTLSSDTNDSGVELGEESRSSPLKLEFDFTEDTGNIEARKALPRKLGRKLGSTLTPKIQKDGISKSAGLEQPTDPVARDGPLSQTSSKPDPSQWESPSFNPFGSHSVLQNSPPLSSEGSYHFDPDNFDESMDPFKPTTTLTSSDFCSPTGNHVNEILESPKKAKSRLITSGCKVKKHETQSLALDACSRDEGAVISQISDISNRDGHATDEEKLASTSCGQKSAGAEVKGEPEEDLEYFECSNVPVSTINHAFSSSEAGIEKETCQKMEEDGSTVLGLLESSAEKAPVSVSCGGESPLDGICLSESDKTAVLTLIREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRTSMTSQKSFQQLTMEKEQALADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAKAESAALHAGLRKEQMKVESLERALQQKNQEIEELTKICDELIAKLGKTD
| null | null |
cell division [GO:0051301]; cell population proliferation [GO:0008283]; cerebral cortex development [GO:0021987]; microtubule cytoskeleton organization [GO:0000226]; mitotic spindle organization [GO:0007052]
|
centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; midbody [GO:0030496]; nucleus [GO:0005634]
|
nuclear estrogen receptor binding [GO:0030331]; nuclear glucocorticoid receptor binding [GO:0035259]; nuclear receptor binding [GO:0016922]; nuclear receptor coactivator activity [GO:0030374]; nuclear retinoic acid receptor binding [GO:0042974]; nuclear retinoid X receptor binding [GO:0046965]; nuclear thyroid hormone receptor binding [GO:0046966]; peroxisome proliferator activated receptor binding [GO:0042975]
|
PF05010;
|
1.20.5.1700;
|
TACC family
|
PTM: Isoform 1 is heavily phosphorylated; isoform 6 is not. {ECO:0000269|PubMed:12165861, ECO:0000269|PubMed:21531210}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14767476}. Nucleus {ECO:0000269|PubMed:14767476}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:21531210}. Midbody {ECO:0000269|PubMed:21531210}. Note=Nucleus during interphase. Weakly concentrated at centrosomes during mitosis and colocalizes with AURKC at the midbody during cytokinesis. {ECO:0000269|PubMed:21531210}.; SUBCELLULAR LOCATION: [Isoform 5]: Membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 10]: Cytoplasm {ECO:0000269|PubMed:20078863}.
| null | null | null | null | null |
FUNCTION: Involved in transcription regulation induced by nuclear receptors, including in T3 thyroid hormone and all-trans retinoic acid pathways (PubMed:20078863). Might promote the nuclear localization of the receptors (PubMed:20078863). Likely involved in the processes that promote cell division prior to the formation of differentiated tissues. {ECO:0000269|PubMed:20078863}.
|
Homo sapiens (Human)
|
O75414
|
NDK6_HUMAN
|
MASILRSPQALQLTLALIKPDAVAHPLILEAVHQQILSNKFLIVRMRELLWRKEDCQRFYREHEGRFFYQRLVEFMASGPIRAYILAHKDAIQLWRTLMGPTRVFRARHVAPDSIRGSFGLTDTRNTTHGSDSVVSASREIAAFFPDFSEQRWYEEEEPQLRCGPVCYSPEGGVHYVAGTGGLGPA
|
2.7.4.6
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
|
apoptotic process [GO:0006915]; CTP biosynthetic process [GO:0006241]; GTP biosynthetic process [GO:0006183]; negative regulation of cell growth [GO:0030308]; negative regulation of mitotic nuclear division [GO:0045839]; phosphorylation [GO:0016310]; UTP biosynthetic process [GO:0006228]
|
mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]
|
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; nucleoside diphosphate kinase activity [GO:0004550]
|
PF00334;
|
3.30.70.141;
|
NDK family
| null | null |
CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:44640, ChEBI:CHEBI:30616, ChEBI:CHEBI:61560, ChEBI:CHEBI:73316, ChEBI:CHEBI:456216; EC=2.7.4.6; Evidence={ECO:0000255|PROSITE-ProRule:PRU10030}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-diphosphate + ATP = a ribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:18113, ChEBI:CHEBI:30616, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557, ChEBI:CHEBI:456216; EC=2.7.4.6; Evidence={ECO:0000255|PROSITE-ProRule:PRU10030};
| null | null | null | null |
FUNCTION: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Inhibitor of p53-induced apoptosis.
|
Homo sapiens (Human)
|
O75417
|
DPOLQ_HUMAN
|
MNLLRRSGKRRRSESGSDSFSGSGGDSSASPQFLSGSVLSPPPGLGRCLKAAAAGECKPTVPDYERDKLLLANWGLPKAVLEKYHSFGVKKMFEWQAECLLLGQVLEGKNLVYSAPTSAGKTLVAELLILKRVLEMRKKALFILPFVSVAKEKKYYLQSLFQEVGIKVDGYMGSTSPSRHFSSLDIAVCTIERANGLINRLIEENKMDLLGMVVVDELHMLGDSHRGYLLELLLTKICYITRKSASCQADLASSLSNAVQIVGMSATLPNLELVASWLNAELYHTDFRPVPLLESVKVGNSIYDSSMKLVREFEPMLQVKGDEDHVVSLCYETICDNHSVLLFCPSKKWCEKLADIIAREFYNLHHQAEGLVKPSECPPVILEQKELLEVMDQLRRLPSGLDSVLQKTVPWGVAFHHAGLTFEERDIIEGAFRQGLIRVLAATSTLSSGVNLPARRVIIRTPIFGGRPLDILTYKQMVGRAGRKGVDTVGESILICKNSEKSKGIALLQGSLKPVRSCLQRREGEEVTGSMIRAILEIIVGGVASTSQDMHTYAACTFLAASMKEGKQGIQRNQESVQLGAIEACVMWLLENEFIQSTEASDGTEGKVYHPTHLGSATLSSSLSPADTLDIFADLQRAMKGFVLENDLHILYLVTPMFEDWTTIDWYRFFCLWEKLPTSMKRVAELVGVEEGFLARCVKGKVVARTERQHRQMAIHKRFFTSLVLLDLISEVPLREINQKYGCNRGQIQSLQQSAAVYAGMITVFSNRLGWHNMELLLSQFQKRLTFGIQRELCDLVRVSLLNAQRARVLYASGFHTVADLARANIVEVEVILKNAVPFKSARKAVDEEEEAVEERRNMRTIWVTGRKGLTEREAAALIVEEARMILQQDLVEMGVQWNPCALLHSSTCSLTHSESEVKEHTFISQTKSSYKKLTSKNKSNTIFSDSYIKHSPNIVQDLNKSREHTSSFNCNFQNGNQEHQTCSIFRARKRASLDINKEKPGASQNEGKTSDKKVVQTFSQKTKKAPLNFNSEKMSRSFRSWKRRKHLKRSRDSSPLKDSGACRIHLQGQTLSNPSLCEDPFTLDEKKTEFRNSGPFAKNVSLSGKEKDNKTSFPLQIKQNCSWNITLTNDNFVEHIVTGSQSKNVTCQATSVVSEKGRGVAVEAEKINEVLIQNGSKNQNVYMKHHDIHPINQYLRKQSHEQTSTITKQKNIIERQMPCEAVSSYINRDSNVTINCERIKLNTEENKPSHFQALGDDISRTVIPSEVLPSAGAFSKSEGQHENFLNISRLQEKTGTYTTNKTKNNHVSDLGLVLCDFEDSFYLDTQSEKIIQQMATENAKLGAKDTNLAAGIMQKSLVQQNSMNSFQKECHIPFPAEQHPLGATKIDHLDLKTVGTMKQSSDSHGVDILTPESPIFHSPILLEENGLFLKKNEVSVTDSQLNSFLQGYQTQETVKPVILLIPQKRTPTGVEGECLPVPETSLNMSDSLLFDSFSDDYLVKEQLPDMQMKEPLPSEVTSNHFSDSLCLQEDLIKKSNVNENQDTHQQLTCSNDESIIFSEMDSVQMVEALDNVDIFPVQEKNHTVVSPRALELSDPVLDEHHQGDQDGGDQDERAEKSKLTGTRQNHSFIWSGASFDLSPGLQRILDKVSSPLENEKLKSMTINFSSLNRKNTELNEEQEVISNLETKQVQGISFSSNNEVKSKIEMLENNANHDETSSLLPRKESNIVDDNGLIPPTPIPTSASKLTFPGILETPVNPWKTNNVLQPGESYLFGSPSDIKNHDLSPGSRNGFKDNSPISDTSFSLQLSQDGLQLTPASSSSESLSIIDVASDQNLFQTFIKEWRCKKRFSISLACEKIRSLTSSKTATIGSRFKQASSPQEIPIRDDGFPIKGCDDTLVVGLAVCWGGRDAYYFSLQKEQKHSEISASLVPPSLDPSLTLKDRMWYLQSCLRKESDKECSVVIYDFIQSYKILLLSCGISLEQSYEDPKVACWLLDPDSQEPTLHSIVTSFLPHELPLLEGMETSQGIQSLGLNAGSEHSGRYRASVESILIFNSMNQLNSLLQKENLQDVFRKVEMPSQYCLALLELNGIGFSTAECESQKHIMQAKLDAIETQAYQLAGHSFSFTSSDDIAEVLFLELKLPPNREMKNQGSKKTLGSTRRGIDNGRKLRLGRQFSTSKDVLNKLKALHPLPGLILEWRRITNAITKVVFPLQREKCLNPFLGMERIYPVSQSHTATGRITFTEPNIQNVPRDFEIKMPTLVGESPPSQAVGKGLLPMGRGKYKKGFSVNPRCQAQMEERAADRGMPFSISMRHAFVPFPGGSILAADYSQLELRILAHLSHDRRLIQVLNTGADVFRSIAAEWKMIEPESVGDDLRQQAKQICYGIIYGMGAKSLGEQMGIKENDAACYIDSFKSRYTGINQFMTETVKNCKRDGFVQTILGRRRYLPGIKDNNPYRKAHAERQAINTIVQGSAADIVKIATVNIQKQLETFHSTFKSHGHREGMLQSDQTGLSRKRKLQGMFCPIRGGFFILQLHDELLYEVAEEDVVQVAQIVKNEMESAVKLSVKLKVKVKIGASWGELKDFDV
|
2.7.7.49; 2.7.7.7; 3.6.4.12
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:25775267, ECO:0000269|PubMed:27311885, ECO:0000269|PubMed:33577776};
|
base-excision repair [GO:0006284]; DNA damage response [GO:0006974]; DNA repair [GO:0006281]; double-strand break repair [GO:0006302]; double-strand break repair via alternative nonhomologous end joining [GO:0097681]; error-prone translesion synthesis [GO:0042276]; negative regulation of double-strand break repair via homologous recombination [GO:2000042]; protein homooligomerization [GO:0051260]; replication fork processing [GO:0031297]; somatic hypermutation of immunoglobulin genes [GO:0016446]
|
cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; nucleoplasm [GO:0005654]; site of DNA damage [GO:0090734]; site of double-strand break [GO:0035861]
|
5'-deoxyribose-5-phosphate lyase activity [GO:0051575]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; chromatin binding [GO:0003682]; damaged DNA binding [GO:0003684]; DNA helicase activity [GO:0003678]; DNA-directed DNA polymerase activity [GO:0003887]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; RNA-directed DNA polymerase activity [GO:0003964]; single-stranded DNA endodeoxyribonuclease activity [GO:0000014]; single-stranded DNA helicase activity [GO:0017116]
|
PF00270;PF00476;PF00271;PF20470;PF21099;
|
1.10.3380.20;3.30.70.370;1.10.150.20;3.40.50.300;3.30.420.10;
|
DNA polymerase type-A family
|
PTM: Phosphorylated by PLK1; promoting interaction with TOPBP1 and recruitment to DNA damage sites. {ECO:0000269|PubMed:37674080}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O18475}. Chromosome {ECO:0000269|PubMed:25642963, ECO:0000269|PubMed:34179826, ECO:0000269|PubMed:37440612, ECO:0000269|PubMed:37674080}. Note=Enriched in chromatin in response to ultaviolet (UV) light (PubMed:25642963, PubMed:34179826). Binds to chromatin during early G1 (PubMed:24989122). Recruited to DNA damage sites, such as double-stranded breaks (DSBs), following interaction with TOPBP1 and RHNO1 (PubMed:37440612, PubMed:37674080). {ECO:0000269|PubMed:24989122, ECO:0000269|PubMed:25642963, ECO:0000269|PubMed:34179826, ECO:0000269|PubMed:37440612, ECO:0000269|PubMed:37674080}.
