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
O15353
FOXN1_HUMAN
MVSLPPPQSDVTLPGPTRLEGERQGDLMQAPGLPGSPAPQSKHAGFSCSSFVSDGPPERTPSLPPHSPRIASPGPEQVQGHCPAGPGPGPFRLSPSDKYPGFGFEEAAASSPGRFLKGSHAPFHPYKRPFHEDVFPEAETTLALKGHSFKTPGPLEAFEEIPVDVAEAEAFLPGFSAEAWCNGLPYPSQEHGPQVLGSEVKVKPPVLESGAGMFCYQPPLQHMYCSSQPPFHQYSPGGGSYPIPYLGSSHYQYQRMAPQASTDGHQPLFPKPIYSYSILIFMALKNSKTGSLPVSEIYNFMTEHFPYFKTAPDGWKNSVR...
null
null
animal organ morphogenesis [GO:0009887]; blood vessel morphogenesis [GO:0048514]; defense response [GO:0006952]; epidermis development [GO:0008544]; hair follicle development [GO:0001942]; keratinocyte differentiation [GO:0030216]; lymphoid lineage cell migration into thymus [GO:0097535]; nail development [GO:0035878];...
chromatin [GO:0000785]; 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]; transcription cis-regulatory region binding [GO:0000976]
PF00250;
1.10.10.10;
null
null
SUBCELLULAR LOCATION: Nucleus.
null
null
null
null
null
FUNCTION: Transcriptional regulator which regulates the development, differentiation, and function of thymic epithelial cells (TECs) both in the prenatal and postnatal thymus. Acts as a master regulator of the TECs lineage development and is required from the onset of differentiation in progenitor TECs in the developin...
Homo sapiens (Human)
O15354
GPR37_HUMAN
MRAPGALLARMSRLLLLLLLKVSASSALGVAPASRNETCLGESCAPTVIQRRGRDAWGPGNSARDVLRARAPREEQGAAFLAGPSWDLPAAPGRDPAAGRGAEASAAGPPGPPTRPPGPWRWKGARGQEPSETLGRGNPTALQLFLQISEEEEKGPRGAGISGRSQEQSVKTVPGASDLFYWPRRAGKLQGSHHKPLSKTANGLAGHEGWTIALPGRALAQNGSLGEGIHEPGGPRRGNSTNRRVRLKNPFYPLTQESYGAYAVMCLSVVIFGTGIIGNLAVMCIVCHNYYMRSISNSLLANLAFWDFLIIFFCLPLVIF...
null
null
adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway [GO:0007193]; cellular response to reactive oxygen species [GO:0034614]; dendrite development [GO:0016358]; dopamine biosynthetic process [GO:0042416]; G protein-coupled receptor signaling pathway [GO:0007186]; locomotion involved in locomotory b...
cell surface [GO:0009986]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]; synapse [GO:0045202]; ubiquitin ligase complex [GO:0000151]
G protein-coupled peptide receptor activity [GO:0008528]; G protein-coupled receptor activity [GO:0004930]; heat shock protein binding [GO:0031072]; Hsp70 protein binding [GO:0030544]; neuropeptide binding [GO:0042923]; neuropeptide receptor activity [GO:0008188]; PDZ domain binding [GO:0030165]; peptide binding [GO:00...
PF00001;
1.20.1070.10;
G-protein coupled receptor 1 family
PTM: The N-terminus is cleaved by ADAM10 metalloproteinase; mediating limited proteolysis leading to the release of receptor ectodomain by shedding (PubMed:26869225, PubMed:34042202). In addition, cleaved by FURIN between Arg-54 and Asp-55 (PubMed:34042202). {ECO:0000269|PubMed:26869225, ECO:0000269|PubMed:34042202}.; ...
SUBCELLULAR LOCATION: Cell projection, dendrite {ECO:0000269|PubMed:25977097}. Synapse {ECO:0000269|PubMed:25977097}. Cell membrane {ECO:0000269|PubMed:17059562, ECO:0000269|PubMed:25977097, ECO:0000269|PubMed:26869225}; Multi-pass membrane protein {ECO:0000269|PubMed:17059562}. Endoplasmic reticulum membrane {ECO:0000...
null
null
null
null
null
FUNCTION: G-protein-coupled receptor that plays a role in several physiological pathways such as resolution of inflammatory pain and oligodendrocyte differentiation (By similarity). Acts as a receptor for several ligands including prosaposin, osteocalcin or neuroprotectin D1. Ligand binding induces endocytosis, followe...
Homo sapiens (Human)
O15355
PPM1G_HUMAN
MGAYLSQPNTVKCSGDGVGAPRLPLPYGFSAMQGWRVSMEDAHNCIPELDSETAMFSVYDGHGGEEVALYCAKYLPDIIKDQKAYKEGKLQKALEDAFLAIDAKLTTEEVIKELAQIAGRPTEDEDEKEKVADEDDVDNEEAALLHEEATMTIEELLTRYGQNCHKGPPHSKSGGGTGEEPGSQGLNGEAGPEDSTRETPSQENGPTAKAYTGFSSNSERGTEAGQVGEPGIPTGEAGPSCSSASDKLPRVAKSKFFEDSEDESDEAEEEEEDSEECSEEEDGYSSEEAENEEDEDDTEEAEEDDEEEEEEMMVPGMEGK...
3.1.3.16
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000250};
peptidyl-threonine dephosphorylation [GO:0035970]; protein dephosphorylation [GO:0006470]; regulation of cell cycle [GO:0051726]
cytoplasm [GO:0005737]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
metal ion binding [GO:0046872]; myosin phosphatase activity [GO:0017018]; protein serine/threonine phosphatase activity [GO:0004722]
PF00481;
3.60.40.10;
PP2C family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.
CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-...
null
null
null
null
null
Homo sapiens (Human)
O15357
SHIP2_HUMAN
MASACGAPGPGGALGSQAPSWYHRDLSRAAAEELLARAGRDGSFLVRDSESVAGAFALCVLYQKHVHTYRILPDGEDFLAVQTSQGVPVRRFQTLGELIGLYAQPNQGLVCALLLPVEGEREPDPPDDRDASDGEDEKPPLPPRSGSTSISAPTGPSSPLPAPETPTAPAAESAPNGLSTVSHDYLKGSYGLDLEAVRGGASHLPHLTRTLATSCRRLHSEVDKVLSGLEILSKVFDQQSSPMVTRLLQQQNLPQTGEQELESLVLKLSVLKDFLSGIQKKALKALQDMSSTAPPAPQPSTRKAKTIPVQAFEVKLDVTL...
3.1.3.86
null
actin filament organization [GO:0007015]; apoptotic process [GO:0006915]; cell adhesion [GO:0007155]; endochondral ossification [GO:0001958]; endocytosis [GO:0006897]; ERK1 and ERK2 cascade [GO:0070371]; establishment of mitotic spindle orientation [GO:0000132]; gene expression [GO:0010467]; glucose metabolic process [...
basal plasma membrane [GO:0009925]; cytosol [GO:0005829]; filopodium [GO:0030175]; Golgi apparatus [GO:0005794]; lamellipodium [GO:0030027]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; spindle pole [GO:0000922]
actin binding [GO:0003779]; inositol-polyphosphate 5-phosphatase activity [GO:0004445]; phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity [GO:0034485]; SH2 domain binding [GO:0042169]; SH3 domain binding [GO:0017124]
PF00536;PF00017;
3.60.10.10;3.30.505.10;1.10.150.50;
Inositol 1,4,5-trisphosphate 5-phosphatase family
PTM: Tyrosine phosphorylated by the members of the SRC family after exposure to a diverse array of extracellular stimuli such as insulin, growth factors such as EGF or PDGF, chemokines, integrin ligands and hypertonic and oxidative stress. May be phosphorylated upon IgG receptor FCGR2B-binding. Phosphorylated at Tyr-98...
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:11349134}. Cytoplasm, cytoskeleton. Membrane {ECO:0000269|PubMed:11739414}; Peripheral membrane protein. Cell projection, filopodium {ECO:0000269|PubMed:12676785}. Cell projection, lamellipodium {ECO:0000269|PubMed:12676785}. Basal cell membrane {ECO:0000250|...
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-trisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4-bisphosphate) + phosphate; Xref=Rhea:RHEA:25528, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57658, ChEBI:CHEBI:57836; EC=3.1.3.86; Evidence={ECO:0000...
null
null
null
null
FUNCTION: Phosphatidylinositol (PtdIns) phosphatase that specifically hydrolyzes the 5-phosphate of phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3) to produce PtdIns(3,4)P2, thereby negatively regulating the PI3K (phosphoinositide 3-kinase) pathways (PubMed:16824732). Required for correct mitotic spindle ori...
Homo sapiens (Human)
O15360
FANCA_HUMAN
MSDSWVPNSASGQDPGGRRRAWAELLAGRVKREKYNPERAQKLKESAVRLLRSHQDLNALLLEVEGPLCKKLSLSKVIDCDSSEAYANHSSSFIGSALQDQASRLGVPVGILSAGMVASSVGQICTAPAETSHPVLLTVEQRKKLSSLLEFAQYLLAHSMFSRLSFCQELWKIQSSLLLEAVWHLHVQGIVSLQELLESHPDMHAVGSWLFRNLCCLCEQMEASCQHADVARAMLSDFVQMFVLRGFQKNSDLRRTVEPEKMPQVTVDVLQRMLIFALDALAAGVQEESSTHKIVRCWFGVFSGHTLGSVISTDPLKRFF...
null
null
DNA repair [GO:0006281]; female gonad development [GO:0008585]; interstrand cross-link repair [GO:0036297]; male gonad development [GO:0008584]; male meiotic nuclear division [GO:0007140]; protein-containing complex assembly [GO:0065003]; regulation of CD40 signaling pathway [GO:2000348]; regulation of germ cell prolif...
chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; Fanconi anaemia nuclear complex [GO:0043240]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
null
PF03511;PF15865;
null
null
PTM: Phosphorylation is required for the formation of the nuclear complex. Not phosphorylated in cells derived from groups A, B, C, E, F, G, and H. {ECO:0000269|PubMed:9789045}.
SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=The major form is nuclear. The minor form is cytoplasmic.
null
null
null
null
null
FUNCTION: DNA repair protein that may operate in a postreplication repair or a cell cycle checkpoint function. May be involved in interstrand DNA cross-link repair and in the maintenance of normal chromosome stability.
Homo sapiens (Human)
O15370
SOX12_HUMAN
MVQQRGARAKRDGGPPPPGPGPAEEGAREPGWCKTPSGHIKRPMNAFMVWSQHERRKIMDQWPDMHNAEISKRLGRRWQLLQDSEKIPFVREAERLRLKHMADYPDYKYRPRKKSKGAPAKARPRPPGGSGGGSRLKPGPQLPGRGGRRAAGGPLGGGAAAPEDDDEDDDEELLEVRLVETPGRELWRMVPAGRAARGQAERAQGPSGEGAAAAAAASPTPSEDEEPEEEEEEAAAAEEGEEETVASGEESLGFLSRLPPGPAGLDCSALDRDPDLQPPSGTSHFEFPDYCTPEVTEMIAGDWRPSSIADLVFTY
null
null
anatomical structure morphogenesis [GO:0009653]; brain development [GO:0007420]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neuron differentiation [GO:0030182]; positive regulation of regulatory T cell differentiation [GO:0045591]; positive regulation of transcription by RNA polymerase II [...
chromatin [GO:0000785]; nucleoplasm [GO:0005654]; 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]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific double-stranded DNA b...
PF00505;
1.10.30.10;
null
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267, ECO:0000269|PubMed:9215677}.
null
null
null
null
null
FUNCTION: Transcription factor that binds to DNA at the consensus sequence 5'-ACCAAAG-3' (By similarity). Acts as a transcriptional activator (By similarity). Binds cooperatively with POU3F2/BRN2 or POU3F1/OCT6 to gene promoters, which enhances transcriptional activation (By similarity). Involved in the differentiation...
Homo sapiens (Human)
O15371
EIF3D_HUMAN
MAKFMTPVIQDNPSGWGPCAVPEQFRDMPYQPFSKGDRLGKVADWTGATYQDKRYTNKYSSQFGGGSQYAYFHEEDESSFQLVDTARTQKTAYQRNRMRFAQRNLRRDKDRRNMLQFNLQILPKSAKQKERERIRLQKKFQKQFGVRQKWDQKSQKPRDSSVEVRSDWEVKEEMDFPQLMKMRYLEVSEPQDIECCGALEYYDKAFDRITTRSEKPLRSIKRIFHTVTTTDDPVIRKLAKTQGNVFATDAILATLMSCTRSVYSWDIVVQRVGSKLFFDKRDNSDFDLLTVSETANEPPQDEGNSFNSPRNLAMEATYIN...
null
null
cap-dependent translational initiation [GO:0002191]; formation of cytoplasmic translation initiation complex [GO:0001732]; IRES-dependent viral translational initiation [GO:0075522]; positive regulation of mRNA binding [GO:1902416]; positive regulation of translation [GO:0045727]; translational initiation [GO:0006413];...
cytosol [GO:0005829]; eukaryotic 43S preinitiation complex [GO:0016282]; eukaryotic 48S preinitiation complex [GO:0033290]; eukaryotic translation initiation factor 3 complex [GO:0005852]; eukaryotic translation initiation factor 3 complex, eIF3m [GO:0071541]; membrane [GO:0016020]; synapse [GO:0045202]
mRNA cap binding [GO:0098808]; RNA binding [GO:0003723]; translation initiation factor activity [GO:0003743]
PF05091;
null
EIF-3 subunit D family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03003}.
null
null
null
null
null
FUNCTION: mRNA cap-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, a complex required for several steps in the initiation of protein synthesis of a specialized repertoire of mRNAs (PubMed:27462815). The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment o...
Homo sapiens (Human)
O15372
EIF3H_HUMAN
MASRKEGTGSTATSSSSTAGAAGKGKGKGGSGDSAVKQVQIDGLVVLKIIKHYQEEGQGTEVVQGVLLGLVVEDRLEITNCFPFPQHTEDDADFDEVQYQMEMMRSLRHVNIDHLHVGWYQSTYYGSFVTRALLDSQFSYQHAIEESVVLIYDPIKTAQGSLSLKAYRLTPKLMEVCKEKDFSPEALKKANITFEYMFEEVPIVIKNSHLINVLMWELEKKSAVADKHELLSLASSNHLGKNLQLLMDRVDEMSQDIVKYNTYMRNTSKQQQQKHQYQQRRQQENMQRQSRGEPPLPEEDLSKLFKPPQPPARMDSLLIA...
null
null
formation of cytoplasmic translation initiation complex [GO:0001732]; negative regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032435]; regulation of translational initiation [GO:0006446]; translational initiation [GO:0006413]
cytosol [GO:0005829]; eukaryotic 43S preinitiation complex [GO:0016282]; eukaryotic 48S preinitiation complex [GO:0033290]; eukaryotic translation initiation factor 3 complex [GO:0005852]; eukaryotic translation initiation factor 3 complex, eIF3m [GO:0071541]; extracellular exosome [GO:0070062]; membrane [GO:0016020]
metal-dependent deubiquitinase activity [GO:0140492]; metallopeptidase activity [GO:0008237]; RNA binding [GO:0003723]; translation initiation factor activity [GO:0003743]
PF19445;PF01398;
3.40.140.10;
EIF-3 subunit H family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03007}.
null
null
null
null
null
FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis (PubMed:17581632, PubMed:25849773, PubMed:27462815). The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-...
Homo sapiens (Human)
O15374
MOT5_HUMAN
MLKREGKVQPYTKTLDGGWGWMIVIHFFLVNVFVMGMTKTFAIFFVVFQEEFEGTSEQIGWIGSIMSSLRFCAGPLVAIICDILGEKTTSILGAFVVTGGYLISSWATSIPFLCVTMGLLPGLGSAFLYQVAAVVTTKYFKKRLALSTAIARSGMGLTFLLAPFTKFLIDLYDWTGALILFGAIALNLVPSSMLLRPIHIKSENNSGIKDKGSSLSAHGPEAHATETHCHETEESTIKDSTTQKAGLPSKNLTVSQNQSEEFYNGPNRNRLLLKSDEESDKVISWSCKQLFDISLFRNPFFYIFTWSFLLSQLAYFIPTF...
null
null
monocarboxylic acid transport [GO:0015718]
membrane [GO:0016020]; plasma membrane [GO:0005886]
monocarboxylic acid transmembrane transporter activity [GO:0008028]; symporter activity [GO:0015293]
PF07690;
1.20.1250.20;
Major facilitator superfamily, Monocarboxylate porter (TC 2.A.1.13) family
null
SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
null
null
null
null
null
FUNCTION: Proton-linked monocarboxylate transporter. Catalyzes the rapid transport across the plasma membrane of many monocarboxylates such as lactate, pyruvate, branched-chain oxo acids derived from leucine, valine and isoleucine, and the ketone bodies acetoacetate, beta-hydroxybutyrate and acetate (By similarity). {E...
Homo sapiens (Human)
O15379
HDAC3_HUMAN
MAKTVAYFYDPDVGNFHYGAGHPMKPHRLALTHSLVLHYGLYKKMIVFKPYQASQHDMCRFHSEDYIDFLQRVSPTNMQGFTKSLNAFNVGDDCPVFPGLFEFCSRYTGASLQGATQLNNKICDIAINWAGGLHHAKKFEASGFCYVNDIVIGILELLKYHPRVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKYGNYFFPGTGDMYEVGAESGRYYCLNVPLRDGIDDQSYKHLFQPVINQVVDFYQPTCIVLQCGADSLGCDRLGCFNLSIRGHGECVEYVKSFNIPLLVLGGGGYTVRNVARCWTYETSLLVEEAIS...
3.5.1.-; 3.5.1.98
null
cellular response to fluid shear stress [GO:0071498]; chromatin organization [GO:0006325]; circadian regulation of gene expression [GO:0032922]; cornified envelope assembly [GO:1903575]; DNA repair-dependent chromatin remodeling [GO:0140861]; establishment of mitotic spindle orientation [GO:0000132]; establishment of s...
cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; histone deacetylase complex [GO:0000118]; mitotic spindle [GO:0072686]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; Rpd3L-Expanded complex [GO:0070210]; transcription repressor complex [GO:0017053]
chromatin binding [GO:0003682]; chromatin DNA binding [GO:0031490]; cyclin binding [GO:0030332]; DNA-binding transcription factor binding [GO:0140297]; enzyme binding [GO:0019899]; histone deacetylase activity [GO:0004407]; histone deacetylase binding [GO:0042826]; histone decrotonylase activity [GO:0160009]; NF-kappaB...
PF00850;
3.40.800.20;
Histone deacetylase family, HD type 1 subfamily
PTM: Sumoylated in vitro. {ECO:0000269|PubMed:12032081}.; PTM: Deubiquitinated on 'Lys-63'-linked ubiquitin chains by USP38; leading to a decreased level of histone acetylation. {ECO:0000269|PubMed:32404892}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21030595}. Cytoplasm {ECO:0000269|PubMed:25190803}. Cytoplasm, cytosol {ECO:0000269|PubMed:21030595}. Note=Colocalizes with XBP1 and AKT1 in the cytoplasm (PubMed:25190803). Predominantly expressed in the nucleus in the presence of CCAR2 (PubMed:21030595). {ECO:0000269|...
CATALYTIC ACTIVITY: Reaction=H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-[histone]; Xref=Rhea:RHEA:58196, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:11338, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089, ChEBI:CHEBI:61930; EC=3.5.1.98; Evidence={ECO:0000269|PubMed:28497810, ECO:0000305|PubMed:23911289}; P...
null
null
null
null
FUNCTION: Histone deacetylase that catalyzes the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4), and some other non-histone substrates (PubMed:21030595, PubMed:21444723, PubMed:23911289, PubMed:25301942, PubMed:28167758, PubMed:28497810, PubMed:32404892). Histone deac...
Homo sapiens (Human)
O15381
NVL_HUMAN
MKPRPAGFVDNKLKQRVIQYLTSNKCGKYVDIGVLASDLQRVYSIDYGRRKRNAFRIQVEKVFSIISSEKELKNLTELEDEHLAKRARQGEEDNEYTESYSDDDSSMEDYPDPQSANHMNSSLLSLYRKGNPDSVSNTPEMEQRETTSSTPRISSKTGSIPLKTPAKDSEGGWFIDKTPSVKKDSFFLDLSCEKSNPKKPITEIQDSKDSSLLESDMKRKGKLKNKGSKRKKEDLQEVDGEIEAVLQKKAKARGLEFQISNVKFEDVGGNDMTLKEVCKMLIHMRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAG...
null
null
positive regulation of protein binding [GO:0032092]; positive regulation of telomerase activity [GO:0051973]; regulation of protein localization to nucleolus [GO:1904749]; ribosomal large subunit biogenesis [GO:0042273]; ribosome biogenesis [GO:0042254]; rRNA processing [GO:0006364]
membrane [GO:0016020]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; telomerase holoenzyme complex [GO:0005697]
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; preribosome binding [GO:1990275]; RNA binding [GO:0003723]
PF00004;PF17862;PF16725;
1.10.10.2010;1.10.8.60;3.40.50.300;
AAA ATPase family
null
SUBCELLULAR LOCATION: [Isoform 2]: Nucleus, nucleoplasm {ECO:0000269|PubMed:15469983}.; SUBCELLULAR LOCATION: [Isoform 1]: Nucleus, nucleolus {ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:15469983, ECO:0000269|PubMed:22226966, ECO:0000269|PubMed:26456651, ECO:0000269|PubMed:9286697}. Nucleus, nucleoplasm {ECO:000026...
null
null
null
null
null
FUNCTION: Participates in the assembly of the telomerase holoenzyme and effecting of telomerase activity via its interaction with TERT (PubMed:22226966). Involved in both early and late stages of the pre-rRNA processing pathways (PubMed:26166824). Spatiotemporally regulates 60S ribosomal subunit biogenesis in the nucle...
Homo sapiens (Human)
O15382
BCAT2_HUMAN
MAAAALGQIWARKLLSVPWLLCGPRRYASSSFKAADLQLEMTQKPHKKPGPGEPLVFGKTFTDHMLMVEWNDKGWGQPRIQPFQNLTLHPASSSLHYSLQLFEGMKAFKGKDQQVRLFRPWLNMDRMLRSAMRLCLPSFDKLELLECIRRLIEVDKDWVPDAAGTSLYVRPVLIGNEPSLGVSQPTRALLFVILCPVGAYFPGGSVTPVSLLADPAFIRAWVGGVGNYKLGGNYGPTVLVQQEALKRGCEQVLWLYGPDHQLTEVGTMNIFVYWTHEDGVLELVTPPLNGVILPGVVRQSLLDMAQTWGEFRVVERTITM...
2.6.1.42
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:12269802, ECO:0000269|PubMed:16141215, ECO:0000269|PubMed:17050531};
amino acid biosynthetic process [GO:0008652]; branched-chain amino acid biosynthetic process [GO:0009082]; cellular response to leukemia inhibitory factor [GO:1990830]; isoleucine catabolic process [GO:0006550]; leucine biosynthetic process [GO:0009098]; lipid metabolic process [GO:0006629]; regulation of hormone level...
mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]
branched-chain-amino-acid transaminase activity [GO:0004084]; L-isoleucine transaminase activity [GO:0052656]; L-leucine transaminase activity [GO:0052654]; L-leucine:2-oxoglutarate aminotransferase activity [GO:0050048]; L-valine transaminase activity [GO:0052655]
PF01063;
3.30.470.10;3.20.10.10;
Class-IV pyridoxal-phosphate-dependent aminotransferase family
null
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:O35854}.
CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:18321, ChEBI:CHEBI:16810, ChEBI:CHEBI:17865, ChEBI:CHEBI:29985, ChEBI:CHEBI:57427; EC=2.6.1.42; Evidence={ECO:0000269|PubMed:8702755}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-isoleucine = (S)-3-methy...
null
null
null
null
FUNCTION: Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine (PubMed:17050531, PubMed:25653144, PubMed:8702755). May also function as a transporter of branched chain alpha-keto acids (By similarity). {ECO:0000250|UniProtKB:O35854, ECO:0000269|PubMe...
Homo sapiens (Human)
O15389
SIGL5_HUMAN
MLPLLLLPLLWGGSLQEKPVYELQVQKSVTVQEGLCVLVPCSFSYPWRSWYSSPPLYVYWFRDGEIPYYAEVVATNNPDRRVKPETQGRFRLLGDVQKKNCSLSIGDARMEDTGSYFFRVERGRDVKYSYQQNKLNLEVTALIEKPDIHFLEPLESGRPTRLSCSLPGSCEAGPPLTFSWTGNALSPLDPETTRSSELTLTPRPEDHGTNLTCQMKRQGAQVTTERTVQLNVSYAPQTITIFRNGIALEILQNTSYLPVLEGQALRLLCDAPSNPPAHLSWFQGSPALNATPISNTGILELRRVRSAEEGGFTCRAQHPL...
null
null
cell adhesion [GO:0007155]
ficolin-1-rich granule membrane [GO:0101003]; plasma membrane [GO:0005886]; secretory granule membrane [GO:0030667]; tertiary granule membrane [GO:0070821]
carbohydrate binding [GO:0030246]; sialic acid binding [GO:0033691]
PF13927;PF07686;
2.60.40.10;
Immunoglobulin superfamily, SIGLEC (sialic acid binding Ig-like lectin) family
null
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
null
null
null
null
null
FUNCTION: Putative adhesion molecule that mediates sialic-acid dependent binding to cells. Binds equally to alpha-2,3-linked and alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface.
Homo sapiens (Human)
O15391
TYY2_HUMAN
MASNEDFSITQDLEIPADIVELHDINVEPLPMEDIPTESVQYEDVDGNWIYGGHNHPPLMVLQPLFTNTGYGDHDQEMLMLQTQEEVVGYCDSDNQLGNDLEDQLALPDSIEDEHFQMTLASLSASAASTSTSTQSRSKKPSKKPSGKSATSTEANPAGSSSSLGTRKWEQKQMQVKTLEGEFSVTMWSPNDNNDQGAVGEGQAENPPDYSEYLKGKKLPPGGLPGIDLSDPKQLAEFTKVKPKRSKGEPPKTVPCSYSGCEKMFRDYAAMRKHLHIHGPRVHVCAECGKAFLESSKLRRHQLVHTGEKPFQCTFEGCGK...
null
null
positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]
nucleus [GO:0005634]; PcG protein complex [GO:0031519]; transcription regulator complex [GO:0005667]
cis-regulatory region sequence-specific DNA binding [GO:0000987]; 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]; RNA polymerase II cis-regulatory region sequence-sp...
PF00096;
3.30.160.60;
YY transcription factor family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
null
null
null
null
null
FUNCTION: Functions as a multifunctional transcription factor that may exhibit positive and negative control on a large number of genes. May antagonize YY1 and function in development and differentiation. {ECO:0000269|PubMed:16260628}.
Homo sapiens (Human)
O15392
BIRC5_HUMAN
MGAPTLPPAWQPFLKDHRISTFKNWPFLEGCACTPERMAEAGFIHCPTENEPDLAQCFFCFKELEGWEPDDDPIEEHKKHSSGCAFLSVKKQFEELTLGEFLKLDRERAKNKIAKETNNKKKEFEETAKKVRRAIEQLAAMD
null
null
apoptotic process [GO:0006915]; cell division [GO:0051301]; establishment of chromosome localization [GO:0051303]; G2/M transition of mitotic cell cycle [GO:0000086]; mitotic cell cycle [GO:0000278]; mitotic cytokinesis [GO:0000281]; mitotic spindle assembly [GO:0090307]; mitotic spindle assembly checkpoint signaling [...
centriole [GO:0005814]; chromosome passenger complex [GO:0032133]; chromosome, centromeric region [GO:0000775]; cytoplasm [GO:0005737]; cytoplasmic microtubule [GO:0005881]; cytosol [GO:0005829]; interphase microtubule organizing center [GO:0031021]; kinetochore [GO:0000776]; microtubule [GO:0005874]; microtubule cytos...
cobalt ion binding [GO:0050897]; cysteine-type endopeptidase inhibitor activity [GO:0004869]; cysteine-type endopeptidase inhibitor activity involved in apoptotic process [GO:0043027]; enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; microtubule binding [GO:0008017]; ...
PF00653;
null
IAP family
PTM: Ubiquitinated by the Cul9-RING ubiquitin-protein ligase complex, leading to its degradation. Ubiquitination is required for centrosomal targeting. Deubiquitinated by USP35 or USP38; leading to stabilization (PubMed:34438346). {ECO:0000269|PubMed:16322459, ECO:0000269|PubMed:24793696, ECO:0000269|PubMed:34438346}.;...
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20627126, ECO:0000269|PubMed:20826784, ECO:0000269|PubMed:21364656}. Nucleus {ECO:0000269|PubMed:20627126, ECO:0000269|PubMed:20826784, ECO:0000269|PubMed:21364656}. Chromosome {ECO:0000269|PubMed:14610074}. Chromosome, centromere {ECO:0000269|PubMed:11084331, ECO:000...
null
null
null
null
null
FUNCTION: Multitasking protein that has dual roles in promoting cell proliferation and preventing apoptosis (PubMed:20627126, PubMed:21364656, PubMed:25778398, PubMed:28218735, PubMed:9859993). Component of a chromosome passage protein complex (CPC) which is essential for chromosome alignment and segregation during mit...
Homo sapiens (Human)
O15393
TMPS2_HUMAN
MALNSGSPPAIGPYYENHGYQPENPYPAQPTVVPTVYEVHPAQYYPSPVPQYAPRVLTQASNPVVCTQPKSPSGTVCTSKTKKALCITLTLGTFLVGAALAAGLLWKFMGSKCSNSGIECDSSGTCINPSNWCDGVSHCPGGEDENRCVRLYGPNFILQVYSSQRKSWHPVCQDDWNENYGRAACRDMGYKNNFYSSQGIVDDSGSTSFMKLNTSAGNVDIYKKLYHSDACSSKAVVSLRCIACGVNLNSSRQSRIVGGESALPGAWPWQVSLHVQNVHVCGGSIITPEWIVTAAHCVEKPLNNPWHWTAFAGILRQSFM...
3.4.21.122
null
positive regulation of viral entry into host cell [GO:0046598]; protein autoprocessing [GO:0016540]; proteolysis [GO:0006508]; viral translation [GO:0019081]
extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]
serine-type endopeptidase activity [GO:0004252]; serine-type peptidase activity [GO:0008236]
PF15494;PF00089;
4.10.400.10;3.10.250.10;2.40.10.10;
Peptidase S1 family
PTM: Proteolytically processed; by an autocatalytic mechanism.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20382709, ECO:0000269|PubMed:21068237}; Single-pass type II membrane protein {ECO:0000269|PubMed:20382709, ECO:0000269|PubMed:21068237}.; SUBCELLULAR LOCATION: [Transmembrane protease serine 2 catalytic chain]: Secreted {ECO:0000269|PubMed:20382709}. Note=Activate...
CATALYTIC ACTIVITY: Reaction=The enzyme cleaves angiotensin-converting enzyme 2 (EC 3.4.17.23) and cleaves influenzea A and B virus and coronavirus spike glycoproteins at arginine residues.; EC=3.4.21.122; Evidence={ECO:0000269|PubMed:32703818};
null
null
null
null
FUNCTION: Plasma membrane-anchored serine protease that cleaves at arginine residues (PubMed:32703818). Participates in proteolytic cascades of relevance for the normal physiologic function of the prostate (PubMed:25122198). Androgen-induced TMPRSS2 activates several substrates that include pro-hepatocyte growth factor...
Homo sapiens (Human)
O15394
NCAM2_HUMAN
MSLLLSFYLLGLLVSSGQALLQVTISLSKVELSVGESKFFTCTAIGEPESIDWYNPQGEKIISTQRVVVQKEGVRSRLTIYNANIEDAGIYRCQATDAKGQTQEATVVLEIYQKLTFREVVSPQEFKQGEDAEVVCRVSSSPAPAVSWLYHNEEVTTISDNRFAMLANNNLQILNINKSDEGIYRCEGRVEARGEIDFRDIIVIVNVPPAISMPQKSFNATAERGEEMTFSCRASGSPEPAISWFRNGKLIEENEKYILKGSNTELTVRNIINSDGGPYVCRATNKAGEDEKQAFLQVFVQPHIIQLKNETTYENGQVTL...
null
null
axonal fasciculation [GO:0007413]; neuron cell-cell adhesion [GO:0007158]
axon [GO:0030424]; membrane [GO:0016020]; nuclear body [GO:0016604]; plasma membrane [GO:0005886]
identical protein binding [GO:0042802]
PF00041;PF07679;PF13927;
2.60.40.10;
null
null
SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein.
null
null
null
null
null
FUNCTION: May play important roles in selective fasciculation and zone-to-zone projection of the primary olfactory axons.
Homo sapiens (Human)
O15397
IPO8_HUMAN
MDLNRIIQALKGTIDPKLRIAAENELNQSYKIINFAPSLLRIIVSDHVEFPVRQAAAIYLKNMVTQYWPDREPPPGEAIFPFNIHENDRQQIRDNIVEGIIRSPDLVRVQLTMCLRAIIKHDFPGHWPGVVDKIDYYLQSQSSASWLGSLLCLYQLVKTYEYKKAEEREPLIIAMQIFLPRIQQQIVQLLPDSSYYSVLLQKQILKIFYALVQYALPLQLVNNQTMTTWMEIFRTIIDRTVPPETLHIDEDDRPELVWWKCKKWALHIVARLFERYGSPGNVTKEYFEFSEFFLKTYAVGIQQVLLKILDQYRQKEYVAP...
null
null
protein import into nucleus [GO:0006606]; signal transduction [GO:0007165]
cytosol [GO:0005829]; nuclear envelope [GO:0005635]; nucleoplasm [GO:0005654]
small GTPase binding [GO:0031267]
PF08506;PF03810;
1.25.10.10;
Importin beta family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
null
null
null
null
null
FUNCTION: Involved in nuclear protein import, either by acting as autonomous nuclear transport receptor or as an adapter-like protein in association with the importin-beta subunit KPNB1. Acting autonomously, may serve as receptor for nuclear localization signals (NLS) and promote translocation of import substrates thro...
Homo sapiens (Human)
O15399
NMDE4_HUMAN
MRGAGGPRGPRGPAKMLLLLALACASPFPEEAPGPGGAGGPGGGLGGARPLNVALVFSGPAYAAEAARLGPAVAAAVRSPGLDVRPVALVLNGSDPRSLVLQLCDLLSGLRVHGVVFEDDSRAPAVAPILDFLSAQTSLPIVAVHGGAALVLTPKEKGSTFLQLGSSTEQQLQVIFEVLEEYDWTSFVAVTTRAPGHRAFLSYIEVLTDGSLVGWEHRGALTLDPGAGEAVLSAQLRSVSAQIRLLFCAREEAEPVFRAAEEAGLTGSGYVWFMVGPQLAGGGGSGAPGEPPLLPGGAPLPAGLFAVRSAGWRDDLARRV...
null
null
adult locomotory behavior [GO:0008344]; brain development [GO:0007420]; calcium ion transmembrane import into cytosol [GO:0097553]; cellular response to L-glutamate [GO:1905232]; excitatory chemical synaptic transmission [GO:0098976]; excitatory postsynaptic potential [GO:0060079]; ionotropic glutamate receptor signali...
endoplasmic reticulum membrane [GO:0005789]; glutamatergic synapse [GO:0098978]; hippocampal mossy fiber to CA3 synapse [GO:0098686]; NMDA selective glutamate receptor complex [GO:0017146]; plasma membrane [GO:0005886]; postsynaptic density membrane [GO:0098839]; postsynaptic membrane [GO:0045211]; presynaptic active z...
glutamate binding [GO:0016595]; glutamate-gated calcium ion channel activity [GO:0022849]; glutamate-gated receptor activity [GO:0004970]; ligand-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential [GO:0099507]; NMDA glutamate receptor activity [GO:0004972]; transmitter-gated ...
PF01094;PF00060;PF10613;PF00497;
3.40.50.2300;3.40.190.10;
Glutamate-gated ion channel (TC 1.A.10.1) family, NR2D/GRIN2D subfamily
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26875626, ECO:0000269|PubMed:28126851, ECO:0000269|PubMed:9489750}; Multi-pass membrane protein. Postsynaptic cell membrane; Multi-pass membrane protein.
null
null
null
null
null
FUNCTION: Component of NMDA receptor complexes that function as heterotetrameric, ligand-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Channel activation requires binding of the neurotransmitter glutamate to the epsilon subunit, glycine binding to the zeta subunit, pl...
Homo sapiens (Human)
O15400
STX7_HUMAN
MSYTPGVGGDPAQLAQRISSNIQKITQCSVEIQRTLNQLGTPQDSPELRQQLQQKQQYTNQLAKETDKYIKEFGSLPTTPSEQRQRKIQKDRLVAEFTTSLTNFQKVQRQAAEREKEFVARVRASSRVSGSFPEDSSKERNLVSWESQTQPQVQVQDEEITEDDLRLIHERESSIRQLEADIMDINEIFKDLGMMIHEQGDVIDSIEANVENAEVHVQQANQQLSRAADYQRKSRKTLCIIILILVIGVAIISLIIWGLNH
null
null
intracellular protein transport [GO:0006886]; organelle assembly [GO:0070925]; organelle localization [GO:0051640]; positive regulation of receptor localization to synapse [GO:1902685]; positive regulation of T cell mediated cytotoxicity [GO:0001916]; regulation of protein localization to plasma membrane [GO:1903076]; ...
azurophil granule [GO:0042582]; early endosome [GO:0005769]; early endosome membrane [GO:0031901]; endocytic vesicle [GO:0030139]; endomembrane system [GO:0012505]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; immunological synapse [GO:0001772]; late endosome [GO:0005770]; lysosomal membrane [GO:0005765];...
chloride channel inhibitor activity [GO:0019869]; SNAP receptor activity [GO:0005484]; SNARE binding [GO:0000149]; syntaxin binding [GO:0019905]
PF05739;PF14523;
1.20.5.110;1.20.58.70;
Syntaxin family
null
SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}.
null
null
null
null
null
FUNCTION: May be involved in protein trafficking from the plasma membrane to the early endosome (EE) as well as in homotypic fusion of endocytic organelles. Mediates the endocytic trafficking from early endosomes to late endosomes and lysosomes.
Homo sapiens (Human)
O15405
TOX3_HUMAN
MDVRFYPAAAGDPASLDFAQCLGYYGYSKFGNNNNYMNMAEANNAFFAASEQTFHTPSLGDEEFEIPPITPPPESDPALGMPDVLLPFQALSDPLPSQGSEFTPQFPPQSLDLPSITISRNLVEQDGVLHSSGLHMDQSHTQVSQYRQDPSLIMRSIVHMTDAARSGVMPPAQLTTINQSQLSAQLGLNLGGASMPHTSPSPPASKSATPSPSSSINEEDADEANRAIGEKRAAPDSGKKPKTPKKKKKKDPNEPQKPVSAYALFFRDTQAAIKGQNPNATFGEVSKIVASMWDSLGEEQKQVYKRKTEAAKKEYLKALA...
null
null
apoptotic process [GO:0006915]; negative regulation of neuron apoptotic process [GO:0043524]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of apoptotic process [GO:0042981]; regulation of transcription by RNA polymerase II [GO:0006357]
cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
chromatin binding [GO:0003682]; chromatin DNA binding [GO:0031490]; phosphoprotein binding [GO:0051219]; protein homodimerization activity [GO:0042803]; transcription coactivator activity [GO:0003713]
PF00505;
1.10.30.10;
null
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
null
null
null
null
null
FUNCTION: Transcriptional coactivator of the p300/CBP-mediated transcription complex. Activates transactivation through cAMP response element (CRE) sites. Protects against cell death by inducing antiapoptotic and repressing pro-apoptotic transcripts. Stimulates transcription from the estrogen-responsive or BCL-2 promot...
Homo sapiens (Human)
O15409
FOXP2_HUMAN
MMQESATETISNSSMNQNGMSTLSSQLDAGSRDGRSSGDTSSEVSTVELLHLQQQQALQAARQLLLQQQTSGLKSPKSSDKQRPLQVPVSVAMMTPQVITPQQMQQILQQQVLSPQQLQALLQQQQAVMLQQQQLQEFYKKQQEQLHLQLLQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQHPGKQAKEQQQQQQQQQQLAAQQLVFQQQLLQMQQLQQQQHLLSLQRQGLISIPPGQAALPVQSLPQAGLSPAEIQQLWKEVTGVHSMEDNGIKHGGLDLTTNNSSSTTSSNTSKASPPITHHSIVNGQ...
null
null
caudate nucleus development [GO:0021757]; cerebral cortex development [GO:0021987]; negative regulation of DNA-templated transcription [GO:0045892]; putamen development [GO:0021758]; regulation of transcription by RNA polymerase II [GO:0006357]
chromatin [GO:0000785]; nucleus [GO:0005634]
DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; identical protein binding [GO:0042802]; metal ion binding [GO:00468...
PF00250;PF16159;
1.20.5.340;1.10.10.10;
null
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
null
null
null
null
null
FUNCTION: Transcriptional repressor that may play a role in the specification and differentiation of lung epithelium. May also play a role in developing neural, gastrointestinal and cardiovascular tissues. Can act with CTBP1 to synergistically repress transcription but CTPBP1 is not essential. Plays a role in synapse f...
Homo sapiens (Human)
O15427
MOT4_HUMAN
MGGAVVDEGPTGVKAPDGGWGWAVLFGCFVITGFSYAFPKAVSVFFKELIQEFGIGYSDTAWISSILLAMLYGTGPLCSVCVNRFGCRPVMLVGGLFASLGMVAASFCRSIIQVYLTTGVITGLGLALNFQPSLIMLNRYFSKRRPMANGLAAAGSPVFLCALSPLGQLLQDRYGWRGGFLILGGLLLNCCVCAALMRPLVVTAQPGSGPPRPSRRLLDLSVFRDRGFVLYAVAASVMVLGLFVPPVFVVSYAKDLGVPDTKAAFLLTILGFIDIFARPAAGFVAGLGKVRPYSVYLFSFSMFFNGLADLAGSTAGDYGG...
null
null
lactate transmembrane transport [GO:0035873]; monocarboxylic acid transport [GO:0015718]; protein catabolic process [GO:0030163]; pyruvate catabolic process [GO:0042867]; pyruvate transmembrane transport [GO:1901475]
apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; lateral plasma membrane [GO:0016328]; membrane [GO:0016020]; nuclear membrane [GO:0031965]; plasma membrane [GO:0005886]; synapse [GO:0045202]
lactate:proton symporter activity [GO:0015650]; monocarboxylic acid transmembrane transporter activity [GO:0008028]; pyruvate transmembrane transporter activity [GO:0050833]; RNA binding [GO:0003723]
PF07690;
1.20.1250.20;
Major facilitator superfamily, Monocarboxylate porter (TC 2.A.1.13) family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10921872, ECO:0000269|PubMed:11101640, ECO:0000269|PubMed:15505343, ECO:0000269|PubMed:23935841}; Multi-pass membrane protein. Basolateral cell membrane {ECO:0000269|PubMed:21199217}; Multi-pass membrane protein {ECO:0000255}. Note=Plasma membrane localization is ...
CATALYTIC ACTIVITY: Reaction=(S)-lactate(in) + H(+)(in) = (S)-lactate(out) + H(+)(out); Xref=Rhea:RHEA:29415, ChEBI:CHEBI:15378, ChEBI:CHEBI:16651; Evidence={ECO:0000269|PubMed:11101640, ECO:0000269|PubMed:23935841, ECO:0000269|PubMed:31719150}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29416; Evidence={ECO:...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.4 mM for (S)-lactate (pH 5.5) {ECO:0000269|PubMed:23935841}; KM=37.6 mM for (S)-lactate (pH 7.5) {ECO:0000269|PubMed:23935841}; KM=28 mM for (S)-lactate {ECO:0000269|PubMed:11101640}; KM=519 mM for D-lactate {ECO:0000269|PubMed:11101640}; KM=153 mM for pyruvate {...
null
null
null
FUNCTION: Proton-dependent transporter of monocarboxylates such as L-lactate and pyruvate (PubMed:11101640, PubMed:23935841, PubMed:31719150). Plays a predominant role in L-lactate efflux from highly glycolytic cells (By similarity). {ECO:0000250|UniProtKB:O35910, ECO:0000269|PubMed:11101640, ECO:0000269|PubMed:2393584...
Homo sapiens (Human)
O15431
COPT1_HUMAN
MDHSHHMGMSYMDSNSTMQPSHHHPTTSASHSHGGGDSSMMMMPMTFYFGFKNVELLFSGLVINTAGEMAGAFVAVFLLAMFYEGLKIARESLLRKSQVSIRYNSMPVPGPNGTILMETHKTVGQQMLSFPHLLQTVLHIIQVVISYFLMLIFMTYNGYLCIAVAAGAGTGYFLFSWKKAVVVDITEHCH
null
null
angiogenesis [GO:0001525]; copper ion import [GO:0015677]; copper ion transport [GO:0006825]; establishment of localization in cell [GO:0051649]; intracellular copper ion homeostasis [GO:0006878]; plasma membrane copper ion transport [GO:0015679]; protein complex oligomerization [GO:0051259]; silver ion transmembrane t...
apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; early endosome membrane [GO:0031901]; intercalated disc [GO:0014704]; late endosome membrane [GO:0031902]; plasma membrane [GO:0005886]; recycling endosome membrane [GO:0055038]
copper ion binding [GO:0005507]; copper ion transmembrane transporter activity [GO:0005375]; identical protein binding [GO:0042802]; silver ion transmembrane transporter activity [GO:0015080]; xenobiotic transmembrane transporter activity [GO:0042910]
PF04145;
null
Copper transporter (Ctr) (TC 1.A.56) family, SLC31A subfamily
PTM: O-Glycosylation at Thr-27 protects from proteolytic cleavage in the N-terminal extracellular domain. {ECO:0000269|PubMed:17525160}.; PTM: Proteolytic cleavage, leading to a truncated form, is facilitated by SLC31A2 (PubMed:24167251) and initiated preferentially by CTSL and to a minor extend by CTSB in endolysosoma...
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11734551, ECO:0000269|PubMed:12023893, ECO:0000269|PubMed:15326162, ECO:0000269|PubMed:17525160, ECO:0000269|PubMed:20451502, ECO:0000269|PubMed:26205368, ECO:0000269|PubMed:26945057, ECO:0000269|PubMed:35913762}; Multi-pass membrane protein {ECO:0000255}. Early e...
CATALYTIC ACTIVITY: Reaction=Ag(+)(out) = Ag(+)(in); Xref=Rhea:RHEA:75207, ChEBI:CHEBI:49468; Evidence={ECO:0000269|PubMed:20569931}; CATALYTIC ACTIVITY: Reaction=Cu(+)(out) = Cu(+)(in); Xref=Rhea:RHEA:75211, ChEBI:CHEBI:49552; Evidence={ECO:0000269|PubMed:11734551, ECO:0000269|PubMed:16135512, ECO:0000269|PubMed:17525...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.71 uM for copper(1+) {ECO:0000269|PubMed:11734551}; KM=8.9 uM for copper(1+) {ECO:0000269|PubMed:16135512}; KM=9.2 uM for copper(1+) (in Sf9 cells expressing SLC31A1) {ECO:0000269|PubMed:16135512}; KM=4.4 uM for copper(1+) {ECO:0000269|PubMed:23658018}; Vmax=6.76...
null
null
null
FUNCTION: [High affinity copper uptake protein 1]: Uniporter that mediates the transport of copper(1+) from the extracellular space to the cytoplasm, across the plasma membrane (PubMed:11734551, PubMed:16135512, PubMed:17525160, PubMed:19740744, PubMed:20451502, PubMed:20569931, PubMed:23658018) and delivers directly c...
