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
|
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
O59763
|
OCA2_SCHPO
|
MSVTPPNVQFNLNGDSDHKSDNSSSSLENKLDTELKITSPPRNPPQRLHPVDFSEHADTDDDMNHPLPRVQSPVHIKNHIDPKLAEDRYRSSAARHFEPISIPPSAITSEDEDDYHGSANSSTVLPPRTENALHAASPKPSGSTGYTSPALSQNSGSGGEGESDEGSFNTQHHRSPIFQAYPSSEDLVGDPNDPYRRTRRAPIKTNPHDIPSQFIFRKLGLHHGKHGHHGHSGSLSLKSLVPNHHDKHDKHDKHEKHHSSLDLRRFFKSHQKTDKEKKPSVSKSKSSANLQDDHFGLFKKYGKFGRMLGSGAGGSVRIMKRSSDGKIFAVKEFRARRPTETEREYARKVTAEFCIGSALHHTNIIETLDIVEENKKFYEVMEYAPYDMFSIVMSGKMTMPEVYCCFKQLLSGVAYLHSMGLAHRDLKLDNLVVDSNCFVKIIDFGSAVVFKYPFEADIVEATGVVGSDPYLAPETLVRKLYDPRAVDIWSSAIIFCCMALRRFPWKYPKLSDNSFRLFCMKQPSNDAESPSDILADIKKQRLVEQGCEPIRKTDESHSPNSKTDNSSTHKQELYGPWRLLRLLPRETRAVIAHMLELDPVKRYDIHRVFADNWINDISMCHMENGKVIHSPTHVHNLVASEESPAPPAKH
|
2.7.11.1
| null |
cell cycle [GO:0007049]; intracellular signal transduction [GO:0035556]; negative regulation of transcription by RNA polymerase II [GO:0000122]; phosphorylation [GO:0016310]; regulation of nitrogen utilization [GO:0006808]; signaling [GO:0023052]
|
cell division site [GO:0032153]; cell tip [GO:0051286]; cytosol [GO:0005829]
|
ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, Ser/Thr protein kinase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Note=Barrier septum. Cell tip. {ECO:0000269|PubMed:16823372}.
|
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:0000250|UniProtKB:Q08732}; 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:0000250|UniProtKB:Q08732};
| null | null | null | null |
FUNCTION: Overexpression causes cell cycle arrest. {ECO:0000269|PubMed:12237855}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O59767
|
MAD3_SCHPO
|
MEPLDAGKNWVHMDVIEQSKENIEPRKAGHSASALAKSSSRNHTEKEVAGLQKERMGHERKIETSESLDDPLQVWIDYIKWTLDNFPQGETKTSGLVTLLERCTREFVRNPLYKDDVRYLRIWMQYVNYIDEPVELFSFLAHHHIGQESSIFYEEYANYFESRGLFQKADEVYQKGKRMKAKPFLRFQQKYQQFTHRWLEFAPQSFSSNTNSVNPLQTTFESTNIQEISQSRTKISKPKFKFSVYSDADGSGKDGQPGTWQTLGTVDQRRKENNISATSWVGEKLPLKSPRKLDPLGKFQVHCDEEVSKE
| null | null |
cell division [GO:0051301]; meiotic sister chromatid cohesion, centromeric [GO:0051754]; mitotic spindle assembly checkpoint signaling [GO:0007094]; negative regulation of mitotic metaphase/anaphase transition [GO:0045841]
|
cytosol [GO:0005829]; kinetochore [GO:0000776]; mitotic checkpoint complex [GO:0033597]; nucleus [GO:0005634]
|
anaphase-promoting complex binding [GO:0010997]; protein kinase activity [GO:0004672]; ubiquitin ligase inhibitor activity [GO:1990948]
|
PF08311;
|
1.25.40.430;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11909965}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:11909965}. Note=Associated with the kinetochore.
| null | null | null | null | null |
FUNCTION: Has a role in transducing the anaphase inhibitory signal to the anaphase promoting complex (APC). Forms part of the mad2 feedback control. {ECO:0000269|PubMed:11909965}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O59790
|
ARK1_SCHPO
|
MSDSKLADSLNCLSVSTPSTTANPGRQQLLRLAVSNQRQVNNVSLANGKENKRTSNSKFNSSLRKIEEPIAGVPSSAGPQWREFHIGMFEIGKPLGKGKFGRVYLAKEKKTGFIVALKTLHKSELVQSKIEKQVRREIEIQSNLRHKNILRLYGHFHDEKRIYLILEFAGRGELYQHLRRAKRFSEEVASKYIFQMANALSYLHKKHVIHRDIKPENILLGIDGEIKLSDFGWSVHAPSNRRTTLCGTLDYLPPEMVEGKEHTEKVDLWSLGVLTYEFLVGAPPFEDMSGHSATYKRIAKVDLKIPSFVPPDARDLISRLLQHNPEKRMSLEQVMRHPWIVKYKDSWTRKSSESS
|
2.7.11.1
| null |
attachment of meiotic spindle microtubules to kinetochore [GO:0051316]; interphase mitotic telomere clustering [GO:0120110]; meiotic spindle assembly checkpoint signaling [GO:0033316]; mitotic sister chromatid biorientation [GO:1990758]; mitotic sister chromatid segregation [GO:0000070]; mitotic spindle assembly checkpoint signaling [GO:0007094]; mitotic spindle organization [GO:0007052]; phosphorylation [GO:0016310]; positive regulation of G2/M transition of mitotic cell cycle [GO:0010971]; positive regulation of kinetochore assembly [GO:1905561]; positive regulation of mitotic cell cycle spindle assembly checkpoint [GO:0090267]; positive regulation of mitotic chromosome condensation [GO:1903380]; positive regulation of mitotic sister chromatid arm separation [GO:1905824]; positive regulation of mitotic sister chromatid biorientation [GO:0140429]; protein localization to kinetochore [GO:0034501]; regulation of cytokinesis [GO:0032465]; regulation of mitotic cytokinesis [GO:1902412]; regulation of spindle attachment to meiosis I kinetochore [GO:1904967]; repair of mitotic kinetochore microtubule attachment defect [GO:0140273]
|
chromosome passenger complex [GO:0032133]; chromosome, centromeric region [GO:0000775]; chromosome, telomeric region [GO:0000781]; cytoplasm [GO:0005737]; inner kinetochore [GO:0000939]; kinetochore [GO:0000776]; meiotic spindle [GO:0072687]; meiotic spindle midzone [GO:1990385]; mitotic spindle midzone [GO:1990023]; nucleolar peripheral inclusion body [GO:0140602]; spindle microtubule [GO:0005876]; spindle midzone [GO:0051233]
|
ATP binding [GO:0005524]; histone H3S10 kinase activity [GO:0035175]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, Ser/Thr protein kinase family, Aurora subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:16823372}. Note=Associates with the elongating spindle during anaphase.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
| null | null | null | null |
FUNCTION: Required for the spindle checkpoint attachment response during spindle formation, kinetochore microtubule interactions and chromosome segregation during anaphase. Ark1 activity depends upon cut17 function and phosphorylation. Ark1 with bir1 is required for full-scale association with kinetochores and formation of a complex with mad3. Ark1 is also required for phosphorylation of histone H3 that accompanies chromosome condensation and condensin recruitment to mitotic chromatin. Ark1 with pic1 is required for the execution of cytokinesis. {ECO:0000269|PubMed:11792803, ECO:0000269|PubMed:11950927, ECO:0000269|PubMed:12676091}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O59791
|
SRR_SCHPO
|
MSDNLVLPTYDDVASASERIKKFANKTPVLTSSTVNKEFVAEVFFKCENFQKMGAFKFRGALNALSQLNEAQRKAGVLTFSSGNHAQAIALSAKILGIPAKIIMPLDAPEAKVAATKGYGGQVIMYDRYKDDREKMAKEISEREGLTIIPPYDHPHVLAGQGTAAKELFEEVGPLDALFVCLGGGGLLSGSALAARHFAPNCEVYGVEPEAGNDGQQSFRKGSIVHIDTPKTIADGAQTQHLGNYTFSIIKEKVDDILTVSDEELIDCLKFYAARMKIVVEPTGCLSFAAARAMKEKLKNKRIGIIISGGNVDIERYAHFLSQ
|
4.3.1.17; 4.3.1.18; 5.1.1.18
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:19155267, ECO:0000269|PubMed:19640845, ECO:0000269|Ref.2}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q9GZT4}; Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:Q9GZT4}; COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:19155267, ECO:0000269|PubMed:19640845, ECO:0000269|Ref.2};
|
D-serine biosynthetic process [GO:0070179]; D-serine metabolic process [GO:0070178]; L-serine metabolic process [GO:0006563]
|
cytoplasm [GO:0005737]
|
ATP binding [GO:0005524]; D-serine ammonia-lyase activity [GO:0008721]; L-serine ammonia-lyase activity [GO:0003941]; magnesium ion binding [GO:0000287]; protein homodimerization activity [GO:0042803]; pyridoxal phosphate binding [GO:0030170]; serine racemase activity [GO:0030378]; threonine racemase activity [GO:0018114]
|
PF00291;
|
3.40.50.1100;
|
Serine/threonine dehydratase family
|
PTM: Modification of the active site Lys by its substrate Ser to lysino-D-alanine reduces but does not abolish enzyme activity.
| null |
CATALYTIC ACTIVITY: Reaction=L-serine = D-serine; Xref=Rhea:RHEA:10980, ChEBI:CHEBI:33384, ChEBI:CHEBI:35247; EC=5.1.1.18; Evidence={ECO:0000269|PubMed:19640845}; CATALYTIC ACTIVITY: Reaction=L-serine = NH4(+) + pyruvate; Xref=Rhea:RHEA:19169, ChEBI:CHEBI:15361, ChEBI:CHEBI:28938, ChEBI:CHEBI:33384; EC=4.3.1.17; Evidence={ECO:0000269|PubMed:19640845}; CATALYTIC ACTIVITY: Reaction=D-serine = NH4(+) + pyruvate; Xref=Rhea:RHEA:13977, ChEBI:CHEBI:15361, ChEBI:CHEBI:28938, ChEBI:CHEBI:35247; EC=4.3.1.18; Evidence={ECO:0000269|PubMed:19640845};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=36 mM for serine {ECO:0000269|PubMed:19640845}; Vmax=870 nmol/min/mg enzyme {ECO:0000269|PubMed:19640845};
| null | null | null |
FUNCTION: Catalyzes the synthesis of D-serine from L-serine. Has dehydratase activity towards both L-serine and D-serine. {ECO:0000269|PubMed:19640845}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O59836
|
HIM1_SCHPO
|
MNLGRCPLAPRSANIVLPKHDAVSKQKEYRIEEKTNEAQREEIITWKDNREDEGEVKTDFEVVNNENIITTTPKHQTVITPKSYRKSVKRIKHDAPQNEDIPVMKGLAPINADTESKAESMAAGKVLGSKNSSQKARLQEWKRQYKKAFPHFRFYLDGCDPSVAHRVKKQIQQLGGHVETFFSGNVTHVATVRAIQDVSVKYAKQDVITKARQLNMKIWSMEKLCNRVLKTLMENDQCTTNAPTKQGNDLSYLLYVEKVQGTNERDLSVPRQDFVHFRGPYLYVHDIANIYKPILLREWQKPLPDRDVPWPTFRATSIGRCPFVPETKYRLSTSKSLVAKNDQQLLQRQSQEPSLILRANSMKASLPDISNTGISGMNTNTTYNTNINNTPQTAISGITQDTSPSIRTNCHHCLDDGMQASGIVQSNLTSAAMSNNSAIRSGSAASVPVVTINGRDIAELKKRIIQQKSGMIGKDYSYKAMLHNTSQRKIRVDAKPGYCENCREKFDNFESHIRSSRHRRFAENNDNFKDLDELFALVQRPLRPD
| null | null |
DNA damage response [GO:0006974]; mitotic DNA replication checkpoint signaling [GO:0033314]; positive regulation of DNA repair [GO:0045739]; positive regulation of DNA replication initiation [GO:1903468]; positive regulation of nuclear cell cycle DNA replication [GO:0010571]; regulation of cell cycle phase transition [GO:1901987]
|
Dbf4-dependent protein kinase complex [GO:0031431]; mitotic spindle pole body [GO:0044732]; nucleus [GO:0005634]
|
nucleic acid binding [GO:0003676]; protein kinase activator activity [GO:0030295]; protein serine/threonine kinase activator activity [GO:0043539]; zinc ion binding [GO:0008270]
|
PF08630;PF07535;
|
3.40.50.10190;6.10.250.3410;
| null |
PTM: Hyperphosphorylated at the G1/S and S-phases of the cell cycle.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10409743}.
| null | null | null | null | null |
FUNCTION: Activates hsk1 kinase and is essential for G1/S transition. Has a role in S-phase checkpoint control induced by replication fork blocks after nucleotide deprivation and DNA damage. {ECO:0000269|PubMed:10409743}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O59855
|
HSP72_SCHPO
|
MSKSIGIDLGTTYSCVGHFSNNRVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPHNTIFDAKRLIGRKFDDPEVQSDMKHWPFKVISKDGKPVLQVEYKGETKTFTPEEISSMVLMKMRETAEAYLGGKVTDAVVTVPAYFNDSQRQATKDAGLIAGLNVLRIINEPTAAAIAYGLDRSNQGESNVLIFDLGGGTFDVSLLTIEEGIFEVKATAGDTHLGGEDFDSRLVNHFIQEFKRKNKKDITGNARAVRRLRTACERAKRTLSSSAQASIEIDSLFEGIDFYTSITRARFEELCADLFRKTMEPVERVLRDSKVDKASVNEIVLVGGSTRIPRVQKLVSDFFNGKEPCKSINPDEAVAYGAAVQAAVLTGDTSEKTQDLLLLDVAPLSMGIETAGGVMTPLIKRNTTIPTKKSEIFSTYSDNQPGVLIQVFEGERARTKDCNLLGKFELSGIPPAPRGVPQIEVTFDVDANGILNVSALEKGTGKTQKITITNDKGRLSKEEIDRMVAEAEKYKAEDEAESGRIQAKNHLESYAYSLRNSLDDPNLKDKVDASDKETVDKAVKETIEWLDSNTTAAKDEFEAKQKELESVANPIMAKIYQAGGAPGGMPGAAPGAAPGAAPGAAPGGDNGPEVEEVD
| null | null |
cellular response to heat [GO:0034605]; chaperone cofactor-dependent protein refolding [GO:0051085]; protein refolding [GO:0042026]; SRP-dependent cotranslational protein targeting to membrane, translocation [GO:0006616]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleolar peripheral inclusion body [GO:0140602]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; post-mRNA release spliceosomal complex [GO:0071014]; protein aggregate center [GO:0140453]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein folding chaperone [GO:0140662]; heat shock protein binding [GO:0031072]; protein folding chaperone [GO:0044183]; unfolded protein binding [GO:0051082]
|
PF00012;
|
1.20.1270.10;3.30.30.30;3.30.420.40;
|
Heat shock protein 70 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
| null | null | null | null | null | null |
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O59858
|
GPX1_SCHPO
|
MSHFYDLAPKDKDGNPFPFSNLKGKVVLVVNTASKCGFTPQYKGLEALYQKYKDRGFIILGFPCNQFGNQEPGSDEEIAQFCQKNYGVTFPVLAKINVNGDNVDPVYQFLKSQKKQLGLERIKWNFEKFLVNRQGQVIERYSSISKPEHLENDIESVL
|
1.11.1.24
| null |
cell redox homeostasis [GO:0045454]; cellular detoxification of hydrogen peroxide [GO:0061692]; cellular response to oxidative stress [GO:0034599]; hydrogen peroxide catabolic process [GO:0042744]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleus [GO:0005634]
|
phospholipid-hydroperoxide glutathione peroxidase activity [GO:0047066]; thioredoxin peroxidase activity [GO:0008379]; thioredoxin-dependent peroxiredoxin activity [GO:0140824]
|
PF00255;
|
3.40.30.10;
|
Glutathione peroxidase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18162174}. Mitochondrion {ECO:0000269|PubMed:18162174}.
|
CATALYTIC ACTIVITY: Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:50058; EC=1.11.1.24; Evidence={ECO:0000269|PubMed:18162174};
| null | null | null | null |
FUNCTION: Glutathione peroxidase-like protein that protects cells during oxidative stress. Has peroxidase activity reducing hydrogen peroxide, alkyl and phospholipid hydroperoxides using preferentially thioredoxin as a reducing power. May act as a scavenger of H(2)O(2). {ECO:0000269|PubMed:10455235, ECO:0000269|PubMed:20356456}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O59868
|
ATC1_SCHPO
|
MSVQYDAFSVEQTCADLETDMYNGLSSLQEITRRNKVHGDNDLKVEDEENMVVQFLKQFVKDPLILLLFASSAISVTLGNIDDAISIALAIVIVVTVGFVQEYRSEQSLKALNNLVPHYCNVIRSGKTEHIVASKLVPGDLVILQIGDRVPADLRIVEATELEIDESNLTGENSPRKKSSEAISSNISLTERNNIAFMGTLVRHGHGRGIVVATGSDTEFGRVFLTMQQTEKPKTPLQNSMDDLGKQLSLISLIGIAVIVLVGFFQGKNWLEMLTIGVSLAVAAIPEGLPIIVTVTLALGVLRMSKKRAIIRRLPSVETLGSVNVICSDKTGTLTMNHMTVTKIYTCGMLAAFSLPESEHIELSVRRTVGIEKALLAAALCNNSKVHNKADSILDTTCPWAGFPVDVALIECSERFGLKDPRETYSRISEVSFSSERKYMSVAVQYNSSKMNFMKGATEQVLSSCAYFSDQDGVQHELTAEMKENIQRNEFEMAASGLRIIAVASGINTNKLVFHGLFGINDPPRPQVRESVQYLMTGGVRVIMITGDSVVTAISIARSLGMAIPSNDEEAIRNYALTGAQLDDLDSSSLRDAVSRVVVFARTTPQHKMKIVEALQSLGDVVAMTGDGVNDAPALKLADIGIAMGRQGTDVAKEAADMILTDDSFATILSAVEEGKGIFNNIKNFITFQLSTSVAALSLIAISSVFGFQNPLNAMQILWINILMDGPPAQSLGVESVDEDVMMKPPRPRNAPIISVQLLQRVLLSAFIIVTVTIVVFRVQMQDGNVTARDTTMTFTCFVFFDMFNALACRSETKSVFKLGIFSNRMFNIAVGGSLIGQALVVYASPFQRIFQTEAIGLKDVLILLACTSSVLWVDEIRKWYRRRKGLVRTKSNYLLRNV
|
7.2.2.10
| null |
calcium ion transmembrane transport [GO:0070588]; intracellular calcium ion homeostasis [GO:0006874]; manganese ion transmembrane transport [GO:0071421]; manganese ion transport [GO:0006828]; release of sequestered calcium ion into cytosol by Golgi [GO:0061454]
|
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; nuclear envelope [GO:0005635]; plasma membrane [GO:0005886]
|
ABC-type manganese transporter activity [GO:0015410]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; calcium ion binding [GO:0005509]; P-type calcium transporter activity [GO:0005388]
|
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
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15470240}; Multi-pass membrane protein {ECO:0000269|PubMed:15470240}.
|
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;
| null | null | null | null |
FUNCTION: Transports calcium and manganese ions into the cell. Regulates cell morphogenesis through control of manganese and calcium homeostasis. {ECO:0000269|PubMed:14723709, ECO:0000269|PubMed:15470240}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O59893
|
AXE2_TALPU
|
MHSKFFAASLLGLGAAAIPLEGVMEKRSCPAIHVFGARETTASPGYGSSSTVVNGVLSAYPGSTAEAINYPACGGQSSCGGASYSSSVAQGIAAVASAVNSFNSQCPSTKIVLVGYSQGGEIMDVALCGGGDPNQGYTNTAVQLSSSAVNMVKAAIFMGDPMFRAGLSYEVGTCAAGGFDQRPAGFSCPSAAKIKSYCDASDPYCCNGSNAATHQGYGSEYGSQALAFVKSKLG
|
3.1.1.72
| null |
cellulose catabolic process [GO:0030245]; xylan catabolic process [GO:0045493]
|
extracellular region [GO:0005576]
|
acetylxylan esterase activity [GO:0046555]
|
PF01083;
|
3.40.50.1820;
|
Cutinase family, Acetylxylan esterase subfamily
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8756392}.
|
CATALYTIC ACTIVITY: Reaction=Deacetylation of xylans and xylo-oligosaccharides.; EC=3.1.1.72;
| null |
PATHWAY: Glycan degradation; xylan degradation.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6. {ECO:0000269|PubMed:8756392};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 60 degrees Celsius. {ECO:0000269|PubMed:8756392};
|
FUNCTION: Degrades acetylated xylans by cleaving acetyl side groups from the hetero-xylan backbone. {ECO:0000269|PubMed:8756392}.
|
Talaromyces purpureogenus (Soft rot fungus) (Penicillium purpureogenum)
|
O59923
|
SIR2_CANAL
|
MTTFWSQTINRQNGGVATATATATATAATTTPTAGGTGAGTTTSTKGMITPTPFNIDINNDLNDFDGKFIETFKPDLELQKKYRSFIQREGALSFLRTEITQSMSKRDICVLILNLGYPKKAVEDYPILTLKELAYILLKLMLTDSAQLEPKVEIDENDNKNDGTNNSDIDSDIDSNSDMDSQSESGELDDAMDVDDSLSENEDEYDQDMSTTTLKRTINMTPFKYKLPDLISDLSRAKKIMVVTGAGISTSLGIPDFRSFKGLYNQLSKLNLSDPQKVFDLQTFMREPGLFYTIAHLVLPPDGKFSLLHAFLKLLQDKHKLLRNYTQNIDNLEQRAGLKSEKLVQCHGSFAKAKCVSCQGIFAGEKIYNHIRRKQVPRCAICWKNTKQAPIHFGAIKPTITFFGEDLPERFHTLMDKDLQQIDLFLVIGTSLKVEPVASIIERVPYKVPKILINKDPIPNRGFNLQLLGLCDDVVSYLCKCLKWDIPHADFNNNDEFKLSKLKNGDWEIVKKSTSTKK
|
2.3.1.286
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P06700}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P06700};
|
negative regulation of DNA recombination at telomere [GO:0048239]; rDNA heterochromatin formation [GO:0000183]; regulation of cell differentiation [GO:0045595]
|
nuclear inner membrane [GO:0005637]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; rDNA heterochromatin [GO:0033553]
|
metal ion binding [GO:0046872]; NAD+ binding [GO:0070403]; NAD-dependent histone H4K16 deacetylase activity [GO:0046970]; transcription corepressor activity [GO:0003714]; transferase activity [GO:0016740]
|
PF02146;
|
3.30.1600.10;3.40.50.1220;
|
Sirtuin family, Class I subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250, ECO:0000250|UniProtKB:P06700}.
|
CATALYTIC ACTIVITY: Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:43636, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:61930, ChEBI:CHEBI:83767; EC=2.3.1.286; Evidence={ECO:0000255|PROSITE-ProRule:PRU00236};
| null | null | null | null |
FUNCTION: NAD-dependent deacetylase. Heterochromatin component that silences transcription at silent mating loci, telomeres and the ribosomal DNA, and that also suppresses recombination in the rDNA and extends replicative life span. It acts as a NAD-dependent histone deacetylase, which deacetylates 'Lys-9' and 'Lys-14' of Histone H3 and 'Lys-16' of Histone H4. Functions in the distribution of oxidatively damaged proteins during cell division. Mediates phenotypic switching. {ECO:0000269|PubMed:10228170, ECO:0000269|PubMed:18691183, ECO:0000269|PubMed:23341961}.
|
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
|
O59924
|
SODC_CANAX
|
MVKAVAVVRGDSKVQGTVHFEQESESAPTTISWEIEGNDPNALRGFHIHQFGDNTNGCTSAGPHFNPFGKQHGAPEDDERHVGDLGNISTDGNGVAKGTKQDLLIKLIGKDSILGRTIVVHAGTDDYGKGGFEDSKTTGHAGARPACGVIGLTQ
|
1.15.1.1
|
COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250|UniProtKB:P00445}; Note=Binds 1 copper ion per subunit. {ECO:0000250|UniProtKB:P00445}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P00445}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P00445};
|
cell redox homeostasis [GO:0045454]; cellular response to oxidative stress [GO:0034599]; filamentous growth [GO:0030447]; filamentous growth of a population of unicellular organisms in response to starvation [GO:0036170]; fungal-type cell wall organization [GO:0031505]; intracellular copper ion homeostasis [GO:0006878]; intracellular zinc ion homeostasis [GO:0006882]; negative regulation of cellular respiration [GO:1901856]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein maturation by copper ion transfer [GO:0015680]; protein stabilization [GO:0050821]
|
cytosol [GO:0005829]; mitochondrial intermembrane space [GO:0005758]; nucleus [GO:0005634]; peroxisome [GO:0005777]; superoxide dismutase complex [GO:1902693]
|
copper ion binding [GO:0005507]; superoxide dismutase activity [GO:0004784]
|
PF00080;
|
2.60.40.200;
|
Cu-Zn superoxide dismutase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P00445}.
|
CATALYTIC ACTIVITY: Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:18421; EC=1.15.1.1; Evidence={ECO:0000250|UniProtKB:P85978};
| null | null | null | null |
FUNCTION: Destroys radicals which are normally produced within the cells and which are toxic to biological systems. {ECO:0000250|UniProtKB:P00442}.
|
Candida albicans (Yeast)
|
O59933
|
ERG25_CANAL
|
MSSISNVYHDYSSFSNATTFSQVYQNFNQLDNLNVFEKLWGSYYYYMANDLFATGLLFFLTHEIFYFGRCLPWAIIDRIPYFRKWKIQDEKIPSDKEQWECLKSVLTSHFLVEAFPIWFFHPLCQKIGISYQVPFPKITDMLIQWAVFFVLEDTWHYWFHRGLHYGVFYKYIHKQHHRYAAPFGLAAEYAHPVEVALLGLGTVGIPIVWCLITGNLHLFTVSIWIILRLFQAVDAHSGYEFPWSLHNFLPFWAGADHHDEHHHYFIGGYSSSFRWWDFILDTEAGPKAKKGREDKVKQNVEKLQKKNL
|
1.14.18.9
|
COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250|UniProtKB:P53045};
|
cholesterol biosynthetic process via lathosterol [GO:0033490]; ergosterol biosynthetic process [GO:0006696]; sphingolipid biosynthetic process [GO:0030148]
|
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]
|
C-4 methylsterol oxidase activity [GO:0000254]; C-5 sterol desaturase activity [GO:0000248]; iron ion binding [GO:0005506]; sphingolipid delta-4 desaturase activity [GO:0042284]; sphingosine hydroxylase activity [GO:0000170]
|
PF04116;
| null |
Sterol desaturase family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=4,4-dimethyl-5alpha-cholest-7-en-3beta-ol + 6 Fe(II)-[cytochrome b5] + 5 H(+) + 3 O2 = 4alpha-carboxy-4beta-methyl-5alpha-cholest-7-ene-3beta-ol + 6 Fe(III)-[cytochrome b5] + 4 H2O; Xref=Rhea:RHEA:55220, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16455, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:58387; EC=1.14.18.9; Evidence={ECO:0000305|PubMed:10783002}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55221; Evidence={ECO:0000305|PubMed:10783002};
| null |
PATHWAY: Steroid biosynthesis; zymosterol biosynthesis; zymosterol from lanosterol: step 3/6. {ECO:0000269|PubMed:10783002}.
| null | null |
FUNCTION: C-4 methylsterol oxidase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (PubMed:10783002). ERG25 is a catalytic component of the C-4 demethylation complex that catalyzes the conversion of 4,4-dimethylfecosterol into fecosterol via 4-methylfecosterol (PubMed:10783002). Catalyzes the three-step monooxygenation required for the demethylation of 4,4-dimethyl and 4alpha-methylsterols (PubMed:10783002). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase ERG9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, the squalene epoxidase ERG1 catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, which is considered to be a rate-limiting enzyme in steroid biosynthesis. Then, the lanosterol synthase ERG7 catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol core. In the next steps, lanosterol is transformed to zymosterol through a complex process involving various demethylation, reduction and desaturation reactions. The lanosterol 14-alpha-demethylase ERG11 (also known as CYP51) catalyzes C14-demethylation of lanosterol to produce 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol, which is critical for ergosterol biosynthesis. The C-14 reductase ERG24 reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24-dienol. 4,4-dimethyl-cholesta-8,24-dienol is substrate of the C-4 demethylation complex ERG25-ERG26-ERG27 in which ERG25 catalyzes the three-step monooxygenation required for the demethylation of 4,4-dimethyl and 4alpha-methylsterols, ERG26 catalyzes the oxidative decarboxylation that results in a reduction of the 3-beta-hydroxy group at the C-3 carbon to an oxo group, and ERG27 is responsible for the reduction of the keto group on the C-3. ERG28 has a role as a scaffold to help anchor ERG25, ERG26 and ERG27 to the endoplasmic reticulum and ERG29 regulates the activity of the iron-containing C4-methylsterol oxidase ERG25. Then, the sterol 24-C-methyltransferase ERG6 catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol. The C-8 sterol isomerase ERG2 catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase ERG3 then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The C-22 sterol desaturase ERG5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductase ERG4 to produce ergosterol (Probable). {ECO:0000269|PubMed:10783002, ECO:0000305}.
|
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
|
O59945
|
FIMB_SCHPO
|
MLALKLQKKYPELTNEEILTLTDQFNKLDVDGKGYLDQPTTIKAFEDSKKGSYDEVREAIREVNVDSSGRVEPEDFVGIFNVLKKGVEGTEVKKGRITIKGSSSSVSHTINEEERREFIKHINSVLAGDPDVGSRVPINTETFEFFDQCKDGLILSKLINDSVPDTIDERVLNKQRNNKPLDNFKCIENNNVVINSAKAMGGISITNIGAGDILEGREHLILGLVWQIIRRGLLGKIDITLHPELYRLLEEDETLDQFLRLPPEKILLRWFNYHLKAANWPRTVSNFSKDVSDGENYTVLLNQLAPELCSRAPLQTTDVLQRAEQVLQNAEKLDCRKYLTPTAMVAGNPKLNLAFVAHLFNTHPGLEPLNEEEKPEIEPFDAEGEREARVFTLWLNSLDVTPSIHDFFNNLRDGLILLQAYDKITPNTVNWKKVNKAPASGDEMMRFKAVENCNYAVDLGKNQGFSLVGIQGADITDGSRTLTLALVWQMMRMNITKTLHSLSRGGKTLSDSDMVAWANSMAAKGGKGSQIRSFRDPSISTGVFVLDVLHGIKSEYVDYNLVTDGSTEELAIQNARLAISIARKLGAVIFILPEDIVAVRPRLVLHFIGSLMAV
| null | null |
actin cortical patch localization [GO:0051666]; actin cortical patch organization [GO:0044396]; actin filament bundle assembly [GO:0051017]; actin filament network formation [GO:0051639]; actomyosin contractile ring organization [GO:0044837]; endocytosis [GO:0006897]; formin-nucleated actin cable organization [GO:0110009]
|
actin body [GO:0099079]; actin cortical patch [GO:0030479]; actin filament [GO:0005884]; actin filament bundle [GO:0032432]; cell division site [GO:0032153]; cytoplasm [GO:0005737]; medial cortex [GO:0031097]; mitotic actomyosin contractile ring, distal actin filament layer [GO:0120106]
|
actin filament binding [GO:0051015]; calcium ion binding [GO:0005509]
|
PF00307;
|
1.10.418.10;1.10.238.10;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch {ECO:0000269|PubMed:11294907}. Note=Localizes both to the cortical actin patches and to the medial ring in an F-actin-dependent manner.
| null | null | null | null | null |
FUNCTION: Binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Plays a role in cytokinesis. Plays important roles in mating and in spore formation. {ECO:0000269|PubMed:11294907, ECO:0000269|PubMed:11694585}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O59954
|
UBA4_EMENI
|
MEDLETRCASLRTEIAAAEAQLTKLKRELHEAEGAALRAQSQKTASANATTGQRTKSKWPLHGEEYRRYGRQMIVPQFGLQGQLKLRDAKVLIVGAGGLGCPAALYLAGAGVGTIGLVDGDTVEASNLHRQVLHRSRNVGKLKVDSAIEYLRELNPHPTYIAHQAHLTPREAPDIFKDYDLILDCTDNPATRYLISDTAVLLGKPLVSASALRTEGQLMVLNNPPQPPGDKTGGPCYRCVFPKPPPANSVTSCADGGILGPVVGTMGVLQASEAIKVLTSAGESVEATPPSLLIFSAYSSPQFRTIKLRSRRPNCAVCSAEATVTLESVRSGSMDYVFFCGTVDPADILSPEERISPSEYGNVDSAGAQRHIIDVREKVQFDICSLENSINIPMSTILASAYSAPTLDADEPKRLPSWLPPEVAHESNKPIYVVCRQGNDSQTVVRKLKELGLDHGGERPVVDIKGGFRSWREQVDPDWPDY
|
2.7.7.80; 2.8.1.11
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_03049}; Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03049};
|
Mo-molybdopterin cofactor biosynthetic process [GO:0006777]; protein urmylation [GO:0032447]; tRNA wobble position uridine thiolation [GO:0002143]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]
|
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; molybdopterin-synthase adenylyltransferase activity [GO:0061605]; molybdopterin-synthase sulfurtransferase activity [GO:0061604]; nucleotidyltransferase activity [GO:0016779]; sulfotransferase activity [GO:0008146]; thiosulfate sulfurtransferase activity [GO:0004792]; URM1 activating enzyme activity [GO:0042292]
|
PF00581;PF00899;
|
3.40.50.720;3.40.250.10;
|
HesA/MoeB/ThiF family, UBA4 subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03049}.
|
CATALYTIC ACTIVITY: Reaction=[molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly + ATP + H(+) = [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly-AMP + diphosphate; Xref=Rhea:RHEA:43616, Rhea:RHEA-COMP:12159, Rhea:RHEA-COMP:12202, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:90618, ChEBI:CHEBI:90778; EC=2.7.7.80; Evidence={ECO:0000255|HAMAP-Rule:MF_03049}; CATALYTIC ACTIVITY: Reaction=[molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly-AMP + AH2 + S-sulfanyl-L-cysteinyl-[cysteine desulfurase] = [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-NH-CH2-C(O)SH + A + AMP + H(+) + L-cysteinyl-[cysteine desulfurase]; Xref=Rhea:RHEA:48612, Rhea:RHEA-COMP:12157, Rhea:RHEA-COMP:12158, Rhea:RHEA-COMP:12159, Rhea:RHEA-COMP:12160, ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:17499, ChEBI:CHEBI:29950, ChEBI:CHEBI:61963, ChEBI:CHEBI:90618, ChEBI:CHEBI:90619, ChEBI:CHEBI:456215; EC=2.8.1.11; Evidence={ECO:0000255|HAMAP-Rule:MF_03049};
| null |
PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03049}.; PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03049}.
| null | null |
FUNCTION: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers urm1 and mocs2a. Its N-terminus first activates urm1 and mocs2a as acyl-adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to urm1 and mocs2a to form thiocarboxylation (-COSH) of their C-terminus. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as a nucleophile towards urm1 and mocs2a. Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor; nfs1 probably acting as a sulfur donor for thiocarboxylation reactions (By similarity). {ECO:0000250, ECO:0000269|PubMed:9614089}.
|
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
|
O60016
|
CLR4_SCHPO
|
MSPKQEEYEVERIVDEKLDRNGAVKLYRIRWLNYSSRSDTWEPPENLSGCSAVLAEWKRRKRRLKGSNSDSDSPHHASNPHPNSRQKHQHQTSKSVPRSQRFSRELNVKKENKKVFSSQTTKRQSRKQSTALTTNDTSIILDDSLHTNSKKLGKTRNEVKEESQKRELVSNSIKEATSPKTSSILTKPRNPSKLDSYTHLSFYEKRELFRKKLREIEGPEVTLVNEVDDEPCPSLDFQFISQYRLTQGVIPPDPNFQSGCNCSSLGGCDLNNPSRCECLDDLDEPTHFAYDAQGRVRADTGAVIYECNSFCSCSMECPNRVVQRGRTLPLEIFKTKEKGWGVRSLRFAPAGTFITCYLGEVITSAEAAKRDKNYDDDGITYLFDLDMFDDASEYTVDAQNYGDVSRFFNHSCSPNIAIYSAVRNHGFRTIYDLAFFAIKDIQPLEELTFDYAGAKDFSPVQSQKSQQNRISKLRRQCKCGSANCRGWLFG
|
2.1.1.355; 2.1.1.366; 2.1.1.367
| null |
methylation [GO:0032259]; nuclear polyadenylation-dependent antisense transcript catabolic process [GO:0071040]; pericentric heterochromatin formation [GO:0031508]; positive regulation of pericentric heterochromatin formation [GO:0090053]; silent mating-type cassette heterochromatin formation [GO:0030466]; siRNA-mediated pericentric heterochromatin formation [GO:0140727]
|
chromosome, subtelomeric region [GO:0099115]; CLRC complex [GO:0043494]; cytoplasm [GO:0005737]; mating-type region heterochromatin [GO:0031934]; nucleus [GO:0005634]; pericentric heterochromatin [GO:0005721]; spindle pole body [GO:0005816]
|
double-stranded DNA binding [GO:0003690]; histone H3K9 methyltransferase activity [GO:0046974]; histone H3K9 monomethyltransferase activity [GO:0140948]; histone H3K9 trimethyltransferase activity [GO:0140949]; histone H3K9me2 methyltransferase activity [GO:0140947]; histone methyltransferase activity [GO:0042054]; histone reader activity [GO:0140566]; methyltransferase activity [GO:0008168]; protein-lysine N-methyltransferase activity [GO:0016279]; single-stranded DNA binding [GO:0003697]; single-stranded RNA binding [GO:0003727]; ubiquitin binding [GO:0043130]; ubiquitin modification-dependent histone binding [GO:0061649]; zinc ion binding [GO:0008270]
|
PF00385;PF05033;PF00856;
|
2.40.50.40;2.170.270.10;
|
Class V-like SAM-binding methyltransferase superfamily, Histone-lysine methyltransferase family, Suvar3-9 subfamily
|
PTM: Autocatalytic methylation of specific lysine residues in an internal loop (autoregulatory loop) promote a conformational switch that enhances the H3K9me activity of clr4. {ECO:0000269|PubMed:30051891}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:18345014}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:16823372}. Chromosome {ECO:0000269|PubMed:18345014, ECO:0000305|PubMed:16823372}.
|
CATALYTIC ACTIVITY: Reaction=L-lysyl(9)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(9)-[histone H3] + 3 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60276, Rhea:RHEA-COMP:15538, Rhea:RHEA-COMP:15546, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.355; Evidence={ECO:0000269|PubMed:11283354}; CATALYTIC ACTIVITY: Reaction=N(6)-methyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-methionine = H(+) + N(6),N(6)-dimethyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60284, Rhea:RHEA-COMP:15541, Rhea:RHEA-COMP:15542, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61929, ChEBI:CHEBI:61976; Evidence={ECO:0000269|PubMed:11283354, ECO:0000269|PubMed:30051891}; CATALYTIC ACTIVITY: Reaction=N(6),N(6)-dimethyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-methionine = H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60288, Rhea:RHEA-COMP:15538, Rhea:RHEA-COMP:15541, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961, ChEBI:CHEBI:61976; EC=2.1.1.366; Evidence={ECO:0000269|PubMed:30051891}; CATALYTIC ACTIVITY: Reaction=L-lysyl-[protein] + S-adenosyl-L-methionine = H(+) + N(6)-methyl-L-lysyl-[protein] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:51736, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:13053, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; Evidence={ECO:0000269|PubMed:28143796}; CATALYTIC ACTIVITY: Reaction=N(6)-methyl-L-lysyl-[protein] + S-adenosyl-L-methionine = H(+) + N(6),N(6)-dimethyl-L-lysyl-[protein] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:54196, Rhea:RHEA-COMP:13053, Rhea:RHEA-COMP:13827, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61929, ChEBI:CHEBI:61976; Evidence={ECO:0000269|PubMed:28143796}; CATALYTIC ACTIVITY: Reaction=N(6),N(6)-dimethyl-L-lysyl-[protein] + S-adenosyl-L-methionine = H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:54200, Rhea:RHEA-COMP:13826, Rhea:RHEA-COMP:13827, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961, ChEBI:CHEBI:61976; Evidence={ECO:0000269|PubMed:28143796}; CATALYTIC ACTIVITY: Reaction=L-lysyl(9)-[histone H3] + S-adenosyl-L-methionine = H(+) + N(6)-methyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60280, Rhea:RHEA-COMP:15542, Rhea:RHEA-COMP:15546, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.367; Evidence={ECO:0000269|PubMed:10949293, ECO:0000269|PubMed:11283354};
| null | null | null | null |
FUNCTION: Histone methyltransferase which contributes to the establishment of heterochromatin by specifically methylating histone H3 to form H3K9me (PubMed:16024659, PubMed:8138176). Part of the Clr4 methyltransferase complex (ClrC). ClrC preferentially ubiquitylates H3K14 and ClrC-mediated H3 ubiquitination promotes clr4 methyltransferase activity (PubMed:31468675). Clr4 functions as a reader and writer of H3K9 methylation. It sets the H3K9me mark and afterwards this H3K9me mark is recognized by the chromodomains of clr4 and swi6/HP1, which then recruit additional clr4 leading to the methylation of neighboring nucleosomes (PubMed:11242054, PubMed:18345014, PubMed:21224386). H3K9me represents a specific tag for epigenetic transcriptional repression by recruiting swi6/HP1 to methylated histones which leads to transcriptional silencing within centromeric heterochromatin, telomeres, ribosomal DNA repeats, and the silent mating-type region (PubMed:16024659, PubMed:8138176). Clr4 methyltransferase activity promotes the assembly of a tripartite complex composed of ClrC and complexes involved in siRNA generation (PubMed:20705239). Apart from H3K9, methylates also non-histone proteins such as mlo3 (PubMed:21436456, PubMed:28143796). Interacts with mlo3 to promote the processing of centromeric and antisense RNAs (PubMed:21436456). {ECO:0000269|PubMed:11242054, ECO:0000269|PubMed:16024659, ECO:0000269|PubMed:18345014, ECO:0000269|PubMed:20705239, ECO:0000269|PubMed:21224386, ECO:0000269|PubMed:21436456, ECO:0000269|PubMed:28143796, ECO:0000269|PubMed:31468675, ECO:0000269|PubMed:8138176}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O60020
|
ASPR1_PHARH
|
MISDTVIAILAVALVGSTVQAAPVDATATSTSGIIAVPISKSAAQLAREADPVVSLDWLKKTKAQAQYKHKQANARLHSKRATGASVLTDQGSESLWTGPITIGGQSFTVDWDTGSSDLWVPSSACSSAACNAHHKYTLTSTGKKQSGTFSISYGDGSSASGPVYKDNVVASGLQATSQVFGAVTSESSSFSSDPSDGISGLGWPALAQLSGTSYFWSLINQGTVTSPVFSFRLATTNSELYLGGINSAHYTGAITYTPVTQKAYWTIALGGVSVNGAAINPSVSSAIIDTGTTLVYGPTAGVAALYAKIPGSASMADTYGSDYQGYYTFPCSAVPTVALTFGGSSFSVPTSAFNLGTVSSGSKQCVGGIVGQGDGSWLVGDVFLQGVYSIYDVGNARVGFAKTV
|
3.4.23.-
| null |
proteolysis [GO:0006508]; proteolysis involved in protein catabolic process [GO:0051603]
|
extracellular region [GO:0005576]; fungal-type vacuole [GO:0000324]
|
aspartic-type endopeptidase activity [GO:0004190]
|
PF00026;
|
2.40.70.10;
|
Peptidase A1 family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10091328}.
| null | null | null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4-6. {ECO:0000269|PubMed:10091328};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is approximately 40 degrees Celsius. {ECO:0000269|PubMed:10091328};
|
FUNCTION: Possesses acidic protease activity. Hydrolyzes casein and azoalbumin in vitro. {ECO:0000269|PubMed:10091328}.
|
Phaffia rhodozyma (Yeast) (Xanthophyllomyces dendrorhous)
|
O60052
|
FNTA_SCHPO
|
MDPIDPELNEILDFTEYGPLTPIPQDDGENPLAKICYTTGYEQGMAYFRAIMAKKEYSLRALNLTGFLIMNNPAHYTVWAYRFQILNHTPSYIDNELEWLDEIAEDFQKNYQVWHHRQKILSLTKNYERELEFTKKMFEIDSKNYHVWSYRVWILQNFNDYSQELKLTNELLEKDIYNNSAWNHRFYVLFETSKVVSWSLEEELNYLKDKILFAPDNQSAWNYLCGVLDKSGPSKLDNLIANLRKNLPALHKPLLEFLAMYEPSSSEEIYQKLANEVDVPHAALWTWMSQRSNP
|
2.5.1.58; 2.5.1.59
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P29703};
|
protein farnesylation [GO:0018343]; protein geranylgeranylation [GO:0018344]; protein localization to plasma membrane [GO:0072659]
|
CAAX-protein geranylgeranyltransferase complex [GO:0005953]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; protein farnesyltransferase complex [GO:0005965]
|
CAAX-protein geranylgeranyltransferase activity [GO:0004662]; protein farnesyltransferase activity [GO:0004660]; Rab geranylgeranyltransferase activity [GO:0004663]
|
PF01239;
|
1.25.40.120;
|
Protein prenyltransferase subunit alpha family
| null | null |
CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate + L-cysteinyl-[protein] = diphosphate + S-(2E,6E)-farnesyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:13345, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11535, ChEBI:CHEBI:29950, ChEBI:CHEBI:33019, ChEBI:CHEBI:86019, ChEBI:CHEBI:175763; EC=2.5.1.58; Evidence={ECO:0000269|PubMed:10617635}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13346; Evidence={ECO:0000269|PubMed:10617635}; CATALYTIC ACTIVITY: Reaction=geranylgeranyl diphosphate + L-cysteinyl-[protein] = diphosphate + S-geranylgeranyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:21240, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11537, ChEBI:CHEBI:29950, ChEBI:CHEBI:33019, ChEBI:CHEBI:57533, ChEBI:CHEBI:86021; EC=2.5.1.59; Evidence={ECO:0000269|PubMed:9781874}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21241; Evidence={ECO:0000269|PubMed:9781874};
| null | null | null | null |
FUNCTION: Catalyzes the transfer of a farnesyl or geranyl-geranyl moiety from farnesyl or geranyl-geranyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. The alpha(cwp1) subunit is thought to participate in a stable complex with the substrate. The beta(cpp1 or cwg2) subunits bind the peptide substrate. {ECO:0000269|PubMed:10617635, ECO:0000269|PubMed:9781874}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O60060
|
CARA_SCHPO
|
MLRFLKPFPLRFGKRFYSKVPPVTNHERILPKQPSFPTAPAQNEIATLTIRNGPIFHGTSFGANRNVSGEAVFTTSPVGYVESLTDPSYKQQILIFTQPLIGNYGVPDCKKRDENGLLRHFESPHIQCAGVVVNDYATKYSHWTAVESLGEWCAREGVAAITGVDTRAIVTFLREQGSSLAKISIGEEYDANDDEAFINPEEVNLVSQVSTREPFFVSGGDGMLNIAVIDCGVKENILRSLVSRGASVTVFPFDYPIQNVASNYDGIFLTNGPGDPTHLTKTVNNLRELMNTYNGPIMGICMGHQLLALSTGAKTIKLKYGNRGHNIPALDIASGNCHITSQNHGYAVDASTLPAEWKATWTNLNDQSNEGIAHVSRPISSVQFHPEARGGPMDTFYLFDNYIKEAIKYQKSRTA
|
6.3.5.5
| null |
'de novo' pyrimidine nucleobase biosynthetic process [GO:0006207]; arginine biosynthetic process [GO:0006526]; glutamine metabolic process [GO:0006541]; urea cycle [GO:0000050]
|
carbamoyl-phosphate synthase complex [GO:0005951]; cytoplasm [GO:0005737]; mitochondrion [GO:0005739]
|
ATP binding [GO:0005524]; carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity [GO:0004088]; glutaminase activity [GO:0004359]
|
PF00988;PF00117;
|
3.40.50.880;3.50.30.20;
|
CarA family
| null |
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:200419}. Cytoplasm {ECO:0000269|PubMed:16823372}.
|
CATALYTIC ACTIVITY: Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate; Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.5.5; Evidence={ECO:0000250|UniProtKB:P22572}; CATALYTIC ACTIVITY: [Carbamoyl phosphate synthase arginine-specific small chain]: Reaction=H2O + L-glutamine = L-glutamate + NH4(+); Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; Evidence={ECO:0000250|UniProtKB:P22572};
| null |
PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1. {ECO:0000305|Ref.3}.
| null | null |
FUNCTION: Small subunit of the arginine-specific carbamoyl phosphate synthase (CPSase). CPSase catalyzes the formation of carbamoyl phosphate from the ammonia moiety of glutamine, carbonate, and phosphate donated by ATP, the first step of the arginine biosynthetic pathway (Ref.3). The small subunit (glutamine amidotransferase) binds and cleaves glutamine to supply the large subunit with the substrate ammonia (By similarity). {ECO:0000250|UniProtKB:P22572, ECO:0000269|Ref.3}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O60070
|
ASH2_SCHPO
|
MLAHGSNDYGVSLKGNKTGSSPSKASSLNWNEPHTLNEQNTYCYCGKDRNLRFPDLQCSVCLNMFHLSCLSPPCTSMMGFSTNYQFVCKHCTEDGFERFERGVSAWKAITATAMANLVVKRYVETNPDVPVDSFNAEKMRNFQANTYFFKKKEDLIPFIEEHWQLLCPDREKVQTWQATLGSCLVANRDTYRAKDETMRNQNSEYALNNPNLFDFRSGYIFPFQRVGATVPKKRLVETETPPPSSSKLKEDYKDSKREMKRSNTPWSNASIKKNEVPTVPIRYKPPPWRDSDFETVPKLPIFYPNSSSPNFFSLSEIPFNRRGFRYSPCEAAKDLPNVMYREIELPPFTSRINWHDISTPVFIDHSALCATVEKGFRMARSNVFMTSGEWYFEIKIEKGGGDDGAHVRIGVSRREAPLDAPVGYDAYSYGLRDLGGQKVHMSRPRNFMDSFGTGDIIGLHISLPKPSFAQHTTLPSCHDRIPIRYKGQLYFEQPDYVPSKMMDELMIPSKHNRYIDLPYIPGSFIKVYKNGSYMGTAFENLLDFNPPNSINSNHYSFDDGSLGYYPSISMYGGGIARFQFGPQFSHRPLVLGSNVRPVSERYNEQIAEDVLCDILDEIDYAEDPNTSSVTIDVPQEPNAGITIIPEIKDITE
| null | null |
negative regulation of gene expression, epigenetic [GO:0045814]; transcription initiation-coupled chromatin remodeling [GO:0045815]
|
chromatin [GO:0000785]; Lid2 complex [GO:0048189]; nucleus [GO:0005634]; Set1C/COMPASS complex [GO:0048188]
|
metal ion binding [GO:0046872]; transcription cis-regulatory region binding [GO:0000976]
|
PF21198;PF00622;
|
2.60.120.920;3.90.980.20;
|
CclA family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:25252312}.
