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
MSVTPPNVQFNLNGDSDHKSDNSSSSLENKLDTELKITSPPRNPPQRLHPVDFSEHADTDDDMNHPLPRVQSPVHIKNHIDPKLAEDRYRSSAARHFEPISIPPSAITSEDEDDYHGSANSSTVLPPRTENALHAASPKPSGSTGYTSPALSQNSGSGGEGESDEGSFNTQHHRSPIFQAYPSSEDLVGDPNDPYRRTRRAPIKTNPHDIPSQFIFRKLGLHHGKHGHHGHSGSLSLKSLVPNHHDKHDKHDKHEKHHSSLDLRRFFKSHQKTDKEKKPSVSKSKSSANLQDDHFGLFKKYGKFGRMLGSGAGGSVRIMK...
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}; CATALYTI...
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
MSDSKLADSLNCLSVSTPSTTANPGRQQLLRLAVSNQRQVNNVSLANGKENKRTSNSKFNSSLRKIEEPIAGVPSSAGPQWREFHIGMFEIGKPLGKGKFGRVYLAKEKKTGFIVALKTLHKSELVQSKIEKQVRREIEIQSNLRHKNILRLYGHFHDEKRIYLILEFAGRGELYQHLRRAKRFSEEVASKYIFQMANALSYLHKKHVIHRDIKPENILLGIDGEIKLSDFGWSVHAPSNRRTTLCGTLDYLPPEMVEGKEHTEKVDLWSLGVLTYEFLVGAPPFEDMSGHSATYKRIAKVDLKIPSFVPPDARDLISRL...
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 checkp...
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]; n...
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-[pr...
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 formatio...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O59791
SRR_SCHPO
MSDNLVLPTYDDVASASERIKKFANKTPVLTSSTVNKEFVAEVFFKCENFQKMGAFKFRGALNALSQLNEAQRKAGVLTFSSGNHAQAIALSAKILGIPAKIIMPLDAPEAKVAATKGYGGQVIMYDRYKDDREKMAKEISEREGLTIIPPYDHPHVLAGQGTAAKELFEEVGPLDALFVCLGGGGLLSGSALAARHFAPNCEVYGVEPEAGNDGQQSFRKGSIVHIDTPKTIADGAQTQHLGNYTFSIIKEKVDDILTVSDEELIDCLKFYAARMKIVVEPTGCLSFAAARAMKEKLKNKRIGIIISGGNVDIERYAHF...
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'-p...
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:00181...
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; Eviden...
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
MNLGRCPLAPRSANIVLPKHDAVSKQKEYRIEEKTNEAQREEIITWKDNREDEGEVKTDFEVVNNENIITTTPKHQTVITPKSYRKSVKRIKHDAPQNEDIPVMKGLAPINADTESKAESMAAGKVLGSKNSSQKARLQEWKRQYKKAFPHFRFYLDGCDPSVAHRVKKQIQQLGGHVETFFSGNVTHVATVRAIQDVSVKYAKQDVITKARQLNMKIWSMEKLCNRVLKTLMENDQCTTNAPTKQGNDLSYLLYVEKVQGTNERDLSVPRQDFVHFRGPYLYVHDIANIYKPILLREWQKPLPDRDVPWPTFRATSIGR...
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 [...
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
MSKSIGIDLGTTYSCVGHFSNNRVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPHNTIFDAKRLIGRKFDDPEVQSDMKHWPFKVISKDGKPVLQVEYKGETKTFTPEEISSMVLMKMRETAEAYLGGKVTDAVVTVPAYFNDSQRQATKDAGLIAGLNVLRIINEPTAAAIAYGLDRSNQGESNVLIFDLGGGTFDVSLLTIEEGIFEVKATAGDTHLGGEDFDSRLVNHFIQEFKRKNKKDITGNARAVRRLRTACERAKRTLSSSAQASIEIDSLFEGIDFYTSITRARFEELCADLFRKTMEPVERVLR...
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:1...
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:...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O59868
ATC1_SCHPO
MSVQYDAFSVEQTCADLETDMYNGLSSLQEITRRNKVHGDNDLKVEDEENMVVQFLKQFVKDPLILLLFASSAISVTLGNIDDAISIALAIVIVVTVGFVQEYRSEQSLKALNNLVPHYCNVIRSGKTEHIVASKLVPGDLVILQIGDRVPADLRIVEATELEIDESNLTGENSPRKKSSEAISSNISLTERNNIAFMGTLVRHGHGRGIVVATGSDTEFGRVFLTMQQTEKPKTPLQNSMDDLGKQLSLISLIGIAVIVLVGFFQGKNWLEMLTIGVSLAVAAIPEGLPIIVTVTLALGVLRMSKKRAIIRRLPSVETL...
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
MTTFWSQTINRQNGGVATATATATATAATTTPTAGGTGAGTTTSTKGMITPTPFNIDINNDLNDFDGKFIETFKPDLELQKKYRSFIQREGALSFLRTEITQSMSKRDICVLILNLGYPKKAVEDYPILTLKELAYILLKLMLTDSAQLEPKVEIDENDNKNDGTNNSDIDSDIDSNSDMDSQSESGELDDAMDVDDSLSENEDEYDQDMSTTTLKRTINMTPFKYKLPDLISDLSRAKKIMVVTGAGISTSLGIPDFRSFKGLYNQLSKLNLSDPQKVFDLQTFMREPGLFYTIAHLVLPPDGKFSLLHAFLKLLQDKH...
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=...
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'...
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]...
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...
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 (P...
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
O59945
FIMB_SCHPO
MLALKLQKKYPELTNEEILTLTDQFNKLDVDGKGYLDQPTTIKAFEDSKKGSYDEVREAIREVNVDSSGRVEPEDFVGIFNVLKKGVEGTEVKKGRITIKGSSSSVSHTINEEERREFIKHINSVLAGDPDVGSRVPINTETFEFFDQCKDGLILSKLINDSVPDTIDERVLNKQRNNKPLDNFKCIENNNVVINSAKAMGGISITNIGAGDILEGREHLILGLVWQIIRRGLLGKIDITLHPELYRLLEEDETLDQFLRLPPEKILLRWFNYHLKAANWPRTVSNFSKDVSDGENYTVLLNQLAPELCSRAPLQTTDVL...
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:01100...
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
MEDLETRCASLRTEIAAAEAQLTKLKRELHEAEGAALRAQSQKTASANATTGQRTKSKWPLHGEEYRRYGRQMIVPQFGLQGQLKLRDAKVLIVGAGGLGCPAALYLAGAGVGTIGLVDGDTVEASNLHRQVLHRSRNVGKLKVDSAIEYLRELNPHPTYIAHQAHLTPREAPDIFKDYDLILDCTDNPATRYLISDTAVLLGKPLVSASALRTEGQLMVLNNPPQPPGDKTGGPCYRCVFPKPPPANSVTSCADGGILGPVVGTMGVLQASEAIKVLTSAGESVEATPPSLLIFSAYSSPQFRTIKLRSRRPNCAVCSA...
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:000...
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, ...
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 urm...
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
O60016
CLR4_SCHPO
MSPKQEEYEVERIVDEKLDRNGAVKLYRIRWLNYSSRSDTWEPPENLSGCSAVLAEWKRRKRRLKGSNSDSDSPHHASNPHPNSRQKHQHQTSKSVPRSQRFSRELNVKKENKKVFSSQTTKRQSRKQSTALTTNDTSIILDDSLHTNSKKLGKTRNEVKEESQKRELVSNSIKEATSPKTSSILTKPRNPSKLDSYTHLSFYEKRELFRKKLREIEGPEVTLVNEVDDEPCPSLDFQFISQYRLTQGVIPPDPNFQSGCNCSSLGGCDLNNPSRCECLDDLDEPTHFAYDAQGRVRADTGAVIYECNSFCSCSMECPNR...
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-mediat...
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]; his...
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:...
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 c...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O60020
ASPR1_PHARH
MISDTVIAILAVALVGSTVQAAPVDATATSTSGIIAVPISKSAAQLAREADPVVSLDWLKKTKAQAQYKHKQANARLHSKRATGASVLTDQGSESLWTGPITIGGQSFTVDWDTGSSDLWVPSSACSSAACNAHHKYTLTSTGKKQSGTFSISYGDGSSASGPVYKDNVVASGLQATSQVFGAVTSESSSFSSDPSDGISGLGWPALAQLSGTSYFWSLINQGTVTSPVFSFRLATTNSELYLGGINSAHYTGAITYTPVTQKAYWTIALGGVSVNGAAINPSVSSAIIDTGTTLVYGPTAGVAALYAKIPGSASMADTY...
