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
O75473
LGR5_HUMAN
MDTSRLGVLLSLPVLLQLATGGSSPRSGVLLRGCPTHCHCEPDGRMLLRVDCSDLGLSELPSNLSVFTSYLDLSMNNISQLLPNPLPSLRFLEELRLAGNALTYIPKGAFTGLYSLKVLMLQNNQLRHVPTEALQNLRSLQSLRLDANHISYVPPSCFSGLHSLRHLWLDDNALTEIPVQAFRSLSALQAMTLALNKIHHIPDYAFGNLSSLVVLHLHNNRIHSLGKKCFDGLHSLETLDLNYNNLDEFPTAIRTLSNLKELGFHSNNIRSIPEKAFVGNPSLITIHFYDNPIQFVGRSAFQHLPELRTLTLNGASQITE...
null
null
adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; epithelial cell proliferation involved in renal tubule morphogenesis [GO:2001013]; G protein-coupled receptor signaling pathway [GO:0007186]; hair follicle development [GO:0001942]; inner ear development [GO:0048839]; oocyte differe...
Golgi apparatus [GO:0005794]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; trans-Golgi network membrane [GO:0032588]
G protein-coupled peptide receptor activity [GO:0008528]; G protein-coupled receptor activity [GO:0004930]; protein-hormone receptor activity [GO:0016500]; transmembrane signaling receptor activity [GO:0004888]
PF00001;PF00560;PF13855;PF01462;
1.20.1070.10;3.80.10.10;
G-protein coupled receptor 1 family
null
SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Golgi apparatus, trans-Golgi network membrane; Multi-pass membrane protein. Note=Rapidly and constitutively internalized to the trans-Golgi network at steady state. Internalization to the trans-Golgi network may be the result of phosphorylation at Ser-86...
null
null
null
null
null
FUNCTION: Receptor for R-spondins that potentiates the canonical Wnt signaling pathway and acts as a stem cell marker of the intestinal epithelium and the hair follicle. Upon binding to R-spondins (RSPO1, RSPO2, RSPO3 or RSPO4), associates with phosphorylated LRP6 and frizzled receptors that are activated by extracellu...
Homo sapiens (Human)
O75475
PSIP1_HUMAN
MTRDFKPGDLIFAKMKGYPHWPARVDEVPDGAVKPPTNKLPIFFFGTHETAFLGPKDIFPYSENKEKYGKPNKRKGFNEGLWEIDNNPKVKFSSQQAATKQSNASSDVEVEEKETSVSKEDTDHEEKASNEDVTKAVDITTPKAARRGRKRKAEKQVETEEAGVVTTATASVNLKVSPKRGRPAATEVKIPKPRGRPKMVKQPCPSESDIITEEDKSKKKGQEEKQPKKQPKKDEEGQKEEDKPRKEPDKKEGKKEVESKRKNLAKTGVTSTSDSEEEGDDQEGEKKRKGGRNFQTAHRRNMLKGQHEKEAADRKRKQEE...
null
null
chromatin remodeling [GO:0006338]; mRNA 5'-splice site recognition [GO:0000395]; positive regulation of transcription by RNA polymerase II [GO:0045944]; response to heat [GO:0009408]; response to oxidative stress [GO:0006979]
cytosol [GO:0005829]; euchromatin [GO:0000791]; heterochromatin [GO:0000792]; nuclear periphery [GO:0034399]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
chromatin binding [GO:0003682]; DNA-binding transcription factor binding [GO:0140297]; RNA binding [GO:0003723]; supercoiled DNA binding [GO:0097100]; transcription coactivator activity [GO:0003713]
PF11467;PF00855;
2.30.30.140;1.20.930.10;
HDGF family
PTM: Citrullinated by PADI4. {ECO:0000250|UniProtKB:Q99JF8}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15642333, ECO:0000269|PubMed:9885563}. Note=Remains chromatin-associated throughout the cell cycle.
null
null
null
null
null
FUNCTION: Transcriptional coactivator involved in neuroepithelial stem cell differentiation and neurogenesis. Involved in particular in lens epithelial cell gene regulation and stress responses. May play an important role in lens epithelial to fiber cell terminal differentiation. May play a protective role during stres...
Homo sapiens (Human)
O75477
ERLN1_HUMAN
MNMTQARVLVAAVVGLVAVLLYASIHKIEEGHLAVYYRGGALLTSPSGPGYHIMLPFITTFRSVQTTLQTDEVKNVPCGTSGGVMIYIDRIEVVNMLAPYAVFDIVRNYTADYDKTLIFNKIHHELNQFCSAHTLQEVYIELFDQIDENLKQALQKDLNLMAPGLTIQAVRVTKPKIPEAIRRNFELMEAEKTKLLIAAQKQKVVEKEAETERKKAVIEAEKIAQVAKIRFQQKVMEKETEKRISEIEDAAFLAREKAKADAEYYAAHKYATSNKHKLTPEYLELKKYQAIASNSKIYFGSNIPNMFVDSSCALKYSDIR...
null
null
cholesterol metabolic process [GO:0008203]; ERAD pathway [GO:0036503]; negative regulation of cholesterol biosynthetic process [GO:0045541]; negative regulation of fatty acid biosynthetic process [GO:0045717]; regulation of cholesterol biosynthetic process [GO:0045540]; SREBP signaling pathway [GO:0032933]
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; membrane raft [GO:0045121]; protein-containing complex [GO:0032991]
cholesterol binding [GO:0015485]; ubiquitin protein ligase binding [GO:0031625]
PF01145;
3.30.479.30;
Band 7/mec-2 family
PTM: Deubiquitinated by USP25; leading to stabilization. {ECO:0000269|PubMed:37683630}.
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11118313, ECO:0000269|PubMed:16835267, ECO:0000269|PubMed:19240031}; Single-pass type II membrane protein {ECO:0000269|PubMed:11118313, ECO:0000269|PubMed:16835267, ECO:0000269|PubMed:19240031}. Note=Associated with lipid raft-like domains of the ...
null
null
null
null
null
FUNCTION: Component of the ERLIN1/ERLIN2 complex which mediates the endoplasmic reticulum-associated degradation (ERAD) of inositol 1,4,5-trisphosphate receptors (IP3Rs). Involved in regulation of cellular cholesterol homeostasis by regulation the SREBP signaling pathway (PubMed:37683630). Binds cholesterol and may pro...
Homo sapiens (Human)
O75478
TAD2A_HUMAN
MDRLGPFSNDPSDKPPCRGCSSYLMEPYIKCAECGPPPFFLCLQCFTRGFEYKKHQSDHTYEIMTSDFPVLDPSWTAQEEMALLEAVMDCGFGNWQDVANQMCTKTKEECEKHYMKHFINNPLFASTLLNLKQAEEAKTADTAIPFHSTDDPPRPTFDSLLSRDMAGYMPARADFIEEFDNYAEWDLRDIDFVEDDSDILHALKMAVVDIYHSRLKERQRRKKIIRDHGLINLRKFQLMERRYPKEVQDLYETMRRFARIVGPVEHDKFIESHALEFELRREIKRLQEYRTAGITNFCSARTYDHLKKTREEERLKRTML...
null
null
chromatin remodeling [GO:0006338]; regulation of cell cycle [GO:0051726]; regulation of cell division [GO:0051302]; regulation of DNA-templated transcription [GO:0006355]; regulation of embryonic development [GO:0045995]; regulation of transcription by RNA polymerase II [GO:0006357]; regulation of tubulin deacetylation...
ATAC complex [GO:0140672]; mitotic spindle [GO:0072686]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; SAGA complex [GO:0000124]; SAGA-type complex [GO:0070461]
chromatin binding [GO:0003682]; DNA binding [GO:0003677]; transcription coactivator activity [GO:0003713]; zinc ion binding [GO:0008270]
PF00249;PF04433;
3.30.60.90;1.10.10.60;1.10.10.10;
null
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22644376}. Chromosome {ECO:0000250|UniProtKB:Q8CHV6}.
null
null
null
null
null
FUNCTION: Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4. Required for the function of some acidic activation domains, which activate transcription from a distant site (By similarity). Binds double-stranded DNA. Binds dinucleosomes, probably at the linker region b...
Homo sapiens (Human)
O75486
SUPT3_HUMAN
MNNTAASPMSTATSSSGRSTGKSISFATELQSMMYSLGDARRPLHETAVLVEDVVHTQLINLLQQAAEVSQLRGARVITPEDLLFLMRKDKKKLRRLLKYMFIRDYKSKIVKGIDEDDLLEDKLSGSNNANKRQKIAQDFLNSIDQTGELLAMFEDDEIDEVKQERMERAERQTRIMDSAQYAEFCESRQLSFSKKASKFRDWLDCSSMEIKPNVVAMEILAYLAYETVAQLVDLALLVRQDMVTKAGDPFSHAISATFIQYHNSAESTAACGVEAHSDAIQPCHIREAIRRYSHRIGPLSPFTNAYRRNGMAFLAC
null
null
positive regulation of DNA-templated transcription [GO:0045893]; regulation of DNA repair [GO:0006282]; regulation of DNA-templated transcription [GO:0006355]; regulation of RNA splicing [GO:0043484]; regulation of transcription by RNA polymerase II [GO:0006357]; RNA polymerase II preinitiation complex assembly [GO:005...
nucleoplasm [GO:0005654]; nucleus [GO:0005634]; SAGA complex [GO:0000124]; transcription factor TFIID complex [GO:0005669]; transcription factor TFTC complex [GO:0033276]
protein heterodimerization activity [GO:0046982]; transcription coactivator activity [GO:0003713]
PF02269;
1.10.20.10;
SPT3 family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11564863, ECO:0000269|PubMed:9726987}.
null
null
null
null
null
FUNCTION: Probable transcriptional activator. {ECO:0000269|PubMed:9787080}.
Homo sapiens (Human)
O75487
GPC4_HUMAN
MARFGLPALLCTLAVLSAALLAAELKSKSCSEVRRLYVSKGFNKNDAPLHEINGDHLKICPQGSTCCSQEMEEKYSLQSKDDFKSVVSEQCNHLQAVFASRYKKFDEFFKELLENAEKSLNDMFVKTYGHLYMQNSELFKDLFVELKRYYVVGNVNLEEMLNDFWARLLERMFRLVNSQYHFTDEYLECVSKYTEQLKPFGDVPRKLKLQVTRAFVAARTFAQGLAVAGDVVSKVSVVNPTAQCTHALLKMIYCSHCRGLVTVKPCYNYCSNIMRGCLANQGDLDFEWNNFIDAMLMVAERLEGPFNIESVMDPIDVKIS...
null
null
cell migration [GO:0016477]; regulation of neurotransmitter receptor localization to postsynaptic specialization membrane [GO:0098696]; regulation of presynapse assembly [GO:1905606]; regulation of signal transduction [GO:0009966]; synaptic membrane adhesion [GO:0099560]; Wnt signaling pathway [GO:0016055]
cell surface [GO:0009986]; collagen-containing extracellular matrix [GO:0062023]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; glutamatergic synapse [GO:0098978]; Golgi lumen [GO:0005796]; lysosomal lumen [GO:0043202]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; synapse [GO...
coreceptor activity [GO:0015026]
PF01153;
null
Glypican family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}; Extracellular side {ECO:0000250}.; SUBCELLULAR LOCATION: [Secreted glypican-4]: Secreted, extracellular space {ECO:0000250}.
null
null
null
null
null
FUNCTION: Cell surface proteoglycan that bears heparan sulfate. May be involved in the development of kidney tubules and of the central nervous system (By similarity). {ECO:0000250}.
Homo sapiens (Human)
O75489
NDUS3_HUMAN
MAAAAVARLWWRGILGASALTRGTGRPSVLLLPVRRESAGADTRPTVRPRNDVAHKQLSAFGEYVAEILPKYVQQVQVSCFNELEVCIHPDGVIPVLTFLRDHTNAQFKSLVDLTAVDVPTRQNRFEIVYNLLSLRFNSRIRVKTYTDELTPIESAVSVFKAANWYEREIWDMFGVFFANHPDLRRILTDYGFEGHPFRKDFPLSGYVELRYDDEVKRVVAEPVELAQEFRKFDLNSPWEAFPVYRQPPESLKLEAGDKKPDAK
7.1.1.2
null
aerobic respiration [GO:0009060]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; mitochondrial respiratory chain complex I assembly [GO:0032981]; negative regulation of cell growth [GO:0030308]; negative regulation of intrinsic apoptotic signaling pathway [GO:2001243]; proton motive force-driven mit...
mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrial membrane [GO:0031966]; mitochondrial respiratory chain complex I [GO:0005747]; mitochondrion [GO:0005739]; nuclear body [GO:0016604]
electron transfer activity [GO:0009055]; NADH dehydrogenase (ubiquinone) activity [GO:0008137]; NADH dehydrogenase activity [GO:0003954]
PF00329;
3.30.460.80;
Complex I 30 kDa subunit family
null
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:18826940, ECO:0000305|PubMed:12611891, ECO:0000305|PubMed:17209039}; Peripheral membrane protein {ECO:0000305|PubMed:18826940}; Matrix side {ECO:0000269|PubMed:18826940}.
CATALYTIC ACTIVITY: Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2; Evidence={ECO:0000269|PubMed:14729820, ECO:000026...
null
null
null
null
FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor (PubMed:14729820, PubMed:30140060). Essential for the catalytic activity and assembly of complex I (Pu...
Homo sapiens (Human)
O75494
SRS10_HUMAN
MSRYLRPPNTSLFVRNVADDTRSEDLRREFGRYGPIVDVYVPLDFYTRRPRGFAYVQFEDVRDAEDALHNLDRKWICGRQIEIQFAQGDRKTPNQMKAKEGRNVYSSSRYDDYDRYRRSRSRSYERRRSRSRSFDYNYRRSYSPRNSRPTGRPRRSRSHSDNDRFKHRNRSFSRSKSNSRSRSKSQPKKEMKAKSRSRSASHTKTRGTSKTDSKTHYKSGSRYEKESRKKEPPRSKSQSRSQSRSRSKSRSRSWTSPKSSGH
null
null
cytosolic transport [GO:0016482]; mRNA splice site recognition [GO:0006376]; mRNA splicing, via spliceosome [GO:0000398]; negative regulation of mRNA splicing, via spliceosome [GO:0048025]; regulation of DNA-templated transcription [GO:0006355]; regulation of mRNA splicing, via spliceosome [GO:0048024]; RNA splicing, v...
axon terminus [GO:0043679]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; neuronal cell body [GO:0043025]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
RNA binding [GO:0003723]; RS domain binding [GO:0050733]; unfolded protein binding [GO:0051082]
PF00076;
3.30.70.330;
Splicing factor SR family
PTM: Phosphorylated. Fully dephosphorylated in mitosis and partially dephosphorylated on heat shock. {ECO:0000269|PubMed:12419250, ECO:0000269|PubMed:14765198}.
SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:11684676, ECO:0000269|PubMed:26876937}. Cytoplasm {ECO:0000269|PubMed:11684676}.
null
null
null
null
null
FUNCTION: Splicing factor that in its dephosphorylated form acts as a general repressor of pre-mRNA splicing (PubMed:11684676, PubMed:12419250, PubMed:14765198). Seems to interfere with the U1 snRNP 5'-splice recognition of SNRNP70 (PubMed:14765198). Required for splicing repression in M-phase cells and after heat shoc...
Homo sapiens (Human)
O75496
GEMI_HUMAN
MNPSMKQKQEEIKENIKNSSVPRRTLKMIQPSASGSLVGRENELSAGLSKRKHRNDHLTSTTSSPGVIVPESSENKNLGGVTQESFDLMIKENPSSQYWKEVAEKRRKALYEALKENEKLHKEIEQKDNEIARLKKENKELAEVAEHVQYMAELIERLNGEPLDNFESLDNQEFDSEEETVEDSLVEDSEIGTCAEGTVSSSTDAKPCI
null
null
animal organ morphogenesis [GO:0009887]; DNA replication preinitiation complex assembly [GO:0071163]; negative regulation of cell cycle [GO:0045786]; negative regulation of DNA replication [GO:0008156]; negative regulation of DNA-templated DNA replication [GO:2000104]; negative regulation of DNA-templated transcription...
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription repressor complex [GO:0017053]
chromatin binding [GO:0003682]; DNA-binding transcription factor binding [GO:0140297]; histone deacetylase binding [GO:0042826]; transcription corepressor activity [GO:0003714]
PF07412;
1.20.5.1180;
Geminin family
PTM: Phosphorylated during mitosis. Phosphorylation at Ser-184 by CK2 results in enhanced binding to Hox proteins and more potent inhibitory effect on Hox transcriptional activity. {ECO:0000269|PubMed:22615398, ECO:0000269|PubMed:22645314}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21543332}. Nucleus {ECO:0000269|PubMed:21543332}. Note=Mainly cytoplasmic but can be relocalized to the nucleus. {ECO:0000269|PubMed:21543332}.
null
null
null
null
null
FUNCTION: Inhibits DNA replication by preventing the incorporation of MCM complex into pre-replication complex (pre-RC) (PubMed:14993212, PubMed:20129055, PubMed:24064211, PubMed:9635433). It is degraded during the mitotic phase of the cell cycle (PubMed:14993212, PubMed:24064211, PubMed:9635433). Its destruction at th...
Homo sapiens (Human)
O75503
CLN5_HUMAN
MAQEVDTAQGAEMRRGAGAARGRASWCWALALLWLAVVPGWSRVSGIPSRRHWPVPYKRFDFRPKPDPYCQAKYTFCPTGSPIPVMEGDDDIEVFRLQAPVWEFKYGDLLGHLKIMHDAIGFRSTLTGKNYTMEWYELFQLGNCTFPHLRPEMDAPFWCNQGAACFFEGIDDVHWKENGTLVQVATISGNMFNQMAKWVKQDNETGIYYETWNVKASPEKGAETWFDSYDCSKFVLRTFNKLAEFGAEFKNIETNYTRIFLYSGEPTYLGNETSVFGPTGNKTLGLAIKRFYYPFKPHLPTKEFLLSLLQIFDAVIVHKQ...
2.3.1.-; 3.1.2.22
null
brain development [GO:0007420]; glycosylation [GO:0070085]; lysosomal lumen acidification [GO:0007042]; lysosome organization [GO:0007040]; neurogenesis [GO:0022008]; neuron maturation [GO:0042551]; positive regulation of GTP binding [GO:1904426]; protein catabolic process [GO:0030163]; retrograde transport, endosome t...
cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; membrane [GO:0016020]; perinuclear region of cytoplasm [GO:0048471]; vacuolar lumen [GO:0005775]
bis(monoacylglycero)phosphate synthase activity [GO:0160121]; hydrolase activity, acting on glycosyl bonds [GO:0016798]; long-chain fatty acyl-CoA hydrolase activity [GO:0052816]; mannose binding [GO:0005537]
PF15014;
null
CLN5 family
PTM: N-glycosylated with both high mannose and complex type sugars. Glycosylation is important for proper folding and trafficking to the lysosomes. {ECO:0000269|PubMed:11971870, ECO:0000269|PubMed:20052765, ECO:0000269|PubMed:24038957, ECO:0000269|PubMed:24058541, ECO:0000269|PubMed:37708259}.; PTM: [Bis(monoacylglycer...
SUBCELLULAR LOCATION: [Bis(monoacylglycero)phosphate synthase CLN5, secreted form]: Lysosome {ECO:0000269|PubMed:11971870, ECO:0000269|PubMed:20052765, ECO:0000269|PubMed:22431521, ECO:0000269|PubMed:24038957, ECO:0000269|PubMed:24058541, ECO:0000269|PubMed:28442266, ECO:0000269|PubMed:37708259}.; SUBCELLULAR LOCATION:...
CATALYTIC ACTIVITY: Reaction=H2O + S-hexadecanoyl-L-cysteinyl-[protein] = H(+) + hexadecanoate + L-cysteinyl-[protein]; Xref=Rhea:RHEA:19233, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:74151; EC=3.1.2.22; Evidence={ECO:0000269|PubMe...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.3 uM for lysophosphatidylglycerol 18:1 (at pH 5) {ECO:0000269|PubMed:37708259}; KM=4.752 uM for lysophosphatidylglycerol 18:1 (at pH 6.5) {ECO:0000269|PubMed:37708259};
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5 for bis(monoacylglycero)phosphate synthase activity (PubMed:37708259). Optimum pH of 6.5 and 8.5 is seen for palmitoyl thioesterase activity (PubMed:35427157). {ECO:0000269|PubMed:35427157, ECO:0000269|PubMed:37708259};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Thermostable. {ECO:0000269|PubMed:37708259};
FUNCTION: [Bis(monoacylglycero)phosphate synthase CLN5, secreted form]: Catalyzes the synthesis of bis(monoacylglycero)phosphate (BMP) via transacylation of 2 molecules of lysophosphatidylglycerol (LPG) (PubMed:37708259). BMP also known as lysobisphosphatidic acid plays a key role in the formation of intraluminal vesic...
Homo sapiens (Human)
O75506
HSBP1_HUMAN
MAETDPKTVQDLTSVVQTLLQQMQDKFQTMSDQIIGRIDDMSSRIDDLEKNIADLMTQAGVEELESENKIPATQKS
null
null
axonal transport of mitochondrion [GO:0019896]; cellular heat acclimation [GO:0070370]; endodermal cell differentiation [GO:0035987]; negative regulation of transcription by RNA polymerase II [GO:0000122]
axon cytoplasm [GO:1904115]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
identical protein binding [GO:0042802]; transcription corepressor activity [GO:0003714]
PF06825;
1.20.5.430;
HSBP1 family
null
SUBCELLULAR LOCATION: Nucleus.
null
null
null
null
null
FUNCTION: Negative regulator of the heat shock response. Negatively affects HSF1 DNA-binding activity. May have a role in the suppression of the activation of the stress response during the aging process.
Homo sapiens (Human)
O75508
CLD11_HUMAN
MVATCLQVVGFVTSFVGWIGVIVTTSTNDWVVTCGYTIPTCRKLDELGSKGLWADCVMATGLYHCKPLVDILILPGYVQACRALMIAASVLGLPAILLLLTVLPCIRMGQEPGVAKYRRAQLAGVLLILLALCALVATIWFPVCAHRETTIVSFGYSLYAGWIGAVLCLVGGCVILCCAGDAQAFGENRFYYTAGSSSPTHAKSAHV
null
null
axon ensheathment [GO:0008366]; bicellular tight junction assembly [GO:0070830]; calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules [GO:0016338]; cell adhesion [GO:0007155]; spermatogenesis [GO:0007283]; tight junction assembly [GO:0120192]
axon [GO:0030424]; basal part of cell [GO:0045178]; bicellular tight junction [GO:0005923]; cell junction [GO:0030054]; lipid droplet [GO:0005811]; neurofilament [GO:0005883]; plasma membrane [GO:0005886]; tight junction [GO:0070160]
identical protein binding [GO:0042802]; structural molecule activity [GO:0005198]
PF00822;
1.20.140.150;
Claudin family
null
SUBCELLULAR LOCATION: Cell junction, tight junction. Cell membrane {ECO:0000269|PubMed:20375010}; Multi-pass membrane protein {ECO:0000255}.
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}.