| null | null | null | null | null |
FUNCTION: Component of the COMPASS (Set1C) complex that specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation (PubMed:12488447, PubMed:25252312). Regulates MAPK pathway and sporulation through H3K4 methylation (PubMed:25252312). {ECO:0000269|PubMed:12488447, ECO:0000269|PubMed:25252312}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O60094
|
DPO5_SCHPO
|
MATKTQLELFTKLTSNDKAIRLSSAAQLIDSLSNEEELKYSLNRLTKGLSSGRESARIGFAVALTELLTRTKDIRATHVLDLLVKHNTASGNLKGQDERDFYFGLLFGLQSIVYSGILTHKESTIEDFQRVVDLLLQLSGKKNWLQDVCFYVIYKLVEQIPEISFSSNAFLAVNKLLQTPAVSKSTEGVGLFLCLTRVPDNVKSEEVAMANWEPAHPLHKSNLVTLSKIMRQADASETGGQNSAWKQKIPMVWKYIFEEYQRKTYSGLAPFHDFWAVVVDEGIFSSTSSLERKFWGFQIMELALDYVSSDNIGDIFSKNFLHCLINHLSDEDRYLYRAAKRVTSKLEKVSKQNPTLVYPIAIHLLGERGSLNFDRVTNTKLVEHILPLADEQGILQLFQLLLSYVKRCPEDIASDTKAVEWRRQWATDTMLSILRSKRSIKQEPWVRELLEIFIAYGYFEVPESEEVIPKFSEGTQNMFRLRLMSALSYLSSSAFQQSQTDHQLGDKNWPYVALNYLLELEKSPKNNLLISMDESVIEIVQKSLSVLHKVTKKIDKKAQHLQQLNAFQLLYSLVLLQVYAGDTDSIDVLEDIDNCYSKVFNKKSKRESTSNEPTAMEILTEVMLSLLSRPSLLLRKLVDMLFTSFSEDMNRESIHLICDVLKAKESVKDSEGMFAGEEVEEDAFGETEMDEDDFEEIDTDEIEEQSDWEMISNQDASDNEELERKLDKVLEDADAKVKDEESSEEELMNDEQMLALDEKLAEVFRERKKASNKEKKKNAQETKQQIVQFKVKVIDLIDNYYKTQPNNGLGFEFLIPLLEMILKTKHKVLEEKGQAVFRNRLSKLKWTEEKPSSKNVLEALKKVHVLCGKKASLGSTGSSISQLLLKLLADTPYLKEGVEVYLKSFLLWIQEPSKSHYNANIFHDFINWGAQQRLKHQQTSTAASSPQKTGHHENEKTNH
| null | null |
rRNA processing [GO:0006364]; rRNA transcription [GO:0009303]
|
cytosol [GO:0005829]; nucleolus [GO:0005730]; nucleus [GO:0005634]
|
nucleotide binding [GO:0000166]; rDNA binding [GO:0000182]; RNA binding [GO:0003723]; RNA polymerase I transcription regulatory region sequence-specific DNA binding [GO:0001163]; transcription corepressor activity [GO:0003714]
|
PF04931;
| null |
MYBBP1A family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16816948}.
| null | null | null | null | null |
FUNCTION: Plays an important role in the regulation of rRNA transcription. Binds to rDNA promoter fragments. {ECO:0000269|PubMed:16816948}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O60119
|
SCS2_SCHPO
|
MSVECSGELFFYPPFTTMSKELISVHNPNPEPVIFKVKTTAPKHYCVRPNSGKIEPKSTVNVQVLLQAMKEEPAPDFKCRDKFLIQSMAIGDADTSNVENYHEFWTEMEKQGRSIFDRKIRCVYSTKQPPQSADKQVENTSTSNPPVSVEGSENLASSVGGPTAVGVSLDEAQNDFNGAKDHLSNGVNTVVPDSTFRSTFESAQIPDASVVQTVVTDADNGAASVKDTIVTAESASSKGADVARSKVQDIIDNEIPKPSESPRRSVSSTPPVHPPPPVPQNLSAVNEEFDTKKNDFDSKLPESTPAVEKVSENLGSETRESLQGAKPAAGAHSSDNALEQIKPSYSADPSSSTGASLTESPGIPPNIVIILCLIFFLIGYLFF
| null | null |
endoplasmic reticulum membrane organization [GO:0090158]; endoplasmic reticulum-plasma membrane tethering [GO:0061817]; establishment or maintenance of cell polarity [GO:0007163]; maintenance of ER location [GO:0051685]; reticulophagy [GO:0061709]
|
cortical endoplasmic reticulum [GO:0032541]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum-plasma membrane contact site [GO:0140268]; plasma membrane [GO:0005886]
|
FFAT motif binding [GO:0033149]; protein-membrane adaptor activity [GO:0043495]
|
PF00635;
|
2.60.40.10;
|
VAMP-associated protein (VAP) (TC 9.B.17) family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:23041194}; Single-pass type IV membrane protein {ECO:0000255}. Note=Localizes at the cortical endoplasmic reticulum-plasma membrane contact sites. {ECO:0000269|PubMed:23041194}.
| null | null | null | null | null |
FUNCTION: Vesicle-associated membrane protein-associated protein (VAP) implicated in maintaining the cortical endoplasmic reticulum (ER)-plasma membrane (PM) attachment (PubMed:23041194, PubMed:26877082, PubMed:29290560, PubMed:32023460). ER-PM contacts function to modulate the distribution of contractile ring components to ensure robust ring assembly (PubMed:26877082). ER-PM contacts function also in controlling exocytosis and maintenance of cell polarity regulating cell shape (PubMed:29290560). VAPs play an important role in regulating eisosome assembly (PubMed:32023460). VAPs also contribute to ER-phagy by tethering atg8 to the ER membrane, but also by maintaining the ER-plasma membrane contact (Ref.8). {ECO:0000269|PubMed:23041194, ECO:0000269|PubMed:26877082, ECO:0000269|PubMed:29290560, ECO:0000269|PubMed:32023460, ECO:0000269|Ref.8}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O60126
|
TOP3_SCHPO
|
MRVLCVAEKNSIAKSVASILGGGHVRRRDTRSKYVKNYDFSFNFGGNVGSSDVTMTSVSGHLTEASFPSEYSSWSSVPQDVLFDAQIITSVSKNAEVLADNIKKEARNAQYLYIWTDCDREGEHIGVEISNVARASNPSIQVIRADFNNLERSHIISAAKRPRDVSKNAADAVDARIELDFRLGAIFTRLQTIQLQKSFDILQNKIISYGPCQFPTLGFVVDRWQRVEDFVPETYWHLRFVDKRQGKTIQFNWERAKVFDRLTTMIILENCLECKTAKVVNITQKPKTKYKPLPLSTVELTKLGPKHLRISAKKTLELAENLYTNGFVSYPRTETDQFDSSMNLHAIIQKLTGAQEWDSYAEGLLAGDYRPPRKGKHNDRAHPPIHPVQMVHRSALPSQDHWKVYELITRRFLACCSDNAKGAETLVQVKMEEELFSKKGLLVTEKNYLEVYPYEKWESSDQLPEYRLHEEFQPHILDMMDSSTSSPSYITEPELIALMDANGIGTDATMAEHIEKVQEREYVIKRKKRGQGVTEFVPSSLGVALAKGYDEIGLEWSLTKPFLRKEMEVQLKNIENGQLNRNVLVHMILTQFRDVFHLTKQRFDCLKNSCRVYLMSHNEPQT
|
5.6.2.1
| null |
DNA recombination [GO:0006310]; DNA repair [GO:0006281]; DNA topological change [GO:0006265]; maintenance of rDNA [GO:0043007]; mitotic DNA replication [GO:1902969]; postreplication repair [GO:0006301]; resolution of meiotic recombination intermediates [GO:0000712]
|
nucleus [GO:0005634]; RecQ family helicase-topoisomerase III complex [GO:0031422]; site of double-strand break [GO:0035861]
|
DNA binding [GO:0003677]; DNA topoisomerase type I (single strand cut, ATP-independent) activity [GO:0003917]
|
PF01131;PF01751;
|
3.40.50.140;1.10.460.10;2.70.20.10;1.10.290.10;
|
Type IA topoisomerase family
| null | null |
CATALYTIC ACTIVITY: Reaction=ATP-independent breakage of single-stranded DNA, followed by passage and rejoining.; EC=5.6.2.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10131};
| null | null | null | null |
FUNCTION: Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand than undergoes passage around the unbroken strand thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone (By similarity). {ECO:0000250}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O60129
|
FKH2_SCHPO
|
MTVRRLESKSEHISDDEERKEQLDYKKQMDVDTDRNIVLNGRLESQIAKLSVPPHEMRVVDDYSNSKNAERHSGEIQAYAKFAGSTWTYYVKKIRIILGREPANPSPKGKNEDLEVIDMNFGPSKVVSRKHAVVEYDLDDQTWNCSVYGRNGIKVDGKLFKNGETVKLTSGSILEVAGLQMMFVLPNAAEQKQTDESTIKEDAIKSEISAAVNDAAEYGDNKKPPYSYSVMIAQAILSSSECMMTLSNIYSWISTHYPYYRTTKSGWQNSIRHNLSLNKAFRKVPRKSGEQGKGMKWSIVPEFREEFIAKTRKTPRKRSPSSPVPLLAKKREGSPSLPIPILPKMKDTSIPAAEPASSTTSARDQTPSTPKDVGSPSTAETSAEEKQMETYKTPTHAALSDIISTHDYALDANSASQTKKAAFGSPIGSSTYPTSSPAPFWKYVAVPNPHDWPQVGSYDTISPYRNPVNSHLIYSQIQQSSPKKIDEQLHDLQGVDLVNGFEGISSWRESMVNKLRSSVSDSPTMNLANSNSKSSPVAVQRVSTLPQASANKQAKEMESKMSNSPTQKSKTEENNQAVRAILDASATMEKQYDLHRLPTPTSQTESASVPQIANPPNSQNLVKEKSPQQYIQVPQSNVKSSA
| null | null |
division septum assembly [GO:0000917]; negative regulation of cell cycle switching, mitotic to meiotic cell cycle [GO:0110045]; positive regulation of induction of conjugation with cellular fusion [GO:1900237]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]
|
chromatin [GO:0000785]; M/G1 phase-specific MADS box-forkhead transcription factor complex [GO:0097221]; nucleus [GO:0005634]
|
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF00498;PF00250;
|
2.60.200.20;1.10.10.10;
| null |
PTM: Phosphorylated. Occurs periodically during mitosis. {ECO:0000269|PubMed:15302827, ECO:0000269|PubMed:15509866, ECO:0000269|PubMed:18257517}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089, ECO:0000269|PubMed:15302827}.
| null | null | null | null | null |
FUNCTION: Required for promoter sequence element PCB-driven, M-phase-specific transcription. Acts as a transcriptional activator with a role in the regulation of mitosis. Binds, cooperatively with mcm1, the CLB cluster regulatory elements throughout the cell cycle. Regulates the periodic transcription of cdc15 and spo12. Required for the correct timing, positioning and contraction of the division septum. {ECO:0000269|PubMed:15302827, ECO:0000269|PubMed:15509866, ECO:0000269|PubMed:15777722}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O60132
|
TEA4_SCHPO
|
MLHMNSASSADSMEIMESHFDPTQQNDSTIIESRYSPEEYLEQSFEIQRIISGENSEPQTVASQEISDSQEEDTTLTSSQFEDCGTEYNEVVEDDEFRSEDEDDFMDEEEEYALYEAELSSSPSIHEEVIDCNFVHAIRGFEATVEGQVDATKGDMMILLDDSNSYWWLVKMCKNLAIGYLPAEYIETPSERLARLNKYKNSETSNSQQSVTLPPLDIVEKTLEAPSPNFRIKRVTFTCSSNSSDDEMDSENDYEAMVNRTVAENGLEIEFSDSSDSSLSAEYRSESEDHVTDSPAYVDLTELEGGFNQFNSTSFQSTSPLGLEIVETEINGSSTTADSKNSHSPYSKFSSAYPDAENSNISKINISIAGNKELYGNATQSDPSLYSTWIANKHKTASSATVDSPLRRSLSVDAMQSNASFSSYSSTSNTDKSLRPSSYSAVSESSNFTHDVSRDNKEISLNAPKSIIVSQSDSFDTSNVTQDAPNDVEKEPISGQMPNNLSVQSLKQLEVYPIRHSVSIEMPSEKLLSPRLYSSSTPSSPTKGFQKDDEEDSENRKQADKVELSPSSLLRQMSLPVDSSSQSDAQCTTSSVYITAERKAFSQSSIDLSTLSNHHVNNEINRRSFAGGFTSLADELSEMRELLHESPAPLECNEEMVIPTPELDASSAIPSSSISHDEDLLPRKNTEESTSSSSFSSLITSPASLQYDENPFKQSVVAELNNNSSSVPFVDSAHASDIHAYDNDHVSTKNKEFNRRLREFILDPDSLSGLYWSVKSAGVRASRRVSRNIEGESVSSDLDDIFANVLKGLSDEMASLLNTNR
| null | null |
establishment of bipolar cell polarity [GO:0061171]; establishment of cell polarity [GO:0030010]; establishment or maintenance of actin cytoskeleton polarity [GO:0030950]; establishment or maintenance of bipolar cell polarity [GO:0061245]; maintenance of protein location in cell cortex of cell tip [GO:0097248]; positive regulation of protein localization to plasma membrane [GO:1903078]
|
cell cortex of cell tip [GO:0051285]; cell division site [GO:0032153]; cell tip [GO:0051286]; lateral cell cortex [GO:0097575]; microtubule cytoskeleton [GO:0015630]; microtubule plus-end [GO:0035371]; non-growing cell tip [GO:0035839]; old growing cell tip [GO:0035840]
|
cytoskeletal anchor activity [GO:0008093]
|
PF00018;
|
2.30.30.40;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15809031, ECO:0000269|PubMed:15936270}. Note=Through it's binding with tea1, is transported by the cytoplasmic microtubule system and is localized at cell tips, microtubule plus ends and cytoplasmic dots.
| null | null | null | null | null |
FUNCTION: Cell polarity factor essential for the bipolar localization and function of structures containing the cell-end marker tea1 during the normal cell cycle. Regulates cell polarity in complex with tea1 and together with the stress signaling MAPK cascade, contributes to cell polarity maintenance under stress conditions. Required for the localization of for3 at the cell tip specifically during initiation of bipolar growth. During the new end take off (NETO), formation of a protein complex that includes tea1, tea4 and for3 is necessary and sufficient for the establishment of cell polarity and localized actin assembly at new cell ends. {ECO:0000269|PubMed:15809031, ECO:0000269|PubMed:15936270}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O60139
|
UBP4_SCHPO
|
MSDDYFDRLFELAFVYINEDETIQSCSFRGQRWLEEAQTLEQKNSLLKAYYYYLKALKLAYEIPCRFEISVKSTHYGEFKQFQKLAIQAVSKAFTIKSKLAVKHYLPVIQISDALSLSKKSSLKVLFLNFYSQESSKGYVFSKHTIAIPISCLQSMDSSKIYDFLKSAPFHPSMVICYSLERYFEDVSLAYKLYSMLRSLKLDPHFMELANPKKVDSSLSYENYQPIGLTNLGNTCYMNCVLQCLFACKDLTIPMLQGRGLLQNINTKNPLGTGGKITSAFFSLLQSVLLNHGQRSISPRNFLEIVQSLNRDFSIDGQCDAQEFLNFFLDKLHEDLNSNASRSPIAPLTEDQLSAREELPLSHFSHIEWNLHLRSNKSIVVNNFVGQLCSRTQCMTCGRTSTTFAPFTSLAIPIDDVSHVVSLQECLLKFSAPELLQGHDGWHCPVCKVQRSAKKVIMISKLPEYLIIQIQRFKISVMGRKKIDTPLGLSLQIPSKMLVPPSFQSGIGYIPSNYNLFAFICHYGQLENGHYISDVLFNNEWCHIDDSIVRTVGGITDLREDFSSSYILFYKRSSLLEEFEDKCPKMTLKRNVK
|
3.4.19.12
| null |
endosome organization [GO:0007032]; proteolysis [GO:0006508]; Ras protein signal transduction [GO:0007265]
|
cell division site [GO:0032153]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endosome [GO:0005768]; extrinsic component of plasma membrane [GO:0019897]; midbody [GO:0030496]
|
cysteine-type deubiquitinase activity [GO:0004843]; metal-dependent deubiquitinase activity [GO:0140492]
|
PF00443;
|
3.90.70.10;
|
Peptidase C19 family
| null |
SUBCELLULAR LOCATION: Cytoplasm. Endosome.
|
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;
| null | null | null | null |
FUNCTION: Has an ATP-independent isopeptidase activity, cleaving at the C-terminus of the ubiquitin moiety. Acts late in the proteolytic pathway in conjunction with the 26S proteasome. Plays a role in avoiding DNA overreplication (By similarity). {ECO:0000250}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O60158
|
BQT4_SCHPO
|
MTENEKSRSLPAERNPLYKDDTLDHTPLIPKCRAQVIEFPDGPATFVRLKCTNPESKVPHFLMRMAKDSSISATSMFRSAFPKATQEEEDLEMRWIRDNLNPIEDKRVAGLWVPPADALALAKDYSMTPFINALLEASSTPSTYATPSRPTAQKSETSEGEPESSTSATTTSVARRTRQRLAEHLENSKKTILQHDNKEEDKEIHSEENETKDEIKSEKKEPEIKKQEGGSSTEKVGQPSSSDDKAKGSTSKDQPSEEEEKTSDIQDRKIKTPIKPSLLGKIRSSVNKGMTDVASQVNRGMTDVASQVNKGVNGVASQVNKGMNGVANQVNKGVTGVASQVRKPVGKLEKKFENLEKSIGDTLKSSIRSSPKSKKRSREDFEENEDYNAMVPVKRSRITKLESEVYYEKRKVRALGGIAIGLGVGAILPFLF
| null | null |
cell division [GO:0051301]; meiotic attachment of telomere to nuclear envelope [GO:0070197]; meiotic telomere clustering [GO:0045141]; meiotic telomere tethering at nuclear periphery [GO:0044821]; mitotic telomere tethering at nuclear periphery [GO:0044820]; telomere maintenance [GO:0000723]; telomere organization [GO:0032200]
|
cytoplasm [GO:0005737]; membrane [GO:0016020]; nuclear envelope [GO:0005635]; nuclear inner membrane [GO:0005637]; nuclear membrane complex Bqt3-Bqt4 [GO:1990862]; nucleus [GO:0005634]
|
DNA binding [GO:0003677]; telomere-nuclear envelope anchor activity [GO:0140473]
| null |
1.20.120.20;3.10.260.10;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372}. Nucleus inner membrane {ECO:0000269|PubMed:19948484}; Peripheral membrane protein {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Connects telomeres to the nuclear envelop (NE) during both vegetative growth and meiosis. This connection ensures clustering of telomeres to the spindle pole body (SPB) when cells enter meiotic prophase. {ECO:0000269|PubMed:19948484}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O60165
|
SPN7_SCHPO
|
MNKGPRHRPKFLSKKGKKLRIMVAGSSYTSYQACINSLCSKQILEAETEIDPLKAHIDRILEIREFNADILEDEFHVDLTVIEVNGFGDKIDNSASFEVVTHYLESQFDQALIEESKIKRNSKFTDTRVDALLYFIAPRGHCLSEFDLEAMKRFSKRVNVIPVIGNSNAFTEEELKNFKDVIMKDLKQCNIKVFDFPWDPEEDEDEVIEDNKRLWESVPFAVSGGVSEEDEEGYQRIVKKFQWGTFVIDDPAHSDFLNLKTVLFISHLDILKSITKQTYYENYRTEKLSNDSPSNTSLSLQKQNSIVANEDKRSVNGSERTETRSSIDQSEMRTNVSDSTKSEELKKINSIKVDNTSSLKCDSYGNTKTKTNQLNCEQIGLEVISPKEFPHRTTSSRNSLPNNTTKELEMKKMDDLSHERYENLPFYR
| null | null |
cytoskeleton-dependent cytokinesis [GO:0061640]; spore membrane bending pathway [GO:0070583]
|
cell division site [GO:0032153]; cytosol [GO:0005829]; mating projection septin ring [GO:0032175]; meiotic septin complex [GO:0032152]; membrane [GO:0016020]; microtubule cytoskeleton [GO:0015630]; nucleus [GO:0005634]; prospore septin ring [GO:0032169]; septin complex [GO:0031105]; septin ring [GO:0005940]
|
GTP binding [GO:0005525]; GTPase activity [GO:0003924]; lipid binding [GO:0008289]; molecular adaptor activity [GO:0060090]
|
PF00735;
|
3.40.50.300;
|
TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily, Septin GTPase family
| null |
SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Forespore membrane; Peripheral membrane protein. Note=The sporulation-specific septin complex associates to the forespore membrane and forms partial or complete ring-like structures that curl around each haploid nucleus.
| null | null | null | null | null |
FUNCTION: Septin-like protein involved in the correct orientation of forespore membrane extension during sporulation. Binds phosphatidylinositol 4-phosphate. {ECO:0000269|PubMed:20123972}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O60182
|
RFC1_SCHPO
|
MSNSDIRSFFGGGNAQKKPKVSPTPTSPKPKRSLKKKRIVLSDDEDGTIENSKVPASKSKVQKRNESEDISHSLPSIVHEDDKLVGSDGVSTTPDEYFEQQSTRSRSKPRIISNKETTTSKDVVHPVKTENFANDLDTTSDSKPVVHQTRATRKPAQPKAEKSTTSKSKSHTTTATTHTSRSSKSKGLPRFSDEVSQALKNVPLIDVDSMGVMAPGTFYERAATTQTPGSKPVPEGNSDCLSGISFVITGILETLTRQEATDLIKQYGGKVTGAPSVRTDFILLGENAGPRKVETIKQHKIPAINEDGLFYLITHLPASGGTGAAAQAAQQKKEQEEKKILETVARMDDSNKKESQPSQIWTSKYAPTSLKDICGNKGVVQKLQKWLQDYHKNRKSNFNKPGPDGLGLYKAVLLSGPPGIGKTTAAHLVAKLEGYDVLELNASDTRSKRLLDEQLFGVTDSQSLAGYFGTKANPVDMAKSRLVLIMDEIDGMSSGDRGGVGQLNMIIKKSMIPIICICNDRAHPKLRPLDRTTFDLRFRRPDANSMRSRIMSIAYREGLKLSPQAVDQLVQGTQSDMRQIINLLSTYKLSCSEMTPQNSQAVIKNSEKHIVMKPWDICSRYLHGGMFHPSSKSTINDKLELYFNDHEFSYLMVQENYLNTTPDRIRQEPPKMSHLKHLELISSAANSFSDSDLVDSMIHGPQQHWSLMPTHALMSCVRPASFVAGSGSRQIRFTNWLGNNSKTNKLYRMLREIQVHMRLKVSANKLDLRQHYIPILYESLPVKLSTGHSDVVPEIIELMDEYYLNREDFDSITELVLPADAGEKLMKTIPTAAKSAFTRKYNSSSHPIAFFGSSDVLPMKGSAQREVPDVEDAIEAEDEMLEEASDSEAANEEDIDLSKDKFISVPKKPKKRTKAKAEASSSSSTSRRSRKKTA
| null | null |
cell division [GO:0051301]; DNA strand elongation involved in DNA replication [GO:0006271]; mitotic DNA replication leading strand elongation [GO:1903460]; UV-damage excision repair [GO:0070914]
|
chromatin [GO:0000785]; nuclear DNA replication factor C complex [GO:0043599]; nucleolus [GO:0005730]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA clamp loader activity [GO:0003689]; DNA clamp unloader activity [GO:0061860]
|
PF00004;PF00533;PF08519;
|
1.10.8.60;1.20.272.10;3.40.50.10190;3.40.50.300;
|
Activator 1 large subunit family
| null |
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:10759889}.
| null | null | null | null | null |
FUNCTION: The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins PCNA and activator 1. Subunit 1 is essential for cell cycle progression. It may associate with components of the DNA replication machinery and serve to enhance the efficiency of DNA replication. {ECO:0000269|PubMed:16040599}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O60184
|
CYC8_SCHPO
|
MPQSQVATASPSQNAQPNHGMGSKVLSSDPNASLPPQTAYYASPLHANSVSLPPSHLPRSTLHPLLSQQQQPAQQSPSLGPAQQNIQQPPSVSIASQPHYAEAIVPIQQVLQPQQYRQLPPNMVAATNAPQQHPQLQRMMPILSSNQPIQQLPLPNQASPYIPVPLQQQQQSQPQQQPQQQQHQQPQQPQPPQQPLQQQQQQRQLHSGIQQPVSTIVSQNGTYYSIPAVNHPMAGQPIAIAPVPAPNQAALPPIPPQALPANGTPNTLASPVTLPAANSAVQNAQPVPMTSSPAMAVVPQNKTAATSTLAAQQGANVLPPNAPESVRHLISLNEETWIQIGRLAELFDDQDKALSAYESALRQNPYSIPAMLQIATILRNREQFPLAIEYYQTILDCDPKQGEIWSALGHCYLMQDDLSRAYSAYRQALYHLKDPKDPKLWYGIGILYDRYGSHEHAEEAFMQCLRMDPNFEKVNEIYFRLGIIYKQQHKFAQSLELFRHILDNPPKPLTVLDIYFQIGHVYEQRKEYKLAKEAYERVLAETPNHAKVLQQLGWLCHQQSSSFTNQDLAIQYLTKSLEADDTDAQSWYLIGRCYVAQQKYNKAYEAYQQAVYRDGRNPTFWCSIGVLYYQINQYQDALDAYSRAIRLNPYISEVWYDLGTLYESCHNQISDALDAYQRAAELDPTNPHIKARLQLLRGPNNEQHKIVNAPPSNVPNVQTAKYINQPGVPYSNVPVAQLSGNWQPPHLPQAQLPSATGQSGVVQQPYQTQPSVTNNNVATQPVIASTVPVQTAAPSSQTAVPQTIHQSNAFTPRGKHASGSRNSISSTKSPQHKLSDQPRSRNNSISNVSHRERSNSVSSKSRETRTSASNESDPKKSTQRDSSKKLENSTVVSGSPSSSSKSDAAKSIKPQKPEPALKPVEGTADPKSTKRNHQETEKTADTDVSSTEPVKRQKTADVNDDVGEEEVKQSVSEQVDSAQLTSEPKSESLPKSPEEKSDDTSNDVTTENTNDINGDSNMDNVATVDKSTDAVDTSTATVAATTTTAEEELPQKESQERSSPSPENQDSTPLAPKSVSPKQAARTLDIDENYDDDEGEKETVSV
| null | null |
negative regulation of transcription by RNA polymerase II [GO:0000122]
|
chromatin [GO:0000785]; Cyc8(Ssn6)-Tup1 general repressor complex [GO:0160051]; cytoplasm [GO:0005737]; MLL3/4 complex [GO:0044666]; nucleus [GO:0005634]; transcription repressor complex [GO:0017053]
|
chromatin DNA binding [GO:0031490]; histone H3K27me2/H3K27me3 demethylase activity [GO:0071558]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; transcription corepressor activity [GO:0003714]
|
PF00515;PF13432;PF13181;
|
1.25.40.10;
|
CYC8/SSN6 family
| null |
SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Nuclear dots.
| null | null | null | null | null |
FUNCTION: Acts as a component of the ssn6-tup corepressor complexes, which are involved in the repression of many genes in a wide variety of physiological processes. May also be involved in the derepression of at least some target genes. The complex is recruited to target genes by interaction with DNA-bound transcriptional repressors. The complex recruits histone deacetylases to produce a repressive chromatin structure, interacts with hypoacetylated N-terminal tails of histones H3 and H4 that have been programmed for repression by the action of histone deacetylases and interferes directly with the transcriptional machinery by associating with the RNA polymerase II mediator complex (By similarity). {ECO:0000250, ECO:0000269|PubMed:15632072}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O60200
|
MDM35_YEAST
|
MGNIMSASFAPECTDLKTKYDSCFNEWYSEKFLKGKSVENECSKQWYAYTTCVNAALVKQGIKPALDEAREEAPFENGGKLKEVDK
| null | null |
mitochondrial respiratory chain complex assembly [GO:0033108]; mitochondrion organization [GO:0007005]; phospholipid translocation [GO:0045332]; phospholipid transport [GO:0015914]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrial intermembrane space [GO:0005758]; mitochondrion [GO:0005739]; nucleus [GO:0005634]
|
phosphatidic acid transfer activity [GO:1990050]
|
PF05254;
| null |
TRIAP1/MDM35 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}. Mitochondrion intermembrane space {ECO:0000269|PubMed:17095012, ECO:0000269|PubMed:20622808, ECO:0000269|PubMed:20657548, ECO:0000269|PubMed:22984289}.
| null | null | null | null | null |
FUNCTION: Involved in mitochondrial distribution and morphology. Mediates the import of UPS1, UPS2 and UPS3, 3 atypical mitochondrial intermembrane space (IMS) proteins lacking the two major IMS-targeting signals, into the intermembrane space. The UPS1:MDM35 complex mediates the transfer of phosphatidic acid (PA) between liposomes and probably functions as a PA transporter across the mitochondrion intermembrane space (PubMed:26071601, PubMed:26071602, PubMed:26235513). Phosphatidic acid import is required for cardiolipin (CL) synthesis in the mitochondrial inner membrane (PubMed:26071602). {ECO:0000269|PubMed:11907266, ECO:0000269|PubMed:20622808, ECO:0000269|PubMed:20657548, ECO:0000269|PubMed:26071601, ECO:0000269|PubMed:26071602, ECO:0000269|PubMed:26235513}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
O60216
|
RAD21_HUMAN
|
MFYAHFVLSKRGPLAKIWLAAHWDKKLTKAHVFECNLESSVESIISPKVKMALRTSGHLLLGVVRIYHRKAKYLLADCNEAFIKIKMAFRPGVVDLPEENREAAYNAITLPEEFHDFDQPLPDLDDIDVAQQFSLNQSRVEEITMREEVGNISILQENDFGDFGMDDREIMREGSAFEDDDMLVSTTTSNLLLESEQSTSNLNEKINHLEYEDQYKDDNFGEGNDGGILDDKLISNNDGGIFDDPPALSEAGVMLPEQPAHDDMDEDDNVSMGGPDSPDSVDPVEPMPTMTDQTTLVPNEEEAFALEPIDITVKETKAKRKRKLIVDSVKELDSKTIRAQLSDYSDIVTTLDLAPPTKKLMMWKETGGVEKLFSLPAQPLWNNRLLKLFTRCLTPLVPEDLRKRRKGGEADNLDEFLKEFENPEVPREDQQQQHQQRDVIDEPIIEEPSRLQESVMEASRTNIDESAMPPPPPQGVKRKAGQIDPEPVMPPQQVEQMEIPPVELPPEEPPNICQLIPELELLPEKEKEKEKEKEDDEEEEDEDASGGDQDQEERRWNKRTQQMLHGLQRALAKTGAESISLLELCRNTNRKQAAAKFYSFLVLKKQQAIELTQEEPYSDIIATPGPRFHII
| null | null |
apoptotic process [GO:0006915]; cell division [GO:0051301]; chromatin looping [GO:0140588]; chromosome segregation [GO:0007059]; DNA recombination [GO:0006310]; double-strand break repair [GO:0006302]; establishment of meiotic sister chromatid cohesion [GO:0034089]; establishment of mitotic sister chromatid cohesion [GO:0034087]; negative regulation of G2/M transition of mitotic cell cycle [GO:0010972]; negative regulation of glial cell apoptotic process [GO:0034351]; negative regulation of interleukin-1 beta production [GO:0032691]; negative regulation of mitotic metaphase/anaphase transition [GO:0045841]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of tumor necrosis factor production [GO:0032720]; positive regulation of interleukin-10 production [GO:0032733]; positive regulation of sister chromatid cohesion [GO:0045876]; protein localization to chromatin [GO:0071168]; reciprocal meiotic recombination [GO:0007131]; regulation of transcription by RNA polymerase II [GO:0006357]; replication-born double-strand break repair via sister chromatid exchange [GO:1990414]; response to hypoxia [GO:0001666]; sister chromatid cohesion [GO:0007062]
|
chromatin [GO:0000785]; chromosome [GO:0005694]; chromosome, centromeric region [GO:0000775]; cohesin complex [GO:0008278]; condensed nuclear chromosome [GO:0000794]; cytosol [GO:0005829]; meiotic cohesin complex [GO:0030893]; membrane [GO:0016020]; midbody [GO:0030496]; mitotic cohesin complex [GO:0030892]; nuclear matrix [GO:0016363]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spindle pole [GO:0000922]
|
chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-binding transcription factor binding [GO:0140297]; lncRNA binding [GO:0106222]
|
PF04824;PF04825;
|
1.10.10.580;
|
Rad21 family
|
PTM: Cleaved by separase/ESPL1 at the onset of anaphase; this cleavage is required for sister chromatid separation and cytokinesis (PubMed:11509732). Cleaved by caspase-3/CASP3 or caspase-7/CASP7 at the beginning of apoptosis (PubMed:11875078, PubMed:12417729). {ECO:0000269|PubMed:11509732, ECO:0000269|PubMed:11875078, ECO:0000269|PubMed:12417729}.; PTM: Phosphorylated; becomes hyperphosphorylated in M phase of cell cycle. The large dissociation of cohesin from chromosome arms during prophase may be partly due to its phosphorylation by PLK1. {ECO:0000269|PubMed:11073952}.
|
SUBCELLULAR LOCATION: [Double-strand-break repair protein rad21 homolog]: Nucleus {ECO:0000269|PubMed:11073952, ECO:0000269|PubMed:11509732, ECO:0000269|PubMed:12417729}. Nucleus matrix {ECO:0000269|PubMed:10623634, ECO:0000269|PubMed:11590136}. Chromosome {ECO:0000269|PubMed:11073952, ECO:0000269|PubMed:11590136}. Chromosome, centromere {ECO:0000269|PubMed:11073952}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:11073952, ECO:0000269|PubMed:11590136}. Note=Associates with chromatin (PubMed:11073952, PubMed:11590136). Before prophase, scattered along chromosome arms (PubMed:11073952). During prophase and prometaphase, most cohesins dissociate from the arms of condensing chromosome, possibly through PLK1-mediated phosphorylation (PubMed:11931760). A small amount of cohesin remains in centromeric regions and is removed from chromosomes only at the onset of anaphase. At anaphase, cleavage by separase/ESPL1 leads to the dissociation of cohesin from chromosomes and chromosome separation (PubMed:11073952, PubMed:11509732). {ECO:0000269|PubMed:11073952, ECO:0000269|PubMed:11509732, ECO:0000269|PubMed:11590136, ECO:0000269|PubMed:11931760}.; SUBCELLULAR LOCATION: [64-kDa C-terminal product]: Cytoplasm, cytosol {ECO:0000269|PubMed:11875078, ECO:0000269|PubMed:12417729}. Nucleus {ECO:0000269|PubMed:11875078, ECO:0000269|PubMed:12417729}.
| null | null | null | null | null |
FUNCTION: [Double-strand-break repair protein rad21 homolog]: As a member of the cohesin complex, involved in sister chromatid cohesion from the time of DNA replication in S phase to their segregation in mitosis, a function that is essential for proper chromosome segregation, post-replicative DNA repair, and the prevention of inappropriate recombination between repetitive regions (PubMed:11509732). The cohesin complex may also play a role in spindle pole assembly during mitosis (PubMed:11590136). In interphase, cohesins may function in the control of gene expression by binding to numerous sites within the genome (By similarity). May control RUNX1 gene expression (Probable). Binds to and represses APOB gene promoter (PubMed:25575569). May play a role in embryonic gut development, possibly through the regulation of enteric neuron development (By similarity). {ECO:0000250|UniProtKB:Q61550, ECO:0000250|UniProtKB:Q6TEL1, ECO:0000269|PubMed:11509732, ECO:0000269|PubMed:11590136, ECO:0000269|PubMed:25575569, ECO:0000305|PubMed:25575569}.; FUNCTION: [64-kDa C-terminal product]: May promote apoptosis. {ECO:0000269|PubMed:11875078, ECO:0000269|PubMed:12417729}.
|
Homo sapiens (Human)
|
O60218
|
AK1BA_HUMAN
|
MATFVELSTKAKMPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKIQEKAVKREDLFIVSKLWPTFFERPLVRKAFEKTLKDLKLSYLDVYLIHWPQGFKSGDDLFPKDDKGNAIGGKATFLDAWEAMEELVDEGLVKALGVSNFSHFQIEKLLNKPGLKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRPWAKPEDPSLLEDPKIKEIAAKHKKTAAQVLIRFHIQRNVIVIPKSVTPARIVENIQVFDFKLSDEEMATILSFNRNWRACNVLQSSHLEDYPFNAEY
|
1.1.1.300; 1.1.1.54
| null |
cellular detoxification of aldehyde [GO:0110095]; daunorubicin metabolic process [GO:0044597]; doxorubicin metabolic process [GO:0044598]; farnesol catabolic process [GO:0016488]; retinoid metabolic process [GO:0001523]
|
cytosol [GO:0005829]; extracellular region [GO:0005576]; lysosome [GO:0005764]; mitochondrion [GO:0005739]
|
alcohol dehydrogenase (NADP+) activity [GO:0008106]; alditol:NADP+ 1-oxidoreductase activity [GO:0004032]; aldo-keto reductase (NADP) activity [GO:0004033]; allyl-alcohol dehydrogenase activity [GO:0047655]; geranylgeranyl reductase activity [GO:0045550]; indanol dehydrogenase activity [GO:0047718]; NADP-retinol dehydrogenase activity [GO:0052650]; retinal dehydrogenase activity [GO:0001758]
|
PF00248;
|
3.20.20.100;
|
Aldo/keto reductase family
| null |
SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:21585341}. Secreted {ECO:0000269|PubMed:21585341}. Note=Secreted through a lysosome-mediated non-classical pathway.
|
CATALYTIC ACTIVITY: Reaction=all-trans-retinol + NADP(+) = all-trans-retinal + H(+) + NADPH; Xref=Rhea:RHEA:25033, ChEBI:CHEBI:15378, ChEBI:CHEBI:17336, ChEBI:CHEBI:17898, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.300; Evidence={ECO:0000269|PubMed:12732097, ECO:0000269|PubMed:18087047}; CATALYTIC ACTIVITY: Reaction=9-cis-retinol + NADP(+) = 9-cis-retinal + H(+) + NADPH; Xref=Rhea:RHEA:54916, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78272, ChEBI:CHEBI:78273; Evidence={ECO:0000269|PubMed:12732097, ECO:0000269|PubMed:18087047}; CATALYTIC ACTIVITY: Reaction=13-cis-retinol + NADP(+) = 13-cis-retinal + H(+) + NADPH; Xref=Rhea:RHEA:54920, ChEBI:CHEBI:15378, ChEBI:CHEBI:45479, ChEBI:CHEBI:45487, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; Evidence={ECO:0000269|PubMed:12732097}; CATALYTIC ACTIVITY: Reaction=allyl alcohol + NADP(+) = acrolein + H(+) + NADPH; Xref=Rhea:RHEA:12168, ChEBI:CHEBI:15368, ChEBI:CHEBI:15378, ChEBI:CHEBI:16605, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.54; Evidence={ECO:0000269|PubMed:19563777}; CATALYTIC ACTIVITY: Reaction=(E)-4-hydroxynon-2-en-1-ol + NADP(+) = (E)-4-hydroxynon-2-enal + H(+) + NADPH; Xref=Rhea:RHEA:58416, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:58968, ChEBI:CHEBI:142617; Evidence={ECO:0000269|PubMed:19013440}; CATALYTIC ACTIVITY: Reaction=a 4-hydroxynonen-1-ol + NADP(+) = a 4-hydroxynonenal + H(+) + NADPH; Xref=Rhea:RHEA:58336, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:142593, ChEBI:CHEBI:142606; Evidence={ECO:0000269|PubMed:19563777}; CATALYTIC ACTIVITY: Reaction=NADP(+) + prenol = 3-methyl-2-butenal + H(+) + NADPH; Xref=Rhea:RHEA:58420, ChEBI:CHEBI:15378, ChEBI:CHEBI:15825, ChEBI:CHEBI:16019, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; Evidence={ECO:0000269|PubMed:19563777}; CATALYTIC ACTIVITY: Reaction=(E)-hex-2-en-1-ol + NADP(+) = (E)-hex-2-enal + H(+) + NADPH; Xref=Rhea:RHEA:58424, ChEBI:CHEBI:15378, ChEBI:CHEBI:28913, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:141205; Evidence={ECO:0000269|PubMed:19563777}; CATALYTIC ACTIVITY: Reaction=(E,E)-2,4-hexadien-1-ol + NADP(+) = (E,E)-2,4-hexadienal + H(+) + NADPH; Xref=Rhea:RHEA:58428, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:82334, ChEBI:CHEBI:142625; Evidence={ECO:0000269|PubMed:19563777}; CATALYTIC ACTIVITY: Reaction=(E)-4-oxonon-2-en-1-ol + NADP(+) = (E)-4-oxonon-2-enal + H(+) + NADPH; Xref=Rhea:RHEA:58432, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:58972, ChEBI:CHEBI:142624; Evidence={ECO:0000269|PubMed:19013440}; CATALYTIC ACTIVITY: Reaction=4-methylpentan-1-ol + NADP(+) = 4-methylpentanal + H(+) + NADPH; Xref=Rhea:RHEA:58436, ChEBI:CHEBI:15378, ChEBI:CHEBI:17998, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:63910; Evidence={ECO:0000269|PubMed:19013440};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=6000 uM for D,L-glyceraldehyde {ECO:0000269|PubMed:18087047}; KM=0.6 uM for all-trans-retinal {ECO:0000269|PubMed:18087047}; KM=0.7 uM for 9-cis-retinal {ECO:0000269|PubMed:18087047}; KM=37 uM for pyridine-3-aldehyde {ECO:0000269|PubMed:12732097}; KM=110 uM for acrolein {ECO:0000269|PubMed:19563777}; KM=87 uM for 3-methyl-2-butenal {ECO:0000269|PubMed:19563777}; KM=30 uM for 4-hydroxynonenal {ECO:0000269|PubMed:19563777}; KM=61 uM for (E)-2-hexenal {ECO:0000269|PubMed:19563777}; KM=95 uM for (E,E)-2,4-hexadienal {ECO:0000269|PubMed:19563777}; KM=532 uM for GS-acrolein {ECO:0000269|PubMed:19563777}; KM=245 uM for GS-3-methyl-2-butenal {ECO:0000269|PubMed:19563777}; KM=145 uM for GS-(E)-2-hexenal {ECO:0000269|PubMed:19563777}; KM=77 uM for GS-(E,E)-2,4-hexadienal {ECO:0000269|PubMed:19563777}; KM=330 uM for (E)-4-hydroxynon-2-enal {ECO:0000269|PubMed:19013440}; KM=300 uM for (E)-4-oxonon-2-enal {ECO:0000269|PubMed:19013440}; KM=50 uM for 4-methylpentanal {ECO:0000269|PubMed:19013440}; Vmax=3122 nmol/min/mg enzyme with acrolein {ECO:0000269|PubMed:19563777}; Vmax=2647 nmol/min/mg enzyme with 3-methyl-2-butenal as substrate {ECO:0000269|PubMed:19563777}; Vmax=2658 nmol/min/mg enzyme with (E)-2-hexenal as substrate {ECO:0000269|PubMed:19563777}; Vmax=2160 nmol/min/mg enzyme with (E,E)-2,4-hexadienal as substrate {ECO:0000269|PubMed:19563777}; Vmax=3298 nmol/min/mg enzyme with 4-hydroxynonenal {ECO:0000269|PubMed:19563777}; Vmax=64 nmol/min/mg enzyme with GS-acrolein {ECO:0000269|PubMed:19563777}; Vmax=1960 nmol/min/mg enzyme with GS-3-methyl-2-butenal as substrate {ECO:0000269|PubMed:19563777}; Vmax=2049 nmol/min/mg enzyme with GS-(E)-2-hexenal {ECO:0000269|PubMed:19563777}; Vmax=4004 nmol/min/mg enzyme with GS-(E,E)-2,4-hexadienal as substrate {ECO:0000269|PubMed:19563777}; Note=kcat is 640 min(-1) for glyceraldehyde as substrate (PubMed:12732097). kcat is 185 min(-1) for pyridine-3-aldehyde as substrate (PubMed:12732097). kcat is 116 min(-1) for acrolein as substrate. kcat is 103 min(-1) for 3-methyl-2-butenal as substrate. kcat is 97 min(-1) for(E)-2-hexenal as substrate. kcat is 82 min(-1) for (E,E)-2,4-hexadienal as substrate. kcat is 120 min(-1) for 4-hydroxynonenal as substrate. kcat is 3 min(-1) for GS-acrolein as substrate. kcat is 70 min(-1) for GS-3-methyl-2-butenal as substrate. kcat is 71 min(-1) for GS-(E)-2-hexenal as substrate. kcat is 147 min(-1) for (E,E)-2,4-hexadienal as substrate (PubMed:19563777). kcat is 35 min(-1) for D,L-glyceraldehyde as substrate. kcat is 27 min(-1) for all-trans-retinal as substrate. kcat is 1 min(-1) for 9-cis-retinal as substrate (PubMed:18087047). kcat is 43 min(-1) for 4-hydroxynon-2-enal (PubMed:19013440). kcat is 40 min(-1) for (E)-4-oxonon-2-enal (PubMed:19013440). kcat is 25 min(-1) for 4-methylpentanal (PubMed:19013440). {ECO:0000269|PubMed:12732097, ECO:0000269|PubMed:18087047, ECO:0000269|PubMed:19013440, ECO:0000269|PubMed:19563777};
|
PATHWAY: Cofactor metabolism; retinol metabolism. {ECO:0000269|PubMed:12732097, ECO:0000269|PubMed:18087047}.
| null | null |
FUNCTION: Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols (PubMed:12732097, PubMed:18087047, PubMed:19013440, PubMed:19563777, PubMed:9565553). Displays strong enzymatic activity toward all-trans-retinal, 9-cis-retinal, and 13-cis-retinal (PubMed:12732097, PubMed:18087047). Plays a critical role in detoxifying dietary and lipid-derived unsaturated carbonyls, such as crotonaldehyde, 4-hydroxynonenal, trans-2-hexenal, trans-2,4-hexadienal and their glutathione-conjugates carbonyls (GS-carbonyls) (PubMed:19013440, PubMed:19563777). Displays no reductase activity towards glucose (PubMed:12732097). {ECO:0000269|PubMed:12732097, ECO:0000269|PubMed:18087047, ECO:0000269|PubMed:19013440, ECO:0000269|PubMed:19563777, ECO:0000269|PubMed:9565553}.
|
Homo sapiens (Human)
|
O60220
|
TIM8A_HUMAN
|
MDSSSSSSAAGLGAVDPQLQHFIEVETQKQRFQQLVHQMTELCWEKCMDKPGPKLDSRAEACFVNCVERFIDTSQFILNRLEQTQKSKPVFSESLSD
| null | null |
nervous system development [GO:0007399]; protein insertion into mitochondrial inner membrane [GO:0045039]
|
mitochondrial inner membrane [GO:0005743]; mitochondrial intermembrane space [GO:0005758]; mitochondrial intermembrane space protein transporter complex [GO:0042719]; mitochondrion [GO:0005739]
|
identical protein binding [GO:0042802]; zinc ion binding [GO:0008270]
|
PF02953;
|
1.10.287.810;
|
Small Tim family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:11489896}; Peripheral membrane protein {ECO:0000269|PubMed:11489896}; Intermembrane side {ECO:0000269|PubMed:11489896}.
| null | null | null | null | null |
FUNCTION: Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space. The TIMM8-TIMM13 complex mediates the import of proteins such as TIMM23, SLC25A12/ARALAR1 and SLC25A13/ARALAR2, while the predominant TIMM9-TIMM10 70 kDa complex mediates the import of much more proteins. Probably necessary for normal neurologic development. {ECO:0000269|PubMed:11489896, ECO:0000269|PubMed:15254020}.