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|Pu...
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 compl...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O60060
CARA_SCHPO
MLRFLKPFPLRFGKRFYSKVPPVTNHERILPKQPSFPTAPAQNEIATLTIRNGPIFHGTSFGANRNVSGEAVFTTSPVGYVESLTDPSYKQQILIFTQPLIGNYGVPDCKKRDENGLLRHFESPHIQCAGVVVNDYATKYSHWTAVESLGEWCAREGVAAITGVDTRAIVTFLREQGSSLAKISIGEEYDANDDEAFINPEEVNLVSQVSTREPFFVSGGDGMLNIAVIDCGVKENILRSLVSRGASVTVFPFDYPIQNVASNYDGIFLTNGPGDPTHLTKTVNNLRELMNTYNGPIMGICMGHQLLALSTGAKTIKLKY...
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...
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 amidotran...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O60070
ASH2_SCHPO
MLAHGSNDYGVSLKGNKTGSSPSKASSLNWNEPHTLNEQNTYCYCGKDRNLRFPDLQCSVCLNMFHLSCLSPPCTSMMGFSTNYQFVCKHCTEDGFERFERGVSAWKAITATAMANLVVKRYVETNPDVPVDSFNAEKMRNFQANTYFFKKKEDLIPFIEEHWQLLCPDREKVQTWQATLGSCLVANRDTYRAKDETMRNQNSEYALNNPNLFDFRSGYIFPFQRVGATVPKKRLVETETPPPSSSKLKEDYKDSKREMKRSNTPWSNASIKKNEVPTVPIRYKPPPWRDSDFETVPKLPIFYPNSSSPNFFSLSEIPFN...
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...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O60094
DPO5_SCHPO
MATKTQLELFTKLTSNDKAIRLSSAAQLIDSLSNEEELKYSLNRLTKGLSSGRESARIGFAVALTELLTRTKDIRATHVLDLLVKHNTASGNLKGQDERDFYFGLLFGLQSIVYSGILTHKESTIEDFQRVVDLLLQLSGKKNWLQDVCFYVIYKLVEQIPEISFSSNAFLAVNKLLQTPAVSKSTEGVGLFLCLTRVPDNVKSEEVAMANWEPAHPLHKSNLVTLSKIMRQADASETGGQNSAWKQKIPMVWKYIFEEYQRKTYSGLAPFHDFWAVVVDEGIFSSTSSLERKFWGFQIMELALDYVSSDNIGDIFSKNF...
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
MSVECSGELFFYPPFTTMSKELISVHNPNPEPVIFKVKTTAPKHYCVRPNSGKIEPKSTVNVQVLLQAMKEEPAPDFKCRDKFLIQSMAIGDADTSNVENYHEFWTEMEKQGRSIFDRKIRCVYSTKQPPQSADKQVENTSTSNPPVSVEGSENLASSVGGPTAVGVSLDEAQNDFNGAKDHLSNGVNTVVPDSTFRSTFESAQIPDASVVQTVVTDADNGAASVKDTIVTAESASSKGADVARSKVQDIIDNEIPKPSESPRRSVSSTPPVHPPPPVPQNLSAVNEEFDTKKNDFDSKLPESTPAVEKVSENLGSETRE...
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 componen...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O60126
TOP3_SCHPO
MRVLCVAEKNSIAKSVASILGGGHVRRRDTRSKYVKNYDFSFNFGGNVGSSDVTMTSVSGHLTEASFPSEYSSWSSVPQDVLFDAQIITSVSKNAEVLADNIKKEARNAQYLYIWTDCDREGEHIGVEISNVARASNPSIQVIRADFNNLERSHIISAAKRPRDVSKNAADAVDARIELDFRLGAIFTRLQTIQLQKSFDILQNKIISYGPCQFPTLGFVVDRWQRVEDFVPETYWHLRFVDKRQGKTIQFNWERAKVFDRLTTMIILENCLECKTAKVVNITQKPKTKYKPLPLSTVELTKLGPKHLRISAKKTLELAE...
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...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O60129
FKH2_SCHPO
MTVRRLESKSEHISDDEERKEQLDYKKQMDVDTDRNIVLNGRLESQIAKLSVPPHEMRVVDDYSNSKNAERHSGEIQAYAKFAGSTWTYYVKKIRIILGREPANPSPKGKNEDLEVIDMNFGPSKVVSRKHAVVEYDLDDQTWNCSVYGRNGIKVDGKLFKNGETVKLTSGSILEVAGLQMMFVLPNAAEQKQTDESTIKEDAIKSEISAAVNDAAEYGDNKKPPYSYSVMIAQAILSSSECMMTLSNIYSWISTHYPYYRTTKSGWQNSIRHNLSLNKAFRKVPRKSGEQGKGMKWSIVPEFREEFIAKTRKTPRKRSP...
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 po...
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 ...
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 spo1...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O60132
TEA4_SCHPO
MLHMNSASSADSMEIMESHFDPTQQNDSTIIESRYSPEEYLEQSFEIQRIISGENSEPQTVASQEISDSQEEDTTLTSSQFEDCGTEYNEVVEDDEFRSEDEDDFMDEEEEYALYEAELSSSPSIHEEVIDCNFVHAIRGFEATVEGQVDATKGDMMILLDDSNSYWWLVKMCKNLAIGYLPAEYIETPSERLARLNKYKNSETSNSQQSVTLPPLDIVEKTLEAPSPNFRIKRVTFTCSSNSSDDEMDSENDYEAMVNRTVAENGLEIEFSDSSDSSLSAEYRSESEDHVTDSPAYVDLTELEGGFNQFNSTSFQSTSP...
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]; positiv...
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 condi...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O60139
UBP4_SCHPO
MSDDYFDRLFELAFVYINEDETIQSCSFRGQRWLEEAQTLEQKNSLLKAYYYYLKALKLAYEIPCRFEISVKSTHYGEFKQFQKLAIQAVSKAFTIKSKLAVKHYLPVIQISDALSLSKKSSLKVLFLNFYSQESSKGYVFSKHTIAIPISCLQSMDSSKIYDFLKSAPFHPSMVICYSLERYFEDVSLAYKLYSMLRSLKLDPHFMELANPKKVDSSLSYENYQPIGLTNLGNTCYMNCVLQCLFACKDLTIPMLQGRGLLQNINTKNPLGTGGKITSAFFSLLQSVLLNHGQRSISPRNFLEIVQSLNRDFSIDGQCD...
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
MTENEKSRSLPAERNPLYKDDTLDHTPLIPKCRAQVIEFPDGPATFVRLKCTNPESKVPHFLMRMAKDSSISATSMFRSAFPKATQEEEDLEMRWIRDNLNPIEDKRVAGLWVPPADALALAKDYSMTPFINALLEASSTPSTYATPSRPTAQKSETSEGEPESSTSATTTSVARRTRQRLAEHLENSKKTILQHDNKEEDKEIHSEENETKDEIKSEKKEPEIKKQEGGSSTEKVGQPSSSDDKAKGSTSKDQPSEEEEKTSDIQDRKIKTPIKPSLLGKIRSSVNKGMTDVASQVNRGMTDVASQVNKGVNGVASQVN...
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:...
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
MNKGPRHRPKFLSKKGKKLRIMVAGSSYTSYQACINSLCSKQILEAETEIDPLKAHIDRILEIREFNADILEDEFHVDLTVIEVNGFGDKIDNSASFEVVTHYLESQFDQALIEESKIKRNSKFTDTRVDALLYFIAPRGHCLSEFDLEAMKRFSKRVNVIPVIGNSNAFTEEELKNFKDVIMKDLKQCNIKVFDFPWDPEEDEDEVIEDNKRLWESVPFAVSGGVSEEDEEGYQRIVKKFQWGTFVIDDPAHSDFLNLKTVLFISHLDILKSITKQTYYENYRTEKLSNDSPSNTSLSLQKQNSIVANEDKRSVNGSER...