Homo sapiens (Human)
O75509
TNR21_HUMAN
MGTSPSSSTALASCSRIARRATATMIAGSLLLLGFLSTTTAQPEQKASNLIGTYRHVDRATGQVLTCDKCPAGTYVSEHCTNTSLRVCSSCPVGTFTRHENGIEKCHDCSQPCPWPMIEKLPCAALTDRECTCPPGMFQSNATCAPHTVCPVGWGVRKKGTETEDVRCKQCARGTFSDVPSSVMKCKAYTDCLSQNLVVIKPGTKETDNVCGTLPSFSSSTSPSPGTAIFPRPEHMETHEVPSSTYVPKGMNSTESNSSASVRPKVLSSIQEGTVPDNTSSARGKEDVNKTLPNLQVVNHQQGPHHRHILKLLPSMEATG...
null
null
adaptive immune response [GO:0002250]; apoptotic process [GO:0006915]; axonal fasciculation [GO:0007413]; B cell apoptotic process [GO:0001783]; cellular response to tumor necrosis factor [GO:0071356]; humoral immune response [GO:0006959]; myelination [GO:0042552]; negative regulation of B cell proliferation [GO:003088...
axon [GO:0030424]; plasma membrane [GO:0005886]
null
PF00531;PF00020;
1.10.533.10;2.10.50.10;
null
PTM: Oxidized in response to reactive oxygen species (ROS), leading to endocytosis. {ECO:0000269|PubMed:34012073}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19654028}; Single-pass type I membrane protein {ECO:0000269|PubMed:19654028}. Note=Endocytosed following oxidation in response to reactive oxygen species (ROS). {ECO:0000269|PubMed:34012073}.
null
null
null
null
null
FUNCTION: Promotes apoptosis, possibly via a pathway that involves the activation of NF-kappa-B. Can also promote apoptosis mediated by BAX and by the release of cytochrome c from the mitochondria into the cytoplasm. Plays a role in neuronal apoptosis, including apoptosis in response to amyloid peptides derived from AP...
Homo sapiens (Human)
O75521
ECI2_HUMAN
MAMAYLAWRLARRSCPSSLQVTSFPVVQLHMNRTAMRASQKDFENSMNQVKLLKKDPGNEVKLKLYALYKQATEGPCNMPKPGVFDLINKAKWDAWNALGSLPKEAARQNYVDLVSSLSPSLESSSQVEPGTDRKSTGFETLVVTSEDGITKIMFNRPKKKNAINTEMYHEIMRALKAASKDDSIITVLTGNGDYYSSGNDLTNFTDIPPGGVEEKAKNNAVLLREFVGCFIDFPKPLIAVVNGPAVGISVTLLGLFDAVYASDRATFHTPFSHLGQSPEGCSSYTFPKIMSPAKATEMLIFGKKLTAGEACAQGLVTEV...
5.3.3.8
null
fatty acid beta-oxidation [GO:0006635]; fatty acid catabolic process [GO:0009062]
cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; mitochondrion [GO:0005739]; peroxisomal matrix [GO:0005782]; peroxisome [GO:0005777]
delta(3)-delta(2)-enoyl-CoA isomerase activity [GO:0004165]; fatty-acyl-CoA binding [GO:0000062]
PF00887;PF00378;
1.20.80.10;1.10.12.10;
Enoyl-CoA hydratase/isomerase family
null
SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion {ECO:0000250|UniProtKB:Q5XIC0}.; SUBCELLULAR LOCATION: [Isoform 2]: Peroxisome matrix {ECO:0000269|PubMed:10419495}.
CATALYTIC ACTIVITY: Reaction=a (3Z)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA; Xref=Rhea:RHEA:45900, ChEBI:CHEBI:85097, ChEBI:CHEBI:85489; EC=5.3.3.8; Evidence={ECO:0000305|PubMed:10419495}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45901; Evidence={ECO:0000305|PubMed:10419495}; CATALYTIC ACTIVITY: Reaction=(...
null
PATHWAY: Lipid metabolism; fatty acid beta-oxidation. {ECO:0000269|PubMed:10419495}.
null
null
FUNCTION: Able to isomerize both 3-cis and 3-trans double bonds into the 2-trans form in a range of enoyl-CoA species. Has a preference for 3-trans substrates. {ECO:0000269|PubMed:10419495}.
Homo sapiens (Human)
O75525
KHDR3_HUMAN
MEEKYLPELMAEKDSLDPSFTHALRLVNQEIEKFQKGEGKDEEKYIDVVINKNMKLGQKVLIPVKQFPKFNFVGKLLGPRGNSLKRLQEETLTKMSILGKGSMRDKAKEEELRKSGEAKYFHLNDDLHVLIEVFAPPAEAYARMGHALEEIKKFLIPDYNDEIRQAQLQELTYLNGGSENADVPVVRGKPTLRTRGVPAPAITRGRGGVTARPVGVVVPRGTPTPRGVLSTRGPVSRGRGLLTPRARGVPPTGYRPPPPPPTQETYGEYDYDDGYGTAYDEQSYDSYDNSYSTPAQSGADYYDYGHGLSEETYDSYGQEE...
null
null
mRNA processing [GO:0006397]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]
nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]
identical protein binding [GO:0042802]; mRNA binding [GO:0003729]; protein domain specific binding [GO:0019904]; RNA binding [GO:0003723]; SH3 domain binding [GO:0017124]
PF16274;PF16568;
3.30.1370.10;
KHDRBS family
PTM: Phosphorylated on tyrosine residues. Isoform 1 C-terminal region is tyrosine-rich, but isoform 2 lacking this C-terminal region is also tyrosine-phosphorylated. {ECO:0000269|PubMed:10564820}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10332027, ECO:0000269|PubMed:15901763}. Note=Localized in a compartment adjacent to the nucleolus, but distinct from the peri-nucleolar one.
null
null
null
null
null
FUNCTION: RNA-binding protein that plays a role in the regulation of alternative splicing and influences mRNA splice site selection and exon inclusion. Binds preferentially to the 5'-[AU]UAAA-3' motif in vitro. Binds optimally to RNA containing 5'-[AU]UAA-3' as a bipartite motif spaced by more than 15 nucleotides. Bind...
Homo sapiens (Human)
O75528
TADA3_HUMAN
MSELKDCPLQFHDFKSVDHLKVCPRYTAVLARSEDDGIGIEELDTLQLELETLLSSASRRLRVLEAETQILTDWQDKKGDRRFLKLGRDHELGAPPKHGKPKKQKLEGKAGHGPGPGPGRPKSKNLQPKIQEYEFTDDPIDVPRIPKNDAPNRFWASVEPYCADITSEEVRTLEELLKPPEDEAEHYKIPPLGKHYSQRWAQEDLLEEQKDGARAAAVADKKKGLMGPLTELDTKDVDALLKKSEAQHEQPEDGCPFGALTQRLLQALVEENIISPMEDSPIPDMSGKESGADGASTSPRNQNKPFSVPHTKSLESRIKE...
null
null
chromatin organization [GO:0006325]; intracellular estrogen receptor signaling pathway [GO:0030520]; mitotic cell cycle [GO:0000278]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of gene expression [GO:001062...
ATAC complex [GO:0140672]; mitotic spindle [GO:0072686]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; SAGA complex [GO:0000124]; transcription factor TFTC complex [GO:0033276]
nuclear receptor binding [GO:0016922]; nuclear receptor coactivator activity [GO:0030374]; protein domain specific binding [GO:0019904]; transcription coactivator activity [GO:0003713]
PF10198;
null
NGG1 family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11564863, ECO:0000269|PubMed:9674425}.
null
null
null
null
null
FUNCTION: Functions as a component of the PCAF complex. The PCAF complex is capable of efficiently acetylating histones in a nucleosomal context. The PCAF complex could be considered as the human version of the yeast SAGA complex. Also known as a coactivator for p53/TP53-dependent transcriptional activation. Component ...
Homo sapiens (Human)
O75529
TAF5L_HUMAN
MKRVRTEQIQMAVSCYLKRRQYVDSDGPLKQGLRLSQTAEEMAANLTVQSESGCANIVSAAPCQAEPQQYEVQFGRLRNFLTDSDSQHSHEVMPLLYPLFVYLHLNLVQNSPKSTVESFYSRFHGMFLQNASQKDVIEQLQTTQTIQDILSNFKLRAFLDNKYVVRLQEDSYNYLIRYLQSDNNTALCKVLTLHIHLDVQPAKRTDYQLYASGSSSRSENNGLEPPDMPSPILQNEAALEVLQESIKRVKDGPPSLTTICFYAFYNTEQLLNTAEISPDSKLLAAGFDNSCIKLWSLRSKKLKSEPHQVDVSRIHLACDI...
null
null
positive regulation of DNA-templated transcription [GO:0045893]; regulation of DNA repair [GO:0006282]; regulation of DNA-templated transcription [GO:0006355]; regulation of RNA splicing [GO:0043484]; regulation of somatic stem cell population maintenance [GO:1904672]; regulation of transcription by RNA polymerase II [...
cytoplasmic ribonucleoprotein granule [GO:0036464]; histone acetyltransferase complex [GO:0000123]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; SAGA complex [GO:0000124]; transcription factor TFTC complex [GO:0033276]
transcription coactivator activity [GO:0003713]
PF04494;PF00400;
1.25.40.500;2.130.10.10;
WD repeat TAF5 family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11564863, ECO:0000269|PubMed:9674425}.
null
null
null
null
null
FUNCTION: Functions as a component of the PCAF complex. The PCAF complex is capable of efficiently acetylating histones in a nucleosomal context. The PCAF complex could be considered as the human version of the yeast SAGA complex (Probable). With TAF6L, acts as an epigenetic regulator essential for somatic reprogrammin...
Homo sapiens (Human)
O75530
EED_HUMAN
MSEREVSTAPAGTDMPAAKKQKLSSDENSNPDLSGDENDDAVSIESGTNTERPDTPTNTPNAPGRKSWGKGKWKSKKCKYSFKCVNSLKEDHNQPLFGVQFNWHSKEGDPLVFATVGSNRVTLYECHSQGEIRLLQSYVDADADENFYTCAWTYDSNTSHPLLAVAGSRGIIRIINPITMQCIKHYVGHGNAINELKFHPRDPNLLLSVSKDHALRLWNIQTDTLVAIFGGVEGHRDEVLSADYDLLGEKIMSCGMDHSLKLWRINSKRMMNAIKESYDYNPNKTNRPFISQKIHFPDFSTRDIHRNYVDCVRWLGDLIL...
null
null
negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of transcription by RNA polymerase II [GO:0000122]; spinal cord development [GO:0021510]
chromosome [GO:0005694]; cytosol [GO:0005829]; ESC/E(Z) complex [GO:0035098]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
enzyme activator activity [GO:0008047]; histone methyltransferase activity [GO:0042054]; identical protein binding [GO:0042802]; nucleosome binding [GO:0031491]; transcription corepressor binding [GO:0001222]
PF00400;
2.130.10.10;
WD repeat ESC family
PTM: Methylated. Binding to histone H1 'Lys-26' promotes mono-, di-, and trimethylation of internal lysines. {ECO:0000269|PubMed:20974918}.
SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Transiently colocalizes with XIST at inactive X chromosomes.
null
null
null
null
null
FUNCTION: Polycomb group (PcG) protein. Component of the PRC2/EED-EZH2 complex, which methylates 'Lys-9' and 'Lys-27' of histone H3, leading to transcriptional repression of the affected target gene. Also recognizes 'Lys-26' trimethylated histone H1 with the effect of inhibiting PRC2 complex methyltransferase activity ...
Homo sapiens (Human)
O75531
BAF_HUMAN
MTTSQKHRDFVAEPMGEKPVGSLAGIGEVLGKKLEERGFDKAYVVLGQFLVLKKDEDLFREWLKDTCGANAKQSRDCFGCLREWCDAFL
null
null
chromatin organization [GO:0006325]; chromosome organization [GO:0051276]; DNA integration [GO:0015074]; mitotic nuclear membrane reassembly [GO:0007084]; negative regulation of cGAS/STING signaling pathway [GO:0160049]; negative regulation of innate immune response [GO:0045824]; negative regulation of protein ADP-ribo...
chromatin [GO:0000785]; condensed chromosome [GO:0000793]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nuclear envelope [GO:0005635]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
DNA binding [GO:0003677]; double-stranded DNA binding [GO:0003690]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]
PF02961;
1.10.150.40;
BAF family
PTM: Ser-4 is the major site of phosphorylation as compared to Thr-2 and Thr-3. Phosphorylation on Thr-2; Thr-3 and Ser-4 disrupts its ability to bind DNA and reduces its ability to bind LEM domain-containing proteins. Non phosphorylated BAF seems to enhance binding between EMD and LMNA. Dephosphorylated by protein pho...
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16495336, ECO:0000269|PubMed:18005698, ECO:0000269|PubMed:24600006}. Chromosome {ECO:0000269|PubMed:16495336, ECO:0000269|PubMed:28841419, ECO:0000269|PubMed:31796734, ECO:0000269|PubMed:32792394}. Nucleus envelope {ECO:0000269|PubMed:24600006}. Cytoplasm {ECO:0000269|P...
null
null
null
null
null
FUNCTION: Non-specific DNA-binding protein that plays key roles in mitotic nuclear reassembly, chromatin organization, DNA damage response, gene expression and intrinsic immunity against foreign DNA (PubMed:10908652, PubMed:11792822, PubMed:12163470, PubMed:18005698, PubMed:25991860, PubMed:28841419, PubMed:31796734, P...
Homo sapiens (Human)
O75533
SF3B1_HUMAN
MAKIAKTHEDIEAQIREIQGKKAALDEAQGVGLDSTGYYDQEIYGGSDSRFAGYVTSIAATELEDDDDDYSSSTSLLGQKKPGYHAPVALLNDIPQSTEQYDPFAEHRPPKIADREDEYKKHRRTMIISPERLDPFADGGKTPDPKMNARTYMDVMREQHLTKEEREIRQQLAEKAKAGELKVVNGAAASQPPSKRKRRWDQTADQTPGATPKKLSSWDQAETPGHTPSLRWDETPGRAKGSETPGATPGSKIWDPTPSHTPAGAATPGRGDTPGHATPGHGGATSSARKNRWDETPKTERDTPGHGSGWAETPRTDRGG...
null
null
chromatin remodeling [GO:0006338]; mRNA splicing, via spliceosome [GO:0000398]; positive regulation of transcription by RNA polymerase I [GO:0045943]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of transcription by RNA polymerase III [GO:0045945]; RNA splicing [GO:0008380...
B-WICH complex [GO:0110016]; catalytic step 2 spliceosome [GO:0071013]; nuclear speck [GO:0016607]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spliceosomal complex [GO:0005681]; U11/U12 snRNP [GO:0034693]; U12-type spliceosomal complex [GO:0005689]; U2 snRNP [GO:0005686]; U2-type precatalyt...
mRNA binding [GO:0003729]; RNA binding [GO:0003723]; splicing factor binding [GO:1990935]
PF08920;
1.25.10.10;
SF3B1 family
PTM: Phosphorylated. Phosphorylation occurs concomitantly with the splicing catalytic steps. Phosphorylation on Thr-244, Thr-248 and Thr-313 by cyclin-dependent kinases promotes interaction with PPP1R8 during mitosis. {ECO:0000269|PubMed:12105215, ECO:0000269|PubMed:9585501}.; PTM: Citrullinated by PADI4. {ECO:0000250|...
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27720643, ECO:0000269|PubMed:28541300, ECO:0000269|PubMed:34023904}. Nucleus speckle {ECO:0000269|PubMed:12105215, ECO:0000269|PubMed:28541300, ECO:0000269|PubMed:34023904}. Note=During mitosis, transiently dispersed from the nuclear speckles to the cytoplasm. {ECO:0000...
null
null
null
null
null
FUNCTION: Component of the 17S U2 SnRNP complex of the spliceosome, a large ribonucleoprotein complex that removes introns from transcribed pre-mRNAs (PubMed:12234937, PubMed:27720643, PubMed:32494006, PubMed:34822310). The 17S U2 SnRNP complex (1) directly participates in early spliceosome assembly and (2) mediates re...
Homo sapiens (Human)
O75534
CSDE1_HUMAN
MSFDPNLLHNNGHNGYPNGTSAALRETGVIEKLLTSYGFIQCSERQARLFFHCSQYNGNLQDLKVGDDVEFEVSSDRRTGKPIAVKLVKIKQEILPEERMNGQVVCAVPHNLESKSPAAPGQSPTGSVCYERNGEVFYLTYTPEDVEGNVQLETGDKINFVIDNNKHTGAVSARNIMLLKKKQARCQGVVCAMKEAFGFIERGDVVKEIFFHYSEFKGDLETLQPGDDVEFTIKDRNGKEVATDVRLLPQGTVIFEDISIEHFEGTVTKVIPKVPSKNQNDPLPGRIKVDFVIPKELPFGDKDTKSKVTLLEGDHVRFNI...
null
null
CRD-mediated mRNA stabilization [GO:0070934]; IRES-dependent viral translational initiation [GO:0075522]; male gonad development [GO:0008584]; negative regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:1900152]; nuclear-transcribed mRNA catabolic process, no-go decay [GO:007096...
CRD-mediated mRNA stability complex [GO:0070937]; cytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; mCRD-mediated mRNA stability complex [GO:0106002]; P-body [GO:0000932]; plasma membrane [GO:0005886]
RISC complex binding [GO:1905172]; RNA binding [GO:0003723]; RNA stem-loop binding [GO:0035613]
PF00313;PF12901;
2.40.50.140;
UNR family
null
SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, Stress granule {ECO:0000305|PubMed:29395067}. Cytoplasm, P-body {ECO:0000269|PubMed:32354837}.
null
null
null
null
null
FUNCTION: RNA-binding protein involved in translationally coupled mRNA turnover (PubMed:11051545, PubMed:15314026). Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain (...
Homo sapiens (Human)
O75553
DAB1_HUMAN
MSTETELQVAVKTSAKKDSRKKGQDRSEATLIKRFKGEGVRYKAKLIGIDEVSAARGDKLCQDSMMKLKGVVAGARSKGEHKQKIFLTISFGGIKIFDEKTGALQHHHAVHEISYIAKDITDHRAFGYVCGKEGNHRFVAIKTAQAAEPVILDLRDLFQLIYELKQREELEKKAQKDKQCEQAVYQTILEEDVEDPVYQYIVFEAGHEPIRDPETEENIYQVPTSQKKEGVYDVPKSQPVSNGYSFEDFEERFAAATPNRNLPTDFDEIFEATKAVTQLELFGDMSTPPDITSPPTPATPGDAFIPSSSQTLPASADVFS...
null
null
adult walking behavior [GO:0007628]; astrocyte differentiation [GO:0048708]; axonogenesis [GO:0007409]; cell-cell adhesion involved in neuronal-glial interactions involved in cerebral cortex radial glia guided migration [GO:0021813]; cerebellum structural organization [GO:0021589]; dendrite development [GO:0016358]; Go...
cytoplasm [GO:0005737]; cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; perinuclear region of cytoplasm [GO:0048471]
null
PF21792;PF00640;
2.30.29.30;
null
PTM: Phosphorylated on Tyr-198 and Tyr-220 upon reelin induction in embryonic neurons. Also phosphorylated on Ser-524 independently of reelin signaling. {ECO:0000250|UniProtKB:P97318}.
null
null
null
null
null
null
FUNCTION: Adapter molecule functioning in neural development. May regulate SIAH1 activity. {ECO:0000250|UniProtKB:P97318}.
Homo sapiens (Human)
O75554
WBP4_HUMAN
MADYWKSQPKKFCDYCKCWIADNRPSVEFHERGKNHKENVAKRISEIKQKSLDKAKEEEKASKEFAAMEAAALKAYQEDLKRLGLESEILEPSITPVTSTIPPTSTSNQQKEKKEKKKRKKDPSKGRWVEGITSEGYHYYYDLISGASQWEKPEGFQGDLKKTAVKTVWVEGLSEDGFTYYYNTETGESRWEKPDDFIPHTSDLPSSKVNENSLGTLDESKSSDSHSDSDGEQEAEEGGVSTETEKPKIKFKEKNKNSDGGSDPETQKEKSIQKQNSLGSNEEKSKTLKKSNPYGEWQEIKQEVESHEEVDLELPSTENE...
null
null
mRNA cis splicing, via spliceosome [GO:0045292]; mRNA splicing, via spliceosome [GO:0000398]; RNA splicing [GO:0008380]
nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; precatalytic spliceosome [GO:0071011]; U2-type precatalytic spliceosome [GO:0071005]
proline-rich region binding [GO:0070064]; RNA binding [GO:0003723]; zinc ion binding [GO:0008270]
PF00397;PF06220;
2.20.70.10;3.30.160.60;
null
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28781166}. Nucleus speckle {ECO:0000255|PROSITE-ProRule:PRU00130, ECO:0000269|PubMed:19592703, ECO:0000269|PubMed:9724750}.
null
null
null
null
null
FUNCTION: Involved in pre-mRNA splicing as a component of the spliceosome (PubMed:19592703, PubMed:28781166, PubMed:9724750). May play a role in cross-intron bridging of U1 and U2 snRNPs in the mammalian A complex (PubMed:9724750). {ECO:0000269|PubMed:19592703, ECO:0000269|PubMed:28781166, ECO:0000269|PubMed:9724750}.
Homo sapiens (Human)
O75556
SG2A1_HUMAN
MKLLMVLMLAALLLHCYADSGCKLLEDMVEKTINSDISIPEYKELLQEFIDSDAAAEAMGKFKQCFLNQSHRTLKNFGLMMHTVYDSIWCNMKSN
null
null
androgen receptor signaling pathway [GO:0030521]
extracellular space [GO:0005615]
null
PF01099;
null
Secretoglobin family, Lipophilin subfamily
null
SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
null
null
null
null
null
FUNCTION: May bind androgens and other steroids, may also bind estramustine, a chemotherapeutic agent used for prostate cancer. May be under transcriptional regulation of steroid hormones.
Homo sapiens (Human)
O75558
STX11_HUMAN
MKDRLAELLDLSKQYDQQFPDGDDEFDSPHEDIVFETDHILESLYRDIRDIQDENQLLVADVKRLGKQNARFLTSMRRLSSIKRDTNSIAKAIKARGEVIHCKLRAMKELSEAAEAQHGPHSAVARISRAQYNALTLTFQRAMHDYNQAEMKQRDNCKIRIQRQLEIMGKEVSGDQIEDMFEQGKWDVFSENLLADVKGARAALNEIESRHRELLRLESRIRDVHELFLQMAVLVEKQADTLNVIELNVQKTVDYTGQAKAQVRKAVQYEEKNPCRTLCCFCCPCLK
null
null
exocytosis [GO:0006887]; intracellular protein transport [GO:0006886]; membrane fusion [GO:0061025]; synaptic vesicle fusion to presynaptic active zone membrane [GO:0031629]; vesicle docking [GO:0048278]
endomembrane system [GO:0012505]; Golgi apparatus [GO:0005794]; plasma membrane [GO:0005886]; presynaptic active zone membrane [GO:0048787]; SNARE complex [GO:0031201]; synaptic vesicle [GO:0008021]
SNAP receptor activity [GO:0005484]; SNARE binding [GO:0000149]
PF00804;
1.20.5.110;1.20.58.70;
Syntaxin family
null
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
null
null
null
null
null
FUNCTION: SNARE that acts to regulate protein transport between late endosomes and the trans-Golgi network.