|
CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7; Evidence={ECO:0000269|PubMed:14576298, ECO:0000269|PubMed:22135286, ECO:0000269|PubMed:25775267, ECO:0000269|PubMed:27311885, ECO:0000269|PubMed:27591252}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; Evidence={ECO:0000269|PubMed:36455556}; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.49; Evidence={ECO:0000305|PubMed:34117057};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.095 uM for dATP:T {ECO:0000269|PubMed:22135286}; KM=0.622 uM for dATP: abasic site {ECO:0000269|PubMed:22135286}; KM=3.08 uM for dGTP: no template {ECO:0000269|PubMed:22135286};
| null | null | null |
FUNCTION: Low-fidelity DNA polymerase with a helicase activity that promotes microhomology-mediated end-joining (MMEJ), an alternative non-homologous end-joining (NHEJ) machinery required to repair double-strand breaks in DNA during mitosis (PubMed:14576298, PubMed:18503084, PubMed:24648516, PubMed:25642963, PubMed:25643323, PubMed:25775267, PubMed:26636256, PubMed:27311885, PubMed:27591252, PubMed:30655289, PubMed:31562312, PubMed:32873648, PubMed:34140467, PubMed:34179826, PubMed:36455556, PubMed:37440612, PubMed:37674080). MMEJ is an error-prone repair pathway that produces deletions of sequences from the strand being repaired and promotes genomic rearrangements, such as telomere fusions, some of them leading to cellular transformation (PubMed:25642963, PubMed:25643323, PubMed:25775267, PubMed:27311885, PubMed:27591252, PubMed:31562312, PubMed:32873648). MMEJ is required during mitosis to repair persistent double-strand breaks that originate in S-phase (PubMed:37440612, PubMed:37674080). Although error-prone, MMEJ protects against chromosomal instability and tumorigenesis (By similarity). The polymerase acts by binding directly the 2 ends of resected double-strand breaks, allowing microhomologous sequences in the overhangs to form base pairs (PubMed:25643323, PubMed:25775267, PubMed:27311885, PubMed:27591252). It then extends each strand from the base-paired region using the opposing overhang as a template (PubMed:25643323, PubMed:25775267, PubMed:27311885, PubMed:27591252). Requires partially resected DNA containing 2 to 6 base pairs of microhomology to perform MMEJ (PubMed:25643323, PubMed:25775267, PubMed:27311885, PubMed:27591252). The polymerase lacks proofreading activity and is highly promiscuous: unlike most polymerases, promotes extension of ssDNA and partial ssDNA (pssDNA) substrates (PubMed:18503084, PubMed:21050863, PubMed:22135286). When the ends of a break do not contain terminal microhomology must identify embedded complementary sequences through a scanning step (PubMed:32234782). Also shows endonuclease activity, which is required to trim the 3' ends before synthesis can occur, thereby preventing non-paired tails (PubMed:33577776). Also acts as a DNA helicase, promoting dissociation of the replication protein A complex (RPA/RP-A), composed of RPA1, RPA2 and RPA3, from resected double-strand breaks to allow their annealing and subsequent joining by MMEJ (PubMed:36455556). Removal of RPA/RP-A complex proteins prevents RAD51 accumulation at resected ends, thereby inhibiting homology-recombination repair (HR) pathway (PubMed:25642963, PubMed:28695890). Also shows RNA-directed DNA polymerase activity to mediate DNA repair in vitro; however this activity needs additional evidence in vivo (PubMed:34117057). May also have lyase activity (PubMed:19188258). Involved in somatic hypermutation of immunoglobulin genes, a process that requires the activity of DNA polymerases to ultimately introduce mutations at both A/T and C/G base pairs (By similarity). POLQ-mediated end joining activity is involved in random integration of exogenous DNA hampers (PubMed:28695890). {ECO:0000250|UniProtKB:Q8CGS6, ECO:0000269|PubMed:14576298, ECO:0000269|PubMed:18503084, ECO:0000269|PubMed:19188258, ECO:0000269|PubMed:21050863, ECO:0000269|PubMed:22135286, ECO:0000269|PubMed:24648516, ECO:0000269|PubMed:25642963, ECO:0000269|PubMed:25643323, ECO:0000269|PubMed:25775267, ECO:0000269|PubMed:26636256, ECO:0000269|PubMed:27311885, ECO:0000269|PubMed:27591252, ECO:0000269|PubMed:28695890, ECO:0000269|PubMed:30655289, ECO:0000269|PubMed:31562312, ECO:0000269|PubMed:32234782, ECO:0000269|PubMed:32873648, ECO:0000269|PubMed:33577776, ECO:0000269|PubMed:34117057, ECO:0000269|PubMed:34140467, ECO:0000269|PubMed:34179826, ECO:0000269|PubMed:36455556, ECO:0000269|PubMed:37440612, ECO:0000269|PubMed:37674080}.
|
Homo sapiens (Human)
|
O75419
|
CDC45_HUMAN
|
MFVSDFRKEFYEVVQSQRVLLFVASDVDALCACKILQALFQCDHVQYTLVPVSGWQELETAFLEHKEQFHYFILINCGANVDLLDILQPDEDTIFFVCDTHRPVNVVNVYNDTQIKLLIKQDDDLEVPAYEDIFRDEEEDEEHSGNDSDGSEPSEKRTRLEEEIVEQTMRRRQRREWEARRRDILFDYEQYEYHGTSSAMVMFELAWMLSKDLNDMLWWAIVGLTDQWVQDKITQMKYVTDVGVLQRHVSRHNHRNEDEENTLSVDCTRISFEYDLRLVLYQHWSLHDSLCNTSYTAARFKLWSVHGQKRLQEFLADMGLPLKQVKQKFQAMDISLKENLREMIEESANKFGMKDMRVQTFSIHFGFKHKFLASDVVFATMSLMESPEKDGSGTDHFIQALDSLSRSNLDKLYHGLELAKKQLRATQQTIASCLCTNLVISQGPFLYCSLMEGTPDVMLFSRPASLSLLSKHLLKSFVCSTKNRRCKLLPLVMAAPLSMEHGTVTVVGIPPETDSSDRKNFFGRAFEKAAESTSSRMLHNHFDLSVIELKAEDRSKFLDALISLLS
| null | null |
DNA replication checkpoint signaling [GO:0000076]; DNA replication initiation [GO:0006270]; DNA unwinding involved in DNA replication [GO:0006268]; double-strand break repair via break-induced replication [GO:0000727]; mitotic DNA replication preinitiation complex assembly [GO:1902977]
|
centrosome [GO:0005813]; ciliary basal body [GO:0036064]; CMG complex [GO:0071162]; DNA replication preinitiation complex [GO:0031261]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
chromatin binding [GO:0003682]; DNA replication origin binding [GO:0003688]; single-stranded DNA binding [GO:0003697]
|
PF02724;
| null |
CDC45 family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:35585232}. Chromosome {ECO:0000305|PubMed:35585232}. Note=Associates with chromatin. {ECO:0000305|PubMed:35585232}.
| null | null | null | null | null |
FUNCTION: Required for initiation of chromosomal DNA replication. Core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and around which the replisome is built. {ECO:0000269|PubMed:32453425, ECO:0000269|PubMed:34694004, ECO:0000269|PubMed:34700328, ECO:0000269|PubMed:35585232}.
|
Homo sapiens (Human)
|
O75420
|
GGYF1_HUMAN
|
MAAETLNFGPEWLRALSGGGSVASPPPSPAMPKYKLADYRYGREEMLALYVKENKVPEELQDKEFAAVLQDEPLQPLALEPLTEEEQRNFSLSVNSVAVLRLMGKGAGPPLAGTSRGRGSTRSRGRGRGDSCFYQRSIEEGDGAFGRSPREIQRSQSWDDRGERRFEKSARRDGARCGFEEGGAGPRKEHARSDSENWRSLREEQEEEEEGSWRLGAGPRRDGDRWRSASPDGGPRSAGWREHGERRRKFEFDLRGDRGGCGEEEGRGGGGSSHLRRCRAPEGFEEDKDGLPEWCLDDEDEEMGTFDASGAFLPLKKGPKEPIPEEQELDFQGLEEEEEPSEGLEEEGPEAGGKELTPLPPQEEKSSSPSPLPTLGPLWGTNGDGDETAEKEPPAAEDDIRGIQLSPGVGSSAGPPGDLEDDEGLKHLQQEAEKLVASLQDSSLEEEQFTAAMQTQGLRHSAAATALPLSHGAARKWFYKDPQGEIQGPFTTQEMAEWFQAGYFSMSLLVKRGCDEGFQPLGEVIKMWGRVPFAPGPSPPPLLGNMDQERLKKQQELAAAALYQQLQHQQFLQLVSSRQLPQCALREKAALGDLTPPPPPPPQQQQQQLTAFLQQLQALKPPRGGDQNLLPTMSRSLSVPDSGRLWDVHTSASSQSGGEASLWDIPINSSTQGPILEQLQLQHKFQERREVELRAKREEEERKRREEKRRQQQQEEQKRRQEEEELFRRKHVRQQELLLKLLQQQQAVPVPPAPSSPPPLWAGLAKQGLSMKTLLELQLEGERQLHKQPPPREPARAQAPNHRVQLGGLGTAPLNQWVSEAGPLWGGPDKSGGGSSGLGLWEDTPKSGGSLVRGLGLKNSRSSPSLSDSYSHLSGRPIRKKTEEEEKLLKLLQGIPRPQDGFTQWCEQMLHTLSATGSLDVPMAVAILKEVESPYDVHDYIRSCLGDTLEAKEFAKQFLERRAKQKASQQRQQQQEAWLSSASLQTAFQANHSTKLGPGEGSKAKRRALMLHSDPSILGYSLHGSSGEIESVDDY
| null | null |
insulin-like growth factor receptor signaling pathway [GO:0048009]
|
cytosol [GO:0005829]; protein-containing complex [GO:0032991]
| null |
PF02213;
|
3.30.1490.40;
|
GIGYF family
| null | null | null | null | null | null | null |
FUNCTION: May act cooperatively with GRB10 to regulate tyrosine kinase receptor signaling. May increase IGF1 receptor phosphorylation under IGF1 stimulation as well as phosphorylation of IRS1 and SHC1 (By similarity). {ECO:0000250, ECO:0000269|PubMed:12771153}.