|
Homo sapiens (Human)
|
O60229
|
KALRN_HUMAN
|
MTDRFWDQWYLWYLRLLRLLDRGSFRNDGLKASDVLPILKEKVAFVSGGRDKRGGPILTFPARSNHDRIRQEDLRKLVTYLASVPSEDVCKRGFTVIIDMRGSKWDLIKPLLKTLQEAFPAEIHVALIIKPDNFWQKQKTNFGSSKFIFETSMVSVEGLTKLVDPSQLTEEFDGSLDYNHEEWIELRLSLEEFFNSAVHLLSRLEDLQEMLARKEFPVDVEGSRRLIDEHTQLKKKVLKAPVEELDREGQRLLQCIRCSDGFSGRNCIPGSADFQSLVPKITSLLDKLHSTRQHLHQMWHVRKLKLDQCFQLRLFEQDAEKMFDWISHNKELFLQSHTEIGVSYQYALDLQTQHNHFAMNSMNAYVNINRIMSVASRLSEAGHYASQQIKQISTQLDQEWKSFAAALDERSTILAMSAVFHQKAEQFLSGVDAWCKMCSEGGLPSEMQDLELAIHHHQTLYEQVTQAYTEVSQDGKALLDVLQRPLSPGNSESLTATANYSKAVHQVLDVVHEVLHHQRRLESIWQHRKVRLHQRLQLCVFQQDVQQVLDWIENHGEAFLSKHTGVGKSLHRARALQKRHDDFEEVAQNTYTNADKLLEAAEQLAQTGECDPEEIYKAARHLEVRIQDFVRRVEQRKLLLDMSVSFHTHTKELWTWMEDLQKEMLEDVCADSVDAVQELIKQFQQQQTATLDATLNVIKEGEDLIQQLRSAPPSLGEPSEARDSAVSNNKTPHSSSISHIESVLQQLDDAQVQMEELFHERKIKLDIFLQLRIFEQYTIEVTAELDAWNEDLLRQMNDFNTEDLTLAEQRLQRHTERKLAMNNMTFEVIQQGQDLHQYITEVQASGIELICEKDIDLAAQVQELLEFLHEKQHELELNAEQTHKRLEQCLQLRHLQAEVKQVLGWIRNGESMLNASLVNASSLSEAEQLQREHEQFQLAIESLFHATSLQKTHQSALQVQQKAEVLLQAGHYDADAIRECAEKVALHWQQLMLKMEDRLKLVNASVAFYKTSEQVCSVLESLEQEYRRDEDWCGGRDKLGPAAEIDHVIPLISKHLEQKEAFLKACTLARRNAEVFLKYIHRNNVSMPSVASHTRGPEQQVKAILSELLQRENRVLHFWTLKKRRLDQCQQYVVFERSAKQALDWIQETGEFYLSTHTSTGETTEETQELLKEYGEFRVPAKQTKEKVKLLIQLADSFVEKGHIHATEIRKWVTTVDKHYRDFSLRMGKYRYSLEKALGVNTEDNKDLELDIIPASLSDREVKLRDANHEVNEEKRKSARKKEFIMAELLQTEKAYVRDLHECLETYLWEMTSGVEEIPPGILNKEHIIFGNIQEIYDFHNNIFLKELEKYEQLPEDVGHCFVTWADKFQMYVTYCKNKPDSNQLILEHAGTFFDEIQQRHGLANSISSYLIKPVQRITKYQLLLKELLTCCEEGKGELKDGLEVMLSVPKKANDAMHVSMLEGFDENLDVQGELILQDAFQVWDPKSLIRKGRERHLFLFEISLVFSKEIKDSSGHTKYVYKNKLLTSELGVTEHVEGDPCKFALWSGRTPSSDNKTVLKASNIETKQEWIKNIREVIQERIIHLKGALKEPLQLPKTPAKQRNNSKRDGVEDIDSQGDGSSQPDTISIASRTSQNTVDSDKLSGGCELTVVLQDFSAGHSSELTIQVGQTVELLERPSERPGWCLVRTTERSPPLEGLVPSSALCISHSRSSVEMDCFFPLVKDAYSHSSSENGGKSESVANLQAQPSLNSIHSSPGPKRSTNTLKKWLTSPVRRLNSGKADGNIKKQKKVRDGRKSFDLGSPKPGDETTPQGDSADEKSKKGWGEDEPDEESHTPLPPPMKIFDNDPTQDEMSSSLLAARQASTEVPTAADLVNAIEKLVKNKLSLEGSSYRGSLKDPAGCLNEGMAPPTPPKNPEEEQKAKALRGRMFVLNELVQTEKDYVKDLGIVVEGFMKRIEEKGVPEDMRGKDKIVFGNIHQIYDWHKDFFLAELEKCIQEQDRLAQLFIKHERKLHIYVWYCQNKPRSEYIVAEYDAYFEEVKQEINQRLTLSDFLIKPIQRITKYQLLLKDFLRYSEKAGLECSDIEKAVELMCLVPKRCNDMMNLGRLQGFEGTLTAQGKLLQQDTFYVIELDAGMQSRTKERRVFLFEQIVIFSELLRKGSLTPGYMFKRSIKMNYLVLEENVDNDPCKFALMNRETSERVVLQAANADIQQAWVQDINQVLETQRDFLNALQSPIEYQRKERSTAVMRSQPARLPQASPRPYSSVPAGSEKPPKGSSYNPPLPPLKISTSNGSPGFEYHQPGDKFEASKQNDLGGCNGTSSMAVIKDYYALKENEICVSQGEVVQVLAVNQQNMCLVYQPASDHSPAAEGWVPGSILAPLTKATAAESSDGSIKKSCSWHTLRMRKRAEVENTGKNEATGPRKPKDILGNKVSVKETNSSEESECDDLDPNTSMEILNPNFIQEVAPEFLVPLVDVTCLLGDTVILQCKVCGRPKPTITWKGPDQNILDTDNSSATYTVSSCDSGEITLKICNLMPQDSGIYTCIATNDHGTTSTSATVKVQGVPAAPNRPIAQERSCTSVILRWLPPSSTGNCTISGYTVEYREEGSQIWQQSVASTLDTYLVIEDLSPGCPYQFRVSASNPWGISLPSEPSEFVRLPEYDAAADGATISWKENFDSAYTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVPRVKLIDLEDAVQISGHFHIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYFCGVSNAARDFINVILQEDFRRRPTAATCLQHPWLQPHNGSYSKIPLDTSRLACFIERRKHQNDVRPIPNVKSYIVNRVNQGT
|
2.7.11.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
|
axon guidance [GO:0007411]; ephrin receptor signaling pathway [GO:0048013]; intracellular signal transduction [GO:0035556]; nervous system development [GO:0007399]; protein phosphorylation [GO:0006468]; regulation of small GTPase mediated signal transduction [GO:0051056]; signal transduction [GO:0007165]; vesicle-mediated transport [GO:0016192]
|
actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extrinsic component of membrane [GO:0019898]; nucleoplasm [GO:0005654]; postsynaptic density [GO:0014069]
|
ATP binding [GO:0005524]; guanyl-nucleotide exchange factor activity [GO:0005085]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF13716;PF00041;PF07679;PF00169;PF00069;PF00621;PF16609;PF00435;
|
1.20.58.60;3.40.525.10;1.20.900.10;2.60.40.10;2.30.29.30;2.30.30.40;1.10.510.10;
|
Protein kinase superfamily, CAMK Ser/Thr protein kinase family
|
PTM: Autophosphorylated.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10023074}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10023074}. Note=Associated with the cytoskeleton.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
| null | null | null | null |
FUNCTION: Promotes the exchange of GDP by GTP. Activates specific Rho GTPase family members, thereby inducing various signaling mechanisms that regulate neuronal shape, growth, and plasticity, through their effects on the actin cytoskeleton. Induces lamellipodia independent of its GEF activity. {ECO:0000269|PubMed:10023074}.
|
Homo sapiens (Human)
|
O60231
|
DHX16_HUMAN
|
MATPAGLERWVQDELHSVLGLSERHVAQFLIGTAQRCTSAEEFVQRLRDTDTLDLSGPARDFALRLWNKVPRKAVVEKPARAAEREARALLEKNRSYRLLEDSEESSEETVSRAGSSLQKKRKKRKHLRKKREEEEEEEASEKGKKKTGGSKQQTEKPESEDEWERTERERLQDLEERDAFAERVRQRDKDRTRNVLERSDKKAYEEAQKRLKMAEEDRKAMVPELRKKSRREYLAKREREKLEDLEAELADEEFLFGDVELSRHERQELKYKRRVRDLAREYRAAGEQEKLEATNRYHMPKETRGQPARAVDLVEEESGAPGEEQRRWEEARLGAASLKFGARDAASQEPKYQLVLEEEETIEFVRATQLQGDEEPSAPPTSTQAQQKESIQAVRRSLPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEGYTNKGMKIACTQPRRVAAMSVAARVAREMGVKLGNEVGYSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFRPELKVLVASATMDTARFSTFFDDAPVFRIPGRRFPVDIFYTKAPEADYLEACVVSVLQIHVTQPPGDILVFLTGQEEIEAACEMLQDRCRRLGSKIRELLVLPIYANLPSDMQARIFQPTPPGARKVVVATNIAETSLTIEGIIYVLDPGFCKQKSYNPRTGMESLTVTPCSKASANQRAGRAGRVAAGKCFRLYTAWAYQHELEETTVPEIQRTSLGNVVLLLKSLGIHDLMHFDFLDPPPYETLLLALEQLYALGALNHLGELTTSGRKMAELPVDPMLSKMILASEKYSCSEEILTVAAMLSVNNSIFYRPKDKVVHADNARVNFFLPGGDHLVLLNVYTQWAESGYSSQWCYENFVQFRSMRRARDVREQLEGLLERVEVGLSSCQGDYIRVRKAITAGYFYHTARLTRSGYRTVKQQQTVFIHPNSSLFEQQPRWLLYHELVLTTKEFMRQVLEIESSWLLEVAPHYYKAKELEDPHAKKMPKKIGKTREELG
|
3.6.4.13
| null |
antiviral innate immune response [GO:0140374]; mRNA splicing, via spliceosome [GO:0000398]; RNA splicing [GO:0008380]
|
catalytic step 2 spliceosome [GO:0071013]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spliceosomal complex [GO:0005681]; U2-type precatalytic spliceosome [GO:0071005]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; helicase activity [GO:0004386]; molecular adaptor activity [GO:0060090]; pattern recognition receptor activity [GO:0038187]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; ubiquitin binding [GO:0043130]
|
PF00270;PF21010;PF04408;PF00271;PF07717;
|
1.20.120.1080;3.40.50.300;
|
DEAD box helicase family, DEAH subfamily, DDX16/PRP8 sub-subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20423332, ECO:0000269|PubMed:20841358, ECO:0000269|PubMed:25296192, ECO:0000269|PubMed:29360106}. Nucleus, nucleoplasm {ECO:0000269|PubMed:20423332}. Cytoplasm {ECO:0000269|PubMed:35263596}.
|
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=3.6.4.13;
| null | null | null | null |
FUNCTION: Required for pre-mRNA splicing as component of the spliceosome (PubMed:20423332, PubMed:20841358, PubMed:25296192, PubMed:29360106). Contributes to pre-mRNA splicing after spliceosome formation and prior to the first transesterification reaction. As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). Plays also a role in innate antiviral response by acting as a pattern recognition receptor sensing splicing signals in viral RNA (PubMed:35263596). Mechanistically, TRIM6 promotes the interaction between unanchored 'Lys-48'-polyubiquitin chains and DHX16, leading to DHX16 interaction with RIGI and ssRNA to amplify RIGI-dependent innate antiviral immune responses (PubMed:35263596). {ECO:0000269|PubMed:20423332, ECO:0000269|PubMed:20841358, ECO:0000269|PubMed:25296192, ECO:0000269|PubMed:29360106, ECO:0000269|PubMed:35263596, ECO:0000305|PubMed:33509932}.
|
Homo sapiens (Human)
|
O60232
|
ZNRD2_HUMAN
|
MALNGAEVDDFSWEPPTEAETKVLQARRERQDRISRLMGDYLLRGYRMLGETCADCGTILLQDKQRKIYCVACQELDSDVDKDNPALNAQAALSQAREHQLASASELPLGSRPAPQPPVPRPEHCEGAAAGLKAAQGPPAPAVPPNTDVMACTQTALLQKLTWASAELGSSTSLETSIQLCGLIRACAEALRSLQQLQH
| null | null |
cell division [GO:0051301]; mitotic cell cycle [GO:0000278]
| null | null |
PF06677;
| null | null | null | null | null | null | null | null | null |
FUNCTION: Might play a role in mitosis. Antigenic molecule. Could be a centromere-associated protein. May induce anti-centromere antibodies. {ECO:0000305|PubMed:9486406}.
|
Homo sapiens (Human)
|
O60235
|
TM11D_HUMAN
|
MYRPARVTSTSRFLNPYVVCFIVVAGVVILAVTIALLVYFLAFDQKSYFYRSSFQLLNVEYNSQLNSPATQEYRTLSGRIESLITKTFKESNLRNQFIRAHVAKLRQDGSGVRADVVMKFQFTRNNNGASMKSRIESVLRQMLNNSGNLEINPSTEITSLTDQAAANWLINECGAGPDLITLSEQRILGGTEAEEGSWPWQVSLRLNNAHHCGGSLINNMWILTAAHCFRSNSNPRDWIATSGISTTFPKLRMRVRNILIHNNYKSATHENDIALVRLENSVTFTKDIHSVCLPAATQNIPPGSTAYVTGWGAQEYAGHTVPELRQGQVRIISNDVCNAPHSYNGAILSGMLCAGVPQGGVDACQGDSGGPLVQEDSRRLWFIVGIVSWGDQCGLPDKPGVYTRVTAYLDWIRQQTGI
|
3.4.21.-
| null |
proteolysis [GO:0006508]; respiratory gaseous exchange by respiratory system [GO:0007585]
|
extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; plasma membrane [GO:0005886]
|
peptidase activity [GO:0008233]; serine-type endopeptidase activity [GO:0004252]
|
PF01390;PF00089;
|
3.30.70.960;2.40.10.10;
|
Peptidase S1 family
| null |
SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein. Note=Activated by cleavage and secreted.; SUBCELLULAR LOCATION: [Transmembrane protease serine 11D catalytic chain]: Secreted. Note=Activated by cleavage and secreted.
| null | null | null | null | null |
FUNCTION: May play some biological role in the host defense system on the mucous membrane independently of or in cooperation with other substances in airway mucous or bronchial secretions. Plays a role in the proteolytic processing of ACE2. Proteolytically cleaves and activates the human coronavirus 229E (HCoV-229E) spike glycoprotein which facilitate virus-cell membrane fusions; spike proteins are synthesized and maintained in precursor intermediate folding states and proteolysis permits the refolding and energy release required to create stable virus-cell linkages and membrane coalescence. Preferentially cleaves the C-terminal side of arginine residues at the P1 position of certain peptides, cleaving Boc-Phe-Ser-Arg-4-methylcoumaryl-7-amide most efficiently and having an optimum pH of 8.6 with this substrate. {ECO:0000269|PubMed:23536651, ECO:0000269|PubMed:24227843}.
|
Homo sapiens (Human)
|
O60237
|
MYPT2_HUMAN
|
MAELEHLGGKRAESARMRRAEQLRRWRGSLTEQEPAERRGAGRQPLTRRGSPRVRFEDGAVFLAACSSGDTDEVRKLLARGADINTVNVDGLTALHQACIDENLDMVKFLVENRANVNQQDNEGWTPLHAAASCGYLNIAEYFINHGASVGIVNSEGEVPSDLAEEPAMKDLLLEQVKKQGVDLEQSRKEEEQQMLQDARQWLNSGKIEDVRQARSGATALHVAAAKGYSEVLRLLIQAGYELNVQDYDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVADEGLVEHLELLQKKQNVLRSEKETRNKLIESDLNSKIQSGFFKNKEKMLYEEETPKSQEMEEENKESSSSSSEEEEGEDEASESETEKEADKKPEAFVNHSNSESKSSITEQIPAPAQNTFSASSARRFSSGLFNKPEEPKDESPSSWRLGLRKTGSHNMLSEVANSREPIRDRGSSIYRSSSSPRISALLDNKDKERENKSYISSLAPRKLNSTSDIEEKENRESAVNLVRSGSYTRQLWRDEAKGNEIPQTIAPSTYVSTYLKRTPHKSQADTTAEKTADNVSSSTPLCVITNRPLPSTANGVTATPVLSITGTDSSVEAREKRRSYLTPVRDEEAESLRKARSRQARQTRRSTQGVTLTDLQEAERTFSRSRAERQAQEQPREKPTDTEGLEGSPEKHEPSAVPATEAGEGQQPWGRSLDEEPICHRLRCPAQPDKPTTPASPSTSRPSLYTSSHLLWTNRFSVPDSESSETTTNTTTAKEMDKNENEEADLDEQSSKRLSIRERRRPKERRRGTGINFWTKDEDETDGSEEVKETWHERLSRLESGGSNPTTSDSYGDRASARARREAREARLATLTSRVEEDSNRDYKKLYESALTENQKLKTKLQEAQLELADIKSKLEKVAQQKQEKTSDRSSVLEMEKRERRALERKMSEMEEEMKVLTELKSDNQRLKDENGALIRVISKLSK
| null | null |
regulation of muscle contraction [GO:0006937]; signal transduction [GO:0007165]
|
A band [GO:0031672]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; stress fiber [GO:0001725]; Z disc [GO:0030018]
|
enzyme activator activity [GO:0008047]; enzyme inhibitor activity [GO:0004857]; phosphatase regulator activity [GO:0019208]; protein kinase binding [GO:0019901]
|
PF12796;PF15898;
|
6.10.140.390;6.10.250.1820;1.25.40.20;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12923170}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000269|PubMed:12923170}. Note=Along actomyosin filaments. {ECO:0000269|PubMed:12923170}.
| null | null | null | null | null |
FUNCTION: Regulates myosin phosphatase activity. Augments Ca(2+) sensitivity of the contractile apparatus. {ECO:0000269|PubMed:11067852, ECO:0000269|PubMed:9570949}.
|
Homo sapiens (Human)
|
O60238
|
BNI3L_HUMAN
|
MSSHLVEPPPPLHNNNNNCEENEQSLPPPAGLNSSWVELPMNSSNGNDNGNGKNGGLEHVPSSSSIHNGDMEKILLDAQHESGQSSSRGSSHCDSPSPQEDGQIMFDVEMHTSRDHSSQSEEEVVEGEKEVEALKKSADWVSDWSSRPENIPPKEFHFRHPKRSVSLSMRKSGAMKKGGIFSAEFLKVFIPSLFLSHVLALGLGIYIGKRLSTPSASTY
| null | null |
cellular response to hypoxia [GO:0071456]; defense response to virus [GO:0051607]; mitochondrial outer membrane permeabilization [GO:0097345]; mitochondrial protein catabolic process [GO:0035694]; negative regulation of apoptotic process [GO:0043066]; negative regulation of mitochondrial membrane potential [GO:0010917]; negative regulation of programmed cell death [GO:0043069]; positive regulation of apoptotic process [GO:0043065]; positive regulation of macroautophagy [GO:0016239]; regulation of mitophagy [GO:1901524]; regulation of programmed cell death [GO:0043067]; regulation of protein targeting to mitochondrion [GO:1903214]
|
endoplasmic reticulum [GO:0005783]; membrane [GO:0016020]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; nuclear envelope [GO:0005635]; nuclear speck [GO:0016607]; nucleus [GO:0005634]
|
identical protein binding [GO:0042802]; lamin binding [GO:0005521]; protein homodimerization activity [GO:0042803]
|
PF06553;
|
6.10.250.1020;
|
NIP3 family
|
PTM: Undergoes progressive proteolysis to an 11 kDa C-terminal fragment, which is blocked by the proteasome inhibitor lactacystin.
|
SUBCELLULAR LOCATION: Nucleus envelope. Endoplasmic reticulum. Mitochondrion outer membrane. Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Note=Colocalizes with SPATA18 at the mitochondrion outer membrane.
| null | null | null | null | null |
FUNCTION: Induces apoptosis. Interacts with viral and cellular anti-apoptosis proteins. Can overcome the suppressors BCL-2 and BCL-XL, although high levels of BCL-XL expression will inhibit apoptosis. Inhibits apoptosis induced by BNIP3. Involved in mitochondrial quality control via its interaction with SPATA18/MIEAP: in response to mitochondrial damage, participates in mitochondrial protein catabolic process (also named MALM) leading to the degradation of damaged proteins inside mitochondria. The physical interaction of SPATA18/MIEAP, BNIP3 and BNIP3L/NIX at the mitochondrial outer membrane regulates the opening of a pore in the mitochondrial double membrane in order to mediate the translocation of lysosomal proteins from the cytoplasm to the mitochondrial matrix. May function as a tumor suppressor. {ECO:0000269|PubMed:10381623, ECO:0000269|PubMed:21264228}.
|
Homo sapiens (Human)
|
O60239
|
3BP5_HUMAN
|
MDAALKRSRSEEPAEILPPARDEEEEEEEGMEQGLEEEEEVDPRIQGELEKLNQSTDDINRRETELEDARQKFRSVLVEATVKLDELVKKIGKAVEDSKPYWEARRVARQAQLEAQKATQDFQRATEVLRAAKETISLAEQRLLEDDKRQFDSAWQEMLNHATQRVMEAEQTKTRSELVHKETAARYNAAMGRMRQLEKKLKRAINKSKPYFELKAKYYVQLEQLKKTVDDLQAKLTLAKGEYKMALKNLEMISDEIHERRRSSAMGPRGCGVGAEGSSTSVEDLPGSKPEPDAISVASEAFEDDSCSNFVSEDDSETQSVSSFSSGPTSPSEMPDQFPAVVRPGSLDLPSPVSLSEFGMMFPVLGPRSECSGASSPECEVERGDRAEGAENKTSDKANNNRGLSSSSGSGGSSKSQSSTSPEGQALENRMKQLSLQCSKGRDGIIADIKMVQIG
| null | null |
intracellular signal transduction [GO:0035556]; signal transduction [GO:0007165]
|
cytoplasm [GO:0005737]; cytoplasmic vesicle membrane [GO:0030659]; mitochondrion [GO:0005739]; nuclear body [GO:0016604]; nucleoplasm [GO:0005654]
|
guanyl-nucleotide exchange factor activity [GO:0005085]; protein kinase inhibitor activity [GO:0004860]; SH3 domain binding [GO:0017124]
|
PF05276;
| null |
SH3BP5 family
| null |
SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000269|PubMed:30217979}; Peripheral membrane protein {ECO:0000269|PubMed:30217979}. Mitochondrion {ECO:0000269|PubMed:12167088}. Note=Colocalizes with RAB11A on cytoplasmic vesicle membranes. {ECO:0000269|PubMed:30217979}.
| null | null | null | null | null |
FUNCTION: Functions as a guanine nucleotide exchange factor (GEF) with specificity for RAB11A and RAB25 (PubMed:26506309, PubMed:30217979). Inhibits the auto- and transphosphorylation activity of BTK. Plays a negative regulatory role in BTK-related cytoplasmic signaling in B-cells. May be involved in BCR-induced apoptotic cell death. {ECO:0000269|PubMed:10339589, ECO:0000269|PubMed:26506309, ECO:0000269|PubMed:30217979, ECO:0000269|PubMed:9571151}.
|
Homo sapiens (Human)
|
O60240
|
PLIN1_HUMAN
|
MAVNKGLTLLDGDLPEQENVLQRVLQLPVVSGTCECFQKTYTSTKEAHPLVASVCNAYEKGVQSASSLAAWSMEPVVRRLSTQFTAANELACRGLDHLEEKIPALQYPPEKIASELKDTISTRLRSARNSISVPIASTSDKVLGAALAGCELAWGVARDTAEFAANTRAGRLASGGADLALGSIEKVVEYLLPPDKEESAPAPGHQQAQKSPKAKPSLLSRVGALTNTLSRYTVQTMARALEQGHTVAMWIPGVVPLSSLAQWGASVAMQAVSRRRSEVRVPWLHSLAAAQEEDHEDQTDTEGEDTEEEEELETEENKFSEVAALPGPRGLLGGVAHTLQKTLQTTISAVTWAPAAVLGMAGRVLHLTPAPAVSSTKGRAMSLSDALKGVTDNVVDTVVHYVPLPRLSLMEPESEFRDIDNPPAEVERREAERRASGAPSAGPEPAPRLAQPRRSLRSAQSPGAPPGPGLEDEVATPAAPRPGFPAVPREKPKRRVSDSFFRPSVMEPILGRTHYSQLRKKS
| null | null |
cellular response to cold [GO:0070417]; lipid catabolic process [GO:0016042]; lipid metabolic process [GO:0006629]
|
cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; lipid droplet [GO:0005811]
|
lipid binding [GO:0008289]
|
PF03036;
| null |
Perilipin family
|
PTM: Major cAMP-dependent protein kinase-substrate in adipocytes, also dephosphorylated by PP1. When phosphorylated, may be maximally sensitive to HSL and when unphosphorylated, may play a role in the inhibition of lipolysis, by acting as a barrier in lipid droplet (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:23399566}. Lipid droplet {ECO:0000269|PubMed:23399566, ECO:0000305|PubMed:26357594}. Note=Lipid droplet surface-associated. {ECO:0000269|PubMed:23399566}.
| null | null | null | null | null |
FUNCTION: Modulator of adipocyte lipid metabolism. Coats lipid storage droplets to protect them from breakdown by hormone-sensitive lipase (HSL). Its absence may result in leanness. Plays a role in unilocular lipid droplet formation by activating CIDEC. Their interaction promotes lipid droplet enlargement and directional net neutral lipid transfer. May modulate lipolysis and triglyceride levels. {ECO:0000269|PubMed:23399566}.
|
Homo sapiens (Human)
|
O60241
|
AGRB2_HUMAN
|
MENTGWMGKGHRMTPACPLLLSVILSLRLATAFDPAPSACSALASGVLYGAFSLQDLFPTIASGCSWTLENPDPTKYSLYLRFNRQEQVCAHFAPRLLPLDHYLVNFTCLRPSPEEAVAQAESEVGRPEEEEAEAAAGLELCSGSGPFTFLHFDKNFVQLCLSAEPSEAPRLLAPAALAFRFVEVLLINNNNSSQFTCGVLCRWSEECGRAAGRACGFAQPGCSCPGEAGAGSTTTTSPGPPAAHTLSNALVPGGPAPPAEADLHSGSSNDLFTTEMRYGEEPEEEPKVKTQWPRSADEPGLYMAQTGDPAAEEWSPWSVCSLTCGQGLQVRTRSCVSSPYGTLCSGPLRETRPCNNSATCPVHGVWEEWGSWSLCSRSCGRGSRSRMRTCVPPQHGGKACEGPELQTKLCSMAACPVEGQWLEWGPWGPCSTSCANGTQQRSRKCSVAGPAWATCTGALTDTRECSNLECPATDSKWGPWNAWSLCSKTCDTGWQRRFRMCQATGTQGYPCEGTGEEVKPCSEKRCPAFHEMCRDEYVMLMTWKKAAAGEIIYNKCPPNASGSASRRCLLSAQGVAYWGLPSFARCISHEYRYLYLSLREHLAKGQRMLAGEGMSQVVRSLQELLARRTYYSGDLLFSVDILRNVTDTFKRATYVPSADDVQRFFQVVSFMVDAENKEKWDDAQQVSPGSVHLLRVVEDFIHLVGDALKAFQSSLIVTDNLVISIQREPVSAVSSDITFPMRGRRGMKDWVRHSEDRLFLPKEVLSLSSPGKPATSGAAGSPGRGRGPGTVPPGPGHSHQRLLPADPDESSYFVIGAVLYRTLGLILPPPRPPLAVTSRVMTVTVRPPTQPPAEPLITVELSYIINGTTDPHCASWDYSRADASSGDWDTENCQTLETQAAHTRCQCQHLSTFAVLAQPPKDLTLELAGSPSVPLVIGCAVSCMALLTLLAIYAAFWRFIKSERSIILLNFCLSILASNILILVGQSRVLSKGVCTMTAAFLHFFFLSSFCWVLTEAWQSYLAVIGRMRTRLVRKRFLCLGWGLPALVVAVSVGFTRTKGYGTSSYCWLSLEGGLLYAFVGPAAVIVLVNMLIGIIVFNKLMARDGISDKSKKQRAGSERCPWASLLLPCSACGAVPSPLLSSASARNAMASLWSSCVVLPLLALTWMSAVLAMTDRRSVLFQALFAVFNSAQGFVITAVHCFLRREVQDVVKCQMGVCRADESEDSPDSCKNGQLQILSDFEKDVDLACQTVLFKEVNTCNPSTITGTLSRLSLDEDEEPKSCLVGPEGSLSFSPLPGNILVPMAASPGLGEPPPPQEANPVYMCGEGGLRQLDLTWLRPTEPGSEGDYMVLPRRTLSLQPGGGGGGGEDAPRARPEGTPRRAAKTVAHTEGYPSFLSVDHSGLGLGPAYGSLQNPYGMTFQPPPPTPSARQVPEPGERSRTMPRTVPGSTMKMGSLERKKLRYSDLDFEKVMHTRKRHSELYHELNQKFHTFDRYRSQSTAKREKRWSVSSGGAAERSVCTDKPSPGERPSLSQHRRHQSWSTFKSMTLGSLPPKPRERLTLHRAAAWEPTEPPDGDFQTEV
| null | null |
adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; calcineurin-NFAT signaling cascade [GO:0033173]; cell surface receptor signaling pathway [GO:0007166]; G protein-coupled receptor signaling pathway [GO:0007186]; negative regulation of angiogenesis [GO:0016525]; peripheral nervous system development [GO:0007422]
|
extracellular region [GO:0005576]; membrane [GO:0016020]; plasma membrane [GO:0005886]
|
G protein-coupled receptor activity [GO:0004930]
|
PF00002;PF19188;PF16489;PF01825;PF00090;
|
1.25.40.610;2.60.220.50;4.10.1240.10;1.20.1070.10;2.20.100.10;
|
G-protein coupled receptor 2 family, Adhesion G-protein coupled receptor (ADGR) subfamily
|
PTM: Glycosylated. {ECO:0000269|PubMed:20367554}.; PTM: Autoproteolytically processed at the GPS region of the GAIN-B domain; this cleavage modulates receptor activity (By similarity). Additionally, furin is involved in the cleavage at another site, in the middle of the extracellular domain, generating a soluble fragment. {ECO:0000255|PROSITE-ProRule:PRU00098, ECO:0000269|PubMed:20367554}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28891236}; Multi-pass membrane protein {ECO:0000255}. Secreted {ECO:0000269|PubMed:25326458}.
| null | null | null | null | null |
FUNCTION: Orphan G-protein coupled receptor involved in cell adhesion and probably in cell-cell interactions. Activates NFAT-signaling pathway, a transcription factor, via the G-protein GNAZ (PubMed:20367554, PubMed:28891236). Involved in angiogenesis inhibition (By similarity). {ECO:0000250|UniProtKB:Q8CGM1, ECO:0000269|PubMed:20367554, ECO:0000269|PubMed:28891236}.
|
Homo sapiens (Human)
|
O60242
|
AGRB3_HUMAN
|
MKAVRNLLIYIFSTYLLVMFGFNAAQDFWCSTLVKGVIYGSYSVSEMFPKNFTNCTWTLENPDPTKYSIYLKFSKKDLSCSNFSLLAYQFDHFSHEKIKDLLRKNHSIMQLCNSKNAFVFLQYDKNFIQIRRVFPTNFPGLQKKGEEDQKSFFEFLVLNKVSPSQFGCHVLCTWLESCLKSENGRTESCGIMYTKCTCPQHLGEWGIDDQSLILLNNVVLPLNEQTEGCLTQELQTTQVCNLTREAKRPPKEEFGMMGDHTIKSQRPRSVHEKRVPQEQADAAKFMAQTGESGVEEWSQWSTCSVTCGQGSQVRTRTCVSPYGTHCSGPLRESRVCNNTALCPVHGVWEEWSPWSLCSFTCGRGQRTRTRSCTPPQYGGRPCEGPETHHKPCNIALCPVDGQWQEWSSWSQCSVTCSNGTQQRSRQCTAAAHGGSECRGPWAESRECYNPECTANGQWNQWGHWSGCSKSCDGGWERRIRTCQGAVITGQQCEGTGEEVRRCNEQRCPAPYEICPEDYLMSMVWKRTPAGDLAFNQCPLNATGTTSRRCSLSLHGVAFWEQPSFARCISNEYRHLQHSIKEHLAKGQRMLAGDGMSQVTKTLLDLTQRKNFYAGDLLMSVEILRNVTDTFKRASYIPASDGVQNFFQIVSNLLDEENKEKWEDAQQIYPGSIELMQVIEDFIHIVGMGMMDFQNSYLMTGNVVASIQKLPAASVLTDINFPMKGRKGMVDWARNSEDRVVIPKSIFTPVSSKELDESSVFVLGAVLYKNLDLILPTLRNYTVINSKIIVVTIRPEPKTTDSFLEIELAHLANGTLNPYCVLWDDSKTNESLGTWSTQGCKTVLTDASHTKCLCDRLSTFAILAQQPREIIMESSGTPSVTLIVGSGLSCLALITLAVVYAALWRYIRSERSIILINFCLSIISSNILILVGQTQTHNKSICTTTTAFLHFFFLASFCWVLTEAWQSYMAVTGKIRTRLIRKRFLCLGWGLPALVVATSVGFTRTKGYGTDHYCWLSLEGGLLYAFVGPAAAVVLVNMVIGILVFNKLVSRDGILDKKLKHRAGQMSEPHSGLTLKCAKCGVVSTTALSATTASNAMASLWSSCVVLPLLALTWMSAVLAMTDKRSILFQILFAVFDSLQGFVIVMVHCILRREVQDAFRCRLRNCQDPINADSSSSFPNGHAQIMTDFEKDVDIACRSVLHKDIGPCRAATITGTLSRISLNDDEEEKGTNPEGLSYSTLPGNVISKVIIQQPTGLHMPMSMNELSNPCLKKENSELRRTVYLCTDDNLRGADMDIVHPQERMMESDYIVMPRSSVNNQPSMKEESKMNIGMETLPHERLLHYKVNPEFNMNPPVMDQFNMNLEQHLAPQEHMQNLPFEPRTAVKNFMASELDDNAGLSRSETGSTISMSSLERRKSRYSDLDFEKVMHTRKRHMELFQELNQKFQTLDRFRDIPNTSSMENPAPNKNPWDTFKNPSEYPHYTTINVLDTEAKDALELRPAEWEKCLNLPLDVQEGDFQTEV
| null | null |
adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; cell surface receptor signaling pathway [GO:0007166]; G protein-coupled receptor signaling pathway [GO:0007186]; maintenance of synapse structure [GO:0099558]; motor learning [GO:0061743]; myoblast fusion [GO:0007520]; negative regulation of angiogenesis [GO:0016525]; neuron remodeling [GO:0016322]; positive regulation of synapse assembly [GO:0051965]; regulation of dendrite morphogenesis [GO:0048814]; regulation of synapse maturation [GO:0090128]; regulation of synapse pruning [GO:1905806]
|
cerebellar climbing fiber to Purkinje cell synapse [GO:0150053]; membrane [GO:0016020]; plasma membrane [GO:0005886]; postsynapse [GO:0098794]; postsynaptic density membrane [GO:0098839]; synaptic cleft [GO:0043083]
|
G protein-coupled receptor activity [GO:0004930]; GTPase activator activity [GO:0005096]
|
PF00002;PF19188;PF16489;PF01825;PF02793;PF00090;
|
1.25.40.610;2.60.220.50;4.10.1240.10;1.20.1070.10;2.20.100.10;
|
G-protein coupled receptor 2 family, Adhesion G-protein coupled receptor (ADGR) subfamily
|
PTM: The endogenous protein is proteolytically cleaved into 2 subunits, an extracellular subunit and a seven-transmembrane subunit. {ECO:0000269|PubMed:22333914}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21262840, ECO:0000269|PubMed:22333914}; Multi-pass membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Receptor that plays a role in the regulation of synaptogenesis and dendritic spine formation at least partly via interaction with ELMO1 and RAC1 activity (By similarity). Promotes myoblast fusion through ELMO/DOCK1 (PubMed:24567399). {ECO:0000250|UniProtKB:Q80ZF8, ECO:0000269|PubMed:24567399}.
|
Homo sapiens (Human)
|
O60243
|
H6ST1_HUMAN
|
MRRRRAGGRTMVERASKFVLVVAGSVCFMLILYQYAGPGLSLGAPGGRAPPDDLDLFPTPDPHYEKKYYFPVRELERSLRFDMKGDDVIVFLHIQKTGGTTFGRHLVQNVRLEVPCDCRPGQKKCTCYRPNRRETWLFSRFSTGWSCGLHADWTELTNCVPGVLDRRDSAALRTPRKFYYITLLRDPVSRYLSEWRHVQRGATWKTSLHMCDGRTPTPEELPPCYEGTDWSGCTLQEFMDCPYNLANNRQVRMLADLSLVGCYNLSFIPEGKRAQLLLESAKKNLRGMAFFGLTEFQRKTQYLFERTFNLKFIRPFMQYNSTRAGGVEVDEDTIRRIEELNDLDMQLYDYAKDLFQQRYQYKRQLERREQRLRSREERLLHRAKEALPREDADEPGRVPTEDYMSHIIEKW
|
2.8.2.-
| null |
angiogenesis [GO:0001525]; heparan sulfate proteoglycan biosynthetic process, enzymatic modification [GO:0015015]; labyrinthine layer blood vessel development [GO:0060716]; lung alveolus development [GO:0048286]; neuron development [GO:0048666]
|
Golgi membrane [GO:0000139]; plasma membrane [GO:0005886]
|
heparan sulfate 6-O-sulfotransferase activity [GO:0017095]; sulfotransferase activity [GO:0008146]
|
PF03567;
|
3.40.50.300;
|
Sulfotransferase 6 family
|
PTM: N-glycosylated. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + alpha-D-glucosaminyl-[heparan sulfate](n) = 6-sulfo-alpha-D-glucosaminyl-[heparan sulfate](n) + adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:56604, Rhea:RHEA-COMP:9830, Rhea:RHEA-COMP:14621, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:58388, ChEBI:CHEBI:140604; Evidence={ECO:0000269|PubMed:21700882, ECO:0000269|PubMed:9535912}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56605; Evidence={ECO:0000305|PubMed:21700882};
| null | null | null | null |
FUNCTION: 6-O-sulfation enzyme which catalyzes the transfer of sulfate from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to position 6 of the N-sulfoglucosamine residue (GlcNS) of heparan sulfate. Critical for normal neuronal development where it may play a role in neuron branching. May also play a role in limb development. May prefer iduronic acid. {ECO:0000269|PubMed:21700882, ECO:0000269|PubMed:9535912}.
|
Homo sapiens (Human)
|
O60244
|
MED14_HUMAN
|
MAPVQLENHQLVPPGGGGGGSGGPPSAPAPPPPGAAVAAAAAAAASPGYRLSTLIEFLLHRAYSELMVLTDLLPRKSDVERKIEIVQFASRTRQLFVRLLALVKWANNAGKVEKCAMISSFLDQQAILFVDTADRLASLARDALVHARLPSFAIPYAIDVLTTGSYPRLPTCIRDKIIPPDPITKIEKQATLHQLNQILRHRLVTTDLPPQLANLTVANGRVKFRVEGEFEATLTVMGDDPDVPWRLLKLEILVEDKETGDGRALVHSMQISFIHQLVQSRLFADEKPLQDMYNCLHSFCLSLQLEVLHSQTLMLIRERWGDLVQVERYHAGKCLSLSVWNQQVLGRKTGTASVHKVTIKIDENDVSKPLQIFHDPPLPASDSKLVERAMKIDHLSIEKLLIDSVHARAHQKLQELKAILRGFNANENSSIETALPALVVPILEPCGNSECLHIFVDLHSGMFQLMLYGLDQATLDDMEKSVNDDMKRIIPWIQQLKFWLGQQRCKQSIKHLPTISSETLQLSNYSTHPIGNLSKNKLFIKLTRLPQYYIVVEMLEVPNKPTQLSYKYYFMSVNAADREDSPAMALLLQQFKENIQDLVFRTKTGKQTRTNAKRKLSDDPCPVESKKTKRAGEMCAFNKVLAHFVAMCDTNMPFVGLRLELSNLEIPHQGVQVEGDGFSHAIRLLKIPPCKGITEETQKALDRSLLDCTFRLQGRNNRTWVAELVFANCPLNGTSTREQGPSRHVYLTYENLLSEPVGGRKVVEMFLNDWNSIARLYECVLEFARSLPDIPAHLNIFSEVRVYNYRKLILCYGTTKGSSISIQWNSIHQKFHISLGTVGPNSGCSNCHNTILHQLQEMFNKTPNVVQLLQVLFDTQAPLNAINKLPTVPMLGLTQRTNTAYQCFSILPQSSTHIRLAFRNMYCIDIYCRSRGVVAIRDGAYSLFDNSKLVEGFYPAPGLKTFLNMFVDSNQDARRRSVNEDDNPPSPIGGDMMDSLISQLQPPPQQQPFPKQPGTSGAYPLTSPPTSYHSTVNQSPSMMHTQSPGNLHAASSPSGALRAPSPASFVPTPPPSSHGISIGPGASFASPHGTLDPSSPYTMVSPSGRAGNWPGSPQVSGPSPAARMPGMSPANPSLHSPVPDASHSPRAGTSSQTMPTNMPPPRKLPQRSWAASIPTILTHSALNILLLPSPTPGLVPGLAGSYLCSPLERFLGSVIMRRHLQRIIQQETLQLINSNEPGVIMFKTDALKCRVALSPKTNQTLQLKVTPENAGQWKPDELQVLEKFFETRVAGPPFKANTLIAFTKLLGAPTHILRDCVHIMKLELFPDQATQLKWNVQFCLTIPPSAPPIAPPGTPAVVLKSKMLFFLQLTQKTSVPPQEPVSIIVPIIYDMASGTTQQADIPRQQNSSVAAPMMVSNILKRFAEMNPPRQGECTIFAAVRDLMANLTLPPGGRP
| null | null |
positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; positive regulation of transcription initiation by RNA polymerase II [GO:0060261]; regulation of transcription by RNA polymerase II [GO:0006357]; RNA polymerase II preinitiation complex assembly [GO:0051123]; somatic stem cell population maintenance [GO:0035019]
|
core mediator complex [GO:0070847]; mediator complex [GO:0016592]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
nuclear receptor coactivator activity [GO:0030374]; nuclear vitamin D receptor binding [GO:0042809]; transcription coactivator activity [GO:0003713]; transcription coregulator activity [GO:0003712]
|
PF08638;
| null |
Mediator complex subunit 14 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:15340088, ECO:0000269|PubMed:15625066, ECO:0000269|PubMed:16595664}.
|
Homo sapiens (Human)
|
O60248
|
SOX15_HUMAN
|
MALPGSSQDQAWSLEPPAATAAASSSSGPQEREGAGSPAAPGTLPLEKVKRPMNAFMVWSSAQRRQMAQQNPKMHNSEISKRLGAQWKLLDEDEKRPFVEEAKRLRARHLRDYPDYKYRPRRKAKSSGAGPSRCGQGRGNLASGGPLWGPGYATTQPSRGFGYRPPSYSTAYLPGSYGSSHCKLEAPSPCSLPQSDPRLQGELLPTYTHYLPPGSPTPYNPPLAGAPMPLTHL
| null | null |
anatomical structure morphogenesis [GO:0009653]; brain development [GO:0007420]; cell differentiation [GO:0030154]; chromatin organization [GO:0006325]; male gonad development [GO:0008584]; myoblast development [GO:0048627]; negative regulation of striated muscle tissue development [GO:0045843]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neuron differentiation [GO:0030182]; positive regulation of G0 to G1 transition [GO:0070318]; positive regulation of myoblast proliferation [GO:2000288]; positive regulation of satellite cell activation involved in skeletal muscle regeneration [GO:0014718]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of DNA-templated transcription [GO:0006355]; regulation of transcription by RNA polymerase II [GO:0006357]; skeletal muscle tissue regeneration [GO:0043403]; trophoblast giant cell differentiation [GO:0060707]
|
chromatin [GO:0000785]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667]
|
chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF00505;
|
1.10.30.10;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}.
| null | null | null | null | null |
FUNCTION: Transcription factor that binds to DNA at the 5'-AACAATG-3' consensus sequence (By similarity). Acts as a transcriptional activator and repressor (By similarity). Binds synergistically with POU5F1 (OCT3/4) to gene promoters (By similarity). Binds to the FOXK1 promoter and recruits FHL3, resulting in transcriptional activation of FOXK1 which leads to myoblast proliferation (By similarity). Acts as an inhibitor of myoblast differentiation via transcriptional repression which leads to down-regulation of the muscle-specific genes MYOD and MYOG (By similarity). Involved in trophoblast giant cell differentiation via enhancement of HAND1 transcriptional activity (By similarity). Regulates transcription of HRC via binding to it proximal enhancer region (By similarity). Involved in skeletal muscle regeneration (By similarity). Also plays a role in the development of myogenic precursor cells (By similarity). {ECO:0000250|UniProtKB:P43267}.
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Homo sapiens (Human)
|
O60256
|
KPRB_HUMAN
|
MFCVTPPELETKMNITKGGLVLFSANSNSSCMELSKKIAERLGVEMGKVQVYQEPNRETRVQIQESVRGKDVFIIQTVSKDVNTTIMELLIMVYACKTSCAKSIIGVIPYFPYSKQCKMRKRGSIVSKLLASMMCKAGLTHLITMDLHQKEIQGFFNIPVDNLRASPFLLQYIQEEIPDYRNAVIVAKSPASAKRAQSFAERLRLGIAVIHGEAQDAESDLVDGRHSPPMVRSVAAIHPSLEIPMLIPKEKPPITVVGDVGGRIAIIVDDIIDDVDSFLAAAETLKERGAYKIFVMATHGLLSSDAPRRIEESAIDEVVVTNTIPHEVQKLQCPKIKTVDISMILSEAIRRIHNGESMSYLFRNIGLDD
| null | null |
5-phosphoribose 1-diphosphate biosynthetic process [GO:0006015]; bone development [GO:0060348]; nucleobase-containing compound metabolic process [GO:0006139]; purine nucleotide biosynthetic process [GO:0006164]
|
cytoplasm [GO:0005737]; ribose phosphate diphosphokinase complex [GO:0002189]
|
ATP binding [GO:0005524]; enzyme inhibitor activity [GO:0004857]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; ribose phosphate diphosphokinase activity [GO:0004749]
|
PF14572;PF13793;
|
3.40.50.2020;
|
Ribose-phosphate pyrophosphokinase family
| null | null | null | null | null | null | null |
FUNCTION: Seems to play a negative regulatory role in 5-phosphoribose 1-diphosphate synthesis.
|
Homo sapiens (Human)
|
O60258
|
FGF17_HUMAN
|
MGAARLLPNLTLCLQLLILCCQTQGENHPSPNFNQYVRDQGAMTDQLSRRQIREYQLYSRTSGKHVQVTGRRISATAEDGNKFAKLIVETDTFGSRVRIKGAESEKYICMNKRGKLIGKPSGKSKDCVFTEIVLENNYTAFQNARHEGWFMAFTRQGRPRQASRSRQNQREAHFIKRLYQGQLPFPNHAEKQKQFEFVGSAPTRRTKRTRRPQPLT
| null | null |
animal organ morphogenesis [GO:0009887]; cell differentiation [GO:0030154]; cell-cell signaling [GO:0007267]; fibroblast growth factor receptor signaling pathway [GO:0008543]; nervous system development [GO:0007399]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of gene expression [GO:0010628]; positive regulation of protein phosphorylation [GO:0001934]; regulation of cell migration [GO:0030334]; signal transduction [GO:0007165]
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cytoplasm [GO:0005737]; extracellular region [GO:0005576]; extracellular space [GO:0005615]
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growth factor activity [GO:0008083]; type 1 fibroblast growth factor receptor binding [GO:0005105]; type 2 fibroblast growth factor receptor binding [GO:0005111]
|
PF00167;
|
2.80.10.50;
|
Heparin-binding growth factors family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Plays an important role in the regulation of embryonic development and as signaling molecule in the induction and patterning of the embryonic brain. Required for normal brain development. {ECO:0000269|PubMed:16597617}.
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Homo sapiens (Human)
|
O60259
|
KLK8_HUMAN
|
MGRPRPRAAKTWMFLLLLGGAWAGHSRAQEDKVLGGHECQPHSQPWQAALFQGQQLLCGGVLVGGNWVLTAAHCKKPKYTVRLGDHSLQNKDGPEQEIPVVQSIPHPCYNSSDVEDHNHDLMLLQLRDQASLGSKVKPISLADHCTQPGQKCTVSGWGTVTSPRENFPDTLNCAEVKIFPQKKCEDAYPGQITDGMVCAGSSKGADTCQGDSGGPLVCDGALQGITSWGSDPCGRSDKPGVYTNICRYLDWIKKIIGSKG
|
3.4.21.118
| null |
keratinocyte proliferation [GO:0043616]; memory [GO:0007613]; neuron projection morphogenesis [GO:0048812]; proteolysis [GO:0006508]; regulation of synapse organization [GO:0050807]; response to wounding [GO:0009611]; synapse organization [GO:0050808]
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cytoplasm [GO:0005737]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; secretory granule [GO:0030141]; serine protease inhibitor complex [GO:0097180]
|
serine-type endopeptidase activity [GO:0004252]
|
PF00089;
|
2.40.10.10;
|
Peptidase S1 family, Kallikrein subfamily
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17761692}. Cytoplasm {ECO:0000269|PubMed:17761692}. Note=Shows a cytoplasmic distribution in the keratinocytes.
|
CATALYTIC ACTIVITY: Reaction=Cleavage of amide substrates following the basic amino acids Arg or Lys at the P1 position, with a preference for Arg over Lys.; EC=3.4.21.118; Evidence={ECO:0000269|PubMed:16337200};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.07 mM for Pro-Phe-Arg-MCA {ECO:0000269|PubMed:16337200}; KM=0.07 mM for Z-Val-Val-Arg-MCA {ECO:0000269|PubMed:16337200}; KM=0.07 mM for Boc-Val-Pro-Arg-MCA {ECO:0000269|PubMed:16337200}; KM=0.1 mM for Boc-Leu-Lys-Arg-MCA {ECO:0000269|PubMed:16337200}; KM=0.1 mM for Boc-Val-Leu-Lys-MCA {ECO:0000269|PubMed:16337200}; KM=0.07 mM for Boc-Phe-Ser-Arg-MCA {ECO:0000269|PubMed:16337200}; Vmax=7.1 umol/min/mg enzyme toward Pro-Phe-Arg-MCA {ECO:0000269|PubMed:16337200}; Vmax=5.4 umol/min/mg enzyme toward Z-Val-Val-Arg-MCA {ECO:0000269|PubMed:16337200}; Vmax=3.9 umol/min/mg enzyme toward Boc-Val-Pro-Arg-MCA {ECO:0000269|PubMed:16337200}; Vmax=2.6 umol/min/mg enzyme toward Boc-Leu-Lys-Arg-MCA {ECO:0000269|PubMed:16337200}; Vmax=1.9 umol/min/mg enzyme toward Boc-Val-Leu-Lys-MCA {ECO:0000269|PubMed:16337200}; Vmax=1.6 umol/min/mg enzyme toward Boc-Phe-Ser-Arg-MCA {ECO:0000269|PubMed:16337200};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5. Active from pH 7-10. {ECO:0000269|PubMed:16337200};
| null |
FUNCTION: Serine protease which is capable of degrading a number of proteins such as casein, fibrinogen, kininogen, fibronectin and collagen type IV. Also cleaves L1CAM in response to increased neural activity. Induces neurite outgrowth and fasciculation of cultured hippocampal neurons. Plays a role in the formation and maturation of orphan and small synaptic boutons in the Schaffer-collateral pathway, regulates Schaffer-collateral long-term potentiation in the hippocampus and is required for memory acquisition and synaptic plasticity. Involved in skin desquamation and keratinocyte proliferation. Plays a role in the secondary phase of pathogenesis following spinal cord injury. {ECO:0000269|PubMed:16337200}.