Homo sapiens (Human)
O75563
SKAP2_HUMAN
MPNPSSTSSPYPLPEEIRNLLADVETFVADILKGENLSKKAKEKRESLIKKIKDVKSIYLQEFQDKGDAEDGEEYDDPFAGPPDTISLASERYDKDDEAPSDGAQFPPIAAQDLPFVLKAGYLEKRRKDHSFLGFEWQKRWCALSKTVFYYYGSDKDKQQKGEFAIDGYSVRMNNTLRKDGKKDCCFEISAPDKRIYQFTAASPKDAEEWVQQLKFVLQDMESDIIPEDYDERGELYDDVDHPLPISNPLTSSQPIDDEIYEELPEEEEDSAPVKVEEQRKMSQDSVHHTSGDKSTDYANFYQGLWDCTGAFSDELSFKR...
null
null
B cell activation [GO:0042113]; negative regulation of cell population proliferation [GO:0008285]; signal transduction [GO:0007165]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]
null
PF00169;PF00018;
6.10.250.220;2.30.29.30;2.30.30.40;
SKAP family
PTM: Phosphorylated in resting platelets. Phosphorylated by FYN on Tyr-261 upon T-cell activation (Probable). Dephosphorylated on Tyr-75 by PTPN22. {ECO:0000269|PubMed:10942756, ECO:0000269|PubMed:12893833, ECO:0000269|PubMed:21719704, ECO:0000269|PubMed:9671755, ECO:0000269|PubMed:9755858, ECO:0000305}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12893833}.
null
null
null
null
null
FUNCTION: May be involved in B-cell and macrophage adhesion processes. In B-cells, may act by coupling the B-cell receptor (BCR) to integrin activation. May play a role in src signaling pathway. {ECO:0000269|PubMed:12893833, ECO:0000269|PubMed:9837776}.
Homo sapiens (Human)
O75564
JERKY_HUMAN
MASKPAAGKSRGEKRKRVVLTLKEKIDICTRLEKGESRKALMQEYNVGMSTLYDIRAHKAQLLRFFASSDSNKALEQRRTLHTPKLEHLDRVLYEWFLGKRSEGVPVSGPMLIEKAKDFYEQMQLTEPCVFSGGWLWRFKARHGIKKLDASSEKQSADHQAAEQFCAFFRSLAAEHGLSAEQVYNADETGLFWRCLPNPTPEGGAVPGPKQGKDRLTVLMCANATGSHRLKPLAIGKCSGPRAFKGIQHLPVAYKAQGNAWVDKEIFSDWFHHIFVPSVREHFRTIGLPEDSKAVLLLDSSRAHPQEAELVSSNVFTIFL...
null
null
positive regulation of canonical Wnt signaling pathway [GO:0090263]
cytoplasm [GO:0005737]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:1990904]
DNA binding [GO:0003677]; mRNA binding [GO:0003729]
PF04218;PF03184;PF03221;
1.10.10.60;
Tigger transposable element derived protein family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00583}.
null
null
null
null
null
FUNCTION: May bind DNA. {ECO:0000250}.
Homo sapiens (Human)
O75569
PRKRA_HUMAN
MSQSRHRAEAPPLEREDSGTFSLGKMITAKPGKTPIQVLHEYGMKTKNIPVYECERSDVQIHVPTFTFRVTVGDITCTGEGTSKKLAKHRAAEAAINILKANASICFAVPDPLMPDPSKQPKNQLNPIGSLQELAIHHGWRLPEYTLSQEGGPAHKREYTTICRLESFMETGKGASKKQAKRNAAEKFLAKFSNISPENHISLTNVVGHSLGCTWHSLRNSPGEKINLLKRSLLSIPNTDYIQLLSEIAKEQGFNITYLDIDELSANGQYQCLAELSTSPITVCHGSGISCGNAQSDAAHNALQYLKIIAERK
null
null
antiviral innate immune response [GO:0140374]; cellular response to oxidative stress [GO:0034599]; immune response [GO:0006955]; middle ear morphogenesis [GO:0042474]; miRNA processing [GO:0035196]; negative regulation of cell population proliferation [GO:0008285]; outer ear morphogenesis [GO:0042473]; positive regulat...
cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; RISC complex [GO:0016442]; RISC-loading complex [GO:0070578]
double-stranded RNA binding [GO:0003725]; enzyme activator activity [GO:0008047]; enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; pre-miRNA binding [GO:0070883]; protein homodimerization activity [GO:0042803]; protein kinase activator activity [GO:0030295]; RNA binding [GO:0003723]; siRNA binding [...
PF00035;
3.30.160.20;
PRKRA family
PTM: Phosphorylated at Ser-246 in unstressed cells and at Ser-287 in stressed cells. Phosphorylation at Ser-246 appears to be a prerequisite for subsequent phosphorylation at Ser-287. Phosphorylation at Ser-246 and Ser-287 are necessary for activation of EIF2AK2/PKR under conditions of stress. {ECO:0000269|PubMed:16982...
SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Cytoplasm.
null
null
null
null
null
FUNCTION: Activates EIF2AK2/PKR in the absence of double-stranded RNA (dsRNA), leading to phosphorylation of EIF2S1/EFI2-alpha and inhibition of translation and induction of apoptosis. Required for siRNA production by DICER1 and for subsequent siRNA-mediated post-transcriptional gene silencing. Does not seem to be requ...
Homo sapiens (Human)
O75570
RF1M_HUMAN
MNRHLCVWLFRHPSLNGYLQCHIQLHSHQFRQIHLDTRLQVFRQNRNCILHLLSKNWSRRYCHQDTKMLWKHKALQKYMENLSKEYQTLEQCLQHIPVNEENRRSLNRRHAELAPLAAIYQEIQETEQAIEELESMCKSLNKQDEKQLQELALEERQTIDQKINMLYNELFQSLVPKEKYDKNDVILEVTAGRTTGGDICQQFTREIFDMYQNYSCYKHWQFELLNYTPADYGGLHHAAARISGDGVYKHLKYEGGIHRVQRIPEVGLSSRMQRIHTGTMSVIVLPQPDEVDVKLDPKDLRIDTFRAKGAGGQHVNKTDS...
null
null
mitochondrial translational termination [GO:0070126]
mitochondrion [GO:0005739]
translation release factor activity [GO:0003747]; translation release factor activity, codon specific [GO:0016149]
PF03462;PF00472;
3.30.160.20;3.30.70.1660;6.10.140.1950;
Prokaryotic/mitochondrial release factor family
PTM: Methylation of glutamine in the GGQ triplet by HEMK1 is conserved from bacteria to mammals. {ECO:0000269|PubMed:35260756}.
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:17803939, ECO:0000269|PubMed:37141370}.
null
null
null
null
null
FUNCTION: Mitochondrial peptide chain release factor that directs the termination of translation in response to the peptide chain non-canonical stop codons AGG and AGA (PubMed:36302763, PubMed:36596788, PubMed:37141370). Non-canonical termination codons AGG and AGA are found at the end of MT-CO1/COX1 and MT-ND6/ND6 ope...
Homo sapiens (Human)
O75575
RPC9_HUMAN
MEVKDANSALLSNYEVFQLLTDLKEQRKESGKNKHSSGQQNLNTITYETLKYISKTPCRHQSPEIVREFLTALKSHKLTKAEKLQLLNHRPVTAVEIQLMVEESEERLTEEQIEALLHTVTSILPAEPEAEQKKNTNSNVAMDEEDPA
null
null
defense response to virus [GO:0051607]; innate immune response [GO:0045087]; neuropeptide signaling pathway [GO:0007218]; transcription by RNA polymerase III [GO:0006383]; transcription initiation at RNA polymerase III promoter [GO:0006384]
acrosomal vesicle [GO:0001669]; cytosol [GO:0005829]; DNA polymerase III complex [GO:0009360]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; RNA polymerase III complex [GO:0005666]
calcitonin gene-related peptide receptor activity [GO:0001635]; DNA-directed 5'-3' RNA polymerase activity [GO:0003899]; nucleotide binding [GO:0000166]
PF03874;
1.20.1250.40;
Eukaryotic RPC9 RNA polymerase subunit family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:33335104}. Cell membrane {ECO:0000250|UniProtKB:O35427}; Peripheral membrane protein {ECO:0000250|UniProtKB:O35427}; Cytoplasmic side {ECO:0000250|UniProtKB:O35427}.
null
null
null
null
null
FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates (PubMed:20413673, PubMed:33558764, PubMed:34675218). Specific peripheric component of RNA polymerase III (Pol III) which synthesizes small non-coding RNAs including 5S rRNA, snRNA...
Homo sapiens (Human)
O75578
ITA10_HUMAN
MELPFVTHLFLPLVFLTGLCSPFNLDEHHPRLFPGPPEAEFGYSVLQHVGGGQRWMLVGAPWDGPSGDRRGDVYRCPVGGAHNAPCAKGHLGDYQLGNSSHPAVNMHLGMSLLETDGDGGFMACAPLWSRACGSSVFSSGICARVDASFQPQGSLAPTAQRCPTYMDVVIVLDGSNSIYPWSEVQTFLRRLVGKLFIDPEQIQVGLVQYGESPVHEWSLGDFRTKEEVVRAAKNLSRREGRETKTAQAIMVACTEGFSQSHGGRPEAARLLVVVTDGESHDGEELPAALKACEAGRVTRYGIAVLGHYLRRQRDPSSFLR...
null
null
cell adhesion mediated by integrin [GO:0033627]; cell-cell adhesion [GO:0098609]; cell-matrix adhesion [GO:0007160]; integrin-mediated signaling pathway [GO:0007229]
external side of plasma membrane [GO:0009897]; integrin alpha10-beta1 complex [GO:0034680]; integrin complex [GO:0008305]; plasma membrane [GO:0005886]
collagen binding [GO:0005518]; collagen binding involved in cell-matrix adhesion [GO:0098639]; integrin binding [GO:0005178]; metal ion binding [GO:0046872]
PF01839;PF08441;PF20805;PF00092;
1.20.5.930;2.130.10.130;2.60.40.1460;2.60.40.1510;2.60.40.1530;3.40.50.410;
Integrin alpha chain family
null
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
null
null
null
null
null
FUNCTION: Integrin alpha-10/beta-1 is a receptor for collagen.
Homo sapiens (Human)
O75581
LRP6_HUMAN
MGAVLRSLLACSFCVLLRAAPLLLYANRRDLRLVDATNGKENATIVVGGLEDAAAVDFVFSHGLIYWSDVSEEAIKRTEFNKTESVQNVVVSGLLSPDGLACDWLGEKLYWTDSETNRIEVSNLDGSLRKVLFWQELDQPRAIALDPSSGFMYWTDWGEVPKIERAGMDGSSRFIIINSEIYWPNGLTLDYEEQKLYWADAKLNFIHKSNLDGTNRQAVVKGSLPHPFALTLFEDILYWTDWSTHSILACNKYTGEGLREIHSDIFSPMDIHAFSQQRQPNATNPCGIDNGGCSHLCLMSPVKPFYQCACPTGVKLLENG...
null
null
canonical Wnt signaling pathway [GO:0060070]; cell-cell adhesion [GO:0098609]; cellular response to cholesterol [GO:0071397]; chemical synaptic transmission [GO:0007268]; dopaminergic neuron differentiation [GO:0071542]; midbrain dopaminergic neuron differentiation [GO:1904948]; negative regulation of protein serine/th...
cell surface [GO:0009986]; cytoplasmic vesicle [GO:0031410]; early endosome membrane [GO:0031901]; endoplasmic reticulum [GO:0005783]; extracellular region [GO:0005576]; membrane raft [GO:0045121]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; synapse [GO:0045202]; Wnt signalosome [GO:1990909]; Wnt-Fri...
coreceptor activity [GO:0015026]; frizzled binding [GO:0005109]; identical protein binding [GO:0042802]; kinase inhibitor activity [GO:0019210]; low-density lipoprotein particle receptor activity [GO:0005041]; protein homodimerization activity [GO:0042803]; signaling receptor binding [GO:0005102]; toxin transmembrane t...
PF14670;PF00057;PF00058;
2.10.25.10;4.10.400.10;2.120.10.30;
LDLR family
PTM: Dual phosphorylation of cytoplasmic PPPSP motifs sequentially by GSK3 and CK1 is required for AXIN1-binding, and subsequent stabilization and activation of beta-catenin via preventing GSK3-mediated phosphorylation of beta-catenin. Phosphorylated, in vitro, by GRK5/6 within and outside the PPPSP motifs. Phosphoryla...
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26387593}; Single-pass type I membrane protein. Endoplasmic reticulum {ECO:0000269|PubMed:26387593}. Membrane raft {ECO:0000269|PubMed:23987510}. Note=On Wnt signaling, undergoes a cycle of caveolin- or clathrin-mediated endocytosis and plasma membrane location. R...
null
null
null
null
null
FUNCTION: Component of the Wnt-Fzd-LRP5-LRP6 complex that triggers beta-catenin signaling through inducing aggregation of receptor-ligand complexes into ribosome-sized signalosomes. Cell-surface coreceptor of Wnt/beta-catenin signaling, which plays a pivotal role in bone formation. The Wnt-induced Fzd/LRP6 coreceptor c...
Homo sapiens (Human)
O75582
KS6A5_HUMAN
MEEEGGSSGGAAGTSADGGDGGEQLLTVKHELRTANLTGHAEKVGIENFELLKVLGTGAYGKVFLVRKISGHDTGKLYAMKVLKKATIVQKAKTTEHTRTERQVLEHIRQSPFLVTLHYAFQTETKLHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADETERAYSFCGTIEYMAPDIVRGGDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQEMSALAKDLIQRLLMKDPKKRLGCGPRDADEIKEHLFFQK...
2.7.11.1
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:12628924, ECO:0000269|PubMed:9687510, ECO:0000269|PubMed:9873047};
axon guidance [GO:0007411]; inflammatory response [GO:0006954]; interleukin-1-mediated signaling pathway [GO:0070498]; intracellular signal transduction [GO:0035556]; negative regulation of cytokine production [GO:0001818]; negative regulation of DNA-templated transcription [GO:0045892]; positive regulation of CREB tra...
cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
ATP binding [GO:0005524]; histone H2AS1 kinase activity [GO:0044024]; histone H3S10 kinase activity [GO:0035175]; histone H3S28 kinase activity [GO:0044022]; magnesium ion binding [GO:0000287]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein tyrosine kinase ac...
PF00069;PF00433;
1.10.510.10;
Protein kinase superfamily, AGC Ser/Thr protein kinase family, S6 kinase subfamily
PTM: Ser-376 and Thr-581 phosphorylation is required for kinase activity. Ser-376 and Ser-212 are autophosphorylated by the C-terminal kinase domain, and their phosphorylation is essential for the catalytic activity of the N-terminal kinase domain. Phosphorylated at Ser-360, Thr-581 and Thr-700 by MAPK1/ERK2, MAPK3/ERK...
SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Predominantly nuclear. Exported into cytoplasm in response to glucocorticoid.
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:12628924, ECO:000026...
null
null
null
null
FUNCTION: Serine/threonine-protein kinase that is required for the mitogen or stress-induced phosphorylation of the transcription factors CREB1 and ATF1 and for the regulation of the transcription factors RELA, STAT3 and ETV1/ER81, and that contributes to gene activation by histone phosphorylation and functions in the ...
Homo sapiens (Human)
O75586
MED6_HUMAN
MAAVDIRDNLLGISWVDSSWIPILNSGSVLDYFSERSNPFYDRTCNNEVVKMQRLTLEHLNQMVGIEYILLHAQEPILFIIRKQQRQSPAQVIPLADYYIIAGVIYQAPDLGSVINSRVLTAVHGIQSAFDEAMSYCRYHPSKGYWWHFKDHEEQDKVRPKAKRKEEPSSIFQRQRVDALLLDLRQKFPPKFVQLKPGEKPVPVDQTKKEAEPIPETVKPEEKETTKNVQQTVSAKGPPEKRMRLQ
null
null
positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; positive regulation of transcription initiation by RNA polymerase II [GO:0060261]; protein ubiquitination [GO:0016567]; regulation of transcription by RNA polymerase...
core mediator complex [GO:0070847]; mediator complex [GO:0016592]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ubiquitin ligase complex [GO:0000151]
DNA binding [GO:0003677]; transcription coactivator activity [GO:0003713]; transcription coactivator binding [GO:0001223]; ubiquitin protein ligase activity [GO:0061630]
PF04934;
3.10.450.580;
Mediator complex subunit 6 family
null
SUBCELLULAR LOCATION: Nucleus.
null
null
null
null
null
FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to...
Homo sapiens (Human)
O75592
MYCB2_HUMAN
MMMCAATASPAAASSGLGGDGFYPAATFSSSPAPGALFMPVPDGSVAAAGLGLGLPAADSRGHYQLLLSGRALADRYRRIYTAALNDRDQGGGSAGHPASRNKKILNKKKLKRKQKSKSKVKTRSKSENLENTVIIPDIKLHSNPSAFNIYCNVRHCVLEWQKKEISLAAASKNSVQSGESDSDEEEESKEPPIKLPKIIEVGLCEVFELIKETRFSHPSLCLRSLQALLNVLQGQQPEGLQSEPPEVLESLFQLLLEITVRSTGMNDSTGQSLTALSCACLFSLVASWGETGRTLQAISAILTNNGSHACQTIQVPTIL...
2.3.2.33
null
axon guidance [GO:0007411]; branchiomotor neuron axon guidance [GO:0021785]; central nervous system projection neuron axonogenesis [GO:0021952]; circadian regulation of gene expression [GO:0032922]; negative regulation of protein catabolic process [GO:0042177]; neuromuscular process [GO:0050905]; positive regulation of...
axon [GO:0030424]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; microtubule cytoskeleton [GO:0015630]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
guanyl-nucleotide exchange factor activity [GO:0005085]; identical protein binding [GO:0042802]; small GTPase binding [GO:0031267]; ubiquitin protein ligase activity [GO:0061630]; zinc ion binding [GO:0008270]
PF03256;PF08005;PF00415;PF13540;
2.60.120.260;2.60.40.10;2.60.120.820;2.130.10.30;3.30.40.10;
RING-Cys relay (RCR) family
PTM: Autoubiquitinated. {ECO:0000269|PubMed:18308511}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26304119, ECO:0000269|PubMed:9689053}. Cell projection, axon {ECO:0000250|UniProtKB:Q7TPH6}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q7TPH6}. Note=Localizes to axon shafts and associates with microtubule cytoskeleton (By similarity). Translocates to the nucleus f...
CATALYTIC ACTIVITY: Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-threonine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-3-O-ubiquitinyl-L-threonine.; EC=2.3.2.33; Evidence={ECO:0000269|PubMed:29643511};
null
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:18308511, ECO:0000269|PubMed:29643511}.
null
null
FUNCTION: Atypical E3 ubiquitin-protein ligase which specifically mediates ubiquitination of threonine and serine residues on target proteins, instead of ubiquitinating lysine residues (PubMed:29643511). Shows esterification activity towards both threonine and serine, with a preference for threonine, and acts via two e...
Homo sapiens (Human)
O75593
FOXH1_HUMAN
MGPCSGSRLGPPEAESPSQPPKRRKKRYLRHDKPPYTYLAMIALVIQAAPSRRLKLAQIIRQVQAVFPFFREDYEGWKDSIRHNLSSNRCFRKVPKDPAKPQAKGNFWAVDVSLIPAEALRLQNTALCRRWQNGGARGAFAKDLGPYVLHGRPYRPPSPPPPPSEGFSIKSLLGGSGEGAPWPGLAPQSSPVPAGTGNSGEEAVPTPPLPSSERPLWPLCPLPGPTRVEGETVQGGAIGPSTLSPEPRAWPLHLLQGTAVPGGRSSGGHRASLWGQLPTSYLPIYTPNVVMPLAPPPTSCPQCPSTSPAYWGVAPETRGP...
null
null
aorta morphogenesis [GO:0035909]; axial mesoderm development [GO:0048318]; cardiac right ventricle morphogenesis [GO:0003215]; cellular response to cytokine stimulus [GO:0071345]; determination of left/right asymmetry in lateral mesoderm [GO:0003140]; embryonic heart tube anterior/posterior pattern specification [GO:00...
activin responsive factor complex [GO:0032444]; chromatin [GO:0000785]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667]
bHLH transcription factor binding [GO:0043425]; cis-regulatory region sequence-specific DNA binding [GO:0000987]; co-SMAD binding [GO:0070410]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-b...
PF00250;
1.10.10.10;
null
null
SUBCELLULAR LOCATION: Nucleus.
null
null
null
null
null
FUNCTION: Transcriptional activator. Recognizes and binds to the DNA sequence 5'-TGT[GT][GT]ATT-3'. Required for induction of the goosecoid (GSC) promoter by TGF-beta or activin signaling. Forms a transcriptionally active complex containing FOXH1/SMAD2/SMAD4 on a site on the GSC promoter called TARE (TGF-beta/activin r...
Homo sapiens (Human)
O75594
PGRP1_HUMAN
MSRRSMLLAWALPSLLRLGAAQETEDPACCSPIVPRNEWKALASECAQHLSLPLRYVVVSHTAGSSCNTPASCQQQARNVQHYHMKTLGWCDVGYNFLIGEDGLVYEGRGWNFTGAHSGHLWNPMSIGISFMGNYMDRVPTPQAIRAAQGLLACGVAQGALRSNYVLKGHRDVQRTLSPGNQLYHLIQNWPHYRSP
null
null
antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; biological process involved in interaction with host [GO:0051701]; defense response to Gram-positive bacterium [GO:0050830]; detection of bacterium [GO:0016045]; innate immune response [GO:0045087]; killing of cells of another organis...
extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; phagocytic vesicle lumen [GO:0097013]; specific granule lumen [GO:0035580]; tertiary granule lumen [GO:1904724]
Hsp70 protein binding [GO:0030544]; molecular adaptor activity [GO:0060090]; N-acetylmuramoyl-L-alanine amidase activity [GO:0008745]; peptidoglycan binding [GO:0042834]; peptidoglycan immune receptor activity [GO:0016019]; receptor ligand activity [GO:0048018]; zinc ion binding [GO:0008270]
PF01510;
3.40.80.10;
N-acetylmuramoyl-L-alanine amidase 2 family
PTM: N-glycosylated. N-glycosylation is required for bactericidal activity. {ECO:0000269|PubMed:16354652}.
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16354652}. Cytoplasmic granule {ECO:0000250}.
null
null
null
null
null
FUNCTION: Innate immunity protein that plays several important functions in antimicrobial and antitumor defense systems. Acts as a pattern receptor that binds to murein peptidoglycans (PGN) of Gram-positive bacteria and thus provides bactericidal activity (PubMed:9707603). Forms an equimolar complex with heat shock pro...
Homo sapiens (Human)
O75600
KBL_HUMAN
MWPGNAWRAALFWVPRGRRAQSALAQLRGILEGELEGIRGAGTWKSERVITSRQGPHIRVDGVSGGILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQREDAILYPSCYDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQEAQKHRLRLVATDGAFSMDGDIAPLQEICCLASRYGALVFMDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALGGASGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGCASKALDLLMGSNTIV...
2.3.1.29
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250|UniProtKB:Q0P5L8};
amino acid metabolic process [GO:0006520]; biosynthetic process [GO:0009058]; threonine catabolic process [GO:0006567]
mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
glycine C-acetyltransferase activity [GO:0008890]; pyridoxal phosphate binding [GO:0030170]
PF00155;
3.90.1150.10;3.40.640.10;
Class-II pyridoxal-phosphate-dependent aminotransferase family
null
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q0P5L8}. Nucleus {ECO:0000269|PubMed:17688197}. Note=Translocates to the nucleus upon cold and osmotic stress. {ECO:0000269|PubMed:17688197}.
CATALYTIC ACTIVITY: Reaction=acetyl-CoA + glycine = (2S)-2-amino-3-oxobutanoate + CoA; Xref=Rhea:RHEA:20736, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57305, ChEBI:CHEBI:78948; EC=2.3.1.29; Evidence={ECO:0000250|UniProtKB:Q0P5L8}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:20738; Evidence={ECO:0000250...
null
null
null
null
FUNCTION: Pyridoxal phosphate (PLP) dependent enzyme, which catalyzes the cleavage of 2-amino-3-oxobutanoate to glycine and acetyl-CoA. {ECO:0000250|UniProtKB:Q0P5L8}.
Homo sapiens (Human)
O75601
CASPD_BOVIN
MAEDKHNKNPLKMLESLGKELISGLLDDFVEKNVLKLEEEEKKKIYDAKLQDKARVLVDSIRQKNQEAGQVFVQTFLNIDKNSTSIKAPEETVAGPDESVGSAATLKLCPHEEFLKLCKERAGEIYPIKERKDRTRLALIICNTEFDHMPPRNGAALDILGMKQLLEGLGYTVEVEEKLTARDMESVLWKFAAREEHKSSDSTFLVFMSHGILDGICGTMHSEEEPDVLPYDTIFRTFNNRNCLSLKDKPKVIIVQACRGANRGELWVSDSPPALADSFSQSSENLEEDAVYKTHVEKDFIAFCSSTPHNVSWRDIKKGS...
3.4.22.-
null
apoptotic process [GO:0006915]; positive regulation of inflammatory response [GO:0050729]; positive regulation of neuron apoptotic process [GO:0043525]; proteolysis [GO:0006508]
AIM2 inflammasome complex [GO:0097169]; cytoplasm [GO:0005737]; IPAF inflammasome complex [GO:0072557]; NLRP1 inflammasome complex [GO:0072558]; NLRP3 inflammasome complex [GO:0072559]
caspase binding [GO:0089720]; cysteine-type endopeptidase activity [GO:0004197]
PF00619;PF00656;
3.40.50.1460;1.10.533.10;
Peptidase C14A family
PTM: The two subunits are derived from the precursor sequence by an autocatalytic mechanism or by cleavage by Caspase-8.
null
null
null
null
null
null
FUNCTION: Involved in the activation cascade of caspases responsible for apoptosis execution. Might function by either activating some proteins required for cell death or inactivating proteins necessary for cell survival.
Bos taurus (Bovine)
O75602
SPAG6_HUMAN
MSQRQVLQVFEQYQKARTQFVQMVAELATRPQNIETLQNAGVMSLLRTLLLDVVPTIQQTAALALGRLANYNDDLAEAVVKCDILPQLVYSLAEQNRFYKKAAAFVLRAVGKHSPQLAQAIVDCGALDTLVICLEDFDPGVKEAAAWALRYIARHNAELSQAVVDAGAVPLLVLCIQEPEIALKRIAASALSDIAKHSPELAQTVVDAGAVAHLAQMILNPDAKLKHQILSALSQVSKHSVDLAEMVVEAEIFPVVLTCLKDKDEYVKKNASTLIREIAKHTPELSQLVVNAGGVAAVIDCIGSCKGNTRLPGIMMLGYV...
null
null
epithelial cilium movement involved in extracellular fluid movement [GO:0003351]; filopodium assembly [GO:0046847]; neuron projection extension [GO:1990138]; sperm axoneme assembly [GO:0007288]
acrosomal vesicle [GO:0001669]; axoneme [GO:0005930]; extracellular region [GO:0005576]; microtubule [GO:0005874]; microtubule cytoskeleton [GO:0015630]; nucleus [GO:0005634]; sperm principal piece [GO:0097228]
microtubule binding [GO:0008017]
PF00514;
1.25.10.10;
null
null
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10493827}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:10493827}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q9JLI7}. Note=Associated with microtubules. Detected on the sperm flagellum (PubMed:10493827). Localizes in the ci...
null
null
null
null
null
FUNCTION: Important for structural integrity of the central apparatus in the sperm tail and for flagellar motility. {ECO:0000250, ECO:0000269|PubMed:10493827}.
Homo sapiens (Human)
O75603
GCM2_HUMAN
MPAAAVQEAVGVCSYGMQLSWDINDPQMPQELALFDQFREWPDGYVRFIYSSDEKKAQRHLSGWAMRNTNNHNGHILKKSCLGVVVCTQACTLPDGSRLQLRPAICDKARLKQQKKACPNCHSALELIPCRGHSGYPVTNFWRLDGNAIFFQAKGVHDHPRPESKSETEARRSAIKRQMASFYQPQKKRIRESEAEENQDSSGHFSNIPPLENPEDFDIVTETSFPIPGQPCPSFPKSDVYKATCDLATFQGDKMPPFQKYSSPRIYLPRPPCSYELANPGYTNSSPYPTLYKDSTSIPNDTDWVHLNTLQCNVNSYSSY...
null
null
gliogenesis [GO:0042063]; intracellular calcium ion homeostasis [GO:0006874]; intracellular phosphate ion homeostasis [GO:0030643]; parathyroid gland development [GO:0060017]; regulation of transcription by RNA polymerase II [GO:0006357]; transcription by RNA polymerase II [GO:0006366]
chromatin [GO:0000785]; nucleus [GO:0005634]
DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequenc...
PF03615;
2.20.25.670;3.30.70.3530;
null
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20190276}.
null
null
null
null
null
FUNCTION: Transcription factor that binds specific sequences on gene promoters and activate their transcription. Through the regulation of gene transcription, may play a role in parathyroid gland development. {ECO:0000269|PubMed:20190276, ECO:0000269|PubMed:27745835, ECO:0000269|PubMed:9928992}.
Homo sapiens (Human)
O75604
UBP2_HUMAN
MSQLSSTLKRYTESARYTDAHYAKSGYGAYTPSSYGANLAASLLEKEKLGFKPVPTSSFLTRPRTYGPSSLLDYDRGRPLLRPDITGGGKRAESQTRGTERPLGSGLSGGSGFPYGVTNNCLSYLPINAYDQGVTLTQKLDSQSDLARDFSSLRTSDSYRIDPRNLGRSPMLARTRKELCTLQGLYQTASCPEYLVDYLENYGRKGSASQVPSQAPPSRVPEIISPTYRPIGRYTLWETGKGQAPGPSRSSSPGRDGMNSKSAQGLAGLRNLGNTCFMNSILQCLSNTRELRDYCLQRLYMRDLHHGSNAHTALVEEFAK...
3.4.19.12
null
cell cycle [GO:0007049]; circadian behavior [GO:0048512]; circadian regulation of gene expression [GO:0032922]; entrainment of circadian clock by photoperiod [GO:0043153]; locomotor rhythm [GO:0045475]; muscle organ development [GO:0007517]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positi...
centrosome [GO:0005813]; cytoplasm [GO:0005737]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; perinuclear region of cytoplasm [GO:0048471]
cyclin binding [GO:0030332]; cysteine-type deubiquitinase activity [GO:0004843]; cysteine-type endopeptidase activity [GO:0004197]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; ubiquitin protein ligase binding [GO:0031625]
PF00443;
3.90.70.10;
Peptidase C19 family, USP2 subfamily
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O88623}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O88623}. Note=Localizes in the spermatid head in late-elongating spermatids in the thin area between the outer acrosomal membrane and the plasma membrane. {ECO:0000250|UniProtKB:Q5U349}.; SUBCELLULAR LOC...
CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12;
null
null
null
null
FUNCTION: Hydrolase that deubiquitinates polyubiquitinated target proteins such as MDM2, MDM4 and CCND1 (PubMed:17290220, PubMed:19838211, PubMed:19917254). Isoform 1 and isoform 4 possess both ubiquitin-specific peptidase and isopeptidase activities (By similarity). Deubiquitinates MDM2 without reversing MDM2-mediated...
Homo sapiens (Human)
O75607
NPM3_HUMAN
MAAGTAAALAFLSQESRTRAGGVGGLRVPAPVTMDSFFFGCELSGHTRSFTFKVEEEDDAEHVLALTMLCLTEGAKDECNVVEVVARNHDHQEIAVPVANLKLSCQPMLSLDDFQLQPPVTFRLKSGSGPVRITGRHQIVTMSNDVSEEESEEEEEDSDEEEVELCPILPAKKQGGRP
null
null
chromatin remodeling [GO:0006338]; rRNA processing [GO:0006364]; rRNA transcription [GO:0009303]
actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]
chromatin binding [GO:0003682]; histone binding [GO:0042393]; RNA binding [GO:0003723]
PF03066;
2.60.120.340;
Nucleoplasmin family
PTM: Phosphorylated. {ECO:0000305}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11722795}. Nucleus, nucleolus {ECO:0000269|PubMed:15596447, ECO:0000269|PubMed:22362753}. Note=Mainly found in the granular component of the nucleolus. {ECO:0000269|PubMed:22362753}.
null
null
null
null
null
FUNCTION: Plays a role in the regulation of diverse cellular processes such as ribosome biogenesis, chromatin remodeling or protein chaperoning (PubMed:20073534, PubMed:22362753). Modulates the histone chaperone function and the RNA-binding activity of nucleolar phosphoprotein B23/NPM (PubMed:22362753). Efficiently med...
Homo sapiens (Human)
O75608
LYPA1_HUMAN
MCGNNMSTPLPAIVPAARKATAAVIFLHGLGDTGHGWAEAFAGIRSSHIKYICPHAPVRPVTLNMNVAMPSWFDIIGLSPDSQEDESGIKQAAENIKALIDQEVKNGIPSNRIILGGFSQGGALSLYTALTTQQKLAGVTALSCWLPLRASFPQGPIGGANRDISILQCHGDCDPLVPLMFGSLTVEKLKTLVNPANVTFKTYEGMMHSSCQQEMMDVKQFIDKLLPPID
3.1.2.-; 3.1.2.22
null
fatty acid metabolic process [GO:0006631]; fatty acid transport [GO:0015908]; negative regulation of aggrephagy [GO:1905336]; negative regulation of Golgi to plasma membrane protein transport [GO:0042997]; protein depalmitoylation [GO:0002084]
cell surface [GO:0009986]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; nuclear membrane [GO:0031965]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]
carboxylic ester hydrolase activity [GO:0052689]; lipase activity [GO:0016298]; lysophospholipase activity [GO:0004622]; palmitoyl-(protein) hydrolase activity [GO:0008474]; phospholipase activity [GO:0004620]
PF02230;
3.40.50.1820;
AB hydrolase superfamily, AB hydrolase 2 family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19439193}. Cell membrane {ECO:0000269|PubMed:19439193}. Nucleus membrane {ECO:0000269|PubMed:19439193}. Endoplasmic reticulum {ECO:0000269|PubMed:19439193}. Note=Shows predominantly a cytoplasmic localization with a weak expression in the cell membrane, nuclear membra...
CATALYTIC ACTIVITY: Reaction=H2O + S-hexadecanoyl-L-cysteinyl-[protein] = H(+) + hexadecanoate + L-cysteinyl-[protein]; Xref=Rhea:RHEA:19233, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:74151; EC=3.1.2.22; Evidence={ECO:0000269|PubMe...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=27.3 uM for lysophosphatidylcholine for lysophospholipase activity {ECO:0000269|PubMed:19439193}; KM=3.49 uM for thioesterase activity {ECO:0000269|PubMed:19439193}; Vmax=1.62 umol/min/mg enzyme toward lysophosphatidylcholine for lysophospholipase activity {ECO:000...
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.4 for the thioesterase activity. {ECO:0000269|PubMed:19439193};
null
FUNCTION: Acts as an acyl-protein thioesterase (PubMed:19439193, PubMed:20418879). Hydrolyzes fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS (PubMed:20418879). Acts as a palmitoyl thioesterase that catalyzes depalmitoylation of proteins, such as ADRB2, KCNMA1 and SQS...
Homo sapiens (Human)
O75610
LFTY1_HUMAN
MQPLWLCWALWVLPLASPGAALTGEQLLGSLLRQLQLKEVPTLDRADMEELVIPTHVRAQYVALLQRSHGDRSRGKRFSQSFREVAGRFLALEASTHLLVFGMEQRLPPNSELVQAVLRLFQEPVPKAALHRHGRLSPRSARARVTVEWLRVRDDGSNRTSLIDSRLVSVHESGWKAFDVTEAVNFWQQLSRPRQPLLLQVSVQREHLGPLASGAHKLVRFASQGAPAGLGEPQLELHTLDLGDYGAQGDCDPEAPMTEGTRCCRQEMYIDLQGMKWAENWVLEPPGFLAYECVGTCRQPPEALAFKWPFLGPRQCIASE...
null
null
anterior/posterior axis specification [GO:0009948]; determination of left/right symmetry [GO:0007368]; heart morphogenesis [GO:0003007]; negative regulation of transcription by RNA polymerase II [GO:0000122]; transforming growth factor beta receptor signaling pathway [GO:0007179]
extracellular space [GO:0005615]
cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; transforming growth factor beta receptor binding [GO:0005160]
PF00019;PF00688;
2.60.120.970;2.10.90.10;
TGF-beta family
PTM: The processing of the protein may also occur at the second R-X-X-R site located at AA 132-135. Processing appears to be regulated in a cell-type specific manner.
SUBCELLULAR LOCATION: Secreted.
null
null
null
null
null
FUNCTION: Required for left-right axis determination as a regulator of LEFTY2 and NODAL.
Homo sapiens (Human)
O75616
ERAL1_HUMAN
MAAPSWRGARLVQSVLRVWQVGPHVARERVIPFSSLLGFQRRCVSCVAGSAFSGPRLASASRSNGQGSALDHFLGFSQPDSSVTPCVPAVSMNRDEQDVLLVHHPDMPENSRVLRVVLLGAPNAGKSTLSNQLLGRKVFPVSRKVHTTRCQALGVITEKETQVILLDTPGIISPGKQKRHHLELSLLEDPWKSMESADLVVVLVDVSDKWTRNQLSPQLLRCLTKYSQIPSVLVMNKVDCLKQKSVLLELTAALTEGVVNGKKLKMRQAFHSHPGTHCPSPAVKDPNTQSVGNPQRIGWPHFKEIFMLSALSQEDVKTLK...
null
null
ribosomal small subunit assembly [GO:0000028]
cytosol [GO:0005829]; mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]
GTP binding [GO:0005525]; ribosomal small subunit binding [GO:0043024]; RNA binding [GO:0003723]; rRNA binding [GO:0019843]
PF01926;
3.30.300.20;3.40.50.300;
TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily, Era GTPase family
null
SUBCELLULAR LOCATION: Mitochondrion matrix. Mitochondrion inner membrane; Peripheral membrane protein. Note=Localizes on the matrix side on the mitochondrial inner membrane.
null
null
null
null
null
FUNCTION: Probable GTPase that plays a role in the mitochondrial ribosomal small subunit assembly. Specifically binds the 12S mitochondrial rRNA (12S mt-rRNA) to a 33 nucleotide section delineating the 3' terminal stem-loop region. May act as a chaperone that protects the 12S mt-rRNA on the 28S mitoribosomal subunit du...
Homo sapiens (Human)
O75618
DEDD_HUMAN
MAGLKRRASQVWPEEHGEQEHGLYSLHRMFDIVGTHLTHRDVRVLSFLFVDVIDDHERGLIRNGRDFLLALERQGRCDESNFRQVLQLLRIITRHDLLPYVTLKRRRAVCPDLVDKYLEETSIRYVTPRALSDPEPRPPQPSKTVPPHYPVVCCPTSGPQMCSKRPARGRATLGSQRKRRKSVTPDPKEKQTCDIRLRVRAEYCQHETALQGNVFSNKQDPLERQFERFNQANTILKSRDLGSIICDIKFSELTYLDAFWRDYINGSLLEALKGVFITDSLKQAVGHEAIKLLVNVDEEDYELGRQKLLRNLMLQALP
null
null
decidualization [GO:0046697]; extrinsic apoptotic signaling pathway via death domain receptors [GO:0008625]; negative regulation of protein catabolic process [GO:0042177]; negative regulation of transcription of nucleolar large rRNA by RNA polymerase I [GO:1901837]; regulation of apoptotic process [GO:0042981]; spermat...
cytoplasm [GO:0005737]; nucleolus [GO:0005730]
DNA binding [GO:0003677]
PF01335;PF20694;
1.10.533.10;
null
PTM: Exists predominantly in a mono- or diubiquitinated form.
SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleolus {ECO:0000250}. Note=Translocated to the nucleus during CD95-mediated apoptosis where it is localized in the nucleoli (By similarity). Following apoptosis induction, the mono and/or diubiquitination form increases and forms filamentous structures that colocalize with K...
null
null
null
null
null
FUNCTION: A scaffold protein that directs CASP3 to certain substrates and facilitates their ordered degradation during apoptosis. May also play a role in mediating CASP3 cleavage of KRT18. Regulates degradation of intermediate filaments during apoptosis. May play a role in the general transcription machinery in the nuc...
Homo sapiens (Human)
O75626
PRDM1_HUMAN
MLDICLEKRVGTTLAAPKCNSSTVRFQGLAEGTKGTMKMDMEDADMTLWTEAEFEEKCTYIVNDHPWDSGADGGTSVQAEASLPRNLLFKYATNSEEVIGVMSKEYIPKGTRFGPLIGEIYTNDTVPKNANRKYFWRIYSRGELHHFIDGFNEEKSNWMRYVNPAHSPREQNLAACQNGMNIYFYTIKPIPANQELLVWYCRDFAERLHYPYPGELTMMNLTQTQSSLKQPSTEKNELCPKNVPKREYSVKEILKLDSNPSKGKDLYRSNISPLTSEKDLDDFRRRGSPEMPFYPRVVYPIRAPLPEDFLKASLAYGIER...
2.1.1.-
null
adaptive immune response [GO:0002250]; aorta development [GO:0035904]; artery morphogenesis [GO:0048844]; cell fate commitment [GO:0045165]; coronary vasculature development [GO:0060976]; eye photoreceptor cell development [GO:0042462]; gene expression [GO:0010467]; germ cell development [GO:0007281]; heart valve devel...
cytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; histone methyltransferase binding [GO:1990226]; metal ion binding [GO:0046872]; methyltransferase activity [GO:0008168]; promoter-specific chromatin binding [GO:1990841]; RNA po...
PF21549;PF00096;
3.30.160.60;2.170.270.10;
Class V-like SAM-binding methyltransferase superfamily
PTM: Sumoylation at Lys-816 by PIAS1 augments transcriptional repressor activity, and is critical for plasma cell differentiation (PubMed:22555612). Can be sumoylated with SUMO1 and SUMO2 by PML. Degradation of the wild-type protein mostly depends upon sumoylation, rather than ubiquitination (PubMed:28842558). Desumoyl...
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28842558}. Cytoplasm {ECO:0000269|PubMed:21421998}.
null
null
null
null
null
FUNCTION: Transcription factor that mediates a transcriptional program in various innate and adaptive immune tissue-resident lymphocyte T cell types such as tissue-resident memory T (Trm), natural killer (trNK) and natural killer T (NKT) cells and negatively regulates gene expression of proteins that promote the egress...
Homo sapiens (Human)
O75628
REM1_HUMAN
MTLNTEQEAKTPLHRRASTPLPLSPRGHQPGRLSTVPSTQSQHPRLGQSASLNPPTQKPSPAPDDWSSESSDSEGSWEALYRVVLLGDPGVGKTSLASLFAGKQERDLHEQLGEDVYERTLTVDGEDTTLVVVDTWEAEKLDKSWSQESCLQGGSAYVIVYSIADRGSFESASELRIQLRRTHQADHVPIILVGNKADLARCREVSVEEGRACAVVFDCKFIETSATLQHNVAELFEGVVRQLRLRRRDSAAKEPPAPRRPASLAQRARRFLARLTARSARRRALKARSKSCHNLAVL
null
null
negative regulation of calcium ion transmembrane transport via high voltage-gated calcium channel [GO:1904878]; regulation of skeletal muscle contraction by calcium ion signaling [GO:0014722]
I band [GO:0031674]; plasma membrane [GO:0005886]; T-tubule [GO:0030315]
calcium channel regulator activity [GO:0005246]; calmodulin binding [GO:0005516]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; transmembrane transporter binding [GO:0044325]
PF00071;
3.40.50.300;
Small GTPase superfamily, RGK family
null
null
null
null
null
null
null
FUNCTION: Promotes endothelial cell sprouting and actin cytoskeletal reorganization. May be involved in angiogenesis. May function in Ca(2+) signaling.
Homo sapiens (Human)
O75629
CREG1_HUMAN
MAGLSRGSARALLAALLASTLLALLVSPARGRGGRDHGDWDEASRLPPLPPREDAARVARFVTHVSDWGALATISTLEAVRGRPFADVLSLSDGPPGAGSGVPYFYLSPLQLSVSNLQENPYATLTMTLAQTNFCKKHGFDPQSPLCVHIMLSGTVTKVNETEMDIAKHSLFIRHPEMKTWPSSHNWFFAKLNITNIWVLDYFGGPKIVTPEEYYNVTVQ
null
null
autophagy [GO:0006914]; endocytosis [GO:0006897]; lysosomal lumen acidification [GO:0007042]; regulation of transcription by RNA polymerase II [GO:0006357]
azurophil granule lumen [GO:0035578]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; transcription regulator complex [GO:0005667]
transcription corepressor activity [GO:0003714]
PF13883;
null
CREG family
PTM: N-glycosylated. {ECO:0000269|PubMed:10815803, ECO:0000269|PubMed:19159218}.
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10815803}.
null
null
null
null
null
FUNCTION: May contribute to the transcriptional control of cell growth and differentiation. Antagonizes transcriptional activation and cellular transformation by the adenovirus E1A protein. The transcriptional control activity of cell growth requires interaction with IGF2R. {ECO:0000269|PubMed:12934103, ECO:0000269|Pub...