|
Homo sapiens (Human)
|
O75425
|
MSPD3_HUMAN
|
MRRGAPQDQELVGPGPPGRGSRGAPPPLGPVVPVLVFPPDLVFRADQRSGPRQLLTLYNPTGTALRFRVLCTAPAKYTVFDAEGYVKPQSCIDIVIRHVAPIPSHYDVQDRFRIELSEEGAEGRVVGRKDITSILRAPAYPLELQGQPDPAPRPGPPAGTPPPTARHFQEHPRQQLATSSFLLFLLTGIVSVAFLLLPLPDELGSQLPQVLHVSLGQKLVAAYVLGLLTMVFLRT
| null | null |
heart development [GO:0007507]
|
cytoplasm [GO:0005737]; membrane [GO:0016020]
| null |
PF00635;
|
2.60.40.10;
| null | null |
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
| null | null | null | null | null | null |
Homo sapiens (Human)
|
O75427
|
LRCH4_HUMAN
|
MAAAVAAPLAAGGEEAAATTSVPGSPGLPGRRSAERALEEAVATGTLNLSNRRLKHFPRGAARSYDLSDITQADLSRNRFPEVPEAACQLVSLEGLSLYHNCLRCLNPALGNLTALTYLNLSRNQLSLLPPYICQLPLRVLIVSNNKLGALPPDIGTLGSLRQLDVSSNELQSLPSELCGLSSLRDLNVRRNQLSTLPEELGDLPLVRLDFSCNRVSRIPVSFCRLRHLQVILLDSNPLQSPPAQVCLKGKLHIFKYLSTEAGQRGSALGDLAPSRPPSFSPCPAEDLFPGHRYDGGLDSGFHSVDSGSKRWSGNESTDEFSELSFRISELAREPRGPRERKEDGSADGDPVQIDFIDSHVPGEDEERGTVEEQRPPELSPGAGDRERAPSSRREEPAGEERRRPDTLQLWQERERRQQQQSGAWGAPRKDSLLKPGLRAVVGGAAAVSTQAMHNGSPKSSASQAGAAAGQGAPAPAPASQEPLPIAGPATAPAPRPLGSIQRPNSFLFRSSSQSGSGPSSPDSVLRPRRYPQVPDEKDLMTQLRQVLESRLQRPLPEDLAEALASGVILCQLANQLRPRSVPFIHVPSPAVPKLSALKARKNVESFLEACRKMGVPEADLCSPSDLLQGTARGLRTALEAVKRVGGKALPPLWPPSGLGGFVVFYVVLMLLLYVTYTRLLGS
| null | null |
membrane raft assembly [GO:0001765]; nervous system development [GO:0007399]; positive regulation of toll-like receptor signaling pathway [GO:0034123]
|
plasma membrane [GO:0005886]; PML body [GO:0016605]
| null |
PF00307;PF13855;
|
1.10.418.10;3.80.10.10;
| null | null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q921G6}; Single-pass membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Accessory protein that regulates signaling by multiple TLRs, acting as a broad-spanning regulator of the innate immune response. In macrophages, binds LPS and promotes proper docking of LPS in lipid raft membrane. May be required for lipid raft maintenance. {ECO:0000250|UniProtKB:Q921G6}.
|
Homo sapiens (Human)
|
O75431
|
MTX2_HUMAN
|
MSLVAEAFVSQIAAAEPWPENATLYQQLKGEQILLSDNAASLAVQAFLQMCNLPIKVVCRANAEYMSPSGKVPFIHVGNQVVSELGPIVQFVKAKGHSLSDGLEEVQKAEMKAYMELVNNMLLTAELYLQWCDEATVGEITHARYGSPYPWPLNHILAYQKQWEVKRKMKAIGWGKKTLDQVLEDVDQCCQALSQRLGTQPYFFNKQPTELDALVFGHLYTILTTQLTNDELSEKVKNYSNLLAFCRRIEQHYFEDRGKGRLS
| null | null |
inner mitochondrial membrane organization [GO:0007007]; mitochondrial transport [GO:0006839]; mitochondrion organization [GO:0007005]; protein insertion into mitochondrial outer membrane [GO:0045040]
|
cytoplasm [GO:0005737]; MIB complex [GO:0140275]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]; SAM complex [GO:0001401]
| null |
PF17171;PF10568;
|
1.20.1050.10;
|
Metaxin family
| null |
SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:10381257}. Mitochondrion {ECO:0000269|PubMed:25997101}.
| null | null | null | null | null |
FUNCTION: Involved in transport of proteins into the mitochondrion. {ECO:0000269|PubMed:10381257}.
|
Homo sapiens (Human)
|
O75436
|
VP26A_HUMAN
|
MSFLGGFFGPICEIDIVLNDGETRKMAEMKTEDGKVEKHYLFYDGESVSGKVNLAFKQPGKRLEHQGIRIEFVGQIELFNDKSNTHEFVNLVKELALPGELTQSRSYDFEFMQVEKPYESYIGANVRLRYFLKVTIVRRLTDLVKEYDLIVHQLATYPDVNNSIKMEVGIEDCLHIEFEYNKSKYHLKDVIVGKIYFLLVRIKIQHMELQLIKKEITGIGPSTTTETETIAKYEIMDGAPVKGESIPIRLFLAGYDPTPTMRDVNKKFSVRYFLNLVLVDEEDRRYFKQQEIILWRKAPEKLRKQRTNFHQRFESPESQASAEQPEM
| null | null |
endocytic recycling [GO:0032456]; intracellular protein transport [GO:0006886]; regulation of macroautophagy [GO:0016241]; retrograde transport, endosome to Golgi [GO:0042147]
|
cytosol [GO:0005829]; early endosome [GO:0005769]; endosome [GO:0005768]; endosome membrane [GO:0010008]; lysosome [GO:0005764]; retromer complex [GO:0030904]; retromer, cargo-selective complex [GO:0030906]; tubular endosome [GO:0097422]; vesicle [GO:0031982]
| null |
PF03643;
|
2.60.40.640;
|
VPS26 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15078903}. Endosome membrane {ECO:0000269|PubMed:22431521}; Peripheral membrane protein {ECO:0000250|UniProtKB:P40336}. Early endosome {ECO:0000269|PubMed:15078903, ECO:0000269|PubMed:16190980, ECO:0000269|PubMed:16732284, ECO:0000269|PubMed:20682791}. Note=Localizes to tubular profiles adjacent to endosomes (PubMed:15078903). Predominantly found in early not late endosomes (By similarity). {ECO:0000250|UniProtKB:P40336}.
| null | null | null | null | null |
FUNCTION: Acts as a component of the retromer cargo-selective complex (CSC). The CSC is believed to be the core functional component of retromer or respective retromer complex variants acting to prevent missorting of selected transmembrane cargo proteins into the lysosomal degradation pathway. The recruitment of the CSC to the endosomal membrane involves RAB7A and SNX3. The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX3-retromer mediates the retrograde endosome-to-TGN transport of WLS distinct from the SNX-BAR retromer pathway. The SNX27-retromer is believed to be involved in endosome-to-plasma membrane trafficking and recycling of a broad spectrum of cargo proteins (Probable). The CSC seems to act as recruitment hub for other proteins, such as the WASH complex and TBC1D5 (Probable). Required for retrograde transport of lysosomal enzyme receptor IGF2R (PubMed:15078902, PubMed:15078903). Required to regulate transcytosis of the polymeric immunoglobulin receptor (pIgR-pIgA) (PubMed:15247922). Required for the endosomal localization of WASHC2A (indicative for the WASH complex) (PubMed:22070227). Required for the endosomal localization of TBC1D5 (PubMed:20923837). Mediates retromer cargo recognition of SORL1 and is involved in trafficking of SORL1 implicated in sorting and processing of APP (PubMed:22279231). Involved in retromer-independent lysosomal sorting of F2R (PubMed:16407403). Involved in recycling of ADRB2 (PubMed:21602791). Enhances the affinity of SNX27 for PDZ-binding motifs in cargo proteins (By similarity). {ECO:0000250|UniProtKB:P40336, ECO:0000269|PubMed:15078902, ECO:0000269|PubMed:15078903, ECO:0000269|PubMed:15247922, ECO:0000269|PubMed:16407403, ECO:0000269|PubMed:22070227, ECO:0000269|PubMed:22279231, ECO:0000303|PubMed:20923837, ECO:0000303|PubMed:21602791, ECO:0000303|PubMed:21725319, ECO:0000303|PubMed:23563491, ECO:0000305}.
|
Homo sapiens (Human)
|
O75438
|
NDUB1_HUMAN
|
MVNLLQIVRDHWVHVLVPMGFVIGCYLDRKSDERLTAFRNKSMLFKRELQPSEEVTWK
| 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 respiratory chain complex I [GO:0005747]; mitochondrion [GO:0005739]; nuclear speck [GO:0016607]
|
NADH dehydrogenase (ubiquinone) activity [GO:0008137]
|
PF08040;
| null |
Complex I NDUFB1 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)
|
O75439
|
MPPB_HUMAN
|
MAAAAARVVLSSAARRRLWGFSESLLIRGAAGRSLYFGENRLRSTQAATQVVLNVPETRVTCLESGLRVASEDSGLSTCTVGLWIDAGSRYENEKNNGTAHFLEHMAFKGTKKRSQLDLELEIENMGAHLNAYTSREQTVYYAKAFSKDLPRAVEILADIIQNSTLGEAEIERERGVILREMQEVETNLQEVVFDYLHATAYQNTALGRTILGPTENIKSISRKDLVDYITTHYKGPRIVLAAAGGVSHDELLDLAKFHFGDSLCTHKGEIPALPPCKFTGSEIRVRDDKMPLAHLAIAVEAVGWAHPDTICLMVANTLIGNWDRSFGGGMNLSSKLAQLTCHGNLCHSFQSFNTSYTDTGLWGLYMVCESSTVADMLHVVQKEWMRLCTSVTESEVARARNLLKTNMLLQLDGSTPICEDIGRQMLCYNRRIPIPELEARIDAVNAETIREVCTKYIYNRSPAIAAVGPIKQLPDFKQIRSNMCWLRD
|
3.4.24.64
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P10507}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P10507};
|
mitochondrial calcium ion transmembrane transport [GO:0006851]; protein processing involved in protein targeting to mitochondrion [GO:0006627]
|
mitochondrial inner membrane [GO:0005743]; mitochondrial processing peptidase complex [GO:0017087]; mitochondrion [GO:0005739]
|
metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]
|
PF00675;PF05193;
|
3.30.830.10;
|
Peptidase M16 family
| null |
SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:22354088}.