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Homo sapiens (Human)
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O60260
|
PRKN_HUMAN
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MIVFVRFNSSHGFPVEVDSDTSIFQLKEVVAKRQGVPADQLRVIFAGKELRNDWTVQNCDLDQQSIVHIVQRPWRKGQEMNATGGDDPRNAAGGCEREPQSLTRVDLSSSVLPGDSVGLAVILHTDSRKDSPPAGSPAGRSIYNSFYVYCKGPCQRVQPGKLRVQCSTCRQATLTLTQGPSCWDDVLIPNRMSGECQSPHCPGTSAEFFFKCGAHPTSDKETSVALHLIATNSRNITCITCTDVRSPVLVFQCNSRHVICLDCFHLYCVTRLNDRQFVHDPQLGYSLPCVAGCPNSLIKELHHFRILGEEQYNRYQQYGAEECVLQMGGVLCPRPGCGAGLLPEPDQRKVTCEGGNGLGCGFAFCRECKEAYHEGECSAVFEASGTTTQAYRVDERAAEQARWEAASKETIKKTTKPCPRCHVPVEKNGGCMHMKCPQPQCRLEWCWNCGCEWNRVCMGDHWFDV
|
2.3.2.31
| null |
adult locomotory behavior [GO:0008344]; aggresome assembly [GO:0070842]; amyloid fibril formation [GO:1990000]; autophagy of mitochondrion [GO:0000422]; cellular response to dopamine [GO:1903351]; cellular response to manganese ion [GO:0071287]; cellular response to oxidative stress [GO:0034599]; cellular response to toxic substance [GO:0097237]; cellular response to unfolded protein [GO:0034620]; central nervous system development [GO:0007417]; dopamine metabolic process [GO:0042417]; dopamine uptake involved in synaptic transmission [GO:0051583]; ERAD pathway [GO:0036503]; free ubiquitin chain polymerization [GO:0010994]; learning [GO:0007612]; macroautophagy [GO:0016236]; mitochondrial fission [GO:0000266]; mitochondrion organization [GO:0007005]; mitochondrion to lysosome vesicle-mediated transport [GO:0099074]; mitophagy [GO:0000423]; negative regulation by host of viral genome replication [GO:0044828]; negative regulation of actin filament bundle assembly [GO:0032232]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway [GO:1902236]; negative regulation of endoplasmic reticulum stress-induced neuron intrinsic apoptotic signaling pathway [GO:1903382]; negative regulation of exosomal secretion [GO:1903542]; negative regulation of gene expression [GO:0010629]; negative regulation of glucokinase activity [GO:0033132]; negative regulation of insulin secretion [GO:0046676]; negative regulation of intralumenal vesicle formation [GO:1905366]; negative regulation of intrinsic apoptotic signaling pathway by p53 class mediator [GO:1902254]; negative regulation of JNK cascade [GO:0046329]; negative regulation of mitochondrial fusion [GO:0010637]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway [GO:1903377]; negative regulation of primary amine oxidase activity [GO:1902283]; negative regulation of protein phosphorylation [GO:0001933]; negative regulation of reactive oxygen species metabolic process [GO:2000378]; negative regulation of release of cytochrome c from mitochondria [GO:0090201]; negative regulation of spontaneous neurotransmitter secretion [GO:1904049]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neuron cellular homeostasis [GO:0070050]; norepinephrine metabolic process [GO:0042415]; parkin-mediated stimulation of mitophagy in response to mitochondrial depolarization [GO:0061734]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of dendrite extension [GO:1903861]; positive regulation of DNA binding [GO:0043388]; positive regulation of gene expression [GO:0010628]; positive regulation of mitochondrial fission [GO:0090141]; positive regulation of mitochondrial fusion [GO:0010636]; positive regulation of mitophagy [GO:1901526]; positive regulation of mitophagy in response to mitochondrial depolarization [GO:0098779]; positive regulation of neurotransmitter uptake [GO:0051582]; positive regulation of proteasomal protein catabolic process [GO:1901800]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; positive regulation of protein binding [GO:0032092]; positive regulation of protein catabolic process [GO:0045732]; positive regulation of protein linear polyubiquitination [GO:1902530]; positive regulation of protein localization to membrane [GO:1905477]; positive regulation of retrograde transport, endosome to Golgi [GO:1905281]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of tumor necrosis factor-mediated signaling pathway [GO:1903265]; proteasomal protein catabolic process [GO:0010498]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein autoubiquitination [GO:0051865]; protein destabilization [GO:0031648]; protein K11-linked ubiquitination [GO:0070979]; protein K27-linked ubiquitination [GO:0044314]; protein K29-linked ubiquitination [GO:0035519]; protein K48-linked ubiquitination [GO:0070936]; protein K6-linked ubiquitination [GO:0085020]; protein K63-linked ubiquitination [GO:0070534]; protein localization to mitochondrion [GO:0070585]; protein monoubiquitination [GO:0006513]; protein polyubiquitination [GO:0000209]; protein stabilization [GO:0050821]; protein ubiquitination [GO:0016567]; regulation of apoptotic process [GO:0042981]; regulation of autophagy [GO:0010506]; regulation of canonical Wnt signaling pathway [GO:0060828]; regulation of cellular response to oxidative stress [GO:1900407]; regulation of dopamine metabolic process [GO:0042053]; regulation of dopamine secretion [GO:0014059]; regulation of glucose metabolic process [GO:0010906]; regulation of lipid transport [GO:0032368]; regulation of mitochondrial membrane potential [GO:0051881]; regulation of mitochondrion organization [GO:0010821]; regulation of necroptotic process [GO:0060544]; regulation of protein stability [GO:0031647]; regulation of protein targeting to mitochondrion [GO:1903214]; regulation of protein ubiquitination [GO:0031396]; regulation of reactive oxygen species metabolic process [GO:2000377]; regulation of synaptic vesicle endocytosis [GO:1900242]; regulation of synaptic vesicle transport [GO:1902803]; regulation protein catabolic process at presynapse [GO:0140251]; response to endoplasmic reticulum stress [GO:0034976]; response to oxidative stress [GO:0006979]; startle response [GO:0001964]; synaptic transmission, glutamatergic [GO:0035249]; ubiquitin-dependent protein catabolic process [GO:0006511]
|
aggresome [GO:0016235]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dopaminergic synapse [GO:0098691]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; Lewy body [GO:0097413]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; neuron projection [GO:0043005]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; Parkin-FBXW7-Cul1 ubiquitin ligase complex [GO:1990452]; perinuclear region of cytoplasm [GO:0048471]; postsynaptic density [GO:0014069]; presynapse [GO:0098793]; ubiquitin ligase complex [GO:0000151]
|
actin binding [GO:0003779]; beta-catenin binding [GO:0008013]; cullin family protein binding [GO:0097602]; enzyme binding [GO:0019899]; F-box domain binding [GO:1990444]; G protein-coupled receptor binding [GO:0001664]; heat shock protein binding [GO:0031072]; histone deacetylase binding [GO:0042826]; Hsp70 protein binding [GO:0030544]; identical protein binding [GO:0042802]; kinase binding [GO:0019900]; PDZ domain binding [GO:0030165]; phospholipase binding [GO:0043274]; protein kinase binding [GO:0019901]; protein-containing complex binding [GO:0044877]; protein-folding chaperone binding [GO:0051087]; SH3 domain binding [GO:0017124]; transcription corepressor activity [GO:0003714]; tubulin binding [GO:0015631]; ubiquitin binding [GO:0043130]; ubiquitin conjugating enzyme binding [GO:0031624]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin protein ligase binding [GO:0031625]; ubiquitin-protein transferase activity [GO:0004842]; ubiquitin-specific protease binding [GO:1990381]; zinc ion binding [GO:0008270]
|
PF00240;PF17976;PF17978;
|
1.20.120.1750;2.20.25.20;
|
RBR family, Parkin subfamily
|
PTM: ISGylated. Conjugated to ubiquitin-like protein ISG15 upon IFN-beta stimulation. ISGylation positively regulates its E3 ligase activity. {ECO:0000269|PubMed:27534820}.; PTM: Auto-ubiquitinates in an E2-dependent manner leading to its own degradation (PubMed:19229105, PubMed:23770917, PubMed:25474007). Also polyubiquitinated by RNF41 for proteasomal degradation (PubMed:19229105). {ECO:0000269|PubMed:19229105, ECO:0000269|PubMed:23770917, ECO:0000269|PubMed:25474007}.; PTM: S-nitrosylated. The inhibition of PRKN ubiquitin E3 ligase activity by S-nitrosylation could contribute to the degenerative process in PD by impairing the ubiquitination of PRKN substrates. {ECO:0000269|PubMed:15105460}.; PTM: Phosphorylated (PubMed:18957282, PubMed:23754282, PubMed:24660806, PubMed:24784582, PubMed:25474007). Activation requires phosphorylation at Ser-65 by PINK1 and binding to PINK1 phosphorylated ubiquitin (PubMed:18957282, PubMed:23754282, PubMed:24660806, PubMed:24784582, PubMed:25474007). Phosphorylation at Thr-175 by PINK1 and at Thr-217 is important for mitochondrial localization (PubMed:18957282). {ECO:0000269|PubMed:18957282, ECO:0000269|PubMed:23754282, ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:25474007}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:10319893, ECO:0000269|PubMed:16955485, ECO:0000269|PubMed:17846173, ECO:0000269|PubMed:18957282, ECO:0000269|PubMed:19029340, ECO:0000269|PubMed:19229105, ECO:0000269|PubMed:19501131, ECO:0000269|PubMed:22082830, ECO:0000269|PubMed:23620051, ECO:0000269|PubMed:23933751, ECO:0000269|PubMed:24898855}. Nucleus {ECO:0000269|PubMed:16955485}. Endoplasmic reticulum {ECO:0000269|PubMed:19501131}. Mitochondrion {ECO:0000269|PubMed:18957282, ECO:0000269|PubMed:19029340, ECO:0000269|PubMed:19229105, ECO:0000269|PubMed:20889974, ECO:0000269|PubMed:22082830, ECO:0000269|PubMed:23620051, ECO:0000269|PubMed:23754282, ECO:0000269|PubMed:23933751, ECO:0000269|PubMed:24898855}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q9WVS6}. Cell projection, neuron projection {ECO:0000269|PubMed:12925569}. Postsynaptic density {ECO:0000250|UniProtKB:Q9WVS6}. Presynapse {ECO:0000250|UniProtKB:Q9WVS6}. Note=Mainly localizes in the cytosol (PubMed:19029340, PubMed:19229105). Co-localizes with SYT11 in neutrites (PubMed:12925569). Co-localizes with SNCAIP in brainstem Lewy bodies (PubMed:10319893, PubMed:11431533). Translocates to dysfunctional mitochondria that have lost the mitochondrial membrane potential; recruitment to mitochondria is PINK1-dependent (PubMed:18957282, PubMed:19966284, PubMed:23620051, PubMed:24898855). Mitochondrial localization also gradually increases with cellular growth (PubMed:22082830). {ECO:0000269|PubMed:10319893, ECO:0000269|PubMed:11431533, ECO:0000269|PubMed:12925569, ECO:0000269|PubMed:18957282, ECO:0000269|PubMed:19029340, ECO:0000269|PubMed:19229105, ECO:0000269|PubMed:19966284, ECO:0000269|PubMed:22082830, ECO:0000269|PubMed:23620051, ECO:0000269|PubMed:24898855}.
|
CATALYTIC ACTIVITY: Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.; EC=2.3.2.31; Evidence={ECO:0000269|PubMed:23770887};
| null |
PATHWAY: Protein modification; protein ubiquitination.
| null | null |
FUNCTION: Functions within a multiprotein E3 ubiquitin ligase complex, catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins (PubMed:10888878, PubMed:10973942, PubMed:11431533, PubMed:12150907, PubMed:12628165, PubMed:15105460, PubMed:16135753, PubMed:21376232, PubMed:21532592, PubMed:22396657, PubMed:23620051, PubMed:23754282, PubMed:24660806, PubMed:24751536, PubMed:29311685, PubMed:32047033). Substrates include SYT11 and VDAC1 (PubMed:29311685, PubMed:32047033). Other substrates are BCL2, CCNE1, GPR37, RHOT1/MIRO1, MFN1, MFN2, STUB1, SNCAIP, SEPTIN5, TOMM20, USP30, ZNF746, MIRO1 and AIMP2 (PubMed:10888878, PubMed:10973942, PubMed:11431533, PubMed:12150907, PubMed:12628165, PubMed:15105460, PubMed:16135753, PubMed:21376232, PubMed:21532592, PubMed:22396657, PubMed:23620051, PubMed:23754282, PubMed:24660806, PubMed:24751536). Mediates monoubiquitination as well as 'Lys-6', 'Lys-11', 'Lys-48'-linked and 'Lys-63'-linked polyubiquitination of substrates depending on the context (PubMed:19229105, PubMed:20889974, PubMed:25474007, PubMed:25621951, PubMed:32047033). Participates in the removal and/or detoxification of abnormally folded or damaged protein by mediating 'Lys-63'-linked polyubiquitination of misfolded proteins such as PARK7: 'Lys-63'-linked polyubiquitinated misfolded proteins are then recognized by HDAC6, leading to their recruitment to aggresomes, followed by degradation (PubMed:17846173, PubMed:19229105). Mediates 'Lys-63'-linked polyubiquitination of a 22 kDa O-linked glycosylated isoform of SNCAIP, possibly playing a role in Lewy-body formation (PubMed:11431533, PubMed:11590439, PubMed:15105460, PubMed:15728840, PubMed:19229105). Mediates monoubiquitination of BCL2, thereby acting as a positive regulator of autophagy (PubMed:20889974). Protects against mitochondrial dysfunction during cellular stress, by acting downstream of PINK1 to coordinate mitochondrial quality control mechanisms that remove and replace dysfunctional mitochondrial components (PubMed:11439185, PubMed:18957282, PubMed:19029340, PubMed:19966284, PubMed:21376232, PubMed:22082830, PubMed:22396657, PubMed:23620051, PubMed:23933751, PubMed:24660806, PubMed:24784582, PubMed:24896179, PubMed:25474007, PubMed:25527291, PubMed:32047033). Depending on the severity of mitochondrial damage and/or dysfunction, activity ranges from preventing apoptosis and stimulating mitochondrial biogenesis to regulating mitochondrial dynamics and eliminating severely damaged mitochondria via mitophagy (PubMed:11439185, PubMed:19029340, PubMed:19801972, PubMed:19966284, PubMed:21376232, PubMed:22082830, PubMed:22396657, PubMed:23620051, PubMed:23933751, PubMed:24896179, PubMed:25527291, PubMed:32047033, PubMed:33499712). Activation and recruitment onto the outer membrane of damaged/dysfunctional mitochondria (OMM) requires PINK1-mediated phosphorylation of both PRKN and ubiquitin (PubMed:24660806, PubMed:24784582, PubMed:25474007, PubMed:25527291). After mitochondrial damage, functions with PINK1 to mediate the decision between mitophagy or preventing apoptosis by inducing either the poly- or monoubiquitination of VDAC1, respectively; polyubiquitination of VDAC1 promotes mitophagy, while monoubiquitination of VDAC1 decreases mitochondrial calcium influx which ultimately inhibits apoptosis (PubMed:27534820, PubMed:32047033). When cellular stress results in irreversible mitochondrial damage, promotes the autophagic degradation of dysfunctional depolarized mitochondria (mitophagy) by promoting the ubiquitination of mitochondrial proteins such as TOMM20, RHOT1/MIRO1, MFN1 and USP30 (PubMed:19029340, PubMed:19966284, PubMed:21753002, PubMed:22396657, PubMed:23620051, PubMed:23933751, PubMed:24896179, PubMed:25527291). Preferentially assembles 'Lys-6'-, 'Lys-11'- and 'Lys-63'-linked polyubiquitin chains, leading to mitophagy (PubMed:25621951, PubMed:32047033). The PINK1-PRKN pathway also promotes fission of damaged mitochondria by PINK1-mediated phosphorylation which promotes the PRKN-dependent degradation of mitochondrial proteins involved in fission such as MFN2 (PubMed:23620051). This prevents the refusion of unhealthy mitochondria with the mitochondrial network or initiates mitochondrial fragmentation facilitating their later engulfment by autophagosomes (PubMed:23620051). Regulates motility of damaged mitochondria via the ubiquitination and subsequent degradation of MIRO1 and MIRO2; in motor neurons, this likely inhibits mitochondrial intracellular anterograde transport along the axons which probably increases the chance of the mitochondria undergoing mitophagy in the soma (PubMed:22396657). Involved in mitochondrial biogenesis via the 'Lys-48'-linked polyubiquitination of transcriptional repressor ZNF746/PARIS which leads to its subsequent proteasomal degradation and allows activation of the transcription factor PPARGC1A (PubMed:21376232). Limits the production of reactive oxygen species (ROS) (PubMed:18541373). Regulates cyclin-E during neuronal apoptosis (PubMed:12628165). In collaboration with CHPF isoform 2, may enhance cell viability and protect cells from oxidative stress (PubMed:22082830). Independently of its ubiquitin ligase activity, protects from apoptosis by the transcriptional repression of p53/TP53 (PubMed:19801972). May protect neurons against alpha synuclein toxicity, proteasomal dysfunction, GPR37 accumulation, and kainate-induced excitotoxicity (PubMed:11439185). May play a role in controlling neurotransmitter trafficking at the presynaptic terminal and in calcium-dependent exocytosis. May represent a tumor suppressor gene (PubMed:12719539). {ECO:0000269|PubMed:10888878, ECO:0000269|PubMed:10973942, ECO:0000269|PubMed:11431533, ECO:0000269|PubMed:11439185, ECO:0000269|PubMed:11590439, ECO:0000269|PubMed:12150907, ECO:0000269|PubMed:12628165, ECO:0000269|PubMed:12719539, ECO:0000269|PubMed:15105460, ECO:0000269|PubMed:15728840, ECO:0000269|PubMed:16135753, ECO:0000269|PubMed:17846173, ECO:0000269|PubMed:18541373, ECO:0000269|PubMed:18957282, ECO:0000269|PubMed:19029340, ECO:0000269|PubMed:19229105, ECO:0000269|PubMed:19801972, ECO:0000269|PubMed:19966284, ECO:0000269|PubMed:20889974, ECO:0000269|PubMed:21376232, ECO:0000269|PubMed:21532592, ECO:0000269|PubMed:21753002, ECO:0000269|PubMed:22082830, ECO:0000269|PubMed:22396657, ECO:0000269|PubMed:23620051, ECO:0000269|PubMed:23754282, ECO:0000269|PubMed:23933751, ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:24896179, ECO:0000269|PubMed:25474007, ECO:0000269|PubMed:25527291, ECO:0000269|PubMed:25621951, ECO:0000269|PubMed:27534820, ECO:0000269|PubMed:29311685, ECO:0000269|PubMed:32047033, ECO:0000269|PubMed:33499712}.
|
Homo sapiens (Human)
|
O60264
|
SMCA5_HUMAN
|
MSSAAEPPPPPPPESAPSKPAASIASGGSNSSNKGGPEGVAAQAVASAASAGPADAEMEEIFDDASPGKQKEIQEPDPTYEEKMQTDRANRFEYLLKQTELFAHFIQPAAQKTPTSPLKMKPGRPRIKKDEKQNLLSVGDYRHRRTEQEEDEELLTESSKATNVCTRFEDSPSYVKWGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNWMSEFKRWVPTLRSVCLIGDKEQRAAFVRDVLLPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWSLLNFLLPDVFNSADDFDSWFDTNNCLGDQKLVERLHMVLRPFLLRRIKADVEKSLPPKKEVKIYVGLSKMQREWYTRILMKDIDILNSAGKMDKMRLLNILMQLRKCCNHPYLFDGAEPGPPYTTDMHLVTNSGKMVVLDKLLPKLKEQGSRVLIFSQMTRVLDILEDYCMWRNYEYCRLDGQTPHDERQDSINAYNEPNSTKFVFMLSTRAGGLGINLATADVVILYDSDWNPQVDLQAMDRAHRIGQTKTVRVFRFITDNTVEERIVERAEMKLRLDSIVIQQGRLVDQNLNKIGKDEMLQMIRHGATHVFASKESEITDEDIDGILERGAKKTAEMNEKLSKMGESSLRNFTMDTESSVYNFEGEDYREKQKIAFTEWIEPPKRERKANYAVDAYFREALRVSEPKAPKAPRPPKQPNVQDFQFFPPRLFELLEKEILFYRKTIGYKVPRNPELPNAAQAQKEEQLKIDEAESLNDEELEEKEKLLTQGFTNWNKRDFNQFIKANEKWGRDDIENIAREVEGKTPEEVIEYSAVFWERCNELQDIEKIMAQIERGEARIQRRISIKKALDTKIGRYKAPFHQLRISYGTNKGKNYTEEEDRFLICMLHKLGFDKENVYDELRQCIRNSPQFRFDWFLKSRTAMELQRRCNTLITLIERENMELEEKEKAEKKKRGPKPSTQKRKMDGAPDGRGRKKKLKL
|
3.6.4.-
| null |
cellular response to leukemia inhibitory factor [GO:1990830]; chromatin organization [GO:0006325]; chromatin remodeling [GO:0006338]; DNA damage response [GO:0006974]; DNA repair [GO:0006281]; DNA-templated transcription initiation [GO:0006352]; heterochromatin formation [GO:0031507]; negative regulation of mitotic chromosome condensation [GO:1905213]; negative regulation of transcription by RNA polymerase I [GO:0016479]; nucleosome assembly [GO:0006334]; positive regulation of DNA replication [GO:0045740]; positive regulation of transcription by RNA polymerase I [GO:0045943]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of transcription by RNA polymerase III [GO:0045945]; rDNA heterochromatin formation [GO:0000183]; regulation of DNA methylation [GO:0044030]; regulation of DNA replication [GO:0006275]; regulation of DNA-templated transcription [GO:0006355]; regulation of transcription by RNA polymerase II [GO:0006357]
|
ACF complex [GO:0016590]; B-WICH complex [GO:0110016]; CHRAC [GO:0008623]; chromatin silencing complex [GO:0005677]; condensed chromosome [GO:0000793]; fibrillar center [GO:0001650]; NoRC complex [GO:0090536]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; NURF complex [GO:0016589]; pericentric heterochromatin [GO:0005721]; RSF complex [GO:0031213]; site of double-strand break [GO:0035861]; WICH complex [GO:0090535]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent activity, acting on DNA [GO:0008094]; ATP-dependent chromatin remodeler activity [GO:0140658]; DNA binding [GO:0003677]; helicase activity [GO:0004386]; histone binding [GO:0042393]; histone octamer slider activity [GO:0140751]; nucleosome binding [GO:0031491]
|
PF09110;PF00271;PF09111;PF00176;
|
1.10.10.60;1.20.5.1190;1.10.1040.30;3.40.50.300;3.40.50.10810;
|
SNF2/RAD54 helicase family, ISWI subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00624, ECO:0000269|PubMed:12434153, ECO:0000269|PubMed:12972596, ECO:0000269|PubMed:15543136, ECO:0000269|PubMed:33092197}. Chromosome {ECO:0000269|PubMed:12972596, ECO:0000269|PubMed:23911928}. Note=Localizes to mitotic chromosomes (PubMed:12972596). Co-localizes with RSF1 in the nucleus (PubMed:12972596). Co-localizes with PCNA at replication foci during S phase (PubMed:15543136). Co-localizes with BAZ1B/WSTF at replication foci during late-S phase (PubMed:15543136). Recruited to DNA damage sites following interactiuon with SIRT6 (PubMed:23911928). {ECO:0000269|PubMed:12972596, ECO:0000269|PubMed:15543136, ECO:0000269|PubMed:23911928}.
| null | null | null | null | null |
FUNCTION: Helicase that possesses intrinsic ATP-dependent nucleosome-remodeling activity (PubMed:12972596, PubMed:28801535). Catalytic subunit of ISWI chromatin-remodeling complexes, which form ordered nucleosome arrays on chromatin and facilitate access to DNA during DNA-templated processes such as DNA replication, transcription, and repair; this may require intact histone H4 tails (PubMed:10880450, PubMed:12198550, PubMed:12434153, PubMed:12972596, PubMed:23911928, PubMed:28801535). Within the ISWI chromatin-remodeling complexes, slides edge- and center-positioned histone octamers away from their original location on the DNA template (PubMed:28801535). Catalytic activity and histone octamer sliding propensity is regulated and determined by components of the ISWI chromatin-remodeling complexes (PubMed:28801535). The BAZ1A/ACF1-, BAZ1B/WSTF-, BAZ2A/TIP5- and BAZ2B-containing ISWI chromatin-remodeling complexes regulate the spacing of nucleosomes along the chromatin and have the ability to slide mononucleosomes to the center of a DNA template in an ATP-dependent manner (PubMed:14759371, PubMed:15543136, PubMed:28801535). The CECR2- and RSF1-containing ISWI chromatin-remodeling complexes do not have the ability to slide mononucleosomes to the center of a DNA template (PubMed:28801535). Binds to core histones together with RSF1, and is required for the assembly of regular nucleosome arrays by the RSF-5 ISWI chromatin-remodeling complex (PubMed:12972596). Involved in DNA replication and together with BAZ1A/ACF1 is required for replication of pericentric heterochromatin in S-phase (PubMed:12434153). Probably plays a role in repression of RNA polymerase I dependent transcription of the rDNA locus, through the recruitment of the SIN3/HDAC1 corepressor complex to the rDNA promoter (By similarity). Essential component of the WICH-5 ISWI chromatin-remodeling complex (also called the WICH complex), a chromatin-remodeling complex that mobilizes nucleosomes and reconfigures irregular chromatin to a regular nucleosomal array structure (PubMed:11980720, PubMed:15543136). The WICH-5 ISWI chromatin-remodeling complex regulates the transcription of various genes, has a role in RNA polymerase I transcription (By similarity). Within the B-WICH complex has a role in RNA polymerase III transcription (PubMed:16603771). Mediates the histone H2AX phosphorylation at 'Tyr-142', and is involved in the maintenance of chromatin structures during DNA replication processes (By similarity). Essential component of NoRC-5 ISWI chromatin-remodeling complex, a complex that mediates silencing of a fraction of rDNA by recruiting histone-modifying enzymes and DNA methyltransferases, leading to heterochromatin formation and transcriptional silencing (By similarity). {ECO:0000250|UniProtKB:Q91ZW3, ECO:0000269|PubMed:10880450, ECO:0000269|PubMed:11980720, ECO:0000269|PubMed:12198550, ECO:0000269|PubMed:12434153, ECO:0000269|PubMed:12972596, ECO:0000269|PubMed:14759371, ECO:0000269|PubMed:15543136, ECO:0000269|PubMed:16603771, ECO:0000269|PubMed:23911928, ECO:0000269|PubMed:28801535}.
|
Homo sapiens (Human)
|
O60266
|
ADCY3_HUMAN
|
MPRNQGFSEPEYSAEYSAEYSVSLPSDPDRGVGRTHEISVRNSGSCLCLPRFMRLTFVPESLENLYQTYFKRQRHETLLVLVVFAALFDCYVVVMCAVVFSSDKLASLAVAGIGLVLDIILFVLCKKGLLPDRVTRRVLPYVLWLLITAQIFSYLGLNFARAHAASDTVGWQVFFVFSFFITLPLSLSPIVIISVVSCVVHTLVLGVTVAQQQQEELKGMQLLREILANVFLYLCAIAVGIMSYYMADRKHRKAFLEARQSLEVKMNLEEQSQQQENLMLSILPKHVADEMLKDMKKDESQKDQQQFNTMYMYRHENVSILFADIVGFTQLSSACSAQELVKLLNELFARFDKLAAKYHQLRIKILGDCYYCICGLPDYREDHAVCSILMGLAMVEAISYVREKTKTGVDMRVGVHTGTVLGGVLGQKRWQYDVWSTDVTVANKMEAGGIPGRVHISQSTMDCLKGEFDVEPGDGGSRCDYLEEKGIETYLIIASKPEVKKTATQNGLNGSALPNGAPASSKSSSPALIETKEPNGSAHSSGSTSEKPEEQDAQADNPSFPNPRRRLRLQDLADRVVDASEDEHELNQLLNEALLERESAQVVKKRNTFLLSMRFMDPEMETRYSVEKEKQSGAAFSCSCVVLLCTALVEILIDPWLMTNYVTFMVGEILLLILTICSLAAIFPRAFPKKLVAFSTWIDRTRWARNTWAMLAIFILVMANVVDMLSCLQYYTGPSNATAGMETEGSCLENPKYYNYVAVLSLIATIMLVQVSHMVKLTLMLLVAGAVATINLYAWRPVFDEYDHKRFREHDLPMVALEQMQGFNPGLNGTDRLPLVPSKYSMTVMVFLMMLSFYYFSRHVEKLARTLFLWKIEVHDQKERVYEMRRWNEALVTNMLPEHVARHFLGSKKRDEELYSQTYDEIGVMFASLPNFADFYTEESINNGGIECLRFLNEIISDFDSLLDNPKFRVITKIKTIGSTYMAASGVTPDVNTNGFASSNKEDKSERERWQHLADLADFALAMKDTLTNINNQSFNNFMLRIGMNKGGVLAGVIGARKPHYDIWGNTVNVASRMESTGVMGNIQVVEETQVILREYGFRFVRRGPIFVKGKGELLTFFLKGRDKLATFPNGPSVTLPHQVVDNS
|
4.6.1.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P30803}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P30803}; Note=Binds 2 magnesium ions per subunit. Is also active with manganese (in vitro). {ECO:0000250|UniProtKB:P30803};
|
acrosome reaction [GO:0007340]; adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; cAMP biosynthetic process [GO:0006171]; cellular response to forskolin [GO:1904322]; flagellated sperm motility [GO:0030317]; intracellular signal transduction [GO:0035556]; olfactory learning [GO:0008355]; sensory perception of smell [GO:0007608]; signal transduction [GO:0007165]; single fertilization [GO:0007338]
|
ciliary membrane [GO:0060170]; cilium [GO:0005929]; cytoplasm [GO:0005737]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; plasma membrane [GO:0005886]
|
adenylate cyclase activity [GO:0004016]; ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; metal ion binding [GO:0046872]
|
PF16214;PF00211;
|
3.30.70.1230;
|
Adenylyl cyclase class-4/guanylyl cyclase family
|
PTM: Sumoylated. Sumoylation is required for targeting ot olfactory cilia. {ECO:0000250|UniProtKB:P21932}.; PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q8VHH7}.; PTM: Rapidly phosphorylated after stimulation by odorants or forskolin. Phosphorylation by CaMK2 at Ser-1076 down-regulates enzyme activity. {ECO:0000250|UniProtKB:Q8VHH7}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11549699}; Multi-pass membrane protein {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:11549699}. Cell projection, cilium {ECO:0000250|UniProtKB:Q8VHH7}. Golgi apparatus {ECO:0000250|UniProtKB:P21932}. Note=Also detected in the cytoplasm, close to lipid droplets. {ECO:0000269|PubMed:11549699}.
|
CATALYTIC ACTIVITY: Reaction=ATP = 3',5'-cyclic AMP + diphosphate; Xref=Rhea:RHEA:15389, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58165; EC=4.6.1.1; Evidence={ECO:0000250|UniProtKB:Q8VHH7};
| null | null | null | null |
FUNCTION: Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling. Participates in signaling cascades triggered by odorant receptors via its function in cAMP biosynthesis. Required for the perception of odorants. Required for normal sperm motility and normal male fertility. Plays a role in regulating insulin levels and body fat accumulation in response to a high fat diet. {ECO:0000250|UniProtKB:Q8VHH7}.
|
Homo sapiens (Human)
|
O60269
|
GRIN2_HUMAN
|
MSSSRPEPGPWAPLSPRLQPLSQSSSSLLGEGREQRPELRKTASSTVWQAQLGEASTRPQAPEEEGNPPESMKPARASGPKARPSAGGHWWSSTVGNVSTMGGSDLCRLRAPSAAAMQRSHSDLVRSTQMRGHSGARKASLSCSALGSSPVHRAQLQPGGTSGQGGQAPAGLERDLAPEDETSNSAWMLGASQLSVPPLDLGDTTAHSSSAQAEPKAAEQLATTTCHALPPAALLCGMREVRAGGCCHALPATGILAFPKLVASVSESGLQAQHGVKIHCRLSGGLPGHSHCCAHLWGPAGLVPEPGSRTKDVWTMTSANDLAPAEASPLSAQDAGVQAAPVAACKAVATSPSLEAPAALHVFPEVTLGSSLEEVPSPVRDVRWDAEGMTWEVYGAAVDLEVLGVAIQKHLEMQFEQLQRAPASEDSLSVEGRRGPLRAVMQSLRRPSCCGCSGAAPE
| null | null |
neuron projection development [GO:0031175]
|
plasma membrane [GO:0005886]
| null |
PF15235;
| null | null | null | null | null | null | null | null | null |
FUNCTION: May be involved in neurite outgrowth. {ECO:0000269|PubMed:10480904}.
|
Homo sapiens (Human)
|
O60271
|
JIP4_HUMAN
|
MELEDGVVYQEEPGGSGAVMSERVSGLAGSIYREFERLIGRYDEEVVKELMPLVVAVLENLDSVFAQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFEDSQEQEKKDLQTRVESLESQTRQLELKAKNYADQISRLEEREAELKKEYNALHQRHTEMIHNYMEHLERTKLHQLSGSDQLESTAHSRIRKERPISLGIFPLPAGDGLLTPDAQKGGETPGSEQWKFQELSQPRSHTSLKVSNSPEPQKAVEQEDELSDVSQGGSKATTPASTANSDVATIPTDTPLKEENEGFVKVTDAPNKSEISKHIEVQVAQETRNVSTGSAENEEKSEVQAIIESTPELDMDKDLSGYKGSSTPTKGIENKAFDRNTESLFEELSSAGSGLIGDVDEGADLLGMGREVENLILENTQLLETKNALNIVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEEKNRELEEELRKARAEAEDARQKAKDDDDSDIPTAQRKRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASRENPAMQEKKRSSIWQFFSRLFSSSSNTTKKPEPPVNLKYNAPTSHVTPSVKKRSSTLSQLPGDKSKAFDFLSEETEASLASRREQKREQYRQVKAHVQKEDGRVQAFGWSLPQKYKQVTNGQGENKMKNLPVPVYLRPLDEKDTSMKLWCAVGVNLSGGKTRDGGSVVGASVFYKDVAGLDTEGSKQRSASQSSLDKLDQELKEQQKELKNQEELSSLVWICTSTHSATKVLIIDAVQPGNILDSFTVCNSHVLCIASVPGARETDYPAGEDLSESGQVDKASLCGSMTSNSSAETDSLLGGITVVGCSAEGVTGAATSPSTNGASPVMDKPPEMEAENSEVDENVPTAEEATEATEGNAGSAEDTVDISQTGVYTEHVFTDPLGVQIPEDLSPVYQSSNDSDAYKDQISVLPNEQDLVREEAQKMSSLLPTMWLGAQNGCLYVHSSVAQWRKCLHSIKLKDSILSIVHVKGIVLVALADGTLAIFHRGVDGQWDLSNYHLLDLGRPHHSIRCMTVVHDKVWCGYRNKIYVVQPKAMKIEKSFDAHPRKESQVRQLAWVGDGVWVSIRLDSTLRLYHAHTYQHLQDVDIEPYVSKMLGTGKLGFSFVRITALMVSCNRLWVGTGNGVIISIPLTETNKTSGVPGNRPGSVIRVYGDENSDKVTPGTFIPYCSMAHAQLCFHGHRDAVKFFVAVPGQVISPQSSSSGTDLTGDKAGPSAQEPGSQTPLKSMLVISGGEGYIDFRMGDEGGESELLGEDLPLEPSVTKAERSHLIVWQVMYGNE
| null | null |
lysosome localization [GO:0032418]; negative regulation of dendrite extension [GO:1903860]; negative regulation of neuron differentiation [GO:0045665]; negative regulation of protein phosphorylation [GO:0001933]; positive regulation of cell migration [GO:0030335]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of neuron differentiation [GO:0045666]; retrograde transport, endosome to Golgi [GO:0042147]; striated muscle cell differentiation [GO:0051146]; vesicle-mediated transport [GO:0016192]
|
acrosomal vesicle [GO:0001669]; centriolar satellite [GO:0034451]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; lysosomal membrane [GO:0005765]; perinuclear region of cytoplasm [GO:0048471]
|
identical protein binding [GO:0042802]; JUN kinase binding [GO:0008432]; kinesin binding [GO:0019894]; MAP-kinase scaffold activity [GO:0005078]; signaling receptor complex adaptor activity [GO:0030159]
|
PF16471;PF09744;PF19056;
|
1.20.58.1770;1.20.5.1000;2.130.10.10;
|
JIP scaffold family
|
PTM: Phosphorylated by MAPK8 and MAPK14. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q58A65}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q58A65}. Lysosome membrane {ECO:0000269|PubMed:29146937}. Note=Perinuclear distribution in response to stress signals such as UV radiation. {ECO:0000250|UniProtKB:Q58A65}.; SUBCELLULAR LOCATION: [Isoform 5]: Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:15693750}. Note=Associated with the plasma membrane of the acrosomal compartment and also localizes in the acrosome matrix. {ECO:0000269|PubMed:15693750}.
| null | null | null | null | null |
FUNCTION: The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module (PubMed:14743216). Regulates lysosomal positioning by acting as an adapter protein which links PIP4P1-positive lysosomes to the dynein-dynactin complex (PubMed:29146937). Assists PIKFYVE selective functionality in microtubule-based endosome-to-TGN trafficking (By similarity). {ECO:0000250|UniProtKB:Q58A65, ECO:0000269|PubMed:14743216, ECO:0000269|PubMed:29146937}.
|
Homo sapiens (Human)
|
O60281
|
ZN292_HUMAN
|
MADEEAEQERLSCGEGGCVAELQRLGERLQELELQLRESRVPAVEAATDYCQQLCQTLLEYAEKWKTSEDPLPLLEVYTVAIQSYVKARPYLTSECENVALVLERLALSCVELLLCLPVELSDKQWEQFQTLVQVAHEKLMENGSCELHFLATLAQETGVWKNPVLCTILSQEPLDKDKVNEFLAFEGPILLDMRIKHLIKTNQLSQATALAKLCSDHPEIGIKGSFKQTYLVCLCTSSPNGKLIEEISEVDCKDALEMICNLESEGDEKSALVLCTAFLSRQLQQGDMYCAWELTLFWSKLQQRVEPSIQVYLERCRQLSLLTKTVYHIFFLIKVINSETEGAGLATCIELCVKALRLESTENTEVKISICKTISCLLPDDLEVKRACQLSEFLIEPTVDAYYAVEMLYNQPDQKYDEENLPIPNSLRCELLLVLKTQWPFDPEFWDWKTLKRQCLALMGEEASIVSSIDELNDSEVYEKVVDYQEESKETSMNGLSGGVGANSGLLKDIGDEKQKKREIKQLRERGFISARFRNWQAYMQYCVLCDKEFLGHRIVRHAQKHYKDGIYSCPICAKNFNSKETFVPHVTLHVKQSSKERLAAMKPLRRLGRPPKITTTNENQKTNTVAKQEQRPIKKNSLYSTDFIVFNDNDGSDDENDDKDKSYEPEVIPVQKPVPVNEFNCPVTFCKKGFKYFKNLIAHVKGHKDNEDAKRFLEMQSKKVICQYCRRHFVSVTHLNDHLQMHCGSKPYICIQMKCKAGFNSYAELLTHRKEHQVFRAKCMFPKCGRIFSEAYLLYDHEAQHYNTYTCKFTGCGKVYRSQGELEKHLDDHSTPPEKVLPPEAQLNSSGDSIQPSEVNQNTAENIEKERSMLPSENNIENSLLADRSDAWDKSKAESAVTKQDQISASELRQANGPLSNGLENPATTPLLQSSEVAVSIKVSLNQGIEDNFGKQENSTVEGSGEALVTDLHTPVEDTCNDLCHPGFQERKEQDCFNDAHVTQNSLVNSETLKIGDLTPQNLERQVNNLMTFSVQNQAAFQNNLPTSKFECGDNVKTSSNLYNLPLKTLESIAFVPPQSDLSNSLGTPSVPPKAPVQKFSCQVEGCTRTYNSSQSIGKHMKTAHPDQYAAFKMQRKSKKGQKANNLNTPNNGKFVYFLPSPVNSSNPFFTSQTKANGNPACSAQLQHVSPPIFPAHLASVSTPLLSSMESVINPNITSQDKNEQGGMLCSQMENLPSTALPAQMEDLTKTVLPLNIDSGSDPFLPLPAESSSMSLFPSPADSGTNSVFSQLENNTNHYSSQIEGNTNSSFLKGGNGENAVFPSQVNVANNFSSTNAQQSAPEKVKKDRGRGPNGKERKPKHNKRAKWPAIIRDGKFICSRCYRAFTNPRSLGGHLSKRSYCKPLDGAEIAQELLQSNGQPSLLASMILSTNAVNLQQPQQSTFNPEACFKDPSFLQLLAENRSPAFLPNTFPRSGVTNFNTSVSQEGSEIIKQALETAGIPSTFEGAEMLSHVSTGCVSDASQVNATVMPNPTVPPLLHTVCHPNTLLTNQNRTSNSKTSSIEECSSLPVFPTNDLLLKTVENGLCSSSFPNSGGPSQNFTSNSSRVSVISGPQNTRSSHLNKKGNSASKRRKKVAPPLIAPNASQNLVTSDLTTMGLIAKSVEIPTTNLHSNVIPTCEPQSLVENLTQKLNNVNNQLFMTDVKENFKTSLESHTVLAPLTLKTENGDSQMMALNSCTTSINSDLQISEDNVIQNFEKTLEIIKTAMNSQILEVKSGSQGAGETSQNAQINYNIQLPSVNTVQNNKLPDSSPFSSFISVMPTKSNIPQSEVSHKEDQIQEILEGLQKLKLENDLSTPASQCVLINTSVTLTPTPVKSTADITVIQPVSEMINIQFNDKVNKPFVCQNQGCNYSAMTKDALFKHYGKIHQYTPEMILEIKKNQLKFAPFKCVVPTCTKTFTRNSNLRAHCQLVHHFTTEEMVKLKIKRPYGRKSQSENVPASRSTQVKKQLAMTEENKKESQPALELRAETQNTHSNVAVIPEKQLVEKKSPDKTESSLQVITVTSEQCNTNALTNTQTKGRKIRRHKKEKEEKKRKKPVSQSLEFPTRYSPYRPYRCVHQGCFAAFTIQQNLILHYQAVHKSDLPAFSAEVEEESEAGKESEETETKQTLKEFRCQVSDCSRIFQAITGLIQHYMKLHEMTPEEIESMTASVDVGKFPCDQLECKSSFTTYLNYVVHLEADHGIGLRASKTEEDGVYKCDCEGCDRIYATRSNLLRHIFNKHNDKHKAHLIRPRRLTPGQENMSSKANQEKSKSKHRGTKHSRCGKEGIKMPKTKRKKKNNLENKNAKIVQIEENKPYSLKRGKHVYSIKARNDALSECTSRFVTQYPCMIKGCTSVVTSESNIIRHYKCHKLSKAFTSQHRNLLIVFKRCCNSQVKETSEQEGAKNDVKDSDTCVSESNDNSRTTATVSQKEVEKNEKDEMDELTELFITKLINEDSTSVETQANTSSNVSNDFQEDNLCQSERQKASNLKRVNKEKNVSQNKKRKVEKAEPASAAELSSVRKEEETAVAIQTIEEHPASFDWSSFKPMGFEVSFLKFLEESAVKQKKNTDKDHPNTGNKKGSHSNSRKNIDKTAVTSGNHVCPCKESETFVQFANPSQLQCSDNVKIVLDKNLKDCTELVLKQLQEMKPTVSLKKLEVHSNDPDMSVMKDISIGKATGRGQY
| null | null |
regulation of transcription by RNA polymerase II [GO:0006357]
|
nucleus [GO:0005634]
|
DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]
|
PF00096;
|
3.30.160.60;
|
Krueppel C2H2-type zinc-finger protein family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: May be involved in transcriptional regulation.
|
Homo sapiens (Human)
|
O60282
|
KIF5C_HUMAN
|
MADPAECSIKVMCRFRPLNEAEILRGDKFIPKFKGDETVVIGQGKPYVFDRVLPPNTTQEQVYNACAKQIVKDVLEGYNGTIFAYGQTSSGKTHTMEGKLHDPQLMGIIPRIAHDIFDHIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLAVHEDKNRVPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIKQENVETEKKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTKTHVPYRDSKMTRILQDSLGGNCRTTIVICCSPSVFNEAETKSTLMFGQRAKTIKNTVSVNLELTAEEWKKKYEKEKEKNKTLKNVIQHLEMELNRWRNGEAVPEDEQISAKDQKNLEPCDNTPIIDNIAPVVAGISTEEKEKYDEEISSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQALEELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKRATEILNLLLKDLGEIGGIIGTNDVKTLADVNGVIEEEFTMARLYISKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQDAEEMKKALEQQMESHREAHQKQLSRLRDEIEEKQKIIDEIRDLNQKLQLEQEKLSSDYNKLKIEDQEREMKLEKLLLLNDKREQAREDLKGLEETVSRELQTLHNLRKLFVQDLTTRVKKSVELDNDDGGGSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENAMRDRKRYQQEVDRIKEAVRAKNMARRAHSAQIAKPIRPGHYPASSPTAVHAIRGGGGSSSNSTHYQK
|
3.6.4.-
| null |
anterograde axonal protein transport [GO:0099641]; anterograde dendritic transport of messenger ribonucleoprotein complex [GO:0098964]; anterograde dendritic transport of neurotransmitter receptor complex [GO:0098971]; axon guidance [GO:0007411]; intracellular mRNA localization [GO:0008298]; mitotic cell cycle [GO:0000278]; motor neuron axon guidance [GO:0008045]; mRNA transport [GO:0051028]; organelle organization [GO:0006996]; synaptic vesicle transport [GO:0048489]
|
axon cytoplasm [GO:1904115]; axonal growth cone [GO:0044295]; ciliary rootlet [GO:0035253]; dendrite cytoplasm [GO:0032839]; distal axon [GO:0150034]; kinesin complex [GO:0005871]; microtubule [GO:0005874]; neuronal cell body [GO:0043025]; postsynaptic cytosol [GO:0099524]
|
apolipoprotein receptor binding [GO:0034190]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; microtubule binding [GO:0008017]; microtubule motor activity [GO:0003777]; plus-end-directed microtubule motor activity [GO:0008574]
|
PF00225;
|
6.10.250.1590;3.40.850.10;
|
TRAFAC class myosin-kinesin ATPase superfamily, Kinesin family, Kinesin subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. Cell projection, dendrite {ECO:0000269|PubMed:24812067}. Note=Abundant in distal regions of dendrites. {ECO:0000269|PubMed:24812067}.
|
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; Evidence={ECO:0000250|UniProtKB:P56536};
| null | null | null | null |
FUNCTION: Microtubule-associated force-producing protein that may play a role in organelle transport. Has ATPase activity (By similarity). Involved in synaptic transmission (PubMed:24812067). Mediates dendritic trafficking of mRNAs (By similarity). Required for anterograde axonal transportation of MAPK8IP3/JIP3 which is essential for MAPK8IP3/JIP3 function in axon elongation (By similarity). {ECO:0000250|UniProtKB:P28738, ECO:0000250|UniProtKB:P56536, ECO:0000269|PubMed:24812067}.
|
Homo sapiens (Human)
|
O60284
|
ST18_HUMAN
|
MDAEAEDKTLRTRSKGTEVPMDSLIQELSVAYDCSMAKKRTAEDQALGVPVNKRKSLLMKPRHYSPKADCQEDRSDRTEDDGPLETHGHSTAEEIMIKPMDESLLSTAQENSSRKEDRYSCYQELMVKSLMHLGKFEKNVSVQTVSENLNDSGIQSLKAESDEADECFLIHSDDGRDKIDDSQPPFCSSDDNESNSESAENGWDSGSNFSEETKPPRVPKYVLTDHKKDLLEVPEIKTEGDKFIPCENRCDSETERKDPQNALAEPLDGNAQPSFPDVEEEDSESLAVMTEEGSDLEKAKGNLSLLEQAIALQAERGCVFHNTYKELDRFLLEHLAGERRQTKVIDMGGRQIFNNKHSPRPEKRETKCPIPGCDGTGHVTGLYPHHRSLSGCPHKVRVPLEILAMHENVLKCPTPGCTGRGHVNSNRNTHRSLSGCPIAAAEKLAMSQDKNQLDSPQTGQCPDQAHRTSLVKQIEFNFPSQAITSPRATVSKEQEKFGKVPFDYASFDAQVFGKRPLIQTVQGRKTPPFPESKHFPNPVKFPNRLPSAGAHTQSPGRASSYSYGQCSEDTHIAAAAAILNLSTRCREATDILSNKPQSLHAKGAEIEVDENGTLDLSMKKNRILDKSAPLTSSNTSIPTPSSSPFKTSSILVNAAFYQALCDQEGWDTPINYSKTHGKTEEEKEKDPVSSLENLEEKKFPGEASIPSPKPKLHARDLKKELITCPTPGCDGSGHVTGNYASHRSVSGCPLADKTLKSLMAANSQELKCPTPGCDGSGHVTGNYASHRSLSGCPRARKGGVKMTPTKEEKEDPELKCPVIGCDGQGHISGKYTSHRTASGCPLAAKRQKENPLNGASLSWKLNKQELPHCPLPGCNGLGHVNNVFVTHRSLSGCPLNAQVIKKGKVSEELMTIKLKATGGIESDEEIRHLDEEIKELNESNLKIEADMMKLQTQITSMESNLKTIEEENKLIEQNNESLLKELAGLSQALISSLADIQLPQMGPISEQNFEAYVNTLTDMYSNLERDYSPECKALLESIKQAVKGIHV
| null | null |
interleukin-1-mediated signaling pathway [GO:0070498]; interleukin-6-mediated signaling pathway [GO:0070102]; negative regulation of cell population proliferation [GO:0008285]; positive regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway [GO:2001269]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of gene expression [GO:0010468]; tumor necrosis factor-mediated signaling pathway [GO:0033209]
|
chromatin [GO:0000785]; nucleus [GO:0005634]; protein-DNA complex [GO:0032993]
|
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; zinc ion binding [GO:0008270]
|
PF08474;PF01530;
|
4.10.320.30;
|
MYT1 family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15489893}.
| null | null | null | null | null |
FUNCTION: Repressor that binds to DNA sequences containing a bipartite element consisting of a direct repeat of the sequence 5'-AAAGTTT-3' separated by 2-9 nucleotides. Represses basal transcription activity from target promoters (By similarity). Inhibits colony formation in cultured breast cancer cells. {ECO:0000250, ECO:0000269|PubMed:15489893}.