Homo sapiens (Human)
O75631
UPK3A_HUMAN
MPPLWALLALGCLRFGSAVNLQPQLASVTFATNNPTLTTVALEKPLCMFDSKEALTGTHEVYLYVLVDSAISRNASVQDSTNTPLGSTFLQTEGGRTGPYKAVAFDLIPCSDLPSLDAIGDVSKASQILNAYLVRVGANGTCLWDPNFQGLCNAPLSAATEYRFKYVLVNMSTGLVEDQTLWSDPIRTNQLTPYSTIDTWPGRRSGGMIVITSILGSLPFFLLVGFAGAIALSLVDMGSSDGETTHDSQITQEAVPKSLGASESSYTSVNRGPPLDRAEVYSSKLQD
null
null
cell morphogenesis [GO:0000902]; epithelial cell differentiation [GO:0030855]; kidney development [GO:0001822]; potassium ion homeostasis [GO:0055075]; sodium ion homeostasis [GO:0055078]; urea transport [GO:0015840]; urinary bladder development [GO:0060157]; water transport [GO:0006833]
apical plasma membrane urothelial plaque [GO:0120001]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; plasma membrane [GO:0005886]
null
null
null
Uroplakin-3 family
null
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Heterodimer formation with UPK1B is a prerequisite to exit out of the endoplasmic reticulum (ER). {ECO:0000250}.
null
null
null
null
null
FUNCTION: Component of the asymmetric unit membrane (AUM); a highly specialized biomembrane elaborated by terminally differentiated urothelial cells. May play an important role in AUM-cytoskeleton interaction in terminally differentiated urothelial cells. It also contributes to the formation of urothelial glycocalyx wh...
Homo sapiens (Human)
O75636
FCN3_HUMAN
MDLLWILPSLWLLLLGGPACLKTQEHPSCPGPRELEASKVVLLPSCPGAPGSPGEKGAPGPQGPPGPPGKMGPKGEPGDPVNLLRCQEGPRNCRELLSQGATLSGWYHLCLPEGRALPVFCDMDTEGGGWLVFQRRQDGSVDFFRSWSSYRAGFGNQESEFWLGNENLHQLTLQGNWELRVELEDFNGNRTFAHYATFRLLGEVDHYQLALGKFSEGTAGDSLSLHSGRPFTTYDADHDSSNSNCAVIVHGAWWYASCYRSNLNGRYAVSEAAAHKYGIDWASGRGVGHPYRRVRMMLR
null
null
cell surface pattern recognition receptor signaling pathway [GO:0002752]; complement activation [GO:0006956]; complement activation, lectin pathway [GO:0001867]; defense response to virus [GO:0051607]; negative regulation of RNA biosynthetic process [GO:1902679]; negative regulation of viral entry into host cell [GO:00...
blood microparticle [GO:0072562]; collagen trimer [GO:0005581]; collagen-containing extracellular matrix [GO:0062023]; external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; serine-type endopeptidase complex [GO:1905370]
antigen binding [GO:0003823]; carbohydrate binding [GO:0030246]; carbohydrate derivative binding [GO:0097367]; metal ion binding [GO:0046872]; signaling receptor binding [GO:0005102]
PF00147;
3.90.215.10;4.10.530.10;
Ficolin lectin family
PTM: The N-terminus is blocked.
SUBCELLULAR LOCATION: Secreted. Note=Found in blood plasma, bronchus, alveolus and bile duct.
null
null
null
null
null
FUNCTION: May function in innate immunity through activation of the lectin complement pathway. Calcium-dependent and GlcNAc-binding lectin. Has affinity with GalNAc, GlcNAc, D-fucose, as mono/oligosaccharide and lipopolysaccharides from S.typhimurium and S.minnesota. {ECO:0000269|PubMed:11907111, ECO:0000269|PubMed:172...
Homo sapiens (Human)
O75638
CTAG2_HUMAN
MQAEGRGTGGSTGDADGPGGPGIPDGPGGNAGGPGEAGATGGRGPRGAGAARASGPRGGAPRGPHGGAASAQDGRCPCGARRPDSRLLELHITMPFSSPMEAELVRRILSRDAAPLPRPGAVLKDFTVSGNLLFMSVRDQDREGAGRMRVVGWGLGSASPEGQKARDLRTPKHKVSEQRPGTPGPPPPEGAQGDGCRGVAFNVMFSAPHI
null
null
tRNA threonylcarbamoyladenosine metabolic process [GO:0070525]
centrosome [GO:0005813]
null
PF09341;
3.30.310.50;
CTAG/PCC1 family
null
null
null
null
null
null
null
null
Homo sapiens (Human)
O75643
U520_HUMAN
MADVTARSLQYEYKANSNLVLQADRSLIDRTRRDEPTGEVLSLVGKLEGTRMGDKAQRTKPQMQEERRAKRRKRDEDRHDINKMKGYTLLSEGIDEMVGIIYKPKTKETRETYEVLLSFIQAALGDQPRDILCGAADEVLAVLKNEKLRDKERRKEIDLLLGQTDDTRYHVLVNLGKKITDYGGDKEIQNMDDNIDETYGVNVQFESDEEEGDEDVYGEVREEASDDDMEGDEAVVRCTLSANLVASGELMSSKKKDLHPRDIDAFWLQRQLSRFYDDAIVSQKKADEVLEILKTASDDRECENQLVLLLGFNTFDFIKV...
3.6.4.13
null
cis assembly of pre-catalytic spliceosome [GO:0000354]; mRNA splicing, via spliceosome [GO:0000398]; osteoblast differentiation [GO:0001649]; spliceosome conformational change to release U4 (or U4atac) and U1 (or U11) [GO:0000388]
catalytic step 2 spliceosome [GO:0071013]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spliceosomal complex [GO:0005681]; U2-type catalytic step 1 spliceosome [GO:0071006]; U2-type precatalytic spliceosome [GO:0071005]; U4/U6 x U5 tri-snRNP complex [GO:0046540]; U5 snRNP [GO:0005682]
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; helicase activity [GO:0004386]; identical protein binding [GO:0042802]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]
PF21188;PF00270;PF00271;PF18149;PF02889;
1.10.150.20;2.60.40.150;3.40.50.300;1.10.3380.10;1.10.10.10;
Helicase family, SKI2 subfamily
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:28781166, ECO:0000269|PubMed:29301961, ECO:0000269|PubMed:29360106, ECO:0000269|PubMed:29361316, ECO:0000269|PubMed:30315277, ECO:0000269|PubMed:30705154, ECO:0000269|PubMed:30728453, ECO:0000269|PubMed:9539711}.
CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; Evidence={ECO:0000269|PubMed:23045696, ECO:0000269|PubMed:35241646};
null
null
null
null
FUNCTION: Catalyzes the ATP-dependent unwinding of U4/U6 RNA duplices, an essential step in the assembly of a catalytically active spliceosome (PubMed:35241646). Plays a role in pre-mRNA splicing as a core component of precatalytic, catalytic and postcatalytic spliceosomal complexes (PubMed:28502770, PubMed:28781166, P...
Homo sapiens (Human)
O75648
MTU1_HUMAN
MQALRHVVCALSGGVDSAVAALLLRRRGYQVTGVFMKNWDSLDEHGVCTADKDCEDAYRVCQILDIPFHQVSYVKEYWNDVFSDFLNEYEKGRTPNPDIVCNKHIKFSCFFHYAVDNLGADAIATGHYARTSLEDEEVFEQKHVKKPEGLFRNRFEVRNAVKLLQAADSFKDQTFFLSQVSQDALRRTIFPLGGLTKEFVKKIAAENRLHHVLQKKESMGMCFIGKRNFEHFLLQYLQPRPGHFISIEDNKVLGTHKGWFLYTLGQRANIGGLREPWYVVEKDSVKGDVFVAPRTDHPALYRDLLRTSRVHWIAEEPPAA...
2.8.1.14
null
tRNA wobble position uridine thiolation [GO:0002143]
mitochondrion [GO:0005739]
ATP binding [GO:0005524]; tRNA binding [GO:0000049]; tRNA-5-taurinomethyluridine 2-sulfurtransferase [GO:0061708]
PF03054;PF20258;PF20259;
2.30.30.280;3.40.50.620;2.40.30.10;
MnmA/TRMU family
null
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:15509579, ECO:0000269|PubMed:15944150, ECO:0000269|PubMed:16513084, ECO:0000269|PubMed:16826519}.
CATALYTIC ACTIVITY: Reaction=5-taurinomethyluridine(34) in tRNA + AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] = 5-taurinomethyl-2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]; Xref=Rhea:RHEA:47040, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11726, Rhea:RHEA-COMP:11732, Rhea:RHEA-COMP:11733,...
null
null
null
null
FUNCTION: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln). Required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. ATP is required to activate the C2 atom of t...
Homo sapiens (Human)
O75663
TIPRL_HUMAN
MMIHGFQSSHRDFCFGPWKLTASKTHIMKSADVEKLADELHMPSLPEMMFGDNVLRIQHGSGFGIEFNATDALRCVNNYQGMLKVACAEEWQESRTEGEHSKEVIKPYDWTYTTDYKGTLLGESLKLKVVPTTDHIDTEKLKAREQIKFFEEVLLFEDELHDHGVSSLSVKIRVMPSSFFLLLRFFLRIDGVLIRMNDTRLYHEADKTYMLREYTSRESKISSLMHVPPSLFTEPNEISQYLPIKEAVCEKLIFPERIDPNPADSQKSTQVE
null
null
DNA damage checkpoint signaling [GO:0000077]; negative regulation of phosphoprotein phosphatase activity [GO:0032515]; TOR signaling [GO:0031929]
cytosol [GO:0005829]
null
PF04176;
null
TIP41 family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17944932}.
null
null
null
null
null
FUNCTION: May be a allosteric regulator of serine/threonine-protein phosphatase 2A (PP2A). Isoform 1 inhibits catalytic activity of the PP2A(D) core complex in vitro. The PP2A(C):TIPRL complex does not show phosphatase activity. Acts as a negative regulator of serine/threonine-protein phosphatase 4 probably by inhibiti...
Homo sapiens (Human)
O75665
OFD1_HUMAN
MMAQSNMFTVADVLSQDELRKKLYQTFKDRGILDTLKTQLRNQLIHELMHPVLSGELQPRSISVEGSSLLIGASNSLVADHLQRCGYEYSLSVFFPESGLAKEKVFTMQDLLQLIKINPTSSLYKSLVSGSDKENQKGFLMHFLKELAEYHQAKESCNMETQTSSTFNRDSLAEKLQLIDDQFADAYPQRIKFESLEIKLNEYKREIEEQLRAEMCQKLKFFKDTEIAKIKMEAKKKYEKELTMFQNDFEKACQAKSEALVLREKSTLERIHKHQEIETKEIYAQRQLLLKDMDLLRGREAELKQRVEAFELNQKLQEEK...
null
null
axoneme assembly [GO:0035082]; cilium assembly [GO:0060271]; embryonic body morphogenesis [GO:0010172]; epithelial cilium movement involved in determination of left/right asymmetry [GO:0060287]; negative regulation of fibroblast growth factor receptor signaling pathway involved in neural plate anterior/posterior patter...
centriolar satellite [GO:0034451]; centriole [GO:0005814]; centrosome [GO:0005813]; ciliary basal body [GO:0036064]; cilium [GO:0005929]; cytosol [GO:0005829]; extracellular region [GO:0005576]; membrane [GO:0016020]; microtubule cytoskeleton [GO:0015630]; motile cilium [GO:0031514]; nucleus [GO:0005634]
alpha-tubulin binding [GO:0043014]; gamma-tubulin binding [GO:0043015]; identical protein binding [GO:0042802]; molecular adaptor activity [GO:0060090]
PF16045;
null
OFD1 family
PTM: Phosphorylated. Phosphorylation at Ser-735, by the cAMP-dependent protein kinase PKA, triggers ubiquitination and proteasomal degradation of OFD1. Also increases its interaction with TBC1D31 and regulates its function in ciliogenesis. {ECO:0000269|PubMed:33934390}.; PTM: Ubiquitinated by PJA2, upon phosphorylation...
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:12595504, ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:20230748, ECO:0000269|PubMed:26643951}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:17761535}. Nucleus {ECO:0000269|PubMed:...
null
null
null
null
null
FUNCTION: Component of the centrioles controlling mother and daughter centrioles length. Recruits to the centriole IFT88 and centriole distal appendage-specific proteins including CEP164 (By similarity). Involved in the biogenesis of the cilium, a centriole-associated function. The cilium is a cell surface projection f...
Homo sapiens (Human)
O75674
TM1L1_HUMAN
MAFGKSHRDPYATSVGHLIEKATFAGVQTEDWGQFMHICDIINTTQDGPKDAVKALKKRISKNYNHKEIQLTLSLIDMCVQNCGPSFQSLIVKKEFVKENLVKLLNPRYNLPLDIQNRILNFIKTWSQGFPGGVDVSEVKEVYLDLVKKGVQFPPSEAEAETARQETAQISSNPPTSVPTAPALSSVIAPKNSTVTLVPEQIGKLHSELDMVKMNVRVMSAILMENTPGSENHEDIELLQKLYKTGREMQERIMDLLVVVENEDVTVELIQVNEDLNNAILGYERFTRNQQRILEQNKNQKEATNTTSEPSAPSQDLLDL...
null
null
activation of protein kinase activity [GO:0032147]; negative regulation of mitotic nuclear division [GO:0045839]; positive regulation of protein autophosphorylation [GO:0031954]; protein transport [GO:0015031]; signal transduction [GO:0007165]; ubiquitin-dependent protein catabolic process via the multivesicular body s...
cytoplasm [GO:0005737]; cytosol [GO:0005829]; endosome [GO:0005768]; endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; Golgi stack [GO:0005795]; lysosome [GO:0005764]; membrane [GO:0016020]
clathrin binding [GO:0030276]; phosphatidylinositol binding [GO:0035091]; protein kinase activator activity [GO:0030295]; protein kinase binding [GO:0019901]; SH3 domain binding [GO:0017124]; ubiquitin binding [GO:0043130]
PF03127;PF00790;
1.20.58.160;1.25.40.90;
TOM1 family
PTM: Phosphorylated on tyrosines by FYN and LYN. {ECO:0000250}.
SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack. Endosome membrane {ECO:0000305}. Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=A small proportion is membrane-associated. {ECO:0000250}.
null
null
null
null
null
FUNCTION: Probable adapter protein involved in signaling pathways. Interacts with the SH2 and SH3 domains of various signaling proteins when it is phosphorylated. May promote FYN activation, possibly by disrupting intramolecular SH3-dependent interactions (By similarity). {ECO:0000250}.
Homo sapiens (Human)
O75676
KS6A4_HUMAN
MGDEDDDESCAVELRITEANLTGHEEKVSVENFELLKVLGTGAYGKVFLVRKAGGHDAGKLYAMKVLRKAALVQRAKTQEHTRTERSVLELVRQAPFLVTLHYAFQTDAKLHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTEEKERTFSFCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFTLEGERNTQAEVSRRILKCSPPFPPRIGPVAQDLLQRLLCKDPKKRLGAGPQGAQEVRNHPFFQGLDWVALAARKIPAPFRP...
2.7.11.1
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:9792677};
inflammatory response [GO:0006954]; interleukin-1-mediated signaling pathway [GO:0070498]; intracellular signal transduction [GO:0035556]; negative regulation of cytokine production [GO:0001818]; positive regulation of CREB transcription factor activity [GO:0032793]; positive regulation of NF-kappaB transcription facto...
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; synapse [GO:0045202]
ATP binding [GO:0005524]; histone H3S10 kinase activity [GO:0035175]; histone H3S28 kinase activity [GO:0044022]; magnesium ion binding [GO:0000287]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; ribosomal protein S6 kinase activity [GO:0004711]
PF00069;PF00433;
1.10.510.10;
Protein kinase superfamily, AGC Ser/Thr protein kinase family, S6 kinase subfamily
PTM: Ser-343 and Thr-568 phosphorylation is required for kinase activity. Ser-343 and Ser-196 are autophosphorylated by the C-terminal kinase domain, and their phosphorylation is essential for the catalytic activity of the N-terminal kinase domain. Phosphorylated at Ser-343, Thr-568 and Thr-687 by MAPK1/ERK2, MAPK3/ERK...
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11035004, ECO:0000269|PubMed:9792677}.
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:9792677}; CATALYTIC ...
null
null
null
null
FUNCTION: Serine/threonine-protein kinase that is required for the mitogen or stress-induced phosphorylation of the transcription factors CREB1 and ATF1 and for the regulation of the transcription factor RELA, and that contributes to gene activation by histone phosphorylation and functions in the regulation of inflamma...
Homo sapiens (Human)
O75677
RFPL1_HUMAN
MKRLSLVTTNRLSPHGNFLPLCTFPLAVDMAALFQEASSCPVCSDYLEKPMSLECGCAVCFKCINSLQKEPHGEDLLCCCCSMVSQKNKIRPSWQLERLASHIKELEPKLKKILQMNPRMRKFQVDMTLDADTANNFLLISDDLRSVRSGCITQNRQDLAERFDVSICILGSPRFTCGRHYWEVDVGTSTEWDLGVCRESVHRKGRIHLTTERGFWTVSLRDGSRLSASTVPLTFLFVDRKLQRVGIFLDMGMQNVSFFDAEGGSHVYTFRSVSAEEPLHLFFAPPSPPNGDKSVLSICPVINPGTTDAPVHPGEAK
null
null
cell cycle [GO:0007049]; innate immune response [GO:0045087]; negative regulation of cell division [GO:0051782]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of G2/M transition of mitotic cell cycle [GO:0010972]; negative regulation of mitotic cell cycle [GO:0045930]; positive ...
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]
metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; protein kinase binding [GO:0019901]; ubiquitin protein ligase activity [GO:0061630]
PF13765;PF11002;PF00622;PF15227;
2.60.120.920;3.30.40.10;
null
PTM: Phosphorylated by PKC and CDK1 (PubMed:20725088). The antiproliferative effect seems to be positively regulated by PKC phosphorylation and negatively by CDK1 phosphorylation (PubMed:20725088). {ECO:0000269|PubMed:20725088}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20725088}. Nucleus {ECO:0000269|PubMed:20725088}. Note=A higher concentration is observed in the cytoplasm compared to the nucleus. {ECO:0000269|PubMed:20725088}.
null
null
null
null
null
FUNCTION: Negatively regulates the G2-M phase transition, possibly by promoting cyclin B1/CCNB1 and CDK1 proteasomal degradation and thereby preventing their accumulation during interphase. {ECO:0000269|PubMed:20725088}.
Homo sapiens (Human)
O75678
RFPL2_HUMAN
MEVAELGFPETAVSQSRICLCAVLCGHWDFADMMVIRSLSLIRLEGVEGRDPVGGGNLTNKRPSCAPSPQDLSAQWKQLEDRGASSRRVDMAALFQEASSCPVCSDYLEKPMSLECGCAVCLKCINSLQKEPHGEDLLCCCSSMVSRKNKIRRNRQLERLASHIKELEPKLKKILQMNPRMRKFQVDMTLDANTANNFLLISDDLRSVRSGRIRQNRQDLAERFDVSVCILGSPRFTCGRHCWEVDVGTSTEWDLGVCRESVHRKGRIQLTTELGFWTVSLRDGGRLSATTVPLTFLFVDRKLQRVGIFLDMGMQNVSFF...
null
null
innate immune response [GO:0045087]; positive regulation of autophagy [GO:0010508]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; protein polyubiquitination [GO:0000209]; regulation of gene expression [GO:0010468]; regulation of protein localization [GO:0032880]; regulation of viral entry...
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]
metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; protein kinase binding [GO:0019901]; ubiquitin protein ligase activity [GO:0061630]
PF13765;PF11002;PF00622;PF15227;
2.60.120.920;3.30.40.10;
null
null
null
null
null
null
null
null
null
Homo sapiens (Human)
O75679
RFPL3_HUMAN
MKRLSLVTTNRLSPQGNFLPLCTFPLAVDMAALFQEASSCPVCSDYLEKPMSLECGCTVCLKCINSLQKEPHGEDLLCCCCSMVSQRNKIRPNRQLERLVSHIKELEPKLKKILQMNPRMRKFQVDMTLDADTANNFLLISDDLRSVRSGLITQNRQDLAERFDVSVCILGSPRFTCGRHYWEVDVGTSTEWDLGVCRESVHCKGKIQLTTELGFWTVSLRDGSRLSASTVPLTFLLVDRKLQRVGIFLDMGMQNVSFFDAESGSHVYTFRSVSAEEPLRPFLAPSIPPNGDQGVLSICPLMNSGTTDAPVRPGEAK
null
null
innate immune response [GO:0045087]; positive regulation of autophagy [GO:0010508]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; protein polyubiquitination [GO:0000209]; regulation of gene expression [GO:0010468]; regulation of protein localization [GO:0032880]; regulation of viral entry...
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]
metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; protein kinase binding [GO:0019901]; ubiquitin protein ligase activity [GO:0061630]
PF13765;PF11002;PF00622;PF15227;
2.60.120.920;3.30.40.10;
null
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25107902}. Nucleus {ECO:0000269|PubMed:25107902}. Note=A higher concentration of RFPL3 is observed in the cytoplasm compared to the nucleus. {ECO:0000269|PubMed:25107902}.
null
null
null
null
null
FUNCTION: (Microbial infection) Stimulates the activity of Human Immunodeficiency Virus 1/HIV-1 pre-integration complex. {ECO:0000269|PubMed:25107902}.
Homo sapiens (Human)
O75683
SURF6_HUMAN
MASLLAKDAYLQSLAKKICSHSAPEQQARTRAGKTQGSETAGPPKKKRKKTQKKFRKREEKAAEHKAKSLGEKSPAASGARRPEAAKEEAAWASSSAGNPADGLATEPESVFALDVLRQRLHEKIQEARGQGSAKELSPAALEKRRRRKQERDRKKRKRKELRAKEKARKAEEATEAQEVVEATPEGACTEPREPPGLIFNKVEVSEDEPASKAQRRKEKRQRVKGNLTPLTGRNYRQLLERLQARQSRLDELRGQDEGKAQELEAKMKWTNLLYKAEGVKIRDDERLLQEALKRKEKRRAQRQRRWEKRTAGVVEKMQQ...
null
null
ribosomal large subunit biogenesis [GO:0042273]; ribosomal small subunit biogenesis [GO:0042274]
chromosome [GO:0005694]; granular component [GO:0001652]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]
DNA binding [GO:0003677]; molecular condensate scaffold activity [GO:0140693]; RNA binding [GO:0003723]
PF04935;
null
SURF6 family
null
SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Note=Granular component of the nucleolus. {ECO:0000250}.
null
null
null
null
null
FUNCTION: Binds to both DNA and RNA in vitro, with a stronger binding capacity for RNA. May represent a nucleolar constitutive protein involved in ribosomal biosynthesis or assembly (By similarity). {ECO:0000250}.
Homo sapiens (Human)
O75688
PPM1B_HUMAN
MGAFLDKPKTEKHNAHGAGNGLRYGLSSMQGWRVEMEDAHTAVVGIPHGLEDWSFFAVYDGHAGSRVANYCSTHLLEHITTNEDFRAAGKSGSALELSVENVKNGIRTGFLKIDEYMRNFSDLRNGMDRSGSTAVGVMISPKHIYFINCGDSRAVLYRNGQVCFSTQDHKPCNPREKERIQNAGGSVMIQRVNGSLAVSRALGDYDYKCVDGKGPTEQLVSPEPEVYEILRAEEDEFIILACDGIWDVMSNEELCEYVKSRLEVSDDLENVCNWVVDTCLHKGSRDNMSIVLVCFSNAPKVSDEAVKKDSELDKHLESRV...