|
CATALYTIC ACTIVITY: Reaction=Release of N-terminal transit peptides from precursor proteins imported into the mitochondrion, typically with Arg in position P2.; EC=3.4.24.64; Evidence={ECO:0000305|PubMed:22354088};
| null | null | null | null |
FUNCTION: Catalytic subunit of the essential mitochondrial processing protease (MPP), which cleaves the mitochondrial sequence off newly imported precursors proteins (Probable) (PubMed:29576218). Preferentially, cleaves after an arginine at position P2 (By similarity). Required for PINK1 turnover by coupling PINK1 mitochondrial import and cleavage, which results in subsequent PINK1 proteolysis (PubMed:22354088). {ECO:0000250|UniProtKB:Q03346, ECO:0000269|PubMed:22354088, ECO:0000269|PubMed:29576218, ECO:0000305|PubMed:22354088}.
|
Homo sapiens (Human)
|
O75443
|
TECTA_HUMAN
|
MNYSSFLRIWVSFIFALVQHQAQPRELMYPFWQNDTKTPKVDDGSSSEIKLAIPVFFFGVPYRTVYVNNNGVVSFNVLVSQFTPESFPLTDGRAFVAPFWADVHNGIRGEIYYRETMEPAILKRATKDIRKYFKDMATFSATWVFIVTWEEVTFYGGSSTTPVNTFQAVLVSDGSYTFTLFNYYEINWTTGTASGGDPLTGLGGVMAQAGFNGGNLTNFFSLPGSRTPEIVNIQETTNVNVPGRWAFKVDGKEIDPANGCTSRGQFLRRGEVFWDDLNCTVKCRCLDFNNEIYCQEASCSPYEVCEPKGKFFYCSAVETSTCVVFGEPHYHTFDGFLFHFQGSCAYLLARQCLQTSSLPFFSVEAKNEHRRGSAVSWVKELSVEVNGYKILIPKGSYGRVKVNDLVTSLPVTLDLGTVKIYQSGISTAVETDFGLLVTFDGQHYASISVPGSYINSTCGLCGNYNKNPLDDFLRPDGRPAMSVLDLGESWRVYHADWKCDSGCVDNCTQCDAATEALYFGSDYCGFLNKTDGPLWECGTVVDPTAFVHSCVYDLCSVRDNGTLLCQAIQAYALVCQALGIPIGDWRTQTGCVSTVQCPSFSHYSVCTSSCPDTCSDLTASRNCATPCTEGCECNQGFVLSTSQCVPLHKCGCDFDGHYYTMGEFFWATANCTVQCLCEEGGDVYCFNKTCGSGEVCAVEDGYQGCFPKRETVCLLSQNQVLHTFDGASYAFPSEFSYTLLKTCPERPEYLEIDINKKKPDAGPAWLRGLRILVADQEVKIGGIGASEVKLNGQEVELPFFHPSGKLEIYRNKNSTTVESKGVVTVQYSDIGLLYIRLSTTYFNCTGGLCGFYNANASDEFCLPNGKCTDNLAVFLESWTTFEEICNGECGDLLKACNNDSELLKFYRSRSRCGIINDPSNSSFLECHGVVNVTAYYRTCLFRLCQSGGNESELCDSVARYASACKNADVEVGPWRTYDFCPLECPENSHFEECITCTETCETLTLGPICVDSCSEGCQCDEGYALLGSQCVTRSECGCNFEGHQLATNETFWVDLDCQIFCYCSGTDNRVHCETIPCKDDEYCMEEGGLYYCQARTDASCIVSGYGHYLTFDGFPFDFQTSCPLILCTTGSRPSSDSFPKFVVTAKNEDRDPSLALWVKQVDVTVFGYSIVIHRAYKHTVLVNSERLYLPLKLGQGKINIFSFGFHVVVETDFGLKVVYDWKTFLSITVPRSMQNSTYGLCGRYNGNPDDDLEMPMGLLASSVNEFGQSWVKRDTFCQVGCGDRCPSCAKVEGFSKVQQLCSLIPNQNAAFSKCHSKVNPTFFYKNCLFDSCIDGGAVQTACSWLQNYASTCQTQGITVTGWRNYTSCTVTCPPNSHYESCVSVCQPRCAAIRLKSDCSHYCVEGCHCDAGYVLNGKSCILPHSCGCYSDGKYYEPKQLFWNSDCTRRCRCFRRNVIQCDPRQCKSDEECALRNGVRGCFSTKTSYCLAAGGGVFRTFDGAFLRFPANCAFVLSTICQKLPDISFQLIINFDKWSAPNLTIISPVYFYINEEQILINDRNTVKVNGTQVNVPFITGLATKIYSSEGFLVIDTSPDIQIYYNGFNVIKISISERLQNKVCGLCGNFNGDLTDDYVTLRGKPVVSSVVLAQSWKTNGMQKRPLAPSCNELQFSQYAAMCDNVHIQKMQGDGYCLKLTDMKGFFQPCYGLLDPLPFYESCYLDGCYSHKKFQLCGSLAAYGEACRSFGILSTEWIEKENCSGVVEDPCVGADCPNRTCELGNGRELCGCIEPPPYGNNSHDIIDAEVTCKAAQMEVSISKCKLFQLGFEREGVRINDRQCTGIEGEDFISFQINNTKGNCGNIVQSNGTHIMYKNTLWIESANNTGNIITRDRTINVEFSCAYELDIKISLDSVVKPMLSVINLTVPTQEGSFITKMALYKNASYKHPYRQGEVVLTTRDVLYVGVFVVGADATHLILTLNKCYATPTRDSNDKLRYFIIEGGCQNLKDNTIGIEENAVSLTCRFHVTVFKFIGDYDEVHLHCAVSLCDSEKYSCKITCPHNSRIATDYTKEPKEQIISVGPIRRKRLDWCEDNGGCEQICTSRVDGPLCSCVTGTLQEDGKSCRASNSSMELQVWTLLLIMIQISLWHFVYKSGTTS
| null | null |
auditory receptor cell stereocilium organization [GO:0060088]; cell-matrix adhesion [GO:0007160]; sensory perception of sound [GO:0007605]
|
extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]
|
extracellular matrix structural constituent [GO:0005201]
|
PF08742;PF06119;PF01826;PF12714;PF00094;PF00100;
|
2.10.25.10;2.60.40.4100;2.60.40.3210;
| null |
PTM: The presence of a hydrophobic C-terminus preceded by a potential cleavage site strongly suggests that tectorins are synthesized as glycosylphosphatidylinositol-linked, membrane-bound precursors. Tectorins are targeted to the apical surface of the inner ear epithelia by the lipid and proteolytically released into the extracellular compartment.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}; Extracellular side {ECO:0000305}. Secreted, extracellular space, extracellular matrix. Note=Found in the non-collagenous matrix of the tectorial membrane. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: One of the major non-collagenous components of the tectorial membrane (By similarity). The tectorial membrane is an extracellular matrix of the inner ear that covers the neuroepithelium of the cochlea and contacts the stereocilia bundles of specialized sensory hair cells. Sound induces movement of these hair cells relative to the tectorial membrane, deflects the stereocilia and leads to fluctuations in hair-cell membrane potential, transducing sound into electrical signals. {ECO:0000250}.
|
Homo sapiens (Human)
|
O75444
|
MAF_HUMAN
|
MASELAMSNSDLPTSPLAMEYVNDFDLMKFEVKKEPVETDRIISQCGRLIAGGSLSSTPMSTPCSSVPPSPSFSAPSPGSGSEQKAHLEDYYWMTGYPQQLNPEALGFSPEDAVEALISNSHQLQGGFDGYARGAQQLAAAAGAGAGASLGGSGEEMGPAAAVVSAVIAAAAAQSGAGPHYHHHHHHAAGHHHHPTAGAPGAAGSAAASAGGAGGAGGGGPASAGGGGGGGGGGGGGGAAGAGGALHPHHAAGGLHFDDRFSDEQLVTMSVRELNRQLRGVSKEEVIRLKQKRRTLKNRGYAQSCRFKRVQQRHVLESEKNQLLQQVDHLKQEISRLVRERDAYKEKYEKLVSSGFRENGSSSDNPSSPEFFM
| null | null |
inner ear development [GO:0048839]; integrated stress response signaling [GO:0140467]; lens fiber cell differentiation [GO:0070306]; megakaryocyte differentiation [GO:0030219]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of gene expression [GO:0010628]; regulation of chondrocyte differentiation [GO:0032330]; regulation of transcription by RNA polymerase II [GO:0006357]; transcription by RNA polymerase II [GO:0006366]
|
chromatin [GO:0000785]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575]
|
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; identical protein binding [GO:0042802]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific double-stranded DNA binding [GO:1990837]
|
PF03131;PF08383;
|
1.20.5.170;
|
BZIP family, Maf subfamily
|
PTM: Ubiquitinated, leading to its degradation by the proteasome. Ubiquitination is triggered by glucocorticoids. {ECO:0000269|PubMed:17875808}.; PTM: Phosphorylated by GSK3 and MAPK13 on serine and threonine residues (Probable). The phosphorylation status can serve to either stimulate or inhibit transcription. {ECO:0000269|PubMed:15963504, ECO:0000269|PubMed:18042454, ECO:0000305}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
| null | null | null | null | null |
FUNCTION: Acts as a transcriptional activator or repressor. Involved in embryonic lens fiber cell development. Recruits the transcriptional coactivators CREBBP and/or EP300 to crystallin promoters leading to up-regulation of crystallin gene during lens fiber cell differentiation. Activates the expression of IL4 in T helper 2 (Th2) cells. Increases T-cell susceptibility to apoptosis by interacting with MYB and decreasing BCL2 expression. Together with PAX6, transactivates strongly the glucagon gene promoter through the G1 element. Activates transcription of the CD13 proximal promoter in endothelial cells. Represses transcription of the CD13 promoter in early stages of myelopoiesis by affecting the ETS1 and MYB cooperative interaction. Involved in the initial chondrocyte terminal differentiation and the disappearance of hypertrophic chondrocytes during endochondral bone development. Binds to the sequence 5'-[GT]G[GC]N[GT]NCTCAGNN-3' in the L7 promoter. Binds to the T-MARE (Maf response element) sites of lens-specific alpha- and beta-crystallin gene promoters. Binds element G1 on the glucagon promoter. Binds an AT-rich region adjacent to the TGC motif (atypical Maf response element) in the CD13 proximal promoter in endothelial cells (By similarity). When overexpressed, represses anti-oxidant response element (ARE)-mediated transcription. Involved either as an oncogene or as a tumor suppressor, depending on the cell context. Binds to the ARE sites of detoxifying enzyme gene promoters. {ECO:0000250, ECO:0000269|PubMed:12149651, ECO:0000269|PubMed:14998494, ECO:0000269|PubMed:15007382, ECO:0000269|PubMed:16247450, ECO:0000269|PubMed:19143053}.