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
MSNSDIRSFFGGGNAQKKPKVSPTPTSPKPKRSLKKKRIVLSDDEDGTIENSKVPASKSKVQKRNESEDISHSLPSIVHEDDKLVGSDGVSTTPDEYFEQQSTRSRSKPRIISNKETTTSKDVVHPVKTENFANDLDTTSDSKPVVHQTRATRKPAQPKAEKSTTSKSKSHTTTATTHTSRSSKSKGLPRFSDEVSQALKNVPLIDVDSMGVMAPGTFYERAATTQTPGSKPVPEGNSDCLSGISFVITGILETLTRQEATDLIKQYGGKVTGAPSVRTDFILLGENAGPRKVETIKQHKIPAINEDGLFYLITHLPASG...
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 replica...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O60184
CYC8_SCHPO
MPQSQVATASPSQNAQPNHGMGSKVLSSDPNASLPPQTAYYASPLHANSVSLPPSHLPRSTLHPLLSQQQQPAQQSPSLGPAQQNIQQPPSVSIASQPHYAEAIVPIQQVLQPQQYRQLPPNMVAATNAPQQHPQLQRMMPILSSNQPIQQLPLPNQASPYIPVPLQQQQQSQPQQQPQQQQHQQPQQPQPPQQPLQQQQQQRQLHSGIQQPVSTIVSQNGTYYSIPAVNHPMAGQPIAIAPVPAPNQAALPPIPPQALPANGTPNTLASPVTLPAANSAVQNAQPVPMTSSPAMAVVPQNKTAATSTLAAQQGANVLPP...
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 transcripti...
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) betwe...
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
O60216
RAD21_HUMAN
MFYAHFVLSKRGPLAKIWLAAHWDKKLTKAHVFECNLESSVESIISPKVKMALRTSGHLLLGVVRIYHRKAKYLLADCNEAFIKIKMAFRPGVVDLPEENREAAYNAITLPEEFHDFDQPLPDLDDIDVAQQFSLNQSRVEEITMREEVGNISILQENDFGDFGMDDREIMREGSAFEDDDMLVSTTTSNLLLESEQSTSNLNEKINHLEYEDQYKDDNFGEGNDGGILDDKLISNNDGGIFDDPPALSEAGVMLPEQPAHDDMDEDDNVSMGGPDSPDSVDPVEPMPTMTDQTTLVPNEEEAFALEPIDITVKETKAKR...
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 [G...
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 ma...
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,...
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}. Chr...
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 preven...
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 dehydr...
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: Reactio...
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 acr...
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 (PubMe...
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 me...
Homo sapiens (Human)
O60229
KALRN_HUMAN
MTDRFWDQWYLWYLRLLRLLDRGSFRNDGLKASDVLPILKEKVAFVSGGRDKRGGPILTFPARSNHDRIRQEDLRKLVTYLASVPSEDVCKRGFTVIIDMRGSKWDLIKPLLKTLQEAFPAEIHVALIIKPDNFWQKQKTNFGSSKFIFETSMVSVEGLTKLVDPSQLTEEFDGSLDYNHEEWIELRLSLEEFFNSAVHLLSRLEDLQEMLARKEFPVDVEGSRRLIDEHTQLKKKVLKAPVEELDREGQRLLQCIRCSDGFSGRNCIPGSADFQSLVPKITSLLDKLHSTRQHLHQMWHVRKLKLDQCFQLRLFEQDAE...
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-media...
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-[pr...
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:1002...
Homo sapiens (Human)
O60231
DHX16_HUMAN
MATPAGLERWVQDELHSVLGLSERHVAQFLIGTAQRCTSAEEFVQRLRDTDTLDLSGPARDFALRLWNKVPRKAVVEKPARAAEREARALLEKNRSYRLLEDSEESSEETVSRAGSSLQKKRKKRKHLRKKREEEEEEEASEKGKKKTGGSKQQTEKPESEDEWERTERERLQDLEERDAFAERVRQRDKDRTRNVLERSDKKAYEEAQKRLKMAEEDRKAMVPELRKKSRREYLAKREREKLEDLEAELADEEFLFGDVELSRHERQELKYKRRVRDLAREYRAAGEQEKLEATNRYHMPKETRGQPARAVDLVEEESG...
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 splici...
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
MYRPARVTSTSRFLNPYVVCFIVVAGVVILAVTIALLVYFLAFDQKSYFYRSSFQLLNVEYNSQLNSPATQEYRTLSGRIESLITKTFKESNLRNQFIRAHVAKLRQDGSGVRADVVMKFQFTRNNNGASMKSRIESVLRQMLNNSGNLEINPSTEITSLTDQAAANWLINECGAGPDLITLSEQRILGGTEAEEGSWPWQVSLRLNNAHHCGGSLINNMWILTAAHCFRSNSNPRDWIATSGISTTFPKLRMRVRNILIHNNYKSATHENDIALVRLENSVTFTKDIHSVCLPAATQNIPPGSTAYVTGWGAQEYAGHT...
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) sp...
Homo sapiens (Human)
O60237
MYPT2_HUMAN
MAELEHLGGKRAESARMRRAEQLRRWRGSLTEQEPAERRGAGRQPLTRRGSPRVRFEDGAVFLAACSSGDTDEVRKLLARGADINTVNVDGLTALHQACIDENLDMVKFLVENRANVNQQDNEGWTPLHAAASCGYLNIAEYFINHGASVGIVNSEGEVPSDLAEEPAMKDLLLEQVKKQGVDLEQSRKEEEQQMLQDARQWLNSGKIEDVRQARSGATALHVAAAKGYSEVLRLLIQAGYELNVQDYDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVADEGLVEHLELLQKKQNVLRSEKETRNKLIE...
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]...
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: ...
Homo sapiens (Human)
O60239
3BP5_HUMAN
MDAALKRSRSEEPAEILPPARDEEEEEEEGMEQGLEEEEEVDPRIQGELEKLNQSTDDINRRETELEDARQKFRSVLVEATVKLDELVKKIGKAVEDSKPYWEARRVARQAQLEAQKATQDFQRATEVLRAAKETISLAEQRLLEDDKRQFDSAWQEMLNHATQRVMEAEQTKTRSELVHKETAARYNAAMGRMRQLEKKLKRAINKSKPYFELKAKYYVQLEQLKKTVDDLQAKLTLAKGEYKMALKNLEMISDEIHERRRSSAMGPRGCGVGAEGSSTSVEDLPGSKPEPDAISVASEAFEDDSCSNFVSEDDSETQS...
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 apopto...
Homo sapiens (Human)
O60240
PLIN1_HUMAN
MAVNKGLTLLDGDLPEQENVLQRVLQLPVVSGTCECFQKTYTSTKEAHPLVASVCNAYEKGVQSASSLAAWSMEPVVRRLSTQFTAANELACRGLDHLEEKIPALQYPPEKIASELKDTISTRLRSARNSISVPIASTSDKVLGAALAGCELAWGVARDTAEFAANTRAGRLASGGADLALGSIEKVVEYLLPPDKEESAPAPGHQQAQKSPKAKPSLLSRVGALTNTLSRYTVQTMARALEQGHTVAMWIPGVVPLSSLAQWGASVAMQAVSRRRSEVRVPWLHSLAAAQEEDHEDQTDTEGEDTEEEEELETEENKFS...
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 direction...
Homo sapiens (Human)
O60241
AGRB2_HUMAN
MENTGWMGKGHRMTPACPLLLSVILSLRLATAFDPAPSACSALASGVLYGAFSLQDLFPTIASGCSWTLENPDPTKYSLYLRFNRQEQVCAHFAPRLLPLDHYLVNFTCLRPSPEEAVAQAESEVGRPEEEEAEAAAGLELCSGSGPFTFLHFDKNFVQLCLSAEPSEAPRLLAPAALAFRFVEVLLINNNNSSQFTCGVLCRWSEECGRAAGRACGFAQPGCSCPGEAGAGSTTTTSPGPPAAHTLSNALVPGGPAPPAEADLHSGSSNDLFTTEMRYGEEPEEEPKVKTQWPRSADEPGLYMAQTGDPAAEEWSPWSV...
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 s...
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 fragme...
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:00002...