Homo sapiens (Human)
O15432
COPT2_HUMAN
MAMHFIFSDTAVLLFDFWSVHSPAGMALSVLVLLLLAVLYEGIKVGKAKLLNQVLVNLPTSISQQTIAETDGDSAGSDSFPVGRTHHRWYLCHFGQSLIHVIQVVIGYFIMLAVMSYNTWIFLGVVLGSAVGYYLAYPLLSTA
null
null
copper ion import [GO:0015677]; copper ion transport [GO:0006825]; intracellular copper ion homeostasis [GO:0006878]; regulation of copper ion transmembrane transport [GO:1902311]
late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]
copper ion transmembrane transporter activity [GO:0005375]
PF04145;
null
Copper transporter (Ctr) (TC 1.A.56) family, SLC31A subfamily
PTM: Ubiquitinated; ubiquitination and the subsequent proteasomal degradation are prevent by SLC31A1 that stabilizes it. {ECO:0000269|PubMed:26205368}.
SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:17944601}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:17944601}; Multi-pass membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000269|PubMed:17617060}; Multi-pass membrane protein {ECO:0000255}. Lysosome membra...
null
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=11 uM for copper (in COS-7 cells transfected with human SLC31A1) {ECO:0000269|PubMed:17944601}; Vmax=10.2 pmol/min/mg protein for copper (in COS-7 cells transfected with human SLC31A1) {ECO:0000269|PubMed:17944601};
null
null
null
FUNCTION: Does not function as a copper(1+) importer in vivo (By similarity). However, in vitro functions as a low-affinity copper(1+) importer (PubMed:17617060, PubMed:17944601). Regulator of SLC31A1 which facilitates the cleavage of the SLC31A1 ecto-domain or which stabilizes the truncated form of SLC31A1 (Truncated ...
Homo sapiens (Human)
O15438
MRP3_HUMAN
MDALCGSGELGSKFWDSNLSVHTENPDLTPCFQNSLLAWVPCIYLWVALPCYLLYLRHHCRGYIILSHLSKLKMVLGVLLWCVSWADLFYSFHGLVHGRAPAPVFFVTPLVVGVTMLLATLLIQYERLQGVQSSGVLIIFWFLCVVCAIVPFRSKILLAKAEGEISDPFRFTTFYIHFALVLSALILACFREKPPFFSAKNVDPNPYPETSAGFLSRLFFWWFTKMAIYGYRHPLEEKDLWSLKEEDRSQMVVQQLLEAWRKQEKQTARHKASAAPGKNASGEDEVLLGARPRPRKPSFLKALLATFGSSFLISACFKLI...
7.6.2.-; 7.6.2.2; 7.6.2.3
null
bile acid and bile salt transport [GO:0015721]; leukotriene transport [GO:0071716]; transmembrane transport [GO:0055085]; transport across blood-brain barrier [GO:0150104]; xenobiotic metabolic process [GO:0006805]; xenobiotic transmembrane transport [GO:0006855]; xenobiotic transport [GO:0042908]
basal plasma membrane [GO:0009925]; basolateral plasma membrane [GO:0016323]; membrane [GO:0016020]; plasma membrane [GO:0005886]
ABC-type bile acid transporter activity [GO:0015432]; ABC-type glutathione S-conjugate transporter activity [GO:0015431]; ABC-type transporter activity [GO:0140359]; ABC-type xenobiotic transporter activity [GO:0008559]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled inorganic anion tran...
PF00664;PF00005;
1.20.1560.10;3.40.50.300;
ABC transporter superfamily, ABCC family, Conjugate transporter (TC 3.A.1.208) subfamily
null
SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000269|PubMed:10094960, ECO:0000269|PubMed:10359813, ECO:0000269|PubMed:15083066, ECO:0000269|PubMed:28408210}; Multi-pass membrane protein {ECO:0000255}. Basal cell membrane {ECO:0000269|PubMed:35307651}; Multi-pass membrane protein {ECO:0000255}. Note=Localized to...
CATALYTIC ACTIVITY: Reaction=ATP + H2O + taurocholate(in) = ADP + H(+) + phosphate + taurocholate(out); Xref=Rhea:RHEA:50052, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36257, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O88563}; PhysiologicalDirection=left-to-right; ...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=17.7 uM for oestradiol-17-(beta-D-glucuronide) {ECO:0000269|PubMed:11581266}; KM=24.2 uM for oestradiol-17-(beta-D-glucuronide) {ECO:0000269|PubMed:15083066}; KM=46.3 uM for dehydroepiandrosterone- 3-sulfate {ECO:0000269|PubMed:15083066}; Vmax=281 pmol/min/mg enzym...
null
null
null
FUNCTION: ATP-dependent transporter of the ATP-binding cassette (ABC) family that binds and hydrolyzes ATP to enable active transport of various substrates including many drugs, toxicants and endogenous compound across cell membranes (PubMed:10359813, PubMed:11581266, PubMed:15083066). Transports glucuronide conjugates...
Homo sapiens (Human)
O15439
MRP4_HUMAN
MLPVYQEVKPNPLQDANLCSRVFFWWLNPLFKIGHKRRLEEDDMYSVLPEDRSQHLGEELQGFWDKEVLRAENDAQKPSLTRAIIKCYWKSYLVLGIFTLIEESAKVIQPIFLGKIINYFENYDPMDSVALNTAYAYATVLTFCTLILAILHHLYFYHVQCAGMRLRVAMCHMIYRKALRLSNMAMGKTTTGQIVNLLSNDVNKFDQVTVFLHFLWAGPLQAIAVTALLWMEIGISCLAGMAVLIILLPLQSCFGKLFSSLRSKTATFTDARIRTMNEVITGIRIIKMYAWEKSFSNLITNLRKKEISKILRSSCLRGMN...
7.6.2.-; 7.6.2.2; 7.6.2.3
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:15364914};
bile acid and bile salt transport [GO:0015721]; cAMP transport [GO:0070730]; cilium assembly [GO:0060271]; export across plasma membrane [GO:0140115]; leukotriene transport [GO:0071716]; platelet degranulation [GO:0002576]; prostaglandin secretion [GO:0032310]; prostaglandin transport [GO:0015732]; transmembrane transp...
apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; external side of apical plasma membrane [GO:0098591]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; nucleolus [GO:0005730]; plasma membrane [GO:0005886]; platelet dense granule membrane [GO:0031088]
15-hydroxyprostaglandin dehydrogenase (NAD+) activity [GO:0016404]; ABC-type bile acid transporter activity [GO:0015432]; ABC-type glutathione S-conjugate transporter activity [GO:0015431]; ABC-type transporter activity [GO:0140359]; ABC-type xenobiotic transporter activity [GO:0008559]; ATP binding [GO:0005524]; ATP h...
PF00664;PF00005;
1.20.1560.10;3.40.50.300;
ABC transporter superfamily, ABCC family, Conjugate transporter (TC 3.A.1.208) subfamily
PTM: N-glycosylated; leading to substrate-selective effects on its transport activity. {ECO:0000269|PubMed:26721430}.
SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000269|PubMed:11106685, ECO:0000269|PubMed:12883481, ECO:0000269|PubMed:26721430}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000269|PubMed:11856762, ECO:0000269|PubMed:26721430}; Multi-pass membrane protein {ECO:0000255}. Note=Its localiz...
CATALYTIC ACTIVITY: Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate + xenobioticSide 2.; EC=7.6.2.2; Evidence={ECO:0000269|PubMed:11856762, ECO:0000269|PubMed:12105214, ECO:0000269|PubMed:15454390, ECO:0000269|PubMed:17344354, ECO:0000269|PubMed:18300232}; CATALYTIC ACTIVITY: Reaction=an S-substituted glutathio...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.1 uM for prostaglandin E1 {ECO:0000269|PubMed:12835412}; KM=3.4 uM for prostaglandin E2 {ECO:0000269|PubMed:12835412}; KM=25.8 uM for cholylglycine (in the presence of 5 mM GSH) {ECO:0000269|PubMed:16282361}; KM=7.7 uM for cholyltaurine (in the presence of 5 mM G...
null
null
null
FUNCTION: ATP-dependent transporter of the ATP-binding cassette (ABC) family that actively extrudes physiological compounds and xenobiotics from cells. Transports a range of endogenous molecules that have a key role in cellular communication and signaling, including cyclic nucleotides such as cyclic AMP (cAMP) and cycl...
Homo sapiens (Human)
O15440
MRP5_HUMAN
MKDIDIGKEYIIPSPGYRSVRERTSTSGTHRDREDSKFRRTRPLECQDALETAARAEGLSLDASMHSQLRILDEEHPKGKYHHGLSALKPIRTTSKHQHPVDNAGLFSCMTFSWLSSLARVAHKKGELSMEDVWSLSKHESSDVNCRRLERLWQEELNEVGPDAASLRRVVWIFCRTRLILSIVCLMITQLAGFSGPAFMVKHLLEYTQATESNLQYSLLLVLGLLLTEIVRSWSLALTWALNYRTGVRLRGAILTMAFKKILKLKNIKEKSLGELINICSNDGQRMFEAAAVGSLLAGGPVVAILGMIYNVIILGPTGF...
7.6.2.-; 7.6.2.2
null
cAMP transport [GO:0070730]; cGMP transport [GO:0070731]; export across plasma membrane [GO:0140115]; folate transmembrane transport [GO:0098838]; glutathione transmembrane transport [GO:0034775]; heme transmembrane transport [GO:0035351]; hyaluronan biosynthetic process [GO:0030213]; purine nucleotide transport [GO:00...
apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; endosome membrane [GO:0010008]; Golgi lumen [GO:0005796]; membrane [GO:0016020]; plasma membrane [GO:0005886]
ABC-type xenobiotic transporter activity [GO:0008559]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled inorganic anion transmembrane transporter activity [GO:0043225]; ATPase-coupled transmembrane transporter activity [GO:0042626]; carbohydrate derivative transmembrane transporter activit...
PF00664;PF00005;
1.20.1560.10;3.40.50.300;
ABC transporter superfamily, ABCC family, Conjugate transporter (TC 3.A.1.208) subfamily
null
SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000269|PubMed:24836561}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus lumen {ECO:0000269|PubMed:24836561}. Endosome membrane {ECO:0000269|PubMed:24836561}. Cytoplasmic granule {ECO:0000250|UniProtKB:Q9R1X5}. Apical cell membrane {ECO:0000269|PubMed:155...
CATALYTIC ACTIVITY: Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate + xenobioticSide 2.; EC=7.6.2.2; Evidence={ECO:0000269|PubMed:10840050, ECO:0000269|PubMed:12435799, ECO:0000269|PubMed:12695538, ECO:0000269|PubMed:15899835}; CATALYTIC ACTIVITY: Reaction=3',5'-cyclic GMP(in) + ATP + H2O = 3',5'-cyclic GMP(out...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=379 uM for cAMP {ECO:0000269|PubMed:10893247}; KM=2.1 uM for cGMP {ECO:0000269|PubMed:10893247}; KM=132 uM for cGMP {ECO:0000269|PubMed:17229149}; KM=1 mM for folate {ECO:0000269|PubMed:15899835}; KM=1 mM for N-[(S)-lactoyl]-L-phenylalanine {ECO:0000269|PubMed:2596...
null
null
null
FUNCTION: ATP-dependent transporter of the ATP-binding cassette (ABC) family that actively extrudes physiological compounds, and xenobiotics from cells. Mediates ATP-dependent transport of endogenous metabolites such as cAMP and cGMP, folic acid and N-lactoyl-amino acids (in vitro) (PubMed:10893247, PubMed:12637526, Pu...
Homo sapiens (Human)
O15444
CCL25_HUMAN
MNLWLLACLVAGFLGAWAPAVHTQGVFEDCCLAYHYPIGWAVLRRAWTYRIQEVSGSCNLPAAIFYLPKRHRKVCGNPKSREVQRAMKLLDARNKVFAKLHHNTQTFQAGPHAVKKLSSGNSKLSSSKFSNPISSSKRNVSLLISANSGL
null
null
cell chemotaxis [GO:0060326]; cell surface receptor signaling pathway [GO:0007166]; cellular response to interleukin-1 [GO:0071347]; cellular response to tumor necrosis factor [GO:0071356]; cellular response to type II interferon [GO:0071346]; chemokine-mediated signaling pathway [GO:0070098]; chemotaxis [GO:0006935]; ...
extracellular region [GO:0005576]; extracellular space [GO:0005615]
CCR chemokine receptor binding [GO:0048020]; CCR10 chemokine receptor binding [GO:0031735]; chemokine activity [GO:0008009]; chemokine receptor binding [GO:0042379]; hormone activity [GO:0005179]
PF00048;
2.40.50.40;
Intercrine beta (chemokine CC) family
null
SUBCELLULAR LOCATION: Secreted.
null
null
null
null
null
FUNCTION: Potentially involved in T-cell development. Recombinant protein shows chemotactic activity on thymocytes, macrophages, THP-1 cells, and dendritics cells but is inactive on peripheral blood lymphocytes and neutrophils. Binds to CCR9. Isoform 2 is an antagonist of isoform 1. Binds to atypical chemokine receptor...
Homo sapiens (Human)
O15446
RPA34_HUMAN
MEEPQAGDAARFSCPPNFTAKPPASESPRFSLEALTGPDTELWLIQAPADFAPECFNGRHVPLSGSQIVKGKLAGKRHRYRVLSSCPQAGEATLLAPSTEAGGGLTCASAPQGTLRILEGPQQSLSGSPLQPIPASPPPQIPPGLRPRFCAFGGNPPVTGPRSALAPNLLTSGKKKKEMQVTEAPVTQEAVNGHGALEVDMALGSPEMDVRKKKKKKNQQLKEPEAAGPVGTEPTVETLEPLGVLFPSTTKKRKKPKGKETFEPEDKTVKQEQINTEPLEDTVLSPTKKRKRQKGTEGMEPEEGVTVESQPQVKVEPLEE...
null
null
rRNA transcription [GO:0009303]; transcription initiation at RNA polymerase I promoter [GO:0006361]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]
chromosome [GO:0005694]; cytosol [GO:0005829]; fibrillar center [GO:0001650]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; RNA polymerase I complex [GO:0005736]; RNA polymerase I transcription regulator complex [GO:0000120]
RNA binding [GO:0003723]
PF08208;
6.20.250.70;
Eukaryotic RPA34 RNA polymerase subunit family
PTM: [Isoform 2]: Undergoes tyrosine phosphorylation upon T-cell receptor (TCR) stimulation. This phosphorylation has not been confirmed by other groups. {ECO:0000269|PubMed:10373416}.; PTM: [Isoform 1]: Phosphorylated on tyrosine residues in initiation-competent Pol I-beta complexes but not in Pol I-alpha complexes. {...
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:9426281}. Chromosome {ECO:0000269|PubMed:9426281}. Note=Found at the fibrillar centers of the nucleolus in interphase and during cell division it is localized to the nucleolus organizer regions of the chromosomes.
null
null
null
null
null
FUNCTION: Component of RNA polymerase I (Pol I), a DNA-dependent RNA polymerase which synthesizes ribosomal RNA precursors using the four ribonucleoside triphosphates as substrates. Involved in UBTF-activated transcription, presumably at a step following PIC formation. {ECO:0000269|PubMed:34671025, ECO:0000269|PubMed:3...
Homo sapiens (Human)
O15455
TLR3_HUMAN
MRQTLPCIYFWGGLLPFGMLCASSTTKCTVSHEVADCSHLKLTQVPDDLPTNITVLNLTHNQLRRLPAANFTRYSQLTSLDVGFNTISKLEPELCQKLPMLKVLNLQHNELSQLSDKTFAFCTNLTELHLMSNSIQKIKNNPFVKQKNLITLDLSHNGLSSTKLGTQVQLENLQELLLSNNKIQALKSEELDIFANSSLKKLELSSNQIKEFSPGCFHAIGRLFGLFLNNVQLGPSLTEKLCLELANTSIRNLSLSNSQLSTTSNTTFLGLKWTNLTMLDLSYNNLNVVGNDSFAWLPQLEYFFLEYNNIQHLFSHSLHG...
null
null
activation of NF-kappaB-inducing kinase activity [GO:0007250]; cellular response to exogenous dsRNA [GO:0071360]; cellular response to interferon-beta [GO:0035458]; cellular response to mechanical stimulus [GO:0071260]; cellular response to type II interferon [GO:0071346]; cellular response to virus [GO:0098586]; cellu...
cytoplasm [GO:0005737]; early endosome [GO:0005769]; endolysosome membrane [GO:0036020]; endoplasmic reticulum membrane [GO:0005789]; endosome membrane [GO:0010008]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; Golgi membrane [GO:0000139]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; ...
double-stranded RNA binding [GO:0003725]; identical protein binding [GO:0042802]; pattern recognition receptor activity [GO:0038187]; signaling receptor activity [GO:0038023]; transmembrane signaling receptor activity [GO:0004888]
PF13516;PF13855;PF01582;PF17968;
3.80.10.10;3.40.50.10140;
Toll-like receptor family
PTM: Heavily N-glycosylated, except on that part of the surface of the ectodomain that is involved in ligand binding. {ECO:0000269|PubMed:15961631, ECO:0000269|PubMed:16043704, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:22579623}.; PTM: TLR3 signaling requires a proteolytic cleavage mediated by cathepsins CTSB and...
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein. Endosome membrane. Early endosome {ECO:0000269|PubMed:25736436}.
null
null
null
null
null
FUNCTION: Key component of innate and adaptive immunity. TLRs (Toll-like receptors) control host immune response against pathogens through recognition of molecular patterns specific to microorganisms. TLR3 is a nucleotide-sensing TLR which is activated by double-stranded RNA, a sign of viral infection. Acts via the ada...
Homo sapiens (Human)
O15457
MSH4_HUMAN
MLRPEISSTSPSAPAVSPSSGETRSPQGPRYNFGLQETPQSRPSVQVVSASTCPGTSGAAGDRSSSSSSLPCPAPNSRPAQGSYFGNKRAYAENTVASNFTFGASSSSARDTNYPQTLKTPLSTGNPQRSGYKSWTPQVGYSASSSSAISAHSPSVIVAVVEGRGLARGEIGMASIDLKNPQIILSQFADNTTYAKVITKLKILSPLEIIMSNTACAVGNSTKLFTLITENFKNVNFTTIQRKYFNETKGLEYIEQLCIAEFSTVLMEVQSKYYCLAAVAALLKYVEFIQNSVYAPKSLKICFQGSEQTAMIDSSSAQNL...
null
null
female gamete generation [GO:0007292]; homologous chromosome pairing at meiosis [GO:0007129]; mismatch repair [GO:0006298]; ovarian follicle development [GO:0001541]; reciprocal meiotic recombination [GO:0007131]; spermatogenesis [GO:0007283]
chromosome [GO:0005694]; nucleus [GO:0005634]; recombination nodule [GO:0005713]; synaptonemal complex [GO:0000795]
ATP binding [GO:0005524]; ATP-dependent DNA damage sensor activity [GO:0140664]; DNA binding [GO:0003677]; double-stranded DNA binding [GO:0003690]; mismatched DNA binding [GO:0030983]
PF05188;PF05192;PF05190;PF00488;
1.10.1420.10;3.30.420.110;3.40.50.300;
DNA mismatch repair MutS family
null
SUBCELLULAR LOCATION: Chromosome {ECO:0000250|UniProtKB:Q99MT2}.
null
null
null
null
null
FUNCTION: Involved in meiotic recombination. Required for reciprocal recombination and proper segregation of homologous chromosomes at meiosis.
Homo sapiens (Human)
O15460
P4HA2_HUMAN
MKLWVSALLMAWFGVLSCVQAEFFTSIGHMTDLIYAEKELVQSLKEYILVEEAKLSKIKSWANKMEALTSKSAADAEGYLAHPVNAYKLVKRLNTDWPALEDLVLQDSAAGFIANLSVQRQFFPTDEDEIGAAKALMRLQDTYRLDPGTISRGELPGTKYQAMLSVDDCFGMGRSAYNEGDYYHTVLWMEQVLKQLDAGEEATTTKSQVLDYLSYAVFQLGDLHRALELTRRLLSLDPSHERAGGNLRYFEQLLEEEREKTLTNQTEAELATPEGIYERPVDYLPERDVYESLCRGEGVKLTPRRQKRLFCRYHHGNRAP...
1.14.11.2
COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000255|PROSITE-ProRule:PRU00805}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-ProRule:PRU00805}; COFACTOR: Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000305|PubMed:9211872};
null
cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; intracellular membrane-bounded organelle [GO:0043231]; nucleoplasm [GO:0005654]
electron transfer activity [GO:0009055]; iron ion binding [GO:0005506]; L-ascorbic acid binding [GO:0031418]; procollagen-proline 4-dioxygenase activity [GO:0004656]
PF13640;PF08336;
6.10.140.1460;2.60.120.620;1.25.40.10;
P4HA family
null
SUBCELLULAR LOCATION: Endoplasmic reticulum lumen.
CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-prolyl-[collagen] + O2 = CO2 + succinate + trans-4-hydroxy-L-prolyl-[collagen]; Xref=Rhea:RHEA:18945, Rhea:RHEA-COMP:11676, Rhea:RHEA-COMP:11680, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:50342, ChEBI:CHEBI:61965; EC=1.14.11.2...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=22 uM for 2-oxoglutarate {ECO:0000269|PubMed:9211872};
null
null
null
FUNCTION: Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins. {ECO:0000269|PubMed:9211872}.
Homo sapiens (Human)
O15466
SIA8E_HUMAN
MRYADPSANRDLLGSRTLLFIFICAFALVTLLQQILYGRNYIKRYFEFYEGPFEYNSTRCLELRHEILEVKVLSMVKQSELFDRWKSLQMCKWAMNISEANQFKSTLSRCCNAPAFLFTTQKNTPLGTKLKYEVDTSGIYHINQEIFRMFPKDMPYYRSQFKKCAVVGNGGILKNSRCGREINSADFVFRCNLPPISEKYTMDVGVKTDVVTVNPSIITERFHKLEKWRRPFYRVLQVYENASVLLPAFYNTRNTDVSIRVKYVLDDFESPQAVYYFHPQYLVNVSRYWLSLGVRAKRISTGLILVTAALELCEEVHLFG...
2.4.99.-
null
carbohydrate metabolic process [GO:0005975]; glycosphingolipid biosynthetic process [GO:0006688]; N-glycan processing [GO:0006491]; oligosaccharide metabolic process [GO:0009311]; protein glycosylation [GO:0006486]
Golgi membrane [GO:0000139]
alpha-N-acetylneuraminate alpha-2,8-sialyltransferase activity [GO:0003828]; sialyltransferase activity [GO:0008373]
PF00777;
3.90.1480.20;
Glycosyltransferase 29 family
null
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q6ZXC8}; Single-pass type II membrane protein {ECO:0000255}.
CATALYTIC ACTIVITY: [Isoform 1]: Reaction=a ganglioside GT1b (d18:1(4E)) + CMP-N-acetyl-beta-neuraminate = a ganglioside GQ1b (d18:1(4E)) + CMP + H(+); Xref=Rhea:RHEA:41772, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:78452, ChEBI:CHEBI:78455; Evidence={ECO:0000269|PubMed:9199191}; Physiologica...
null
PATHWAY: Protein modification; protein glycosylation. {ECO:0000269|PubMed:9199191}.
null
null
FUNCTION: Involved in the synthesis of gangliosides GD1c, GT1a, GQ1b, GP1c and GT3 from GD1a, GT1b, GM1b and GD3 respectively. {ECO:0000269|PubMed:9199191}.