|
Homo sapiens (Human)
|
O75445
|
USH2A_HUMAN
|
MNCPVLSLGSGFLFQVIEMLIFAYFASISLTESRGLFPRLENVGAFKKVSIVPTQAVCGLPDRSTFCHSSAAAESIQFCTQRFCIQDCPYRSSHPTYTALFSAGLSSCITPDKNDLHPNAHSNSASFIFGNHKSCFSSPPSPKLMASFTLAVWLKPEQQGVMCVIEKTVDGQIVFKLTISEKETMFYYRTVNGLQPPIKVMTLGRILVKKWIHLSVQVHQTKISFFINGVEKDHTPFNARTLSGSITDFASGTVQIGQSLNGLEQFVGRMQDFRLYQVALTNREILEVFSGDLLRLHAQSHCRCPGSHPRVHPLAQRYCIPNDAGDTADNRVSRLNPEAHPLSFVNDNDVGTSWVSNVFTNITQLNQGVTISVDLENGQYQVFYIIIQFFSPQPTEIRIQRKKENSLDWEDWQYFARNCGAFGMKNNGDLEKPDSVNCLQLSNFTPYSRGNVTFSILTPGPNYRPGYNNFYNTPSLQEFVKATQIRFHFHGQYYTTETAVNLRHRYYAVDEITISGRCQCHGHADNCDTTSQPYRCLCSQESFTEGLHCDRCLPLYNDKPFRQGDQVYAFNCKPCQCNSHSKSCHYNISVDPFPFEHFRGGGGVCDDCEHNTTGRNCELCKDYFFRQVGADPSAIDVCKPCDCDTVGTRNGSILCDQIGGQCNCKRHVSGRQCNQCQNGFYNLQELDPDGCSPCNCNTSGTVDGDITCHQNSGQCKCKANVIGLRCDHCNFGFKFLRSFNDVGCEPCQCNLHGSVNKFCNPHSGQCECKKEAKGLQCDTCRENFYGLDVTNCKACDCDTAGSLPGTVCNAKTGQCICKPNVEGRQCNKCLEGNFYLRQNNSFLCLPCNCDKTGTINGSLLCNKSTGQCPCKLGVTGLRCNQCEPHRYNLTIDNFQHCQMCECDSLGTLPGTICDPISGQCLCVPNRQGRRCNQCQPGFYISPGNATGCLPCSCHTTGAVNHICNSLTGQCVCQDASIAGQRCDQCKDHYFGFDPQTGRCQPCNCHLSGALNETCHLVTGQCFCKQFVTGSKCDACVPSASHLDVNNLLGCSKTPFQQPPPRGQVQSSSAINLSWSPPDSPNAHWLTYSLLRDGFEIYTTEDQYPYSIQYFLDTDLLPYTKYSYYIETTNVHGSTRSVAVTYKTKPGVPEGNLTLSYIIPIGSDSVTLTWTTLSNQSGPIEKYILSCAPLAGGQPCVSYEGHETSATIWNLVPFAKYDFSVQACTSGGCLHSLPITVTTAQAPPQRLSPPKMQKISSTELHVEWSPPAELNGIIIRYELYMRRLRSTKETTSEESRVFQSSGWLSPHSFVESANENALKPPQTMTTITGLEPYTKYEFRVLAVNMAGSVSSAWVSERTGESAPVFMIPPSVFPLSSYSLNISWEKPADNVTRGKVVGYDINMLSEQSPQQSIPMAFSQLLHTAKSQELSYTVEGLKPYRIYEFTITLCNSVGCVTSASGAGQTLAAAPAQLRPPLVKGINSTTIHLRWFPPEELNGPSPIYQLERRESSLPALMTTMMKGIRFIGNGYCKFPSSTHPVNTDFTGIKASFRTKVPEGLIVFAASPGNQEEYFALQLKKGRLYFLFDPQGSPVEVTTTNDHGKQYSDGKWHEIIAIRHQAFGQITLDGIYTGSSAILNGSTVIGDNTGVFLGGLPRSYTILRKDPEIIQKGFVGCLKDVHFMKNYNPSAIWEPLDWQSSEEQINVYNSWEGCPASLNEGAQFLGAGFLELHPYMFHGGMNFEISFKFRTDQLNGLLLFVYNKDGPDFLAMELKSGILTFRLNTSLAFTQVDLLLGLSYCNGKWNKVIIKKEGSFISASVNGLMKHASESGDQPLVVNSPVYVGGIPQELLNSYQHLCLEQGFGGCMKDVKFTRGAVVNLASVSSGAVRVNLDGCLSTDSAVNCRGNDSILVYQGKEQSVYEGGLQPFTEYLYRVIASHEGGSVYSDWSRGRTTGAAPQSVPTPSRVRSLNGYSIEVTWDEPVVRGVIEKYILKAYSEDSTRPPRMPSASAEFVNTSNLTGILTGLLPFKNYAVTLTACTLAGCTESSHALNISTPQEAPQEVQPPVAKSLPSSLLLSWNPPKKANGIITQYCLYMDGRLIYSGSEENYIVTDLAVFTPHQFLLSACTHVGCTNSSWVLLYTAQLPPEHVDSPVLTVLDSRTIHIQWKQPRKISGILERYVLYMSNHTHDFTIWSVIYNSTELFQDHMLQYVLPGNKYLIKLGACTGGGCTVSEASEALTDEDIPEGVPAPKAHSYSPDSFNVSWTEPEYPNGVITSYGLYLDGILIHNSSELSYRAYGFAPWSLHSFRVQACTAKGCALGPLVENRTLEAPPEGTVNVFVKTQGSRKAHVRWEAPFRPNGLLTHSVLFTGIFYVDPVGNNYTLLNVTKVMYSGEETNLWVLIDGLVPFTNYTVQVNISNSQGSLITDPITIAMPPGAPDGVLPPRLSSATPTSLQVVWSTPARNNAPGSPRYQLQMRSGDSTHGFLELFSNPSASLSYEVSDLQPYTEYMFRLVASNGFGSAHSSWIPFMTAEDKPGPVVPPILLDVKSRMMLVTWQHPRKSNGVITHYNIYLHGRLYLRTPGNVTNCTVMHLHPYTAYKFQVEACTSKGCSLSPESQTVWTLPGAPEGIPSPELFSDTPTSVIISWQPPTHPNGLVENFTIERRVKGKEEVTTLVTLPRSHSMRFIDKTSALSPWTKYEYRVLMSTLHGGTNSSAWVEVTTRPSRPAGVQPPVVTVLEPDAVQVTWKPPLIQNGDILSYEIHMPDPHITLTNVTSAVLSQKVTHLIPFTNYSVTIVACSGGNGYLGGCTESLPTYVTTHPTVPQNVGPLSVIPLSESYVVISWQPPSKPNGPNLRYELLRRKIQQPLASNPPEDLNRWHNIYSGTQWLYEDKGLSRFTTYEYMLFVHNSVGFTPSREVTVTTLAGLPERGANLTASVLNHTAIDVRWAKPTVQDLQGEVEYYTLFWSSATSNDSLKILPDVNSHVIGHLKPNTEYWIFISVFNGVHSINSAGLHATTCDGEPQGMLPPEVVIINSTAVRVIWTSPSNPNGVVTEYSIYVNNKLYKTGMNVPGSFILRDLSPFTIYDIQVEVCTIYACVKSNGTQITTVEDTPSDIPTPTIRGITSRSLQIDWVSPRKPNGIILGYDLLWKTWYPCAKTQKLVQDQSDELCKAVRCQKPESICGHICYSSEAKVCCNGVLYNPKPGHRCCEEKYIPFVLNSTGVCCGGRIQEAQPNHQCCSGYYARILPGEVCCPDEQHNRVSVGIGDSCCGRMPYSTSGNQICCAGRLHDGHGQKCCGRQIVSNDLECCGGEEGVVYNRLPGMFCCGQDYVNMSDTICCSASSGESKAHIKKNDPVPVKCCETELIPKSQKCCNGVGYNPLKYVCSDKISTGMMMKETKECRILCPASMEATEHCGRCDFNFTSHICTVIRGSHNSTGKASIEEMCSSAEETIHTGSVNTYSYTDVNLKPYMTYEYRISAWNSYGRGLSKAVRARTKEDVPQGVSPPTWTKIDNLEDTIVLNWRKPIQSNGPIIYYILLRNGIERFRGTSLSFSDKEGIQPFQEYSYQLKACTVAGCATSSKVVAATTQGVPESILPPSITALSAVALHLSWSVPEKSNGVIKEYQIRQVGKGLIHTDTTDRRQHTVTGLQPYTNYSFTLTACTSAGCTSSEPFLGQTLQAAPEGVWVTPRHIIINSTTVELYWSLPEKPNGLVSQYQLSRNGNLLFLGGSEEQNFTDKNLEPNSRYTYKLEVKTGGGSSASDDYIVQTPMSTPEEIYPPYNITVIGPYSIFVAWIPPGILIPEIPVEYNVLLNDGSVTPLAFSVGHHQSTLLENLTPFTQYEIRIQACQNGSCGVSSRMFVKTPEAAPMDLNSPVLKALGSACIEIKWMPPEKPNGIIINYFIYRRPAGIEEESVLFVWSEGALEFMDEGDTLRPFTLYEYRVRACNSKGSVESLWSLTQTLEAPPQDFPAPWAQATSAHSVLLNWTKPESPNGIISHYRVVYQERPDDPTFNSPTVHAFTVKGTSHQAHLYGLEPFTTYRIGVVAANHAGEILSPWTLIQTLESSPSGLRNFIVEQKENGRALLLQWSEPMRTNGVIKTYNIFSDGFLEYSGLNRQFLFRRLDPFTLYTLTLEACTRAGCAHSAPQPLWTDEAPPDSQLAPTVHSVKSTSVELSWSEPVNPNGKIIRYEVIRRCFEGKAWGNQTIQADEKIVFTEYNTERNTFMYNDTGLQPWTQCEYKIYTWNSAGHTCSSWNVVRTLQAPPEGLSPPVISYVSMNPQKLLISWIPPEQSNGIIQSYRLQRNEMLYPFSFDPVTFNYTDEELLPFSTYSYALQACTSGGCSTSKPTSITTLEAAPSEVSPPDLWAVSATQMNVCWSPPTVQNGKITKYLVRYDNKESLAGQGLCLLVSHLQPYSQYNFSLVACTNGGCTASVSKSAWTMEALPENMDSPTLQVTGSESIEITWKPPRNPNGQIRSYELRRDGTIVYTGLETRYRDFTLTPGVEYSYTVTASNSQGGILSPLVKDRTSPSAPSGMEPPKLQARGPQEILVNWDPPVRTNGDIINYTLFIRELFERETKIIHINTTHNSFGMQSYIVNQLKPFHRYEIRIQACTTLGCASSDWTFIQTPEIAPLMQPPPHLEVQMAPGGFQPTVSLLWTGPLQPNGKVLYYELYRRQIATQPRKSNPVLIYNGSSTSFIDSELLPFTEYEYQVWAVNSAGKAPSSWTWCRTGPAPPEGLRAPTFHVISSTQAVVNISAPGKPNGIVSLYRLFSSSAHGAETVLSEGMATQQTLHGLQAFTNYSIGVEACTCFNCCSKGPTAELRTHPAPPSGLSSPQIGTLASRTASFRWSPPMFPNGVIHSYELQFHVACPPDSALPCTPSQIETKYTGLGQKASLGGLQPYTTYKLRVVAHNEVGSTASEWISFTTQKELPQYRAPFSVDSNLSVVCVNWSDTFLLNGQLKEYVLTDGGRRVYSGLDTTLYIPRTADKTFFFQVICTTDEGSVKTPLIQYDTSTGLGLVLTTPGKKKGSRSKSTEFYSELWFIVLMAMLGLILLAIFLSLILQRKIHKEPYIRERPPLVPLQKRMSPLNVYPPGENHMGLADTKIPRSGTPVSIRSNRSACVLRIPSQNQTSLTYSQGSLHRSVSQLMDIQDKKVLMDNSLWEAIMGHNSGLYVDEEDLMNAIKDFSSVTKERTTFTDTHL
| null | null |
establishment of localization in cell [GO:0051649]; establishment of protein localization [GO:0045184]; hair cell differentiation [GO:0035315]; inner ear auditory receptor cell differentiation [GO:0042491]; inner ear receptor cell differentiation [GO:0060113]; maintenance of animal organ identity [GO:0048496]; photoreceptor cell maintenance [GO:0045494]; response to stimulus [GO:0050896]; sensory perception of light stimulus [GO:0050953]; sensory perception of sound [GO:0007605]; visual perception [GO:0007601]
|
apical plasma membrane [GO:0016324]; basement membrane [GO:0005604]; ciliary basal body [GO:0036064]; cytoplasm [GO:0005737]; extracellular region [GO:0005576]; periciliary membrane compartment [GO:1990075]; photoreceptor connecting cilium [GO:0032391]; photoreceptor inner segment [GO:0001917]; receptor complex [GO:0043235]; stereocilia ankle link [GO:0002141]; stereocilia ankle link complex [GO:0002142]; stereocilium bundle [GO:0032421]; stereocilium membrane [GO:0060171]; USH2 complex [GO:1990696]
|
collagen binding [GO:0005518]; identical protein binding [GO:0042802]; myosin binding [GO:0017022]
|
PF00041;PF00053;PF02210;PF13385;PF00055;
|
2.60.120.200;2.60.120.260;2.60.40.10;2.10.25.10;
| null | null |
SUBCELLULAR LOCATION: Cell projection, stereocilium membrane {ECO:0000269|PubMed:14676276}; Single-pass type I membrane protein {ECO:0000269|PubMed:14676276}. Note=Component of the interstereocilia ankle links in the inner ear sensory cells. In photoreceptors, localizes at a plasma membrane microdomain in the apical inner segment that surrounds the connecting cilia called periciliary membrane complex. {ECO:0000250|UniProtKB:Q2QI47}.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted.