Homo sapiens (Human)
O60242
AGRB3_HUMAN
MKAVRNLLIYIFSTYLLVMFGFNAAQDFWCSTLVKGVIYGSYSVSEMFPKNFTNCTWTLENPDPTKYSIYLKFSKKDLSCSNFSLLAYQFDHFSHEKIKDLLRKNHSIMQLCNSKNAFVFLQYDKNFIQIRRVFPTNFPGLQKKGEEDQKSFFEFLVLNKVSPSQFGCHVLCTWLESCLKSENGRTESCGIMYTKCTCPQHLGEWGIDDQSLILLNNVVLPLNEQTEGCLTQELQTTQVCNLTREAKRPPKEEFGMMGDHTIKSQRPRSVHEKRVPQEQADAAKFMAQTGESGVEEWSQWSTCSVTCGQGSQVRTRTCVS...
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 regu...
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
MRRRRAGGRTMVERASKFVLVVAGSVCFMLILYQYAGPGLSLGAPGGRAPPDDLDLFPTPDPHYEKKYYFPVRELERSLRFDMKGDDVIVFLHIQKTGGTTFGRHLVQNVRLEVPCDCRPGQKKCTCYRPNRRETWLFSRFSTGWSCGLHADWTELTNCVPGVLDRRDSAALRTPRKFYYITLLRDPVSRYLSEWRHVQRGATWKTSLHMCDGRTPTPEELPPCYEGTDWSGCTLQEFMDCPYNLANNRQVRMLADLSLVGCYNLSFIPEGKRAQLLLESAKKNLRGMAFFGLTEFQRKTQYLFERTFNLKFIRPFMQYN...
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:C...
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 develop...
Homo sapiens (Human)
O60244
MED14_HUMAN
MAPVQLENHQLVPPGGGGGGSGGPPSAPAPPPPGAAVAAAAAAAASPGYRLSTLIEFLLHRAYSELMVLTDLLPRKSDVERKIEIVQFASRTRQLFVRLLALVKWANNAGKVEKCAMISSFLDQQAILFVDTADRLASLARDALVHARLPSFAIPYAIDVLTTGSYPRLPTCIRDKIIPPDPITKIEKQATLHQLNQILRHRLVTTDLPPQLANLTVANGRVKFRVEGEFEATLTVMGDDPDVPWRLLKLEILVEDKETGDGRALVHSMQISFIHQLVQSRLFADEKPLQDMYNCLHSFCLSLQLEVLHSQTLMLIRERW...
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 tra...
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...
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 ...
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 re...
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 transcrip...
Homo sapiens (Human)
O60256
KPRB_HUMAN
MFCVTPPELETKMNITKGGLVLFSANSNSSCMELSKKIAERLGVEMGKVQVYQEPNRETRVQIQESVRGKDVFIIQTVSKDVNTTIMELLIMVYACKTSCAKSIIGVIPYFPYSKQCKMRKRGSIVSKLLASMMCKAGLTHLITMDLHQKEIQGFFNIPVDNLRASPFLLQYIQEEIPDYRNAVIVAKSPASAKRAQSFAERLRLGIAVIHGEAQDAESDLVDGRHSPPMVRSVAAIHPSLEIPMLIPKEKPPITVVGDVGGRIAIIVDDIIDDVDSFLAAAETLKERGAYKIFVMATHGLLSSDAPRRIEESAIDEVVV...
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 expressi...
cytoplasm [GO:0005737]; extracellular region [GO:0005576]; extracellular space [GO:0005615]
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}.
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]
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 f...
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 an...
Homo sapiens (Human)
O60260
PRKN_HUMAN
MIVFVRFNSSHGFPVEVDSDTSIFQLKEVVAKRQGVPADQLRVIFAGKELRNDWTVQNCDLDQQSIVHIVQRPWRKGQEMNATGGDDPRNAAGGCEREPQSLTRVDLSSSVLPGDSVGLAVILHTDSRKDSPPAGSPAGRSIYNSFYVYCKGPCQRVQPGKLRVQCSTCRQATLTLTQGPSCWDDVLIPNRMSGECQSPHCPGTSAEFFFKCGAHPTSDKETSVALHLIATNSRNITCITCTDVRSPVLVFQCNSRHVICLDCFHLYCVTRLNDRQFVHDPQLGYSLPCVAGCPNSLIKELHHFRILGEEQYNRYQQYGA...
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 t...
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:0016...
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 bin...
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 polyubi...
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|PubMe...
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:2239665...
Homo sapiens (Human)
O60264
SMCA5_HUMAN
MSSAAEPPPPPPPESAPSKPAASIASGGSNSSNKGGPEGVAAQAVASAASAGPADAEMEEIFDDASPGKQKEIQEPDPTYEEKMQTDRANRFEYLLKQTELFAHFIQPAAQKTPTSPLKMKPGRPRIKKDEKQNLLSVGDYRHRRTEQEEDEELLTESSKATNVCTRFEDSPSYVKWGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNWMSEFKRWVPTLRSVCLIGDKEQRAAFVRDVLLPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKL...
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 chr...
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...
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 bi...
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-loc...
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, tr...
Homo sapiens (Human)
O60266
ADCY3_HUMAN
MPRNQGFSEPEYSAEYSAEYSVSLPSDPDRGVGRTHEISVRNSGSCLCLPRFMRLTFVPESLENLYQTYFKRQRHETLLVLVVFAALFDCYVVVMCAVVFSSDKLASLAVAGIGLVLDIILFVLCKKGLLPDRVTRRVLPYVLWLLITAQIFSYLGLNFARAHAASDTVGWQVFFVFSFFITLPLSLSPIVIISVVSCVVHTLVLGVTVAQQQQEELKGMQLLREILANVFLYLCAIAVGIMSYYMADRKHRKAFLEARQSLEVKMNLEEQSQQQENLMLSILPKHVADEMLKDMKKDESQKDQQQFNTMYMYRHENVSI...
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:000...
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|UniP...
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. {EC...
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 rol...
Homo sapiens (Human)
O60269
GRIN2_HUMAN
MSSSRPEPGPWAPLSPRLQPLSQSSSSLLGEGREQRPELRKTASSTVWQAQLGEASTRPQAPEEEGNPPESMKPARASGPKARPSAGGHWWSSTVGNVSTMGGSDLCRLRAPSAAAMQRSHSDLVRSTQMRGHSGARKASLSCSALGSSPVHRAQLQPGGTSGQGGQAPAGLERDLAPEDETSNSAWMLGASQLSVPPLDLGDTTAHSSSAQAEPKAAEQLATTTCHALPPAALLCGMREVRAGGCCHALPATGILAFPKLVASVSESGLQAQHGVKIHCRLSGGLPGHSHCCAHLWGPAGLVPEPGSRTKDVWTMTSAN...
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
MELEDGVVYQEEPGGSGAVMSERVSGLAGSIYREFERLIGRYDEEVVKELMPLVVAVLENLDSVFAQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFEDSQEQEKKDLQTRVESLESQTRQLELKAKNYADQISRLEEREAELKKEYNALHQRHTEMIHNYMEHLERTKLHQLSGSDQLESTAHSRIRKERPISLGIFPLPAGDGLLTPDAQKGGETPGSEQWKFQELSQPRSHTSLKVSNSPEPQKAVEQEDELSDVSQGGSKATTPASTANSDVATIPTDTPLKEENEGFVKVTDAPNKSEISKHIEVQ...
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]; posit...
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...
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 lysoso...
Homo sapiens (Human)
O60281
ZN292_HUMAN
MADEEAEQERLSCGEGGCVAELQRLGERLQELELQLRESRVPAVEAATDYCQQLCQTLLEYAEKWKTSEDPLPLLEVYTVAIQSYVKARPYLTSECENVALVLERLALSCVELLLCLPVELSDKQWEQFQTLVQVAHEKLMENGSCELHFLATLAQETGVWKNPVLCTILSQEPLDKDKVNEFLAFEGPILLDMRIKHLIKTNQLSQATALAKLCSDHPEIGIKGSFKQTYLVCLCTSSPNGKLIEEISEVDCKDALEMICNLESEGDEKSALVLCTAFLSRQLQQGDMYCAWELTLFWSKLQQRVEPSIQVYLERCRQL...
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
MADPAECSIKVMCRFRPLNEAEILRGDKFIPKFKGDETVVIGQGKPYVFDRVLPPNTTQEQVYNACAKQIVKDVLEGYNGTIFAYGQTSSGKTHTMEGKLHDPQLMGIIPRIAHDIFDHIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLAVHEDKNRVPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIKQENVETEKKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTKTHVPYRDSKMTRILQDSLGGNCRTTIVICCSPSVFNEAETKSTLMF...