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};
N-terminal protein myristoylation [GO:0006499]; negative regulation of canonical NF-kappaB signal transduction [GO:0043124]; negative regulation of defense response to virus [GO:0050687]; negative regulation of interferon-beta production [GO:0032688]; negative regulation of non-canonical NF-kappaB signal transduction [...
cytosol [GO:0005829]; membrane [GO:0016020]; nucleolus [GO:0005730]; nucleus [GO:0005634]
magnesium ion binding [GO:0000287]; manganese ion binding [GO:0030145]; myosin phosphatase activity [GO:0017018]; protein serine/threonine phosphatase activity [GO:0004722]
PF00481;PF07830;
1.10.10.430;3.60.40.10;
PP2C family
PTM: Isgylation negatively regulates its activity. {ECO:0000269|PubMed:16872604}.; PTM: N-myristoylation is essential for the recognition of its substrates for dephosphorylation. {ECO:0000250}.
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:22781750}. Membrane {ECO:0000250|UniProtKB:P36993}; Lipid-anchor {ECO:0000250|UniProtKB:P36993}. Note=Weakly associates at the membrane and N-myristoylation mediates the membrane localization. {ECO:0000250|UniProtKB:P36993}.
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: Enzyme with a broad specificity. Dephosphorylates CDK2 and CDK6 in vitro. Dephosphorylates PRKAA1 and PRKAA2. Inhibits TBK1-mediated antiviral signaling by dephosphorylating it at 'Ser-172'. Plays an important role in the termination of TNF-alpha-mediated NF-kappa-B activation through dephosphorylating and in...
Homo sapiens (Human)
O75689
ADAP1_HUMAN
MAKERRRAVLELLQRPGNARCADCGAPDPDWASYTLGVFICLSCSGIHRNIPQVSKVKSVRLDAWEEAQVEFMASHGNDAARARFESKVPSFYYRPTPSDCQLLREQWIRAKYERQEFIYPEKQEPYSAGYREGFLWKRGRDNGQFLSRKFVLTEREGALKYFNRNDAKEPKAVMKIEHLNATFQPAKIGHPHGLQVTYLKDNSTRNIFIYHEDGKEIVDWFNALRAARFHYLQVAFPGAGDADLVPKLSRNYLKEGYMEKTGPKQTEGFRKRWFTMDDRRLMYFKDPLDAFARGEVFIGSKESGYTVLHGFPPSTQGHH...
null
null
cell surface receptor signaling pathway [GO:0007166]; regulation of GTPase activity [GO:0043087]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
GTPase activator activity [GO:0005096]; inositol 1,3,4,5 tetrakisphosphate binding [GO:0043533]; metal ion binding [GO:0046872]; phosphatidylinositol bisphosphate binding [GO:1902936]; phosphatidylinositol-3,4,5-trisphosphate binding [GO:0005547]
PF01412;PF00169;
1.10.220.150;2.30.29.30;
null
PTM: Phosphorylated by PRKCA, PRKCI, PRKCZ and PRKD1 in vitro. {ECO:0000269|PubMed:12893243}.
SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Recruited to the plasma membrane upon epidermal growth factor-dependent activation of phosphatidylinositol 4,5-diphosphate (PtdInsP2) 3-kinase.
null
null
null
null
null
FUNCTION: GTPase-activating protein for the ADP ribosylation factor family (Probable). Binds phosphatidylinositol 3,4,5-trisphosphate (PtdInsP3) and inositol 1,3,4,5-tetrakisphosphate (InsP4). {ECO:0000269|PubMed:10448098, ECO:0000303|PubMed:10333475, ECO:0000305}.
Homo sapiens (Human)
O75691
UTP20_HUMAN
MKTKPVSHKTENTYRFLTFAERLGNVNIDIIHRIDRTASYEEEVETYFFEGLLKWRELNLTEHFGKFYKEVIDKCQSFNQLVYHQNEIVQSLKTHLQVKNSFAYQPLLDLVVQLARDLQMDFYPHFPEFFLTITSILETQDTELLEWAFTSLSYLYKYLWRLMVKDMSSIYSMYSTLLAHKKLHIRNFAAESFTFLMRKVSDKNALFNLMFLDLDKHPEKVEGVGQLLFEMCKGVRNMFHSCTGQAVKLILRKLGPVTETETQLPWMLIGETLKNMVKSTVSYISKEHFGTFFECLQESLLDLHTKVTKTNCCESSEQIK...
null
null
endonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000480]; endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000447]; endonucleolytic cleavage to generate mature 5...
90S preribosome [GO:0030686]; cytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; preribosome, small subunit precursor [GO:0030688]; small-subunit processome [GO:0032040]
RNA binding [GO:0003723]
PF20416;PF07539;
null
UTP20 family
null
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11790298, ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:16458307, ECO:0000269|PubMed:34516797}. Note=Colocalizes with NCL in the nucleolus.
null
null
null
null
null
FUNCTION: Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA f...
Homo sapiens (Human)
O75694
NU155_HUMAN
MPSSLLGAAMPASTSAAALQEALENAGRLIDRQLQEDRMYPDLSELLMVSAPNNPTVSGMSDMDYPLQGPGLLSVPNLPEISSIRRVPLPPELVEQFGHMQCNCMMGVFPPISRAWLTIDSDIFMWNYEDGGDLAYFDGLSETILAVGLVKPKAGIFQPHVRHLLVLATPVDIVILGLSYANLQTGSGVLNDSLSGGMQLLPDPLYSLPTDNTYLLTITSTDNGRIFLAGKDGCLYEVAYQAEAGWFSQRCRKINHSKSSLSFLVPSLLQFTFSEDDPILQIAIDNSRNILYTRSEKGVIQVYDLGQDGQGMSRVASVSQ...
null
null
atrial cardiac muscle cell action potential [GO:0086014]; miRNA processing [GO:0035196]; mRNA export from nucleus [GO:0006406]; nuclear envelope organization [GO:0006998]; nucleocytoplasmic transport [GO:0006913]; protein import into nucleus [GO:0006606]; protein localization to nuclear inner membrane [GO:0036228]; RNA...
cytosol [GO:0005829]; membrane [GO:0016020]; nuclear envelope [GO:0005635]; nuclear membrane [GO:0031965]; nuclear pore [GO:0005643]; nuclear pore inner ring [GO:0044611]
structural constituent of nuclear pore [GO:0017056]
PF08801;
1.20.58.1780;1.20.120.1880;1.25.40.440;1.25.40.450;
Non-repetitive/WGA-negative nucleoporin family
PTM: Phosphorylated. Phosphorylation and dephosphorylation may be important for the function of NUP155 and may play a role in the reversible disassembly of the nuclear pore complex during mitosis (By similarity). {ECO:0000250}.; PTM: Disulfide-linked to NUP62. The inner channel of the NPC has a different redox environm...
SUBCELLULAR LOCATION: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P37199}. Nucleus membrane {ECO:0000250|UniProtKB:P37199}; Peripheral membrane protein {ECO:0000250|UniProtKB:P37199}; Cytoplasmic side {ECO:0000250|UniProtKB:P37199}. Nucleus membrane {ECO:0000250|UniProtKB:P37199}; Peripheral membrane protein {...
null
null
null
null
null
FUNCTION: Essential component of nuclear pore complex. Could be essessential for embryogenesis. Nucleoporins may be involved both in binding and translocating proteins during nucleocytoplasmic transport. {ECO:0000250|UniProtKB:Q99P88}.
Homo sapiens (Human)
O75695
XRP2_HUMAN
MGCFFSKRRKADKESRPENEEERPKQYSWDQREKVDPKDYMFSGLKDETVGRLPGTVAGQQFLIQDCENCNIYIFDHSATVTIDDCTNCIIFLGPVKGSVFFRNCRDCKCTLACQQFRVRDCRKLEVFLCCATQPIIESSSNIKFGCFQWYYPELAFQFKDAGLSIFNNTWSNIHDFTPVSGELNWSLLPEDAVVQDYVPIPTTEELKAVRVSTEANRSIVPISRGQRQKSSDESCLVVLFAGDYTIANARKLIDEMVGKGFFLVQTKEVSMKAEDAQRVFREKAPDFLPLLNKGPVIALEFNGDGAVEVCQLIVNEIFN...
null
null
cilium assembly [GO:0060271]; post-Golgi vesicle-mediated transport [GO:0006892]; protein folding [GO:0006457]; protein transport [GO:0015031]; visual perception [GO:0007601]
centriole [GO:0005814]; ciliary basal body [GO:0036064]; cilium [GO:0005929]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; nuclear body [GO:0016604]; nucleoplasm [GO:0005654]; periciliary membrane compartment [GO:1990075]; plasma membrane [G...
GTP binding [GO:0005525]; GTPase activator activity [GO:0005096]; magnesium ion binding [GO:0000287]; unfolded protein binding [GO:0051082]
PF07986;
2.160.20.70;3.30.70.141;
TBCC family
PTM: Myristoylated on Gly-2; which may be required for membrane targeting. {ECO:0000305|PubMed:10942419}.; PTM: Palmitoylated on Cys-3; which may be required for plasma membrane targeting (Probable). Mutation of Cys-3 targets the protein to internal membranes. {ECO:0000269|PubMed:10942419, ECO:0000305}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10942419, ECO:0000269|PubMed:12417528}; Lipid-anchor {ECO:0000269|PubMed:10942419}; Cytoplasmic side {ECO:0000269|PubMed:10942419}. Cell projection, cilium {ECO:0000269|PubMed:20106869}. Note=Detected predominantly at the plasma membrane of rod and cone photorecep...
null
null
null
null
null
FUNCTION: Acts as a GTPase-activating protein (GAP) involved in trafficking between the Golgi and the ciliary membrane. Involved in localization of proteins, such as NPHP3, to the cilium membrane by inducing hydrolysis of GTP ARL3, leading to the release of UNC119 (or UNC119B). Acts as a GTPase-activating protein (GAP)...
Homo sapiens (Human)
O75712
CXB3_HUMAN
MDWKTLQALLSGVNKYSTAFGRIWLSVVFVFRVLVYVVAAERVWGDEQKDFDCNTKQPGCTNVCYDNYFPISNIRLWALQLIFVTCPSLLVILHVAYREERERRHRQKHGDQCAKLYDNAGKKHGGLWWTYLFSLIFKLIIEFLFLYLLHTLWHGFNMPRLVQCANVAPCPNIVDCYIARPTEKKIFTYFMVGASAVCIVLTICELCYLICHRVLRGLHKDKPRGGCSPSSSASRASTCRCHHKLVEAGEVDPDPGNNKLQASAPNLTPI
null
null
cell-cell signaling [GO:0007267]; cellular response to retinoic acid [GO:0071300]; in utero embryonic development [GO:0001701]; placenta development [GO:0001890]; skin development [GO:0043588]; spermatogenesis [GO:0007283]
cell junction [GO:0030054]; connexin complex [GO:0005922]; cytoplasm [GO:0005737]; gap junction [GO:0005921]; intracellular membrane-bounded organelle [GO:0043231]
gap junction channel activity [GO:0005243]
PF00029;
1.20.1440.80;
Connexin family, Beta-type (group I) subfamily
null
SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cell junction, gap junction.
null
null
null
null
null
FUNCTION: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell.
Homo sapiens (Human)
O75716
STK16_HUMAN
MGHALCVCSRGTVIIDNKRYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQREADMHRLFNHPNILRLVAYCLRERGAKHEAWLLLPFFKRGTLWNEIERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQACIHVEGSRQALTLQDWAAQRCTISYRAPELFSVQSHCVIDERTDVWSLGCVLYAMMFGEGPYDMVFQKGDSVALAVQNQLSIPQSPRHSSALRQLLNSMMTVDPHQRPHIPLLLSQLEALQPPAPGQHTTQI
2.7.10.2; 2.7.11.1
null
cellular response to transforming growth factor beta stimulus [GO:0071560]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein autophosphorylation [GO:0046777]; regulation of vacuole fusion, non-autophagic [GO:0032889]; vacuolar protein processing [GO:0006624]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; Golgi-associated vesicle [GO:0005798]; nucleoplasm [GO:0005654]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]
ATP binding [GO:0005524]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
PF00069;
1.10.510.10;
Protein kinase superfamily, Ser/Thr protein kinase family
PTM: Mainly autophosphorylated on serine/threonine residues. Also autophosphorylated on Tyr-198. {ECO:0000269|PubMed:18184589}.; PTM: It is uncertain whether palmitoylation is on Cys-6 and/or Cys-8. {ECO:0000269|PubMed:10364453}.
SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Note=Associates with Golgi and Golgi-derived vesicles. {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[pr...
null
null
null
null
FUNCTION: Membrane-associated protein kinase that phosphorylates on serine and threonine residues. In vitro substrates include DRG1, ENO1 and EIF4EBP1. Also autophosphorylates. May be involved in secretory vesicle trafficking or intracellular signaling. May have a role in regulating stromal-epithelial interactions that...
Homo sapiens (Human)
O75717
WDHD1_HUMAN
MPATRKPMRYGHTEGHTEVCFDDSGSFIVTCGSDGDVRIWEDLDDDDPKFINVGEKAYSCALKSGKLVTAVSNNTIQVHTFPEGVPDGILTRFTTNANHVVFNGDGTKIAAGSSDFLVKIVDVMDSSQQKTFRGHDAPVLSLSFDPKDIFLASASCDGSVRVWQISDQTCAISWPLLQKCNDVINAKSICRLAWQPKSGKLLAIPVEKSVKLYRRESWSHQFDLSDNFISQTLNIVTWSPCGQYLAAGSINGLIIVWNVETKDCMERVKHEKGYAICGLAWHPTCGRISYTDAEGNLGLLENVCDPSGKTSSSKVSSRVE...
null
null
DNA repair [GO:0006281]; DNA-templated DNA replication [GO:0006261]; mitotic cell cycle [GO:0000278]
cytoplasm [GO:0005737]; nuclear replication fork [GO:0043596]; nucleoplasm [GO:0005654]
chromatin binding [GO:0003682]; DNA binding [GO:0003677]
PF12894;PF20946;PF12341;PF00400;
1.10.30.10;2.130.10.10;
null
null
SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000305|PubMed:34694004, ECO:0000305|PubMed:35585232}.
null
null
null
null
null
FUNCTION: Core replisome component that acts as a replication initiation factor. Binds directly to the CMG complex and functions as a hub to recruit additional proteins to the replication fork. {ECO:0000269|PubMed:19805216, ECO:0000269|PubMed:34694004, ECO:0000269|PubMed:35585232}.
Homo sapiens (Human)
O75718
CRTAP_HUMAN
MEPGRRGAAALLALLCVACALRAGRAQYERYSFRSFPRDELMPLESAYRHALDKYSGEHWAESVGYLEISLRLHRLLRDSEAFCHRNCSAAPQPEPAAGLASYPELRLFGGLLRRAHCLKRCKQGLPAFRQSQPSREVLADFQRREPYKFLQFAYFKANNLPKAIAAAHTFLLKHPDDEMMKRNMAYYKSLPGAEDYIKDLETKSYESLFIRAVRAYNGENWRTSITDMELALPDFFKAFYECLAACEGSREIKDFKDFYLSIADHYVEVLECKIQCEENLTPVIGGYPVEKFVATMYHYLQFAYYKLNDLKNAAPCAVS...
null
null
chaperone-mediated protein folding [GO:0061077]; collagen fibril organization [GO:0030199]; negative regulation of post-translational protein modification [GO:1901874]; protein stabilization [GO:0050821]; spermatogenesis [GO:0007283]
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; extracellular space [GO:0005615]; protein-containing complex [GO:0032991]
collagen binding [GO:0005518]
null
1.25.40.10;
Leprecan family
null
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}.
null
null
null
null
null
FUNCTION: Necessary for efficient 3-hydroxylation of fibrillar collagen prolyl residues. {ECO:0000269|PubMed:17055431}.
Homo sapiens (Human)
O75746
S2512_HUMAN
MAVKVQTTKRGDPHELRNIFLQYASTEVDGERYMTPEDFVQRYLGLYNDPNSNPKIVQLLAGVADQTKDGLISYQEFLAFESVLCAPDSMFIVAFQLFDKSGNGEVTFENVKEIFGQTIIHHHIPFNWDCEFIRLHFGHNRKKHLNYTEFTQFLQELQLEHARQAFALKDKSKSGMISGLDFSDIMVTIRSHMLTPFVEENLVSAAGGSISHQVSFSYFNAFNSLLNNMELVRKIYSTLAGTRKDVEVTKEEFAQSAIRYGQVTPLEIDILYQLADLYNASGRLTLADIERIAPLAEGALPYNLAELQRQQSPGLGRPIW...
null
null
aspartate family amino acid metabolic process [GO:0009066]; aspartate transmembrane transport [GO:0015810]; gluconeogenesis [GO:0006094]; L-glutamate transmembrane transport [GO:0015813]; malate-aspartate shuttle [GO:0043490]; response to calcium ion [GO:0051592]
membrane [GO:0016020]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]
3-sulfino-L-alanine: proton, glutamate antiporter activity [GO:0000514]; acidic amino acid transmembrane transporter activity [GO:0015172]; aspartate:glutamate, proton antiporter activity [GO:0000515]; calcium ion binding [GO:0005509]; identical protein binding [GO:0042802]; L-aspartate transmembrane transporter activi...
PF00153;
1.10.238.10;1.50.40.10;
Mitochondrial carrier (TC 2.A.29) family
null
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:11566871, ECO:0000269|PubMed:19641205, ECO:0000269|PubMed:24515575, ECO:0000269|PubMed:9722566}; Multi-pass membrane protein {ECO:0000269|PubMed:11566871}.
CATALYTIC ACTIVITY: Reaction=H(+)(out) + L-aspartate(in) + L-glutamate(out) = H(+)(in) + L-aspartate(out) + L-glutamate(in); Xref=Rhea:RHEA:70783, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; Evidence={ECO:0000269|PubMed:11566871, ECO:0000269|PubMed:19641205, ECO:0000269|PubMed:24515575}; CATALYTIC ACTIVITY...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=24.7 umol/min/g enzyme toward L-aspartate {ECO:0000269|PubMed:11566871};
null
null
null
FUNCTION: Mitochondrial electrogenic aspartate/glutamate antiporter that favors efflux of aspartate and entry of glutamate and proton within the mitochondria as part of the malate-aspartate shuttle (PubMed:11566871, PubMed:19641205, PubMed:24515575). Also mediates the uptake of L-cysteinesulfinate by mitochondria in ex...
Homo sapiens (Human)
O75747
P3C2G_HUMAN
MAYSWQTDPNPNESHEKQYEHQEFLFVNQPHSSSQVSLGFDQIVDEISGKIPHYESEIDENTFFVPTAPKWDSTGHSLNEAHQISLNEFTSKSRELSWHQVSKAPAIGFSPSVLPKPQNTNKECSWGSPIGKHHGADDSRFSILAPSFTSLDKINLEKELENENHNYHIGFESSIPPTNSSFSSDFMPKEENKRSGHVNIVEPSLMLLKGSLQPGMWESTWQKNIESIGCSIQLVEVPQSSNTSLASFCNKVKKIRERYHAADVNFNSGKIWSTTTAFPYQLFSKTKFNIHIFIDNSTQPLHFMPCANYLVKDLIAEILH...
2.7.1.137; 2.7.1.154
null
cell migration [GO:0016477]; chemotaxis [GO:0006935]; modulation by host of viral process [GO:0044788]; phosphatidylinositol-3-phosphate biosynthetic process [GO:0036092]; phosphatidylinositol-mediated signaling [GO:0048015]; phosphorylation [GO:0016310]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; phosphatidylinositol 3-kinase complex [GO:0005942]; plasma membrane [GO:0005886]
1-phosphatidylinositol-3-kinase activity [GO:0016303]; 1-phosphatidylinositol-4-phosphate 3-kinase activity [GO:0035005]; ATP binding [GO:0005524]; phosphatidylinositol binding [GO:0035091]; phosphatidylinositol kinase activity [GO:0052742]
PF00168;PF00454;PF00792;PF00794;PF00613;PF00787;
2.60.40.150;1.10.1070.11;1.25.40.70;3.30.1520.10;
PI3/PI4-kinase family
null
SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:O70167}; Peripheral membrane protein {ECO:0000250|UniProtKB:O70167}.
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:18373, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57658, ChEBI:CHEBI:58178, ChEBI:CHEBI:456216; EC=2.7.1.154; Evid...
null
null
null
null
FUNCTION: Generates phosphatidylinositol 3-phosphate (PtdIns3P) and phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) that act as second messengers (By similarity). May play a role in SDF1A-stimulated chemotaxis (By similarity). {ECO:0000250|UniProtKB:O70167, ECO:0000250|UniProtKB:O70173}.
Homo sapiens (Human)
O75751
S22A3_HUMAN
MPSFDEALQRVGEFGRFQRRVFLLLCLTGVTFAFLFVGVVFLGTQPDHYWCRGPSAAALAERCGWSPEEEWNRTAPASRGPEPPERRGRCQRYLLEAANDSASATSALSCADPLAAFPNRSAPLVPCRGGWRYAQAHSTIVSEFDLVCVNAWMLDLTQAILNLGFLTGAFTLGYAADRYGRIVIYLLSCLGVGVTGVVVAFAPNFPVFVIFRFLQGVFGKGTWMTCYVIVTEIVGSKQRRIVGIVIQMFFTLGIIILPGIAYFIPNWQGIQLAITLPSFLFLLYYWVVPESPRWLITRKKGDKALQILRRIAKCNGKYLS...
null
null
cellular detoxification [GO:1990748]; dopamine transport [GO:0015872]; dopamine uptake [GO:0090494]; epinephrine transport [GO:0048241]; epinephrine uptake [GO:0051625]; histamine metabolic process [GO:0001692]; histamine transport [GO:0051608]; histamine uptake [GO:0051615]; monoamine transport [GO:0015844]; monoatomi...
apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; endomembrane system [GO:0012505]; membrane [GO:0016020]; mitochondrial membrane [GO:0031966]; neuronal cell body [GO:0043025]; nuclear outer membrane [GO:0005640]; plasma membrane [GO:0005886]; presynapse [GO:0098793]
monoamine transmembrane transporter activity [GO:0008504]; neurotransmitter transmembrane transporter activity [GO:0005326]; organic anion transmembrane transporter activity [GO:0008514]; organic cation transmembrane transporter activity [GO:0015101]; quaternary ammonium group transmembrane transporter activity [GO:001...
PF07690;
1.20.1250.20;
Major facilitator (TC 2.A.1) superfamily, Organic cation transporter (TC 2.A.1.19) family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15817714, ECO:0000269|PubMed:20858707}; Multi-pass membrane protein {ECO:0000305}. Apical cell membrane {ECO:0000269|PubMed:15817714, ECO:0000269|PubMed:16263091}; Multi-pass membrane protein {ECO:0000305}. Basolateral cell membrane {ECO:0000269|PubMed:15817714}; ...