|
Homo sapiens (Human)
|
O60285
|
NUAK1_HUMAN
|
MEGAAAPVAGDRPDLGLGAPGSPREAVAGATAALEPRKPHGVKRHHHKHNLKHRYELQETLGKGTYGKVKRATERFSGRVVAIKSIRKDKIKDEQDMVHIRREIEIMSSLNHPHIISIYEVFENKDKIVIIMEYASKGELYDYISERRRLSERETRHFFRQIVSAVHYCHKNGVVHRDLKLENILLDDNCNIKIADFGLSNLYQKDKFLQTFCGSPLYASPEIVNGRPYRGPEVDSWALGVLLYTLVYGTMPFDGFDHKNLIRQISSGEYREPTQPSDARGLIRWMLMVNPDRRATIEDIANHWWVNWGYKSSVCDCDALHDSESPLLARIIDWHHRSTGLQADTEAKMKGLAKPTTSEVMLERQRSLKKSKKENDFAQSGQDAVPESPSKLSSKRPKGILKKRSNSEHRSHSTGFIEGVVGPALPSTFKMEQDLCRTGVLLPSSPEAEVPGKLSPKQSATMPKKGILKKTQQRESGYYSSPERSESSELLDSNDVMGSSIPSPSPPDPARVTSHSLSCRRKGILKHSSKYSAGTMDPALVSPEMPTLESLSEPGVPAEGLSRSYSRPSSVISDDSVLSSDSFDLLDLQENRPARQRIRSCVSAENFLQIQDFEGLQNRPRPQYLKRYRNRLADSSFSLLTDMDDVTQVYKQALEICSKLN
|
2.7.11.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
|
cell adhesion [GO:0007155]; DNA damage response [GO:0006974]; intracellular signal transduction [GO:0035556]; protein phosphorylation [GO:0006468]; regulation of cell adhesion [GO:0030155]; regulation of cell population proliferation [GO:0042127]; regulation of cellular senescence [GO:2000772]; regulation of myosin-light-chain-phosphatase activity [GO:0035507]; regulation of signal transduction by p53 class mediator [GO:1901796]
|
cytoplasm [GO:0005737]; fibrillar center [GO:0001650]; microtubule cytoskeleton [GO:0015630]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; p53 binding [GO:0002039]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, CAMK Ser/Thr protein kinase family, SNF1 subfamily
|
PTM: Ubiquitinated with 'Lys-29'- and 'Lys-33'-linked polyubiquitins which appear to impede LKB1-mediated phosphorylation. Deubiquitinated by USP9X. {ECO:0000269|PubMed:18254724}.; PTM: Phosphorylated at Thr-211 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39. Not dephosphorylated by the myosin PP1 complex when regulating its activity, due to the presence of PPP1R12A, which prevents myosin PP1 from dephosphorylating NUAK1. Phosphorylated by STK38L upon stimulation with IGF1. {ECO:0000269|PubMed:14976552, ECO:0000269|PubMed:20354225}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21317932}. Cytoplasm {ECO:0000269|PubMed:21317932}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
| null | null | null | null |
FUNCTION: Serine/threonine-protein kinase involved in various processes such as cell adhesion, regulation of cell ploidy and senescence, cell proliferation and tumor progression. Phosphorylates ATM, CASP6, LATS1, PPP1R12A and p53/TP53. Acts as a regulator of cellular senescence and cellular ploidy by mediating phosphorylation of 'Ser-464' of LATS1, thereby controlling its stability. Controls cell adhesion by regulating activity of the myosin protein phosphatase 1 (PP1) complex. Acts by mediating phosphorylation of PPP1R12A subunit of myosin PP1: phosphorylated PPP1R12A then interacts with 14-3-3, leading to reduced dephosphorylation of myosin MLC2 by myosin PP1. May be involved in DNA damage response: phosphorylates p53/TP53 at 'Ser-15' and 'Ser-392' and is recruited to the CDKN1A/WAF1 promoter to participate in transcription activation by p53/TP53. May also act as a tumor malignancy-associated factor by promoting tumor invasion and metastasis under regulation and phosphorylation by AKT1. Suppresses Fas-induced apoptosis by mediating phosphorylation of CASP6, thereby suppressing the activation of the caspase and the subsequent cleavage of CFLAR. Regulates UV radiation-induced DNA damage response mediated by CDKN1A. In association with STK11, phosphorylates CDKN1A in response to UV radiation and contributes to its degradation which is necessary for optimal DNA repair (PubMed:25329316). {ECO:0000269|PubMed:12409306, ECO:0000269|PubMed:14976552, ECO:0000269|PubMed:15060171, ECO:0000269|PubMed:15273717, ECO:0000269|PubMed:19927127, ECO:0000269|PubMed:20354225, ECO:0000269|PubMed:21317932, ECO:0000269|PubMed:25329316}.
|
Homo sapiens (Human)
|
O60291
|
MGRN1_HUMAN
|
MGSILSRRIAGVEDIDIQANSAYRYPPKSGNYFASHFFMGGEKFDTPHPEGYLFGENMDLNFLGSRPVQFPYVTPAPHEPVKTLRSLVNIRKDSLRLVRYKDDADSPTEDGDKPRVLYSLEFTFDADARVAITIYCQASEEFLNGRAVYSPKSPSLQSETVHYKRGVSQQFSLPSFKIDFSEWKDDELNFDLDRGVFPVVIQAVVDEGDVVEVTGHAHVLLAAFEKHMDGSFSVKPLKQKQIVDRVSYLLQEIYGIENKNNQETKPSDDENSDNSNECVVCLSDLRDTLILPCRHLCLCTSCADTLRYQANNCPICRLPFRALLQIRAVRKKPGALSPVSFSPVLAQSLEHDEHSCPFKKSKPHPASLASKKPKRETNSDSVPPGYEPISLLEALNGLRAVSPAIPSAPLYEEITYSGISDGLSQASCPLAAIDHILDSSRQKGRPQSKAPDSTLRSPSSPIHEEDEEKLSEDVDAPPPLGGAELALRESSSPESFITEEVDESSSPQQGTRAASIENVLQDSSPEHCGRGPPADIYLPALGPDSCSVGIDE
|
2.3.2.27
| null |
endosome to lysosome transport [GO:0008333]; negative regulation of cAMP-mediated signaling [GO:0043951]; negative regulation of G protein-coupled receptor signaling pathway [GO:0045744]; negative regulation of smoothened signaling pathway [GO:0045879]; protein monoubiquitination [GO:0006513]; protein polyubiquitination [GO:0000209]; protein ubiquitination [GO:0016567]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; early endosome [GO:0005769]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
metal ion binding [GO:0046872]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]
|
PF13920;
|
3.30.40.10;
| null |
PTM: Autoubiquitinated in vitro. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Early endosome {ECO:0000269|PubMed:17229889, ECO:0000269|PubMed:19737927}. Note=The endosomal localization is dependent on the interaction with TSG101.; SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm, cytosol. Nucleus. Note=Translocation from the cytosol to the nucleus is seen only in the presence of MC1R and MC4R, but not TBXA2R. Excluded from nucleoli.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytosol. Nucleus. Note=Translocation from the cytosol to the nucleus is seen only in the presence of MC1R and MC4R, but not TBXA2R. Excluded from nucleoli.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm, cytosol. Cell membrane.; SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm, cytosol. Cell membrane.
|
CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27;
| null |
PATHWAY: Protein modification; protein ubiquitination.
| null | null |
FUNCTION: E3 ubiquitin-protein ligase. Mediates monoubiquitination at multiple sites of TSG101 in the presence of UBE2D1, but not of UBE2G1, nor UBE2H. Plays a role in the regulation of endosome-to-lysosome trafficking. Impairs MC1R- and MC4R-signaling by competing with GNAS-binding to MCRs and inhibiting agonist-induced cAMP production. Does not inhibit ADRB2-signaling. Does not promote MC1R ubiquitination. Acts also as a negative regulator of hedgehog signaling (By similarity). {ECO:0000250|UniProtKB:Q9D074, ECO:0000269|PubMed:17229889, ECO:0000269|PubMed:19703557, ECO:0000269|PubMed:19737927}.
|
Homo sapiens (Human)
|
O60292
|
SI1L3_HUMAN
|
MTTYRAIPSDGVDLAASCGARVGDVLPGPHTGDYAPLGFWAQNGSMSQPLGESPATATATATATTRPSPTTPAMPKMGVRARVADWPPKREALREHSNPSPSQDTDGTKATKMAHSMRSIQNGQPPTSTPASSGSKAFHRLSRRRSKDVEFQDGWPRSPGRAFLPLRHRSSSEITLSECDAEDAGEPRGARHTGALPLFREYGSTSSIDVQGMPEQSFFDILNEFRSEQPDARGCQALTELLRADPGPHLMGGGGGAKGDSHNGQPAKDSLLPLQPTKEKEKARKKPARGLGGGDTVDSSIFRKLRSSKPEGEAGRSPGEADEGRSPPEASRPWVCQKSFAHFDVQSMLFDLNEAAANRVSVSQRRNTTTGASAASAASAMASLTASRAHSLGGLDPAFTSTEDLNCKENLEQDLGDDNSNDLLLSCPHFRNEIGGECERNVSFSRASVGSPSSGEGHLAEPALSAYRTNASISVLEVPKEQQRTQSRPRQYSIEHVDLGARYYQDYFVGKEHANYFGVDEKLGPVAVSIKREKLEDHKEHGPQYQYRIIFRTRELITLRGSILEDATPTATKHGTGRGLPLKDALEYVIPELNIHCLRLALNTPKVTEQLLKLDEQGLCRKHKVGILYCKAGQSSEEEMYNNEEAGPAFEEFLSLIGEKVCLKGFTKYAAQLDVKTDSTGTHSLYTMYQDYEIMFHVSTLLPYTPNNRQQLLRKRHIGNDIVTIIFQEPGALPFTPKNIRSHFQHVFIIVRVHNPCTDNVCYSMAVTRSKDAPPFGPPIPSGTTFRKSDVFRDFLLAKVINAENAAHKSDKFHTMATRTRQEYLKDLAENCVSNTPIDSTGKFNLISLTSKKKEKTKARAGAEQHSAGAIAWRVVAQDYAQGVEIDCILGISNEFVVLLDLRTKEVVFNCYCGDVIGWTPDSSTLKIFYGRGDHIFLQATEGSVEDIREIVQRLKVMTSGWETVDMTLRRNGLGQLGFHVKYDGTVAEVEDYGFAWQAGLRQGSRLVEICKVAVVTLTHDQMIDLLRTSVTVKVVIIPPFEDGTPRRGWPETYDMNTSEPKTEQESITPGGRPPYRSNAPWQWSGPASHNSLPASKWATPTTPGHAQSLSRPLKQTPIVPFRESQPLHSKRPVSFPETPYTVSPAGADRVPPYRQPSGSFSTPGSATYVRYKPSPERYTAAPHPLLSLDPHFSHDGTSSGDSSSGGLTSQESTMERQKPEPLWHVPAQARLSAIAGSSGNKHPSRQDAAGKDSPNRHSKGEPQYSSHSSSNTLSSNASSSHSDDRWFDPLDPLEPEQDPLSKGGSSDSGIDTTLYTSSPSCMSLAKAPRPAKPHKPPGSMGLCGGGREAAGRSHHADRRREVSPAPAVAGQSKGYRPKLYSSGSSTPTGLAGGSRDPPRQPSDMGSRVGYPAQVYKTASAETPRPSQLAQPSPFQLSASVPKSFFSKQPVRNKHPTGWKRTEEPPPRPLPFSDPKKQVDTNTKNVFGQPRLRASLRDLRSPRKNYKSTIEDDLKKLIIMDNLGPEQERDTGQSPQKGLQRTLSDESLCSGRREPSFASPAGLEPGLPSDVLFTSTCAFPSSTLPARRQHQHPHPPVGPGATPAAGSGFPEKKSTISASELSLADGRDRPLRRLDPGLMPLPDTAAGLEWSSLVNAAKAYEVQRAVSLFSLNDPALSPDIPPAHSPVHSHLSLERGPPTPRTTPTMSEEPPLDLTGKVYQLEVMLKQLHTDLQKEKQDKVVLQSEVASLRQNNQRLQEESQAASEQLRKFAEIFCREKKEL
| null | null |
cytoskeleton organization [GO:0007010]; epithelial cell morphogenesis [GO:0003382]; establishment of epithelial cell polarity [GO:0090162]; eye development [GO:0001654]; hematopoietic progenitor cell differentiation [GO:0002244]; regulation of small GTPase mediated signal transduction [GO:0051056]
|
apical part of cell [GO:0045177]; apical plasma membrane [GO:0016324]; cytoplasm [GO:0005737]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; stress fiber [GO:0001725]; tricellular tight junction [GO:0061689]
|
GTPase activator activity [GO:0005096]
|
PF00595;PF21022;PF02145;PF11881;
|
2.30.42.10;6.10.140.210;3.40.50.11210;
| null | null |
SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:26231217}. Note=Detected in tricellular junctions. Colocalizes with apical F-actin. {ECO:0000269|PubMed:26231217}.
| null | null | null | null | null |
FUNCTION: Plays a critical role in epithelial cell morphogenesis, polarity, adhesion and cytoskeletal organization in the lens (PubMed:26231217). {ECO:0000269|PubMed:26231217}.
|
Homo sapiens (Human)
|
O60293
|
ZC3H1_HUMAN
|
MATADTPAPASSGLSPKEEGELEDGEISDDDNNSQIRSRSSSSSSGGGLLPYPRRRPPHSARGGGSGGGGGSSSSSSSSQQQLRNFSRSRHASERGHLRGPSSYRPKEPFRSHPPSVRMPSSSLSESSPRPSFWERSHLALDRFRFRGRPYRGGSRWSRGRGVGERGGKPGCRPPLGGGAGSGFSSSQSWREPSPPRKSSKSFGRSPSRKQNYSSKNENCVEETFEDLLLKYKQIQLELECINKDEKLALSSKEENVQEDPKTLNFEDQTSTDNVSITKDSSKEVAPEEKTQVKTFQAFELKPLRQKLTLPGDKNRLKKVKDGAKPLSLKSDTTDSSQGLQDKEQNLTRRISTSDILSEKKLGEDEEELSELQLRLLALQSASKKWQQKEQQVMKESKEKLTKTKTVQQKVKTSTKTHSAKKVSTTAKQALRKQQTKAWKKLQQQKEQERQKEEDQRKQAEEEERRKREEEIRKIRDLSNQEEQYNRFMKLVGGKRRSRSKSSDPDLRRSLDKQPTDSGGGIYQYDNYEEVAMDTDSETSSPAPSPVQPPFFSECSLGYFSPAPSLSLPPPPQVSSLPPLSQPYVEGLCVSLEPLPPLPPLPPLPPEDPEQPPKPPFADEEEEEEMLLREELLKSLANKRAFKPEETSSNSDPPSPPVLNNSHPVPRSNLSIVSINTVSQPRIQNPKFHRGPRLPRTVISLPKHKSVVVTLNDSDDSESDGEASKSTNSVFGGLESMIKEARRTAEQASKPKVPPKSEKENDPLRTPEALPEEKKIEYRLLKEEIANREKQRLIKSDQLKTSSSSPANSDVEIDGIGRIAMVTKQVTDAESKLKKHRILLMKDESVLKNLVQQEAKKKESVRNAEAKITKLTEQLQATEKILNVNRMFLKKLQEQIHRVQQRVTIKKALTLKYGEELARAKAVASKEIGKRKLEQDRFGPNKMMRLDSSPVSSPRKHSAELIAMEKRRLQKLEYEYALKIQKLKEARALKAKEQQNISPVVEEEPEFSLPQPSLHDLTQDKLTLDTEENDVDDEILSGSSRERRRSFLESNYFTKPNLKHTDTANKECINKLNKNTVEKPELFLGLKIGELQKLYSKADSLKQLILKTTTGITEKVLHGQEISVDVDFVTAQSKTMEVKPCPFRPYHSPLLVFKSYRFSPYYRTKEKLPLSSVSYSNMIEPDQCFCRFDLTGTCNDDDCQWQHIQDYTLSRKQLFQDILSYNLSLIGCAETSTNEEITASAEKYVEKLFGVNKDRMSMDQMAVLLVSNINESKGHTPPFTTYKDKRKWKPKFWRKPISDNSFSSDEEQSTGPIKYAFQPENQINVPALDTVVTPDDVRYFTNETDDIANLEASVLENPSHVQLWLKLAYKYLNQNEGECSESLDSALNVLARALENNKDNPEIWCHYLRLFSKRGTKDEVQEMCETAVEYAPDYQSFWTFLHLESTFEEKDYVCERMLEFLMGAAKQETSNILSFQLLEALLFRVQLHIFTGRCQSALAILQNALKSANDGIVAEYLKTSDRCLAWLAYIHLIEFNILPSKFYDPSNDNPSRIVNTESFVMPWQAVQDVKTNPDMLLAVFEDAVKACTDESLAVEERIEACLPLYTNMIALHQLLERYEAAMELCKSLLESCPINCQLLEALVALYLQTNQHDKARAVWLTAFEKNPQNAEVFYHMCKFFILQNRGDNLLPFLRKFIASFFKPGFEKYNNLDLFRYLLNIPGPIDIPSRLCKGNFDDDMFNHQVPYLWLIYCLCHPLQSSIKETVEAYEAALGVAMRCDIVQKIWMDYLVFANNRAAGSRNKVQEFKFFTDLVNRCLVTVPARYPIPFSSADYWSNYEFHNRVIFFYLSCVPKTQHSKTLERFCSVMPANSGLALRLLQHEWEESNVQILKLQAKMFTYNIPTCLATWKIAIAAEIVLKGQREVHRLYQRALQKLPLCASLWKDQLLFEASEGGKTDNLRKLVSKCQEIGVSLNELLNLNSNKTESKNH
| null | null |
RNA processing [GO:0006396]
|
exosome (RNase complex) [GO:0000178]; extracellular space [GO:0005615]; nucleus [GO:0005634]
|
metal ion binding [GO:0046872]
|
PF10650;
|
1.25.40.10;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27871484}. Note=Excluded from the nucleolus. {ECO:0000269|PubMed:27871484}.
| null | null | null | null | null |
FUNCTION: Subunit of the trimeric poly(A) tail exosome targeting (PAXT) complex, a complex that directs a subset of long and polyadenylated poly(A) RNAs for exosomal degradation. The RNA exosome is fundamental for the degradation of RNA in eukaryotic nuclei. Substrate targeting is facilitated by its cofactor MTREX, which links to RNA-binding protein adapters. {ECO:0000269|PubMed:27871484}.
|
Homo sapiens (Human)
|
O60294
|
TYW4_HUMAN
|
MGPRSRERRAGAVQNTNDSSALSKRSLAARGYVQDPFAALLVPGAARRAPLIHRGYYVRARAVRHCVRAFLEQIGAPQAALRAQILSLGAGFDSLYFRLKTAGRLARAAVWEVDFPDVARRKAERIGETPELCALTGPFERGEPASALCFESADYCILGLDLRQLQRVEEALGAAGLDAASPTLLLAEAVLTYLEPESAAALIAWAAQRFPNALFVVYEQMRPQDAFGQFMLQHFRQLNSPLHGLERFPDVEAQRRRFLQAGWTACGAVDMNEFYHCFLPAEERRRVENIEPFDEFEEWHLKCAHYFILAASRGDTLSHTLVFPSSEAFPRVNPASPSGVFPASVVSSEGQVPNLKRYGHASVFLSPDVILSAGGFGEQEGRHCRVSQFHLLSRDCDSEWKGSQIGSCGTGVQWDGRLYHTMTRLSESRVLVLGGRLSPVSPALGVLQLHFFKSEDNNTEDLKVTITKAGRKDDSTLCCWRHSTTEVSCQNQEYLFVYGGRSVVEPVLSDWHFLHVGTMAWVRIPVEGEVPEARHSHSACTWQGGALIAGGLGASEEPLNSVLFLRPISCGFLWESVDIQPPITPRYSHTAHVLNGKLLLVGGIWIHSSSFPGVTVINLTTGLSSEYQIDTTYVPWPLMLHNHTSILLPEEQQLLLLGGGGNCFSFGTYFNPHTVTLDLSSLSAGQ
|
2.1.1.290; 2.3.1.231
| null |
tRNA methylation [GO:0030488]; tRNA modification [GO:0006400]; wybutosine biosynthetic process [GO:0031591]
|
cytoplasm [GO:0005737]
|
tRNA methyltransferase activity [GO:0008175]
|
PF04072;
|
2.120.10.80;3.40.50.150;
|
Methyltransferase superfamily, LCMT family
| null | null |
CATALYTIC ACTIVITY: Reaction=7-[(3S)-3-amino-3-carboxypropyl]wyosine(37) in tRNA(Phe) + S-adenosyl-L-methionine = 7-[(3S)-(3-amino-3-methoxycarbonyl)propyl]wyosine(37) in tRNA(Phe) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:36903, Rhea:RHEA-COMP:10379, Rhea:RHEA-COMP:11844, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:73543, ChEBI:CHEBI:74275; EC=2.1.1.290; CATALYTIC ACTIVITY: Reaction=7-[(3S)-(3-amino-3-methoxycarbonyl)propyl]wyosine(37) in tRNA(Phe) + CO2 + S-adenosyl-L-methionine = 2 H(+) + S-adenosyl-L-homocysteine + wybutosine(37) in tRNA(Phe); Xref=Rhea:RHEA:37119, Rhea:RHEA-COMP:11844, Rhea:RHEA-COMP:11847, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:73544, ChEBI:CHEBI:74275; EC=2.3.1.231;
| null |
PATHWAY: tRNA modification; wybutosine-tRNA(Phe) biosynthesis.
| null | null |
FUNCTION: Probable S-adenosyl-L-methionine-dependent methyltransferase that acts as a component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA (By similarity). May methylate the carboxyl group of leucine residues to form alpha-leucine ester residues. {ECO:0000250}.
|
Homo sapiens (Human)
|
O60296
|
TRAK2_HUMAN
|
MSQSQNAIFTSPTGEENLMNSNHRDSESITDVCSNEDLPEVELVSLLEEQLPQYRLKVDTLFLYENQDWTQSPHQRQHASDALSPVLAEETFRYMILGTDRVEQMTKTYNDIDMVTHLLAERDRDLELAARIGQALLKRNHVLSEQNESLEEQLGQAFDQVNQLQHELCKKDELLRIVSIASEESETDSSCSTPLRFNESFSLSQGLLQLEMLQEKLKELEEENMALRSKACHIKTETVTYEEKEQQLVSDCVKELRETNAQMSRMTEELSGKSDELIRYQEELSSLLSQIVDLQHKLKEHVIEKEELKLHLQASKDAQRQLTMELHELQDRNMECLGMLHESQEEIKELRSRSGPTAHLYFSQSYGAFTGESLAAEIEGTMRKKLSLDEESSLFKQKAQQKRVFDTVRIANDTRGRSISFPALLPIPGSNRSSVIMTAKPFESGLQQTEDKSLLNQGSSSEEVAGSSQKMGQPGPSGDSDLATALHRLSLRRQNYLSEKQFFAEEWQRKIQVLADQKEGVSGCVTPTESLASLCTTQSEITDLSSASCLRGFMPEKLQIVKPLEGSQTLYHWQQLAQPNLGTILDPRPGVITKGFTQLPGDAIYHISDLEEDEEEGITFQVQQPLEVEEKLSTSKPVTGIFLPPITSAGGPVTVATANPGKCLSCTNSTFTFTTCRILHPSDITQVTPSSGFPSLSCGSSGSSSSNTAVNSPALSYRLSIGESITNRRDSTTTFSSTMSLAKLLQERGISAKVYHSPISENPLQPLPKSLAIPSTPPNSPSHSPCPSPLPFEPRVHLSENFLASRPAETFLQEMYGLRPSRNPPDVGQLKMNLVDRLKRLGIARVVKNPGAQENGRCQEAEIGPQKPDSAVYLNSGSSLLGGLRRNQSLPVIMGSFAAPVCTSSPKMGVLKED
| null | null |
anterograde axonal transport of mitochondrion [GO:0098957]; anterograde dendritic transport of mitochondrion [GO:0098972]; mitochondrion distribution [GO:0048311]; neurogenesis [GO:0022008]; protein targeting [GO:0006605]; vesicle transport along microtubule [GO:0047496]
|
axon cytoplasm [GO:1904115]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; dendrite [GO:0030425]; dendrite cytoplasm [GO:0032839]; early endosome [GO:0005769]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]
|
GABA receptor binding [GO:0050811]; myosin binding [GO:0017022]; signaling receptor binding [GO:0005102]
|
PF04849;PF12448;
| null |
Milton family
|
PTM: O-glycosylated. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Early endosome {ECO:0000250}. Mitochondrion {ECO:0000250}. Note=Colocalizes with MGARP at the mitochondria. Translocates from the cytoplasm to the mitochondria in a MGARP-dependent manner (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: May regulate endosome-to-lysosome trafficking of membrane cargo, including EGFR. {ECO:0000250}.
|
Homo sapiens (Human)
|
O60303
|
KATIP_HUMAN
|
MDGQTLRKAERSWSCSREKKEGYAKDMVTDFDEKHDEYLILLQQRNRILKHLKSKDPVQLRLEHLEQGFSVYVNGANSELKSSPRKAIHSDFSRSASHTEGTHDYGRRTLFREAEEALRRSSRTAPSKVQRRGWHQKSVQIRTEAGPRLHIEPPVDYSDDFELCGDVTLQANNTSEDRPQELRRSLELSVNLQRKQKDCSSDEYDSIEEDILSEPEPEDPALVGHPRHDRPPSSGDWTQKDVHGEQETEGRSSPGPDTLVVLEFNPASKSHKRERNLSAKRKDNAEVFVPTKPEPNLTPQAPAVFPDQERMCSRPGSRRERPLSATRKTLCEAEYPEEDASAVLQAIQVENAALQRALLSRKAEQPASPLQDAEGPPAKPWTSLLEEKEETLELLPITTATTTQEPAGAAGGARAINQAMDRIGLLGSRQQQKLLKVLQAVESDSAHLGRVVSPTKEQVSDTEDKQRMRADEIKDAIYVTMEILSNWGNSWWVGLTEVEFFDLNDTKLYVSPHDVDIRNTATPGELGRLVNRNLAGKKDSSPWTCPFHPPLQLFFVIRNTRQLGDFHLAKIKVRNYWTADGDLDIGAKNVKLYVNRNLIFNGKLDKGDREAPADHSILVDQKNEKSEQLEEAMNAHSEESKGTHEMAGASGDKELGLGCSPPAETLADAKLSSQGNVSGKRKNSTNCRKDSLSQLEEYLRLSAVPTSMGDMPSAPATSPPVKCPPVHEEPSLIQQLENLMGRKICEPPGKTPSWLQPSPTGKDRKQGGRKPKPLWLSPEKPLAWKGRLPSDDVIGEGPGETEARDKGLRHEPGWGTSRSVNTKERPQRATTKVHSDDSDIFNQPPNRERPASGRRGSRKDAGSSSHGDDQPASREDTWSSRTPSRSRWRSEQEHTLHESWSSLSAFDRSHRGRISNTELPGDILDELLQQKSSRHSDLPPSKKGEQPGLSRGQDGYSGETDAGGDFKIPVLPYGQRLVIDIKSTWGDRHYVGLNGIEIFSSKGEPVQISNIKADPPDINILPAYGKDPRVVTNLIDGVNRTQDDMHVWLAPFTRGRSHSITIDFTHPCHVALIRIWNYNKSRIHSFRGVKDITMLLDTQCIFEGEIAKASGTLAGAPEHFGDTILFTTDDDILEAIFYSDEMFDLDVGSLDSLQDEEAMRRPSTADGEGDERPFTQAGLGADERIPELELPSSSPVPQVTTPEPGIYHGICLQLNFTASWGDLHYLGLTGLEVVGKEGQALPIHLHQISASPRDLNELPEYSDDSRALDKLIDGTNITMEDEHMWLIPFSPGLDHVVTIRLDRAESIAGLRFWNYNKSPEDTYRGAKIVHVSLDGLCVSPPEGFLIRKGPGNCHFDFAQEILFVDYLRAQLLPQPARRLDMRSLECASMDYEAPLMPCGFIFQFQLLTSWGDPYYIGLTGLELYDERGEKIPLSENNIAAFPDSVNSLEGVGGDVRTPDKLIDQVNDTSDGRHMWLAPILPGLVNRVYVIFDLPTTVSMIKLWNYAKTPHRGVKEFGLLVDDLLVYNGILAMVSHLVGGILPTCEPTVPYHTILFTEDRDIRHQEKHTTISNQAEDQDVQMMNENQIITNAKRKQSVVDPALRPKTCISEKETRRRRC
| null | null |
cerebrospinal fluid circulation [GO:0090660]
|
cell projection [GO:0042995]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; extracellular space [GO:0005615]
| null |
PF14652;
| null | null | null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:26714646}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:26714646}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:26714646}. Note=When overexpressed, localizes to the cytoplasm where it associates with acetylated alpha-tubulin. {ECO:0000269|PubMed:26714646}.
| null | null | null | null | null |
FUNCTION: May influence the stability of microtubules (MT), possibly through interaction with the MT-severing katanin complex. {ECO:0000269|PubMed:26714646}.
|
Homo sapiens (Human)
|
O60304
|
ZN500_HUMAN
|
MATVPGLQPLPTLEQDLEQEEILIVKVEEDFCLEEEPSVETEDPSPETFRQLFRLFCYQEVAGPREALSRLWELCCRWLRPELRTKEQILELLVLEQFLTVLPGEIQARVREQQPESGEEAVVLVEGLQRKPRKHRQRGSELLSDDEVPLGIGGQFLKHQAEAQPEDLSLEEEARFSSQQPPAQLSHRPQRGPLLWPERGPPAPRHQEMASASPFLSAWSQVPVNLEDVAVYLSGEEPRCMDPAQRDAPLENEGPGIQLEDGGDGREDAPLRMEWYRVLSARCQGPGHPLPGQRPAPVRGLVRPDQPRGGPPPGRRASHGADKPYTCPECGKGFSKTSHLTKHQRTHTGERPYKCLVCGKGFSDRSNFSTHQRVHTGEKPYPCPECGKRFSQSSSLVIHRRTHSGERPYACTQCGKRFNNSSHFSAHRRTHTGEKPYTCPACGRGFRRGTDLHKHQRTHMGAGSLPTLQPVAPGGPGAKA
| null | null |
regulation of transcription by RNA polymerase II [GO:0006357]
|
nucleus [GO:0005634]
|
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF01352;PF02023;PF00096;
|
3.30.160.60;1.10.4020.10;
|
Krueppel C2H2-type zinc-finger protein family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187}.
| null | null | null | null | null |
FUNCTION: May be involved in transcriptional regulation.
|
Homo sapiens (Human)
|
O60306
|
AQR_HUMAN
|
MAAPAQPKKIVAPTVSQINAEFVTQLACKYWAPHIKKKSPFDIKVIEDIYEKEIVKSRFAIRKIMLLEFSQYLENYLWMNYSPEVSSKAYLMSICCMVNEKFRENVPAWEIFKKKPDHFPFFFKHILKAALAETDGEFSLHEQTVLLLFLDHCFNSLEVDLIRSQVQQLISLPMWMGLQLARLELELKKTPKLRKFWNLIKKNDEKMDPEAREQAYQERRFLSQLIQKFISVLKSVPLSEPVTMDKVHYCERFIELMIDLEALLPTRRWFNTILDDSHLLVHCYLSNLVRREEDGHLFSQLLDMLKFYTGFEINDQTGNALTENEMTTIHYDRITSLQRAAFAHFPELYDFALSNVAEVDTRESLVKFFGPLSSNTLHQVASYLCLLPTLPKNEDTTFDKEFLLELLVSRHERRISQIQQLNQMPLYPTEKIIWDENIVPTEYYSGEGCLALPKLNLQFLTLHDYLLRNFNLFRLESTYEIRQDIEDSVSRMKPWQSEYGGVVFGGWARMAQPIVAFTVVEVAKPNIGENWPTRVRADVTINLNVRDHIKDEWEGLRKHDVCFLITVRPTKPYGTKFDRRRPFIEQVGLVYVRGCEIQGMLDDKGRVIEDGPEPRPNLRGESRTFRVFLDPNQYQQDMTNTIQNGAEDVYETFNIIMRRKPKENNFKAVLETIRNLMNTDCVVPDWLHDIILGYGDPSSAHYSKMPNQIATLDFNDTFLSIEHLKASFPGHNVKVTVEDPALQIPPFRITFPVRSGKGKKRKDADVEDEDTEEAKTLIVEPHVIPNRGPYPYNQPKRNTIQFTHTQIEAIRAGMQPGLTMVVGPPGTGKTDVAVQIISNIYHNFPEQRTLIVTHSNQALNQLFEKIMALDIDERHLLRLGHGEEELETEKDFSRYGRVNYVLARRIELLEEVKRLQKSLGVPGDASYTCETAGYFFLYQVMSRWEEYISKVKNKGSTLPDVTEVSTFFPFHEYFANAPQPIFKGRSYEEDMEIAEGCFRHIKKIFTQLEEFRASELLRSGLDRSKYLLVKEAKIIAMTCTHAALKRHDLVKLGFKYDNILMEEAAQILEIETFIPLLLQNPQDGFSRLKRWIMIGDHHQLPPVIKNMAFQKYSNMEQSLFTRFVRVGVPTVDLDAQGRARASLCNLYNWRYKNLGNLPHVQLLPEFSTANAGLLYDFQLINVEDFQGVGESEPNPYFYQNLGEAEYVVALFMYMCLLGYPADKISILTTYNGQKHLIRDIINRRCGNNPLIGRPNKVTTVDRFQGQQNDYILLSLVRTRAVGHLRDVRRLVVAMSRARLGLYIFARVSLFQNCFELTPAFSQLTARPLHLHIIPTEPFPTTRKNGERPSHEVQIIKNMPQMANFVYNMYMHLIQTTHHYHQTLLQLPPAMVEEGEEVQNQETELETEEEAMTVQADIIPSPTDTSCRQETPAFQTDTTPSETGATSTPEAIPALSETTPTVVGAVSAPAEANTPQDATSAPEETK
|
3.6.4.13
| null |
mRNA splicing, via spliceosome [GO:0000398]
|
catalytic step 2 spliceosome [GO:0071013]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; U2-type catalytic step 2 spliceosome [GO:0071007]
|
3'-5' RNA helicase activity [GO:0034458]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; mRNA binding [GO:0003729]; RNA binding [GO:0003723]; single-stranded RNA binding [GO:0003727]
|
PF13086;PF13087;PF16399;PF21143;PF21144;
|
3.40.50.300;
|
CWF11 family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:25599396, ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770}. Nucleus, nucleoplasm {ECO:0000269|PubMed:16949364}. Note=Localizes to speckle-like regions of the nucleoplasm. {ECO:0000269|PubMed:16949364}.
|
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=3.6.4.13; Evidence={ECO:0000269|PubMed:25599396};
| null | null | null | null |
FUNCTION: Involved in pre-mRNA splicing as component of the spliceosome (PubMed:11991638, PubMed:25599396, PubMed:28076346, PubMed:28502770). Intron-binding spliceosomal protein required to link pre-mRNA splicing and snoRNP (small nucleolar ribonucleoprotein) biogenesis (PubMed:16949364). Plays a key role in position-dependent assembly of intron-encoded box C/D small snoRNP, splicing being required for snoRNP assembly (PubMed:16949364). May act by helping the folding of the snoRNA sequence. Binds to intron of pre-mRNAs in a sequence-independent manner, contacting the region between snoRNA and the branchpoint of introns (40 nucleotides upstream of the branchpoint) during the late stages of splicing (PubMed:16949364). Has ATP-dependent RNA helicase activity and can unwind double-stranded RNA molecules with a 3' overhang (in vitro) (PubMed:25599396). {ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:16949364, ECO:0000269|PubMed:25599396, ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770}.
|
Homo sapiens (Human)
|
O60307
|
MAST3_HUMAN
|
MDESSLLRRRGLQKELSLPRRGRGCRSGNRKSLVVGTPSPTLSRPLSPLSVPTAGSSPLDSPRNFSAASALNFPFARRADGRRWSLASLPSSGYGTNTPSSTLSSSSSSRERLHQLPFQPTPDELHFLSKHFRSSENVLDEEGGRSPRLRPRSRSLSPGRATGTFDNEIVMMNHVYRERFPKATAQMEGRLQEFLTAYAPGARLALADGVLGFIHHQIVELARDCLAKSGENLVTSRYFLEMQEKLERLLQDAHERSDSEEVSFIVQLVRKLLIIISRPARLLECLEFDPEEFYHLLEAAEGHAREGQGIKTDLPQYIIGQLGLAKDPLEEMVPLSHLEEEQPPAPESPESRALVGQSRRKPCESDFETIKLISNGAYGAVYLVRHRDTRQRFAIKKINKQNLILRNQIQQVFVERDILTFAENPFVVSMFCSFETRRHLCMVMEYVEGGDCATLLKNMGPLPVDMARLYFAETVLALEYLHNYGIVHRDLKPDNLLITSLGHIKLTDFGLSKIGLMSMATNLYEGHIEKDAREFIDKQVCGTPEYIAPEVIFRQGYGKPVDWWAMGVVLYEFLVGCVPFFGDTPEELFGQVVSDEIMWPEGDEALPADAQDLITRLLRQSPLDRLGTGGTHEVKQHPFFLALDWAGLLRHKAEFVPQLEAEDDTSYFDTRSERYRHLGSEDDETNDEESSTEIPQFSSCSHRFSKVYSSSEFLAVQPTPTFAERSFSEDREEGWERSEVDYGRRLSADIRLRSWTSSGSSCQSSSSQPERGPSPSLLNTISLDTMPKFAFSSEDEGVGPGPAGPKRPVFILGEPDPPPAATPVMPKPSSLSADTAALSHARLRSNSIGARHSTPRPLDAGRGRRLGGPRDPAPEKSRASSSGGSGGGSGGRVPKSASVSALSLIITADDGSGGPLMSPLSPRSLSSNPSSRDSSPSRDPSPVCGSLRPPIVIHSSGKKYGFSLRAIRVYMGDSDVYTVHHVVWSVEDGSPAQEAGLRAGDLITHINGESVLGLVHMDVVELLLKSGNKISLRTTALENTSIKVGPARKNVAKGRMARRSKRSRRRETQDRRKSLFKKISKQTSVLHTSRSFSSGLHHSLSSSESLPGSPTHSLSPSPTTPCRSPAPDVPADTTASPPSASPSSSSPASPAAAGHTRPSSLHGLAAKLGPPRPKTGRRKSTSSIPPSPLACPPISAPPPRSPSPLPGHPPAPARSPRLRRGQSADKLGTGERLDGEAGRRTRGPEAELVVMRRLHLSERRDSFKKQEAVQEVSFDEPQEEATGLPTSVPQIAVEGEEAVPVALGPTGRD
|
2.7.11.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
|
cytoskeleton organization [GO:0007010]; intracellular signal transduction [GO:0035556]; phosphorylation [GO:0016310]
|
cytoplasm [GO:0005737]
|
ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF08926;PF17820;PF00069;
|
2.30.42.10;1.20.1480.20;1.10.510.10;
|
Protein kinase superfamily, AGC Ser/Thr protein kinase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q3U214}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
| null | null | null | null | null |
Homo sapiens (Human)
|
O60308
|
CE104_HUMAN
|
MPHKIGFVVVSSSGHEDGFSARELMIHAPTVSGWRSPRFCQFPQEIVLQMVERCRIRKLQLLAHQYMISSKIEFYISESLPEYFAPYQAERFRRLGYVSLCDNEKTGCKARELKSVYVDAVGQFLKLIFHQNHVNKYNIYNQVALVAINIIGDPADFSDESNTASREKLIDHYLGHNSEDPALEGTYARKSDYISPLDDLAFDMYQDPEVAQIIRKLDERKREAVQKERYDYAKKLKQAIADLQKVGERLGRYEVEKRCAVEKEDYDLAKEKKQQMEQYRAEVYEQLELHSLLDAELMRRPFDLPLQPLARSGSPCHQKPMPSLPQLEERGTENQFAEPFLQEKPSSYSLTISPQHSAVDPLLPATDPHPKINAESLPYDERPLPAIRKHYGEAVVEPEMSNADISDARRGGMLGEPEPLTEKALREASSAIDVLGETLVAEAYCKTWSYREDALLALSKKLMEMPVGTPKEDLKNTLRASVFLVRRAIKDIVTSVFQASLKLLKMIITQYIPKHKLSKLETAHCVERTIPVLLTRTGDSSARLRVTAANFIQEMALFKEVKSLQIIPSYLVQPLKANSSVHLAMSQMGLLARLLKDLGTGSSGFTIDNVMKFSVSALEHRVYEVRETAVRIILDMYRQHQASILEYLPPDDSNTRRNILYKTIFEGFAKIDGRATDAEMRARRKAATEEAEKQKKEEIKALQGQLAALKEIQAEVQEKESDAVKPKNQDIQGGKAAPAEALGIPDEHYLDNLCIFCGERSESFTEEGLDLHYWKHCLMLTRCDHCKQVVEISSLTEHLLTECDKKDGFGKCYRCSEAVFKEELPRHIKHKDCNPAKPEKLANRCPLCHENFSPGEEAWKAHLMGPAGCTMNLRKTHILQKAPALQPGKSSAVAASGPLGSKAGSKIPTPKGGLSKSSSRTYAKR
| null | null | null |
centriole [GO:0005814]; centrosome [GO:0005813]; cilium [GO:0005929]; cytoplasm [GO:0005737]; spindle pole [GO:0000922]
| null |
PF21040;PF21038;PF21039;
|
1.25.10.10;
| null | null |
SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000269|PubMed:23970417}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:21399614, ECO:0000269|PubMed:23970417}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:23970417}. Cytoplasm, cytoskeleton, spindle pole. Note=In interphase non-ciliated cells, localizes to the distal ends of both the mother and daughter centrioles. In ciliated cells, present at the distal end of the daughter centriole, but not on the mother centriole, and at the tip of primary cilium. Localization at the ciliary tip is also observed in motile cilia. Throughout S phase, associated with both mother and daughter centrioles in each centrosome. During metaphase and telophase, present at both spindle poles. {ECO:0000269|PubMed:23970417}.
| null | null | null | null | null |
FUNCTION: Required for ciliogenesis and for structural integrity at the ciliary tip. {ECO:0000269|PubMed:23970417}.
|
Homo sapiens (Human)
|
O60312
|
AT10A_HUMAN
|
MEREPAGTEEPGPPGRRRRREGRTRTVRSNLLPPPGAEDPAAGAAKGERRRRRGCAQHLADNRLKTTKYTLLSFLPKNLFEQFHRPANVYFVFIALLNFVPAVNAFQPGLALAPVLFILAITAFRDLWEDYSRHRSDHKINHLGCLVFSREEKKYVNRFWKEIHVGDFVRLRCNEIFPADILLLSSSDPDGLCHIETANLDGETNLKRRQVVRGFSELVSEFNPLTFTSVIECEKPNNDLSRFRGCIIHDNGKKAGLYKENLLLRGCTLRNTDAVVGIVIYAGHETKALLNNSGPRYKRSKLERQMNCDVLWCVLLLVCMSLFSAVGHGLWIWRYQEKKSLFYVPKSDGSSLSPVTAAVYSFLTMIIVLQVLIPISLYVSIEIVKACQVYFINQDMQLYDEETDSQLQCRALNITEDLGQIQYIFSDKTGTLTENKMVFRRCTVSGVEYSHDANAQRLARYQEADSEEEEVVPRGGSVSQRGSIGSHQSVRVVHRTQSTKSHRRTGSRAEAKRASMLSKHTAFSSPMEKDITPDPKLLEKVSECDKSLAVARHQEHLLAHLSPELSDVFDFFIALTICNTVVVTSPDQPRTKVRVRFELKSPVKTIEDFLRRFTPSCLTSGCSSIGSLAANKSSHKLGSSFPSTPSSDGMLLRLEERLGQPTSAIASNGYSSQADNWASELAQEQESERELRYEAESPDEAALVYAARAYNCVLVERLHDQVSVELPHLGRLTFELLHTLGFDSVRKRMSVVIRHPLTDEINVYTKGADSVVMDLLQPCSSVDARGRHQKKIRSKTQNYLNVYAAEGLRTLCIAKRVLSKEEYACWLQSHLEAESSLENSEELLFQSAIRLETNLHLLGATGIEDRLQDGVPETISKLRQAGLQIWVLTGDKQETAVNIAYACKLLDHDEEVITLNATSQEACAALLDQCLCYVQSRGLQRAPEKTKGKVSMRFSSLCPPSTSTASGRRPSLVIDGRSLAYALEKNLEDKFLFLAKQCRSVLCCRSTPLQKSMVVKLVRSKLKAMTLAIGDGANDVSMIQVADVGVGISGQEGMQAVMASDFAVPKFRYLERLLILHGHWCYSRLANMVLYFFYKNTMFVGLLFWFQFFCGFSASTMIDQWYLIFFNLLFSSLPPLVTGVLDRDVPANVLLTNPQLYKSGQNMEEYRPRTFWFNMADAAFQSLVCFSIPYLAYYDSNVDLFTWGTPIVTIALLTFLLHLGIETKTWTWLNWITCGFSVLLFFTVALIYNASCATCYPPSNPYWTMQALLGDPVFYLTCLMTPVAALLPRLFFRSLQGRVFPTQLQLARQLTRKSPRRCSAPKETFAQGRLPKDSGTEHSSGRTVKTSVPLSQPSWHTQQPVCSLEASGEPSTVDMSMPVREHTLLEGLSAPAPMSSAPGEAVLRSPGGCPEESKVRAASTGRVTPLSSLFSLPTFSLLNWISSWSLVSRLGSVLQFSRTEQLADGQAGRGLPVQPHSGRSGLQGPDHRLLIGASSRRSQ
|
7.6.2.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9Y2Q0};
|
monoatomic ion transmembrane transport [GO:0034220]; phospholipid translocation [GO:0045332]; positive regulation of membrane tubulation [GO:1903527]; regulation of cell shape [GO:0008360]
|
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; phospholipid-translocating ATPase complex [GO:1990531]; plasma membrane [GO:0005886]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled intramembrane lipid transporter activity [GO:0140326]; glycosylceramide flippase activity [GO:0140351]; magnesium ion binding [GO:0000287]; phosphatidylcholine flippase activity [GO:0140345]; phosphatidylcholine floppase activity [GO:0090554]
|
PF13246;PF16212;PF16209;
|
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 IV subfamily
|
PTM: Autophosphorylated at the conserved aspartate of the P-type ATPase signature sequence. {ECO:0000250|UniProtKB:O94823}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21914794, ECO:0000269|PubMed:25947375, ECO:0000269|PubMed:30530492}; Multi-pass membrane protein {ECO:0000269|PubMed:21914794}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:21914794, ECO:0000269|PubMed:25947375}. Note=Exit from the endoplasmic reticulum requires the presence of TMEM30A, but not that of TMEM30B.
|
CATALYTIC ACTIVITY: Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2.; EC=7.6.2.1; Evidence={ECO:0000269|PubMed:25947375, ECO:0000269|PubMed:29599178, ECO:0000269|PubMed:30530492}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phosphocholine(in) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:38583, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57643, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:25947375, ECO:0000269|PubMed:29599178, ECO:0000269|PubMed:30530492}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38584; Evidence={ECO:0000305|PubMed:25947375, ECO:0000305|PubMed:29599178, ECO:0000305|PubMed:30530492}; CATALYTIC ACTIVITY: Reaction=a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine(out) + ATP + H2O = a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine(in) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:66036, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:22801, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:30530492}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66037; Evidence={ECO:0000305|PubMed:30530492};
| null | null | null | null |
FUNCTION: Catalytic component of P4-ATPase flippase complex, which catalyzes the hydrolysis of ATP coupled to the transport of phosphatidylcholine (PC) from the outer to the inner leaflet of the plasma membrane (PubMed:25947375, PubMed:29599178, PubMed:30530492). Initiates inward plasma membrane bending and recruitment of Bin/amphiphysin/Rvs (BAR) domain-containing proteins involved in membrane tubulation and cell trafficking (PubMed:29599178). Facilitates ITGB1/beta1 integrin endocytosis, delaying cell adhesion and cell spreading on extracellular matrix (PubMed:25947375, PubMed:29599178). Has low flippase activity toward glucosylceramide (GlcCer) (PubMed:30530492). {ECO:0000269|PubMed:25947375, ECO:0000269|PubMed:29599178, ECO:0000269|PubMed:30530492}.
|
Homo sapiens (Human)
|
O60313
|
OPA1_HUMAN
|
MWRLRRAAVACEVCQSLVKHSSGIKGSLPLQKLHLVSRSIYHSHHPTLKLQRPQLRTSFQQFSSLTNLPLRKLKFSPIKYGYQPRRNFWPARLATRLLKLRYLILGSAVGGGYTAKKTFDQWKDMIPDLSEYKWIVPDIVWEIDEYIDFEKIRKALPSSEDLVKLAPDFDKIVESLSLLKDFFTSGSPEETAFRATDRGSESDKHFRKVSDKEKIDQLQEELLHTQLKYQRILERLEKENKELRKLVLQKDDKGIHHRKLKKSLIDMYSEVLDVLSDYDASYNTQDHLPRVVVVGDQSAGKTSVLEMIAQARIFPRGSGEMMTRSPVKVTLSEGPHHVALFKDSSREFDLTKEEDLAALRHEIELRMRKNVKEGCTVSPETISLNVKGPGLQRMVLVDLPGVINTVTSGMAPDTKETIFSISKAYMQNPNAIILCIQDGSVDAERSIVTDLVSQMDPHGRRTIFVLTKVDLAEKNVASPSRIQQIIEGKLFPMKALGYFAVVTGKGNSSESIEAIREYEEEFFQNSKLLKTSMLKAHQVTTRNLSLAVSDCFWKMVRESVEQQADSFKATRFNLETEWKNNYPRLRELDRNELFEKAKNEILDEVISLSQVTPKHWEEILQQSLWERVSTHVIENIYLPAAQTMNSGTFNTTVDIKLKQWTDKQLPNKAVEVAWETLQEEFSRFMTEPKGKEHDDIFDKLKEAVKEESIKRHKWNDFAEDSLRVIQHNALEDRSISDKQQWDAAIYFMEEALQARLKDTENAIENMVGPDWKKRWLYWKNRTQEQCVHNETKNELEKMLKCNEEHPAYLASDEITTVRKNLESRGVEVDPSLIKDTWHQVYRRHFLKTALNHCNLCRRGFYYYQRHFVDSELECNDVVLFWRIQRMLAITANTLRQQLTNTEVRRLEKNVKEVLEDFAEDGEKKIKLLTGKRVQLAEDLKKVREIQEKLDAFIEALHQEK
|
3.6.5.5
| null |
apoptotic process [GO:0006915]; axonal transport of mitochondrion [GO:0019896]; cellular senescence [GO:0090398]; GTP metabolic process [GO:0046039]; inner mitochondrial membrane organization [GO:0007007]; membrane tubulation [GO:0097749]; mitochondrial fission [GO:0000266]; mitochondrial fusion [GO:0008053]; mitochondrial genome maintenance [GO:0000002]; mitochondrion organization [GO:0007005]; negative regulation of apoptotic process [GO:0043066]; negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway [GO:1902236]; negative regulation of release of cytochrome c from mitochondria [GO:0090201]; neural tube closure [GO:0001843]; protein complex oligomerization [GO:0051259]; visual perception [GO:0007601]
|
axon cytoplasm [GO:1904115]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; membrane [GO:0016020]; microtubule [GO:0005874]; mitochondrial crista [GO:0030061]; mitochondrial inner membrane [GO:0005743]; mitochondrial intermembrane space [GO:0005758]; mitochondrial membrane [GO:0031966]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]
|
cardiolipin binding [GO:1901612]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; magnesium ion binding [GO:0000287]; microtubule binding [GO:0008017]; phosphatidic acid binding [GO:0070300]
|
PF00350;PF19434;
|
3.40.50.300;
|
TRAFAC class dynamin-like GTPase superfamily, Dynamin/Fzo/YdjA family
|
PTM: Cleaved by OMA1 or YME1L downstream of the transmembrane region in response to different signals to generate soluble forms (PubMed:16778770, PubMed:17709429, PubMed:20038677, PubMed:24616225, PubMed:27495975, PubMed:33237841). Cleaved by OMA1 at position S1 following stress conditions, generating the short soluble form (Dynamin-like GTPase OPA1, short form; S-OPA1) (PubMed:20038677). AFG3L2 is involved in the regulation of OMA1-dependent processing of OPA1 (PubMed:17615298). PARL-dependent proteolytic processing releases an antiapoptotic soluble form not required for mitochondrial fusion (By similarity). {ECO:0000250|UniProtKB:P58281, ECO:0000269|PubMed:16778770, ECO:0000269|PubMed:17615298, ECO:0000269|PubMed:17709429, ECO:0000269|PubMed:20038677, ECO:0000269|PubMed:24616225, ECO:0000269|PubMed:27495975, ECO:0000269|PubMed:33237841}.; PTM: [Isoform 2]: Cleavage at position S2 by YME1L is required to mediate oxidative phosphorylation (OXPHOS)-induced mitochondrial fusion (PubMed:17709429, PubMed:24616225, PubMed:27495975). Cleavage occurs in the sequence motif Leu-Gln-Gln-Gln-Ile-Gln (LQQQIQ) (PubMed:16778770). {ECO:0000269|PubMed:16778770, ECO:0000269|PubMed:17709429, ECO:0000269|PubMed:24616225, ECO:0000269|PubMed:27495975}.; PTM: [Isoform 3]: Cleavage at position S2 by YME1L is required to mediate oxidative phosphorylation (OXPHOS)-induced mitochondrial fusion (PubMed:17709429, PubMed:24616225, PubMed:27495975). Cleavage occurs in the sequence motif Leu-Gln-Gln-Gln-Ile-Gln (LQQQIQ) (PubMed:16778770). {ECO:0000269|PubMed:16778770, ECO:0000269|PubMed:17709429, ECO:0000269|PubMed:24616225, ECO:0000269|PubMed:27495975}.; PTM: [Isoform 4]: Cleavage at position S2 by YME1L is required to mediate oxidative phosphorylation (OXPHOS)-induced mitochondrial fusion (PubMed:17709429, PubMed:24616225, PubMed:27495975). Cleavage occurs in the sequence motif Leu-Gln-Gln-Gln-Ile-Gln (LQQQIQ) (PubMed:16778770). Cleavage at position S3 by YME1L is required for membrane tubulation (PubMed:33237841). {ECO:0000269|PubMed:16778770, ECO:0000269|PubMed:17709429, ECO:0000269|PubMed:24616225, ECO:0000269|PubMed:27495975, ECO:0000269|PubMed:33237841}.; PTM: [Isoform 5]: Cleavage at position S3 by YME1L is required for membrane tubulation. {ECO:0000269|PubMed:33237841}.