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:0000...
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 i...
Homo sapiens (Human)
O60284
ST18_HUMAN
MDAEAEDKTLRTRSKGTEVPMDSLIQELSVAYDCSMAKKRTAEDQALGVPVNKRKSLLMKPRHYSPKADCQEDRSDRTEDDGPLETHGHSTAEEIMIKPMDESLLSTAQENSSRKEDRYSCYQELMVKSLMHLGKFEKNVSVQTVSENLNDSGIQSLKAESDEADECFLIHSDDGRDKIDDSQPPFCSSDDNESNSESAENGWDSGSNFSEETKPPRVPKYVLTDHKKDLLEVPEIKTEGDKFIPCENRCDSETERKDPQNALAEPLDGNAQPSFPDVEEEDSESLAVMTEEGSDLEKAKGNLSLLEQAIALQAERGCVF...
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 transc...
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, ...
Homo sapiens (Human)
O60285
NUAK1_HUMAN
MEGAAAPVAGDRPDLGLGAPGSPREAVAGATAALEPRKPHGVKRHHHKHNLKHRYELQETLGKGTYGKVKRATERFSGRVVAIKSIRKDKIKDEQDMVHIRREIEIMSSLNHPHIISIYEVFENKDKIVIIMEYASKGELYDYISERRRLSERETRHFFRQIVSAVHYCHKNGVVHRDLKLENILLDDNCNIKIADFGLSNLYQKDKFLQTFCGSPLYASPEIVNGRPYRGPEVDSWALGVLLYTLVYGTMPFDGFDHKNLIRQISSGEYREPTQPSDARGLIRWMLMVNPDRRATIEDIANHWWVNWGYKSSVCDCDAL...
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-lig...
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 dephosphoryl...
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-[pr...
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 phosphor...
Homo sapiens (Human)
O60291
MGRN1_HUMAN
MGSILSRRIAGVEDIDIQANSAYRYPPKSGNYFASHFFMGGEKFDTPHPEGYLFGENMDLNFLGSRPVQFPYVTPAPHEPVKTLRSLVNIRKDSLRLVRYKDDADSPTEDGDKPRVLYSLEFTFDADARVAITIYCQASEEFLNGRAVYSPKSPSLQSETVHYKRGVSQQFSLPSFKIDFSEWKDDELNFDLDRGVFPVVIQAVVDEGDVVEVTGHAHVLLAAFEKHMDGSFSVKPLKQKQIVDRVSYLLQEIYGIENKNNQETKPSDDENSDNSNECVVCLSDLRDTLILPCRHLCLCTSCADTLRYQANNCPICRLPF...
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 polyubiquitinatio...
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 o...
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-induc...
Homo sapiens (Human)
O60292
SI1L3_HUMAN
MTTYRAIPSDGVDLAASCGARVGDVLPGPHTGDYAPLGFWAQNGSMSQPLGESPATATATATATTRPSPTTPAMPKMGVRARVADWPPKREALREHSNPSPSQDTDGTKATKMAHSMRSIQNGQPPTSTPASSGSKAFHRLSRRRSKDVEFQDGWPRSPGRAFLPLRHRSSSEITLSECDAEDAGEPRGARHTGALPLFREYGSTSSIDVQGMPEQSFFDILNEFRSEQPDARGCQALTELLRADPGPHLMGGGGGAKGDSHNGQPAKDSLLPLQPTKEKEKARKKPARGLGGGDTVDSSIFRKLRSSKPEGEAGRSPGE...
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
MATADTPAPASSGLSPKEEGELEDGEISDDDNNSQIRSRSSSSSSGGGLLPYPRRRPPHSARGGGSGGGGGSSSSSSSSQQQLRNFSRSRHASERGHLRGPSSYRPKEPFRSHPPSVRMPSSSLSESSPRPSFWERSHLALDRFRFRGRPYRGGSRWSRGRGVGERGGKPGCRPPLGGGAGSGFSSSQSWREPSPPRKSSKSFGRSPSRKQNYSSKNENCVEETFEDLLLKYKQIQLELECINKDEKLALSSKEENVQEDPKTLNFEDQTSTDNVSITKDSSKEVAPEEKTQVKTFQAFELKPLRQKLTLPGDKNRLKKV...
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, whi...
Homo sapiens (Human)
O60294
TYW4_HUMAN
MGPRSRERRAGAVQNTNDSSALSKRSLAARGYVQDPFAALLVPGAARRAPLIHRGYYVRARAVRHCVRAFLEQIGAPQAALRAQILSLGAGFDSLYFRLKTAGRLARAAVWEVDFPDVARRKAERIGETPELCALTGPFERGEPASALCFESADYCILGLDLRQLQRVEEALGAAGLDAASPTLLLAEAVLTYLEPESAAALIAWAAQRFPNALFVVYEQMRPQDAFGQFMLQHFRQLNSPLHGLERFPDVEAQRRRFLQAGWTACGAVDMNEFYHCFLPAEERRRVENIEPFDEFEEWHLKCAHYFILAASRGDTLSHT...
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:...
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 ca...
Homo sapiens (Human)
O60296
TRAK2_HUMAN
MSQSQNAIFTSPTGEENLMNSNHRDSESITDVCSNEDLPEVELVSLLEEQLPQYRLKVDTLFLYENQDWTQSPHQRQHASDALSPVLAEETFRYMILGTDRVEQMTKTYNDIDMVTHLLAERDRDLELAARIGQALLKRNHVLSEQNESLEEQLGQAFDQVNQLQHELCKKDELLRIVSIASEESETDSSCSTPLRFNESFSLSQGLLQLEMLQEKLKELEEENMALRSKACHIKTETVTYEEKEQQLVSDCVKELRETNAQMSRMTEELSGKSDELIRYQEELSSLLSQIVDLQHKLKEHVIEKEELKLHLQASKDAQR...
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
MDGQTLRKAERSWSCSREKKEGYAKDMVTDFDEKHDEYLILLQQRNRILKHLKSKDPVQLRLEHLEQGFSVYVNGANSELKSSPRKAIHSDFSRSASHTEGTHDYGRRTLFREAEEALRRSSRTAPSKVQRRGWHQKSVQIRTEAGPRLHIEPPVDYSDDFELCGDVTLQANNTSEDRPQELRRSLELSVNLQRKQKDCSSDEYDSIEEDILSEPEPEDPALVGHPRHDRPPSSGDWTQKDVHGEQETEGRSSPGPDTLVVLEFNPASKSHKRERNLSAKRKDNAEVFVPTKPEPNLTPQAPAVFPDQERMCSRPGSRRE...
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-tubu...
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
MATVPGLQPLPTLEQDLEQEEILIVKVEEDFCLEEEPSVETEDPSPETFRQLFRLFCYQEVAGPREALSRLWELCCRWLRPELRTKEQILELLVLEQFLTVLPGEIQARVREQQPESGEEAVVLVEGLQRKPRKHRQRGSELLSDDEVPLGIGGQFLKHQAEAQPEDLSLEEEARFSSQQPPAQLSHRPQRGPLLWPERGPPAPRHQEMASASPFLSAWSQVPVNLEDVAVYLSGEEPRCMDPAQRDAPLENEGPGIQLEDGGDGREDAPLRMEWYRVLSARCQGPGHPLPGQRPAPVRGLVRPDQPRGGPPPGRRASHG...
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
MAAPAQPKKIVAPTVSQINAEFVTQLACKYWAPHIKKKSPFDIKVIEDIYEKEIVKSRFAIRKIMLLEFSQYLENYLWMNYSPEVSSKAYLMSICCMVNEKFRENVPAWEIFKKKPDHFPFFFKHILKAALAETDGEFSLHEQTVLLLFLDHCFNSLEVDLIRSQVQQLISLPMWMGLQLARLELELKKTPKLRKFWNLIKKNDEKMDPEAREQAYQERRFLSQLIQKFISVLKSVPLSEPVTMDKVHYCERFIELMIDLEALLPTRRWFNTILDDSHLLVHCYLSNLVRREEDGHLFSQLLDMLKFYTGFEINDQTGNA...
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-d...