CATALYTIC ACTIVITY: Reaction=(R)-noradrenaline(out) = (R)-noradrenaline(in); Xref=Rhea:RHEA:73871, ChEBI:CHEBI:72587; Evidence={ECO:0000269|PubMed:10196521, ECO:0000269|PubMed:16581093, ECO:0000269|PubMed:20858707}; CATALYTIC ACTIVITY: Reaction=(R)-adrenaline(out) = (R)-adrenaline(in); Xref=Rhea:RHEA:73875, ChEBI:CHEBI...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=126 uM for cyclo(his-pro) {ECO:0000269|PubMed:17460754}; KM=139 uM for salsolinol {ECO:0000269|PubMed:17460754}; KM=220 uM for histamine {ECO:0000269|PubMed:16581093}; KM=641 uM for histamine {ECO:0000269|PubMed:20858707}; KM=240 uM for adrenaline {ECO:0000269|PubM...
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5 for agmatine and MPP(+) transport. {ECO:0000269|PubMed:12538837};
null
FUNCTION: Electrogenic voltage-dependent transporter that mediates the transport of a variety of organic cations such as endogenous bioactive amines, cationic drugs and xenobiotics (PubMed:10196521, PubMed:10966924, PubMed:12538837, PubMed:17460754, PubMed:20858707). Cation cellular uptake or release is driven by the e...
Homo sapiens (Human)
O75752
B3GL1_HUMAN
MASALWTVLPSRMSLRSLKWSLLLLSLLSFFVMWYLSLPHYNVIERVNWMYFYEYEPIYRQDFHFTLREHSNCSHQNPFLVILVTSHPSDVKARQAIRVTWGEKKSWWGYEVLTFFLLGQEAEKEDKMLALSLEDEHLLYGDIIRQDFLDTYNNLTLKTIMAFRWVTEFCPNAKYVMKTDTDVFINTGNLVKYLLNLNHSEKFFTGYPLIDNYSYRGFYQKTHISYQEYPFKVFPPYCSGLGYIMSRDLVPRIYEMMGHVKPIKFEDVYVGICLNLLKVNIHIPEDTNLFFLYRIHLDVCQLRRVIAAHGFSSKEIITFW...
2.4.1.79
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:10993897, ECO:0000269|PubMed:9582303};
glycosphingolipid biosynthetic process [GO:0006688]; oligosaccharide biosynthetic process [GO:0009312]; protein O-linked glycosylation [GO:0006493]
Golgi membrane [GO:0000139]
galactosylgalactosylglucosylceramide beta-D-acetylgalactosaminyltransferase activity [GO:0047273]; UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase activity [GO:0008499]
PF01762;
3.90.550.50;
Glycosyltransferase 31 family
null
SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II membrane protein.
CATALYTIC ACTIVITY: Reaction=a globoside Gb3Cer (d18:1(4E)) + UDP-N-acetyl-alpha-D-galactosamine = a globoside Gb4Cer (d18:1(4E)) + H(+) + UDP; Xref=Rhea:RHEA:22252, ChEBI:CHEBI:15378, ChEBI:CHEBI:18259, ChEBI:CHEBI:18313, ChEBI:CHEBI:58223, ChEBI:CHEBI:67138; EC=2.4.1.79; Evidence={ECO:0000269|PubMed:10993897}; Physio...
null
PATHWAY: Protein modification; protein glycosylation.
null
null
FUNCTION: Transfers N-acetylgalactosamine onto globotriaosylceramide (PubMed:10993897). Plays a critical role in preimplantation stage embryonic development (By similarity). {ECO:0000250|UniProtKB:Q920V1, ECO:0000269|PubMed:10993897}.
Homo sapiens (Human)
O75762
TRPA1_HUMAN
MKRSLRKMWRPGEKKEPQGVVYEDVPDDTEDFKESLKVVFEGSAYGLQNFNKQKKLKRCDDMDTFFLHYAAAEGQIELMEKITRDSSLEVLHEMDDYGNTPLHCAVEKNQIESVKFLLSRGANPNLRNFNMMAPLHIAVQGMNNEVMKVLLEHRTIDVNLEGENGNTAVIIACTTNNSEALQILLKKGAKPCKSNKWGCFPIHQAAFSGSKECMEIILRFGEEHGYSRQLHINFMNNGKATPLHLAVQNGDLEMIKMCLDNGAQIDPVEKGRCTAIHFAATQGATEIVKLMISSYSGSVDIVNTTDGCHETMLHRASLFD...
null
null
calcium ion transmembrane transport [GO:0070588]; cell surface receptor signaling pathway [GO:0007166]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to organic substance [GO:0071310]; detection of chemical stimulus involved in sensory perception of pain [GO:0050968]; detection of mechanical st...
plasma membrane [GO:0005886]; stereocilium bundle [GO:0032421]
calcium channel activity [GO:0005262]; channel activity [GO:0015267]; identical protein binding [GO:0042802]; intracellularly gated calcium channel activity [GO:0015278]; temperature-gated cation channel activity [GO:0097604]
PF00023;PF12796;PF00520;
1.25.40.20;
Transient receptor (TC 1.A.4) family
PTM: TRPA1 activation by electrophiles occurs though covalent modification of specific cysteine residues in the N-terminal cytoplasmic domain (PubMed:25389312). {ECO:0000305|PubMed:25389312}.; PTM: Hydroxylation is required for TRPA1 activity inhibition in normoxia. In hypoxia, the decrease in oxygen concentration dimi...
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20547126, ECO:0000269|PubMed:21873995, ECO:0000269|PubMed:25389312, ECO:0000269|PubMed:25855297}; Multi-pass membrane protein {ECO:0000305}.
null
null
null
null
null
FUNCTION: Receptor-activated non-selective cation channel involved in pain detection and possibly also in cold perception, oxygen concentration perception, cough, itch, and inner ear function (PubMed:21873995, PubMed:23199233, PubMed:25389312, PubMed:25855297). Shows 8-fold preference for divalent over monovalent catio...
Homo sapiens (Human)
O75771
RA51D_HUMAN
MGVLRVGLCPGLTEEMIQLLRSHRIKTVVDLVSADLEEVAQKCGLSYKALVALRRVLLAQFSAFPVNGADLYEELKTSTAILSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVCLCMAANVAHGLQQNVLYVDSNGGLTASRLLQLLQAKTQDEEEQAEALRRIQVVHAFDIFQMLDVLQELRGTVAQQVTGSSGTVKVVVVDSVTAVVSPLLGGQQREGLALMMQLARELKTLARDLGMAVVVTNHITRDRDSGRLKPALGRSWSFVPSTRILLDTIEGAGASGGRRMACLAKSSRQPTGFQEMVDIGTWGTSEQS...
null
null
DNA repair [GO:0006281]; DNA strand invasion [GO:0042148]; double-strand break repair via homologous recombination [GO:0000724]; interstrand cross-link repair [GO:0036297]; reciprocal meiotic recombination [GO:0007131]; regulation of cell cycle [GO:0051726]; telomere maintenance [GO:0000723]; telomere maintenance via r...
centrosome [GO:0005813]; chromosome, telomeric region [GO:0000781]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; Rad51B-Rad51C-Rad51D-XRCC2 complex [GO:0033063]; replication fork [GO:0005657]
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent activity, acting on DNA [GO:0008094]; ATP-dependent DNA damage sensor activity [GO:0140664]; DNA binding [GO:0003677]; four-way junction DNA binding [GO:0000400]; gamma-tubulin binding [GO:0043015]; single-stranded DNA binding [GO:0003697]
PF08423;PF21794;
3.40.50.300;
RecA family, RAD51 subfamily
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Chromosome, telomere.
null
null
null
null
null
FUNCTION: Involved in the homologous recombination repair (HRR) pathway of double-stranded DNA breaks arising during DNA replication or induced by DNA-damaging agents. Bind to single-stranded DNA (ssDNA) and has DNA-dependent ATPase activity. Part of the RAD51 paralog protein complex BCDX2 which acts in the BRCA1-BRCA2...
Homo sapiens (Human)
O75781
PALM_HUMAN
MEVLAAETTSQQERLQAIAEKRKRQAEIENKRRQLEDERRQLQHLKSKALRERWLLEGTPSSASEGDEDLRRQMQDDEQKTRLLEDSVSRLEKEIEVLERGDSAPATAKENAAAPSPVRAPAPSPAKEERKTEVVMNSQQTPVGTPKDKRVSNTPLRTVDGSPMMKAAMYSVEITVEKDKVTGETRVLSSTTLLPRQPLPLGIKVYEDETKVVHAVDGTAENGIHPLSSSEVDELIHKADEVTLSEAGSTAGAAETRGAVEGAARTTPSRREITGVQAQPGEATSGPPGIQPGQEPPVTMIFMGYQNVEDEAETKKVLGL...
null
null
adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway [GO:0007193]; cellular response to electrical stimulus [GO:0071257]; cytoskeleton organization [GO:0007010]; negative regulation of dopamine receptor signaling pathway [GO:0060160]; positive regulation of filopodium assembly [GO:0051491]; protein...
apicolateral plasma membrane [GO:0016327]; axon [GO:0030424]; basolateral plasma membrane [GO:0016323]; cytoplasmic side of plasma membrane [GO:0009898]; cytoplasmic vesicle [GO:0031410]; dendritic spine [GO:0043197]; filopodium membrane [GO:0031527]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; postsynaptic...
D3 dopamine receptor binding [GO:0031750]
PF03285;
null
Paralemmin family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14978216}; Lipid-anchor {ECO:0000269|PubMed:14978216}; Cytoplasmic side {ECO:0000269|PubMed:14978216}. Cell projection, filopodium membrane {ECO:0000269|PubMed:14978216}; Lipid-anchor {ECO:0000269|PubMed:14978216}. Cell projection, axon {ECO:0000250}. Cell project...
null
null
null
null
null
FUNCTION: Involved in plasma membrane dynamics and cell process formation. Isoform 1 and isoform 2 are necessary for axonal and dendritic filopodia induction, for dendritic spine maturation and synapse formation in a palmitoylation-dependent manner. {ECO:0000269|PubMed:14978216}.
Homo sapiens (Human)
O75783
RHBL1_HUMAN
MGRVEDGGTTEELEDWDPGTSALPAPGIKQGPREQTGTGPLSQKCWEPEPDAPSQPGPALWSRGRARTQALAGGSSLQQLDPENTGFIGADTFTGLVHSHELPLDPAKLDMLVALAQSNEQGQVCYQELVDLISSKRSSSFKRAIANGQRALPRDGPLDEPGLGVYKRFVRYVAYEILPCEVDRRWYFYRHRSCPPPVFMASVTLAQIIVFLCYGARLNKWVLQTYHPEYMKSPLVYHPGHRARAWRFLTYMFMHVGLEQLGFNALLQLMIGVPLEMVHGLLRISLLYLAGVLAGSLTVSITDMRAPVVGGSGGVYALCS...
3.4.21.105
null
proteolysis [GO:0006508]; signal transduction [GO:0007165]
membrane [GO:0016020]; plasma membrane [GO:0005886]
serine-type endopeptidase activity [GO:0004252]
PF01694;
1.10.238.10;1.20.1540.10;
Peptidase S54 family
null
SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CATALYTIC ACTIVITY: Reaction=Cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains.; EC=3.4.21.105;
null
null
null
null
FUNCTION: May be involved in regulated intramembrane proteolysis and the subsequent release of functional polypeptides from their membrane anchors. {ECO:0000250}.
Homo sapiens (Human)
O75787
RENR_HUMAN
MAVFVVLLALVAGVLGNEFSILKSPGSVVFRNGNWPIPGERIPDVAALSMGFSVKEDLSWPGLAVGNLFHRPRATVMVMVKGVNKLALPPGSVISYPLENAVPFSLDSVANSIHSLFSEETPVVLQLAPSEERVYMVGKANSVFEDLSVTLRQLRNRLFQENSVLSSLPLNSLSRNNEVDLLFLSELQVLHDISSLLSRHKHLAKDHSPDLYSLELAGLDEIGKRYGEDSEQFRDASKILVDALQKFADDMYSLYGGNAVVELVTVKSFDTSLIRKTRTILEAKQAKNPASPYNLAYKYNFEYSVVFNMVLWIMIALALA...
null
null
angiotensin maturation [GO:0002003]; central nervous system maturation [GO:0021626]; endosomal lumen acidification [GO:0048388]; eye pigmentation [GO:0048069]; Golgi lumen acidification [GO:0061795]; head morphogenesis [GO:0060323]; intracellular pH reduction [GO:0051452]; lysosomal lumen acidification [GO:0007042]; po...
autophagosome membrane [GO:0000421]; axon [GO:0030424]; clathrin-coated vesicle membrane [GO:0030665]; dendritic spine membrane [GO:0032591]; endoplasmic reticulum membrane [GO:0005789]; endosome membrane [GO:0010008]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; ficolin-1-rich gra...
signaling receptor activity [GO:0038023]
PF07850;
null
null
PTM: Phosphorylated. {ECO:0000269|PubMed:12045255}.; PTM: Proteolytically cleaved by a furin-like convertase in the trans-Golgi network to generate N- and C-terminal fragments. {ECO:0000269|PubMed:29127204}.
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:29127204}; Single-pass type I membrane protein {ECO:0000305}. Lysosome membrane {ECO:0000269|PubMed:29127204}; Single-pass type I membrane protein {ECO:0000305}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:Q9CYN9}; Single-pa...
null
null
null
null
null
FUNCTION: Multifunctional protein which functions as a renin, prorenin cellular receptor and is involved in the assembly of the lysosomal proton-transporting V-type ATPase (V-ATPase) and the acidification of the endo-lysosomal system (PubMed:12045255, PubMed:29127204, PubMed:30374053, PubMed:32276428). May mediate reni...
Homo sapiens (Human)
O75791
GRAP2_HUMAN
MEAVAKFDFTASGEDELSFHTGDVLKILSNQEEWFKAELGSQEGYVPKNFIDIQFPKWFHEGLSRHQAENLLMGKEVGFFIIRASQSSPGDFSISVRHEDDVQHFKVMRDNKGNYFLWTEKFPSLNKLVDYYRTNSISRQKQIFLRDRTREDQGHRGNSLDRRSQGGPHLSGAVGEEIRPSMNRKLSDHPPTLPLQQHQHQPQPPQYAPAPQQLQQPPQQRYLQHHHFHQERRGGSLDINDGHCGTGLGSEMNAALMHRRHTDPVQLQAAGRVRWARALYDFEALEDDELGFHSGEVVEVLDSSNPSWWTGRLHNKLGLF...
null
null
cell-cell signaling [GO:0007267]; Ras protein signal transduction [GO:0007265]; regulation of MAPK cascade [GO:0043408]; signal transduction [GO:0007165]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; endosome [GO:0005768]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
phosphotyrosine residue binding [GO:0001784]
PF00017;PF00018;
3.30.505.10;2.30.30.40;
GRB2/sem-5/DRK family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21179510}. Cytoplasm {ECO:0000269|PubMed:21179510}. Endosome {ECO:0000269|PubMed:21179510}.
null
null
null
null
null
FUNCTION: Interacts with SLP-76 to regulate NF-AT activation. Binds to tyrosine-phosphorylated shc.
Homo sapiens (Human)
O75792
RNH2A_HUMAN
MDLSELERDNTGRCRLSSPVPAVCRKEPCVLGVDEAGRGPVLGPMVYAICYCPLPRLADLEALKVADSKTLLESERERLFAKMEDTDFVGWALDVLSPNLISTSMLGRVKYNLNSLSHDTATGLIQYALDQGVNVTQVFVDTVGMPETYQARLQQSFPGIEVTVKAKADALYPVVSAASICAKVARDQAVKKWQFVEKLQDLDTDYGSGYPNDPKTKAWLKEHVEPVFGFPQFVRFSWRTAQTILEKEAEDVIWEDSASENQEGLRKITSYFLNEGSQARPRSSHRYFLERGLESATSL
3.1.26.4
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding. {ECO:0000250};
DNA replication [GO:0006260]; DNA replication, removal of RNA primer [GO:0043137]; mismatch repair [GO:0006298]; RNA catabolic process [GO:0006401]
cytosol [GO:0005829]; nucleoplasm [GO:0005654]; ribonuclease H2 complex [GO:0032299]
metal ion binding [GO:0046872]; RNA binding [GO:0003723]; RNA nuclease activity [GO:0004540]; RNA-DNA hybrid ribonuclease activity [GO:0004523]
PF01351;
3.30.420.10;1.10.10.460;
RNase HII family, Eukaryotic subfamily
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4; Evidence={ECO:0000269|PubMed:21177858};
null
null
null
null
FUNCTION: Catalytic subunit of RNase HII, an endonuclease that specifically degrades the RNA of RNA:DNA hybrids. Participates in DNA replication, possibly by mediating the removal of lagging-strand Okazaki fragment RNA primers during DNA replication. Mediates the excision of single ribonucleotides from DNA:RNA duplexes...
Homo sapiens (Human)
O75794
CD123_HUMAN
MKKEHVLHCQFSAWYPFFRGVTIKSVILPLPQNVKDYLLDDGTLVVSGRDDPPTHSQPDSDDEAEEIQWSDDENTATLTAPEFPEFATKVQEAINSLGGSVFPKLNWSAPRDAYWIAMNSSLKCKTLSDIFLLFKSSDFITRDFTQPFIHCTDDSPDPCIEYELVLRKWCELIPGAEFRCFVKENKLIGISQRDYTQYYDHISKQKEEIRRCIQDFFKKHIQYKFLDEDFVFDIYRDSRGKVWLIDFNPFGEVTDSLLFTWEELISENNLNGDFSEVDAQEQDSPAFRCTNSEVTVQPSPYLSYRLPKDFVDLSTGEDAH...
null
null
eukaryotic translation initiation factor 2 complex assembly [GO:1905143]
cytoplasm [GO:0005737]
ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; protein folding chaperone [GO:0044183]
PF07065;
null
CDC123 family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q62834}.
null
null
null
null
null
FUNCTION: ATP-dependent protein-folding chaperone for the eIF2 complex (PubMed:35031321, PubMed:37507029). Binds to the gamma subunit of the eIF2 complex which allows the subunit to assemble with the alpha and beta subunits (By similarity). {ECO:0000250|UniProtKB:Q05791, ECO:0000269|PubMed:35031321, ECO:0000269|PubMed:...
Homo sapiens (Human)
O75795
UDB17_HUMAN
MSLKWMSVFLLMQLSCYFSSGSCGKVLVWPTEYSHWINMKTILEELVQRGHEVIVLTSSASILVNASKSSAIKLEVYPTSLTKNDLEDFFMKMFDRWTYSISKNTFWSYFSQLQELCWEYSDYNIKLCEDAVLNKKLMRKLQESKFDVLLADAVNPCGELLAELLNIPFLYSLRFSVGYTVEKNGGGFLFPPSYVPVVMSELSDQMIFMERIKNMIYMLYFDFWFQAYDLKKWDQFYSEVLGRPTTLFETMGKAEMWLIRTYWDFEFPRPFLPNVDFVGGLHCKPAKPLPKEMEEFVQSSGENGIVVFSLGSMISNMSEE...
2.4.1.17
null
cellular glucuronidation [GO:0052695]; estrogen metabolic process [GO:0008210]; steroid metabolic process [GO:0008202]; xenobiotic metabolic process [GO:0006805]
endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]
glucuronosyltransferase activity [GO:0015020]
PF00201;
3.40.50.2000;
UDP-glycosyltransferase family
null
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305|PubMed:23288867}; Single-pass membrane protein {ECO:0000255}.
CATALYTIC ACTIVITY: Reaction=glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP; Xref=Rhea:RHEA:21032, ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:132367, ChEBI:CHEBI:132368; EC=2.4.1.17; Evidence={ECO:0000269|PubMed:16595710, ECO:0000269|PubMed:18719240...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=11.4 uM for 17beta-estradiol/estradiol (when assaying glucuronidation at position 17) {ECO:0000269|PubMed:18719240}; KM=10 uM for testosterone (when assaying glucuronidation at position 17) {ECO:0000269|PubMed:19022937}; KM=3.4 uM for testosterone {ECO:0000269|PubM...
null
null
null
FUNCTION: UDP-glucuronosyltransferase (UGT) that catalyzes phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase the metabolite's water solubility, thereby facilitating excretion into either the urine or bile (PubMed:16595710, PubMed:18719240, PubMed:1902293...
Homo sapiens (Human)
O75800
ZMY10_HUMAN
MGDLELLLPGEAEVLVRGLRSFPLREMGSEGWNQQHENLEKLNMQAILDATVSQGEPIQELLVTHGKVPTLVEELIAVEMWKQKVFPVFCRVEDFKPQNTFPIYMVVHHEASIINLLETVFFHKEVCESAEDTVLDLVDYCHRKLTLLVAQSGCGGPPEGEGSQDSNPMQELQKQAELMEFEIALKALSVLRYITDCVDSLSLSTLSRMLSTHNLPCLLVELLEHSPWSRREGGKLQQFEGSRWHTVAPSEQQKLSKLDGQVWIALYNLLLSPEAQARYCLTSFAKGRLLKLRAFLTDTLLDQLPNLAHLQSFLAHLTLT...
null
null
cilium movement [GO:0003341]; inner dynein arm assembly [GO:0036159]; motile cilium assembly [GO:0044458]; outer dynein arm assembly [GO:0036158]; positive regulation of motile cilium assembly [GO:1905505]; protein localization to cilium [GO:0061512]
apical plasma membrane [GO:0016324]; centriolar satellite [GO:0034451]; cytoplasm [GO:0005737]; dynein axonemal particle [GO:0120293]
metal ion binding [GO:0046872]; molecular adaptor activity [GO:0060090]; protein folding chaperone [GO:0044183]
PF01753;
6.10.140.2220;
ZMYND10 family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6AXZ5}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000250|UniProtKB:Q6AXZ5}. Apical cell membrane {ECO:0000250|UniProtKB:Q99ML0}. Dynein axonemal particle {ECO:0000250|UniProtKB:Q5FWU8}.
null
null
null
null
null
FUNCTION: Plays a role in axonemal structure organization and motility (PubMed:23891469, PubMed:23891471). Involved in axonemal pre-assembly of inner and outer dynein arms (IDA and ODA, respectively) for proper axoneme building for cilia motility (By similarity). May act by indirectly regulating transcription of dynein...
Homo sapiens (Human)
O75807
PR15A_HUMAN
MAPGQAPHQATPWRDAHPFFLLSPVMGLLSRAWSRLRGLGPLEPWLVEAVKGAALVEAGLEGEARTPLAIPHTPWGRRPEEEAEDSGGPGEDRETLGLKTSSSLPEAWGLLDDDDGMYGEREATSVPRGQGSQFADGQRAPLSPSLLIRTLQGSDKNPGEEKAEEEGVAEEEGVNKFSYPPSHRECCPAVEEEDDEEAVKKEAHRTSTSALSPGSKPSTWVSCPGEEENQATEDKRTERSKGARKTSVSPRSSGSDPRSWEYRSGEASEEKEEKAHKETGKGEAAPGPQSSAPAQRPQLKSWWCQPSDEEEGEVKALGAA...
null
null
apoptotic process [GO:0006915]; DNA damage response [GO:0006974]; intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress [GO:0070059]; negative regulation of PERK-mediated unfolded protein response [GO:1903898]; negative regulation of phosphoprotein phosphatase activity [GO:0032515]; negative...
cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; protein phosphatase type 1 complex [GO:0000164]
protein kinase binding [GO:0019901]; protein phosphatase 1 binding [GO:0008157]; protein phosphatase activator activity [GO:0072542]; protein phosphatase regulator activity [GO:0019888]
PF10488;
null
PPP1R15 family
PTM: Phosphorylated at multiple Ser/Thr residues. Phosphorylated on tyrosine by LYN; which impairs its antiproliferative activity. Phosphorylation at Tyr-262 enhances proteasomal degradation, this position is dephosphorylated by PTPN2. {ECO:0000269|PubMed:11517336, ECO:0000269|PubMed:24092754}.; PTM: Polyubiquitinated....