| null | null | null | null | null |
FUNCTION: Involved in hearing and vision as member of the USH2 complex. In the inner ear, required for the maintenance of the hair bundle ankle formation, which connects growing stereocilia in developing cochlear hair cells. In retina photoreceptors, the USH2 complex is required for the maintenance of periciliary membrane complex that seems to play a role in regulating intracellular protein transport. {ECO:0000250|UniProtKB:Q2QI47}.
|
Homo sapiens (Human)
|
O75446
|
SAP30_HUMAN
|
MNGFTPDEMSRGGDAAAAVAAVVAAAAAAASAGNGTGAGTGAEVPGAGAVSAAGPPGAAGPGPGQLCCLREDGERCGRAAGNASFSKRIQKSISQKKVKIELDKSARHLYICDYHKNLIQSVRNRRKRKGSDDDGGDSPVQDIDTPEVDLYQLQVNTLRRYKRHFKLPTRPGLNKAQLVEIVGCHFRSIPVNEKDTLTYFIYSVKNDKNKSDLKVDSGVH
| null | null |
modulation by host of symbiont transcription [GO:0052472]; negative regulation of cell migration [GO:0030336]; 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 stem cell population maintenance [GO:1902459]; regulation of DNA-templated transcription [GO:0006355]; skeletal muscle cell differentiation [GO:0035914]
|
histone deacetylase complex [GO:0000118]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
DNA binding [GO:0003677]; metal ion binding [GO:0046872]; transcription coregulator activity [GO:0003712]; transcription corepressor activity [GO:0003714]
|
PF13867;PF13866;
|
6.10.160.20;
|
SAP30 family
| null |
SUBCELLULAR LOCATION: Nucleus.
| null | null | null | null | null |
FUNCTION: Involved in the functional recruitment of the Sin3-histone deacetylase complex (HDAC) to a specific subset of N-CoR corepressor complexes. Capable of transcription repression by N-CoR. Active in deacetylating core histone octamers (when in a complex) but inactive in deacetylating nucleosomal histones. {ECO:0000250|UniProtKB:O88574, ECO:0000269|PubMed:9651585}.; FUNCTION: (Microbial infection) Involved in transcriptional repression of HHV-1 genes TK and gC. {ECO:0000269|PubMed:21221920}.
|
Homo sapiens (Human)
|
O75448
|
MED24_HUMAN
|
MKVVNLKQAILQAWKERWSDYQWAINMKKFFPKGATWDILNLADALLEQAMIGPSPNPLILSYLKYAISSQMVSYSSVLTAISKFDDFSRDLCVQALLDIMDMFCDRLSCHGKAEECIGLCRALLSALHWLLRCTAASAERLREGLEAGTPAAGEKQLAMCLQRLEKTLSSTKNRALLHIAKLEEASSWTAIEHSLLKLGEILANLSNPQLRSQAEQCGTLIRSIPTMLSVHAEQMHKTGFPTVHAVILLEGTMNLTGETQSLVEQLTMVKRMQHIPTPLFVLEIWKACFVGLIESPEGTEELKWTAFTFLKIPQVLVKLKKYSHGDKDFTEDVNCAFEFLLKLTPLLDKADQRCNCDCTNFLLQECGKQGLLSEASVNNLMAKRKADREHAPQQKSGENANIQPNIQLILRAEPTVTNILKTMDADHSKSPEGLLGVLGHMLSGKSLDLLLAAAAATGKLKSFARKFINLNEFTTYGSEESTKPASVRALLFDISFLMLCHVAQTYGSEVILSESRTGAEVPFFETWMQTCMPEEGKILNPDHPCFRPDSTKVESLVALLNNSSEMKLVQMKWHEACLSISAAILEILNAWENGVLAFESIQKITDNIKGKVCSLAVCAVAWLVAHVRMLGLDEREKSLQMIRQLAGPLFSENTLQFYNERVVIMNSILERMCADVLQQTATQIKFPSTGVDTMPYWNLLPPKRPIKEVLTDIFAKVLEKGWVDSRSIHIFDTLLHMGGVYWFCNNLIKELLKETRKEHTLRAVELLYSIFCLDMQQVTLVLLGHILPGLLTDSSKWHSLMDPPGTALAKLAVWCALSSYSSHKGQASTRQKKRHREDIEDYISLFPLDDVQPSKLMRLLSSNEDDANILSSPTDRSMSSSLSASQLHTVNMRDPLNRVLANLFLLISSILGSRTAGPHTQFVQWFMEECVDCLEQGGRGSVLQFMPFTTVSELVKVSAMSSPKVVLAITDLSLPLGRQVAAKAIAAL
| null | null |
positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; positive regulation of transcription initiation by RNA polymerase II [GO:0060261]; RNA polymerase II preinitiation complex assembly [GO:0051123]
|
core mediator complex [GO:0070847]; mediator complex [GO:0016592]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
nuclear receptor coactivator activity [GO:0030374]; nuclear thyroid hormone receptor binding [GO:0046966]; nuclear vitamin D receptor binding [GO:0042809]; transcription coactivator activity [GO:0003713]; transcription coregulator activity [GO:0003712]
|
PF11277;
| null |
Mediator complex subunit 24 family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. {ECO:0000269|PubMed:12218053, ECO:0000269|PubMed:16595664}.
|
Homo sapiens (Human)
|
O75449
|
KTNA1_HUMAN
|
MSLLMISENVKLAREYALLGNYDSAMVYYQGVLDQMNKYLYSVKDTYLQQKWQQVWQEINVEAKHVKDIMKTLESFKLDSTPLKAAQHDLPASEGEVWSMPVPVERRPSPGPRKRQSSQYSDPKSHGNRPSTTVRVHRSSAQNVHNDRGKAVRCREKKEQNKGREEKNKSPAAVTEPETNKFDSTGYDKDLVEALERDIISQNPNVRWDDIADLVEAKKLLKEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYSPATIFIDEIDSICSRRGTSEEHEASRRVKAELLVQMDGVGGTSENDDPSKMVMVLAATNFPWDIDEALRRRLEKRIYIPLPSAKGREELLRISLRELELADDVDLASIAENMEGYSGADITNVCRDASLMAMRRRIEGLTPEEIRNLSKEEMHMPTTMEDFEMALKKVSKSVSAADIERYEKWIFEFGSC
|
5.6.1.1
| null |
cell cycle [GO:0007049]; cell division [GO:0051301]; cytoplasmic microtubule organization [GO:0031122]; microtubule severing [GO:0051013]
|
centrosome [GO:0005813]; cytoplasm [GO:0005737]; katanin complex [GO:0008352]; microtubule [GO:0005874]; microtubule cytoskeleton [GO:0015630]; midbody [GO:0030496]; mitotic spindle pole [GO:0097431]; spindle [GO:0005819]; spindle pole [GO:0000922]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; isomerase activity [GO:0016853]; microtubule binding [GO:0008017]; microtubule severing ATPase activity [GO:0008568]; protein heterodimerization activity [GO:0046982]
|
PF00004;PF17862;PF21126;PF09336;
|
1.10.8.60;3.40.50.300;1.20.58.80;
|
AAA ATPase family, Katanin p60 subunit A1 subfamily
|
PTM: Phosphorylation by DYRK2 triggers ubiquitination and subsequent degradation. {ECO:0000255|HAMAP-Rule:MF_03023, ECO:0000269|PubMed:19261606, ECO:0000269|PubMed:19287380}.; PTM: Ubiquitinated by the BCR(KLHL42) E3 ubiquitin ligase complex, leading to its proteasomal degradation. Ubiquitinated by the EDVP E3 ligase complex and subsequently targeted for proteasomal degradation. {ECO:0000255|HAMAP-Rule:MF_03023, ECO:0000269|PubMed:19261606}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10751153, ECO:0000269|PubMed:26929214, ECO:0000269|PubMed:9658175}. Midbody {ECO:0000269|PubMed:19261606}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03023}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:10751153, ECO:0000269|PubMed:26929214, ECO:0000269|PubMed:9658175}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:26929214}. Note=Predominantly cytoplasmic (PubMed:9658175). Localized diffusely in the cytoplasm during the interphase (PubMed:10751153). During metaphase is localized throughout the cell and more widely dispersed than the microtubules. In anaphase and telophase is localized at the midbody region (PubMed:19261606). Also localized to the interphase centrosome and the mitotic spindle poles (By similarity). Enhanced recruitment to the mitotic spindle poles requires microtubules and interaction with KATNB1 (PubMed:10751153). Localizes within the cytoplasm, partially overlapping with microtubules, in interphase and to the mitotic spindle and spindle poles during mitosis (PubMed:26929214). {ECO:0000255|HAMAP-Rule:MF_03023, ECO:0000269|PubMed:10751153, ECO:0000269|PubMed:19261606, ECO:0000269|PubMed:26929214, ECO:0000269|PubMed:9658175}.