Homo sapiens (Human)
O60307
MAST3_HUMAN
MDESSLLRRRGLQKELSLPRRGRGCRSGNRKSLVVGTPSPTLSRPLSPLSVPTAGSSPLDSPRNFSAASALNFPFARRADGRRWSLASLPSSGYGTNTPSSTLSSSSSSRERLHQLPFQPTPDELHFLSKHFRSSENVLDEEGGRSPRLRPRSRSLSPGRATGTFDNEIVMMNHVYRERFPKATAQMEGRLQEFLTAYAPGARLALADGVLGFIHHQIVELARDCLAKSGENLVTSRYFLEMQEKLERLLQDAHERSDSEEVSFIVQLVRKLLIIISRPARLLECLEFDPEEFYHLLEAAEGHAREGQGIKTDLPQYIIG...
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-[pr...
null
null
null
null
null
Homo sapiens (Human)
O60308
CE104_HUMAN
MPHKIGFVVVSSSGHEDGFSARELMIHAPTVSGWRSPRFCQFPQEIVLQMVERCRIRKLQLLAHQYMISSKIEFYISESLPEYFAPYQAERFRRLGYVSLCDNEKTGCKARELKSVYVDAVGQFLKLIFHQNHVNKYNIYNQVALVAINIIGDPADFSDESNTASREKLIDHYLGHNSEDPALEGTYARKSDYISPLDDLAFDMYQDPEVAQIIRKLDERKREAVQKERYDYAKKLKQAIADLQKVGERLGRYEVEKRCAVEKEDYDLAKEKKQQMEQYRAEVYEQLELHSLLDAELMRRPFDLPLQPLARSGSPCHQKP...
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}. Cytopla...
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
MEREPAGTEEPGPPGRRRRREGRTRTVRSNLLPPPGAEDPAAGAAKGERRRRRGCAQHLADNRLKTTKYTLLSFLPKNLFEQFHRPANVYFVFIALLNFVPAVNAFQPGLALAPVLFILAITAFRDLWEDYSRHRSDHKINHLGCLVFSREEKKYVNRFWKEIHVGDFVRLRCNEIFPADILLLSSSDPDGLCHIETANLDGETNLKRRQVVRGFSELVSEFNPLTFTSVIECEKPNNDLSRFRGCIIHDNGKKAGLYKENLLLRGCTLRNTDAVVGIVIYAGHETKALLNNSGPRYKRSKLERQMNCDVLWCVLLLVCM...
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 requ...
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-glyc...
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...
Homo sapiens (Human)
O60313
OPA1_HUMAN
MWRLRRAAVACEVCQSLVKHSSGIKGSLPLQKLHLVSRSIYHSHHPTLKLQRPQLRTSFQQFSSLTNLPLRKLKFSPIKYGYQPRRNFWPARLATRLLKLRYLILGSAVGGGYTAKKTFDQWKDMIPDLSEYKWIVPDIVWEIDEYIDFEKIRKALPSSEDLVKLAPDFDKIVESLSLLKDFFTSGSPEETAFRATDRGSESDKHFRKVSDKEKIDQLQEELLHTQLKYQRILERLEKENKELRKLVLQKDDKGIHHRKLKKSLIDMYSEVLDVLSDYDASYNTQDHLPRVVVVGDQSAGKTSVLEMIAQARIFPRGSGE...
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]; mitochond...
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]; mitochondr...
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...
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=Detec...
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, ...
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,...
Homo sapiens (Human)
O60315
ZEB2_HUMAN
MKQPIMADGPRCKRRKQANPRRKNVVNYDNVVDTGSETDEEDKLHIAEDDGIANPLDQETSPASVPNHESSPHVSQALLPREEEEDEIREGGVEHPWHNNEILQASVDGPEEMKEDYDTMGPEATIQTAINNGTVKNANCTSDFEEYFAKRKLEERDGHAVSIEEYLQRSDTAIIYPEAPEELSRLGTPEANGQEENDLPPGTPDAFAQLLTCPYCDRGYKRLTSLKEHIKYRHEKNEENFSCPLCSYTFAYRTQLERHMVTHKPGTDQHQMLTQGAGNRKFKCTECGKAFKYKHHLKEHLRIHSGEKPYECPNCKKRFS...
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...
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 [G...
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
MNPTNPFSGQQPSAFSASSSNVGTLPSKPPFRFGQPSLFGQNSTLSGKSSGFSQVSSFPASSGVSHSSSVQTLGFTQTSSVGPFSGLEHTSTFVATSGPSSSSVLGNTGFSFKSPTSVGAFPSTSAFGQEAGEIVNSGFGKTEFSFKPLENAVFKPILGAESEPEKTQSQIASGFFTFSHPISSAPGGLAPFSFPQVTSSSATTSNFTFSKPVSSNNSLSAFTPALSNQNVEEEKRGPKSIFGSSNNSFSSFPVSSAVLGEPFQASKAGVRQGCEEAVSQVEPLPSLMKGLKRKEDQDRSPRRHGHEPAEDSDPLSRGDH...
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:00...
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}; P...
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 gene...
Homo sapiens (Human)
O60331
PI51C_HUMAN
MELEVPDEAESAEAGAVPSEAAWAAESGAAAGLAQKKAAPTEVLSMTAQPGPGHGKKLGHRGVDASGETTYKKTTSSTLKGAIQLGIGYTVGHLSSKPERDVLMQDFYVVESIFFPSEGSNLTPAHHFQDFRFKTYAPVAFRYFRELFGIRPDDYLYSLCNEPLIELSNPGASGSLFYVTSDDEFIIKTVMHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQSGGKNIRVVVMNNILPRVVKMHLKFDLKGSTYKRRASKKEKEKSFPTYKDLDFMQDMPEGLLLDADTFSALVKTLQRDCLVLESFKIMDYSLL...
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]; ...
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 ...
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|PubM...
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; Evide...
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:2294227...
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 adhesio...
Homo sapiens (Human)
O60333
KIF1B_HUMAN
MSGASVKVAVRVRPFNSRETSKESKCIIQMQGNSTSIINPKNPKEAPKSFSFDYSYWSHTSPEDPCFASQNRVYNDIGKEMLLHAFEGYNVCIFAYGQTGAGKSYTMMGKQEESQAGIIPQLCEELFEKINDNCNEEMSYSVEVSYMEIYCERVRDLLNPKNKGNLRVREHPLLGPYVEDLSKLAVTSYTDIADLMDAGNKARTVAATNMNETSSRSHAVFTIVFTQKKHDNETNLSTEKVSKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEVDNCTSKSKKKKKTDFIPYRDSVLTWLLRENLG...
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 ve...
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
MAVEGSTITSRIKNLLRSPSIKLRRSKAGNRREDLSSKVTLEKVLGITVSGGRGLACDPRSGLVAYPAGCVVVLFNPRKHKQHHILNSSRKTITALAFSPDGKYLVTGESGHMPAVRVWDVAEHSQVAELQEHKYGVACVAFSPSAKYIVSVGYQHDMIVNVWAWKKNIVVASNKVSSRVTAVSFSEDCSYFVTAGNRHIKFWYLDDSKTSKVNATVPLLGRSGLLGELRNNLFTDVACGRGKKADSTFCITSSGLLCEFSDRRLLDKWVELRNIDSFTTTVAHCISVSQDYIFCGCADGTVRLFNPSNLHFLSTLPRPH...
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 ...
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
MDTAEEDICRVCRSEGTPEKPLYHPCVCTGSIKFIHQECLVQWLKHSRKEYCELCKHRFAFTPIYSPDMPSRLPIQDIFAGLVTSIGTAIRYWFHYTLVAFAWLGVVPLTACRIYKCLFTGSVSSLLTLPLDMLSTENLLADCLQGCFVVTCTLCAFISLVWLREQIVHGGAPIWLEHAAPPFNAAGHHQNEAPAGGNGAENVAADQPANPPAENAVVGENPDAQDDQAEEEEEDNEEEDDAGVEDAADANNGAQDDMNWNALEWDRAAEELTWERMLGLDGSLVFLEHVFWVVSLNTLFILVFAFCPYHIGHFSLVGLG...
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)....