Homo sapiens (Human)
O15467
CCL16_HUMAN
MKVSEAALSLLVLILIITSASRSQPKVPEWVNTPSTCCLKYYEKVLPRRLVVGYRKALNCHLPAIIFVTKRNREVCTNPNDDWVQEYIKDPNLPLLPTRNLSTVKIITAKNGQPQLLNSQ
null
null
cell communication [GO:0007154]; cell-cell signaling [GO:0007267]; cellular response to interleukin-1 [GO:0071347]; cellular response to tumor necrosis factor [GO:0071356]; cellular response to type II interferon [GO:0071346]; chemokine-mediated signaling pathway [GO:0070098]; chemotaxis [GO:0006935]; eosinophil chemot...
extracellular region [GO:0005576]; extracellular space [GO:0005615]
CCR chemokine receptor binding [GO:0048020]; chemoattractant activity [GO:0042056]; chemokine activity [GO:0008009]
PF00048;
2.40.50.40;
Intercrine beta (chemokine CC) family
null
SUBCELLULAR LOCATION: Secreted.
null
null
null
null
null
FUNCTION: Shows chemotactic activity for lymphocytes and monocytes but not neutrophils. Also shows potent myelosuppressive activity, suppresses proliferation of myeloid progenitor cells. Recombinant SCYA16 shows chemotactic activity for monocytes and THP-1 monocytes, but not for resting lymphocytes and neutrophils. Ind...
Homo sapiens (Human)
O15479
MAGB2_HUMAN
MPRGQKSKLRAREKRRKARDETRGLNVPQVTEAEEEEAPCCSSSVSGGAASSSPAAGIPQEPQRAPTTAAAAAAGVSSTKSKKGAKSHQGEKNASSSQASTSTKSPSEDPLTRKSGSLVQFLLYKYKIKKSVTKGEMLKIVGKRFREHFPEILKKASEGLSVVFGLELNKVNPNGHTYTFIDKVDLTDEESLLSSWDFPRRKLLMPLLGVIFLNGNSATEEEIWEFLNMLGVYDGEEHSVFGEPWKLITKDLVQEKYLEYKQVPSSDPPRFQFLWGPRAYAETSKMKVLEFLAKVNGTTPCAFPTHYEEALKDEEKAGV
null
null
negative regulation of transcription by RNA polymerase II [GO:0000122]
nucleus [GO:0005634]
null
PF01454;PF12440;
1.10.10.1200;1.10.10.1210;
null
null
null
null
null
null
null
null
FUNCTION: May enhance ubiquitin ligase activity of RING-type zinc finger-containing E3 ubiquitin-protein ligases. Proposed to act through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate complex. {ECO:0000269|PubMed:20864041}.
Homo sapiens (Human)
O15481
MAGB4_HUMAN
MPRGQKSKLRAREKRQRTRGQTQDLKVGQPTAAEKEESPSSSSSVLRDTASSSLAFGIPQEPQREPPTTSAAAAMSCTGSDKGDESQDEENASSSQASTSTERSLKDSLTRKTKMLVQFLLYKYKMKEPTTKAEMLKIISKKYKEHFPEIFRKVSQRTELVFGLALKEVNPTTHSYILVSMLGPNDGNQSSAWTLPRNGLLMPLLSVIFLNGNCAREEEIWEFLNMLGIYDGKRHLIFGEPRKLITQDLVQEKYLEYQQVPNSDPPRYQFLWGPRAHAETSKMKVLEFLAKVNDTTPNNFPLLYEEALRDEEERAGARPR...
null
null
negative regulation of transcription by RNA polymerase II [GO:0000122]
cytoplasm [GO:0005737]; nucleus [GO:0005634]
null
PF01454;PF12440;
1.10.10.1200;1.10.10.1210;
null
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A2A9R3}.
null
null
null
null
null
null
Homo sapiens (Human)
O15484
CAN5_HUMAN
MFSCVKPYEDQNYSALRRDCRRRKVLFEDPLFPATDDSLYYKGTPGPAVRWKRPKGICEDPRLFVDGISSHDLHQGQVGNCWFVAACSSLASRESLWQKVIPDWKEQEWDPEKPNAYAGIFHFHFWRFGEWVDVVIDDRLPTVNNQLIYCHSNSRNEFWCALVEKAYAKLAGCYQALDGGNTADALVDFTGGVSEPIDLTEGDFANDETKRNQLFERMLKVHSRGGLISASIKAVTAADMEARLACGLVKGHAYAVTDVRKVRLGHGLLAFFKSEKLDMIRLRNPWGEREWNGPWSDTSEEWQKVSKSEREKMGVTVQDD...
3.4.22.-
null
proteolysis [GO:0006508]; signal transduction [GO:0007165]
cell surface [GO:0009986]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; synapse [GO:0045202]
calcium-dependent cysteine-type endopeptidase activity [GO:0004198]
PF00168;PF01067;PF00648;
2.60.120.380;2.60.40.150;3.90.70.10;
Peptidase C2 family
null
null
null
null
null
null
null
FUNCTION: Calcium-regulated non-lysosomal thiol-protease. {ECO:0000250}.
Homo sapiens (Human)
O15488
GLYG2_HUMAN
MSETEFHHGAQAGLELLRSSNSPTSASQSAGMTVTDQAFVTLATNDIYCQGALVLGQSLRRHRLTRKLVVLITPQVSSLLRVILSKVFDEVIEVNLIDSADYIHLAFLKRPELGLTLTKLHCWTLTHYSKCVFLDADTLVLSNVDELFDRGEFSAAPDPGWPDCFNSGVFVFQPSLHTHKLLLQHAMEHGSFDGADQGLLNSFFRNWSTTDIHKHLPFIYNLSSNTMYTYSPAFKQFGSSAKVVHFLGSMKPWNYKYNPQSGSVLEQGSASSSQHQAAFLHLWWTVYQNNVLPLYKSVQAGEARASPGHTLCHSDVGGPC...
2.4.1.186
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P46976};
glycogen biosynthetic process [GO:0005978]
cytoplasm [GO:0005737]; cytosol [GO:0005829]
glycogenin glucosyltransferase activity [GO:0008466]; glycosyltransferase activity [GO:0016757]; metal ion binding [GO:0046872]; UDP-alpha-D-glucose:glucosyl-glycogenin alpha-D-glucosyltransferase activity [GO:0102751]
PF01501;
null
Glycosyltransferase 8 family, Glycogenin subfamily
PTM: Self-glycosylated by the transfer of glucose residues from UDP-glucose to itself, forming an alpha-1,4-glycan of around 10 residues attached to Tyr-228. {ECO:0000269|PubMed:9857012}.
null
CATALYTIC ACTIVITY: Reaction=L-tyrosyl-[glycogenin] + UDP-alpha-D-glucose = alpha-D-glucosyl-L-tyrosyl-[glycogenin] + H(+) + UDP; Xref=Rhea:RHEA:23360, Rhea:RHEA-COMP:14604, Rhea:RHEA-COMP:14605, ChEBI:CHEBI:15378, ChEBI:CHEBI:46858, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:140573; EC=2.4.1.186; Evidence={ECO:...
null
PATHWAY: Glycan biosynthesis; glycogen biosynthesis. {ECO:0000269|PubMed:9346895, ECO:0000269|PubMed:9857012}.
null
null
FUNCTION: Glycogenin participates in the glycogen biosynthetic process along with glycogen synthase and glycogen branching enzyme. It self-glucosylates, via an inter-subunit mechanism, to form an oligosaccharide primer that serves as substrate for glycogen synthase. {ECO:0000269|PubMed:9346895, ECO:0000269|PubMed:98570...
Homo sapiens (Human)
O15492
RGS16_HUMAN
MCRTLAAFPTTCLERAKEFKTRLGIFLHKSELGCDTGSTGKFEWGSKHSKENRNFSEDVLGWRESFDLLLSSKNGVAAFHAFLKTEFSEENLEFWLACEEFKKIRSATKLASRAHQIFEEFICSEAPKEVNIDHETHELTRMNLQTATATCFDAAQGKTRTLMEKDSYPRFLKSPAYRDLAAQASAASATLSSCSLDEPSHT
null
null
G protein-coupled receptor signaling pathway [GO:0007186]; negative regulation of signal transduction [GO:0009968]; positive regulation of GTPase activity [GO:0043547]; regulation of G protein-coupled receptor signaling pathway [GO:0008277]; visual perception [GO:0007601]
cytoplasm [GO:0005737]; membrane [GO:0016020]; plasma membrane [GO:0005886]
calmodulin binding [GO:0005516]; GTPase activator activity [GO:0005096]; GTPase activity [GO:0003924]
PF00615;
1.10.196.10;1.10.167.10;
null
PTM: Palmitoylated on Cys-2 and/or Cys-12. {ECO:0000250|UniProtKB:P97428}.; PTM: Phosphorylated. Phosphorylation at Tyr-168 by EGFR enhances GTPase accelerating (GAP) activity toward GNAI1. {ECO:0000269|PubMed:11602604}.
SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P97428}; Lipid-anchor {ECO:0000250|UniProtKB:P97428}.
null
null
null
null
null
FUNCTION: Regulates G protein-coupled receptor signaling cascades. Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form (PubMed:11602604, PubMed:18434541). Plays an important role in the phototransduction cascade by regulatin...
Homo sapiens (Human)
O15496
PA2GX_HUMAN
MGPLPVCLPIMLLLLLPSLLLLLLLPGPGSGEASRILRVHRRGILELAGTVGCVGPRTPIAYMKYGCFCGLGGHGQPRDAIDWCCHGHDCCYTRAEEAGCSPKTERYSWQCVNQSVLCGPAENKCQELLCKCDQEIANCLAQTEYNLKYLFYPQFLCEPDSPKCD
3.1.1.4
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:12161451, ECO:0000269|PubMed:9188469}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:12161451};
arachidonic acid metabolic process [GO:0019369]; arachidonic acid secretion [GO:0050482]; axon guidance [GO:0007411]; cellular response to leukemia inhibitory factor [GO:1990830]; cholesterol homeostasis [GO:0042632]; defense response to virus [GO:0051607]; erythrocyte maturation [GO:0043249]; fertilization [GO:0009566...
acrosomal vesicle [GO:0001669]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; lysosome [GO:0005764]
1-alkyl-2-acetylglycerophosphocholine esterase activity [GO:0003847]; calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipase A2 activity [GO:0004623]; phospholipase activity [GO:0004620]; phospholipid binding [GO:0005543]
PF00068;
1.20.90.10;
Phospholipase A2 family
null
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9188469}. Lysosome {ECO:0000250|UniProtKB:Q9QXX3}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250|UniProtKB:Q9QXX3}.
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0...
null
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.4. {ECO:0000269|PubMed:9188469};
null
FUNCTION: Secretory calcium-dependent phospholipase A2 that primarily targets extracellular phospholipids (PubMed:12021277, PubMed:9188469). Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids with preference for phosphatidylcholines and phosphatidylglycerols over phosphatidylet...
Homo sapiens (Human)
O15498
YKT6_HUMAN
MKLYSLSVLYKGEAKVVLLKAAYDVSSFSFFQRSSVQEFMTFTSQLIVERSSKGTRASVKEQDYLCHVYVRNDSLAGVVIADNEYPSRVAFTLLEKVLDEFSKQVDRIDWPVGSPATIHYPALDGHLSRYQNPREADPMTKVQAELDETKIILHNTMESLLERGEKLDDLVSKSEVLGTQSKAFYKTARKQNSCCAIM
2.3.1.-
null
endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; protein transport [GO:0015031]; retrograde transport, endosome to Golgi [GO:0042147]; vesicle docking involved in exocytosis [GO:0006904]; vesicle targeting [GO:0006903]
apical dendrite [GO:0097440]; basal dendrite [GO:0097441]; cytoplasm [GO:0005737]; cytoplasmic vesicle membrane [GO:0030659]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; endosome [GO:0005768]; Golgi apparatus [GO:0005794]; Golgi m...
cadherin binding [GO:0045296]; protein-cysteine S-palmitoyltransferase activity [GO:0019706]; SNAP receptor activity [GO:0005484]
PF13774;PF00957;
1.20.5.110;3.30.450.50;
Synaptobrevin family
PTM: Palmitoylated; catalyzes its own palmitoylation. Palmitoylation is required for Golgi targeting. {ECO:0000269|PubMed:15044687, ECO:0000269|PubMed:15479160}.; PTM: Farnesylation is required for Golgi targeting.
SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cytoplasmic vesicle membrane; Lipid-anchor; Cytoplasmic side. Golgi apparatus membrane; Lipid-anchor; Cytoplasmic side. Note=Probably cycles through vesicles between Golgi and endosomes.
null
null
null
null
null
FUNCTION: Vesicular soluble NSF attachment protein receptor (v-SNARE) mediating vesicle docking and fusion to a specific acceptor cellular compartment. Functions in endoplasmic reticulum to Golgi transport; as part of a SNARE complex composed of GOSR1, GOSR2 and STX5. Functions in early/recycling endosome to TGN transp...
Homo sapiens (Human)
O15499
GSC2_HUMAN
MAAAAGGAASRRGAGRPCPFSIEHILSSLPERSLPARAACPPQPAGRQSPAKPEEPGAPEAAPCACCCCCGPRAAPCGPPEAAAGLGARLAWPLRLGPAVPLSLGAPAGGSGALPGAVGPGSQRRTRRHRTIFSEEQLQALEALFVQNQYPDVSTRERLAGRIRLREERVEVWFKNRRAKWRHQKRASASARLLPGVKKSPKGSC
null
null
anatomical structure morphogenesis [GO:0009653]; regulation of transcription by RNA polymerase II [GO:0006357]
chromatin [GO:0000785]; nucleus [GO:0005634]
DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]; sequence-specific double-s...
PF00046;
1.10.10.60;
Paired homeobox family, Bicoid subfamily
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
null
null
null
null
null
FUNCTION: May have a role in development. May regulate its own transcription. May bind the bicoid consensus sequence TAATCC.
Homo sapiens (Human)
O15503
INSI1_HUMAN
MPRLHDHFWSCSCAHSARRRGPPRASAAGLAAKVGEMINVSVSGPSLLAAHGAPDADPAPRGRSAAMSGPEPGSPYPNTWHHRLLQRSLVLFSVGVVLALVLNLLQIQRNVTLFPEEVIATIFSSAWWVPPCCGTAAAVVGLLYPCIDSHLGEPHKFKREWASVMRCIAVFVGINHASAKLDFANNVQLSLTLAALSLGLWWTFDRSRSGLGLGITIAFLATLITQFLVYNGVYQYTSPDFLYIRSWLPCIFFSGGVTVGNIGRQLAMGVPEKPHSD
null
null
cellular response to insulin stimulus [GO:0032869]; cellular response to sterol [GO:0036315]; cholesterol biosynthetic process [GO:0006695]; cholesterol homeostasis [GO:0042632]; cranial suture morphogenesis [GO:0060363]; inner ear morphogenesis [GO:0042472]; middle ear morphogenesis [GO:0042474]; negative regulation o...
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; SREBP-SCAP-Insig complex [GO:0032937]
oxysterol binding [GO:0008142]; protein sequestering activity [GO:0140311]
PF07281;
null
INSIG family
PTM: Phosphorylation at Ser-207 by PCK1 reduces binding to oxysterol, disrupting the interaction between INSIG1 and SCAP, thereby promoting nuclear translocation of SREBP proteins (SREBF1/SREBP1 or SREBF2/SREBP2) and subsequent transcription of downstream lipogenesis-related genes. {ECO:0000269|PubMed:32322062}.; PTM: ...
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12202038, ECO:0000269|PubMed:32322062}; Multi-pass membrane protein {ECO:0000269|PubMed:12202038}.
null
null
null
null
null
FUNCTION: Oxysterol-binding protein that mediates feedback control of cholesterol synthesis by controlling both endoplasmic reticulum to Golgi transport of SCAP and degradation of HMGCR (PubMed:12202038, PubMed:12535518, PubMed:16168377, PubMed:16399501, PubMed:16606821, PubMed:32322062). Acts as a negative regulator o...
Homo sapiens (Human)
O15504
NUP42_HUMAN
MAICQFFLQGRCRFGDRCWNEHPGARGAGGGRQQPQQQPSGNNRRGWNTTSQRYSNVIQPSSFSKSTPWGGSRDQEKPYFSSFDSGASTNRKEGFGLSENPFASLSPDEQKDEKKLLEGIVKDMEVWESSGQWMFSVYSPVKKKPNISGFTDISPEELRLEYHNFLTSNNLQSYLNSVQRLINQWRNRVNELKSLNISTKVALLSDVKDGVNQAAPAFGFGSSQAATFMSPGFPVNNSSSDNAQNFSFKTNSGFAAASSGSPAGFGSSPAFGAAASTSSGISTSAPAFGFGKPEVTSAASFSFKSPAASSFGSPGFSGLP...
null
null
mRNA transport [GO:0051028]; nucleocytoplasmic transport [GO:0006913]; protein export from nucleus [GO:0006611]
cytosol [GO:0005829]; nuclear envelope [GO:0005635]; nuclear membrane [GO:0031965]; nuclear pore [GO:0005643]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
metal ion binding [GO:0046872]; nuclear export signal receptor activity [GO:0005049]; RNA binding [GO:0003723]
PF18044;
null
null
PTM: O-glycosylated. {ECO:0000269|PubMed:10358091}.
SUBCELLULAR LOCATION: Nucleus, nuclear pore complex {ECO:0000269|PubMed:12228227, ECO:0000269|PubMed:16000379}. Nucleus membrane {ECO:0000269|PubMed:12228227, ECO:0000269|PubMed:16000379}; Peripheral membrane protein; Cytoplasmic side {ECO:0000269|PubMed:12228227}. Note=Excluded from the nucleolus. {ECO:0000269|PubMed:...
null
null
null
null
null
FUNCTION: Required for the export of mRNAs containing poly(A) tails from the nucleus into the cytoplasm. {ECO:0000269|PubMed:10610322, ECO:0000269|PubMed:16000379}.; FUNCTION: (Microbial infection) In case of infection by HIV-1, it may participate in the docking of viral Vpr at the nuclear envelope. {ECO:0000269|PubMed...
Homo sapiens (Human)
O15511
ARPC5_HUMAN
MSKNTVSSARFRKVDVDEYDENKFVDEEDGGDGQAGPDEGEVDSCLRQGNMTAALQAALKNPPINTKSQAVKDRAGSIVLKVLISFKANDIEKAVQSLDKNGVDLLMKYIYKGFESPSDNSSAMLLQWHEKALAAGGVGSIVRVLTARKTV
null
null
actin cytoskeleton organization [GO:0030036]; Arp2/3 complex-mediated actin nucleation [GO:0034314]; cell migration [GO:0016477]; regulation of actin filament polymerization [GO:0030833]
actin cytoskeleton [GO:0015629]; Arp2/3 protein complex [GO:0005885]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; ficolin-1-rich granule lumen [GO:1904813]; focal adhesion [GO:0005925]; lamellipodium [GO:0030027]; nucleus [GO:0005634]; secretory g...
actin filament binding [GO:0051015]; structural constituent of cytoskeleton [GO:0005200]
PF04699;
1.25.40.190;
ARPC5 family
PTM: Polyubiquitinated by RNF128 with 'Lys-63'-linked chains, leading to proteasomal degradation. {ECO:0000269|PubMed:22016387}.
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9230079}. Cell projection {ECO:0000269|PubMed:9230079}. Nucleus {ECO:0000269|PubMed:29925947, ECO:0000269|PubMed:37349293}.
null
null
null
null
null
FUNCTION: Component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF) (PubMed:9230079). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility (PubMed:9230079). In a...
Homo sapiens (Human)
O15514
RPB4_HUMAN
MAAGGSDPRAGDVEEDASQLIFPKEFETAETLLNSEVHMLLEHRKQQNESAEDEQELSEVFMKTLNYTARFSRFKNRETIASVRSLLLQKKLHKFELACLANLCPETAEESKALIPSLEGRFEDEELQQILDDIQTKRSFQY
null
null
recruitment of 3'-end processing factors to RNA polymerase II holoenzyme complex [GO:0034402]; transcription by RNA polymerase II [GO:0006366]; transcription initiation at RNA polymerase II promoter [GO:0006367]
cytosol [GO:0005829]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA polymerase II, core complex [GO:0005665]
nucleotide binding [GO:0000166]; translation initiation factor binding [GO:0031369]
PF03874;
1.20.1250.40;
Eukaryotic RPB4 RNA polymerase subunit family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9852112}.
null
null
null
null
null
FUNCTION: Core component of RNA polymerase II (Pol II), a DNA-dependent RNA polymerase which synthesizes mRNA precursors and many functional non-coding RNAs using the four ribonucleoside triphosphates as substrates. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed o...
Homo sapiens (Human)
O15516
CLOCK_HUMAN
MLFTVSCSKMSSIVDRDDSSIFDGLVEEDDKDKAKRVSRNKSEKKRRDQFNVLIKELGSMLPGNARKMDKSTVLQKSIDFLRKHKEITAQSDASEIRQDWKPTFLSNEEFTQLMLEALDGFFLAIMTDGSIIYVSESVTSLLEHLPSDLVDQSIFNFIPEGEHSEVYKILSTHLLESDSLTPEYLKSKNQLEFCCHMLRGTIDPKEPSTYEYVKFIGNFKSLNSVSSSAHNGFEGTIQRTHRPSYEDRVCFVATVRLATPQFIKEMCTVEEPNEEFTSRHSLEWKFLFLDHRAPPIIGYLPFEVLGTSGYDYYHVDDLEN...
2.3.1.48
null
cellular response to ionizing radiation [GO:0071479]; circadian regulation of gene expression [GO:0032922]; circadian rhythm [GO:0007623]; DNA damage checkpoint signaling [GO:0000077]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of glucocorticoid receptor signaling pathway [GO:2...
chromatin [GO:0000785]; chromatoid body [GO:0033391]; chromosome [GO:0005694]; CLOCK-BMAL transcription complex [GO:1990513]; cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
chromatin DNA binding [GO:0031490]; 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]; E-box binding [GO:0070888]; his...
PF00010;PF00989;PF14598;
4.10.280.10;3.30.450.20;
null
PTM: Ubiquitinated, leading to its proteasomal degradation. {ECO:0000250|UniProtKB:O08785}.; PTM: O-glycosylated; contains O-GlcNAc. O-glycosylation by OGT prevents protein degradation by inhibiting ubiquitination. It also stabilizes the CLOCK-BMAL1 heterodimer thereby increasing CLOCK-BMAL1-mediated transcriptional ac...
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14645221, ECO:0000269|PubMed:23160374, ECO:0000269|PubMed:28985504}. Cytoplasm {ECO:0000250|UniProtKB:O08785}. Cytoplasm, cytosol {ECO:0000269|PubMed:28985504}. Note=Shuttling between the cytoplasm and the nucleus is under circadian regulation and is BMAL1-dependent. Ph...
CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
null
null
null
null
FUNCTION: Transcriptional activator which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism a...
Homo sapiens (Human)
O15519
CFLAR_HUMAN
MSAEVIHQVEEALDTDEKEMLLFLCRDVAIDVVPPNVRDLLDILRERGKLSVGDLAELLYRVRRFDLLKRILKMDRKAVETHLLRNPHLVSDYRVLMAEIGEDLDKSDVSSLIFLMKDYMGRGKISKEKSFLDLVVELEKLNLVAPDQLDLLEKCLKNIHRIDLKTKIQKYKQSVQGAGTSYRNVLQAAIQKSLKDPSNNFRLHNGRSKEQRLKEQLGAQQEPVKKSIQESEAFLPQSIPEERYKMKSKPLGICLIIDCIGNETELLRDTFTSLGYEVQKFLHLSMHGISQILGQFACMPEHRDYDSFVCVLVSRGGSQS...
null
null
apoptotic process [GO:0006915]; cellular response to dexamethasone stimulus [GO:0071549]; cellular response to epidermal growth factor stimulus [GO:0071364]; cellular response to estradiol stimulus [GO:0071392]; cellular response to hypoxia [GO:0071456]; cellular response to insulin stimulus [GO:0032869]; cellular resp...