|
CATALYTIC ACTIVITY: Reaction=n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers.; EC=5.6.1.1; Evidence={ECO:0000255|HAMAP-Rule:MF_03023};
| null | null | null | null |
FUNCTION: Catalytic subunit of a complex which severs microtubules in an ATP-dependent manner. Microtubule severing may promote rapid reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. Microtubule release from the mitotic spindle poles may allow depolymerization of the microtubule end proximal to the spindle pole, leading to poleward microtubule flux and poleward motion of chromosome. Microtubule release within the cell body of neurons may be required for their transport into neuronal processes by microtubule-dependent motor proteins. This transport is required for axonal growth. {ECO:0000255|HAMAP-Rule:MF_03023, ECO:0000269|PubMed:10751153, ECO:0000269|PubMed:11870226, ECO:0000269|PubMed:19287380}.
|
Homo sapiens (Human)
|
O75452
|
RDH16_HUMAN
|
MWLYLAVFVGLYYLLHWYRERQVLSHLRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQTSDRLETVTLDVTKTESVAAAAQWVKECVRDKGLWGLVNNAGISLPTAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRARGRVVNVSSVMGRVSLFGGGYCISKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVTSKERFLKSFLEIWDRSSPEVKEAYGEKFVADYKKSAEQMEQKCTQDLSLVTNCMEHALIACHPRTRYSAGWDAKLLYLPMSYMPTFLVDAIMYWVSPSPAKAL
|
1.1.1.105; 1.1.1.209; 1.1.1.315; 1.1.1.53
| null |
lipid metabolic process [GO:0006629]; retinol metabolic process [GO:0042572]; steroid metabolic process [GO:0008202]
|
endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231]
|
11-cis-retinol dehydrogenase [GO:0106429]; androstan-3-alpha,17-beta-diol dehydrogenase activity [GO:0047044]; androsterone dehydrogenase activity [GO:0047023]; electron transfer activity [GO:0009055]; identical protein binding [GO:0042802]; NAD-retinol dehydrogenase activity [GO:0004745]
|
PF00106;
|
3.40.50.720;
|
Short-chain dehydrogenases/reductases (SDR) family
|
PTM: Not N-glycosylated. {ECO:0000269|PubMed:12534290}.
|
SUBCELLULAR LOCATION: Microsome membrane {ECO:0000269|PubMed:9677409}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O54909}; Single-pass membrane protein {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=all-trans-retinol--[retinol-binding protein] + NAD(+) = all-trans-retinal--[retinol-binding protein] + H(+) + NADH; Xref=Rhea:RHEA:48488, Rhea:RHEA-COMP:14428, Rhea:RHEA-COMP:14430, ChEBI:CHEBI:15378, ChEBI:CHEBI:17336, ChEBI:CHEBI:17898, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:83228; EC=1.1.1.105; Evidence={ECO:0000269|PubMed:10329026, ECO:0000269|PubMed:12534290, ECO:0000269|PubMed:9677409}; CATALYTIC ACTIVITY: Reaction=all-trans-retinol + NAD(+) = all-trans-retinal + H(+) + NADH; Xref=Rhea:RHEA:21284, ChEBI:CHEBI:15378, ChEBI:CHEBI:17336, ChEBI:CHEBI:17898, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.105; Evidence={ECO:0000269|PubMed:10329026, ECO:0000269|PubMed:9677409}; CATALYTIC ACTIVITY: Reaction=13-cis-retinol + NAD(+) = 13-cis-retinal + H(+) + NADH; Xref=Rhea:RHEA:42056, ChEBI:CHEBI:15378, ChEBI:CHEBI:45479, ChEBI:CHEBI:45487, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence={ECO:0000269|PubMed:9677409}; CATALYTIC ACTIVITY: Reaction=11-cis-retinol + NAD(+) = 11-cis-retinal + H(+) + NADH; Xref=Rhea:RHEA:42060, ChEBI:CHEBI:15378, ChEBI:CHEBI:16066, ChEBI:CHEBI:16302, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.315; Evidence={ECO:0000250|UniProtKB:O54909}; CATALYTIC ACTIVITY: Reaction=9-cis-retinol + NAD(+) = 9-cis-retinal + H(+) + NADH; Xref=Rhea:RHEA:42052, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78272, ChEBI:CHEBI:78273; Evidence={ECO:0000250|UniProtKB:O54909}; CATALYTIC ACTIVITY: Reaction=5alpha-androstane-3alpha,17beta-diol + NAD(+) = 17beta-hydroxy-5alpha-androstan-3-one + H(+) + NADH; Xref=Rhea:RHEA:42004, ChEBI:CHEBI:15378, ChEBI:CHEBI:16330, ChEBI:CHEBI:36713, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.53; Evidence={ECO:0000269|PubMed:10329026, ECO:0000269|PubMed:9677409}; CATALYTIC ACTIVITY: Reaction=androsterone + NAD(+) = 5alpha-androstan-3,17-dione + H(+) + NADH; Xref=Rhea:RHEA:20381, ChEBI:CHEBI:15378, ChEBI:CHEBI:15994, ChEBI:CHEBI:16032, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.209; Evidence={ECO:0000269|PubMed:12534290, ECO:0000269|PubMed:29541409, ECO:0000269|PubMed:9677409};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.14 uM for 3alpha-hydroxy-5alpha-androstan-17-one (androsterone) {ECO:0000269|PubMed:12534290, ECO:0000269|PubMed:9677409}; KM=0.22 uM for 5alpha-androstane-3,17-dione (androstanediol) {ECO:0000269|PubMed:9677409}; KM=0.8 uM for 17beta-hydroxy-5alpha-androstan-3-one (dihydrotestosterone) {ECO:0000269|PubMed:9677409}; KM=0.13 uM for NAD {ECO:0000269|PubMed:9677409}; KM=190 uM for NADP {ECO:0000269|PubMed:9677409}; KM=5.8 uM for all-trans-retinol {ECO:0000269|PubMed:9677409}; KM=3.5 uM for 13-cis-retinol {ECO:0000269|PubMed:9677409}; KM=3.6 uM for CRBP-all-trans-retinol {ECO:0000269|PubMed:9677409};
|
PATHWAY: Cofactor metabolism; retinol metabolism. {ECO:0000269|PubMed:10329026, ECO:0000269|PubMed:9677409}.
| null | null |
FUNCTION: Oxidoreductase with a preference for NAD. Oxidizes all-trans-retinol, 9-cis-retinol, 11-cis-retinol and 13-cis-retinol to the corresponding aldehydes (PubMed:10329026, PubMed:12534290, PubMed:9677409). Has higher activity towards CRBP-bound retinol than with free retinol (PubMed:12534290). Oxidizes also 3-alpha-hydroxysteroids. Oxidizes androstanediol and androsterone to dihydrotestosterone and androstanedione. Can also catalyze the reverse reaction (PubMed:10329026, PubMed:29541409, PubMed:9677409). {ECO:0000269|PubMed:10329026, ECO:0000269|PubMed:12534290, ECO:0000269|PubMed:29541409, ECO:0000269|PubMed:9677409}.
|
Homo sapiens (Human)
|
O75460
|
ERN1_HUMAN
|
MPARRLLLLLTLLLPGLGIFGSTSTVTLPETLLFVSTLDGSLHAVSKRTGSIKWTLKEDPVLQVPTHVEEPAFLPDPNDGSLYTLGSKNNEGLTKLPFTIPELVQASPCRSSDGILYMGKKQDIWYVIDLLTGEKQQTLSSAFADSLCPSTSLLYLGRTEYTITMYDTKTRELRWNATYFDYAASLPEDDVDYKMSHFVSNGDGLVVTVDSESGDVLWIQNYASPVVAFYVWQREGLRKVMHINVAVETLRYLTFMSGEVGRITKWKYPFPKETEAKSKLTPTLYVGKYSTSLYASPSMVHEGVAVVPRGSTLPLLEGPQTDGVTIGDKGECVITPSTDVKFDPGLKSKNKLNYLRNYWLLIGHHETPLSASTKMLERFPNNLPKHRENVIPADSEKKSFEEVINLVDQTSENAPTTVSRDVEEKPAHAPARPEAPVDSMLKDMATIILSTFLLIGWVAFIITYPLSMHQQQQLQHQQFQKELEKIQLLQQQQQQLPFHPPGDTAQDGELLDTSGPYSESSGTSSPSTSPRASNHSLCSGSSASKAGSSPSLEQDDGDEETSVVIVGKISFCPKDVLGHGAEGTIVYRGMFDNRDVAVKRILPECFSFADREVQLLRESDEHPNVIRYFCTEKDRQFQYIAIELCAATLQEYVEQKDFAHLGLEPITLLQQTTSGLAHLHSLNIVHRDLKPHNILISMPNAHGKIKAMISDFGLCKKLAVGRHSFSRRSGVPGTEGWIAPEMLSEDCKENPTYTVDIFSAGCVFYYVISEGSHPFGKSLQRQANILLGACSLDCLHPEKHEDVIARELIEKMIAMDPQKRPSAKHVLKHPFFWSLEKQLQFFQDVSDRIEKESLDGPIVKQLERGGRAVVKMDWRENITVPLQTDLRKFRTYKGGSVRDLLRAMRNKKHHYRELPAEVRETLGSLPDDFVCYFTSRFPHLLAHTYRAMELCSHERLFQPYYFHEPPEPQPPVTPDAL
|
2.7.11.1; 3.1.26.-
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:21317875, ECO:0000269|PubMed:9637683};
|
cellular response to glucose stimulus [GO:0071333]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to unfolded protein [GO:0034620]; cellular response to vascular endothelial growth factor stimulus [GO:0035924]; endothelial cell proliferation [GO:0001935]; insulin metabolic process [GO:1901142]; intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress [GO:0070059]; IRE1-mediated unfolded protein response [GO:0036498]; mRNA catabolic process [GO:0006402]; mRNA splicing, via endonucleolytic cleavage and ligation [GO:0070054]; peptidyl-serine autophosphorylation [GO:0036289]; peptidyl-serine trans-autophosphorylation [GO:1990579]; positive regulation of endoplasmic reticulum unfolded protein response [GO:1900103]; positive regulation of JUN kinase activity [GO:0043507]; positive regulation of RNA splicing [GO:0033120]; positive regulation of vascular associated smooth muscle cell proliferation [GO:1904707]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]; regulation of macroautophagy [GO:0016241]; response to endoplasmic reticulum stress [GO:0034976]
|
AIP1-IRE1 complex [GO:1990597]; cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Ire1 complex [GO:1990332]; IRE1-RACK1-PP2A complex [GO:1990630]; IRE1-TRAF2-ASK1 complex [GO:1990604]; mitochondrion [GO:0005739]; nuclear inner membrane [GO:0005637]
|
ADP binding [GO:0043531]; ATP binding [GO:0005524]; enzyme binding [GO:0019899]; Hsp70 protein binding [GO:0030544]; Hsp90 protein binding [GO:0051879]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; platelet-derived growth factor receptor binding [GO:0005161]; protein homodimerization activity [GO:0042803]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; RNA endonuclease activity [GO:0004521]; unfolded protein binding [GO:0051082]
|
PF00069;PF06479;
|
1.20.1440.180;1.10.510.10;2.130.10.10;
|
Protein kinase superfamily, Ser/Thr protein kinase family
|
PTM: Autophosphorylated following homodimerization. Autophosphorylation promotes activation of the endoribonuclease domain (PubMed:12637535, PubMed:21317875, PubMed:28128204, PubMed:9637683). In response to ER stress, phosphorylated at Ser-724, Ser-729 and possibly Ser-726; phosphorylation promotes oligomerization and endoribonuclease activity (PubMed:30118681). Dephosphorylated at Ser-724, Ser-729 and possibly Ser-726 by RPAP2 to abort failed ER-stress adaptation and trigger apoptosis (PubMed:30118681). {ECO:0000269|PubMed:12637535, ECO:0000269|PubMed:21317875, ECO:0000269|PubMed:28128204, ECO:0000269|PubMed:30118681, ECO:0000269|PubMed:9637683}.; PTM: ADP-ribosylated by PARP16 upon ER stress, which increases both kinase and endonuclease activities. {ECO:0000269|PubMed:23103912}.