Homo sapiens (Human)
O60341
KDM1A_HUMAN
MLSGKKAAAAAAAAAAAATGTEAGPGTAGGSENGSEVAAQPAGLSGPAEVGPGAVGERTPRKKEPPRASPPGGLAEPPGSAGPQAGPTVVPGSATPMETGIAETPEGRRTSRRKRAKVEYREMDESLANLSEDEYYSEEERNAKAEKEKKLPPPPPQAPPEEENESEPEEPSGVEGAAFQSRLPHDRMTSQEAACFPDIISGPQQTQKVFLFIRNRTLQLWLDNPKIQLTFEATLQQLEAPYNSDTVLVHRVHSYLERHGLINFGIYKRIKPLPTKKTGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATF...
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 regula...
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...
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:27292...
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:000026...
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...
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 oxidizi...
Homo sapiens (Human)
O60343
TBCD4_HUMAN
MEPPSCIQDEPFPHPLEPEPGVSAQPGPGKPSDKRFRLWYVGGSCLDHRTTLPMLPWLMAEIRRRSQKPEAGGCGAPAAREVILVLSAPFLRCVPAPGAGASGGTSPSATQPNPAVFIFEHKAQHISRFIHNSHDLTYFAYLIKAQPDDPESQMACHVFRATDPSQVPDVISSIRQLSKAAMKEDAKPSKDNEDAFYNSQKFEVLYCGKVTVTHKKAPSSLIDDCMEKFSLHEQQRLKIQGEQRGPDPGEDLADLEVVVPGSPGDCLPEEADGTDTHLGLPAGASQPALTSSRVCFPERILEDSGFDEQQEFRSRCSSVT...
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 ...
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
MEPAAAATVQRLPELGREDRASAPAAAAAAAAAAAAAAAALAAAAGGGRSPEPALTPAAPSGGNGSGSGAREEAPGEAPPGPLPGRAGGAGRRRRRGAPQPIAGGAAPVPGAGGGANSLLLRRGRLKRNLSAAAAAASSSSSSSAAAASHSPGAAGLPASCSASASLCTRSLDRKTLLLKHRQTLQLQPSDRDWVRHQLQRGCVHVFDRHMASTYLRPVLCTLDTTAGEVAARLLQLGHKGGGVVKVLGQGPGAAAAREPAEPPPEAGPRLAPPEPRDSEVPPARSAPGAFGGPPRAPPADLPLPVGGPGGWSRRASPAP...
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 o...
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}; C...
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:17...
Homo sapiens (Human)
O60353
FZD6_HUMAN
MEMFTFLLTCIFLPLLRGHSLFTCEPITVPRCMKMAYNMTFFPNLMGHYDQSIAAVEMEHFLPLANLECSPNIETFLCKAFVPTCIEQIHVVPPCRKLCEKVYSDCKKLIDTFGIRWPEELECDRLQYCDETVPVTFDPHTEFLGPQKKTEQVQRDIGFWCPRHLKTSGGQGYKFLGIDQCAPPCPNMYFKSDELEFAKSFIGTVSIFCLCATLFTFLTFLIDVRRFRYPERPIIYYSVCYSIVSLMYFIGFLLGDSTACNKADEKLELGDTVVLGSQNKACTVLFMLLYFFTMAGTVWWVILTITWFLAAGRKWSCEAI...
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]; negat...
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 ves...
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...
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]; nega...
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:11...
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, glut...
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 com...
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 s...
Homo sapiens (Human)
O60381
HBP1_HUMAN
MVWEVKTNQMPNAVQKLLLVMDKRASGMNDSLELLQCNENLPSSPGYNSCDEHMELDDLPELQAVQSDPTQSGMYQLSSDVSHQEYPRSSWNQNTSDIPETTYRENEVDWLTELANIATSPQSPLMQCSFYNRSSPVHIIATSKSLHSYARPPPVSSSSKSEPAFPHHHWKEETPVRHERANSESESGIFCMSSLSDDDDLGWCNSWPSTVWHCFLKGTRLCFHKGSNKEWQDVEDFARAEGCDNEEDLQMGIHKGYGSDGLKLLSHEESVSFGESVLKLTFDPGTVEDGLLTVECKLDHPFYVKNKGWSSFYPSLTVVQ...
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 betw...
Homo sapiens (Human)
O60383
GDF9_HUMAN
MARPNKFLLWFCCFAWLCFPISLGSQASGGEAQIAASAELESGAMPWSLLQHIDERDRAGLLPALFKVLSVGRGGSPRLQPDSRALHYMKKLYKTYATKEGIPKSNRSHLYNTVRLFTPCTRHKQAPGDQVTGILPSVELLFNLDRITTVEHLLKSVLLYNINNSVSFSSAVKCVCNLMIKEPKSSSRTLGRAPYSFTFNSQFEFGKKHKWIQIDVTSLLQPLVASNKRSIHMSINFTCMKDQLEHPSAQNGLFNMTLVSPSLILYLNDTSAQAYHSWYSLHYKRRPSQGPDQERSLSAYPVGEEAAEDGRSSHHRHRRG...
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 proges...
Homo sapiens (Human)
O60391
NMD3B_HUMAN
MEFVRALWLGLALALGPGSAGGHPQPCGVLARLGGSVRLGALLPRAPLARARARAALARAALAPRLPHNLSLELVVAAPPARDPASLTRGLCQALVPPGVAALLAFPEARPELLQLHFLAAATETPVLSLLRREARAPLGAPNPFHLQLHWASPLETLLDVLVAVLQAHAWEDVGLALCRTQDPGGLVALWTSRAGRPPQLVLDLSRRDTGDAGLRARLAPMAAPVGGEAPVPAAVLLGCDIARARRVLEAVPPGPHWLLGTPLPPKALPTAGLPPGLLALGEVARPPLEAAIHDIVQLVARALGSAAQVQPKRALLPAP...
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:00305...
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
MALLLTLTSPDLEGTWDTRDKDGFKAQEGPPLAVPEFPVCGLYRIYGVCGSFSSFFIIRCSLCALETLKSPQHDPLEIPEQSLKLIPLVSGKRELTRGQKAGEKPLAAGPGEEELLRGSAPHAQDTQSEELPPSCTISGEKKPPAVSGEATGADAGRLCPPPRSRAPHKDRTLARSRPQTQGEDCSLPVGEVKIGKRSYSPAPGKQKKPNAMGLAPTSSPGAPNSARATHNPVPCGSGRGPCHLANLLSTLAQSNQNRDHKQGPPEVTCQIRKKTRTLYRSDQLEELEKIFQEDHYPDSDKRREIAQTVGVTPQRIMVKG...
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
MGTGPAQTPRSTRAGPEPSPAPPGPGDTGDSDVTQEGSGPAGIRGGETVIRAGMGDSPGRGAPERRHKAQPGRARKYEWRPEGPTSMGSLGQREDLQDEDRNSAFTWKVQANNRAYNGQFKEKVILCWQRKKYKTNVIRTAKYNFYSFLPLNLYEQFHRVSNLFFLIIIILQSIPDISTLPWFSLSTPMVCLLFIRATRDLVDDMGRHKSDRAINNRPCQILMGKSFKQKKWQDLCVGDVVCLRKDNIVPADMLLLASTEPSSLCYVETVDIDGETNLKFRQALMVTHKELATIKKMASFQGTVTCEAPNSRMHHFVGCL...
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; Xr...
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 ...
Homo sapiens (Human)
O60427
FADS1_HUMAN
MAPDPVAAETAAQGPTPRYFTWDEVAQRSGCEERWLVIDRKVYNISEFTRRHPGGSRVISHYAGQDATDPFVAFHINKGLVKKYMNSLLIGELSPEQPSFEPTKNKELTDEFRELRATVERMGLMKANHVFFLLYLLHILLLDGAAWLTLWVFGTSFLPFLLCAVLLSAVQAQAGWLQHDFGHLSVFSTSKWNHLLHHFVIGHLKGAPASWWNHMHFQHHAKPNCFRKDPDINMHPFFFALGKILSVELGKQKKKYMPYNHQHKYFFLIGPPALLPLYFQWYIFYFVIQRKKWVDLAWMITFYVRFFLTYVPLLGLKAFL...
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]; p...
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 r...
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 membran...
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, ...
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 fat...
Homo sapiens (Human)
O60437
PEPL_HUMAN
MNSLFRKRNKGKYSPTVQTRSISNKELSELIEQLQKNADQVEKNIVDTEAKMQSDLARLQEGRQPEHRDVTLQKVLDSEKLLYVLEADAAIAKHMKHPQGDMIAEDIRQLKERVTNLRGKHKQIYRLAVKEVDPQVNWAALVEEKLDKLNNQSFGTDLPLVDHQVEEHNIFHNEVKAIGPHLAKDGDKEQNSELRAKYQKLLAASQARQQHLSSLQDYMQRCTNELYWLDQQAKGRMQYDWSDRNLDYPSRRRQYENFINRNLEAKEERINKLHSEGDQLLAAEHPGRNSIEAHMEAVHADWKEYLNLLICEESHLKYME...