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side {ECO:0000269|PubMed:12556489, ECO:0000269|PubMed:21518769, ECO:0000269|PubMed:26742780}. Mitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic side {ECO:0000269|PubMed:21518769}. Note=Associates with mem...
null
null
null
null
null
FUNCTION: Recruits the serine/threonine-protein phosphatase PPP1CA to prevents excessive phosphorylation of the translation initiation factor eIF-2A/EIF2S1, thereby reversing the shut-off of protein synthesis initiated by stress-inducible kinases and facilitating recovery of cells from stress (PubMed:26095357, PubMed:2...
Homo sapiens (Human)
O75808
CAN15_HUMAN
MATVGEWSCVRCTFLNPAGQRQCSICEAPRHKPDLNHILRLSVEEQKWPCARCTFRNFLGKEACEVCGFTPEPAPGAAFLPVLNGVLPKPPAILGEPKGSCQEEAGPVRTAGLVATEPARGQCEDKDEEEKEEQEEEEGAAEPRGGWACPRCTLHNTPVASSCSVCGGPRRLSLPRIPPEALVVPEVVAPAGFHVVPAAPPPGLPGEGAEANPPATSQGPAAEPEPPRVPPFSPFSSTLQNNPVPRSRREVPPQLQPPVPEAAQPSPSAGCRGAPQGSGWAGASRLAELLSGKRLSVLEEEATEGGTSRVEAGSSTSGSD...
3.4.22.-
null
proteolysis [GO:0006508]
cytoplasm [GO:0005737]
calcium-dependent cysteine-type endopeptidase activity [GO:0004198]; metal ion binding [GO:0046872]
PF00648;PF00641;
3.90.70.10;4.10.1060.10;2.30.30.380;
Peptidase C2 family
null
null
null
null
null
null
null
null
Homo sapiens (Human)
O75815
BCAR3_HUMAN
MAAGKFASLPRNMPVNHQFPLASSMDLLSSRSPLAEHRPDAYQDVSIHGTLPRKKKGPPPIRSCDDFSHMGTLPHSKSPRQNSPVTQDGIQESPWQDRHGETFTFRDPHLLDPTVEYVKFSKERHIMDRTPEKLKKELEEELLLSSEDLRSHAWYHGRIPRQVSENLVQRDGDFLVRDSLSSPGNFVLTCQWKNLAQHFKINRTVLRLSEAYSRVQYQFEMESFDSIPGLVRCYVGNRRPISQQSGAIIFQPINRTVPLRCLEEHYGTSPGQAREGSLTKGRPDVAKRLSLTMGGVQAREQNLPRGNLLRNKEKSGSQPA...
null
null
endothelin receptor signaling pathway [GO:0086100]; epidermal growth factor receptor signaling pathway [GO:0007173]; insulin receptor signaling pathway [GO:0008286]; lens morphogenesis in camera-type eye [GO:0002089]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of GTPase activ...
cytoplasm [GO:0005737]; focal adhesion [GO:0005925]; membrane [GO:0016020]
guanyl-nucleotide exchange factor activity [GO:0005085]; kinase binding [GO:0019900]; phosphotyrosine residue binding [GO:0001784]
PF00617;PF00017;
1.10.840.10;3.30.505.10;
null
PTM: Phosphorylated on tyrosine residues. {ECO:0000250|UniProtKB:Q9QZK2}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9QZK2}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q9QZK2}. Note=Localization to focal adhesions depends on interaction with PTPRA. {ECO:0000250|UniProtKB:Q9QZK2}.
null
null
null
null
null
FUNCTION: Acts as an adapter protein downstream of several growth factor receptors to promote cell proliferation, migration, and redistribution of actin fibers (PubMed:24216110). Specifically involved in INS/insulin signaling pathway by mediating MAPK1/ERK2-MAPK3/ERK1 activation and DNA synthesis (PubMed:24216110). Pro...
Homo sapiens (Human)
O75817
POP7_HUMAN
MAENREPRGAVEAELDPVEYTLRKRLPSRLPRRPNDIYVNMKTDFKAQLARCQKLLDGGARGQNACSEIYIHGLGLAINRAINIALQLQAGSFGSLQVAANTSTVELVDELEPETDTREPLTRIRNNSAIHIRVFRVTPK
null
null
rRNA processing [GO:0006364]; tRNA 5'-leader removal [GO:0001682]; tRNA processing [GO:0008033]
cytoplasm [GO:0005737]; intracellular membrane-bounded organelle [GO:0043231]; multimeric ribonuclease P complex [GO:0030681]; nucleolar ribonuclease P complex [GO:0005655]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ribonuclease MRP complex [GO:0000172]
ribonuclease P activity [GO:0004526]; ribonuclease P RNA binding [GO:0033204]; RNA binding [GO:0003723]
PF12328;
3.30.110.20;
Histone-like Alba family
null
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:14715275, ECO:0000269|PubMed:20215441}. Cytoplasm {ECO:0000269|PubMed:14715275}. Cytoplasmic granule {ECO:0000269|PubMed:14715275}. Note=Under stress conditions colocalizes with SMN1 in punctuated cytoplasmic granules. {ECO:0000269|PubMed:14715275}.
null
null
null
null
null
FUNCTION: Component of ribonuclease P, a ribonucleoprotein complex that generates mature tRNA molecules by cleaving their 5'-ends (PubMed:30454648, PubMed:9630247). Also a component of the MRP ribonuclease complex, which cleaves pre-rRNA sequences (PubMed:28115465). {ECO:0000269|PubMed:28115465, ECO:0000269|PubMed:3045...
Homo sapiens (Human)
O75818
RPP40_HUMAN
MATLRRLREAPRHLLVCEKSNFGNHKSRHRHLVQTHYYNYRVSFLIPECGILSEELKNLVMNTGPYYFVKNLPLHELITPEFISTFIKKGSCYALTYNTHIDEDNTVALLPNGKLILSLDKDTYEETGLQGHPSQFSGRKIMKFIVSIDLMELSLNLDSKKYERISWSFKEKKPLKFDFLLAWHKTGSEESTMMSYFSKYQIQEHQPKVALSTLRDLQCPVLQSSELEGTPEVSCRALELFDWLGAVFSNVDLNNEPNNFISTYCCPEPSTVVAKAYLCTITGFILPEKICLLLEHLCHYFDEPKLAPWVTLSVQGFADS...
null
null
endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000447]; tRNA 5'-leader removal [GO:0001682]
multimeric ribonuclease P complex [GO:0030681]; nucleolar ribonuclease P complex [GO:0005655]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ribonuclease MRP complex [GO:0000172]
ribonuclease MRP activity [GO:0000171]; ribonuclease P activity [GO:0004526]; ribonuclease P RNA binding [GO:0033204]
PF08584;
null
null
null
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000305}.
null
null
null
null
null
FUNCTION: Component of ribonuclease P, a ribonucleoprotein complex that generates mature tRNA molecules by cleaving their 5'-ends (PubMed:30454648, PubMed:9630247). Also a component of the MRP ribonuclease complex, which cleaves pre-rRNA sequences (PubMed:28115465). {ECO:0000269|PubMed:28115465, ECO:0000269|PubMed:3045...
Homo sapiens (Human)
O75821
EIF3G_HUMAN
MPTGDFDSKPSWADQVEEEGEDDKCVTSELLKGIPLATGDTSPEPELLPGAPLPPPKEVINGNIKTVTEYKIDEDGKKFKIVRTFRIETRKASKAVARRKNWKKFGNSEFDPPGPNVATTTVSDDVSMTFITSKEDLNCQEEEDPMNKLKGQKIVSCRICKGDHWTTRCPYKDTLGPMQKELAEQLGLSTGEKEKLPGELEPVQATQNKTGKYVPPSLRDGASRRGESMQPNRRADDNATIRVTNLSEDTRETDLQELFRPFGSISRIYLAKDKTTGQSKGFAFISFHRREDAARAIAGVSGFGYDHLILNVEWAKPSTN
null
null
formation of cytoplasmic translation initiation complex [GO:0001732]; translational initiation [GO:0006413]; viral translational termination-reinitiation [GO:0075525]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; eukaryotic 43S preinitiation complex [GO:0016282]; eukaryotic 48S preinitiation complex [GO:0033290]; eukaryotic translation initiation factor 3 complex [GO:0005852]; perinuclear region of cytoplasm [GO:0048471]
RNA binding [GO:0003723]; translation initiation factor activity [GO:0003743]
PF12353;PF00076;
3.30.70.330;
EIF-3 subunit G family
PTM: Phosphorylated. Phosphorylation is enhanced upon serum stimulation. {ECO:0000255|HAMAP-Rule:MF_03006, ECO:0000269|PubMed:17322308}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03006}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03006, ECO:0000269|PubMed:17094969}. Cytoplasm, perinuclear region {ECO:0000255|HAMAP-Rule:MF_03006, ECO:0000269|PubMed:17094969}. Note=Colocalizes with AIFM1 in the nucleus and perinuclear region.
null
null
null
null
null
FUNCTION: RNA-binding 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, ...
Homo sapiens (Human)
O75822
EIF3J_HUMAN
MAAAAAAAGDSDSWDADAFSVEDPVRKVGGGGTAGGDRWEGEDEDEDVKDNWDDDDDEKKEEAEVKPEVKISEKKKIAEKIKEKERQQKKRQEEIKKRLEEPEEPKVLTPEEQLADKLRLKKLQEESDLELAKETFGVNNAVYGIDAMNPSSRDDFTEFGKLLKDKITQYEKSLYYASFLEVLVRDVCISLEIDDLKKITNSLTVLCSEKQKQEKQSKAKKKKKGVVPGGGLKATMKDDLADYGGYDGGYVQDYEDFM
null
null
formation of cytoplasmic translation initiation complex [GO:0001732]; 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]
identical protein binding [GO:0042802]; translation initiation factor activity [GO:0003743]
PF08597;
1.10.246.60;
EIF-3 subunit J family
PTM: Phosphorylated. Phosphorylation is enhanced upon serum stimulation. {ECO:0000255|HAMAP-Rule:MF_03009, ECO:0000269|PubMed:17322308}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03009}.
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:25849773, PubMed:27462815). The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-t...
Homo sapiens (Human)
O75828
CBR3_HUMAN
MSSCSRVALVTGANRGIGLAIARELCRQFSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLNVLVNNAAVAFKSDDPMPFDIKAEMTLKTNFFATRNMCNELLPIMKPHGRVVNISSLQCLRAFENCSEDLQERFHSETLTEGDLVDLMKKFVEDTKNEVHEREGWPNSPYGVSKLGVTVLSRILARRLDEKRKADRILVNACCPGPVKTDMDGKDSIRTVEEGAETPVYLALLPPDATEPQGQLVHDKVVQNW
1.1.1.184; 1.6.5.10
null
cognition [GO:0050890]; phylloquinone catabolic process [GO:0042376]; xenobiotic metabolic process [GO:0006805]
cytosol [GO:0005829]; extracellular space [GO:0005615]; nucleoplasm [GO:0005654]
3-keto sterol reductase activity [GO:0000253]; carbonyl reductase (NADPH) activity [GO:0004090]; NADPH binding [GO:0070402]; NADPH dehydrogenase (quinone) activity [GO:0008753]
PF00106;
3.40.50.720;
Short-chain dehydrogenases/reductases (SDR) family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18493841}.
CATALYTIC ACTIVITY: Reaction=a secondary alcohol + NADP(+) = a ketone + H(+) + NADPH; Xref=Rhea:RHEA:19257, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087, ChEBI:CHEBI:35681, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.184; Evidence={ECO:0000269|PubMed:18493841}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:19259; Evi...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=25 uM for menadione {ECO:0000269|PubMed:15537833}; KM=43 uM for menadione {ECO:0000269|PubMed:18493841}; KM=300 uM for 4-benzoylpyridine {ECO:0000269|PubMed:18493841}; KM=130 uM for 4-nitorobenzaldehyde {ECO:0000269|PubMed:18493841}; KM=420 uM for 1,2-naphthoquinon...
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5-7. {ECO:0000269|PubMed:15537833, ECO:0000269|PubMed:18493841};
null
FUNCTION: Catalyzes the NADPH-dependent reduction of carbonyl compounds to their corresponding alcohols (PubMed:18493841). Has low NADPH-dependent oxidoreductase activity. Acts on several orthoquinones, acts as well on non-quinone compounds, such as isatin or on the anticancer drug oracin (PubMed:15537833, PubMed:18493...
Homo sapiens (Human)
O75829
CNMD_HUMAN
MTENSDKVPIALVGPDDVEFCSPPAYATLTVKPSSPARLLKVGAVVLISGAVLLLFGAIGAFYFWKGSDSHIYNVHYTMSINGKLQDGSMEIDAGNNLETFKMGSGAEEAIAVNDFQNGITGIRFAGGEKCYIKAQVKARIPEVGAVTKQSISSKLEGKIMPVKYEENSLIWVAVDQPVKDNSFLSSKVLELCGDLPIFWLKPTYPKEIQRERREVVRKIVPTTTKRPHSGPRSNPGAGRLNNETRPSVQEDSQAFNPDNPYHQQEGESMTFDPRLDHEGICCIECRRSYTHCQKICEPLGGYYPWPYNYQGCRSACRVI...
null
null
cartilage development [GO:0051216]; cell differentiation [GO:0030154]; negative regulation of angiogenesis [GO:0016525]; negative regulation of endothelial cell proliferation [GO:0001937]; proteoglycan metabolic process [GO:0006029]; skeletal system development [GO:0001501]
endomembrane system [GO:0012505]; extracellular region [GO:0005576]; membrane [GO:0016020]
null
PF04089;
3.30.390.150;
Chondromodulin-1 family
PTM: After cleavage, the post-translationally modified ChM-I is secreted as a glycoprotein.
SUBCELLULAR LOCATION: [Chondromodulin-1]: Secreted, extracellular space, extracellular matrix. Note=Accumulated in the inter-territorial matrix of cartilage.; SUBCELLULAR LOCATION: [Chondrosurfactant protein]: Endomembrane system {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
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FUNCTION: Bifunctional growth regulator that stimulates the growth of cultured chondrocytes in the presence of basic fibroblast growth factor (FGF) but inhibits the growth of cultured vascular endothelial cells. May contribute to the rapid growth of cartilage and vascular invasion prior to the replacement of cartilage ...
Homo sapiens (Human)
O75832
PSD10_HUMAN
MEGCVSNLMVCNLAYSGKLEELKESILADKSLATRTDQDSRTALHWACSAGHTEIVEFLLQLGVPVNDKDDAGWSPLHIAASAGRDEIVKALLGKGAQVNAVNQNGCTPLHYAASKNRHEIAVMLLEGGANPDAKDHYEATAMHRAAAKGNLKMIHILLYYKASTNIQDTEGNTPLHLACDEERVEEAKLLVSQGASIYIENKEEKTPLQVAKGGLGLILKRMVEG
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apoptotic process [GO:0006915]; cytoplasmic sequestering of NF-kappaB [GO:0007253]; negative regulation of apoptotic process [GO:0043066]; negative regulation of DNA damage response, signal transduction by p53 class mediator [GO:0043518]; negative regulation of MAPK cascade [GO:0043409]; negative regulation of NF-kappa...
cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; intermediate filament cytoskeleton [GO:0045111]; neuron projection [GO:0043005]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; proteasome complex [GO:0000502]
cytoskeletal protein binding [GO:0008092]; NAD+ ADP-ribosyltransferase activity [GO:0003950]; protein-macromolecule adaptor activity [GO:0030674]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; transcription factor binding [GO:0008134]; transmembrane transporter binding [GO:0044325]
PF00023;PF12796;
1.25.40.20;
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SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18040287}. Nucleus {ECO:0000269|PubMed:18040287}.
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FUNCTION: Acts as a chaperone during the assembly of the 26S proteasome, specifically of the PA700/19S regulatory complex (RC). In the initial step of the base subcomplex assembly is part of an intermediate PSMD10:PSMC4:PSMC5:PAAF1 module which probably assembles with a PSMD5:PSMC2:PSMC1:PSMD2 module. Independently of ...
Homo sapiens (Human)
O75838
CIB2_HUMAN
MGNKQTIFTEEQLDNYQDCTFFNKKDILKLHSRFYELAPNLVPMDYRKSPIVHVPMSLIIQMPELRENPFKERIVAAFSEDGEGNLTFNDFVDMFSVLCESAPRELKANYAFKIYDFNTDNFICKEDLELTLARLTKSELDEEEVVLVCDKVIEEADLDGDGKLGFADFEDMIAKAPDFLSTFHIRI
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calcium ion homeostasis [GO:0055074]; cellular response to ATP [GO:0071318]; photoreceptor cell maintenance [GO:0045494]; positive regulation of cytosolic calcium ion concentration [GO:0007204]
blood microparticle [GO:0072562]; cell periphery [GO:0071944]; cuticular plate [GO:0032437]; cytoplasm [GO:0005737]; muscle tendon junction [GO:0005927]; neuromuscular junction [GO:0031594]; photoreceptor inner segment [GO:0001917]; photoreceptor outer segment [GO:0001750]; sarcolemma [GO:0042383]; stereocilium [GO:003...
calcium ion binding [GO:0005509]; integrin binding [GO:0005178]; magnesium ion binding [GO:0000287]; protein homodimerization activity [GO:0042803]
PF13499;
1.10.238.10;
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SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Z309}. Cell projection, stereocilium {ECO:0000269|PubMed:26173970, ECO:0000269|PubMed:26426422}. Photoreceptor inner segment {ECO:0000250|UniProtKB:Q9Z309}. Cell projection, cilium, photoreceptor outer segment {ECO:0000250|UniProtKB:Q9Z309}. Cell membrane, sarcol...
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FUNCTION: Calcium- and integrin-binding protein that plays a role in intracellular calcium homeostasis (By similarity). Acts as an auxiliary subunit of the sensory mechanoelectrical transduction (MET) channel in hair cells (By similarity). Essential for mechanoelectrical transduction (MET) currents in auditory hair cel...
Homo sapiens (Human)
O75840
KLF7_HUMAN
MDVLASYSIFQELQLVHDTGYFSALPSLEETWQQTCLELERYLQTEPRRISETFGEDLDCFLHASPPPCIEESFRRLDPLLLPVEAAICEKSSAVDILLSRDKLLSETCLSLQPASSSLDSYTAVNQAQLNAVTSLTPPSSPELSRHLVKTSQTLSAVDGTVTLKLVAKKAALSSVKVGGVATAAAAVTAAGAVKSGQSDSDQGGLGAEACPENKKRVHRCQFNGCRKVYTKSSHLKAHQRTHTGEKPYKCSWEGCEWRFARSDELTRHYRKHTGAKPFKCNHCDRCFSRSDHLALHMKRHI
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axon guidance [GO:0007411]; axonogenesis [GO:0007409]; dendrite morphogenesis [GO:0048813]; glucose homeostasis [GO:0042593]; negative regulation of adipose tissue development [GO:1904178]; negative regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0061179]; negative regulation of tr...
chromatin [GO:0000785]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; zinc ion binding [GO:0008270]
PF00096;
3.30.160.60;
Krueppel C2H2-type zinc-finger protein family
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SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9774444}.
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FUNCTION: Transcriptional factor (PubMed:16339272, PubMed:9774444). Plays a critical role in neuronal morphogenesis and survival of sensory neurons (By similarity). Represses the corneal epithelium differentiation (PubMed:28916725). Acts also as a metabolic regulator, by modulating insulin sensitivity in pancreatic bet...
Homo sapiens (Human)
O75841
UPK1B_HUMAN
MAKDNSTVRCFQGLLIFGNVIIGCCGIALTAECIFFVSDQHSLYPLLEATDNDDIYGAAWIGIFVGICLFCLSVLGIVGIMKSSRKILLAYFILMFIVYAFEVASCITAATQQDFFTPNLFLKQMLERYQNNSPPNNDDQWKNNGVTKTWDRLMLQDNCCGVNGPSDWQKYTSAFRTENNDADYPWPRQCCVMNNLKEPLNLEACKLGVPGFYHNQGCYELISGPMNRHAWGVAWFGFAILCWTFWVLLGTMFYWSRIEY
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epithelial cell differentiation [GO:0030855]; response to bacterium [GO:0009617]
apical plasma membrane urothelial plaque [GO:0120001]; extracellular exosome [GO:0070062]; membrane [GO:0016020]
structural molecule activity [GO:0005198]
PF00335;
1.10.1450.10;
Tetraspanin (TM4SF) family
PTM: N-glycosylated with high-mannose oligosaccharides. {ECO:0000250}.
SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
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FUNCTION: Component of the asymmetric unit membrane (AUM); a highly specialized biomembrane elaborated by terminally differentiated urothelial cells. May play an important role in normal bladder epithelial physiology, possibly in regulating membrane permeability of superficial umbrella cells or in stabilizing the apica...
Homo sapiens (Human)
O75843
AP1G2_HUMAN
MVVPSLKLQDLIEEIRGAKTQAQEREVIQKECAHIRASFRDGDPVHRHRQLAKLLYVHMLGYPAHFGQMECLKLIASSRFTDKRVGYLGAMLLLDERHDAHLLITNSIKNDLSQGIQPVQGLALCTLSTMGSAEMCRDLAPEVEKLLLQPSPYVRKKAILTAVHMIRKVPELSSVFLPPCAQLLHERHHGILLGTITLITELCERSPAALRHFRKVVPQLVHILRTLVTMGYSTEHSISGVSDPFLQVQILRLLRILGRNHEESSETMNDLLAQVATNTDTSRNAGNAVLFETVLTIMDIRSAAGLRVLAVNILGRFLLN...
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Golgi to vacuole transport [GO:0006896]; intracellular protein transport [GO:0006886]; vesicle-mediated transport [GO:0016192]
AP-1 adaptor complex [GO:0030121]; endosome membrane [GO:0010008]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; Golgi-associated vesicle [GO:0005798]; membrane [GO:0016020]; transport vesicle [GO:0030133]
clathrin adaptor activity [GO:0035615]
PF01602;PF02883;
2.60.40.1230;1.25.10.10;
Adaptor complexes large subunit family
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SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:11333915, ECO:0000269|PubMed:9762922}; Peripheral membrane protein; Cytoplasmic side {ECO:0000269|PubMed:11333915}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:9733768}; Peripheral membrane protein. Endosome membrane {ECO:0000269|PubMed:16867982}; ...
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FUNCTION: May function in protein sorting in late endosomes or multivesucular bodies (MVBs). {ECO:0000269|PubMed:9733768}.; FUNCTION: (Microbial infection) Involved in MVB-assisted maturation of hepatitis B virus (HBV). {ECO:0000269|PubMed:16867982, ECO:0000269|PubMed:17553870}.
Homo sapiens (Human)