|
SUBCELLULAR LOCATION: [Dynamin-like GTPase OPA1, long form]: Mitochondrion inner membrane {ECO:0000269|PubMed:11017079, ECO:0000269|PubMed:16778770, ECO:0000269|PubMed:20974897, ECO:0000269|PubMed:28746876, ECO:0000269|PubMed:37612504, ECO:0000269|PubMed:37612506}; Single-pass membrane protein {ECO:0000255}. Note=Detected at contact sites between endoplasmic reticulum and mitochondrion membranes. {ECO:0000269|PubMed:24616225}.; SUBCELLULAR LOCATION: [Dynamin-like GTPase OPA1, short form]: Mitochondrion intermembrane space {ECO:0000269|PubMed:32228866, ECO:0000269|PubMed:37612504, ECO:0000269|PubMed:37612506}.
|
CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.5; Evidence={ECO:0000269|PubMed:20185555, ECO:0000269|PubMed:28628083, ECO:0000269|PubMed:28746876, ECO:0000269|PubMed:32228866, ECO:0000269|PubMed:32245890, ECO:0000269|PubMed:32379273, ECO:0000269|PubMed:37612504, ECO:0000269|PubMed:37612506};
| null | null | null | null |
FUNCTION: Dynamin-related GTPase that is essential for normal mitochondrial morphology by mediating fusion of the mitochondrial inner membranes, regulating cristae morphology and maintaining respiratory chain function (PubMed:16778770, PubMed:17709429, PubMed:20185555, PubMed:24616225, PubMed:28628083, PubMed:28746876, PubMed:31922487, PubMed:32228866, PubMed:32567732, PubMed:33130824, PubMed:33237841, PubMed:37612504, PubMed:37612506). Exists in two forms: the transmembrane, long form (Dynamin-like GTPase OPA1, long form; L-OPA1), which is tethered to the inner mitochondrial membrane, and the short soluble form (Dynamin-like GTPase OPA1, short form; S-OPA1), which results from proteolytic cleavage and localizes in the intermembrane space (PubMed:31922487, PubMed:32228866, PubMed:33237841, PubMed:37612504, PubMed:37612506). Both forms (L-OPA1 and S-OPA1) cooperate to catalyze the fusion of the mitochondrial inner membrane (PubMed:31922487, PubMed:37612504, PubMed:37612506). The equilibrium between L-OPA1 and S-OPA1 is essential: excess levels of S-OPA1, produced by cleavage by OMA1 following loss of mitochondrial membrane potential, lead to an impaired equilibrium between L-OPA1 and S-OPA1, inhibiting mitochondrial fusion (PubMed:20038677, PubMed:31922487). The balance between L-OPA1 and S-OPA1 also influences cristae shape and morphology (By similarity). Involved in remodeling cristae and the release of cytochrome c during apoptosis (By similarity). Proteolytic processing by PARL in response to intrinsic apoptotic signals may lead to disassembly of OPA1 oligomers and release of the caspase activator cytochrome C (CYCS) into the mitochondrial intermembrane space (By similarity). Acts as a regulator of T-helper Th17 cells, which are characterized by cells with fused mitochondria with tight cristae, by mediating mitochondrial membrane remodeling: OPA1 is required for interleukin-17 (IL-17) production (By similarity). Its role in mitochondrial morphology is required for mitochondrial genome maintenance (PubMed:18158317, PubMed:20974897). {ECO:0000250|UniProtKB:P58281, ECO:0000269|PubMed:16778770, ECO:0000269|PubMed:17709429, ECO:0000269|PubMed:18158317, ECO:0000269|PubMed:20038677, ECO:0000269|PubMed:20185555, ECO:0000269|PubMed:20974897, ECO:0000269|PubMed:24616225, ECO:0000269|PubMed:28628083, ECO:0000269|PubMed:28746876, ECO:0000269|PubMed:31922487, ECO:0000269|PubMed:32228866, ECO:0000269|PubMed:32567732, ECO:0000269|PubMed:33130824, ECO:0000269|PubMed:33237841, ECO:0000269|PubMed:37612504, ECO:0000269|PubMed:37612506}.; FUNCTION: [Dynamin-like GTPase OPA1, long form]: Constitutes the transmembrane long form (L-OPA1) that plays a central role in mitochondrial inner membrane fusion and cristae morphology (PubMed:31922487, PubMed:32228866, PubMed:37612504, PubMed:37612506). L-OPA1 and the soluble short form (S-OPA1) form higher-order helical assemblies that coordinate the fusion of mitochondrial inner membranes (PubMed:31922487, PubMed:37612504, PubMed:37612506). Inner membrane-anchored L-OPA1 molecules initiate membrane remodeling by recruiting soluble S-OPA1 to rapidly polymerize into a flexible cylindrical scaffold encaging the mitochondrial inner membrane (PubMed:37612504, PubMed:37612506). Once at the membrane surface, the formation of S-OPA1 helices induce bilayer curvature (PubMed:37612504, PubMed:37612506). OPA1 dimerization through the paddle region, which inserts into cardiolipin-containing membrane, promotes GTP hydrolysis and the helical assembly of a flexible OPA1 lattice on the membrane, which drives membrane curvature and mitochondrial fusion (PubMed:28628083, PubMed:37612504, PubMed:37612506). Plays a role in the maintenance and remodeling of mitochondrial cristae, some invaginations of the mitochondrial inner membrane that provide an increase in the surface area (PubMed:32567732, PubMed:33130824). Probably acts by forming helical filaments at the inside of inner membrane tubes with the shape and dimensions of crista junctions (By similarity). The equilibrium between L-OPA1 and S-OPA1 influences cristae shape and morphology: increased L-OPA1 levels promote cristae stacking and elongated mitochondria, while increased S-OPA1 levels correlated with irregular cristae packing and round mitochondria shape (By similarity). {ECO:0000250|UniProtKB:G0SGC7, ECO:0000250|UniProtKB:P58281, ECO:0000269|PubMed:28628083, ECO:0000269|PubMed:31922487, ECO:0000269|PubMed:32228866, ECO:0000269|PubMed:32567732, ECO:0000269|PubMed:33130824, ECO:0000269|PubMed:37612504, ECO:0000269|PubMed:37612506}.; FUNCTION: [Dynamin-like GTPase OPA1, short form]: Constitutes the soluble short form (S-OPA1) generated by cleavage by OMA1, which plays a central role in mitochondrial inner membrane fusion and cristae morphology (PubMed:31922487, PubMed:32228866, PubMed:32245890, PubMed:37612504, PubMed:37612506). The transmembrane long form (L-OPA1) and the S-OPA1 form higher-order helical assemblies that coordinate the fusion of mitochondrial inner membranes (PubMed:31922487, PubMed:32228866, PubMed:37612504, PubMed:37612506). Inner membrane-anchored L-OPA1 molecules initiate membrane remodeling by recruiting soluble S-OPA1 to rapidly polymerize into a flexible cylindrical scaffold encaging the mitochondrial inner membrane (PubMed:32228866, PubMed:37612504, PubMed:37612506). Once at the membrane surface, the formation of S-OPA1 helices induce bilayer curvature (PubMed:37612504, PubMed:37612506). OPA1 dimerization through the paddle region, which inserts into cardiolipin-containing membrane, promotes GTP hydrolysis and the helical assembly of a flexible OPA1 lattice on the membrane, which drives membrane curvature and mitochondrial fusion (PubMed:28628083, PubMed:37612504, PubMed:37612506). Excess levels of S-OPA1 produced by cleavage by OMA1 following stress conditions that induce loss of mitochondrial membrane potential, lead to an impaired equilibrium between L-OPA1 and S-OPA1, thereby inhibiting mitochondrial fusion (PubMed:20038677). Involved in mitochondrial safeguard in response to transient mitochondrial membrane depolarization by mediating flickering: cleavage by OMA1 leads to excess production of S-OPA1, preventing mitochondrial hyperfusion (By similarity). Plays a role in the maintenance and remodeling of mitochondrial cristae, some invaginations of the mitochondrial inner membrane that provide an increase in the surface area (PubMed:32245890). Probably acts by forming helical filaments at the inside of inner membrane tubes with the shape and dimensions of crista junctions (By similarity). The equilibrium between L-OPA1 and S-OPA1 influences cristae shape and morphology: increased L-OPA1 levels promote cristae stacking and elongated mitochondria, while increased S-OPA1 levels correlated with irregular cristae packing and round mitochondria shape (By similarity). {ECO:0000250|UniProtKB:G0SGC7, ECO:0000250|UniProtKB:P58281, ECO:0000269|PubMed:20038677, ECO:0000269|PubMed:28628083, ECO:0000269|PubMed:31922487, ECO:0000269|PubMed:32228866, ECO:0000269|PubMed:32245890, ECO:0000269|PubMed:37612504, ECO:0000269|PubMed:37612506}.; FUNCTION: [Isoform 1]: Coexpression of isoform 1 with shorter alternative products is required for optimal activity in promoting mitochondrial fusion. {ECO:0000269|PubMed:17709429}.; FUNCTION: [Isoform 4]: Isoforms that contain the alternative exon 4b are required for mitochondrial genome maintenance, possibly by anchoring the mitochondrial nucleoids to the inner mitochondrial membrane. {ECO:0000269|PubMed:20974897}.; FUNCTION: [Isoform 5]: Isoforms that contain the alternative exon 4b are required for mitochondrial genome maintenance, possibly by anchoring the mitochondrial nucleoids to the inner mitochondrial membrane. {ECO:0000269|PubMed:20974897}.
|
Homo sapiens (Human)
|
O60315
|
ZEB2_HUMAN
|
MKQPIMADGPRCKRRKQANPRRKNVVNYDNVVDTGSETDEEDKLHIAEDDGIANPLDQETSPASVPNHESSPHVSQALLPREEEEDEIREGGVEHPWHNNEILQASVDGPEEMKEDYDTMGPEATIQTAINNGTVKNANCTSDFEEYFAKRKLEERDGHAVSIEEYLQRSDTAIIYPEAPEELSRLGTPEANGQEENDLPPGTPDAFAQLLTCPYCDRGYKRLTSLKEHIKYRHEKNEENFSCPLCSYTFAYRTQLERHMVTHKPGTDQHQMLTQGAGNRKFKCTECGKAFKYKHHLKEHLRIHSGEKPYECPNCKKRFSHSGSYSSHISSKKCIGLISVNGRMRNNIKTGSSPNSVSSSPTNSAITQLRNKLENGKPLSMSEQTGLLKIKTEPLDFNDYKVLMATHGFSGTSPFMNGGLGATSPLGVHPSAQSPMQHLGVGMEAPLLGFPTMNSNLSEVQKVLQIVDNTVSRQKMDCKAEEISKLKGYHMKDPCSQPEEQGVTSPNIPPVGLPVVSHNGATKSIIDYTLEKVNEAKACLQSLTTDSRRQISNIKKEKLRTLIDLVTDDKMIENHNISTPFSCQFCKESFPGPIPLHQHERYLCKMNEEIKAVLQPHENIVPNKAGVFVDNKALLLSSVLSEKGMTSPINPYKDHMSVLKAYYAMNMEPNSDELLKISIAVGLPQEFVKEWFEQRKVYQYSNSRSPSLERSSKPLAPNSNPPTKDSLLPRSPVKPMDSITSPSIAELHNSVTNCDPPLRLTKPSHFTNIKPVEKLDHSRSNTPSPLNLSSTSSKNSHSSSYTPNSFSSEELQAEPLDLSLPKQMKEPKSIIATKNKTKASSISLDHNSVSSSSENSDEPLNLTFIKKEFSNSNNLDNKSTNPVFSMNPFSAKPLYTALPPQSAFPPATFMPPVQTSIPGLRPYPGLDQMSFLPHMAYTYPTGAATFADMQQRRKYQRKQGFQGELLDGAQDYMSGLDDMTDSDSCLSRKKIKKTESGMYACDLCDKTFQKSSSLLRHKYEHTGKRPHQCQICKKAFKHKHHLIEHSRLHSGEKPYQCDKCGKRFSHSGSYSQHMNHRYSYCKREAEEREAAEREAREKGHLEPTELLMNRAYLQSITPQGYSDSEERESMPRDGESEKEHEKEGEDGYGKLGRQDGDEEFEEEEEESENKSMDTDPETIRDEEETGDHSMDDSSEDGKMETKSDHEEDNMEDGM
| null | null |
astrocyte activation [GO:0048143]; developmental pigmentation [GO:0048066]; endothelial cell migration [GO:0043542]; endothelial cell proliferation [GO:0001935]; fibroblast activation [GO:0072537]; melanocyte migration [GO:0097324]; myofibroblast differentiation [GO:0036446]; negative regulation of fibroblast migration [GO:0010764]; negative regulation of transcription by RNA polymerase II [GO:0000122]; nervous system development [GO:0007399]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of melanin biosynthetic process [GO:0048023]; positive regulation of melanocyte differentiation [GO:0045636]; positive regulation of myofibroblast contraction [GO:1904330]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of transforming growth factor beta receptor signaling pathway [GO:0030511]; pyroptosis [GO:0070269]; regulation of blood-brain barrier permeability [GO:1905603]; regulation of melanosome organization [GO:1903056]; regulation of myofibroblast cell apoptotic process [GO:1904520]; regulation of transcription by RNA polymerase II [GO:0006357]; response to oxygen-glucose deprivation [GO:0090649]; stress fiber assembly [GO:0043149]
|
chromatin [GO:0000785]; cytosol [GO:0005829]; nucleolus [GO:0005730]; 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]; phosphatase regulator activity [GO:0019208]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF00096;PF05605;PF12874;
|
3.30.160.60;1.10.10.60;
|
Delta-EF1/ZFH-1 C2H2-type zinc-finger family
|
PTM: Sumoylation on Lys-391 and Lys-866 is promoted by the E3 SUMO-protein ligase CBX4, and impairs interaction with CTBP1 and transcription repression activity. {ECO:0000269|PubMed:16061479}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16061479, ECO:0000269|PubMed:9853615}. Chromosome {ECO:0000269|PubMed:20516212}.
| null | null | null | null | null |
FUNCTION: Transcriptional inhibitor that binds to DNA sequence 5'-CACCT-3' in different promoters (PubMed:16061479, PubMed:20516212). Represses transcription of E-cadherin (PubMed:16061479). Represses expression of MEOX2 (PubMed:20516212). {ECO:0000269|PubMed:16061479, ECO:0000269|PubMed:20516212}.
|
Homo sapiens (Human)
|
O60318
|
GANP_HUMAN
|
MNPTNPFSGQQPSAFSASSSNVGTLPSKPPFRFGQPSLFGQNSTLSGKSSGFSQVSSFPASSGVSHSSSVQTLGFTQTSSVGPFSGLEHTSTFVATSGPSSSSVLGNTGFSFKSPTSVGAFPSTSAFGQEAGEIVNSGFGKTEFSFKPLENAVFKPILGAESEPEKTQSQIASGFFTFSHPISSAPGGLAPFSFPQVTSSSATTSNFTFSKPVSSNNSLSAFTPALSNQNVEEEKRGPKSIFGSSNNSFSSFPVSSAVLGEPFQASKAGVRQGCEEAVSQVEPLPSLMKGLKRKEDQDRSPRRHGHEPAEDSDPLSRGDHPPDKRPVRLNRPRGGTLFGRTIQDVFKSNKEVGRLGNKEAKKETGFVESAESDHMAIPGGNQSVLAPSRIPGVNKEEETESREKKEDSLRGTPARQSNRSESTDSLGGLSPSEVTAIQCKNIPDYLNDRTILENHFGKIAKVQRIFTRRSKKLAVVHFFDHASAALARKKGKSLHKDMAIFWHRKKISPNKKPFSLKEKKPGDGEVSPSTEDAPFQHSPLGKAAGRTGASSLLNKSSPVKKPSLLKAHQFEGDSFDSASEGSEGLGPCVLSLSTLIGTVAETSKEKYRLLDQRDRIMRQARVKRTDLDKARTFVGTCLDMCPEKERYMRETRSQLSVFEVVPGTDQVDHAAAVKEYSRSSADQEEPLPHELRPLPVLSRTMDYLVTQIMDQKEGSLRDWYDFVWNRTRGIRKDITQQHLCDPLTVSLIEKCTRFHIHCAHFMCEEPMSSFDAKINNENMTKCLQSLKEMYQDLRNKGVFCASEAEFQGYNVLLSLNKGDILREVQQFHPAVRNSSEVKFAVQAFAALNSNNFVRFFKLVQSASYLNACLLHCYFSQIRKDALRALNFAYTVSTQRSTIFPLDGVVRMLLFRDCEEATDFLTCHGLTVSDGCVELNRSAFLEPEGLSKTRKSVFITRKLTVSVGEIVNGGPLPPVPRHTPVCSFNSQNKYIGESLAAELPVSTQRPGSDTVGGGRGEECGVEPDAPLSSLPQSLPAPAPSPVPLPPVLALTPSVAPSLFQLSVQPEPPPPEPVPMYSDEDLAQVVDELIQEALQRDCEEVGSAGAAYAAAALGVSNAAMEDLLTAATTGILRHIAAEEVSKERERREQERQRAEEERLKQERELVLSELSQGLAVELMERVMMEFVRETCSQELKNAVETDQRVRVARCCEDVCAHLVDLFLVEEIFQTAKETLQELQCFCKYLQRWREAVTARKKLRRQMRAFPAAPCCVDVSDRLRALAPSAECPIAEENLARGLLDLGHAGRLGISCTRLRRLRNKTAHQMKVQHFYQQLLSDVAWASLDLPSLVAEHLPGRQEHVFWKLVLVLPDVEEQSPESCGRILANWLKVKFMGDEGSVDDTSSDAGGIQTLSLFNSLSSKGDQMISVNVCIKVAHGALSDGAIDAVETQKDLLGASGLMLLLPPKMKSEDMAEEDVYWLSALLQLKQLLQAKPFQPALPLVVLVPSPGGDAVEKEVEDGLMLQDLVSAKLISDYTVTEIPDTINDLQGSTKVLQAVQWLVSHCPHSLDLCCQTLIQYVEDGIGHEFSGRFFHDRRERRLGGLASQEPGAIIELFNSVLQFLASVVSSEQLCDLSWPVTEFAEAGGSRLLPHLHWNAPEHLAWLKQAVLGFQLPQMDLPPLGAPWLPVCSMVVQYASQIPSSRQTQPVLQSQVENLLHRTYCRWKSKSPSPVHGAGPSVMEIPWDDLIALCINHKLRDWTPPRLPVTSEALSEDGQICVYFFKNDLKKYDVPLSWEQARLQTQKELQLREGRLAIKPFHPSANNFPIPLLHMHRNWKRSTECAQEGRIPSTEDLMRGASAEELLAQCLSSSLLLEKEENKRFEDQLQQWLSEDSGAFTDLTSLPLYLPQTLVSLSHTIEPVMKTSVTTSPQSDMMREQLQLSEATGTCLGERLKHLERLIRSSREEEVASELHLSALLDMVDI
|
2.3.1.-; 2.3.1.48
| null |
mRNA export from nucleus [GO:0006406]; nucleosome organization [GO:0034728]; poly(A)+ mRNA export from nucleus [GO:0016973]; protein transport [GO:0015031]; somatic hypermutation of immunoglobulin genes [GO:0016446]
|
chromosome [GO:0005694]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nuclear membrane [GO:0031965]; nuclear pore nuclear basket [GO:0044615]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription export complex 2 [GO:0070390]
|
chromatin binding [GO:0003682]; histone acetyltransferase activity [GO:0004402]; histone binding [GO:0042393]; histone H3 acetyltransferase activity [GO:0010484]; nucleic acid binding [GO:0003676]
|
PF16766;PF16769;PF16768;PF03399;
|
1.25.40.990;6.10.250.1340;
|
SAC3 family
| null |
SUBCELLULAR LOCATION: [Isoform GANP]: Nucleus envelope {ECO:0000269|PubMed:20005110, ECO:0000269|PubMed:21195085, ECO:0000269|PubMed:22307388, ECO:0000269|PubMed:23591820, ECO:0000269|PubMed:28633435}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:22307388, ECO:0000269|PubMed:23591820}. Nucleus, nucleoplasm {ECO:0000269|PubMed:20005110}. Chromosome {ECO:0000269|PubMed:23652018}. Note=Predominantly located at the nuclear envelope, facing the nucleus interior (PubMed:20005110, PubMed:21195085, PubMed:23591820). Localization at the nuclear pore complex requires NUP153, TPR and ALYREF/ALY (PubMed:22307388, PubMed:23591820). Also found associated with chromatin (PubMed:23652018). In B-cells, targeted to the immunoglobulin variable region genes (PubMed:23652018). {ECO:0000269|PubMed:20005110, ECO:0000269|PubMed:21195085, ECO:0000269|PubMed:22307388, ECO:0000269|PubMed:23591820, ECO:0000269|PubMed:23652018}.; SUBCELLULAR LOCATION: [Isoform MCM3AP]: Cytoplasm {ECO:0000269|PubMed:12226073, ECO:0000269|PubMed:21195085}. Nucleus {ECO:0000269|PubMed:12226073, ECO:0000269|PubMed:21195085}. Note=Translocates into the nucleus in the presence of MCM3 (PubMed:12226073). Associates with chromatin possibly through interaction with MCM3 (PubMed:12226073). {ECO:0000269|PubMed:12226073}.
|
CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-lysyl-[histone] = CoA + H(+) + N(6)-acetyl-L-lysyl-[histone]; Xref=Rhea:RHEA:21992, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:11338, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48; Evidence={ECO:0000269|PubMed:23652018}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21993; Evidence={ECO:0000269|PubMed:23652018};
| null | null | null | null |
FUNCTION: [Isoform GANP]: As a component of the TREX-2 complex, involved in the export of mRNAs to the cytoplasm through the nuclear pores (PubMed:20005110, PubMed:20384790, PubMed:22307388, PubMed:23591820). Through the acetylation of histones, affects the assembly of nucleosomes at immunoglobulin variable region genes and promotes the recruitment and positioning of transcription complex to favor DNA cytosine deaminase AICDA/AID targeting, hence promoting somatic hypermutations (PubMed:23652018). {ECO:0000269|PubMed:20005110, ECO:0000269|PubMed:20384790, ECO:0000269|PubMed:22307388, ECO:0000269|PubMed:23591820, ECO:0000269|PubMed:23652018}.; FUNCTION: [Isoform MCM3AP]: Binds to and acetylates the replication protein MCM3. Plays a role in the initiation of DNA replication and participates in controls that ensure that DNA replication initiates only once per cell cycle (PubMed:11258703, PubMed:12226073). Through the acetylation of histones, affects the assembly of nucleosomes at immunoglobulin variable region genes and promotes the recruitment and positioning of transcription complex to favor DNA cytosine deaminase AICDA/AID targeting, hence promoting somatic hypermutations (PubMed:23652018). {ECO:0000269|PubMed:11258703, ECO:0000269|PubMed:12226073, ECO:0000269|PubMed:23652018}.
|
Homo sapiens (Human)
|
O60331
|
PI51C_HUMAN
|
MELEVPDEAESAEAGAVPSEAAWAAESGAAAGLAQKKAAPTEVLSMTAQPGPGHGKKLGHRGVDASGETTYKKTTSSTLKGAIQLGIGYTVGHLSSKPERDVLMQDFYVVESIFFPSEGSNLTPAHHFQDFRFKTYAPVAFRYFRELFGIRPDDYLYSLCNEPLIELSNPGASGSLFYVTSDDEFIIKTVMHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQSGGKNIRVVVMNNILPRVVKMHLKFDLKGSTYKRRASKKEKEKSFPTYKDLDFMQDMPEGLLLDADTFSALVKTLQRDCLVLESFKIMDYSLLLGVHNIDQHERERQAQGAQSTSDEKRPVGQKALYSTAMESIQGGAARGEAIESDDTMGGIPAVNGRGERLLLHIGIIDILQSYRFIKKLEHTWKALVHDGDTVSVHRPSFYAERFFKFMSNTVFRKNSSLKSSPSKKGRGGALLAVKPLGPTAAFSASQIPSEREEAQYDLRGARSYPTLEDEGRPDLLPCTPPSFEEATTASIATTLSSTSLSIPERSPSETSEQPRYRRRTQSSGQDGRPQEEPPAEEDLQQITVQVEPACSVEIVVPKEEDAGVEASPAGASAAVEVETASQASDEEGAPASQASDEEDAPATDIYFPTDERSWVYSPLHYSAQAPPASDGESDT
|
2.7.1.68
| null |
actin cytoskeleton organization [GO:0030036]; adherens junction assembly [GO:0034333]; cell-cell adhesion [GO:0098609]; clathrin-dependent endocytosis [GO:0072583]; membrane organization [GO:0061024]; neutrophil chemotaxis [GO:0030593]; phagocytosis [GO:0006909]; phosphatidylinositol biosynthetic process [GO:0006661]; phosphatidylinositol phosphate biosynthetic process [GO:0046854]; phosphorylation [GO:0016310]; regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051896]; synaptic vesicle endocytosis [GO:0048488]; synaptic vesicle exocytosis [GO:0016079]
|
adherens junction [GO:0005912]; cytosol [GO:0005829]; endosome membrane [GO:0010008]; focal adhesion [GO:0005925]; nucleoplasm [GO:0005654]; phagocytic cup [GO:0001891]; plasma membrane [GO:0005886]; presynapse [GO:0098793]; ruffle membrane [GO:0032587]; uropod [GO:0001931]
|
1-phosphatidylinositol-4-phosphate 5-kinase activity [GO:0016308]; ATP binding [GO:0005524]; phosphatidylinositol kinase activity [GO:0052742]
|
PF01504;
|
3.30.810.10;3.30.800.10;
| null |
PTM: Phosphorylation on Ser-650 negatively regulates binding to TLN2 and is strongly stimulated in mitosis. Phosphorylation on Tyr-649 is necessary for targeting to focal adhesions. Phosphorylation on Ser-650 and Tyr-649 are mutually exclusive. Phosphorylated by SYK and CSK (By similarity). Tyrosine phosphorylation is enhanced by PTK2 signaling. Phosphorylated at Tyr-639 upon EGF stimulation. Some studies suggest that phosphorylation on Tyr-649 enhances binding to tailins (TLN1 and TLN2). According to PubMed:15738269 phosphorylation at Tyr-649 does not directly enhance binding to tailins (TLN1 and TLN2) but may act indirectly by inhibiting phosphorylation at Ser-650. {ECO:0000250, ECO:0000269|PubMed:15738269}.; PTM: Acetylation at Lys-265 and Lys-268 seems to decrease lipid 1-phosphatidylinositol-4-phosphate 5-kinase activity. Deacetylation of these sites by SIRT1 positively regulates the exocytosis of TSH-containing granules from pituitary cells. {ECO:0000269|PubMed:20668706}.
|
SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side {ECO:0000250|UniProtKB:Q5I6B8}. Endomembrane system {ECO:0000250|UniProtKB:Q5I6B8}. Cytoplasm {ECO:0000250|UniProtKB:O70161}. Cell junction, focal adhesion {ECO:0000269|PubMed:12422219}. Cell junction, adherens junction {ECO:0000269|PubMed:17261850}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:Q5I6B8}. Cell projection, phagocytic cup {ECO:0000250|UniProtKB:O70161}. Cell projection, uropodium {ECO:0000250|UniProtKB:O70161}. Note=Detected in plasma membrane invaginations. Isoform 3 is detected in intracellular vesicle-like structures.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. Nucleus.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:14425, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58178, ChEBI:CHEBI:58456, ChEBI:CHEBI:456216; EC=2.7.1.68; Evidence={ECO:0000269|PubMed:12422219, ECO:0000269|PubMed:22942276}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14426; Evidence={ECO:0000305|PubMed:12422219, ECO:0000305|PubMed:22942276}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phospho-1D-myo-inositol 4-phosphate + ATP = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phospho-1D-myo-inositol 4,5-bisphosphate + ADP + H(+); Xref=Rhea:RHEA:40363, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:77136, ChEBI:CHEBI:77137, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:22942276}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40364; Evidence={ECO:0000305|PubMed:22942276}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(9Z)-octadecenoyl-sn-glycero-3-phospho-1D-myo-inositol 4-phosphate + ATP = 1-octadecanoyl-2-(9Z)-octadecenoyl-sn-glycero-3-phospho-1D-myo-inositol 4,5-bisphosphate + ADP + H(+); Xref=Rhea:RHEA:40367, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:77139, ChEBI:CHEBI:77140, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:22942276}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40368; Evidence={ECO:0000305|PubMed:22942276}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(9Z)-octadecenoyl-sn-glycero-3-phospho-1D-myo-inositol + ATP = 1-octadecanoyl-2-(9Z)-octadecenoyl-sn-glycero-3-phospho-1D-myo-inositol 5-phosphate + ADP + H(+); Xref=Rhea:RHEA:40379, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:77163, ChEBI:CHEBI:77164, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:22942276}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40380; Evidence={ECO:0000305|PubMed:22942276}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(9Z,12Z)-octadecadienoyl-sn-glycero-3-phospho-1D-myo-inositol + ATP = 1-octadecanoyl-2-(9Z,12Z)-octadecadienoyl-sn-glycero-3-phospho-1D-myo-inositol 5-phosphate + ADP + H(+); Xref=Rhea:RHEA:40383, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:77158, ChEBI:CHEBI:77159, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:22942276}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40384; Evidence={ECO:0000305|PubMed:22942276}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phospho-1D-myo-inositol 5-phosphate + ADP + H(+); Xref=Rhea:RHEA:40375, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:77160, ChEBI:CHEBI:133606, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:22942276}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40376; Evidence={ECO:0000305|PubMed:22942276}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z,12Z)-octadecadienoyl-sn-glycero-3-phospho-1D-myo-inositol + ATP = 1,2-di(9Z,12Z)-octadecadienoyl-sn-glycero-3-phospho-1D-myo-inositol 5-phosphate + ADP + H(+); Xref=Rhea:RHEA:40387, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:77165, ChEBI:CHEBI:77167, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:22942276}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40388; Evidence={ECO:0000305|PubMed:22942276};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.6 uM for 1-octadecanoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phospho-1D-myo-inositol 4-phosphate {ECO:0000269|PubMed:22942276}; KM=15 uM for 1-octadecanoyl-2-(9Z)-octadecenoyl-sn-glycero-3-phospho-1D-myo-inositol 4-phosphate {ECO:0000269|PubMed:22942276};
| null | null | null |
FUNCTION: Catalyzes the phosphorylation of phosphatidylinositol 4-phosphate (PtdIns(4)P/PI4P) to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2/PIP2), a lipid second messenger that regulates several cellular processes such as signal transduction, vesicle trafficking, actin cytoskeleton dynamics, cell adhesion, and cell motility (PubMed:12422219, PubMed:22942276). PtdIns(4,5)P2 can directly act as a second messenger or can be utilized as a precursor to generate other second messengers: inositol 1,4,5-trisphosphate (IP3), diacylglycerol (DAG) or phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3/PIP3) (Probable). PIP5K1A-mediated phosphorylation of PtdIns(4)P is the predominant pathway for PtdIns(4,5)P2 synthesis (By similarity). Together with PIP5K1A, is required for phagocytosis, both enzymes regulating different types of actin remodeling at sequential steps (By similarity). Promotes particle attachment by generating the pool of PtdIns(4,5)P2 that induces controlled actin depolymerization to facilitate Fc-gamma-R clustering. Mediates RAC1-dependent reorganization of actin filaments. Required for synaptic vesicle transport (By similarity). Controls the plasma membrane pool of PtdIns(4,5)P2 implicated in synaptic vesicle endocytosis and exocytosis (PubMed:12847086). Plays a role in endocytosis mediated by clathrin and AP-2 (adaptor protein complex 2) (PubMed:12847086). Required for clathrin-coated pits assembly at the synapse (PubMed:17261850). Participates in cell junction assembly (PubMed:17261850). Modulates adherens junctions formation by facilitating CDH1/cadherin trafficking (PubMed:17261850). Required for focal adhesion dynamics. Modulates the targeting of talins (TLN1 and TLN2) to the plasma membrane and their efficient assembly into focal adhesions (PubMed:12422219). Regulates the interaction between talins (TLN1 and TLN2) and beta-integrins (PubMed:12422219). Required for uropodium formation and retraction of the cell rear during directed migration (By similarity). Has a role in growth factor-stimulated directional cell migration and adhesion (By similarity). Required for talin assembly into nascent adhesions forming at the leading edge toward the direction of the growth factor (PubMed:17635937). Negative regulator of T-cell activation and adhesion (By similarity). Negatively regulates integrin alpha-L/beta-2 (LFA-1) polarization and adhesion induced by T-cell receptor (By similarity). Together with PIP5K1A has a role during embryogenesis and together with PIP5K1B may have a role immediately after birth (By similarity). {ECO:0000250|UniProtKB:O70161, ECO:0000250|UniProtKB:P70182, ECO:0000269|PubMed:12422219, ECO:0000269|PubMed:12847086, ECO:0000269|PubMed:17261850, ECO:0000269|PubMed:17635937, ECO:0000269|PubMed:22942276, ECO:0000305|PubMed:19889969}.
|
Homo sapiens (Human)
|
O60333
|
KIF1B_HUMAN
|
MSGASVKVAVRVRPFNSRETSKESKCIIQMQGNSTSIINPKNPKEAPKSFSFDYSYWSHTSPEDPCFASQNRVYNDIGKEMLLHAFEGYNVCIFAYGQTGAGKSYTMMGKQEESQAGIIPQLCEELFEKINDNCNEEMSYSVEVSYMEIYCERVRDLLNPKNKGNLRVREHPLLGPYVEDLSKLAVTSYTDIADLMDAGNKARTVAATNMNETSSRSHAVFTIVFTQKKHDNETNLSTEKVSKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEVDNCTSKSKKKKKTDFIPYRDSVLTWLLRENLGGNSRTAMVAALSPADINYDETLSTLRYADRAKQIKCNAVINEDPNAKLVRELKEEVTRLKDLLRAQGLGDIIDIDPLIDDYSGSGSKYLKDFQNNKHRYLLASENQRPGHFSTASMGSLTSSPSSCSLSSQVGLTSVTSIQERIMSTPGGEEAIERLKESEKIIAELNETWEEKLRKTEAIRMEREALLAEMGVAIREDGGTLGVFSPKKTPHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQDIVLSGAHIKEEHCIFRSERSNSGEVIVTLEPCERSETYVNGKRVSQPVQLRSGNRIIMGKNHVFRFNHPEQARAEREKTPSAETPSEPVDWTFAQRELLEKQGIDMKQEMEKRLQEMEILYKKEKEEADLLLEQQRLDYESKLQALQKQVETRSLAAETTEEEEEEEEVPWTQHEFELAQWAFRKWKSHQFTSLRDLLWGNAVYLKEANAISVELKKKVQFQFVLLTDTLYSPLPPELLPTEMEKTHEDRPFPRTVVAVEVQDLKNGATHYWSLEKLKQRLDLMREMYDRAGEMASSAQDESETTVTGSDPFYDRFHWFKLVGSSPIFHGCVNERLADRTPSPTFSTADSDITELADEQQDEMEDFDDEAFVDDAGSDAGTEEGSDLFSDGHDPFYDRSPWFILVGRAFVYLSNLLYPVPLIHRVAIVSEKGEVRGFLRVAVQAIAADEEAPDYGSGIRQSGTAKISFDNEYFNQSDFSSVAMTRSGLSLEELRIVEGQGQSSEVITPPEEISRINDLDLKSSTLLDGKMVMEGFSEEIGNHLKLGSAFTFRVTVLQASGILPEYADIFCQFNFLHRHDEAFSTEPLKNNGRGSPLAFYHVQNIAVEITESFVDYIKTKPIVFEVFGHYQQHPLHLQGQELNSPPQPCRRFFPPPMPLSKPVPATKLNTMSKTSLGQSMSKYDLLVWFEISELEPTGEYIPAVVDHTAGLPCQGTFLLHQGIQRRITVTIIHEKGSELHWKDVRELVVGRIRNKPEVDEAAVDAILSLNIISAKYLKSSHNSSRTFYRFEAVWDSSLHNSLLLNRVTPYGEKIYMTLSAYLELDHCIQPAVITKDVCMVFYSRDAKISPPRSLRSLFGSGYSKSPDSNRVTGIYELSLCKMSDTGSPGMQRRRRKILDTSVAYVRGEENLAGWRPRGDSLILEHQWELEKLELLHEVEKTRHFLLLRERLGDSIPKSLSDSLSPSLSSGTLSTSTSISSQISTTTFESAITPSESSGYDSGDIESLVDREKELATKCLQLLTHTFNREFSQVHGSVSDCKLSDISPIGRDPSESSFSSATLTPSSTCPSLVDSRSNSLDQKTPEANSRASSPCPEFEQFQIVPAVETPYLARAGKNEFLNLVPDIEEIRPSSVVSKKGYLHFKEPLYSNWAKHFVVVRRPYVFIYNSDKDPVERGIINLSTAQVEYSEDQQAMVKTPNTFAVCTKHRGVLLQALNDKDMNDWLYAFNPLLAGTIRSKLSRRCPSQSKY
| null | null |
anterograde axonal transport [GO:0008089]; apoptotic process [GO:0006915]; cytoskeleton-dependent intracellular transport [GO:0030705]; microtubule-based movement [GO:0007018]; neuromuscular synaptic transmission [GO:0007274]; neuron-neuron synaptic transmission [GO:0007270]; vesicle-mediated transport [GO:0016192]
|
axon [GO:0030424]; axon cytoplasm [GO:1904115]; cytoplasmic vesicle [GO:0031410]; cytoplasmic vesicle membrane [GO:0030659]; dendrite [GO:0030425]; kinesin complex [GO:0005871]; microtubule [GO:0005874]; microtubule associated complex [GO:0005875]; mitochondrion [GO:0005739]; neuron projection [GO:0043005]; synaptic vesicle [GO:0008021]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; kinesin binding [GO:0019894]; microtubule binding [GO:0008017]; plus-end-directed microtubule motor activity [GO:0008574]
|
PF12473;PF00498;PF12423;PF00225;PF16183;PF00169;
|
2.60.200.20;6.10.250.2520;3.40.850.10;2.30.29.30;
|
TRAFAC class myosin-kinesin ATPase superfamily, Kinesin family, Unc-104 subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Mitochondrion {ECO:0000269|PubMed:16225668}. Cell projection, axon {ECO:0000250|UniProtKB:Q60575}.; SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000250|UniProtKB:O88658}.
| null | null | null | null | null |
FUNCTION: Motor for anterograde transport of mitochondria. Has a microtubule plus end-directed motility. Isoform 2 is required for induction of neuronal apoptosis. {ECO:0000269|PubMed:18334619}.; FUNCTION: Isoform 1 mediates the transport of synaptic vesicles in neuronal cells. {ECO:0000250|UniProtKB:O88658}.
|
Homo sapiens (Human)
|
O60336
|
MABP1_HUMAN
|
MAVEGSTITSRIKNLLRSPSIKLRRSKAGNRREDLSSKVTLEKVLGITVSGGRGLACDPRSGLVAYPAGCVVVLFNPRKHKQHHILNSSRKTITALAFSPDGKYLVTGESGHMPAVRVWDVAEHSQVAELQEHKYGVACVAFSPSAKYIVSVGYQHDMIVNVWAWKKNIVVASNKVSSRVTAVSFSEDCSYFVTAGNRHIKFWYLDDSKTSKVNATVPLLGRSGLLGELRNNLFTDVACGRGKKADSTFCITSSGLLCEFSDRRLLDKWVELRNIDSFTTTVAHCISVSQDYIFCGCADGTVRLFNPSNLHFLSTLPRPHALGTDIASVTEASRLFSGVANARYPDTIALTFDPTNQWLSCVYNDHSIYVWDVRDPKKVGKVYSALYHSSCVWSVEVYPEVKDSNQACLPPSSFITCSSDNTIRLWNTESSGVHGSTLHRNILSSDLIKIIYVDGNTQALLDTELPGGDKADASLLDPRVGIRSVCVSPNGQHLASGDRMGTLRVHELQSLSEMLKVEAHDSEILCLEYSKPDTGLKLLASASRDRLIHVLDAGREYSLQQTLDEHSSSITAVKFAASDGQVRMISCGADKSIYFRTAQKSGDGVQFTRTHHVVRKTTLYDMDVEPSWKYTAIGCQDRNIRIFNISSGKQKKLFKGSQGEDGTLIKVQTDPSGIYIATSCSDKNLSIFDFSSGECVATMFGHSEIVTGMKFSNDCKHLISVSGDSCIFVWRLSSEMTISMRQRLAELRQRQRGGKQQGPSSPQRASGPNRHQAPSMLSPGPALSSDSDKEGEDEGTEEELPALPVLAKSTKKALASVPSPALPRSLSHWEMSRAQESVGFLDPAPAANPGPRRRGRWVQPGVELSVRSMLDLRQLETLAPSLQDPSQDSLAIIPSGPRKHGQEALETSLTSQNEKPPRPQASQPCSYPHIIRLLSQEEGVFAQDLEPAPIEDGIVYPEPSDNPTMDTSEFQVQAPARGTLGRVYPGSRSSEKHSPDSACSVDYSSSCLSSPEHPTEDSESTEPLSVDGISSDLEEPAEGDEEEEEEEGGMGPYGLQEGSPQTPDQEQFLKQHFETLASGAAPGAPVQVPERSESRSISSRFLLQVQTRPLREPSPSSSSLALMSRPAQVPQASGEQPRGNGANPPGAPPEVEPSSGNPSPQQAASVLLPRCRLNPDSSWAPKRVATASPFSGLQKAQSVHSLVPQERHEASLQAPSPGALLSREIEAQDGLGSLPPADGRPSRPHSYQNPTTSSMAKISRSISVGENLGLVAEPQAHAPIRVSPLSKLALPSRAHLVLDIPKPLPDRPTLAAFSPVTKGRAPGEAEKPGFPVGLGKAHSTTERWACLGEGTTPKPRTECQAHPGPSSPCAQQLPVSSLFQGPENLQPPPPEKTPNPMECTKPGAALSQDSEPAVSLEQCEQLVAELRGSVRQAVRLYHSVAGCKMPSAEQSRIAQLLRDTFSSVRQELEAVAGAVLSSPGSSPGAVGAEQTQALLEQYSELLLRAVERRMERKL
| null | null |
negative regulation of canonical NF-kappaB signal transduction [GO:0043124]; negative regulation of defense response to bacterium [GO:1900425]; negative regulation of interleukin-8 production [GO:0032717]; positive regulation of JNK cascade [GO:0046330]
|
cytoplasm [GO:0005737]; mitotic spindle pole [GO:0097431]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]
| null |
PF00400;
|
2.130.10.10;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22700971, ECO:0000269|PubMed:28089251}. Nucleus {ECO:0000269|PubMed:22700971}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:28089251}. Note=Not detected in the cilium. Localized around the poles of the mitotic spindle from prophase to anaphase in mitotic cells. {ECO:0000269|PubMed:28089251}.
| null | null | null | null | null |
FUNCTION: Negative regulator of NOD2 function. It down-regulates NOD2-induced processes such as activation of NF-kappa-B signaling, IL8 secretion and antibacterial response (PubMed:22700971). Involved in JNK signaling pathway (By similarity). {ECO:0000250|UniProtKB:Q6NS57, ECO:0000269|PubMed:22700971}.
|
Homo sapiens (Human)
|
O60337
|
MARH6_HUMAN
|
MDTAEEDICRVCRSEGTPEKPLYHPCVCTGSIKFIHQECLVQWLKHSRKEYCELCKHRFAFTPIYSPDMPSRLPIQDIFAGLVTSIGTAIRYWFHYTLVAFAWLGVVPLTACRIYKCLFTGSVSSLLTLPLDMLSTENLLADCLQGCFVVTCTLCAFISLVWLREQIVHGGAPIWLEHAAPPFNAAGHHQNEAPAGGNGAENVAADQPANPPAENAVVGENPDAQDDQAEEEEEDNEEEDDAGVEDAADANNGAQDDMNWNALEWDRAAEELTWERMLGLDGSLVFLEHVFWVVSLNTLFILVFAFCPYHIGHFSLVGLGFEEHVQASHFEGLITTIVGYILLAITLIICHGLATLVKFHRSRRLLGVCYIVVKVSLLVVVEIGVFPLICGWWLDICSLEMFDATLKDRELSFQSAPGTTMFLHWLVGMVYVFYFASFILLLREVLRPGVLWFLRNLNDPDFNPVQEMIHLPIYRHLRRFILSVIVFGSIVLLMLWLPIRIIKSVLPNFLPYNVMLYSDAPVSELSLELLLLQVVLPALLEQGHTRQWLKGLVRAWTVTAGYLLDLHSYLLGDQEENENSANQQVNNNQHARNNNAIPVVGEGLHAAHQAILQQGGPVGFQPYRRPLNFPLRIFLLIVFMCITLLIASLICLTLPVFAGRWLMSFWTGTAKIHELYTAACGLYVCWLTIRAVTVMVAWMPQGRRVIFQKVKEWSLMIMKTLIVAVLLAGVVPLLLGLLFELVIVAPLRVPLDQTPLFYPWQDWALGVLHAKIIAAITLMGPQWWLKTVIEQVYANGIRNIDLHYIVRKLAAPVISVLLLSLCVPYVIASGVVPLLGVTAEMQNLVHRRIYPFLLMVVVLMAILSFQVRQFKRLYEHIKNDKYLVGQRLVNYERKSGKQGSSPPPPQSSQE
|
2.3.2.27
| null |
ERAD pathway [GO:0036503]; proteasomal protein catabolic process [GO:0010498]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein K48-linked ubiquitination [GO:0070936]; protein ubiquitination [GO:0016567]
|
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; ER ubiquitin ligase complex [GO:0000835]; membrane [GO:0016020]
|
enzyme binding [GO:0019899]; ubiquitin conjugating enzyme binding [GO:0031624]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]; ubiquitin-specific protease binding [GO:1990381]; zinc ion binding [GO:0008270]
|
PF12906;
|
3.30.40.10;
| null |
PTM: Auto-ubiquitinated, which results in proteasomal degradation. {ECO:0000269|PubMed:15673284}.
|
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15673284}; Multi-pass membrane protein {ECO:0000269|PubMed:15673284}.
|
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:15673284};
| null |
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:15673284}.
| null | null |
FUNCTION: E3 ubiquitin-protein ligase that promotes 'Lys-48'-linked ubiquitination of target proteins, leading to their proteasomal degradation (PubMed:15673284). Promotes ubiquitination of DIO2, leading to its degradation (PubMed:19651899). Promotes ubiquitination of SQLE, leading to its degradation (PubMed:24449766). E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates. May cooperate with UBE2G1 (PubMed:15673284). {ECO:0000269|PubMed:15673284, ECO:0000269|PubMed:19651899, ECO:0000269|PubMed:24449766}.