CD95 death-inducing signaling complex [GO:0031265]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; death-inducing signaling complex [GO:0031264]; ripoptosome [GO:0097342]
cysteine-type endopeptidase activity involved in apoptotic signaling pathway [GO:0097199]; cysteine-type endopeptidase activity involved in execution phase of apoptosis [GO:0097200]; death receptor binding [GO:0005123]; enzyme activator activity [GO:0008047]; protease binding [GO:0002020]; protein-containing complex bi...
PF01335;PF00656;
3.40.50.1460;1.10.533.10;
Peptidase C14A family
PTM: Proteolytically processed by CASP8 generating subunit p43 and p12. {ECO:0000269|PubMed:9228018}.
null
null
null
null
null
null
FUNCTION: Apoptosis regulator protein which may function as a crucial link between cell survival and cell death pathways in mammalian cells. Acts as an inhibitor of TNFRSF6 mediated apoptosis. A proteolytic fragment (p43) is likely retained in the death-inducing signaling complex (DISC) thereby blocking further recruit...
Homo sapiens (Human)
O15520
FGF10_HUMAN
MWKWILTHCASAFPHLPGCCCCCFLLLFLVSSVPVTCQALGQDMVSPEATNSSSSSFSSPSSAGRHVRSYNHLQGDVRWRKLFSFTKYFLKIEKNGKVSGTKKENCPYSILEITSVEIGVVAVKAINSNYYLAMNKKGKLYGSKEFNNDCKLKERIEENGYNTYASFNWQHNGRQMYVALNGKGAPRRGQKTRRKNTSAHFLPMVVHS
null
null
actin cytoskeleton organization [GO:0030036]; angiogenesis [GO:0001525]; animal organ morphogenesis [GO:0009887]; blood vessel remodeling [GO:0001974]; branch elongation involved in salivary gland morphogenesis [GO:0060667]; branching morphogenesis of an epithelial tube [GO:0048754]; bronchiole morphogenesis [GO:006043...
cell surface [GO:0009986]; cytoplasm [GO:0005737]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
chemoattractant activity [GO:0042056]; fibroblast growth factor receptor binding [GO:0005104]; growth factor activity [GO:0008083]; heparin binding [GO:0008201]; type 2 fibroblast growth factor receptor binding [GO:0005111]
PF00167;
2.80.10.50;
Heparin-binding growth factors family
null
SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
null
null
null
null
null
FUNCTION: Plays an important role in the regulation of embryonic development, cell proliferation and cell differentiation. Required for normal branching morphogenesis. May play a role in wound healing. {ECO:0000269|PubMed:16597617}.
Homo sapiens (Human)
O15522
NKX28_HUMAN
MATSGRLSFTVRSLLDLPEQDAQHLPRREPEPRAPQPDPCAAWLDSERGHYPSSDESSLETSPPDSSQRPSARPASPGSDAEKRKKRRVLFSKAQTLELERRFRQQRYLSAPEREQLASLLRLTPTQVKIWFQNHRYKLKRARAPGAAESPDLAASAELHAAPGLLRRVVVPVLVRDGQPCGGGGGGEVGTAAAQEKCGAPPAAACPLPGYPAFGPGSALGLFPAYQHLASPALVSWNW
null
null
axonogenesis [GO:0007409]; cell differentiation [GO:0030154]; DNA-templated transcription [GO:0006351]; epithelial cell proliferation [GO:0050673]; liver development [GO:0001889]; lung development [GO:0030324]; negative regulation of epithelial cell proliferation [GO:0050680]; positive regulation of transcription by RN...
chromatin [GO:0000785]; 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]; double-stranded DNA binding [GO:0003690]; RNA polymerase II cis-regulatory region sequence-sp...
PF00046;
1.10.10.60;
NK-2 homeobox family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
null
null
null
null
null
null
Homo sapiens (Human)
O15523
DDX3Y_HUMAN
MSHVVVKNDPELDQQLANLDLNSEKQSGGASTASKGRYIPPHLRNREASKGFHDKDSSGWSCSKDKDAYSSFGSRDSRGKPGYFSERGSGSRGRFDDRGRSDYDGIGNRERPGFGRFERSGHSRWCDKSVEDDWSKPLPPSERLEQELFSGGNTGINFEKYDDIPVEATGSNCPPHIENFSDIDMGEIIMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDGPGEALKAVKENGRYGRRKQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVA...
3.6.4.13
null
cell differentiation [GO:0030154]; gamete generation [GO:0007276]; negative regulation of gene expression [GO:0010629]
cytosol [GO:0005829]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; P granule [GO:0043186]
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; mRNA binding [GO:0003729]; RNA helicase activity [GO:0003724]
PF00270;PF00271;
3.40.50.300;
DEAD box helicase family, DDX3/DED1 subfamily
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15294876, ECO:0000269|PubMed:15383328}. Nucleus {ECO:0000269|PubMed:15383328}. Note=Shuttles between the nucleus and the cytoplasm in an XPO1-dependent manner.
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: Probable ATP-dependent RNA helicase. During immune response, may enhance IFNB1 expression via IRF3/IRF7 pathway (By similarity). {ECO:0000250|UniProtKB:Q62095}.
Homo sapiens (Human)
O15524
SOCS1_HUMAN
MVAHNQVAADNAVSTAAEPRRRPEPSSSSSSSPAAPARPRPCPAVPAPAPGDTHFRTFRSHADYRRITRASALLDACGFYWGPLSVHGAHERLRAEPVGTFLVRDSRQRNCFFALSVKMASGPTSIRVHFQAGRFHLDGSRESFDCLFELLEHYVAAPRRMLGAPLRQRRVRPLQELCRQRIVATVGRENLARIPLNPVLRDYLSSFPFQI
null
null
cellular response to amino acid stimulus [GO:0071230]; cytokine-mediated signaling pathway [GO:0019221]; fat cell differentiation [GO:0045444]; intracellular signal transduction [GO:0035556]; macrophage differentiation [GO:0030225]; negative regulation of CD8-positive, alpha-beta T cell differentiation [GO:0043377]; ne...
cytoplasm [GO:0005737]; cytoplasmic ribonucleoprotein granule [GO:0036464]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; phosphatidylinositol 3-kinase complex [GO:0005942]
1-phosphatidylinositol-3-kinase regulator activity [GO:0046935]; insulin-like growth factor receptor binding [GO:0005159]; kinase inhibitor activity [GO:0019210]; protein kinase binding [GO:0019901]; protein kinase inhibitor activity [GO:0004860]
PF00017;PF07525;
3.30.505.10;1.10.750.20;
SOCS1 family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16410555}. Cytoplasmic vesicle {ECO:0000269|PubMed:16410555}. Note=Detected in perinuclear cytoplasmic vesicles upon interaction with FGFR3.
null
null
PATHWAY: Protein modification; protein ubiquitination.
null
null
FUNCTION: Essential negative regulator of type I and type II interferon (IFN) signaling, as well as that of other cytokines, including IL2, IL4, IL6 and leukemia inhibitory factor (LIF) (PubMed:32499645, PubMed:33087723). Downregulates cytokine signaling by inhibiting the JAK/STAT signaling pathway. Acts by binding to ...
Homo sapiens (Human)
O15525
MAFG_HUMAN
MTTPNKGNKALKVKREPGENGTSLTDEELVTMSVRELNQHLRGLSKEEIVQLKQRRRTLKNRGYAASCRVKRVTQKEELEKQKAELQQEVEKLASENASMKLELDALRSKYEALQTFARTVARSPVAPARGPLAAGLGPLVPGKVAATSVITIVKSKTDARS
null
null
adult behavior [GO:0030534]; in utero embryonic development [GO:0001701]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of gene expression [GO:0010628]; regulation of cell population proliferation [GO:0042127]; regulation of epidermal cell differentiation [GO:0045604]; regu...
nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575]
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; identical protein binding [GO:0042802]; RNA polymerase II cis-regulatory region sequence-spec...
PF03131;
1.20.5.170;
BZIP family, Maf subfamily
PTM: Acetylated in erythroid cells by CREB-binding protein (CBP). Acetylation augments the DNA-binding activity of NFE2, but has no effect on binding NFE2. {ECO:0000269|PubMed:11154691}.; PTM: Sumoylation at Lys-14 is required for active transcriptional repression. {ECO:0000250|UniProtKB:O54790}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978, ECO:0000269|PubMed:11154691}.
null
null
null
null
null
FUNCTION: Since they lack a putative transactivation domain, the small Mafs behave as transcriptional repressors when they dimerize among themselves (PubMed:11154691). However, they seem to serve as transcriptional activators by dimerizing with other (usually larger) basic-zipper proteins, such as NFE2, NFE2L1 and NFE2...
Homo sapiens (Human)
O15527
OGG1_HUMAN
MPARALLPRRMGHRTLASTPALWASIPCPRSELRLDLVLPSGQSFRWREQSPAHWSGVLADQVWTLTQTEEQLHCTVYRGDKSQASRPTPDELEAVRKYFQLDVTLAQLYHHWGSVDSHFQEVAQKFQGVRLLRQDPIECLFSFICSSNNNIARITGMVERLCQAFGPRLIQLDDVTYHGFPSLQALAGPEVEAHLRKLGLGYRARYVSASARAILEEQGGLAWLQQLRESSYEEAHKALCILPGVGTKVADCICLMALDKPQAVPVDVHMWHIAQRDYSWHPTTSQAKGPSPQTNKELGNFFRSLWGPYAGWAQAVLFS...
3.2.2.-; 4.2.99.18
null
base-excision repair [GO:0006284]; base-excision repair, AP site formation [GO:0006285]; cellular response to cadmium ion [GO:0071276]; cellular response to reactive oxygen species [GO:0034614]; depurination [GO:0045007]; depyrimidination [GO:0045008]; DNA damage response [GO:0006974]; negative regulation of apoptotic ...
cytosol [GO:0005829]; mitochondrial matrix [GO:0005759]; nuclear matrix [GO:0016363]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]
8-oxo-7,8-dihydroguanine DNA N-glycosylase activity [GO:0034039]; class I DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0140078]; damaged DNA binding [GO:0003684]; endonuclease activity [GO:0004519]; enzyme binding [GO:0019899]; microtubule binding [GO:0008017]; oxidized purine DNA binding [GO:0032357];...
PF00730;PF07934;
3.30.310.40;1.10.1670.10;
Type-1 OGG1 family
null
SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:17148573}. Nucleus speckle {ECO:0000269|PubMed:17148573}. Nucleus matrix {ECO:0000269|PubMed:17148573}. Note=Together with APEX1 is recruited to nuclear speckles in UVA-irradiated cells.; SUBCELLULAR LOCATION: [Isoform 1A]: Nucleus.; SUBCELLULAR LOCATION: [...
CATALYTIC ACTIVITY: Reaction=2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-phospho-2'-deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:66592, Rhea:RHEA-COMP:13180, Rhea:RHEA-COMP:16897, Rhea:RH...
null
null
null
null
FUNCTION: DNA repair enzyme that incises DNA at 8-oxoG residues. Excises 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine (FAPY) from damaged DNA. Has a beta-lyase activity that nicks DNA 3' to the lesion.
Homo sapiens (Human)
O15528
CP27B_HUMAN
MTQTLKYASRVFHRVRWAPELGASLGYREYHSARRSLADIPGPSTPSFLAELFCKGGLSRLHELQVQGAAHFGPVWLASFGTVRTVYVAAPALVEELLRQEGPRPERCSFSPWTEHRRCRQRACGLLTAEGEEWQRLRSLLAPLLLRPQAAARYAGTLNNVVCDLVRRLRRQRGRGTGPPALVRDVAGEFYKFGLEGIAAVLLGSRLGCLEAQVPPDTETFIRAVGSVFVSTLLTMAMPHWLRHLVPGPWGRLCRDWDQMFAFAQRHVERREAEAAMRNGGQPEKDLESGAHLTHFLFREELPAQSILGNVTELLLAGVD...
1.14.15.18
COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:O35084};
bone mineralization [GO:0030282]; C21-steroid hormone biosynthetic process [GO:0006700]; calcitriol biosynthetic process from calciol [GO:0036378]; calcium ion homeostasis [GO:0055074]; calcium ion transport [GO:0006816]; cellular response to peptide hormone stimulus [GO:0071375]; cholesterol metabolic process [GO:0008...
cytoplasm [GO:0005737]; mitochondrial inner membrane [GO:0005743]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]
calcidiol 1-monooxygenase activity [GO:0004498]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; secalciferol 1-monooxygenase activity [GO:0062185]
PF00067;
1.10.630.10;
Cytochrome P450 family
null
SUBCELLULAR LOCATION: Mitochondrion membrane.
CATALYTIC ACTIVITY: Reaction=calcidiol + 2 H(+) + O2 + 2 reduced [adrenodoxin] = calcitriol + H2O + 2 oxidized [adrenodoxin]; Xref=Rhea:RHEA:20573, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17823, ChEBI:CHEBI:17933, ChEBI:CHEBI:33737, ChEBI:CHEBI:3373...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.7 uM for 25-hydroxyvitamin D3 {ECO:0000269|PubMed:10518789}; KM=1.1 uM for 24,25-dihydroxyvitamin D3 {ECO:0000269|PubMed:10518789}; KM=0.9 uM for 25-hydroxyvitamin D3 {ECO:0000269|PubMed:22862690}; Vmax=3.9 pmol/min/mg enzyme toward 25-hydroxyvitamin D3 {ECO:0000...
PATHWAY: Hormone biosynthesis; vitamin D biosynthesis. {ECO:0000269|PubMed:9486994}.
null
null
FUNCTION: A cytochrome P450 monooxygenase involved in vitamin D metabolism and in calcium and phosphorus homeostasis. Catalyzes the rate-limiting step in the activation of vitamin D in the kidney, namely the hydroxylation of 25-hydroxyvitamin D3/calcidiol at the C1alpha-position to form the hormonally active form of vi...
Homo sapiens (Human)
O15529
GPR42_HUMAN
MDTGPDQSYFSGNHWFVFSVYLLTFLVGLPLNLLALVVFVGKLRCRPVAVDVLLLNLTASDLLLLLFLPFRMVEAANGMHWPLPFILCPLSGFIFFTTIYLTALFLAAVSIERFLSVAHPLWYKTRPRLGQAGLVSVACWLLASAHCSVVYVIEFSGDISHSQGTNGTCYLEFRKDQLAILLPVRLEMAVVLFVVPLIITSYCYSRLVWILGRGGSHRRQRRVAGLVAATLLNFLVCFGPYNVSHVVGYICGESPVWRIYVTLLSTLNSCVDPFVYYFSSSGFQADFHELLRRLCGLWGQWQQESSMELKEQKGGEEQRA...
null
null
cellular response to fatty acid [GO:0071398]; G protein-coupled receptor signaling pathway [GO:0007186]
plasma membrane [GO:0005886]
G protein-coupled receptor activity [GO:0004930]
PF00001;
1.20.1070.10;
G-protein coupled receptor 1 family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
null
null
null
null
null
FUNCTION: G protein-coupled receptor that is activated by short chain fatty acids (SCFAs), such as propionate. Hence may play a role in the regulation of whole-body energy homeostasis and/or in intestinal immunity. {ECO:0000269|PubMed:19630535}.
Homo sapiens (Human)
O15530
PDPK1_HUMAN
MARTTSQLYDAVPIQSSVVLCSCPSPSMVRTQTESSTPPGIPGGSRQGPAMDGTAAEPRPGAGSLQHAQPPPQPRKKRPEDFKFGKILGEGSFSTVVLARELATSREYAIKILEKRHIIKENKVPYVTRERDVMSRLDHPFFVKLYFTFQDDEKLYFGLSYAKNGELLKYIRKIGSFDETCTRFYTAEIVSALEYLHGKGIIHRDLKPENILLNEDMHIQITDFGTAKVLSPESKQARANSFVGTAQYVSPELLTEKSACKSSDLWALGCIIYQLVAGLPPFRAGNEYLIFQKIIKLEYDFPEKFFPKARDLVEKLLVLD...
2.7.11.1
null
actin cytoskeleton organization [GO:0030036]; activation of protein kinase B activity [GO:0032148]; calcium-mediated signaling [GO:0019722]; cell migration [GO:0016477]; cellular response to epidermal growth factor stimulus [GO:0071364]; cellular response to insulin stimulus [GO:0032869]; epidermal growth factor recept...
cell projection [GO:0042995]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; focal adhesion [GO:0005925]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]
3-phosphoinositide-dependent protein kinase activity [GO:0004676]; ATP binding [GO:0005524]; phospholipase activator activity [GO:0016004]; phospholipase binding [GO:0043274]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
PF14593;PF00069;
2.30.29.30;1.10.510.10;
Protein kinase superfamily, AGC Ser/Thr protein kinase family, PDPK1 subfamily
PTM: Phosphorylation on Ser-241 in the activation loop is required for full activity. PDPK1 itself can autophosphorylate Ser-241, leading to its own activation. Autophosphorylation is inhibited by the apoptotic C-terminus cleavage product of PKN2 (By similarity). Tyr-9 phosphorylation is critical for stabilization of b...
SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane; Peripheral membrane protein. Cell junction, focal adhesion. Note=Tyrosine phosphorylation seems to occur only at the cell membrane. Translocates to the cell membrane following insulin stimulation by a mechanism that involves binding to GRB14 and INSR. SRC and HSP...
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 kinase which acts as a master kinase, phosphorylating and activating a subgroup of the AGC family of protein kinases. Its targets include: protein kinase B (PKB/AKT1, PKB/AKT2, PKB/AKT3), p70 ribosomal protein S6 kinase (RPS6KB1), p90 ribosomal protein S6 kinase (RPS6KA1, RPS6KA2 and RPS6KA3)...
Homo sapiens (Human)
O15533
TPSN_HUMAN
MKSLSLLLAVALGLATAVSAGPAVIECWFVEDASGKGLAKRPGALLLRQGPGEPPPRPDLDPELYLSVHDPAGALQAAFRRYPRGAPAPHCEMSRFVPLPASAKWASGLTPAQNCPRALDGAWLMVSISSPVLSLSSLLRPQPEPQQEPVLITMATVVLTVLTHTPAPRVRLGQDALLDLSFAYMPPTSEAASSLAPGPPPFGLEWRRQHLGKGHLLLAATPGLNGQMPAAQEGAVAFAAWDDDEPWGPWTGNGTFWLPTVQPFQEGTYLATIHLPYLQGQVTLELAVYKPPKVSLMPATLARAAPGEAPPELLCLVSHF...
null
null
antigen processing and presentation of endogenous peptide antigen via MHC class I [GO:0019885]; MHC class Ib protein complex assembly [GO:0002398]; peptide antigen assembly with MHC class I protein complex [GO:0002502]; peptide antigen stabilization [GO:0050823]; protein-containing complex assembly [GO:0065003]; regula...
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; Golgi membrane [GO:0000139]; lumenal side of endoplasmic reticulum membrane [GO:0098553]; MHC class I peptide loading complex [GO:0042824]; phagocytic vesicle memb...
MHC class I protein binding [GO:0042288]; MHC class I protein complex binding [GO:0023024]; molecular adaptor activity [GO:0060090]; peptide antigen binding [GO:0042605]; protein folding chaperone [GO:0044183]; TAP complex binding [GO:0062061]; TAP1 binding [GO:0046978]; TAP2 binding [GO:0046979]; unfolded protein bind...
PF07654;
2.60.40.10;
null
null
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
null
null
null
null
null
FUNCTION: Involved in the association of MHC class I with transporter associated with antigen processing (TAP) and in the assembly of MHC class I with peptide (peptide loading). {ECO:0000269|PubMed:10636848, ECO:0000269|PubMed:12582157, ECO:0000269|PubMed:21263072, ECO:0000269|PubMed:26611325}.
Homo sapiens (Human)
O15534
PER1_HUMAN
MSGPLEGADGGGDPRPGESFCPGGVPSPGPPQHRPCPGPSLADDTDANSNGSSGNESNGHESRGASQRSSHSSSSGNGKDSALLETTESSKSTNSQSPSPPSSSIAYSLLSASSEQDNPSTSGCSSEQSARARTQKELMTALRELKLRLPPERRGKGRSGTLATLQYALACVKQVQANQEYYQQWSLEEGEPCSMDMSTYTLEELEHITSEYTLQNQDTFSVAVSFLTGRIVYISEQAAVLLRCKRDVFRGTRFSELLAPQDVGVFYGSTAPSRLPTWGTGASAGSGLRDFTQEKSVFCRIRGGPDRDPGPRYQPFRLTP...
null
null
chromatin remodeling [GO:0006338]; circadian regulation of gene expression [GO:0032922]; circadian regulation of translation [GO:0097167]; circadian rhythm [GO:0007623]; entrainment of circadian clock [GO:0009649]; entrainment of circadian clock by photoperiod [GO:0043153]; negative regulation of canonical NF-kappaB si...
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
chromatin DNA binding [GO:0031490]; DNA-binding transcription factor binding [GO:0140297]; E-box binding [GO:0070888]; kinase binding [GO:0019900]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; transcription cis-regulatory region binding [GO:0000976]; transcription corepressor bind...
PF08447;PF21353;PF12114;
3.30.450.20;
null
PTM: Phosphorylated on serine residues by CSNK1D, CSNK1E and probably also by CSNK1G2. Phosphorylation by CSNK1D or CSNK1E promotes nuclear location of PER proteins as well as ubiquitination and subsequent degradation. May be dephosphorylated by PP1. {ECO:0000269|PubMed:15917222}.; PTM: Ubiquitinated; requires phosphor...
SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Nucleocytoplasmic shuttling is effected by interaction with other circadian core oscillator proteins and/or by phosphorylation. Retention of PER1 in the cytoplasm occurs through PER1-PER2 heterodimer formation. Translocate to the nucleus after phosphorylation by CSNK1D or ...
null
null
null
null
null
FUNCTION: Transcriptional repressor which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism a...
Homo sapiens (Human)
O15535
ZSC9_HUMAN
MNTNSKEVLSLGVQVPEAWEELLTMKVEAKSHLQWQESRLKRSNPLAREIFRRHFRQLCYQETPGPREALTRLQELCYQWLRPHVSTKEQILDLLVLEQFLSILPKELQGWVREHCPESGEEAVILLEDLERELDEPQHEMVAHRHRQEVLCKEMVPLAEQTPLTLQSQPKEPQLTCDSAQKCHSIGETDEVTKTEDRELVLRKDCPKIVEPHGKMFNEQTWEVSQQDPSHGEVGEHKDRIERQWGNLLGEGQHKCDECGKSFTQSSGLIRHQRIHTGERPYECNECGKAFSRSSGLFNHRGIHNIQKRYHCKECGKVFS...