|
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:9637683}; Single-pass type I membrane protein {ECO:0000269|PubMed:9637683}.
|
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; Evidence={ECO:0000269|PubMed:21317875, ECO:0000269|PubMed:9637683}; 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; Evidence={ECO:0000269|PubMed:21317875, ECO:0000269|PubMed:9637683};
| null | null | null | null |
FUNCTION: Serine/threonine-protein kinase and endoribonuclease that acts as a key sensor for the endoplasmic reticulum unfolded protein response (UPR) (PubMed:11175748, PubMed:11779464, PubMed:12637535, PubMed:21317875, PubMed:28128204, PubMed:30118681, PubMed:9637683). In unstressed cells, the endoplasmic reticulum luminal domain is maintained in its inactive monomeric state by binding to the endoplasmic reticulum chaperone HSPA5/BiP (PubMed:21317875). Accumulation of misfolded proteins in the endoplasmic reticulum causes release of HSPA5/BiP, allowing the luminal domain to homodimerize, promoting autophosphorylation of the kinase domain and subsequent activation of the endoribonuclease activity (PubMed:21317875). The endoribonuclease activity is specific for XBP1 mRNA and excises 26 nucleotides from XBP1 mRNA (PubMed:11779464, PubMed:21317875, PubMed:24508390). The resulting spliced transcript of XBP1 encodes a transcriptional activator protein that up-regulates expression of UPR target genes (PubMed:11779464, PubMed:21317875, PubMed:24508390). Acts as an upstream signal for ER stress-induced GORASP2-mediated unconventional (ER/Golgi-independent) trafficking of CFTR to cell membrane by modulating the expression and localization of SEC16A (PubMed:21884936, PubMed:28067262). {ECO:0000269|PubMed:11175748, ECO:0000269|PubMed:11779464, ECO:0000269|PubMed:12637535, ECO:0000269|PubMed:21317875, ECO:0000269|PubMed:21884936, ECO:0000269|PubMed:28067262, ECO:0000269|PubMed:28128204, ECO:0000269|PubMed:30118681, ECO:0000269|PubMed:9637683, ECO:0000305|PubMed:24508390}.
|
Homo sapiens (Human)
|
O75461
|
E2F6_HUMAN
|
MSQQRPARKLPSLLLDPTEETVRRRCRDPINVEGLLPSKIRINLEDNVQYVSMRKALKVKRPRFDVSLVYLTRKFMDLVRSAPGGILDLNKVATKLGVRKRRVYDITNVLDGIDLVEKKSKNHIRWIGSDLSNFGAVPQQKKLQEELSDLSAMEDALDELIKDCAQQLFELTDDKENERLAYVTYQDIHSIQAFHEQIVIAVKAPAETRLDVPAPREDSITVHIRSTNGPIDVYLCEVEQGQTSNKRSEGVGTSSSESTHPEGPEEEENPQQSEELLEVSN
| null | null |
cell cycle [GO:0007049]; negative regulation of transcription by RNA polymerase II [GO:0000122]; regulation of transcription by RNA polymerase II [GO:0006357]
|
chromatin [GO:0000785]; MLL1 complex [GO:0071339]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575]
|
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; protein dimerization activity [GO:0046983]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF16421;PF02319;
|
6.10.250.540;1.10.10.10;
|
E2F/DP family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9689056, ECO:0000269|PubMed:9704927}.
| null | null | null | null | null |
FUNCTION: Inhibitor of E2F-dependent transcription (PubMed:9501179, PubMed:9689056, PubMed:9704927). Binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3' (PubMed:9501179). Has a preference for the 5'-TTTCCCGC-3' E2F recognition site (PubMed:9501179). E2F6 lacks the transcriptional activation and pocket protein binding domains (PubMed:9501179, PubMed:9704927). Appears to regulate a subset of E2F-dependent genes whose products are required for entry into the cell cycle but not for normal cell cycle progression (PubMed:9501179, PubMed:9689056). Represses expression of some meiosis-specific genes, including SLC25A31/ANT4 (By similarity). May silence expression via the recruitment of a chromatin remodeling complex containing histone H3-K9 methyltransferase activity. Overexpression delays the exit of cells from the S-phase (PubMed:9501179). {ECO:0000250|UniProtKB:O54917, ECO:0000269|PubMed:9501179, ECO:0000269|PubMed:9689056, ECO:0000269|PubMed:9704927}.
|
Homo sapiens (Human)
|
O75462
|
CRLF1_HUMAN
|
MPAGRRGPAAQSARRPPPLLPLLLLLCVLGAPRAGSGAHTAVISPQDPTLLIGSSLLATCSVHGDPPGATAEGLYWTLNGRRLPPELSRVLNASTLALALANLNGSRQRSGDNLVCHARDGSILAGSCLYVGLPPEKPVNISCWSKNMKDLTCRWTPGAHGETFLHTNYSLKYKLRWYGQDNTCEEYHTVGPHSCHIPKDLALFTPYEIWVEATNRLGSARSDVLTLDILDVVTTDPPPDVHVSRVGGLEDQLSVRWVSPPALKDFLFQAKYQIRYRVEDSVDWKVVDDVSNQTSCRLAGLKPGTVYFVQVRCNPFGIYGSKKAGIWSEWSHPTAASTPRSERPGPGGGACEPRGGEPSSGPVRRELKQFLGWLKKHAYCSNLSFRLYDQWRAWMQKSHKTRNQDEGILPSGRRGTARGPAR
| null | null |
cytokine-mediated signaling pathway [GO:0019221]; negative regulation of motor neuron apoptotic process [GO:2000672]; negative regulation of neuron apoptotic process [GO:0043524]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of tyrosine phosphorylation of STAT protein [GO:0042531]; ureteric bud development [GO:0001657]
|
CRLF-CLCF1 complex [GO:0097058]; cytosol [GO:0005829]; external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; receptor complex [GO:0043235]
|
cytokine binding [GO:0019955]; cytokine receptor activity [GO:0004896]
|
PF09067;PF00041;
|
2.60.40.10;
|
Type I cytokine receptor family, Type 3 subfamily
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9686600}.
| null | null | null | null | null |
FUNCTION: In complex with CLCF1, forms a heterodimeric neurotropic cytokine that plays a crucial role during neuronal development (Probable). May also play a regulatory role in the immune system. {ECO:0000305|PubMed:26858303}.
|
Homo sapiens (Human)
|
O75469
|
NR1I2_HUMAN
|
MEVRPKESWNHADFVHCEDTESVPGKPSVNADEEVGGPQICRVCGDKATGYHFNVMTCEGCKGFFRRAMKRNARLRCPFRKGACEITRKTRRQCQACRLRKCLESGMKKEMIMSDEAVEERRALIKRKKSERTGTQPLGVQGLTEEQRMMIRELMDAQMKTFDTTFSHFKNFRLPGVLSSGCELPESLQAPSREEAAKWSQVRKDLCSLKVSLQLRGEDGSVWNYKPPADSGGKEIFSLLPHMADMSTYMFKGIISFAKVISYFRDLPIEDQISLLKGAAFELCQLRFNTVFNAETGTWECGRLSYCLEDTAGGFQQLLLEPMLKFHYMLKKLQLHEEEYVLMQAISLFSPDRPGVLQHRVVDQLQEQFAITLKSYIECNRPQPAHRFLFLKIMAMLTELRSINAQHTQRLLRIQDIHPFATPLMQELFGITGS
| null | null |
cell differentiation [GO:0030154]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of gene expression [GO:0010628]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of DNA-templated transcription [GO:0006355]; signal transduction [GO:0007165]; steroid metabolic process [GO:0008202]; xenobiotic catabolic process [GO:0042178]; xenobiotic metabolic process [GO:0006805]; xenobiotic transport [GO:0042908]
|
chromatin [GO:0000785]; intermediate filament cytoskeleton [GO:0045111]; nuclear body [GO:0016604]; nucleoplasm [GO:0005654]; transcription regulator complex [GO:0005667]
|
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; nuclear receptor activity [GO:0004879]; nuclear receptor binding [GO:0016922]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; sequence-specific double-stranded DNA binding [GO:1990837]; zinc ion binding [GO:0008270]
|
PF00104;PF00105;
|
3.30.50.10;1.10.565.10;
|
Nuclear hormone receptor family, NR1 subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407, ECO:0000269|PubMed:12606758}.
| null | null | null | null | null |
FUNCTION: Nuclear receptor that binds and is activated by variety of endogenous and xenobiotic compounds. Transcription factor that activates the transcription of multiple genes involved in the metabolism and secretion of potentially harmful xenobiotics, drugs and endogenous compounds. Activated by the antibiotic rifampicin and various plant metabolites, such as hyperforin, guggulipid, colupulone, and isoflavones. Response to specific ligands is species-specific. Activated by naturally occurring steroids, such as pregnenolone and progesterone. Binds to a response element in the promoters of the CYP3A4 and ABCB1/MDR1 genes. {ECO:0000269|PubMed:11297522, ECO:0000269|PubMed:11668216, ECO:0000269|PubMed:12578355, ECO:0000269|PubMed:18768384, ECO:0000269|PubMed:19297428, ECO:0000269|PubMed:9727070}.
|
Homo sapiens (Human)
|
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