|
Homo sapiens (Human)
|
O60341
|
KDM1A_HUMAN
|
MLSGKKAAAAAAAAAAAATGTEAGPGTAGGSENGSEVAAQPAGLSGPAEVGPGAVGERTPRKKEPPRASPPGGLAEPPGSAGPQAGPTVVPGSATPMETGIAETPEGRRTSRRKRAKVEYREMDESLANLSEDEYYSEEERNAKAEKEKKLPPPPPQAPPEEENESEPEEPSGVEGAAFQSRLPHDRMTSQEAACFPDIISGPQQTQKVFLFIRNRTLQLWLDNPKIQLTFEATLQQLEAPYNSDTVLVHRVHSYLERHGLINFGIYKRIKPLPTKKTGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNYVADLGAMVVTGLGGNPMAVVSKQVNMELAKIKQKCPLYEANGQAVPKEKDEMVEQEFNRLLEATSYLSHQLDFNVLNNKPVSLGQALEVVIQLQEKHVKDEQIEHWKKIVKTQEELKELLNKMVNLKEKIKELHQQYKEASEVKPPRDITAEFLVKSKHRDLTALCKEYDELAETQGKLEEKLQELEANPPSDVYLSSRDRQILDWHFANLEFANATPLSTLSLKHWDQDDDFEFTGSHLTVRNGYSCVPVALAEGLDIKLNTAVRQVRYTASGCEVIAVNTRSTSQTFIYKCDAVLCTLPLGVLKQQPPAVQFVPPLPEWKTSAVQRMGFGNLNKVVLCFDRVFWDPSVNLFGHVGSTTASRGELFLFWNLYKAPILLALVAGEAAGIMENISDDVIVGRCLAILKGIFGSSAVPQPKETVVSRWRADPWARGSYSYVAAGSSGNDYDLMAQPITPGPSIPGAPQPIPRLFFAGEHTIRNYPATVHGALLSGLREAGRIADQFLGAMYTLPRQATPGVPAQQSPSM
|
1.14.99.66
|
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:15620353, ECO:0000269|PubMed:15811342, ECO:0000269|PubMed:16956976, ECO:0000269|PubMed:21300290, ECO:0000269|PubMed:23721412};
|
cellular response to cAMP [GO:0071320]; cellular response to gamma radiation [GO:0071480]; cellular response to UV [GO:0034644]; cerebral cortex development [GO:0021987]; DNA repair-dependent chromatin remodeling [GO:0140861]; guanine metabolic process [GO:0046098]; muscle cell development [GO:0055001]; negative regulation of DNA binding [GO:0043392]; negative regulation of DNA damage response, signal transduction by p53 class mediator [GO:0043518]; negative regulation of DNA-binding transcription factor activity [GO:0043433]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator [GO:1902166]; negative regulation of protein binding [GO:0032091]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neuron maturation [GO:0042551]; positive regulation of cell size [GO:0045793]; positive regulation of cold-induced thermogenesis [GO:0120162]; positive regulation of epithelial to mesenchymal transition [GO:0010718]; positive regulation of neural precursor cell proliferation [GO:2000179]; positive regulation of neuroblast proliferation [GO:0002052]; positive regulation of neuron projection development [GO:0010976]; positive regulation of protein ubiquitination [GO:0031398]; positive regulation of stem cell proliferation [GO:2000648]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein demethylation [GO:0006482]; regulation of androgen receptor signaling pathway [GO:0060765]; regulation of DNA methylation-dependent heterochromatin formation [GO:0090308]; regulation of double-strand break repair via homologous recombination [GO:0010569]; regulation of protein localization [GO:0032880]; regulation of transcription by RNA polymerase II [GO:0006357]; response to fungicide [GO:0060992]
|
chromatin [GO:0000785]; chromosome, telomeric region [GO:0000781]; DNA repair complex [GO:1990391]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; transcription regulator complex [GO:0005667]
|
chromatin binding [GO:0003682]; demethylase activity [GO:0032451]; DNA-binding transcription factor binding [GO:0140297]; enzyme binding [GO:0019899]; FAD-dependent H3K4me/H3K4me3 demethylase activity [GO:0140682]; flavin adenine dinucleotide binding [GO:0050660]; histone demethylase activity [GO:0032452]; histone H3K4 demethylase activity [GO:0032453]; histone H3K9 demethylase activity [GO:0032454]; identical protein binding [GO:0042802]; MRF binding [GO:0043426]; nuclear androgen receptor binding [GO:0050681]; nuclear receptor coactivator activity [GO:0030374]; oxidoreductase activity [GO:0016491]; p53 binding [GO:0002039]; promoter-specific chromatin binding [GO:1990841]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; telomeric repeat-containing RNA binding [GO:0061752]; transcription coactivator activity [GO:0003713]
|
PF01593;PF04433;
|
3.90.660.10;1.10.287.80;3.50.50.60;1.10.10.10;
|
Flavin monoamine oxidase family
|
PTM: Acetylated by KAT8 in epithelial but not in mesenchymal cells, thereby regulating the epithelial-to-mesenchymal transition (PubMed:27292636). Acetylation by KAT8 reduces KDM1A association with nucleosomes, thereby decreasing histone H3 demethylation, leading to transcription activatio of target genes (PubMed:27292636). {ECO:0000269|PubMed:27292636}.; PTM: Polyubiquitinated by JADE2; which leads to its proteasomal degradation (PubMed:25018020). Deubiquitinated by USP38; preventing it from degradation by the 26S proteasome (PubMed:30497519). {ECO:0000269|PubMed:25018020, ECO:0000269|PubMed:30497519}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11102443, ECO:0000269|PubMed:16079795, ECO:0000269|PubMed:20389281, ECO:0000269|PubMed:33980486}. Chromosome {ECO:0000269|PubMed:16079795, ECO:0000269|PubMed:20228790, ECO:0000269|PubMed:27292636, ECO:0000269|PubMed:33980486}. Note=Associates with chromatin. {ECO:0000269|PubMed:16079795, ECO:0000269|PubMed:20228790, ECO:0000269|PubMed:27292636, ECO:0000269|PubMed:33980486}.
|
CATALYTIC ACTIVITY: Reaction=2 A + 2 H2O + N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] = 2 AH2 + 2 formaldehyde + L-lysyl(4)-[histone H3]; Xref=Rhea:RHEA:60244, Rhea:RHEA-COMP:15540, Rhea:RHEA-COMP:15547, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:16842, ChEBI:CHEBI:17499, ChEBI:CHEBI:29969, ChEBI:CHEBI:61976; EC=1.14.99.66; Evidence={ECO:0000269|PubMed:15620353, ECO:0000269|PubMed:15811342, ECO:0000269|PubMed:27292636};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3 uM for H3 monomethyl-K4 {ECO:0000269|PubMed:16223729}; KM=4.2 uM for H3 dimethyl-K4 {ECO:0000269|PubMed:16223729}; KM=3.9 uM for H3 monomethyl-K4-monomethyl-K9 {ECO:0000269|PubMed:16223729}; KM=17.5 uM for monomethyl-K4-acetyl-K9 {ECO:0000269|PubMed:16223729};
| null | null | null |
FUNCTION: Histone demethylase that can demethylate both 'Lys-4' (H3K4me) and 'Lys-9' (H3K9me) of histone H3, thereby acting as a coactivator or a corepressor, depending on the context (PubMed:15620353, PubMed:15811342, PubMed:16079794, PubMed:16079795, PubMed:16140033, PubMed:16223729, PubMed:27292636). Acts by oxidizing the substrate by FAD to generate the corresponding imine that is subsequently hydrolyzed (PubMed:15620353, PubMed:15811342, PubMed:16079794, PubMed:21300290). Acts as a corepressor by mediating demethylation of H3K4me, a specific tag for epigenetic transcriptional activation. Demethylates both mono- (H3K4me1) and di-methylated (H3K4me2) H3K4me (PubMed:15620353, PubMed:20389281, PubMed:21300290, PubMed:23721412). May play a role in the repression of neuronal genes. Alone, it is unable to demethylate H3K4me on nucleosomes and requires the presence of RCOR1/CoREST to achieve such activity (PubMed:16079794, PubMed:16140033, PubMed:16885027, PubMed:21300290, PubMed:23721412). Also acts as a coactivator of androgen receptor (AR)-dependent transcription, by being recruited to AR target genes and mediating demethylation of H3K9me, a specific tag for epigenetic transcriptional repression. The presence of PRKCB in AR-containing complexes, which mediates phosphorylation of 'Thr-6' of histone H3 (H3T6ph), a specific tag that prevents demethylation H3K4me, prevents H3K4me demethylase activity of KDM1A (PubMed:16079795). Demethylates di-methylated 'Lys-370' of p53/TP53 which prevents interaction of p53/TP53 with TP53BP1 and represses p53/TP53-mediated transcriptional activation. Demethylates and stabilizes the DNA methylase DNMT1 (PubMed:29691401). Demethylates methylated 'Lys-42' and methylated 'Lys-117' of SOX2 (PubMed:29358331). Required for gastrulation during embryogenesis. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development (PubMed:16079794, PubMed:16140033). Facilitates epithelial-to-mesenchymal transition by acting as an effector of SNAI1-mediated transcription repression of epithelial markers E-cadherin/CDH1, CDN7 and KRT8 (PubMed:20562920, PubMed:27292636). Required for the maintenance of the silenced state of the SNAI1 target genes E-cadherin/CDH1 and CDN7 (PubMed:20389281). {ECO:0000269|PubMed:12032298, ECO:0000269|PubMed:15620353, ECO:0000269|PubMed:15811342, ECO:0000269|PubMed:16079794, ECO:0000269|PubMed:16079795, ECO:0000269|PubMed:16140033, ECO:0000269|PubMed:16223729, ECO:0000269|PubMed:16885027, ECO:0000269|PubMed:16956976, ECO:0000269|PubMed:17805299, ECO:0000269|PubMed:20228790, ECO:0000269|PubMed:20389281, ECO:0000269|PubMed:20562920, ECO:0000269|PubMed:21300290, ECO:0000269|PubMed:23721412, ECO:0000269|PubMed:27292636, ECO:0000269|PubMed:29358331, ECO:0000269|PubMed:29691401}.
|
Homo sapiens (Human)
|
O60343
|
TBCD4_HUMAN
|
MEPPSCIQDEPFPHPLEPEPGVSAQPGPGKPSDKRFRLWYVGGSCLDHRTTLPMLPWLMAEIRRRSQKPEAGGCGAPAAREVILVLSAPFLRCVPAPGAGASGGTSPSATQPNPAVFIFEHKAQHISRFIHNSHDLTYFAYLIKAQPDDPESQMACHVFRATDPSQVPDVISSIRQLSKAAMKEDAKPSKDNEDAFYNSQKFEVLYCGKVTVTHKKAPSSLIDDCMEKFSLHEQQRLKIQGEQRGPDPGEDLADLEVVVPGSPGDCLPEEADGTDTHLGLPAGASQPALTSSRVCFPERILEDSGFDEQQEFRSRCSSVTGVQRRVHEGSQKSQPRRRHASAPSHVQPSDSEKNRTMLFQVGRFEINLISPDTKSVVLEKNFKDISSCSQGIKHVDHFGFICRESPEPGLSQYICYVFQCASESLVDEVMLTLKQAFSTAAALQSAKTQIKLCEACPMHSLHKLCERIEGLYPPRAKLVIQRHLSSLTDNEQADIFERVQKMKPVSDQEENELVILHLRQLCEAKQKTHVHIGEGPSTISNSTIPENATSSGRFKLDILKNKAKRSLTSSLENIFSRGANRMRGRLGSVDSFERSNSLASEKDYSPGDSPPGTPPASPPSSAWQTFPEEDSDSPQFRRRAHTFSHPPSSTKRKLNLQDGRAQGVRSPLLRQSSSEQCSNLSSVRRMYKESNSSSSLPSLHTSFSAPSFTAPSFLKSFYQNSGRLSPQYENEIRQDTASESSDGEGRKRTSSTCSNESLSVGGTSVTPRRISWRQRIFLRVASPMNKSPSAMQQQDGLDRNELLPLSPLSPTMEEEPLVVFLSGEDDPEKIEERKKSKELRSLWRKAIHQQILLLRMEKENQKLEASRDELQSRKVKLDYEEVGACQKEVLITWDKKLLNCRAKIRCDMEDIHTLLKEGVPKSRRGEIWQFLALQYRLRHRLPNKQQPPDISYKELLKQLTAQQHAILVDLGRTFPTHPYFSVQLGPGQLSLFNLLKAYSLLDKEVGYCQGISFVAGVLLLHMSEEQAFEMLKFLMYDLGFRKQYRPDMMSLQIQMYQLSRLLHDYHRDLYNHLEENEISPSLYAAPWFLTLFASQFSLGFVARVFDIIFLQGTEVIFKVALSLLSSQETLIMECESFENIVEFLKNTLPDMNTSEMEKIITQVFEMDISKQLHAYEVEYHVLQDELQESSYSCEDSETLEKLERANSQLKRQNMDLLEKLQVAHTKIQALESNLENLLTRETKMKSLIRTLEQEKMAYQKTVEQLRKLLPADALVNCDLLLRDLNCNPNNKAKIGNKP
| null | null |
cellular response to insulin stimulus [GO:0032869]; negative regulation of vesicle fusion [GO:0031339]; vesicle-mediated transport [GO:0016192]
|
cytosol [GO:0005829]; vesicle [GO:0031982]
|
GTPase activator activity [GO:0005096]
|
PF11830;PF00640;PF00566;
|
1.10.10.2750;2.30.29.30;1.10.8.270;1.10.472.80;
| null |
PTM: Phosphorylated by AKT1; insulin-induced. Also phosphorylated by AMPK in response to insulin. Insulin-stimulated phosphorylation is required for SLC2A4/GLUT4 translocation. Has no effect on SLC2A4/GLUT4 internalization. Physiological hyperinsulinemia increases phosphorylation in skeletal muscle. Insulin-stimulated phosphorylation is reduced by 39% in type 2 diabetic patients. {ECO:0000269|PubMed:11994271, ECO:0000269|PubMed:15919790, ECO:0000269|PubMed:18771725}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18771725}. Note=Isoform 2 shows a cytoplasmic perinuclear localization in a myoblastic cell line in resting and insulin-stimulated cells.
| null | null | null | null | null |
FUNCTION: May act as a GTPase-activating protein for RAB2A, RAB8A, RAB10 and RAB14. Isoform 2 promotes insulin-induced glucose transporter SLC2A4/GLUT4 translocation at the plasma membrane, thus increasing glucose uptake. {ECO:0000269|PubMed:15971998, ECO:0000269|PubMed:18771725, ECO:0000269|PubMed:22908308}.
|
Homo sapiens (Human)
|
O60346
|
PHLP1_HUMAN
|
MEPAAAATVQRLPELGREDRASAPAAAAAAAAAAAAAAAALAAAAGGGRSPEPALTPAAPSGGNGSGSGAREEAPGEAPPGPLPGRAGGAGRRRRRGAPQPIAGGAAPVPGAGGGANSLLLRRGRLKRNLSAAAAAASSSSSSSAAAASHSPGAAGLPASCSASASLCTRSLDRKTLLLKHRQTLQLQPSDRDWVRHQLQRGCVHVFDRHMASTYLRPVLCTLDTTAGEVAARLLQLGHKGGGVVKVLGQGPGAAAAREPAEPPPEAGPRLAPPEPRDSEVPPARSAPGAFGGPPRAPPADLPLPVGGPGGWSRRASPAPSDSSPGEPFVGGPVSSPRAPRPVVSDTESFSLSPSAESVSDRLDPYSSGGGSSSSSEELEADAASAPTGVPGQPRRPGHPAQPLPLPQTASSPQPQQKAPRAIDSPGGAVREGSCEEKAAAAVAPGGLQSTPGRSGVTAEKAPPPPPPPTLYVQLHGETTRRLEAEEKPLQIQNDYLFQLGFGELWRVQEEGMDSEIGCLIRFYAGKPHSTGSSERIQLSGMYNVRKGKMQLPVNRWTRRQVILCGTCLIVSSVKDSLTGKMHVLPLIGGKVEEVKKHQHCLAFSSSGPQSQTYYICFDTFTEYLRWLRQVSKVASQRISSVDLSCCSLEHLPANLFYSQDLTHLNLKQNFLRQNPSLPAARGLNELQRFTKLKSLNLSNNHLGDFPLAVCSIPTLAELNVSCNALRSVPAAVGVMHNLQTFLLDGNFLQSLPAELENMKQLSYLGLSFNEFTDIPEVLEKLTAVDKLCMSGNCVETLRLQALRKMPHIKHVDLRLNVIRKLIADEVDFLQHVTQLDLRDNKLGDLDAMIFNNIEVLHCERNQLVTLDICGYFLKALYASSNELVQLDVYPVPNYLSYMDVSRNRLENVPEWVCESRKLEVLDIGHNQICELPARLFCNSSLRKLLAGHNQLARLPERLERTSVEVLDVQHNQLLELPPNLLMKADSLRFLNASANKLESLPPATLSEETNSILQELYLTNNSLTDKCVPLLTGHPHLKILHMAYNRLQSFPASKMAKLEELEEIDLSGNKLKAIPTTIMNCRRMHTVIAHSNCIEVFPEVMQLPEIKCVDLSCNELSEVTLPENLPPKLQELDLTGNPRLVLDHKTLELLNNIRCFKIDQPSTGDASGAPAVWSHGYTEASGVKNKLCVAALSVNNFCDNREALYGVFDGDRNVEVPYLLQCTMSDILAEELQKTKNEEEYMVNTFIVMQRKLGTAGQKLGGAAVLCHIKHDPVDPGGSFTLTSANVGKCQTVLCRNGKPLPLSRSYIMSCEEELKRIKQHKAIITEDGKVNGVTESTRILGYTFLHPSVVPRPHVQSVLLTPQDEFFILGSKGLWDSLSVEEAVEAVRNVPDALAAAKKLCTLAQSYGCHDSISAVVVQLSVTEDSFCCCELSAGGAVPPPSPGIFPPSVNMVIKDRPSDGLGVPSSSSGMASEISSELSTSEMSSEVGSTASDEPPPGALSENSPAYPSEQRCMLHPICLSNSFQRQLSSATFSSAFSDNGLDSDDEEPIEGVFTNGSRVEVEVDIHCSRAKEKEKQQHLLQVPAEASDEGIVISANEDEPGLPRKADFSAVGTIGRRRANGSVAPQERSHNVIEVATDAPLRKPGGYFAAPAQPDPDDQFIIPPELEEEVKEIMKHHQEQQQQQQPPPPPQLQPQLPRHYQLDQLPDYYDTPL
|
3.1.3.16
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Binds 2 manganese ions per subunit (By similarity). Mn(2+) is inhibitory below pH 8 and activating above pH 8 (PubMed:24892992). {ECO:0000250, ECO:0000269|PubMed:24892992};
|
apoptotic process [GO:0006915]; entrainment of circadian clock [GO:0009649]; negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051898]; regulation of apoptotic process [GO:0042981]; regulation of JNK cascade [GO:0046328]; regulation of MAPK cascade [GO:0043408]; regulation of p38MAPK cascade [GO:1900744]; regulation of T cell anergy [GO:0002667]; signal transduction [GO:0007165]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
metal ion binding [GO:0046872]; myosin phosphatase activity [GO:0017018]; protein serine/threonine phosphatase activity [GO:0004722]
|
PF13516;PF13855;PF00169;PF00481;
|
2.30.29.30;3.60.40.10;3.80.10.10;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein. Nucleus. Note=In colorectal cancer tissue, expression is concentrated at the lateral membrane of epithelial cells.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000269|PubMed:21804599}.
|
CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; Evidence={ECO:0000269|PubMed:15808505, ECO:0000269|PubMed:24892992}; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; Evidence={ECO:0000269|PubMed:15808505, ECO:0000269|PubMed:24892992};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.5 mM for p-nitrophenyl phosphate {ECO:0000269|PubMed:24892992};
| null | null | null |
FUNCTION: Protein phosphatase involved in regulation of Akt and PKC signaling. Mediates dephosphorylation in the C-terminal domain hydrophobic motif of members of the AGC Ser/Thr protein kinase family; specifically acts on 'Ser-473' of AKT2 and AKT3, 'Ser-660' of PRKCB and 'Ser-657' of PRKCA (PubMed:15808505, PubMed:17386267, PubMed:18162466). Isoform 2 seems to have a major role in regulating Akt signaling in hippocampal neurons (By similarity). Akt regulates the balance between cell survival and apoptosis through a cascade that primarily alters the function of transcription factors that regulate pro- and antiapoptotic genes. Dephosphorylation of 'Ser-473' of Akt triggers apoptosis and suppression of tumor growth. Dephosphorylation of PRKCA and PRKCB leads to their destabilization and degradation (PubMed:18162466). Dephosphorylates STK4 on 'Thr-387' leading to STK4 activation and apoptosis (PubMed:20513427). Dephosphorylates RPS6KB1 and is involved in regulation of cap-dependent translation (PubMed:21986499). Inhibits cancer cell proliferation and may act as a tumor suppressor (PubMed:19079341). Dephosphorylates RAF1 inhibiting its kinase activity (PubMed:24530606). May act as a negative regulator of K-Ras signaling in membrane rafts (By similarity). Involved in the hippocampus-dependent long-term memory formation (By similarity). Involved in circadian control by regulating the consolidation of circadian periodicity after resetting (By similarity). Involved in development and function of regulatory T-cells (By similarity). {ECO:0000250|UniProtKB:Q8CHE4, ECO:0000250|UniProtKB:Q9WTR8, ECO:0000269|PubMed:15808505, ECO:0000269|PubMed:17386267, ECO:0000269|PubMed:18162466, ECO:0000269|PubMed:19079341, ECO:0000269|PubMed:21986499, ECO:0000269|PubMed:24530606}.
|
Homo sapiens (Human)
|
O60353
|
FZD6_HUMAN
|
MEMFTFLLTCIFLPLLRGHSLFTCEPITVPRCMKMAYNMTFFPNLMGHYDQSIAAVEMEHFLPLANLECSPNIETFLCKAFVPTCIEQIHVVPPCRKLCEKVYSDCKKLIDTFGIRWPEELECDRLQYCDETVPVTFDPHTEFLGPQKKTEQVQRDIGFWCPRHLKTSGGQGYKFLGIDQCAPPCPNMYFKSDELEFAKSFIGTVSIFCLCATLFTFLTFLIDVRRFRYPERPIIYYSVCYSIVSLMYFIGFLLGDSTACNKADEKLELGDTVVLGSQNKACTVLFMLLYFFTMAGTVWWVILTITWFLAAGRKWSCEAIEQKAVWFHAVAWGTPGFLTVMLLAMNKVEGDNISGVCFVGLYDLDASRYFVLLPLCLCVFVGLSLLLAGIISLNHVRQVIQHDGRNQEKLKKFMIRIGVFSGLYLVPLVTLLGCYVYEQVNRITWEITWVSDHCRQYHIPCPYQAKAKARPELALFMIKYLMTLIVGISAVFWVGSKKTCTEWAGFFKRNRKRDPISESRRVLQESCEFFLKHNSKVKHKKKHYKPSSHKLKVISKSMGTSTGATANHGTSAVAITSHDYLGQETLTEIQTSPETSMREVKADGASTPRLREQDCGEPASPAASISRLSGEQVDGKGQAGSVSESARSEGRISPKSDITDTGLAQSNNLQVPSSSEPSSLKGSTSLLVHPVSGVRKEQGGGCHSDT
| null | null |
canonical Wnt signaling pathway [GO:0060070]; cell proliferation in midbrain [GO:0033278]; embryonic nail plate morphogenesis [GO:0035880]; establishment of body hair planar orientation [GO:0048105]; hair follicle development [GO:0001942]; inner ear morphogenesis [GO:0042472]; midbrain morphogenesis [GO:1904693]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of DNA-binding transcription factor activity [GO:0043433]; neural tube closure [GO:0001843]; non-canonical Wnt signaling pathway [GO:0035567]; platelet activation [GO:0030168]; Wnt signaling pathway, planar cell polarity pathway [GO:0060071]
|
apical plasma membrane [GO:0016324]; apicolateral plasma membrane [GO:0016327]; cell surface [GO:0009986]; cytoplasmic vesicle membrane [GO:0030659]; endoplasmic reticulum membrane [GO:0005789]; plasma membrane [GO:0005886]
|
G protein-coupled receptor activity [GO:0004930]; ubiquitin protein ligase binding [GO:0031625]; Wnt receptor activity [GO:0042813]; Wnt-protein binding [GO:0017147]
|
PF01534;PF01392;
|
1.10.2000.10;1.20.1070.10;
|
G-protein coupled receptor Fz/Smo family
|
PTM: Ubiquitinated by ZNRF3, leading to its degradation by the proteasome. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q61089}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q61089}; Multi-pass membrane protein {ECO:0000255}. Cell surface {ECO:0000250|UniProtKB:Q61089}. Apical cell membrane; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q61089}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q61089}; Multi-pass membrane protein {ECO:0000255}. Note=Colocalizes with FZD3 at the apical face of cells (By similarity). Localizes to the endoplasmic reticulum membrane in the presence of LMBR1L (By similarity). {ECO:0000250|UniProtKB:Q61089}.
| null | null | null | null | null |
FUNCTION: Receptor for Wnt proteins. Most of frizzled receptors are coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. May be involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues. Together with FZD3, is involved in the neural tube closure and plays a role in the regulation of the establishment of planar cell polarity (PCP), particularly in the orientation of asymmetric bundles of stereocilia on the apical faces of a subset of auditory and vestibular sensory cells located in the inner ear (By similarity). {ECO:0000250|UniProtKB:Q61089}.
|
Homo sapiens (Human)
|
O60356
|
NUPR1_HUMAN
|
MATFPPATSAPQQPPGPEDEDSSLDESDLYSLAHSYLGGGGRKGRTKREAAANTNRPSPGGHERKLVTKLQNSERKKRGARR
| null | null |
acute inflammatory response [GO:0002526]; fibroblast apoptotic process [GO:0044346]; fibroblast proliferation [GO:0048144]; intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator [GO:0042771]; male gonad development [GO:0008584]; negative regulation of apoptotic process [GO:0043066]; negative regulation of autophagosome assembly [GO:1902902]; negative regulation of autophagy [GO:0010507]; negative regulation of cardiac muscle cell apoptotic process [GO:0010667]; negative regulation of cell cycle [GO:0045786]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of DNA-binding transcription factor activity [GO:0043433]; negative regulation of epithelial cell apoptotic process [GO:1904036]; negative regulation of epithelial cell proliferation [GO:0050680]; negative regulation of fibroblast proliferation [GO:0048147]; negative regulation of glycolytic process [GO:0045820]; negative regulation of programmed necrotic cell death [GO:0062099]; negative regulation of type B pancreatic cell proliferation [GO:1904691]; positive regulation of cell cycle [GO:0045787]; positive regulation of fibroblast apoptotic process [GO:2000271]; positive regulation of intrinsic apoptotic signaling pathway [GO:2001244]; positive regulation of neuroinflammatory response [GO:0150078]; positive regulation of neuron apoptotic process [GO:0043525]; positive regulation of oxidative phosphorylation [GO:1903862]; positive regulation of proteasomal protein catabolic process [GO:1901800]; positive regulation of protein modification process [GO:0031401]; protein-containing complex assembly [GO:0065003]; regulation of autophagy [GO:0010506]; regulation of female gonad development [GO:2000194]; regulation of response to endoplasmic reticulum stress [GO:1905897]; response to toxic substance [GO:0009636]; skeletal muscle cell differentiation [GO:0035914]
|
cytoplasm [GO:0005737]; intercellular bridge [GO:0045171]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; protein-DNA complex [GO:0032993]
|
acetyltransferase activator activity [GO:0010698]; chromatin binding [GO:0003682]; DNA binding [GO:0003677]; transcription coactivator activity [GO:0003713]
|
PF10195;
| null |
NUPR family
|
PTM: Phosphorylated in vitro by PKA and CK. Phosphorylation promotes DNA-binding activity. {ECO:0000269|PubMed:11056169}.; PTM: Acetylated by EP300 in vitro. {ECO:0000269|PubMed:11940591}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10092851, ECO:0000269|PubMed:16300740}. Cytoplasm {ECO:0000269|PubMed:16300740}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:16300740}.
| null | null | null | null | null |
FUNCTION: Transcription regulator that converts stress signals into a program of gene expression that empowers cells with resistance to the stress induced by a change in their microenvironment. Thereby participates in regulation of many process namely cell-cycle, apoptosis, autophagy and DNA repair responses (PubMed:11056169, PubMed:11940591, PubMed:16300740, PubMed:16478804, PubMed:18690848, PubMed:19650074, PubMed:19723804, PubMed:20181828, PubMed:22565310, PubMed:22858377, PubMed:30451898). Controls cell cycle progression and protects cells from genotoxic stress induced by doxorubicin through the complex formation with TP53 and EP300 that binds CDKN1A promoter leading to transcriptional induction of CDKN1A (PubMed:18690848). Protects pancreatic cancer cells from stress-induced cell death by binding the RELB promoter and activating its transcription, leading to IER3 transactivation (PubMed:22565310). Negatively regulates apoptosis through interaction with PTMA (PubMed:16478804). Inhibits autophagy-induced apoptosis in cardiac cells through FOXO3 interaction, inducing cytoplasmic translocation of FOXO3 thereby preventing the FOXO3 association with the pro-autophagic BNIP3 promoter (PubMed:20181828). Inhibits cell growth and facilitates programmed cell death by apoptosis after adriamycin-induced DNA damage through transactivation of TP53 (By similarity). Regulates methamphetamine-induced apoptosis and autophagy through DDIT3-mediated endoplasmic reticulum stress pathway (By similarity). Participates in DNA repair following gamma-irradiation by facilitating DNA access of the transcription machinery through interaction with MSL1 leading to inhibition of histone H4' Lys-16' acetylation (H4K16ac) (PubMed:19650074). Coactivator of PAX2 transcription factor activity, both by recruiting EP300 to increase PAX2 transcription factor activity and by binding PAXIP1 to suppress PAXIP1-induced inhibition on PAX2 (PubMed:11940591). Positively regulates cell cycle progression through interaction with COPS5 inducing cytoplasmic translocation of CDKN1B leading to the CDKN1B degradation (PubMed:16300740). Coordinates, through its interaction with EP300, the assiociation of MYOD1, EP300 and DDX5 to the MYOG promoter, leading to inhibition of cell-cycle progression and myogenic differentiation promotion (PubMed:19723804). Negatively regulates beta cell proliferation via inhibition of cell-cycle regulatory genes expression through the suppression of their promoter activities (By similarity). Also required for LHB expression and ovarian maturation (By similarity). Exacerbates CNS inflammation and demyelination upon cuprizone treatment (By similarity). {ECO:0000250|UniProtKB:O54842, ECO:0000250|UniProtKB:Q9WTK0, ECO:0000269|PubMed:11056169, ECO:0000269|PubMed:11940591, ECO:0000269|PubMed:16300740, ECO:0000269|PubMed:16478804, ECO:0000269|PubMed:18690848, ECO:0000269|PubMed:19650074, ECO:0000269|PubMed:19723804, ECO:0000269|PubMed:20181828, ECO:0000269|PubMed:22565310, ECO:0000269|PubMed:22858377, ECO:0000269|PubMed:30451898}.
|
Homo sapiens (Human)
|
O60359
|
CCG3_HUMAN
|
MRMCDRGIQMLITTVGAFAAFSLMTIAVGTDYWLYSRGVCRTKSTSDNETSRKNEEVMTHSGLWRTCCLEGAFRGVCKKIDHFPEDADYEQDTAEYLLRAVRASSVFPILSVTLLFFGGLCVAASEFHRSRHNVILSAGIFFVSAGLSNIIGIIVYISANAGDPGQRDSKKSYSYGWSFYFGAFSFIIAEIVGVVAVHIYIEKHQQLRAKSHSEFLKKSTFARLPPYRYRFRRRSSSRSTEPRSRDLSPISKGFHTIPSTDISMFTLSRDPSKITMGTLLNSDRDHAFLQFHNSTPKEFKESLHNNPANRRTTPV
| null | null |
calcium ion transport [GO:0006816]; neurotransmitter receptor internalization [GO:0099590]; neurotransmitter receptor localization to postsynaptic specialization membrane [GO:0099645]; neurotransmitter receptor transport, postsynaptic endosome to lysosome [GO:0098943]; positive regulation of synaptic transmission, glutamatergic [GO:0051968]; postsynaptic neurotransmitter receptor diffusion trapping [GO:0098970]; protein localization [GO:0008104]; protein targeting [GO:0006605]; regulation of AMPA receptor activity [GO:2000311]; transmission of nerve impulse [GO:0019226]
|
AMPA glutamate receptor complex [GO:0032281]; dendrite [GO:0030425]; endocytic vesicle membrane [GO:0030666]; excitatory synapse [GO:0060076]; glutamatergic synapse [GO:0098978]; plasma membrane [GO:0005886]; postsynaptic density membrane [GO:0098839]; Schaffer collateral - CA1 synapse [GO:0098685]; somatodendritic compartment [GO:0036477]; voltage-gated calcium channel complex [GO:0005891]
|
channel regulator activity [GO:0016247]; ionotropic glutamate receptor binding [GO:0035255]; PDZ domain binding [GO:0030165]; voltage-gated calcium channel activity [GO:0005245]
|
PF00822;
|
1.20.140.150;
|
PMP-22/EMP/MP20 family, CACNG subfamily
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Note=Displays a somatodendritic localization and is excluded from axons in neurons. {ECO:0000250|UniProtKB:Q9JJV5}.
| null | null | null | null | null |
FUNCTION: Regulates the trafficking to the somatodendritic compartment and gating properties of AMPA-selective glutamate receptors (AMPARs). Promotes their targeting to the cell membrane and synapses and modulates their gating properties by slowing their rates of activation, deactivation and desensitization. Does not show subunit-specific AMPA receptor regulation and regulates all AMPAR subunits. Thought to stabilize the calcium channel in an inactivated (closed) state. {ECO:0000250|UniProtKB:Q8VHX0}.
|
Homo sapiens (Human)
|
O60381
|
HBP1_HUMAN
|
MVWEVKTNQMPNAVQKLLLVMDKRASGMNDSLELLQCNENLPSSPGYNSCDEHMELDDLPELQAVQSDPTQSGMYQLSSDVSHQEYPRSSWNQNTSDIPETTYRENEVDWLTELANIATSPQSPLMQCSFYNRSSPVHIIATSKSLHSYARPPPVSSSSKSEPAFPHHHWKEETPVRHERANSESESGIFCMSSLSDDDDLGWCNSWPSTVWHCFLKGTRLCFHKGSNKEWQDVEDFARAEGCDNEEDLQMGIHKGYGSDGLKLLSHEESVSFGESVLKLTFDPGTVEDGLLTVECKLDHPFYVKNKGWSSFYPSLTVVQHGIPCCEVHIGDVCLPPGHPDAINFDDSGVFDTFKSYDFTPMDSSAVYVLSSMARQRRASLSCGGPGGQDFARSGFSKNCGSPGSSQLSSNSLYAKAVKNHSSGTVSATSPNKCKRPMNAFMLFAKKYRVEYTQMYPGKDNRAISVILGDRWKKMKNEERRMYTLEAKALAEEQKRLNPDCWKRKRTNSGSQQH
| null | null |
regulation of cell cycle [GO:0051726]; regulation of transcription by RNA polymerase II [GO:0006357]; Wnt signaling pathway [GO:0016055]
|
chromatin [GO:0000785]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA binding [GO:0003723]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF08517;PF00505;
|
1.10.30.10;
| null |
PTM: Ubiquitinated by the CTLH E3 ubiquitin-protein ligase complex, leading to subsequent proteasomal degradation. {ECO:0000269|PubMed:29911972}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267, ECO:0000269|PubMed:10562551}.
| null | null | null | null | null |
FUNCTION: Transcriptional repressor that binds to the promoter region of target genes. Plays a role in the regulation of the cell cycle and of the Wnt pathway. Binds preferentially to the sequence 5'-TTCATTCATTCA-3'. Binding to the histone H1.0 promoter is enhanced by interaction with RB1. Disrupts the interaction between DNA and TCF4. {ECO:0000269|PubMed:10562551, ECO:0000269|PubMed:10958660, ECO:0000269|PubMed:11500377}.
|
Homo sapiens (Human)
|
O60383
|
GDF9_HUMAN
|
MARPNKFLLWFCCFAWLCFPISLGSQASGGEAQIAASAELESGAMPWSLLQHIDERDRAGLLPALFKVLSVGRGGSPRLQPDSRALHYMKKLYKTYATKEGIPKSNRSHLYNTVRLFTPCTRHKQAPGDQVTGILPSVELLFNLDRITTVEHLLKSVLLYNINNSVSFSSAVKCVCNLMIKEPKSSSRTLGRAPYSFTFNSQFEFGKKHKWIQIDVTSLLQPLVASNKRSIHMSINFTCMKDQLEHPSAQNGLFNMTLVSPSLILYLNDTSAQAYHSWYSLHYKRRPSQGPDQERSLSAYPVGEEAAEDGRSSHHRHRRGQETVSSELKKPLGPASFNLSEYFRQFLLPQNECELHDFRLSFSQLKWDNWIVAPHRYNPRYCKGDCPRAVGHRYGSPVHTMVQNIIYEKLDSSVPRPSCVPAKYSPLSVLTIEPDGSIAYKEYEDMIATKCTCR
| null | null |
female gamete generation [GO:0007292]; negative regulation of cell growth [GO:0030308]; oocyte growth [GO:0001555]; positive regulation of cell population proliferation [GO:0008284]; regulation of progesterone secretion [GO:2000870]; transforming growth factor beta receptor signaling pathway [GO:0007179]
|
cytoplasm [GO:0005737]; extracellular space [GO:0005615]
|
cytokine activity [GO:0005125]; growth factor activity [GO:0008083]
|
PF00019;
|
2.10.90.10;
|
TGF-beta family
|
PTM: Phosphorylated; phosphorylation is critical for GDF9 function. In vitro, can be phosphorylated by CK at Ser-325. {ECO:0000269|PubMed:18006624, ECO:0000269|PubMed:20067794}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Required for ovarian folliculogenesis. Promotes primordial follicle development. Stimulates granulosa cell proliferation. Promotes cell transition from G0/G1 to S and G2/M phases, through an increase of CCND1 and CCNE1 expression, and RB1 phosphorylation. It regulates STAR expression and cAMP-dependent progesterone release in granulosa and thecal cells. Attenuates the suppressive effects of activin A on STAR expression and progesterone production by increasing the expression of inhibin B. It suppresses FST and FSTL3 production in granulosa-lutein cells. {ECO:0000269|PubMed:12050262, ECO:0000269|PubMed:19366876, ECO:0000269|PubMed:20660033, ECO:0000269|PubMed:21632818, ECO:0000269|PubMed:21829661}.
|
Homo sapiens (Human)
|
O60391
|
NMD3B_HUMAN
|
MEFVRALWLGLALALGPGSAGGHPQPCGVLARLGGSVRLGALLPRAPLARARARAALARAALAPRLPHNLSLELVVAAPPARDPASLTRGLCQALVPPGVAALLAFPEARPELLQLHFLAAATETPVLSLLRREARAPLGAPNPFHLQLHWASPLETLLDVLVAVLQAHAWEDVGLALCRTQDPGGLVALWTSRAGRPPQLVLDLSRRDTGDAGLRARLAPMAAPVGGEAPVPAAVLLGCDIARARRVLEAVPPGPHWLLGTPLPPKALPTAGLPPGLLALGEVARPPLEAAIHDIVQLVARALGSAAQVQPKRALLPAPVNCGDLQPAGPESPGRFLARFLANTSFQGRTGPVWVTGSSQVHMSRHFKVWSLRRDPRGAPAWATVGSWRDGQLDLEPGGASARPPPPQGAQVWPKLRVVTLLEHPFVFARDPDEDGQCPAGQLCLDPGTNDSATLDALFAALANGSAPRALRKCCYGYCIDLLERLAEDTPFDFELYLVGDGKYGALRDGRWTGLVGDLLAGRAHMAVTSFSINSARSQVVDFTSPFFSTSLGIMVRARDTASPIGAFMWPLHWSTWLGVFAALHLTALFLTVYEWRSPYGLTPRGRNRSTVFSYSSALNLCYAILFRRTVSSKTPKCPTGRLLMNLWAIFCLLVLSSYTANLAAVMVGDKTFEELSGIHDPKLHHPAQGFRFGTVWESSAEAYIKKSFPDMHAHMRRHSAPTTPRGVAMLTSDPPKLNAFIMDKSLLDYEVSIDADCKLLTVGKPFAIEGYGIGLPQNSPLTSNLSEFISRYKSSGFIDLLHDKWYKMVPCGKRVFAVTETLQMSIYHFAGLFVLLCLGLGSALLSSLGEHAFFRLALPRIRKGSRLQYWLHTSQKIHRALNTEPPEGSKEETAEAEPSGPEVEQQQQQQDQPTAPEGWKRARRAVDKERRVRFLLEPAVVVAPEADAEAEAAPREGPVWLCSYGRPPAARPTGAPQPGELQELERRIEVARERLRQALVRRGQLLAQLGDSARHRPRRLLQARAAPAEAPPHSGRPGSQE
| null | null |
ionotropic glutamate receptor signaling pathway [GO:0035235]; modulation of chemical synaptic transmission [GO:0050804]; protein insertion into membrane [GO:0051205]; regulation of calcium ion transport [GO:0051924]; synaptic transmission, glutamatergic [GO:0035249]
|
neuronal cell body [GO:0043025]; NMDA selective glutamate receptor complex [GO:0017146]; plasma membrane [GO:0005886]; postsynaptic density membrane [GO:0098839]
|
calcium channel activity [GO:0005262]; glutamate receptor activity [GO:0008066]; glycine binding [GO:0016594]; ligand-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential [GO:0099507]; monoatomic cation channel activity [GO:0005261]; neurotransmitter receptor activity [GO:0030594]; NMDA glutamate receptor activity [GO:0004972]; transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential [GO:1904315]
|
PF00060;PF10613;PF00497;
|
3.40.50.2300;3.40.190.10;
|
Glutamate-gated ion channel (TC 1.A.10.1) family, NR3B/GRIN3B subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Postsynaptic cell membrane {ECO:0000250}. Note=Requires the presence of GRIN1 to be targeted at the plasma membrane. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: NMDA receptor subtype of glutamate-gated ion channels with reduced single-channel conductance, low calcium permeability and low voltage-dependent sensitivity to magnesium. Mediated by glycine.
|
Homo sapiens (Human)
|
O60393
|
NOBOX_HUMAN
|
MALLLTLTSPDLEGTWDTRDKDGFKAQEGPPLAVPEFPVCGLYRIYGVCGSFSSFFIIRCSLCALETLKSPQHDPLEIPEQSLKLIPLVSGKRELTRGQKAGEKPLAAGPGEEELLRGSAPHAQDTQSEELPPSCTISGEKKPPAVSGEATGADAGRLCPPPRSRAPHKDRTLARSRPQTQGEDCSLPVGEVKIGKRSYSPAPGKQKKPNAMGLAPTSSPGAPNSARATHNPVPCGSGRGPCHLANLLSTLAQSNQNRDHKQGPPEVTCQIRKKTRTLYRSDQLEELEKIFQEDHYPDSDKRREIAQTVGVTPQRIMVKGAGSLVAGWSGGGPTIETLELQSERSAVAWVWFQNRRAKWRKMEKLNGKESKDNPAAPGPASSQCSSAAEILPAVPMEPKPDPFPQESPLDTFPEPPMLLTSDQTLAPTQPSEGAQRVVTPPLFSPPPVRRADLPFPLGPVHTPQLMPLLMDVAGSDSSHKDGPCGSWGTSITLPPPCSYLEELEPQDYQQSNQPGPFQFSQAPQPPLFQSPQPKLPYLPTFPFSMPSSLTLPPPEDSLFMFPCGPSGGTSQGYCPGASSGQILMQPPAGNIGTASWSDPCLPELPFPGPFCPQALGHPPGGDGYFPDLFPTPCPQALGRQPSSALSWMPEGARPGTGPLLSKAKEEPPAASLDQPSALEEARGDDKNSHVP
| null | null |
oogenesis [GO:0048477]; regulation of transcription by RNA polymerase II [GO:0006357]
|
chromatin [GO:0000785]; nucleus [GO:0005634]
|
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]
|
PF00046;
|
1.10.10.60;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:27798098}.
| null | null | null | null | null |
FUNCTION: Transcription factor which may play a role in oogenesis. Binds preferentially to the DNA sequences 5'-TAATTG-3', 5'-TAGTTG-3' and 5'-TAATTA-3'. {ECO:0000269|PubMed:25514101, ECO:0000269|PubMed:27798098}.
|
Homo sapiens (Human)
|
O60423
|
AT8B3_HUMAN
|
MGTGPAQTPRSTRAGPEPSPAPPGPGDTGDSDVTQEGSGPAGIRGGETVIRAGMGDSPGRGAPERRHKAQPGRARKYEWRPEGPTSMGSLGQREDLQDEDRNSAFTWKVQANNRAYNGQFKEKVILCWQRKKYKTNVIRTAKYNFYSFLPLNLYEQFHRVSNLFFLIIIILQSIPDISTLPWFSLSTPMVCLLFIRATRDLVDDMGRHKSDRAINNRPCQILMGKSFKQKKWQDLCVGDVVCLRKDNIVPADMLLLASTEPSSLCYVETVDIDGETNLKFRQALMVTHKELATIKKMASFQGTVTCEAPNSRMHHFVGCLEWNDKKYSLDIGNLLLRGCRIRNTDTCYGLVIYAGFDTKIMKNCGKIHLKRTKLDLLMNKLVVVIFISVVLVCLVLAFGFGFSVKEFKDHHYYLSGVHGSSVAAESFFVFWSFLILLSVTIPMSMFILSEFIYLGNSVFIDWDVQMYYKPQDVPAKARSTSLNDHLGQVEYIFSDKTGTLTQNILTFNKCCISGRVYGPDSEATTRPKENPYLWNKFADGKLLFHNAALLHLVRTNGDEAVREFWRLLAICHTVMVRESPRERPDQLLYQAASPDEGALVTAARNFGYVFLSRTQDTVTIMELGEERVYQVLAIMDFNSTRKRMSVLVRKPEGAICLYTKGADTVIFERLHRRGAMEFATEEALAAFAQETLRTLCLAYREVAEDIYEDWQQRHQEASLLLQNRAQALQQLLGATAIEDRLQDGVPETIKCLKKSNIKIWVLTGDKQETAVNIGFACELLSENMLILEEKEISRILETYWENSNNLLTRESLSQVKLALVINGDFLDKLLVSLRKEPRALAQNVNMDEAWQELGQSRRDFLYARRLSLLCRRFGLPLAAPPAQDSRARRSSEVLQERAFVDLASKCQAVICCRVTPKQKALIVALVKKYHQVVTLAIGDGANDINMIKTADVGVGLAGQEGMQAVQNSDFVLGQFCFLQRLLLVHGRWSYVRICKFLRYFFYKSMASMMVQVWFACYNGFTGQPLYEGWFLALFNLLYSTLPVLYIGLFEQDVSAEQSLEKPELYVVGQKDELFNYWVFVQAIAHGVTTSLVNFFMTLWISRDTAGPASFSDHQSFAVVVALSCLLSITMEVILIIKYWTALCVATILLSLGFYAIMTTTTQSFWLFRVSPTTFPFLYADLSVMSSPSILLVVLLSVSINTFPVLALRVIFPALKELRAKEEKVEEGPSEEIFTMEPLPHVHRESRARRSSYAFSHREGYANLITQGTILRRGPGVSSDIASESLDPSDEEAASSPKESQ
|
7.6.2.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9Y2Q0};
|
binding of sperm to zona pellucida [GO:0007339]; establishment of localization in cell [GO:0051649]; Golgi organization [GO:0007030]; phospholipid translocation [GO:0045332]
|
acrosomal membrane [GO:0002080]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; phospholipid-translocating ATPase complex [GO:1990531]; plasma membrane [GO:0005886]; trans-Golgi network [GO:0005802]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled intramembrane lipid transporter activity [GO:0140326]; magnesium ion binding [GO:0000287]; phosphatidylserine floppase activity [GO:0090556]
|
PF13246;PF00122;PF00702;PF16212;PF16209;
|
3.40.1110.10;2.70.150.10;3.40.50.1000;
|
Cation transport ATPase (P-type) (TC 3.A.3) family, Type IV subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome membrane {ECO:0000250|UniProtKB:Q6UQ17}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:20947505}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2.; EC=7.6.2.1; Evidence={ECO:0000250|UniProtKB:Q6UQ17}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:38567, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57262, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q6UQ17}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38568; Evidence={ECO:0000250|UniProtKB:Q6UQ17};
| null | null | null | null |
FUNCTION: P4-ATPase flippase which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules. May be responsible for the maintenance of asymmetric distribution of phosphatidylserine (PS) in spermatozoa membranes. Involved in acrosome reactions and binding of spermatozoa to zona pellucida. {ECO:0000250|UniProtKB:Q6UQ17}.
|
Homo sapiens (Human)
|
O60427
|
FADS1_HUMAN
|
MAPDPVAAETAAQGPTPRYFTWDEVAQRSGCEERWLVIDRKVYNISEFTRRHPGGSRVISHYAGQDATDPFVAFHINKGLVKKYMNSLLIGELSPEQPSFEPTKNKELTDEFRELRATVERMGLMKANHVFFLLYLLHILLLDGAAWLTLWVFGTSFLPFLLCAVLLSAVQAQAGWLQHDFGHLSVFSTSKWNHLLHHFVIGHLKGAPASWWNHMHFQHHAKPNCFRKDPDINMHPFFFALGKILSVELGKQKKKYMPYNHQHKYFFLIGPPALLPLYFQWYIFYFVIQRKKWVDLAWMITFYVRFFLTYVPLLGLKAFLGLFFIVRFLESNWFVWVTQMNHIPMHIDHDRNMDWVSTQLQATCNVHKSAFNDWFSGHLNFQIEHHLFPTMPRHNYHKVAPLVQSLCAKHGIEYQSKPLLSAFADIIHSLKESGQLWLDAYLHQ
|
1.14.19.44
| null |
alpha-linolenic acid metabolic process [GO:0036109]; cell-cell signaling [GO:0007267]; cellular response to starvation [GO:0009267]; icosanoid biosynthetic process [GO:0046456]; linoleic acid metabolic process [GO:0043651]; lipid metabolic process [GO:0006629]; long-chain fatty acid biosynthetic process [GO:0042759]; phospholipid biosynthetic process [GO:0008654]; regulation of cell differentiation [GO:0045595]; regulation of DNA-templated transcription [GO:0006355]; unsaturated fatty acid biosynthetic process [GO:0006636]
|
endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; mitochondrion [GO:0005739]
|
acyl-CoA delta5-desaturase activity [GO:0062076]; C-5 sterol desaturase activity [GO:0000248]; linoleoyl-CoA desaturase activity [GO:0016213]; omega-6 fatty acid desaturase activity [GO:0045485]; oxidoreductase activity [GO:0016491]; oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water [GO:0016717]
|
PF00173;PF00487;
|
3.10.120.10;
|
Fatty acid desaturase type 1 family
| null |
SUBCELLULAR LOCATION: [Isoform 1]: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:A4UVI1}; Multi-pass membrane protein {ECO:0000250|UniProtKB:A4UVI1}. Mitochondrion {ECO:0000269|PubMed:22619218}.; SUBCELLULAR LOCATION: [Isoform 2]: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:A4UVI1}; Multi-pass membrane protein {ECO:0000250|UniProtKB:A4UVI1}.
|
CATALYTIC ACTIVITY: Reaction=(8Z,11Z,14Z)-eicosatrienoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:46424, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:57368, ChEBI:CHEBI:74264; EC=1.14.19.44; Evidence={ECO:0000269|PubMed:10601301, ECO:0000269|PubMed:10769175}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46425; Evidence={ECO:0000305|PubMed:10601301}; CATALYTIC ACTIVITY: Reaction=(8Z,11Z,14Z,17Z)-eicosatetraenoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:46420, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:73862, ChEBI:CHEBI:74265; EC=1.14.19.44; Evidence={ECO:0000269|PubMed:10769175}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46421; Evidence={ECO:0000305|PubMed:10769175}; CATALYTIC ACTIVITY: Reaction=(11E)-octadecenoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = (5Z,11E)-octadecadienoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:46060, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:74296, ChEBI:CHEBI:85651; Evidence={ECO:0000250|UniProtKB:Q920R3}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46061; Evidence={ECO:0000250|UniProtKB:Q920R3};
| null |
PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
| null | null |
FUNCTION: [Isoform 1]: Acts as a front-end fatty acyl-coenzyme A (CoA) desaturase that introduces a cis double bond at carbon 5 located between a preexisting double bond and the carboxyl end of the fatty acyl chain. Involved in biosynthesis of highly unsaturated fatty acids (HUFA) from the essential polyunsaturated fatty acids (PUFA) linoleic acid (LA) (18:2n-6) and alpha-linolenic acid (ALA) (18:3n-3) precursors. Specifically, desaturates dihomo-gamma-linoleoate (DGLA) (20:3n-6) and eicosatetraenoate (ETA) (20:4n-3) to generate arachidonate (AA) (20:4n-6) and eicosapentaenoate (EPA) (20:5n-3), respectively (PubMed:10601301, PubMed:10769175). As a rate limiting enzyme for DGLA (20:3n-6) and AA (20:4n-6)-derived eicosanoid biosynthesis, controls the metabolism of inflammatory lipids like prostaglandin E2, critical for efficient acute inflammatory response and maintenance of epithelium homeostasis. Contributes to membrane phospholipid biosynthesis by providing AA (20:4n-6) as a major acyl chain esterified into phospholipids. In particular, regulates phosphatidylinositol-4,5-bisphosphate levels, modulating inflammatory cytokine production in T-cells (By similarity). Also desaturates (11E)-octadecenoate (trans-vaccenoate)(18:1n-9), a metabolite in the biohydrogenation pathway of LA (18:2n-6) (By similarity). {ECO:0000250|UniProtKB:Q920L1, ECO:0000250|UniProtKB:Q920R3, ECO:0000269|PubMed:10601301, ECO:0000269|PubMed:10769175}.; FUNCTION: [Isoform 2]: Does not exhibit any catalytic activity toward 20:3n-6, but it may enhance FADS2 activity. {ECO:0000250|UniProtKB:A4UVI1}.