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]; sequence-specific double-stranded DNA binding [GO:1990837]
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)
O15537
XLRS1_HUMAN
MSRKIEGFLLLLLFGYEATLGLSSTEDEGEDPWYQKACKCDCQGGPNALWSAGATSLDCIPECPYHKPLGFESGEVTPDQITCSNPEQYVGWYSSWTANKARLNSQGFGCAWLSKFQDSSQWLQIDLKEIKVISGILTQGRCDIDEWMTKYSVQYRTDERLNWIYYKDQTGNNRVFYGNSDRTSTVQNLLRPPIISRFIRLIPLGWHVRIAIRMELLECVSKCA
null
null
adaptation of rhodopsin mediated signaling [GO:0016062]; cell adhesion [GO:0007155]; eye development [GO:0001654]; protein homooligomerization [GO:0051260]; retina layer formation [GO:0010842]; visual perception [GO:0007601]
external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; neuron to neuron synapse [GO:0098984]; photoreceptor inner segment [GO:0001917]; protein-containing complex [GO:0032991]
phosphatidylinositol-3,4-bisphosphate binding [GO:0043325]; phosphatidylserine binding [GO:0001786]; protein-containing complex binding [GO:0044877]
PF00754;
2.60.120.260;
null
null
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10915776, ECO:0000269|PubMed:19849666, ECO:0000269|PubMed:26812435}. Cell membrane {ECO:0000250|UniProtKB:Q9Z1L4}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9Z1L4}; Extracellular side {ECO:0000250|UniProtKB:Q9Z1L4}. Note=Binds to phosphatidylserine-containing...
null
null
null
null
null
FUNCTION: Binds negatively charged membrane lipids, such as phosphatidylserine and phosphoinositides (By similarity). May play a role in cell-cell adhesion processes in the retina, via homomeric interaction between octamers present on the surface of two neighboring cells (PubMed:27114531). Required for normal structure...
Homo sapiens (Human)
O15540
FABP7_HUMAN
MVEAFCATWKLTNSQNFDEYMKALGVGFATRQVGNVTKPTVIISQEGDKVVIRTLSTFKNTEISFQLGEEFDETTADDRNCKSVVSLDGDKLVHIQKWDGKETNFVREIKDGKMVMTLTFGDVVAVRHYEKA
null
null
epithelial cell proliferation [GO:0050673]; fatty acid transport [GO:0015908]; negative regulation of cell population proliferation [GO:0008285]; nervous system development [GO:0007399]
cytosol [GO:0005829]; nucleus [GO:0005634]
fatty acid binding [GO:0005504]; lipid binding [GO:0008289]
PF00061;
2.40.128.20;
Calycin superfamily, Fatty-acid binding protein (FABP) family
null
SUBCELLULAR LOCATION: Cytoplasm.
null
null
null
null
null
FUNCTION: B-FABP could be involved in the transport of a so far unknown hydrophobic ligand with potential morphogenic activity during CNS development. It is required for the establishment of the radial glial fiber system in developing brain, a system that is necessary for the migration of immature neurons to establish ...
Homo sapiens (Human)
O15541
R113A_HUMAN
MAEQLSPGKAVDQVCTFLFKKPGRKGAAGRRKRPACDPEPGESGSSSDEGCTVVRPEKKRVTHNPMIQKTRDSGKQKAAYGDLSSEEEEENEPESLGVVYKSTRSAKPVGPEDMGATAVYELDTEKERDAQAIFERSQKIQEELRGKEDDKIYRGINNYQKYMKPKDTSMGNASSGMVRKGPIRAPEHLRATVRWDYQPDICKDYKETGFCGFGDSCKFLHDRSDYKHGWQIERELDEGRYGVYEDENYEVGSDDEEIPFKCFICRQSFQNPVVTKCRHYFCESCALQHFRTTPRCYVCDQQTNGVFNPAKELIAKLEKH...
2.3.2.27
null
DNA repair [GO:0006281]; mRNA splicing, via spliceosome [GO:0000398]; negative regulation of chemokine-mediated signaling pathway [GO:0070100]; protein ubiquitination [GO:0016567]; snoRNA splicing [GO:0034247]
nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; U2-type precatalytic spliceosome [GO:0071005]; U2-type spliceosomal complex [GO:0005684]
metal ion binding [GO:0046872]; ubiquitin protein ligase activity [GO:0061630]
PF13920;PF00642;
3.30.40.10;
null
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:29360106, ECO:0000269|PubMed:29361316}. Nucleus speckle {ECO:0000269|PubMed:29144457}. Note=Colocalizes with ASCC2 in nuclear foci after DNA damage by alkylating agents. In the absence of DNA damage, colocalizes with the spliceosome components SNRNP200/BRR2 and PRPF8 in...
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:28978524, ECO:0000269|PubMed:29144457};
null
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:28978524, ECO:0000269|PubMed:29144457}.
null
null
FUNCTION: Required for pre-mRNA splicing as component of the spliceosome (PubMed:29360106, PubMed:29361316). As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). E3 ubiquitin-protein ligase that catalyzes the transfer of ubiquitin onto target proteins (PubMed:28...
Homo sapiens (Human)
O15547
P2RX6_HUMAN
MCPQLAGAGSMGSPGATTGWGLLDYKTEKYVMTRNWRVGALQRLLQFGIVVYVVGWALLAKKGYQERDLEPQFSIITKLKGVSVTQIKELGNRLWDVADFVKPPQGENVFFLVTNFLVTPAQVQGRCPEHPSVPLANCWVDEDCPEGEGGTHSHGVKTGQCVVFNGTHRTCEIWSWCPVESGVVPSRPLLAQAQNFTLFIKNTVTFSKFNFSKSNALETWDPTYFKHCRYEPQFSPYCPVFRIGDLVAKAGGTFEDLALLGGSVGIRVHWDCDLDTGDSGCWPHYSFQLQEKSYNFRTATHWWEQPGVEARTLLKLYGIR...
null
null
calcium ion transmembrane transport [GO:0070588]; muscle contraction [GO:0006936]; response to ATP [GO:0033198]; signal transduction [GO:0007165]
cell junction [GO:0030054]; cytoplasm [GO:0005737]; dendritic spine [GO:0043197]; glutamatergic synapse [GO:0098978]; neuronal cell body [GO:0043025]; parallel fiber to Purkinje cell synapse [GO:0098688]; plasma membrane [GO:0005886]; postsynaptic specialization membrane [GO:0099634]; receptor complex [GO:0043235]
ATP binding [GO:0005524]; channel activity [GO:0015267]; extracellularly ATP-gated monoatomic cation channel activity [GO:0004931]; protein-containing complex binding [GO:0044877]; purinergic nucleotide receptor activity [GO:0001614]; transmembrane signaling receptor activity [GO:0004888]
PF00864;
1.10.287.940;2.60.490.10;
P2X receptor family
PTM: N-glycosylated. {ECO:0000269|PubMed:15657042}.
SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
null
null
null
null
null
FUNCTION: Receptor for ATP that acts as a ligand-gated ion channel. {ECO:0000250}.
Homo sapiens (Human)
O15550
KDM6A_HUMAN
MKSCGVSLATAAAAAAAFGDEEKKMAAGKASGESEEASPSLTAEEREALGGLDSRLFGFVRFHEDGARTKALLGKAVRCYESLILKAEGKVESDFFCQLGHFNLLLEDYPKALSAYQRYYSLQSDYWKNAAFLYGLGLVYFHYNAFQWAIKAFQEVLYVDPSFCRAKEIHLRLGLMFKVNTDYESSLKHFQLALVDCNPCTLSNAEIQFHIAHLYETQRKYHSAKEAYEQLLQTENLSAQVKATVLQQLGWMHHTVDLLGDKATKESYAIQYLQKSLEADPNSGQSWYFLGRCYSSIGKVQDAFISYRQSIDKSEASADT...
1.14.11.68
COFACTOR: Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000269|PubMed:17761849}; COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:17761849};
chromatin remodeling [GO:0006338]; heart development [GO:0007507]; regulation of gene expression [GO:0010468]
histone methyltransferase complex [GO:0035097]; MLL3/4 complex [GO:0044666]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
chromatin DNA binding [GO:0031490]; histone demethylase activity [GO:0032452]; histone H3K27me2/H3K27me3 demethylase activity [GO:0071558]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
PF02373;PF21322;PF21326;PF13432;PF13181;
1.20.58.1370;2.10.110.20;2.60.120.650;1.25.40.10;
UTX family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CATALYTIC ACTIVITY: Reaction=2 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(27)-[histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + N(6)-methyl-L-lysyl(27)-[histone H3] + 2 succinate; Xref=Rhea:RHEA:60224, Rhea:RHEA-COMP:15535, Rhea:RHEA-COMP:15544, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:1...
null
null
null
null
FUNCTION: Histone demethylase that specifically demethylates 'Lys-27' of histone H3, thereby playing a central role in histone code (PubMed:17713478, PubMed:17761849, PubMed:17851529). Demethylates trimethylated and dimethylated but not monomethylated H3 'Lys-27' (PubMed:17713478, PubMed:17761849, PubMed:17851529). Pla...
Homo sapiens (Human)
O15551
CLD3_HUMAN
MSMGLEITGTALAVLGWLGTIVCCALPMWRVSAFIGSNIITSQNIWEGLWMNCVVQSTGQMQCKVYDSLLALPQDLQAARALIVVAILLAAFGLLVALVGAQCTNCVQDDTAKAKITIVAGVLFLLAALLTLVPVSWSANTIIRDFYNPVVPEAQKREMGAGLYVGWAAAALQLLGGALLCCSCPPREKKYTATKVVYSAPRSTGPGASLGTGYDRKDYV
null
null
actin cytoskeleton organization [GO:0030036]; bicellular tight junction assembly [GO:0070830]; calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules [GO:0016338]; cell adhesion [GO:0007155]; cell junction maintenance [GO:0034331]; epithelial cell morphogenesis [GO:0003382]; establishment of...
apical junction complex [GO:0043296]; apicolateral plasma membrane [GO:0016327]; bicellular tight junction [GO:0005923]; cell-cell junction [GO:0005911]; lateral plasma membrane [GO:0016328]; membrane [GO:0016020]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]; tight junction [GO:0070160]
identical protein binding [GO:0042802]; structural molecule activity [GO:0005198]; transmembrane signaling receptor activity [GO:0004888]
PF00822;
1.20.140.150;
Claudin family
null
SUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000250|UniProtKB:Q9Z0G9}. Cell membrane {ECO:0000250|UniProtKB:Q9Z0G9}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9Z0G9}.
null
null
null
null
null
FUNCTION: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. {ECO:0000250|UniProtKB:Q9Z0G9}.
Homo sapiens (Human)
O15552
FFAR2_HUMAN
MLPDWKSSLILMAYIIIFLTGLPANLLALRAFVGRIRQPQPAPVHILLLSLTLADLLLLLLLPFKIIEAASNFRWYLPKVVCALTSFGFYSSIYCSTWLLAGISIERYLGVAFPVQYKLSRRPLYGVIAALVAWVMSFGHCTIVIIVQYLNTTEQVRSGNEITCYENFTDNQLDVVLPVRLELCLVLFFIPMAVTIFCYWRFVWIMLSQPLVGAQRRRRAVGLAVVTLLNFLVCFGPYNVSHLVGYHQRKSPWWRSIAVVFSSLNASLDPLLFYFSSSVVRRAFGRGLQVLRNQGSSLLGRRGKDTAEGTNEDRGVGQGE...
null
null
cell surface pattern recognition receptor signaling pathway [GO:0002752]; cellular response to fatty acid [GO:0071398]; fat cell differentiation [GO:0045444]; G protein-coupled receptor signaling pathway [GO:0007186]; glucose homeostasis [GO:0042593]; leukocyte chemotaxis involved in inflammatory response [GO:0002232];...
cell projection [GO:0042995]; plasma membrane [GO:0005886]
G protein-coupled receptor activity [GO:0004930]; lipid binding [GO:0008289]
PF00001;
1.20.1070.10;
G-protein coupled receptor 1 family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18801738}; Multi-pass membrane protein {ECO:0000269|PubMed:18801738}.
null
null
null
null
null
FUNCTION: G protein-coupled receptor that is activated by a major product of dietary fiber digestion, the short chain fatty acids (SCFAs), and that plays a role in the regulation of whole-body energy homeostasis and in intestinal immunity. In omnivorous mammals, the short chain fatty acids acetate, propionate and butyr...
Homo sapiens (Human)
O15553
MEFV_HUMAN
MAKTPSDHLLSTLEELVPYDFEKFKFKLQNTSVQKEHSRIPRSQIQRARPVKMATLLVTYYGEEYAVQLTLQVLRAINQRLLAEELHRAAIQEYSTQENGTDDSAASSSLGENKPRSLKTPDHPEGNEGNGPRPYGGGAASLRCSQPEAGRGLSRKPLSKRREKASEGLDAQGKPRTRSPALPGGRSPGPCRALEGGQAEVRLRRNASSAGRLQGLAGGAPGQKECRPFEVYLPSGKMRPRSLEVTISTGEKAPANPEILLTLEEKTAANLDSATEPRARPTPDGGASADLKEGPGNPEHSVTGRPPDTAASPRCHAQEG...
null
null
inflammatory response [GO:0006954]; innate immune response [GO:0045087]; negative regulation of cytokine production involved in inflammatory response [GO:1900016]; negative regulation of inflammatory response [GO:0050728]; negative regulation of interleukin-1 beta production [GO:0032691]; negative regulation of interle...
autophagosome [GO:0005776]; canonical inflammasome complex [GO:0061702]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; lamellipodium [GO:0030027]; microtubule [GO:0005874]; microtubule associated complex [GO:0005875]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ruffle [GO:0001726]
actin binding [GO:0003779]; identical protein binding [GO:0042802]; ubiquitin protein ligase activity [GO:0061630]; zinc ion binding [GO:0008270]
PF13765;PF02758;PF00622;PF00643;
2.60.120.920;3.30.160.60;1.10.533.10;
null
PTM: Cleaved by CASP1 (Probable). The N-terminal cleavage product localizes to the nucleus as a filamentous network and to the cytoplasm, interacts more strongly with RELA and NFKBIA than the full-length protein, enhances the nuclear localization of RELA and induces NFKBIA proteolysis. The C-terminal cleavage product l...
SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11468188, ECO:0000269|PubMed:19109554}. Cell projection, ruffle {ECO:0000269|PubMed:11468188}. Cell projection, lamellipodium {ECO:0000269|PubMed:11468188}. Nucleus {ECO:0000269|PubMed:11115844}. Cytoplasm {ECO:0000269|PubMed:10666224, ECO:0...
null
null
null
null
null
FUNCTION: Involved in the regulation of innate immunity and the inflammatory response in response to IFNG/IFN-gamma (PubMed:10807793, PubMed:11468188, PubMed:16037825, PubMed:16785446, PubMed:17431422, PubMed:17964261, PubMed:18577712, PubMed:19109554, PubMed:19584923, PubMed:26347139, PubMed:27030597, PubMed:28835462)...
Homo sapiens (Human)
O15554
KCNN4_HUMAN
MGGDLVLGLGALRRRKRLLEQEKSLAGWALVLAGTGIGLMVLHAEMLWFGGCSWALYLFLVKCTISISTFLLLCLIVAFHAKEVQLFMTDNGLRDWRVALTGRQAAQIVLELVVCGLHPAPVRGPPCVQDLGAPLTSPQPWPGFLGQGEALLSLAMLLRLYLVPRAVLLRSGVLLNASYRSIGALNQVRFRHWFVAKLYMNTHPGRLLLGLTLGLWLTTAWVLSVAERQAVNATGHLSDTLWLIPITFLTIGYGDVVPGTMWGKIVCLCTGVMGVCCTALLVAVVARKLEFNKAEKHVHNFMMDIQYTKEMKESAARVLQ...
null
null
calcium ion transport [GO:0006816]; cell volume homeostasis [GO:0006884]; defense response [GO:0006952]; establishment of localization in cell [GO:0051649]; immune system process [GO:0002376]; phospholipid translocation [GO:0045332]; positive regulation of potassium ion transmembrane transport [GO:1901381]; positive re...
cytosol [GO:0005829]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; vesicle [GO:0031982]; voltage-gated potassium channel complex [GO:0008076]
calcium-activated potassium channel activity [GO:0015269]; calmodulin binding [GO:0005516]; intermediate conductance calcium-activated potassium channel activity [GO:0022894]; potassium channel activity [GO:0005267]; protein phosphatase binding [GO:0019903]; small conductance calcium-activated potassium channel activit...
PF02888;PF07885;PF03530;
1.10.287.70;
Potassium channel KCNN family, KCa3.1/KCNN4 subfamily
PTM: Phosphorylation at His-358 by NDKB activates the channel, and conversely it's dephosphorylation by PHPT1 inhibits the channel. {ECO:0000269|PubMed:17157250}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26148990}; Multi-pass membrane protein {ECO:0000255}.
null
null
null
null
null
FUNCTION: Forms a voltage-independent potassium channel that is activated by intracellular calcium (PubMed:26148990). Activation is followed by membrane hyperpolarization which promotes calcium influx. Required for maximal calcium influx and proliferation during the reactivation of naive T-cells (PubMed:17157250, PubMe...
Homo sapiens (Human)
O15648
PFKA_TRYBB
MAVESRSRVTSKLVKAHRAMLNSVTQEDLKVDRLPGADYPNPSKKYSSRTEFRDKTDYIMYNPRPRDEPSSENPVSVSPLLCELAAARSRIHFNPTETTIGIVTCGGICPGLNDVIRSITLTGINVYNVKRVIGFRFGYWGLSKKGSQTAIELHRGRVTNIHHYGGTILGSSRGPQDPKEMVDTLERLGVNILFTVGGDGTQRGALVISQEAKRRGVDISVFGVPKTIDNDLSFSHRTFGFQTAVEKAVQAIRAAYAEAVSANYGVGVVKLMGRDSGFIAAQAAVASAQANICLVPENPISEQEVMSLLERRFCHSRSCV...
2.7.1.11
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_03186};
fructose 6-phosphate metabolic process [GO:0006002]; glycolytic process [GO:0006096]
glycosome [GO:0020015]
6-phosphofructokinase activity [GO:0003872]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; phosphate ion binding [GO:0042301]
PF00365;
3.40.50.450;
Phosphofructokinase type A (PFKA) family, PPi-dependent PFK group II subfamily, Atypical ATP-dependent clade 'X' sub-subfamily
null
SUBCELLULAR LOCATION: Glycosome {ECO:0000255|HAMAP-Rule:MF_03186, ECO:0000269|PubMed:2940090}.
CATALYTIC ACTIVITY: Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+); Xref=Rhea:RHEA:16109, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:57634, ChEBI:CHEBI:456216; EC=2.7.1.11; Evidence={ECO:0000255|HAMAP-Rule:MF_03186, ECO:0000269|PubMed:9461292};
null
PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. {ECO:0000255|HAMAP-Rule:MF_03186}.
null
null
FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis. {ECO:0000255|HAMAP-Rule:MF_03186}.
Trypanosoma brucei brucei
O15706
VACA_DICDI
MIEGSGSKTPKRNSDEISVKSLSIHEANTLSSEHEHESGNEELTLSQIVIRSDFANESSERQSKIILDRFNQGIGKNSAFTDSPALGRGLSRVDVSYFVMGHRNQVAELYDPRGQRFSTVLTPDPTVNIKYVGPVSKTAHYFGAYGKHVLNVPAGHYAKAFSKNRPVLYGEGPHVIIDPTFQFDENNGFVNQQEPFIEHSTINILRIPAGKIAKVWIGTQPHILESRRDPYVFVDAQFKLVSPDGAKKAQLFESSSCTFVEHGSIKRIIPHTGEVAITYNNGILTIIPTPKDGKPVIIDSPTHNFEGFISTSLQTCLFPS...
null
null
establishment of protein localization to plasma membrane [GO:0061951]; phagocytosis, recognition [GO:0006910]; phagosome maturation [GO:0090382]; regulation of DNA-templated transcription [GO:0006355]; response to bacterium [GO:0009617]
early phagosome [GO:0032009]; endosome membrane [GO:0010008]; late endosome [GO:0005770]; membrane [GO:0016020]; pathogen-containing vacuole [GO:0140220]; phagocytic vesicle [GO:0045335]; phagolysosome [GO:0032010]; vacuole [GO:0005773]
null
PF01145;
3.30.479.30;
Vacuolin family
null
SUBCELLULAR LOCATION: Endosome membrane; Peripheral membrane protein. Lysosome. Note=Post-lysosome.
null
null
null
null
null
null
Dictyostelium discoideum (Social amoeba)
O15726
KC1_PLAF4
MEIRVANKYALGKKLGSGSFGDIYVAKDIVTMEEFAVKLESTRSKHPQLLYESKLYKILGGGIGVPKVYWYGIEGDFTIMVLDLLGPSLEDLFTLCNRKFSLKTVRMTADQMLNRIEYVHSKNFIHRDIKPDNFLIGRGKKVTLIHIIDFGLAKKYRDSRSHTSYPYKEGKNLTGTARYASINTHLGIEQSRRDDIEALGYVLMYFLRGSLPWQGLKAISKKDKYDKIMEKKISTSVEVLCRNASFEFVTYLNYCRSLRFEDRPDYTYLRRLLKDLFIREGFTYDFLFDWTCVYASEKDKKKMLENKNRFDQTADQEGRD...
2.7.11.1
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:9334178};
endocytosis [GO:0006897]; non-motile cilium assembly [GO:1905515]; phosphorylation [GO:0016310]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; regulation of circadian rhythm [GO:0042752]; signal transdu...
cytoplasmic vesicle [GO:0031410]; extracellular region [GO:0005576]; host cell surface [GO:0044228]; microneme [GO:0020009]; nucleus [GO:0005634]; spindle microtubule [GO:0005876]
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
PF00069;
1.10.510.10;
Protein kinase superfamily, CK1 Ser/Thr protein kinase family, Casein kinase I subfamily
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8IHZ9}. Cytoplasmic vesicle, secretory vesicle, microneme {ECO:0000250|UniProtKB:Q8IHZ9}. Secreted {ECO:0000250|UniProtKB:Q8IHZ9}. Host cell surface {ECO:0000250|UniProtKB:Q8IHZ9}. Note=At the ring and early trophozoite stages, localizes to the host erythrocyte ce...
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:9334178}; CATALYTIC ...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=14 uM for ATP (at pH 7.5 and 37 degrees Celsius) {ECO:0000269|PubMed:9334178}; Note=kcat is 1550 sec(-1) with ATP as substrate (at pH 7.5 and 37 degrees Celsius). {ECO:0000269|PubMed:9334178};
null
null
null
FUNCTION: Serine/threonine-protein kinase likely to be involved in many cellular processes (PubMed:9334178). Phosphorylates rhoptry protein RON3, nucleosome assembly protein NAPL and DNA/RNA-binding protein ALBA4 in vitro (By similarity). {ECO:0000250|UniProtKB:Q8IHZ9, ECO:0000269|PubMed:9334178}.
Plasmodium falciparum (isolate Dd2)
O15736
TIPD_DICDI
MFSSQNNSYMMMMGGGGIGNINNNQFYSPIISTSAQSFNSIVEWKRDIIRQLNDRNQNQTNNYSEFMRIYTDLLKRERTLNDRTLLYEKEIVSLRNEKKTQQQPPSGSSKMDSSSSSSSSNRVSGMGSTIEEMEQKLFKLQEDLTNSYKRNADNASSILLLNDKNKDLQNELMSKEIEIERIRSTIQQDLDSIKRLEMVVIEKENVSQIIRDELSSLQTEFLHNESKVVKLEQENSSLVERWLRKKNEEASKMNEANDFYQKMVEQRDSTPAKAAVQLSESISNLVVKLPDANDVPIPIVLERGVFSSEAMLPSKAKKRW...
null
null
autophagosome assembly [GO:0000045]; autophagosome maturation [GO:0097352]; culmination involved in sorocarp development [GO:0031154]; macroautophagy [GO:0016236]; negative stranded viral RNA replication [GO:0039689]; phagocytosis [GO:0006909]; pinocytosis [GO:0006907]; proteasome-mediated ubiquitin-dependent protein c...