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
MFAKATRNFLREVDADGDLIAVSNLNDSDKLQLLSLVTKKKRFWCWQRPKYQFLSLTLGDVLIEDQFPSPVVVESDFVKYEGKFANHVSGTLETALGKVKLNLGGSSRVESQSSFGTLRKQEVDLQQLIRDSAERTINLRNPVLQQVLEGRNEVLCVLTQKITTMQKCVISEHMQVEEKCGGIVGIQTKTVQVSATEDGNVTKDSNVVLEIPAATTIAYGVIELYVKLDGQFEFCLLRGKQGGFENKKRIDSVYLDPLVFREFAFIDMPDAAHGISSQDGPLSVLKQATLLLERNFHPFAELPEPQQTALSDIFQAVLFD...
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 in...
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 Kr...
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 (Gasde...
Homo sapiens (Human)
O60447
EVI5_HUMAN
MVTNKMTAAFRNPSGKQVATDKVAEKLSSTLSWVKNTVSHTVSQMASQVASPSTSLHTTSSSTTLSTPALSPSSPSQLSPDDLELLAKLEEQNRLLETDSKSLRSVNGSRRNSGSSLVSSSSASSNLSHLEEDSWILWGRIVNEWEDVRKKKEKQVKELVHKGIPHHFRAIVWQLLCSAQSMPIKDQYSELLKMTSPCEKLIRRDIARTYPEHNFFKEKDSLGQEVLFNVMKAYSLVDREVGYCQGSAFIVGLLLMQMPEEEAFCVFVKLMQDYRLRELFKPSMAELGLCMYQFECMIQEHLPELFVHFQSQSFHTSMYA...
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
MRTGWATPRRPAGLLMLLFWFFDLAEPSGRAANDPFTIVHGNTGKCIKPVYGWIVADDCDETEDKLWKWVSQHRLFHLHSQKCLGLDITKSVNELRMFSCDSSAMLWWKCEHHSLYGAARYRLALKDGHGTAISNASDVWKKGGSEESLCDQPYHEIYTRDGNSYGRPCEFPFLIDGTWHHDCILDEDHSGPWCATTLNYEYDRKWGICLKPENGCEDNWEKNEQFGSCYQFNTQTALSWKEAYVSCQNQGADLLSINSAAELTYLKEKEGIAKIFWIGLNQLYSARGWEWSDHKPLNFLNWDPDRPSAPTIGGSSCARM...
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
MDMFPLTWVFLALYFSRHQVRGQPDPPCGGRLNSKDAGYITSPGYPQDYPSHQNCEWIVYAPEPNQKIVLNFNPHFEIEKHDCKYDFIEIRDGDSESADLLGKHCGNIAPPTIISSGSMLYIKFTSDYARQGAGFSLRYEIFKTGSEDCSKNFTSPNGTIESPGFPEKYPHNLDCTFTILAKPKMEIILQFLIFDLEHDPLQVGEGDCKYDWLDIWDGIPHVGPLIGKYCGTKTPSELRSSTGILSLTFHTDMAVAKDGFSARYYLVHQEPLENFQCNVPLGMESGRIANEQISASSTYSDGRWTPQQSRLHGDDNGWTP...
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 structura...
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
MWILALSLFQSFANVFSEDLHSSLYFVNASLQEVVFASTTGTLVPCPAAGIPPVTLRWYLATGEEIYDVPGIRHVHPNGTLQIFPFPPSSFSTLIHDNTYYCTAENPSGKIRSQDVHIKAVLREPYTVRVEDQKTMRGNVAVFKCIIPSSVEAYITVVSWEKDTVSLVSGSRFLITSTGALYIKDVQNEDGLYNYRCITRHRYTGETRQSNSARLFVSDPANSAPSILDGFDHRKAMAGQRVELPCKALGHPEPDYRWLKDNMPLELSGRFQKTVTGLLIENIRPSDSGSYVCEVSNRYGTAKVIGRLYVKQPLKATISP...
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...
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:Q...
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 arbori...
Homo sapiens (Human)
O60476
MA1A2_HUMAN
MTTPALLPLSGRRIPPLNLGPPSFPHHRATLRLSEKFILLLILSAFITLCFGAFFFLPDSSKHKRFDLGLEDVLIPHVDAGKGAKNPGVFLIHGPDEHRHREEEERLRNKIRADHEKALEEAKEKLRKSREEIRAEIQTEKNKVVQEMKIKENKPLPPVPIPNLVGIRGGDPEDNDIREKREKIKEMMKHAWDNYRTYGWGHNELRPIARKGHSPNIFGSSQMGATIVDALDTLYIMGLHDEFLDGQRWIEDNLDFSVNSEVSVFEVNIRFIGGLLAAYYLSGEEIFKIKAVQLAEKLLPAFNTPTGIPWAMVNLKSGVG...
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...
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
MNWRFVELLYFLFIWGRISVQPSHQEPAGTDQHVSKEFDWLISDRGPFHHSRSYLSFVERHRQGFTTRYKIYREFARWKVRNTAIERRDLVRHPVPLMPEFQRSIRLLGRRPTTQQFIDTIIKKYGTHLLISATLGGEEALTMYMDKSRLDRKSGNATQSVEALHQLASSYFVDRDGTMRRLHEIQISTGAIKVTETRTGPLGCNSYDNLDSVSSVLLQSTESKLHLQGLQIIFPQYLQEKFVQSALSYIMCNGEGEYLCQNSQCRCQCAEEFPQCNCPITDIQIMEYTLANMAKSWAEAYKDLENSDEFKSFMKRLPSN...
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]; nega...
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
MRPERPRPRGSAPGPMETPPWDPARNDSLPPTLTPAVPPYVKLGLTVVYTVFYALLFVFIYVQLWLVLRYRHKRLSYQSVFLFLCLFWASLRTVLFSFYFKDFVAANSLSPFVFWLLYCFPVCLQFFTLTLMNLYFTQVIFKAKSKYSPELLKYRLPLYLASLFISLVFLLVNLTCAVLVKTGNWERKVIVSVRVAINDTLFVLCAVSLSICLYKISKMSLANIYLESKGSSVCQVTAIGVTVILLYTSRACYNLFILSFSQNKSVHSFDYDWYNVSDQADLKNQLGDAGYVLFGVVLFVWELLPTTLVVYFFRVRNPTK...
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 GTPa...
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 GTPase...
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]; odontob...
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 re...
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
MTMLLDGGPQFPGLGVGSFGAPRHHEMPNREPAGMGLNPFGDSTHAAAAAAAAAAFKLSPAAAHDLSSGQSSAFTPQGSGYANALGHHHHHHHHHHHTSQVPSYGGAASAAFNSTREFLFRQRSSGLSEAASGGGQHGLFAGSASSLHAPAGIPEPPSYLLFPGLHEQGAGHPSPTGHVDNNQVHLGLRGELFGRADPYRPVASPRTDPYAAGAQFPNYSPMNMNMGVNVAAHHGPGAFFRYMRQPIKQELSCKWIDEAQLSRPKKSCDRTFSTMHELVTHVTMEHVGGPEQNNHVCYWEECPREGKSFKAKYKLVNHIR...
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]; determi...
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...
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
MEVSRRKAPPRPPRPAAPLPLLAYLLALAAPGRGADEPVWRSEQAIGAIAASQEDGVFVASGSCLDQLDYSLEHSLSRLYRDQAGNCTEPVSLAPPARPRPGSSFSKLLLPYREGAAGLGGLLLTGWTFDRGACEVRPLGNLSRNSLRNGTEVVSCHPQGSTAGVVYRAGRNNRWYLAVAATYVLPEPETASRCNPAASDHDTAIALKDTEGRSLATQELGRLKLCEGAGSLHFVDAFLWNGSIYFPYYPYNYTSGAATGWPSMARIAQSTEVLFQGQASLDCGHGHPDGRRLLLSSSLVEALDVWAGVFSAAAGEGQER...
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...
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)