|
Homo sapiens (Human)
|
O60437
|
PEPL_HUMAN
|
MNSLFRKRNKGKYSPTVQTRSISNKELSELIEQLQKNADQVEKNIVDTEAKMQSDLARLQEGRQPEHRDVTLQKVLDSEKLLYVLEADAAIAKHMKHPQGDMIAEDIRQLKERVTNLRGKHKQIYRLAVKEVDPQVNWAALVEEKLDKLNNQSFGTDLPLVDHQVEEHNIFHNEVKAIGPHLAKDGDKEQNSELRAKYQKLLAASQARQQHLSSLQDYMQRCTNELYWLDQQAKGRMQYDWSDRNLDYPSRRRQYENFINRNLEAKEERINKLHSEGDQLLAAEHPGRNSIEAHMEAVHADWKEYLNLLICEESHLKYMEDYHQFHEDVKDAQELLRKVDSDLNQKYGPDFKDRYQIELLLRELDDQEKVLDKYEDVVQGLQKRGQQVVPLKYRRETPLKPIPVEALCDFEGEQGLISRGYSYTLQKNNGESWELMDSAGNKLIAPAVCFVIPPTDPEALALADSLGSQYRSVRQKAAGSKRTLQQRYEVLKTENPGDASDLQGRQLLAGLDKVASDLDRQEKAITGILRPPLEQGRAVQDSAERAKDLKNITNELLRIEPEKTRSTAEGEAFIQALPGSGTTPLLRTRVEDTNRKYEHLLQLLDLAQEKVDVANRLEKSLQQSWELLATHENHLNQDDTVPESSRVLDSKGQELAAMACELQAQKSLLGEVEQNLQAAKQCSSTLASRFQEHCPDLERQEAEVHKLGQRFNNLRQQVERRAQSLQSAKAAYEHFHRGHDHVLQFLVSIPSYEPQETDSLSQMETKLKNQKNLLDEIASREQEVQKICANSQQYQQAVKDYELEAEKLRSLLDLENGRRSHVSKRARLQSPATKVKEEEAALAAKFTEVYAINRQRLQNLEFALNLLRQQPEVEVTHETLQRNRPDSGVEEAWKIRKELDEETERRRQLENEVKSTQEEIWTLRNQGPQESVVRKEVLKKVPDPVLEESFQQLQRTLAEEQHKNQLLQEELEALQLQLRALEQETRDGGQEYVVKEVLRIEPDRAQADEVLQLREELEALRRQKGAREAEVLLLQQRVAALAEEKSRAQEKVTEKEVVKLQNDPQLEAEYQQLQEDHQRQDQLREKQEEELSFLQDKLKRLEKERAMAEGKITVKEVLKVEKDAATEREVSDLTRQYEDEAAKARASQREKTELLRKIWALEEENAKVVVQEKVREIVRPDPKAESEVANLRLELVEQERKYRGAEEQLRSYQSELEALRRRGPQVEVKEVTKEVIKYKTDPEMEKELQRLREEIVDKTRLIERCDLEIYQLKKEIQALKDTKPQVQTKEVVQEILQFQEDPQTKEEVASLRAKLSEEQKKQVDLERERASQEEQIARKEEELSRVKERVVQQEVVRYEEEPGLRAEASAFAESIDVELRQIDKLRAELRRLQRRRTELERQLEELERERQARREAEREVQRLQQRLAALEQEEAEAREKVTHTQKVVLQQDPQQAREHALLRLQLEEEQHRRQLLEGELETLRRKLAALEKAEVKEKVVLSESVQVEKGDTEQEIQRLKSSLEEESRSKRELDVEVSRLEARLSELEFHNSKSSKELDFLREENHKLQLERQNLQLETRRLQSEINMAATETRDLRNMTVADSGTNHDSRLWSLERELDDLKRLSKDKDLEIDELQKRLGSVAVKREQRENHLRRSIVVIHPDTGRELSPEEAHRAGLIDWNMFVKLRSQECDWEEISVKGPNGESSVIHDRKSGKKFSIEEALQSGRLTPAQYDRYVNKDMSIQELAVLVSGQK
| null | null |
intermediate filament cytoskeleton organization [GO:0045104]; keratinization [GO:0031424]; response to mechanical stimulus [GO:0009612]; wound healing [GO:0042060]
|
cornified envelope [GO:0001533]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; desmosome [GO:0030057]; extracellular exosome [GO:0070062]; intermediate filament [GO:0005882]; membrane [GO:0016020]; plasma membrane [GO:0005886]
|
cadherin binding [GO:0045296]; structural constituent of cytoskeleton [GO:0005200]; structural molecule activity [GO:0005198]
|
PF17902;
|
1.20.58.60;3.30.160.780;2.30.30.40;
|
Plakin or cytolinker family
| null |
SUBCELLULAR LOCATION: Cell junction, desmosome {ECO:0000269|PubMed:9412476}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9412476}. Cell membrane {ECO:0000250|UniProtKB:Q9R269}. Cytoplasm {ECO:0000250|UniProtKB:Q9R269}.
| null | null | null | null | null |
FUNCTION: Component of the cornified envelope of keratinocytes. May link the cornified envelope to desmosomes and intermediate filaments. May act as a localization signal in PKB/AKT-mediated signaling. {ECO:0000269|PubMed:9412476}.
|
Homo sapiens (Human)
|
O60443
|
GSDME_HUMAN
|
MFAKATRNFLREVDADGDLIAVSNLNDSDKLQLLSLVTKKKRFWCWQRPKYQFLSLTLGDVLIEDQFPSPVVVESDFVKYEGKFANHVSGTLETALGKVKLNLGGSSRVESQSSFGTLRKQEVDLQQLIRDSAERTINLRNPVLQQVLEGRNEVLCVLTQKITTMQKCVISEHMQVEEKCGGIVGIQTKTVQVSATEDGNVTKDSNVVLEIPAATTIAYGVIELYVKLDGQFEFCLLRGKQGGFENKKRIDSVYLDPLVFREFAFIDMPDAAHGISSQDGPLSVLKQATLLLERNFHPFAELPEPQQTALSDIFQAVLFDDELLMVLEPVCDDLVSGLSPTVAVLGELKPRQQQDLVAFLQLVGCSLQGGCPGPEDAGSKQLFMTAYFLVSALAEMPDSAAALLGTCCKLQIIPTLCHLLRALSDDGVSDLEDPTLTPLKDTERFGIVQRLFASADISLERLKSSVKAVILKDSKVFPLLLCITLNGLCALGREHS
| null | null |
cellular response to tumor necrosis factor [GO:0071356]; cellular response to virus [GO:0098586]; inner ear auditory receptor cell differentiation [GO:0042491]; negative regulation of cell population proliferation [GO:0008285]; positive regulation of immune response to tumor cell [GO:0002839]; positive regulation of intrinsic apoptotic signaling pathway [GO:2001244]; positive regulation of MAPK cascade [GO:0043410]; programmed cell death [GO:0012501]; pyroptosis [GO:0070269]; sensory perception of sound [GO:0007605]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; plasma membrane [GO:0005886]
|
cardiolipin binding [GO:1901612]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; wide pore channel activity [GO:0022829]
|
PF04598;PF17708;
| null |
Gasdermin family
|
PTM: Cleavage at Asp-270 by CASP3 (mature and uncleaved precursor forms) or granzyme B (GZMB) relieves autoinhibition and is sufficient to initiate pyroptosis. {ECO:0000269|PubMed:28045099, ECO:0000269|PubMed:28459430, ECO:0000269|PubMed:31953257, ECO:0000269|PubMed:32188940}.; PTM: [Gasdermin-E]: Succination by the Krebs cycle intermediate fumarate, which leads to S-(2-succinyl)cysteine residues, inhibits processing by caspases, and ability to initiate pyroptosis (PubMed:32820063). Succination modification is catalyzed by a non-enzymatic reaction caused by an accumulation of fumarate (PubMed:32820063). {ECO:0000269|PubMed:32820063}.; PTM: [Gasdermin-E]: Ubiquitinated at Lys-120 and Lys-189 via 'Lys-48'-linked polyubiquitin chains, leading to proteasomal degradation. Deubiquitinated by USP48, leading to increased stability. {ECO:0000269|PubMed:36607699}.
|
SUBCELLULAR LOCATION: [Gasdermin-E, N-terminal]: Cell membrane {ECO:0000269|PubMed:28045099, ECO:0000269|PubMed:28459430}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5Y4Y6}.; SUBCELLULAR LOCATION: [Gasdermin-E]: Cytoplasm, cytosol {ECO:0000269|PubMed:28045099}.
| null | null | null | null | null |
FUNCTION: [Gasdermin-E]: Precursor of a pore-forming protein that converts non-inflammatory apoptosis to pyroptosis (PubMed:27281216, PubMed:28459430, PubMed:33852854, PubMed:35594856, PubMed:36607699). This form constitutes the precursor of the pore-forming protein: upon cleavage, the released N-terminal moiety (Gasdermin-E, N-terminal) binds to membranes and forms pores, triggering pyroptosis (PubMed:28459430). {ECO:0000269|PubMed:27281216, ECO:0000269|PubMed:28459430, ECO:0000269|PubMed:33852854, ECO:0000269|PubMed:35594856, ECO:0000269|PubMed:36607699}.; FUNCTION: [Gasdermin-E, N-terminal]: Pore-forming protein produced by cleavage by CASP3 or granzyme B (GZMB), which converts non-inflammatory apoptosis to pyroptosis or promotes granzyme-mediated pyroptosis, respectively (PubMed:27281216, PubMed:28459430, PubMed:32188940, PubMed:33852854, PubMed:35594856). After cleavage, moves to the plasma membrane, homooligomerizes within the membrane and forms pores of 10-15 nanometers (nm) of inner diameter, allowing the release of mature interleukins (IL1B and IL16) and triggering pyroptosis (PubMed:28459430, PubMed:32188940, PubMed:33852854, PubMed:35594856). Binds to inner leaflet lipids, bisphosphorylated phosphatidylinositols, such as phosphatidylinositol (4,5)-bisphosphate (PubMed:28459430). Cleavage by CASP3 switches CASP3-mediated apoptosis induced by TNF or danger signals, such as chemotherapy drugs, to pyroptosis (PubMed:27281216, PubMed:28459430, PubMed:32188940). Mediates secondary necrosis downstream of the mitochondrial apoptotic pathway and CASP3 activation as well as in response to viral agents (PubMed:28045099). Exhibits bactericidal activity (PubMed:27281216). Cleavage by GZMB promotes tumor suppressor activity by triggering robust anti-tumor immunity (PubMed:21522185, PubMed:32188940). Suppresses tumors by mediating granzyme-mediated pyroptosis in target cells of natural killer (NK) cells: cleavage by granzyme B (GZMB), delivered to target cells from NK-cells, triggers pyroptosis of tumor cells and tumor suppression (PubMed:31953257, PubMed:32188940). May play a role in the p53/TP53-regulated cellular response to DNA damage (PubMed:16897187). {ECO:0000269|PubMed:16897187, ECO:0000269|PubMed:21522185, ECO:0000269|PubMed:27281216, ECO:0000269|PubMed:28045099, ECO:0000269|PubMed:28459430, ECO:0000269|PubMed:31953257, ECO:0000269|PubMed:32188940, ECO:0000269|PubMed:33852854, ECO:0000269|PubMed:35594856}.; FUNCTION: [Gasdermin-E, N-terminal]: (Microbial infection) Pore-forming protein, which promotes maternal placental pyroptosis in response to Zika virus infection, contributing to adverse fetal outcomes. {ECO:0000269|PubMed:35972780}.
|
Homo sapiens (Human)
|
O60447
|
EVI5_HUMAN
|
MVTNKMTAAFRNPSGKQVATDKVAEKLSSTLSWVKNTVSHTVSQMASQVASPSTSLHTTSSSTTLSTPALSPSSPSQLSPDDLELLAKLEEQNRLLETDSKSLRSVNGSRRNSGSSLVSSSSASSNLSHLEEDSWILWGRIVNEWEDVRKKKEKQVKELVHKGIPHHFRAIVWQLLCSAQSMPIKDQYSELLKMTSPCEKLIRRDIARTYPEHNFFKEKDSLGQEVLFNVMKAYSLVDREVGYCQGSAFIVGLLLMQMPEEEAFCVFVKLMQDYRLRELFKPSMAELGLCMYQFECMIQEHLPELFVHFQSQSFHTSMYASSWFLTIFLTTFPLPIATRIFDIFMSEGLEIVFRVGLALLQMNQAELMQLDMEGMLQHFQKVIPHQFDGVPDKLIQAAYQVKYNSKKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETLEKHKCSSNYNEDFVLQLEKELVQARLSEAESQCALKEMQDKVLDIEKRNNSLPDENNIARLQEELIAVKLREAEAIMGLKELRQQVKDLEEHWQRHLARTTGRWKDPPKKNAMNELQDELMTIRLREAETQAEIREIKQRMMEMETQNQINSNHLRRAEQEVISLQEKVQYLSAQNKGLLTQLSEAKRKQAEIECKNKEEVMAVRLREADSIAAVAELRQHIAELEIQKEEGKLQGQLNKSDSNQYIGELKDQIAELNHELRCLKGQRGFSGQPPFDGIHIVNHLIGDDESFHSSDEDFIDNSLQETGVGFPLHGKSGSMSLDPAVADGSESETEDSVLETRESNQVVQKERPPRRRESYSTTV
| null | null |
cell cycle [GO:0007049]; cell division [GO:0051301]; positive regulation of GTPase activity [GO:0043547]; retrograde transport, endosome to Golgi [GO:0042147]
|
centrosome [GO:0005813]; cytosol [GO:0005829]; nucleus [GO:0005634]; spindle [GO:0005819]
|
GTPase activator activity [GO:0005096]; small GTPase binding [GO:0031267]
|
PF00566;
|
1.10.8.270;1.10.10.750;1.10.472.80;
| null |
PTM: Probably phosphorylated by PLK1; may be required for degradation during mitosis. {ECO:0000269|PubMed:16439210}.; PTM: Ubiquitinated. Degradation during prophase is ubiquitin-dependent. {ECO:0000269|PubMed:16439210}.
|
SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle. Note=Associates with the mitotic spindle through anaphase and remains within the midzone and midbody until completion of cytokinesis.
| null | null | null | null | null |
FUNCTION: Functions as a regulator of cell cycle progression by stabilizing the FBXO5 protein and promoting cyclin-A accumulation during interphase. May play a role in cytokinesis. {ECO:0000269|PubMed:16439210}.
|
Homo sapiens (Human)
|
O60449
|
LY75_HUMAN
|
MRTGWATPRRPAGLLMLLFWFFDLAEPSGRAANDPFTIVHGNTGKCIKPVYGWIVADDCDETEDKLWKWVSQHRLFHLHSQKCLGLDITKSVNELRMFSCDSSAMLWWKCEHHSLYGAARYRLALKDGHGTAISNASDVWKKGGSEESLCDQPYHEIYTRDGNSYGRPCEFPFLIDGTWHHDCILDEDHSGPWCATTLNYEYDRKWGICLKPENGCEDNWEKNEQFGSCYQFNTQTALSWKEAYVSCQNQGADLLSINSAAELTYLKEKEGIAKIFWIGLNQLYSARGWEWSDHKPLNFLNWDPDRPSAPTIGGSSCARMDAESGLWQSFSCEAQLPYVCRKPLNNTVELTDVWTYSDTRCDAGWLPNNGFCYLLVNESNSWDKAHAKCKAFSSDLISIHSLADVEVVVTKLHNEDIKEEVWIGLKNINIPTLFQWSDGTEVTLTYWDENEPNVPYNKTPNCVSYLGELGQWKVQSCEEKLKYVCKRKGEKLNDASSDKMCPPDEGWKRHGETCYKIYEDEVPFGTNCNLTITSRFEQEYLNDLMKKYDKSLRKYFWTGLRDVDSCGEYNWATVGGRRRAVTFSNWNFLEPASPGGCVAMSTGKSVGKWEVKDCRSFKALSICKKMSGPLGPEEASPKPDDPCPEGWQSFPASLSCYKVFHAERIVRKRNWEEAERFCQALGAHLSSFSHVDEIKEFLHFLTDQFSGQHWLWIGLNKRSPDLQGSWQWSDRTPVSTIIMPNEFQQDYDIRDCAAVKVFHRPWRRGWHFYDDREFIYLRPFACDTKLEWVCQIPKGRTPKTPDWYNPDRAGIHGPPLIIEGSEYWFVADLHLNYEEAVLYCASNHSFLATITSFVGLKAIKNKIANISGDGQKWWIRISEWPIDDHFTYSRYPWHRFPVTFGEECLYMSAKTWLIDLGKPTDCSTKLPFICEKYNVSSLEKYSPDSAAKVQCSEQWIPFQNKCFLKIKPVSLTFSQASDTCHSYGGTLPSVLSQIEQDFITSLLPDMEATLWIGLRWTAYEKINKWTDNRELTYSNFHPLLVSGRLRIPENFFEEESRYHCALILNLQKSPFTGTWNFTSCSERHFVSLCQKYSEVKSRQTLQNASETVKYLNNLYKIIPKTLTWHSAKRECLKSNMQLVSITDPYQQAFLSVQALLHNSSLWIGLFSQDDELNFGWSDGKRLHFSRWAETNGQLEDCVVLDTDGFWKTVDCNDNQPGAICYYSGNETEKEVKPVDSVKCPSPVLNTPWIPFQNCCYNFIITKNRHMATTQDEVHTKCQKLNPKSHILSIRDEKENNFVLEQLLYFNYMASWVMLGITYRNKSLMWFDKTPLSYTHWRAGRPTIKNEKFLAGLSTDGFWDIQTFKVIEEAVYFHQHSILACKIEMVDYKEEYNTTLPQFMPYEDGIYSVIQKKVTWYEALNMCSQSGGHLASVHNQNGQLFLEDIVKRDGFPLWVGLSSHDGSESSFEWSDGSTFDYIPWKGQTSPGNCVLLDPKGTWKHEKCNSVKDGAICYKPTKSKKLSRLTYSSRCPAAKENGSRWIQYKGHCYKSDQALHSFSEAKKLCSKHDHSATIVSIKDEDENKFVSRLMRENNNITMRVWLGLSQHSVDQSWSWLDGSEVTFVKWENKSKSGVGRCSMLIASNETWKKVECEHGFGRVVCKVPLGPDYTAIAIIVATLSILVLMGGLIWFLFQRHRLHLAGFSSVRYAQGVNEDEIMLPSFHD
| null | null |
endocytosis [GO:0006897]; immune response [GO:0006955]; inflammatory response [GO:0006954]
|
external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; plasma membrane [GO:0005886]
|
carbohydrate binding [GO:0030246]; signaling receptor activity [GO:0038023]
|
PF00040;PF00059;
|
2.80.10.50;2.10.10.10;3.10.100.10;
| null |
PTM: N-glycosylated. {ECO:0000269|PubMed:9862343}.
|
SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Acts as an endocytic receptor to direct captured antigens from the extracellular space to a specialized antigen-processing compartment (By similarity). Causes reduced proliferation of B-lymphocytes. {ECO:0000250}.
|
Homo sapiens (Human)
|
O60462
|
NRP2_HUMAN
|
MDMFPLTWVFLALYFSRHQVRGQPDPPCGGRLNSKDAGYITSPGYPQDYPSHQNCEWIVYAPEPNQKIVLNFNPHFEIEKHDCKYDFIEIRDGDSESADLLGKHCGNIAPPTIISSGSMLYIKFTSDYARQGAGFSLRYEIFKTGSEDCSKNFTSPNGTIESPGFPEKYPHNLDCTFTILAKPKMEIILQFLIFDLEHDPLQVGEGDCKYDWLDIWDGIPHVGPLIGKYCGTKTPSELRSSTGILSLTFHTDMAVAKDGFSARYYLVHQEPLENFQCNVPLGMESGRIANEQISASSTYSDGRWTPQQSRLHGDDNGWTPNLDSNKEYLQVDLRFLTMLTAIATQGAISRETQNGYYVKSYKLEVSTNGEDWMVYRHGKNHKVFQANNDATEVVLNKLHAPLLTRFVRIRPQTWHSGIALRLELFGCRVTDAPCSNMLGMLSGLIADSQISASSTQEYLWSPSAARLVSSRSGWFPRIPQAQPGEEWLQVDLGTPKTVKGVIIQGARGGDSITAVEARAFVRKFKVSYSLNGKDWEYIQDPRTQQPKLFEGNMHYDTPDIRRFDPIPAQYVRVYPERWSPAGIGMRLEVLGCDWTDSKPTVETLGPTVKSEETTTPYPTEEEATECGENCSFEDDKDLQLPSGFNCNFDFLEEPCGWMYDHAKWLRTTWASSSSPNDRTFPDDRNFLRLQSDSQREGQYARLISPPVHLPRSPVCMEFQYQATGGRGVALQVVREASQESKLLWVIREDQGGEWKHGRIILPSYDMEYQIVFEGVIGKGRSGEIAIDDIRISTDVPLENCMEPISAFAGENFKVDIPEIHEREGYEDEIDDEYEVDWSNSSSATSGSGAPSTDKEKSWLYTLDPILITIIAMSSLGVLLGATCAGLLLYCTCSYSGLSSRSCTTLENYNFELYDGLKHKVKMNHQKCCSEA
| null | null |
angiogenesis [GO:0001525]; axon extension involved in axon guidance [GO:0048846]; axon guidance [GO:0007411]; branchiomotor neuron axon guidance [GO:0021785]; cell adhesion [GO:0007155]; cellular response to leukemia inhibitory factor [GO:1990830]; dorsal root ganglion morphogenesis [GO:1904835]; facial nerve structural organization [GO:0021612]; facioacoustic ganglion development [GO:1903375]; gonadotrophin-releasing hormone neuronal migration to the hypothalamus [GO:0021828]; negative chemotaxis [GO:0050919]; nerve development [GO:0021675]; neural crest cell migration involved in autonomic nervous system development [GO:1901166]; outflow tract septum morphogenesis [GO:0003148]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of endothelial cell proliferation [GO:0001938]; regulation of postsynapse organization [GO:0099175]; semaphorin-plexin signaling pathway [GO:0071526]; sensory neuron axon guidance [GO:0097374]; sympathetic ganglion development [GO:0061549]; sympathetic neuron projection extension [GO:0097490]; sympathetic neuron projection guidance [GO:0097491]; trigeminal ganglion development [GO:0061551]; trigeminal nerve structural organization [GO:0021637]; ventral trunk neural crest cell migration [GO:0036486]; vestibulocochlear nerve structural organization [GO:0021649]
|
axon [GO:0030424]; extracellular region [GO:0005576]; glutamatergic synapse [GO:0098978]; membrane [GO:0016020]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; semaphorin receptor complex [GO:0002116]
|
cytokine binding [GO:0019955]; growth factor binding [GO:0019838]; heparin binding [GO:0008201]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; semaphorin receptor activity [GO:0017154]; signaling receptor activity [GO:0038023]; vascular endothelial growth factor receptor activity [GO:0005021]
|
PF00431;PF11980;PF00754;PF00629;
|
2.60.120.200;2.60.120.260;2.60.120.290;
|
Neuropilin family
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:11112349}; Single-pass type I membrane protein {ECO:0000269|PubMed:11112349}.; SUBCELLULAR LOCATION: [Isoform s9]: Secreted {ECO:0000269|PubMed:11112349}.
| null | null | null | null | null |
FUNCTION: High affinity receptor for semaphorins 3C, 3F, VEGF-165 and VEGF-145 isoforms of VEGF, and the PLGF-2 isoform of PGF.; FUNCTION: (Microbial infection) Acts as a receptor for human cytomegalovirus pentamer-dependent entry in epithelial and endothelial cells. {ECO:0000269|PubMed:30057110}.
|
Homo sapiens (Human)
|
O60469
|
DSCAM_HUMAN
|
MWILALSLFQSFANVFSEDLHSSLYFVNASLQEVVFASTTGTLVPCPAAGIPPVTLRWYLATGEEIYDVPGIRHVHPNGTLQIFPFPPSSFSTLIHDNTYYCTAENPSGKIRSQDVHIKAVLREPYTVRVEDQKTMRGNVAVFKCIIPSSVEAYITVVSWEKDTVSLVSGSRFLITSTGALYIKDVQNEDGLYNYRCITRHRYTGETRQSNSARLFVSDPANSAPSILDGFDHRKAMAGQRVELPCKALGHPEPDYRWLKDNMPLELSGRFQKTVTGLLIENIRPSDSGSYVCEVSNRYGTAKVIGRLYVKQPLKATISPRKVKSSVGSQVSLSCSVTGTEDQELSWYRNGEILNPGKNVRITGINHENLIMDHMVKSDGGAYQCFVRKDKLSAQDYVQVVLEDGTPKIISAFSEKVVSPAEPVSLMCNVKGTPLPTITWTLDDDPILKGGSHRISQMITSEGNVVSYLNISSSQVRDGGVYRCTANNSAGVVLYQARINVRGPASIRPMKNITAIAGRDTYIHCRVIGYPYYSIKWYKNSNLLPFNHRQVAFENNGTLKLSDVQKEVDEGEYTCNVLVQPQLSTSQSVHVTVKVPPFIQPFEFPRFSIGQRVFIPCVVVSGDLPITITWQKDGRPIPGSLGVTIDNIDFTSSLRISNLSLMHNGNYTCIARNEAAAVEHQSQLIVRVPPKFVVQPRDQDGIYGKAVILNCSAEGYPVPTIVWKFSKGAGVPQFQPIALNGRIQVLSNGSLLIKHVVEEDSGYYLCKVSNDVGADVSKSMYLTVKIPAMITSYPNTTLATQGQKKEMSCTAHGEKPIIVRWEKEDRIINPEMARYLVSTKEVGEEVISTLQILPTVREDSGFFSCHAINSYGEDRGIIQLTVQEPPDPPEIEIKDVKARTITLRWTMGFDGNSPITGYDIECKNKSDSWDSAQRTKDVSPQLNSATIIDIHPSSTYSIRMYAKNRIGKSEPSNELTITADEAAPDGPPQEVHLEPISSQSIRVTWKAPKKHLQNGIIRGYQIGYREYSTGGNFQFNIISVDTSGDSEVYTLDNLNKFTQYGLVVQACNRAGTGPSSQEIITTTLEDVPSYPPENVQAIATSPESISISWSTLSKEALNGILQGFRVIYWANLMDGELGEIKNITTTQPSLELDGLEKYTNYSIQVLAFTRAGDGVRSEQIFTRTKEDVPGPPAGVKAAAASASMVFVSWLPPLKLNGIIRKYTVFCSHPYPTVISEFEASPDSFSYRIPNLSRNRQYSVWVVAVTSAGRGNSSEIITVEPLAKAPARILTFSGTVTTPWMKDIVLPCKAVGDPSPAVKWMKDSNGTPSLVTIDGRRSIFSNGSFIIRTVKAEDSGYYSCIANNNWGSDEIILNLQVQVPPDQPRLTVSKTTSSSITLSWLPGDNGGSSIRGYILQYSEDNSEQWGSFPISPSERSYRLENLKCGTWYKFTLTAQNGVGPGRISEIIEAKTLGKEPQFSKEQELFASINTTRVRLNLIGWNDGGCPITSFTLEYRPFGTTVWTTAQRTSLSKSYILYDLQEATWYELQMRVCNSAGCAEKQANFATLNYDGSTIPPLIKSVVQNEEGLTTNEGLKMLVTISCILVGVLLLFVLLLVVRRRRREQRLKRLRDAKSLAEMLMSKNTRTSDTLSKQQQTLRMHIDIPRAQLLIEERDTMETIDDRSTVLLTDADFGEAAKQKSLTVTHTVHYQSVSQATGPLVDVSDARPGTNPTTRRNAKAGPTARNRYASQWTLNRPHPTISAHTLTTDWRLPTPRAAGSVDKESDSYSVSPSQDTDRARSSMVSTESASSTYEELARAYEHAKMEEQLRHAKFTITECFISDTSSEQLTAGTNEYTDSLTSSTPSESGICRFTASPPKPQDGGRVMNMAVPKAHRPGDLIHLPPYLRMDFLLNRGGPGTSRDLSLGQACLEPQKSRTLKRPTVLEPIPMEAASSASSTREGQSWQPGAVATLPQREGAELGQAAKMSSSQESLLDSRGHLKGNNPYAKSYTLV
| null | null |
axon guidance [GO:0007411]; camera-type eye photoreceptor cell differentiation [GO:0060219]; cell adhesion [GO:0007155]; central nervous system development [GO:0007417]; dendrite morphogenesis [GO:0048813]; dendrite self-avoidance [GO:0070593]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; locomotory behavior [GO:0007626]; negative regulation of cell adhesion [GO:0007162]; nervous system development [GO:0007399]; positive regulation of axon extension involved in axon guidance [GO:0048842]; positive regulation of phosphorylation [GO:0042327]; post-embryonic retina morphogenesis in camera-type eye [GO:0060060]; retina layer formation [GO:0010842]; synapse assembly [GO:0007416]
|
axon [GO:0030424]; dendrite [GO:0030425]; extracellular region [GO:0005576]; growth cone [GO:0030426]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; synapse [GO:0045202]
|
cell-cell adhesion mediator activity [GO:0098632]; netrin receptor binding [GO:1990890]; protein tyrosine kinase binding [GO:1990782]
|
PF00041;PF07679;PF13927;
|
2.60.40.10;
| null |
PTM: Phosphorylated at tyrosine residues. Phosphorylation is enhanced by NTN1. {ECO:0000269|PubMed:19196994}.
|
SUBCELLULAR LOCATION: [Isoform Short]: Secreted {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform Long]: Cell membrane {ECO:0000250|UniProtKB:Q9ERC8}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9ERC8}. Cell projection, axon {ECO:0000250|UniProtKB:Q9ERC8}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q9ERC8}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q9ERC8}. Synapse {ECO:0000250|UniProtKB:F1NY98}. Note=Localized in the soma, cell membrane, axon and growth cone of dissociated commissural axons. {ECO:0000250|UniProtKB:Q9ERC8}.
| null | null | null | null | null |
FUNCTION: Cell adhesion molecule that plays a role in neuronal self-avoidance. Promotes repulsion between specific neuronal processes of either the same cell or the same subtype of cells. Mediates within retinal amacrine and ganglion cell subtypes both isoneuronal self-avoidance for creating an orderly dendritic arborization and heteroneuronal self-avoidance to maintain the mosaic spacing between amacrine and ganglion cell bodies (PubMed:10925149). Receptor for netrin required for axon guidance independently of and in collaboration with the receptor DCC. Might also collaborate with UNC5C in NTN1-mediated axon repulsion independently of DCC (By similarity). In spinal cord development plays a role in guiding commissural axons projection and pathfinding across the ventral midline to reach the floor plate upon ligand binding (PubMed:18585357, PubMed:19196994). Mediates intracellular signaling by stimulating the activation of MAPK8 and MAP kinase p38 (PubMed:18585357, PubMed:19196994). Adhesion molecule that promotes lamina-specific synaptic connections in the retina: expressed in specific subsets of interneurons and retinal ganglion cells (RGCs) and promotes synaptic connectivity via homophilic interactions (By similarity). {ECO:0000250|UniProtKB:F1NY98, ECO:0000250|UniProtKB:Q9ERC8, ECO:0000269|PubMed:10925149, ECO:0000269|PubMed:18585357, ECO:0000269|PubMed:19196994}.
|
Homo sapiens (Human)
|
O60476
|
MA1A2_HUMAN
|
MTTPALLPLSGRRIPPLNLGPPSFPHHRATLRLSEKFILLLILSAFITLCFGAFFFLPDSSKHKRFDLGLEDVLIPHVDAGKGAKNPGVFLIHGPDEHRHREEEERLRNKIRADHEKALEEAKEKLRKSREEIRAEIQTEKNKVVQEMKIKENKPLPPVPIPNLVGIRGGDPEDNDIREKREKIKEMMKHAWDNYRTYGWGHNELRPIARKGHSPNIFGSSQMGATIVDALDTLYIMGLHDEFLDGQRWIEDNLDFSVNSEVSVFEVNIRFIGGLLAAYYLSGEEIFKIKAVQLAEKLLPAFNTPTGIPWAMVNLKSGVGRNWGWASAGSSILAEFGTLHMEFIHLSYLTGDLTYYKKVMHIRKLLQKMDRPNGLYPNYLNPRTGRWGQYHTSVGGLGDSFYEYLLKAWLMSDKTDHEARKMYDDAIEAIEKHLIKKSRGGLTFIGEWKNGHLEKKMGHLACFAGGMFALGADGSRADKAGHYLELGAEIARTCHESYDRTALKLGPESFKFDGAVEAVAVRQAEKYYILRPEVIETYWYLWRFTHDPRYRQWGWEAALAIEKYCRVNGGFSGVKDVYSSTPTHDDVQQSFFLAETLKYLYLLFSGDDLLPLDHWVFNTEAHPLPVLHLANTTLSGNPAVR
|
3.2.1.113
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P45700};
|
carbohydrate metabolic process [GO:0005975]; lung alveolus development [GO:0048286]; N-glycan processing [GO:0006491]; protein glycosylation [GO:0006486]; respiratory gaseous exchange by respiratory system [GO:0007585]
|
endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; membrane [GO:0016020]
|
calcium ion binding [GO:0005509]; mannosyl-oligosaccharide 1,2-alpha-mannosidase activity [GO:0004571]
|
PF01532;
|
1.50.10.10;
|
Glycosyl hydrolase 47 family
| null |
SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II membrane protein.
|
CATALYTIC ACTIVITY: Reaction=4 H2O + N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 9A1,2,3B1,2,3) = 4 beta-D-mannose + N(4)-(alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 5A1,2); Xref=Rhea:RHEA:56008, Rhea:RHEA-COMP:14356, Rhea:RHEA-COMP:14367, ChEBI:CHEBI:15377, ChEBI:CHEBI:28563, ChEBI:CHEBI:59087, ChEBI:CHEBI:139493; EC=3.2.1.113; Evidence={ECO:0000250|UniProtKB:P32906}; CATALYTIC ACTIVITY: Reaction=3 H2O + N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 8A1,2,3B1,3) = 3 beta-D-mannose + N(4)-(alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 5A1,2); Xref=Rhea:RHEA:56028, Rhea:RHEA-COMP:14358, Rhea:RHEA-COMP:14367, ChEBI:CHEBI:15377, ChEBI:CHEBI:28563, ChEBI:CHEBI:59087, ChEBI:CHEBI:60628; EC=3.2.1.113; Evidence={ECO:0000250|UniProtKB:P32906};
| null |
PATHWAY: Protein modification; protein glycosylation. {ECO:0000250|UniProtKB:P32906}.
| null | null |
FUNCTION: Involved in the maturation of Asn-linked oligosaccharides. Progressively trim alpha-1,2-linked mannose residues from Man(9)GlcNAc(2) to produce Man(5)GlcNAc(2).
|
Homo sapiens (Human)
|
O60477
|
BRNP1_HUMAN
|
MNWRFVELLYFLFIWGRISVQPSHQEPAGTDQHVSKEFDWLISDRGPFHHSRSYLSFVERHRQGFTTRYKIYREFARWKVRNTAIERRDLVRHPVPLMPEFQRSIRLLGRRPTTQQFIDTIIKKYGTHLLISATLGGEEALTMYMDKSRLDRKSGNATQSVEALHQLASSYFVDRDGTMRRLHEIQISTGAIKVTETRTGPLGCNSYDNLDSVSSVLLQSTESKLHLQGLQIIFPQYLQEKFVQSALSYIMCNGEGEYLCQNSQCRCQCAEEFPQCNCPITDIQIMEYTLANMAKSWAEAYKDLENSDEFKSFMKRLPSNHFLTIGSIHQHWGNDWDLQNRYKLLQSATEAQRQKIQRTARKLFGLSVRCRHNPNHQLPRERTIQQWLARVQSLLYCNENGFWGTFLESQRSCVCHGSTTLCQRPIPCVIGGNNSCAMCSLANISLCGSCNKGYKLYRGRCEPQNVDSERSEQFISFETDLDFQDLELKYLLQKMDSRLYVHTTFISNEIRLDTFFDPRWRKRMSLTLKSNKNRMDFIHMVIGMSMRICQMRNSSLDPMFFVYVNPFSGSHSEGWNMPFGEFGYPRWEKIRLQNSQCYNWTLLLGNRWKTFFETVHIYLRSRTRLPTLLRNETGQGPVDLSDPSKRQFYIKISDVQVFGYSLRFNADLLRSAVQQVNQSYTQGGQFYSSSSVMLLLLDIRDRINRLAPPVAPGKPQLDLFSCMLKHRLKLTNSEIIRVNHALDLYNTEILKQSDQMTAKLC
| null | null |
behavioral fear response [GO:0001662]; brain development [GO:0007420]; cell cycle [GO:0007049]; cellular response to retinoic acid [GO:0071300]; central nervous system neuron development [GO:0021954]; exploration behavior [GO:0035640]; maternal behavior [GO:0042711]; negative regulation of cell cycle [GO:0045786]; negative regulation of mitotic cell cycle [GO:0045930]; negative regulation of neurogenesis [GO:0050768]; positive regulation of neuron differentiation [GO:0045666]; short-term memory [GO:0007614]; social behavior [GO:0035176]; vocalization behavior [GO:0071625]
|
cytoplasm [GO:0005737]; dendrite [GO:0030425]; neuronal cell body [GO:0043025]
| null |
PF19052;PF01823;
| null |
BRINP family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11420708, ECO:0000269|PubMed:14712213}.
| null | null | null | null | null |
FUNCTION: Plays a role in neurogenesis and brain development (By similarity). May suppress cell cycle progression in postmitotic neurons by inhibiting G1/S transition (PubMed:11420708). {ECO:0000250|UniProtKB:Q920P3, ECO:0000269|PubMed:11420708}.
|
Homo sapiens (Human)
|
O60478
|
G137B_HUMAN
|
MRPERPRPRGSAPGPMETPPWDPARNDSLPPTLTPAVPPYVKLGLTVVYTVFYALLFVFIYVQLWLVLRYRHKRLSYQSVFLFLCLFWASLRTVLFSFYFKDFVAANSLSPFVFWLLYCFPVCLQFFTLTLMNLYFTQVIFKAKSKYSPELLKYRLPLYLASLFISLVFLLVNLTCAVLVKTGNWERKVIVSVRVAINDTLFVLCAVSLSICLYKISKMSLANIYLESKGSSVCQVTAIGVTVILLYTSRACYNLFILSFSQNKSVHSFDYDWYNVSDQADLKNQLGDAGYVLFGVVLFVWELLPTTLVVYFFRVRNPTKDLTNPGMVPSHGFSPRSYFFDNPRRYDSDDDLAWNIAPQGLQGGFAPDYYDWGQQTNSFLAQAGTLQDSTLDPDKPSLG
| null | null |
autophagy [GO:0006914]; negative regulation of bone resorption [GO:0045779]; negative regulation of osteoclast differentiation [GO:0045671]; positive regulation of protein localization to lysosome [GO:0150032]; positive regulation of TORC1 signaling [GO:1904263]; regulation of autophagy [GO:0010506]; regulation of GTPase activity [GO:0043087]; regulation of macrophage activation [GO:0043030]
|
lysosomal membrane [GO:0005765]; membrane [GO:0016020]; plasma membrane [GO:0005886]
| null | null | null |
GPR137 family
| null |
SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:22729905, ECO:0000269|PubMed:31036939}; Multi-pass membrane protein {ECO:0000269|PubMed:22729905}. Note=Colocalized with MTOR in lysosome after amino acid stimulation. {ECO:0000269|PubMed:31036939}.
| null | null | null | null | null |
FUNCTION: Lysosomal integral membrane protein that regulates the localization and activity of mTORC1, a signaling complex promoting cell growth in response to growth factors, energy levels, and amino acids (PubMed:31036939). Interacts with Rag GTPases and increases the lysosomial localization and activity of Rag GTPases and thereby regulates mTORC1 translocation and activity in lysosome (PubMed:31036939). Involved in the regulation of lysosomal morphology and autophagy (PubMed:31036939). {ECO:0000269|PubMed:31036939}.; FUNCTION: Acts also as a negative regulator of osteoclast activity (By similarity). Involved in interleukin-4-induced M2 macrophage polarization (By similarity). {ECO:0000250|UniProtKB:Q8BNQ3}.
|
Homo sapiens (Human)
|
O60479
|
DLX3_HUMAN
|
MSGSFDRKLSSILTDISSSLSCHAGSKDSPTLPESSVTDLGYYSAPQHDYYSGQPYGQTVNPYTYHHQFNLNGLAGTGAYSPKSEYTYGASYRQYGAYREQPLPAQDPVSVKEEPEAEVRMVNGKPKKVRKPRTIYSSYQLAALQRRFQKAQYLALPERAELAAQLGLTQTQVKIWFQNRRSKFKKLYKNGEVPLEHSPNNSDSMACNSPPSPALWDTSSHSTPAPARSQLPPPLPYSASPSYLDDPTNSWYHAQNLSGPHLQQQPPQPATLHHASPGPPPNPGAVY
| null | null |
blood vessel development [GO:0001568]; BMP signaling pathway [GO:0030509]; embryo development [GO:0009790]; epithelial cell differentiation [GO:0030855]; gene expression [GO:0010467]; hair cell differentiation [GO:0035315]; hair follicle cell proliferation [GO:0071335]; hair follicle morphogenesis [GO:0031069]; odontoblast differentiation [GO:0071895]; odontogenesis of dentin-containing tooth [GO:0042475]; placenta development [GO:0001890]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]; Wnt signaling pathway [GO:0016055]
|
chromatin [GO:0000785]; cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific double-stranded DNA binding [GO:1990837]; transcription cis-regulatory region binding [GO:0000976]
|
PF12413;PF00046;
|
1.10.10.60;
|
Distal-less homeobox family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. Cytoplasm {ECO:0000250|UniProtKB:Q64205}.
| null | null | null | null | null |
FUNCTION: Transcriptional activator (By similarity). Activates transcription of GNRHR, via binding to the downstream activin regulatory element (DARE) in the gene promoter (By similarity). {ECO:0000250|UniProtKB:Q64205}.
|
Homo sapiens (Human)
|
O60481
|
ZIC3_HUMAN
|
MTMLLDGGPQFPGLGVGSFGAPRHHEMPNREPAGMGLNPFGDSTHAAAAAAAAAAFKLSPAAAHDLSSGQSSAFTPQGSGYANALGHHHHHHHHHHHTSQVPSYGGAASAAFNSTREFLFRQRSSGLSEAASGGGQHGLFAGSASSLHAPAGIPEPPSYLLFPGLHEQGAGHPSPTGHVDNNQVHLGLRGELFGRADPYRPVASPRTDPYAAGAQFPNYSPMNMNMGVNVAAHHGPGAFFRYMRQPIKQELSCKWIDEAQLSRPKKSCDRTFSTMHELVTHVTMEHVGGPEQNNHVCYWEECPREGKSFKAKYKLVNHIRVHTGEKPFPCPFPGCGKIFARSENLKIHKRTHTGEKPFKCEFEGCDRRFANSSDRKKHMHVHTSDKPYICKVCDKSYTHPSSLRKHMKVHESQGSDSSPAASSGYESSTPPAIASANSKDTTKTPSAVQTSTSHNPGLPPNFNEWYV
| null | null |
atrial cardiac muscle tissue development [GO:0003228]; axial mesoderm development [GO:0048318]; central nervous system development [GO:0007417]; central nervous system segmentation [GO:0035283]; cranial skeletal system development [GO:1904888]; determination of digestive tract left/right asymmetry [GO:0071907]; determination of left/right asymmetry in nervous system [GO:0035545]; determination of left/right symmetry [GO:0007368]; determination of liver left/right asymmetry [GO:0071910]; determination of pancreatic left/right asymmetry [GO:0035469]; embryonic pattern specification [GO:0009880]; face development [GO:0060324]; germ-line stem cell population maintenance [GO:0030718]; heart looping [GO:0001947]; hippocampus development [GO:0021766]; left/right axis specification [GO:0070986]; limb morphogenesis [GO:0035108]; lung development [GO:0030324]; mRNA transcription by RNA polymerase II [GO:0042789]; neural plate development [GO:0001840]; neuron differentiation [GO:0030182]; olfactory bulb development [GO:0021772]; outer ear morphogenesis [GO:0042473]; paraxial mesoderm development [GO:0048339]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of transcription by RNA polymerase II [GO:0045944]; primitive streak formation [GO:0090009]; skeletal system development [GO:0001501]; smoothened signaling pathway [GO:0007224]; stem cell differentiation [GO:0048863]
|
cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]; sequence-specific double-stranded DNA binding [GO:1990837]; transcription coactivator activity [GO:0003713]
|
PF00096;PF18366;
|
3.30.160.60;
|
GLI C2H2-type zinc-finger protein family
| null |
SUBCELLULAR LOCATION: Nucleus. Cytoplasm {ECO:0000250}. Note=Localizes in the cytoplasm in presence of MDFIC overexpression (By similarity). Translocation to the nucleus requires KPNA1 or KPNA6. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Acts as a transcriptional activator. Required in the earliest stages in both axial midline development and left-right (LR) asymmetry specification. Binds to the minimal GLI-consensus sequence 5'-GGGTGGTC-3'. {ECO:0000269|PubMed:17764085}.
|
Homo sapiens (Human)
|
O60486
|
PLXC1_HUMAN
|
MEVSRRKAPPRPPRPAAPLPLLAYLLALAAPGRGADEPVWRSEQAIGAIAASQEDGVFVASGSCLDQLDYSLEHSLSRLYRDQAGNCTEPVSLAPPARPRPGSSFSKLLLPYREGAAGLGGLLLTGWTFDRGACEVRPLGNLSRNSLRNGTEVVSCHPQGSTAGVVYRAGRNNRWYLAVAATYVLPEPETASRCNPAASDHDTAIALKDTEGRSLATQELGRLKLCEGAGSLHFVDAFLWNGSIYFPYYPYNYTSGAATGWPSMARIAQSTEVLFQGQASLDCGHGHPDGRRLLLSSSLVEALDVWAGVFSAAAGEGQERRSPTTTALCLFRMSEIQARAKRVSWDFKTAESHCKEGDQPERVQPIASSTLIHSDLTSVYGTVVMNRTVLFLGTGDGQLLKVILGENLTSNCPEVIYEIKEETPVFYKLVPDPVKNIYIYLTAGKEVRRIRVANCNKHKSCSECLTATDPHCGWCHSLQRCTFQGDCVHSENLENWLDISSGAKKCPKIQIIRSSKEKTTVTMVGSFSPRHSKCMVKNVDSSRELCQNKSQPNRTCTCSIPTRATYKDVSVVNVMFSFGSWNLSDRFNFTNCSSLKECPACVETGCAWCKSARRCIHPFTACDPSDYERNQEQCPVAVEKTSGGGRPKENKGNRTNQALQVFYIKSIEPQKVSTLGKSNVIVTGANFTRASNITMILKGTSTCDKDVIQVSHVLNDTHMKFSLPSSRKEMKDVCIQFDGGNCSSVGSLSYIALPHCSLIFPATTWISGGQNITMMGRNFDVIDNLIISHELKGNINVSEYCVATYCGFLAPSLKSSKVRTNVTVKLRVQDTYLDCGTLQYREDPRFTGYRVESEVDTELEVKIQKENDNFNISKKDIEITLFHGENGQLNCSFENITRNQDLTTILCKIKGIKTASTIANSSKKVRVKLGNLELYVEQESVPSTWYFLIVLPVLLVIVIFAAVGVTRHKSKELSRKQSQQLELLESELRKEIRDGFAELQMDKLDVVDSFGTVPFLDYKHFALRTFFPESGGFTHIFTEDMHNRDANDKNESLTALDALICNKSFLVTVIHTLEKQKNFSVKDRCLFASFLTIALQTKLVYLTSILEVLTRDLMEQCSNMQPKLMLRRTESVVEKLLTNWMSVCLSGFLRETVGEPFYLLVTTLNQKINKGPVDVITCKALYTLNEDWLLWQVPEFSTVALNVVFEKIPENESADVCRNISVNVLDCDTIGQAKEKIFQAFLSKNGSPYGLQLNEIGLELQMGTRQKELLDIDSSSVILEDGITKLNTIGHYEISNGSTIKVFKKIANFTSDVEYSDDHCHLILPDSEAFQDVQGKRHRGKHKFKVKEMYLTKLLSTKVAIHSVLEKLFRSIWSLPNSRAPFAIKYFFDFLDAQAENKKITDPDVVHIWKTNSLPLRFWVNILKNPQFVFDIKKTPHIDGCLSVIAQAFMDAFSLTEQQLGKEAPTNKLLYAKDIPTYKEEVKSYYKAIRDLPPLSSSEMEEFLTQESKKHENEFNEEVALTEIYKYIVKYFDEILNKLERERGLEEAQKQLLHVKVLFDEKKKCKWM
| null | null |
cell adhesion [GO:0007155]; negative regulation of cell adhesion [GO:0007162]; positive regulation of axonogenesis [GO:0050772]; regulation of cell migration [GO:0030334]; regulation of cell shape [GO:0008360]; regulation of synapse pruning [GO:1905806]; semaphorin-plexin signaling pathway involved in axon guidance [GO:1902287]
|
cerebellar climbing fiber to Purkinje cell synapse [GO:0150053]; membrane [GO:0016020]; plasma membrane [GO:0005886]; semaphorin receptor complex [GO:0002116]
|
semaphorin receptor activity [GO:0017154]; signaling receptor binding [GO:0005102]
|
PF08337;PF20170;PF01437;PF01833;
|
2.60.40.10;3.30.1680.10;2.130.10.10;
|
Plexin family
|
PTM: N-glycosylated. {ECO:0000269|PubMed:20727575, ECO:0000269|PubMed:9586637}.
|
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Receptor for SEMA7A, for smallpox semaphorin A39R, vaccinia virus semaphorin A39R and for herpesvirus Sema protein. Binding of semaphorins triggers cellular responses leading to the rearrangement of the cytoskeleton and to secretion of IL6 and IL8 (By similarity). {ECO:0000250, ECO:0000269|PubMed:20727575}.
|
Homo sapiens (Human)
|
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