Atg12-Atg5-Atg16 complex [GO:0034274]; autophagosome membrane [GO:0000421]; extracellular matrix [GO:0031012]; phagophore assembly site membrane [GO:0034045]
Atg8-family ligase activity [GO:0019776]
PF08614;PF00400;
1.20.5.170;2.130.10.10;
WD repeat tipD family
null
null
null
null
null
null
null
FUNCTION: Not known; disruption of the gene for tipD results in morphological defects.
Dictyostelium discoideum (Social amoeba)
O15743
SPNA_DICDI
MKKMLFMNKKEKKEEQSPAHSSLAQQHQLAQQQYQLQQQQLQLQYQQHQQQLQLAQQQKQNEQNLAQLSTSTSSNSSVNNTTNTNTNTTNSSSISSNNNNNNNTAVPILKAHDFCGTIMILGHTESGKTTLQRQLEFIYGVTDPTDAKHYQRLIYGNTLATLIRFIENSERLNITLSPDNLARVKRIQSQPVELARNRLPRFPLKLGWDCKCIWEDKVIQSVYNHSKICSEIRTPGRPKYYMDRMFKVFDPSYTPTEMDIISAYDQKDTIQSSAIIHKRFKVDLFGCSGKQSSPKNWVGLHQNYKPNYIFYVVALKDYFS...
3.1.3.16
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000250};
anatomical structure morphogenesis [GO:0009653]; cell differentiation [GO:0030154]; G protein-coupled receptor signaling pathway [GO:0007186]
cytosol [GO:0005829]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; ruffle [GO:0001726]
G-protein beta/gamma-subunit complex binding [GO:0031683]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; magnesium ion binding [GO:0000287]; myosin phosphatase activity [GO:0017018]; protein serine/threonine phosphatase activity [GO:0004722]
PF00503;PF00481;
1.10.400.10;3.40.50.300;3.60.40.10;
G-alpha family; PP2C family
null
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:9585512}. Cell membrane {ECO:0000269|PubMed:9585512}.
CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-...
null
null
null
null
FUNCTION: Involved in cell-type differentiation and morphogenesis. Dephosphorylates casein; in vitro. May also be involved as modulators or transducers in various transmembrane signaling systems. {ECO:0000269|PubMed:14597204, ECO:0000269|PubMed:9585512}.
Dictyostelium discoideum (Social amoeba)
O15757
PP1_DICDI
MEIDLDSIITRLLEPRTTKPGKLVDLAEEEIRYLTVQATEIFINQPILLELEAPIKICGDIHGQYYDLLRLFEYGGFPPQSNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFILRGNHECASINRIYGFYDECKRRYNSKLWKAFTDCFNCLPVAAIIDEKIFCMHGGLSPDLKNMDQIRRITRPTVVPDFGLLCDLLWADPDKNIQGWEDNDRGVSYTFGADVVESFLKKHDLDLVCRAHQVVEDGYEFFAKRQLVTLFSAPNYFGEFDNAGAMMGVDETLMCSFQILKPADKKKLTNDSNGRPLTPPRNKQQKPK...
3.1.3.16
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Binds 2 manganese ions per subunit. {ECO:0000250};
chromosome segregation [GO:0007059]; regulation of mitotic cell cycle [GO:0007346]
cytoplasm [GO:0005737]; nucleus [GO:0005634]
metal ion binding [GO:0046872]; myosin phosphatase activity [GO:0017018]; protein serine/threonine phosphatase activity [GO:0004722]
PF00149;PF16891;
3.60.21.10;
PPP phosphatase family
null
null
CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-...
null
null
null
null
FUNCTION: Protein phosphatase activity in vitro. {ECO:0000269|PubMed:12737629}.
Dictyostelium discoideum (Social amoeba)
O15770
GSHR_PLAF7
MYKHRYFHFFFFFFFFLVSTKIIRSFTFLNNNTNLSNPVYFKKKANMVYDLIVIGGGSGGMAAARRAARHNAKVALVEKSRLGGTCVNVGCVPKKIMFNAASVHDILENSRHYGFDTKFSFNLPLLVERRDKYIQRLNNIYRQNLSKDKVDLYEGTASFLSENRILIKGTKDNNNKDNGPLNEEILEGRNILIAVGNKPVFPPVKGIENTISSDEFFNIKESKKIGIVGSGYIAVELINVIKRLGIDSYIFARGNRILRKFDESVINVLENDMKKNNINIVTFADVVEIKKVSDKNLSIHLSDGRIYEHFDHVIYCVGRS...
1.8.1.7
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:Q94655}; Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:Q94655};
cell redox homeostasis [GO:0045454]; cellular response to oxidative stress [GO:0034599]; glutathione metabolic process [GO:0006749]; response to oxidative stress [GO:0006979]
apicoplast [GO:0020011]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]
flavin adenine dinucleotide binding [GO:0050660]; glutathione-disulfide reductase (NADP) activity [GO:0004362]
PF07992;PF02852;
3.30.390.30;3.50.50.60;
Class-I pyridine nucleotide-disulfide oxidoreductase family
null
SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm {ECO:0000269|PubMed:21203490}.; SUBCELLULAR LOCATION: [Isoform 2]: Plastid, apicoplast {ECO:0000269|PubMed:21203490}.
CATALYTIC ACTIVITY: Reaction=2 glutathione + NADP(+) = glutathione disulfide + H(+) + NADPH; Xref=Rhea:RHEA:11740, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:58349; EC=1.8.1.7; Evidence={ECO:0000269|PubMed:12729762}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:11742...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=71 uM for glutathione disulfide (GSSG) (at 25 degrees Celsius and pH 6.9) {ECO:0000269|PubMed:12729762};
null
null
null
FUNCTION: Maintains high levels of reduced glutathione in the cytosol. {ECO:0000269|PubMed:12729762}.
Plasmodium falciparum (isolate 3D7)
O15819
H33A_DICDI
MARTKQTARKSTGAKVPRKHIGSKQAHKQTPVSSSSGGVKKVHRFRPGTVALREIRKYQKSTDLLIRKLPFQRLVREIAQEFKTDLRFQSAAIGALQEASEAYLVGLFEDTNLCAIHAKRVTIMPKDIHLARRIRGERS
null
null
chromatin remodeling [GO:0006338]; epigenetic regulation of gene expression [GO:0040029]; response to mercury ion [GO:0046689]
nucleolar chromatin [GO:0030874]; nucleosome [GO:0000786]; nucleus [GO:0005634]
DNA binding [GO:0003677]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527]
PF00125;
1.10.20.10;
Histone H3 family
PTM: Acetylation is generally linked to gene activation. {ECO:0000250}.; PTM: Different methylation states of H3K4 mark distinct developmental phases. H3K4me2 is associated with euchromatic regions. H3K4me3 is a mark of active chromatin. set1 is responsible for all mono-, di- and tri-methylation of H3K4. H3K4me facilit...
SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Associated with pericentromeric heterochromatin.
null
null
null
null
null
FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r...
Dictyostelium discoideum (Social amoeba)
O15865
CDPK2_PLAFK
MGNHLSVNKLKRKKKKKSFLNIYGKNTNENTSKQSNDYKYDINTSCISREGTTTLERKNLILCHSGKLEDKYIIDEKLGQGTYGCVYKGIDKVTNQLYAIKEEKKDRLKNINRFFQEIEIMKKLDHPNIVKLYETYENDNYIYLIMELCSGRELFDSIIENGSFTEKNAATIMKQIFSAIFYLHSLNIVHRDLKPENFLFQSENKDSLLKIIDFGLSKNLGTGEFTTTKAGTPYYVAPQVLDGKYDKKCDIWSSGVIMYTLLCGYPPFYGDTDNEVLKKVKKGEFCFYENDWGSISSDAKNLITKLLTYNPNERCTIEEA...
2.7.11.1
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q8ICR0};
intracellular signal transduction [GO:0035556]; phosphorylation [GO:0016310]
cytoplasm [GO:0005737]; nucleus [GO:0005634]
ATP binding [GO:0005524]; calcium ion binding [GO:0005509]; calcium-dependent protein serine/threonine kinase activity [GO:0009931]; calmodulin binding [GO:0005516]; calmodulin-dependent protein kinase activity [GO:0004683]; mitogen-activated protein kinase binding [GO:0051019]; protein serine kinase activity [GO:01063...
PF13499;PF00069;
1.10.238.10;1.10.510.10;
Protein kinase superfamily, Ser/Thr protein kinase family, CDPK subfamily
PTM: Myristoylated; myristoylation may target it to different subcellular compartments. {ECO:0000250|UniProtKB:P62344}.; PTM: Autophosphorylated in vitro. {ECO:0000269|PubMed:9247932}.
null
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:9247932}; CATALYTIC ...
null
null
null
null
FUNCTION: Calcium-dependent protein kinase which acts as a sensor and effector of intracellular Ca(2+) levels probably in part downstream of cGMP-activated PKG kinase (PubMed:9247932). During male gametogenesis in the mosquito gut, required for male exflagellation, possibly by regulating male gamete exit from the host ...
Plasmodium falciparum (isolate K1 / Thailand)
O15909
RIR1_TRYBB
MLETVKLVTKRDGSVEPYDEKVVRSRIVNLMSGIDSYYVDVDDLVRVVGEGVREGMSTSMLDELLAETAAYCVTKHPDYGLLAGRLAVTALHKTTTESVLDSFRVLHEHVSQATKRHAPLISEELWDIANKHSAALQQIINYERDFDFEYFGYKTLERSYLLRVHKGRGVMEVVERPQQMFLRVALGIHGEDLERVKETYDYMSQGFFTHATPTLFNAGTPFPQMSSCFLVAMREDSIDGIYDTLKQCAIISKSAGGIGIHMHNIRAAGSYIAGTNGTSNGLVPMLRVWNNTARYVDQGGGKRKGAFAIYLEPWHADIFG...
1.17.4.1
null
deoxyribonucleotide biosynthetic process [GO:0009263]; DNA replication [GO:0006260]
nucleoplasm [GO:0005654]; ribonucleoside-diphosphate reductase complex [GO:0005971]
ATP binding [GO:0005524]; ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor [GO:0004748]
PF03477;PF02867;PF00317;
3.20.70.20;
Ribonucleoside diphosphate reductase large chain family
null
null
CATALYTIC ACTIVITY: Reaction=[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-diphosphate; Xref=Rhea:RHEA:23252, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57930, ChEBI:CHEBI:73316;...
null
null
null
null
FUNCTION: Provides the precursors necessary for DNA synthesis. Catalyzes the rate limiting step in the de novo synthesis of deoxyribonucleotides by directly reducing ribonucleotides to the corresponding deoxyribonucleotides. {ECO:0000269|PubMed:9192674}.
Trypanosoma brucei brucei
O15943
CADN_DROME
MAARRCLNQLRQRYITNRFNICTCAIFLISLPFILAIEETTFAGLSAENAARMLAGSPGDVEKSSLSHHSEMSLVLPHDTYPGFSIKKFKTHPVKINGSSHSGAAAYHMLDTDYSKYFTVLEDGVVMTTADISPLVNRPVQLVVVEQTPNATNTHNLQLFVMHRNDMLRFSGSLLDASGEVRENQPAGTRVRGVPLMQAFSGSILDEELATPKKVRYTIIDGNVDDAFALQERKANKNIQISAKSLVINGDDESGVWLVTNRPLDREERAHYDLSVEASDVDGLDRTVSKIQITVLDENDNRPIFKSLDYKFAIAGQKSA...
null
null
adherens junction organization [GO:0034332]; axon extension [GO:0048675]; axon extension involved in axon guidance [GO:0048846]; axon guidance [GO:0007411]; axon target recognition [GO:0007412]; axonal fasciculation [GO:0007413]; calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules [GO:00163...
adherens junction [GO:0005912]; axon [GO:0030424]; catenin complex [GO:0016342]; cell-cell junction [GO:0005911]; dendrite [GO:0030425]; membrane [GO:0016020]; plasma membrane [GO:0005886]
cadherin binding [GO:0045296]; calcium ion binding [GO:0005509]; protein homodimerization activity [GO:0042803]
PF01049;PF00028;PF00008;PF02210;
2.60.120.200;2.60.40.60;2.10.25.10;4.10.900.10;
null
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
null
null
null
null
null
FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. May associate with arm neural isoform and participate in the transmission of developmental ...
Drosophila melanogaster (Fruit fly)
O15945
ARNT_DROME
MDEANIQDKERFASRENHCEIERRRRNKMTAYITELSDMVPTCSALARKPDKLTILRMAVAHMKALRGTGNTSSDGTYKPSFLTDQELKHLILEAADGFLFVVSCDSGRVIYVSDSVTPVLNYTQSDWYGTSLYEHIHPDDREKIREQLSTQESQNAGRILDLKSGTVKKEGHQSSMRLSMGARRGFICRMRVGNVNPESMVSGHLNRLKQRNSLGPSRDGTNYAVVHCTGYIKNWPPTDMFPNMHMERDVDDMSSHCCLVAIGRLQVTSTAANDMSGSNNQSEFITRHAMDGKFTFVDQRVLNILGYTPTELLGKICYD...
null
null
appendage development [GO:0048736]; brain development [GO:0007420]; cellular response to hypoxia [GO:0071456]; cellular response to insulin stimulus [GO:0032869]; central nervous system development [GO:0007417]; glial cell migration [GO:0008347]; imaginal disc-derived leg joint morphogenesis [GO:0016348]; insulin recep...
aryl hydrocarbon receptor complex [GO:0034751]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; RNA polymerase II transcription regulator complex [GO:0090575]
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]; myosin binding [GO:0017022]; protein heterodimerization activity [GO:0046982]; RNA polymerase...
PF00010;PF00989;PF14598;
4.10.280.10;3.30.450.20;
null
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
null
null
null
null
null
FUNCTION: Heterodimers of tgo/trh are involved in the control of breathless expression. Plays a role in the cellular or tissue response to oxygen deprivation. {ECO:0000269|PubMed:10581393, ECO:0000269|PubMed:9284047, ECO:0000269|PubMed:9374395, ECO:0000269|PubMed:9409674}.
Drosophila melanogaster (Fruit fly)
O16000
STX1A_CAEEL
MTKDRLSALKAAQSEDEQDDDMHMDTGNAQYMEEFFEQVEEIRGSVDIIANNVEEVKKKHSAILSNPVNDQKTKEELDELMAVIKRAANKVRGKLKLIENAIDHDEQGAGNADLRIRKTQHSTLSRRFVEVMTDYNKTQTDYRERCKGRIQRQLDIAGKQVGDEDLEEMIESGNPGVFTQGIITDTQQAKQTLADIEARHNDIMKLESSIRELHDMFMDMAMLVESQGEMVDRIEYNVEHAKEFVDRAVADTKKAVQYQSKARRKKICILVTGVILITGLIIFILFYAKVL
null
null
calcium-mediated signaling [GO:0019722]; cell differentiation [GO:0030154]; chemical synaptic transmission [GO:0007268]; exocytosis [GO:0006887]; insulin receptor signaling pathway [GO:0008286]; intracellular protein transport [GO:0006886]; locomotion [GO:0040011]; neurotransmitter secretion [GO:0007269]; positive regu...
axon [GO:0030424]; basolateral plasma membrane [GO:0016323]; dendrite [GO:0030425]; endomembrane system [GO:0012505]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; presynaptic active zone membrane [GO:0048787]; SNARE complex [GO:0031201]; synaptic vesicle...
protein-folding chaperone binding [GO:0051087]; SNAP receptor activity [GO:0005484]; SNARE binding [GO:0000149]; structural constituent of cuticle [GO:0042302]
PF05739;PF00804;
1.20.5.110;1.20.58.70;
Syntaxin family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12973353}; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:P32851, ECO:0000255}. Cell projection, axon {ECO:0000269|PubMed:12973353, ECO:0000269|PubMed:18596236}. Cell projection, dendrite {ECO:0000269|PubMed:12973353, ECO:0000269|PubMed:18596236}. Per...
null
null
null
null
null
FUNCTION: Plays a critical role in several secretory processes, including cuticle secretion and neurotransmitter release, and probably assists in neuronal membrane maturation or the final stages of neuronal differentiation (PubMed:1945043, PubMed:9442061). Plays a role in synaptic vesicle docking and tethering through ...
Caenorhabditis elegans
O16011
MBL_DROME
MANVVNMNSLLNGKDSRWLQLEVCREFQRNKCSRQDTECKFAHPPANVEVQNGKVTACYDSIKGRCNRDKPPCKYFHPPQHLKDQLLINGRNHLALKNALMQQMGIAPGQPVISGQVPAVATNPYLTGIPANSYSPYYTTGHLVPALLGPDPVTSQLGPVVPQTVQVAQQKIPRSDRLETSPLAAHHHQQQQQLQHQLNNINNNNNHSTAGAAATSTTATTTTNNAAAAAAAAAAAAAAAVMGHHTLEVGKKRAADTTDMFPLVFFCSFPSPCVFAFLNCSIFGFLRLWFSLFNLRH
null
null
apoptotic process [GO:0006915]; compound eye photoreceptor cell differentiation [GO:0001751]; eye development [GO:0001654]; muscle cell cellular homeostasis [GO:0046716]; muscle organ development [GO:0007517]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; regulation of female receptivity [GO:00...
cytoplasm [GO:0005737]; H zone [GO:0031673]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; Z disc [GO:0030018]
metal ion binding [GO:0046872]; nucleic acid binding [GO:0003676]; RNA binding [GO:0003723]
null
3.30.1370.210;
Muscleblind family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9334280}.
null
null
null
null
null
FUNCTION: Required for terminal differentiation of photoreceptor cells. Vital for embryonic development. {ECO:0000269|PubMed:9334280}.
Drosophila melanogaster (Fruit fly)
O16025
AOSL_PLEHO
MTWKNFGFEIFGEKYGQEELEKRIKDEHTPPPDSPVFGGLKLKLKKEKFKTLFTLGTTLKGFRRATHTVGTGGIGEITIVNDPKFPEHEFFTAGRTFPARLRHANLKYPDDAGADARSFSIKFADSDSDGPLDIVMNTGEANIFWNSPSLEDFVPVEEGDAAEEYVYKNPYYYYNLVEALRRAPDTFAHLYYYSQVTMPFKAKDGKVRYCRYRALPGDVDIKEEDESGRLTEEEQRKIWIFSRHENEKRPDDYLRKEYVERLQKGPVNYRLQIQIHEASPDDTATIFHAGILWDKETHPWFDLAKVSIKTPLSPDVLEKT...
1.13.11.40; 4.2.1.-
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Note=Binds 2 calcium ions per subunit.; COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Note=Binds 1 Fe cation per subunit.; COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Note=Binds 1 heme group per subunit.;
arachidonic acid metabolic process [GO:0019369]; hepoxilin biosynthetic process [GO:0051122]; linoleic acid metabolic process [GO:0043651]; lipid oxidation [GO:0034440]; lipoxygenase pathway [GO:0019372]; oxylipin biosynthetic process [GO:0031408]
cytoplasm [GO:0005737]; membrane [GO:0016020]
allene oxide synthase activity [GO:0009978]; arachidonate 8(R)-lipoxygenase activity [GO:0047677]; heme binding [GO:0020037]; iron ion binding [GO:0005506]
PF00305;PF01477;
3.10.450.60;2.40.180.10;
Lipoxygenase family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00726, ECO:0000269|PubMed:16162493}. Membrane {ECO:0000269|PubMed:16162493}; Peripheral membrane protein {ECO:0000269|PubMed:16162493}. Note=Calcium binding promotes binding to membranes.
CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = (8R)-hydroperoxy-(5Z,9E,11Z,14Z)-eicosatetraenoate; Xref=Rhea:RHEA:14985, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:57447; EC=1.13.11.40; Evidence={ECO:0000269|PubMed:10559269, ECO:0000269|PubMed:9302294}; PhysiologicalDirection=left-to-right...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=45.28 uM for arachidonate ((5Z,8Z,11Z,14Z)-eicosatetraenoate) {ECO:0000269|PubMed:10559269};
PATHWAY: Lipid metabolism; arachidonate metabolism.; PATHWAY: Lipid metabolism; fatty acid metabolism.
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. {ECO:0000269|PubMed:10559269};
null
FUNCTION: Bifunctional enzyme which is responsible for allene oxide biosynthesis via a two-step reaction; first the lipoxygenase reaction that converts polyunsaturated fatty acids such as arachidonate ((5Z,8Z,11Z,14Z)-eicosatetraenoate) into a (8R)-hydroperoxide intermediate ((8R)-hydroperoxy-(5Z,9E,11Z,14Z)-eicosatetr...
Plexaura homomalla (Black sea rod)
O16076
HSP83_DROPE
MPEEAETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNASDALDKIRYESLTDPSKLDSGKELYIKLIPNKTAGTLTIIDTGIGMTKSDLVNNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLIADRVTVTSKNNDDEQYVWESXXXGSFTXKADNXEPLXRGTKIXLYIKEDQTDYLEESKIKEIVNKHSQFIGYPIKLLVEKEREKEVSDDEADDEKKDDEAKKDMDTDEPKIEDVGEDEDADKKDKDGKKKKTIKEKY
null
null
cellular response to heat [GO:0034605]; centrosome cycle [GO:0007098]; cold acclimation [GO:0009631]; membrane bending [GO:0097753]; multivesicular body fusion to apical plasma membrane [GO:0098866]; negative regulation of cell population proliferation [GO:0008285]; pole plasm mRNA localization [GO:0019094]; positive r...
centrosome [GO:0005813]; cytosol [GO:0005829]; endoplasmic reticulum chaperone complex [GO:0034663]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; polytene chromosome interband [GO:0005705]; protein folding chaperone complex [GO:0101031]
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein folding chaperone [GO:0140662]; disordered domain specific binding [GO:0097718]; insulin receptor binding [GO:0005158]; TPR domain binding [GO:0030911]; unfolded protein binding [GO:0051082]
PF13589;PF00183;
3.30.565.10;
Heat shock protein 90 family
null
SUBCELLULAR LOCATION: Cytoplasm.
null
null
null
null
null
FUNCTION: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes...
Drosophila persimilis (Fruit fly)
O16102
CHD3_DROME
MSSKRGADPDWKTPGKASKDKRPKTNAKKQKFRDEEYCKVCSDGGDLLCCDSCPSVYHRTCLSPPLKSIPKGDWICPRCIPLPGKAEKILSWRWALDRSVELRTSKGEKRREYFIKWHGMSYWHCEWIPEGQMLLHHASMVASFQRRSDMEEPSLEELDDQDGNLHERFYRYGIKPEWLLVQRVINHSEEPNGGTMYLVKWRELSYNDSSWERESDSIPGLNQAIALYKKLRSSNKGRQRDRPAPTIDLNKKYEDQPVFLKEAGLKLHPFQIEGVSWLRYSWGQGIPTILADEMGLGKTIQTVVFLYSLFKEGHCRGPFL...
3.6.4.12
null
chromatin organization [GO:0006325]; chromatin remodeling [GO:0006338]; negative regulation of transcription by RNA polymerase II [GO:0000122]; nucleosome organization [GO:0034728]
chromatin [GO:0000785]; euchromatin [GO:0000791]; nucleus [GO:0005634]; NuRD complex [GO:0016581]
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent chromatin remodeler activity [GO:0140658]; chromatin binding [GO:0003682]; DNA binding [GO:0003677]; helicase activity [GO:0004386]; histone binding [GO:0042393]; metal ion binding [GO:0046872]
PF00385;PF00271;PF00628;PF00176;
2.40.50.40;3.40.50.300;3.40.50.10810;3.30.40.10;
SNF2/RAD54 helicase family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18250149}. Chromosome {ECO:0000269|PubMed:18250149}. Note=During embryogenesis, detected in nuclei before and after their migration to the membrane of the preblastoderm embryo (PubMed:18250149). Remains associated with condensed chromosomes in mitotic nuclei. Not detect...
CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; Evidence={ECO:0000269|PubMed:18250149};
null
null
null
null
FUNCTION: Helicase which acts in nucleosome-remodeling by catalyzing ATP-dependent nucleosome mobilization (PubMed:18250149). Likely to be involved in the regulation of transcription (PubMed:18250149). {ECO:0000269|PubMed:18250149}.
Drosophila melanogaster (Fruit fly)
O16228
DJ12_CAEEL
MAAQKSALILLPPEDAEEIEVIVTGDVLVRGGLQVLYAGSSTEPVKCAKGARIVPDVALKDVKNKTFDIIIIPGGPGCSKLAECPVIGELLKTQVKSGGLIGAICAGPTVLLAHGIVAERVTCHYTVKDKMTEGGYKYLDDNVVISDRVITSKGPGTAFEFALKIVETLEGPEKTNSLLKPLCLAK
4.2.1.130
null
cellular response to glyoxal [GO:0036471]; cellular response to methylglyoxal [GO:0097238]; glycolate biosynthetic process [GO:0046295]; glyoxal metabolic process [GO:1903189]; lactate biosynthetic process [GO:0019249]; methylglyoxal metabolic process [GO:0009438]; negative regulation of oxidative stress-induced intrin...
cytoplasm [GO:0005737]; mitochondrion [GO:0005739]; nucleus [GO:0005634]
glyoxalase III activity [GO:0019172]
PF01965;
3.40.50.880;
Peptidase C56 family, DJ-1 subfamily
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22523093}.
CATALYTIC ACTIVITY: Reaction=H2O + methylglyoxal = (R)-lactate + H(+); Xref=Rhea:RHEA:27754, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16004, ChEBI:CHEBI:17158; EC=4.2.1.130; Evidence={ECO:0000269|PubMed:22523093};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.39 mM for methylglyoxal {ECO:0000269|PubMed:22523093}; KM=0.78 mM for glyoxal {ECO:0000269|PubMed:22523093}; Note=kcat is 60.0 min(-1) with methylglyoxal as substrate and 146.4 min(-1) with glyoxal as substrate. {ECO:0000269|PubMed:22523093};
null
null
null
FUNCTION: Catalyzes the conversion of methylglyoxal (MG) or glyoxal (GO) to D-lactate or glycolic acid respectively in a single glutathione (GSH)-independent step. May play a role in detoxifying endogenously produced glyoxals. Involved in protection against glyoxal-induced cell death. Protects dopaminergic neurons from...
Caenorhabditis elegans
O16259
STIP1_CAEEL
MTDAAIAEKDLGNAAYKQKDFEKAHVHYDKAIELDPSNITFYNNKAAVYFEEKKFAECVQFCEKAVEVGRETRADYKLIAKAMSRAGNAFQKQNDLSLAVQWFHRSLSEFRDPELVKKVKELEKQLKAAERLAYINPELAQEEKNKGNEYFKKGDYPTAMRHYNEAVKRDPENAILYSNRAACLTKLMEFQRALDDCDTCIRLDSKFIKGYIRKAACLVAMREWSKAQRAYEDALQVDPSNEEAREGVRNCLRSNDEDPEKAKERSLADPEVQEILRDPGMRMILEQMSNDPGAVREHLKNPEIFQKLMKLRDAGVIQMR
null
null
determination of adult lifespan [GO:0008340]; protein maturation by protein folding [GO:0022417]; reproduction [GO:0000003]; response to heat [GO:0009408]
cytoplasm [GO:0005737]; protein folding chaperone complex [GO:0101031]
ATPase inhibitor activity [GO:0042030]; Hsp70 protein binding [GO:0030544]; Hsp90 protein binding [GO:0051879]
PF17830;PF13414;
1.10.260.100;1.25.40.10;
null
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19467242}. Note=Detected in cytoplasm in early-stage embryos. {ECO:0000269|PubMed:19467242}.
null
null
null
null
null
FUNCTION: Plays a role in gonad development. Up-regulates longevity and thermotolerance. Binds daf-21/hsp90 and inhibits its ATPase activity. {ECO:0000269|PubMed:19467242, ECO:0000269|PubMed:19559711}.
Caenorhabditis elegans
O16299
FIGL1_CAEEL
MYSPKRVKLNVTSGMRKRPETGENNDDLYPPTALARNGISPYFIGKPRRKIVVETPSDSAQQQPPFKSRSQQNGLDDELDGIIIDEDEDRTVDVSFSQKQDTRKLKSRPFLGEKSSFKLGEIPKPKEEKRREEPFTMRGFDFGSDDKVTKIRDKICDIVDPTNARRTDPNFIRQMHENTLKGIEVASNPHFKKTRAPTKNRAAIQNTLGTLYPSFTTAAGQDPQNSKFQVPLDRQSSSQSIGSLAGIPPARRAPDIPKRCSNPLIRKAMGMDTEGGGKDEKMSGLRAEPTLKHFDENIISLIESEIMSVNNEIGWADVAG...
3.6.4.-
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:15581640};
ATP metabolic process [GO:0046034]; cell cycle [GO:0007049]; cell division [GO:0051301]; positive regulation of mitotic cell cycle [GO:0045931]
nucleus [GO:0005634]
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; hydrolase activity [GO:0016787]; magnesium ion binding [GO:0000287]; microtubule binding [GO:0008017]; microtubule severing ATPase activity [GO:0008568]
PF00004;PF17862;PF09336;
1.10.8.60;3.40.50.300;
AAA ATPase family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17878235}.
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:0000269|PubMed:15581640};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.44 mM for ATP {ECO:0000269|PubMed:15581640}; Vmax=225 nmol/min/mg enzyme {ECO:0000269|PubMed:15581640}; Note=At 25 degrees Celsius and pH 8.0.;
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0-8.8. {ECO:0000269|PubMed:15581640};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 25-30 degrees Celsius. {ECO:0000269|PubMed:15581640};
FUNCTION: Has a role in spindle assembly which acts in the progression through mitosis during embryogenesis. Required for fertility. {ECO:0000269|PubMed:17878235}.
Caenorhabditis elegans
O16305
CALM_CAEEL
MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVTMMTTK
null
null
apoptotic cell clearance [GO:0043277]; cell migration [GO:0016477]; embryo development ending in birth or egg hatching [GO:0009792]; establishment of meiotic spindle orientation [GO:0051296]; negative regulation of gene expression [GO:0010629]; positive chemotaxis [GO:0050918]; regulation of apoptotic process [GO:00429...
calcineurin complex [GO:0005955]; cell periphery [GO:0071944]; centrosome [GO:0005813]; mitotic spindle [GO:0072686]; nuclear membrane [GO:0031965]
calcium ion binding [GO:0005509]; enzyme regulator activity [GO:0030234]
PF13499;
1.10.238.10;
Calmodulin family
null
null
null
null
null
null
null
FUNCTION: Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases.
Caenorhabditis elegans
O16374
GALT1_CAEEL
MPRITASKIVLLIALSFCITVIYHFPIATRSSKEYDEYGNEYENVASIESDIKNVRRLLDEVPDPSQNRLQFLKLDEHAFAFSAYTDDRNGNMGYKYVRVLMFITSQDNFSCEINGRKSTDVSLYEFSENHKMKWQMFILNCKLPDGIDFNNVSSVKVIRSTTKQFVDVPIRYRIQDEKIITPDEYDYKMSICVPALFGNGYDAKRIVEFIELNTLQGIEKIYIYTNQKELDGSMKKTLKYYSDNHKITLIDYTLPFREDGVWYHGQLATVTDCLLRNTGITKYTFFNDFDEFFVPVIKSRTLFETISGLFEDPTIGSQR...
2.4.1.-
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:19858195}; Note=Can also use Fe(2+) and Co(2+). {ECO:0000269|PubMed:19858195};
glycosylation [GO:0070085]; N-glycan processing [GO:0006491]; protein galactosylation [GO:0042125]
cytoplasm [GO:0005737]; Golgi cisterna membrane [GO:0032580]; intracellular organelle [GO:0043229]
beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase activity [GO:0003831]; glycosyltransferase activity [GO:0016757]; metal ion binding [GO:0046872]; UDP-galactosyltransferase activity [GO:0035250]
PF01697;
null
Glycosyltransferase 92 family
PTM: N-glycosylated. {ECO:0000269|PubMed:19858195}.
SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000303|PubMed:19858195}; Single-pass type II membrane protein {ECO:0000303|PubMed:19858195}. Note=Localizes to vesicles or organelles in coelomocytes. {ECO:0000269|PubMed:19858195}.
null
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=84 uM for UDP-galactose {ECO:0000269|PubMed:19858195};
null
null
null
FUNCTION: Catalyzes the transfer of beta-galactose from UDP-galactose to position 4 of alpha-1,6-linked fucose at the reducing end GlcNAc in N-glycan cores (PubMed:19858195). Involved in susceptibility to the nematotoxic C.cinerea galectin Cgl2, likely by contributing to the synthesis of core alpha-1,6-fucosylated N-gl...
Caenorhabditis elegans
O16466
ATG18_CAEEL
MSATTSEENPDSINYIGFNQDSKVICVGHKDGYMFYKTADILENNTLTYEGENLTHLGLNNCLIIERLFSSALMVVISQKDPRVLHVYHFTSRNIICDHRFNKSVLTVRLNRDRIVVCLEDCIYIYNLKDMKMMHNIMDTPTNKLGVLDLTSNPGNALIAYPGSTDTGSVHLFDAINLSSVSTFNAHEGTIACLKFNQEGNMIATASTKGTVIRVYSVPNGHRLFEFRRGVTRCVNIYSLCFSSDSKYLTSSSNTETVHVFKLEKTEGVDNKPEASTEGGGWFDAINKTFSAYMPSQVLQVGELMTTERSFATAKLPGAA...
null
null
apoptotic cell clearance [GO:0043277]; autophagy [GO:0006914]; cellular response to toxic substance [GO:0097237]; dauer larval development [GO:0040024]; determination of adult lifespan [GO:0008340]; embryo development ending in birth or egg hatching [GO:0009792]; embryonic morphogenesis [GO:0048598]; germ cell prolifer...
cytoplasm [GO:0005737]; cytosol [GO:0005829]; extrinsic component of membrane [GO:0019898]; phagocytic vesicle [GO:0045335]; phagocytic vesicle membrane [GO:0030670]; phagophore assembly site membrane [GO:0034045]
phosphatidylinositol-3,5-bisphosphate binding [GO:0080025]; phosphatidylinositol-3-phosphate binding [GO:0032266]; phosphatidylinositol-4-phosphate binding [GO:0070273]; phosphatidylinositol-5-phosphate binding [GO:0010314]
PF21032;
2.130.10.10;
WD repeat PROPPIN family
null
SUBCELLULAR LOCATION: Cytoplasmic vesicle, phagosome membrane {ECO:0000269|PubMed:22451698}; Peripheral membrane protein {ECO:0000305|PubMed:22451698}; Cytoplasmic side {ECO:0000305|PubMed:22451698}. Cytoplasm {ECO:0000269|PubMed:25124690}. Note=Partially localizes to the phagosome membrane of engulfed apoptotic cells....
null
null
null
null
null
FUNCTION: Component of the autophagy machinery that is recruited to phosphatidylinositols on preautophagosomal structures, which are early autophagic structures, to promote autophagosome formation, and the subsequent degradation and clearance of engulfed apoptotic cells and P-granules in somatic cells (PubMed:12958363,...
Caenorhabditis elegans
O16658
S35A3_CAEEL
MNRANDTSSNLKLISLVVLIVQTTALVLTLRYSQTQKSEGPRYLSSTAVVCAEIIKLITCFFVIYRNNGYRFSGMLNELNREIFASPQTRADSLKVAVPAIMYVIQNNLLFFALKKLDAATYQVTYQLKILTTAIFSVTMLGKSLHRYNWMALILLTAGVALVQYPSGDSTTSKSTAAEHDASDNILGLGAVLAACFSSGFAGVYFEKILKTSKVSLWIRNIQLAFFSVFGALLVCWLYDWQAISDDGFLRGYNGVIWIVVLLQAYGGLVIALVVKYADNILKGFAVSLSIILSSFTSWLVLGDLTITTTFAIGATVVIF...
null
null
UDP-galactose transmembrane import into Golgi lumen [GO:0097624]; UDP-N-acetylgalactosamine transmembrane transport [GO:0015789]; UDP-N-acetylglucosamine transmembrane transport [GO:1990569]
Golgi membrane [GO:0000139]
UDP-galactose transmembrane transporter activity [GO:0005459]; UDP-N-acetylgalactosamine transmembrane transporter activity [GO:0005463]; UDP-N-acetylglucosamine transmembrane transporter activity [GO:0005462]
PF04142;
1.10.3730.20;
Nucleotide-sugar transporter family, SLC35A subfamily
null
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9Y2D2}; Multi-pass membrane protein {ECO:0000255}.
null
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=25.2 uM for uridine diphosphate-N-acetylglucosamine as substrate (at 25 degrees Celsius) {ECO:0000269|PubMed:17060606}; KM=24.9 uM for uridine diphosphate-N-acetylgalactosamine as substrate (at 25 degrees Celsius) {ECO:0000269|PubMed:17060606};
null
null
null
FUNCTION: Uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc) transporter in the Golgi apparatus (PubMed:17060606). UDP-N-acetylgalactosamine (UDP-GalNAc) transporter in the Golgi apparatus (PubMed:17060606). Apparently transports UDP-GlcNAc and UDP-GalNAc simultaneously, and independently, by an unknown mechanism (Pu...
Caenorhabditis elegans
O16785
PARV_CAEEL
MSTLGRSKTPSRDEPKKPGVFEKLSGTLSRKKKAPEDEHGNQGGAHHATDEDEVLELELEGREALDQSLVPVLARNIWLEEGEIRRYLTKETARDQKLAQVVDLLIYWLNEELADQRIVVRHLQEDLFDGQIIQKLLEKLEQIRIEVPEVSQSEEGQRQKLQIVVQTANRILGQPREQEKWSADLIHQKDFTAIIQLLVLLALHYRAPVRFPDNVVANVVVAQKEHGQVKTHRITEQITTVQTELAPKGTRDAFDTLFDYGPDKLAHVKTSLLAFCNKHLNKINLEVSDLDNQFQDGVFLVLLVGLLEGYFVPLYHFNLQ...
null
null
actin cytoskeleton organization [GO:0030036]; cell projection assembly [GO:0030031]; establishment or maintenance of cell polarity [GO:0007163]; mitochondrion organization [GO:0007005]; muscle cell cellular homeostasis [GO:0046716]; positive regulation of locomotion [GO:0040017]; positive regulation of sarcomere organi...
actin cytoskeleton [GO:0015629]; axon [GO:0030424]; basal plasma membrane [GO:0009925]; cytoplasm [GO:0005737]; focal adhesion [GO:0005925]; M band [GO:0031430]; perikaryon [GO:0043204]; striated muscle dense body [GO:0055120]
actin binding [GO:0003779]
PF00307;
1.10.418.10;
Parvin family
null
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12781130}. Cytoplasm, myofibril, sarcomere, M line {ECO:0000269|PubMed:23283987}. Perikaryon {ECO:0000269|PubMed:12781130}. Cell projection, axon {ECO:0000269|PubMed:12781130}. Note=Colocalizes with integrins and pat-4/ILK (PubMed:12781130). Colocalizes ...
null
null
null
null
null
FUNCTION: Involved in the regulation of cell adhesion and cytoskeleton organization. Component of an integrin containing attachment complex, which is required for muscle development and maintenance (PubMed:22253611). During embryonic development, required to recruit cpna-1, unc-89 and myofilaments to newly forming inte...
Caenorhabditis elegans
O16810
ORC1_DROME
MVNKENARSVGQQVKWIGSQDELPPVKNLEHKNVYFYQKCIYGPLTLSVGDFILVSNADAAEPDTVSGCDVARILHMYELRELTDREPCRAIVQWYSWPKAIPHNKYDDDEVAIDFSLEVIEEHRPYDNDVALGAIYRKCIVLEGTSKTSAEEILKRHANKLKSTACPMFVSRYRFVKVKRSYRLIPLEIHLEQPEDNARPTRSSRKSLTAHRESKRSISARHDDTAGNKGSSVEKRRRASMAASSSVEFIDVNSFICENKVSPIKIVGGRSVVRLSEKKNAPEINANYLPASPLTEKNAKVETPKSRASAARRNLNLSL...
null
null
DNA amplification [GO:0006277]; DNA replication initiation [GO:0006270]; mitotic DNA replication checkpoint signaling [GO:0033314]
nuclear origin of replication recognition complex [GO:0005664]; nucleus [GO:0005634]
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; chromatin binding [GO:0003682]; DNA replication origin binding [GO:0003688]; metal ion binding [GO:0046872]
PF00004;PF17872;PF01426;PF09079;
1.10.8.60;2.30.30.490;3.40.50.300;
ORC1 family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
null
null
null
null
null
FUNCTION: Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent, however specific DNA sequences that define origins of replication have not been identified so far. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication. {...
Drosophila melanogaster (Fruit fly)
O16829
CECC_DROME
MNFYKIFVFVALILAISIGQSEAGWLKKLGKRIERIGQHTRDATIQGLGIAQQAANVAATARG
null
null
antibacterial humoral response [GO:0019731]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; humoral immune response [GO:0006959]; innate immune response [GO:0045087]
extracellular region [GO:0005576]; extracellular space [GO:0005615]
null
PF00272;
null
Cecropin family
null
SUBCELLULAR LOCATION: Secreted.
null
null
null
null
null
FUNCTION: Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria.
Drosophila melanogaster (Fruit fly)
O16844
COS_DROME
MEIPIQVAVRIFPHRELKDLLRSFGPTEPKKDAQAVDEGADSKDSEAQVPAAEKDNPSISETDPNGNAEQDSAADSKTIPDANGNDSGQKDYPDSAYCVQAIPISASALGLPSALPGGDPMDSIAAGLIQVGPHTVPVTHALPSSSSQEQVYHQTVFPLITLFLEGFDASVVTYGQRGQGKSYTLYGNVQDPTLTDSTEGVVQLCVRDIFSHISLHPERTYAINVGFVEICGGDVCDLLGMGNIHCTNVDAVFHWLQVGLSARQSLPAHTLFTLTLEQQWVSKEGLLQHRLSTASFSDLCGTERCGDQPPGRPLDAGLCM...
null
null
cytoplasmic sequestering of protein [GO:0051220]; follicle cell of egg chamber development [GO:0030707]; imaginal disc-derived wing morphogenesis [GO:0007476]; intraciliary transport [GO:0042073]; microtubule-based movement [GO:0007018]; negative regulation of smoothened signaling pathway [GO:0045879]; regulation of ap...
cilium [GO:0005929]; cytosol [GO:0005829]; Hedgehog signaling complex [GO:0035301]; kinesin complex [GO:0005871]; microtubule [GO:0005874]; microtubule associated complex [GO:0005875]
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cytoskeletal motor activity [GO:0003774]; microtubule binding [GO:0008017]; molecular sequestering activity [GO:0140313]; plus-end-directed microtubule motor activity [GO:0008574]; protein kinase binding [GO:0019901]; RNA polymerase II-specific DNA-binding...
PF00225;
3.40.850.10;
TRAFAC class myosin-kinesin ATPase superfamily, Kinesin family, KIF27 subfamily
PTM: Polyubiquitinated by Ubr3, which leads to proteasomal degradation. {ECO:0000269|PubMed:27195754}.
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9244298}.
null
null
null
null
null
FUNCTION: Regulates cubitus interruptus (ci) processing by recruiting multiple kinases to promote its efficient phosphorylation. Scaffolds multiple kinases and ci into proximity to promote its hyperphosphorylation, which then targets it for SCFSlimb/proteasome-mediated processing to generate its repressor form. Hh sign...
Drosophila melanogaster (Fruit fly)
O16850
FOXO_CAEEL
MQLEQKSSLHCSKCRNFLQKFSQDMQAWNCRELDSPLPSDITLHNLEPARPDSGMSFSTDFDDDFFNLDLHQQERSASFGGVTQYSQQFLREKCSFSPYFHTSLETVDSGRTSLYGSNEQCGQLGGASSNGSTAMLHTPDGSNSHQTSFPSDFRMSESPDDTVSGKKTTTRRNAWGNMSYAELITTAIMASPEKRLTLAQVYEWMVQNVPYFRDKGDSNSSAGWKNSIRHNLSLHSRFMRIQNEGAGKSSWWVINPDAKPGRNPRRTRERSNTIETTTKAQLEKSRRGAKKRIKERALMGSLHSTLNGNSIAGSIQTISH...
null
null
cellular response to heat [GO:0034605]; cellular response to oxidative stress [GO:0034599]; cytoplasmic sequestering of protein [GO:0051220]; dauer larval development [GO:0040024]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; determination of adult ...
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]
14-3-3 protein binding [GO:0071889]; beta-catenin binding [GO:0008013]; DEAD/H-box RNA helicase binding [GO:0017151]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription factor binding [GO:0140297]; enzyme ...
PF00250;
1.10.10.10;
null
PTM: Phosphorylated by akt-1 and/or akt-2 (PubMed:18358814, PubMed:21531333). Phosphorylated by sgk-1 (PubMed:18358814). Phosphorylated by unc-43 (PubMed:23805378). Phosphorylated by jnk-1 (PubMed:15767565). Dephosphorylated by tax-6 in vitro (PubMed:23805378). {ECO:0000269|PubMed:15767565, ECO:0000269|PubMed:18358814,...
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11381260, ECO:0000269|PubMed:11747825, ECO:0000269|PubMed:15767565, ECO:0000269|PubMed:15888317, ECO:0000269|PubMed:17551714, ECO:0000269|PubMed:17894411, ECO:0000269|PubMed:18832074, ECO:0000269|PubMed:19252938, ECO:0000269|PubMed:21531333, ECO:0000269|PubMed:22916022,...
null
null
null
null
null
FUNCTION: Forkhead-type transcription factor (PubMed:9360933). Binds to the promoters of genes that contain the daf-16/FOXO binding element (DBE), TTGTTTAC, in their regulatory region (PubMed:10880363, PubMed:23770237, PubMed:26675724). Functions in the Insulin/IGF-1-like signaling (IIS) mediated pathway which affects ...
Caenorhabditis elegans
O17072
NFYC1_CAEEL
MSQFPEVLDNNLLHAENNETAEYIQNDGTNQSEVFMEHPYTPNMHPINMPSIVEGAVHPYNNLIHHNDAIPPAKYASMRQMTEDFWREKKQKMTEISEEDMLNKSKNMSVPMARVKKIMRIDDDVRNFMIASDAPIFMAQAAEFFIEEMTAMGWQYVSEARRRILQKADIASAVQKSDQFDFLIDFLPPKTVPTTSTNGPGHMSEDSFQDPNMHSDFHQRTSNSSVNRSHHN
null
null
negative regulation of transcription by RNA polymerase II [GO:0000122]; regulation of gene expression [GO:0010468]; regulation of transcription by RNA polymerase II [GO:0006357]; tissue development [GO:0009888]
CCAAT-binding factor complex [GO:0016602]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; perikaryon [GO:0043204]
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription repressor activity [GO:0001217]; protein heterodimerization activity [GO:0046982]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
PF00808;
1.10.20.10;
NFYC/HAP5 subunit family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17574230}. Cytoplasm {ECO:0000269|PubMed:15704008, ECO:0000269|PubMed:17574230}. Perikaryon {ECO:0000269|PubMed:15704008}. Note=Localizes to the cytoplasm of secretory cells and cell bodies of the small ganglia surrounding the pharynx. {ECO:0000269|PubMed:15704008}.
null
null
null
null
null
FUNCTION: Component of sequence-specific heterotrimeric transcription factor (nfya-1-NF-Y and nfya-2-NF-Y) complexes which specifically recognize a 5'-CCAAT-3' box motif found in the promoters of its target genes to regulate their expression and control cellular identity in particular tissue types (PubMed:17574230). In...
Caenorhabditis elegans