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
O00159
MYO1C_HUMAN
MALQVELVPTGEIIRVVHPHRPCKLALGSDGVRVTMESALTARDRVGVQDFVLLENFTSEAAFIENLRRRFRENLIYTYIGPVLVSVNPYRDLQIYSRQHMERYRGVSFYEVPPHLFAVADTVYRALRTERRDQAVMISGESGAGKTEATKRLLQFYAETCPAPERGGAVRDRLLQSNPVLEAFGNAKTLRNDNSSRFGKYMDVQFDFKGAPVGGHILSYLLEKSRVVHQNHGERNFHIFYQLLEGGEEETLRRLGLERNPQSYLYLVKGQCAKVSSINDKSDWKVVRKALTVIDFTEDEVEDLLSIVASVLHLGNIHFA...
null
null
actin filament organization [GO:0007015]; actin filament-based movement [GO:0030048]; cellular response to type II interferon [GO:0071346]; chromatin remodeling [GO:0006338]; endocytosis [GO:0006897]; positive regulation of cell migration [GO:0030335]; positive regulation of cellular response to insulin stimulus [GO:19...
actin cytoskeleton [GO:0015629]; B-WICH complex [GO:0110016]; basal plasma membrane [GO:0009925]; brush border [GO:0005903]; cell cortex [GO:0005938]; cytoplasm [GO:0005737]; cytoplasmic vesicle membrane [GO:0030659]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; filamentous actin [GO:0031941]; lateral plas...
actin filament binding [GO:0051015]; ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; microfilament motor activity [GO:0000146]; signaling receptor binding [GO:0005102]; small GTPase binding [GO:0031267]
PF00612;PF00063;PF06017;
1.10.10.820;1.20.5.190;1.20.58.530;6.20.240.20;3.40.850.10;1.20.120.720;
TRAFAC class myosin-kinesin ATPase superfamily, Myosin family
PTM: Isoform 2 contains a N-acetylmethionine at position 1.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22736583}. Nucleus {ECO:0000269|PubMed:22736583}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q9WTI7}. Cell projection, stereocilium membrane {ECO:0000250|UniProtKB:Q92002}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q9WTI7}. Cell projection, ruffle membrane {ECO:00...
null
null
null
null
null
FUNCTION: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments. Involved in glucose transporter recycling in response to insuli...
Homo sapiens (Human)
O00160
MYO1F_HUMAN
MGSKERFHWQSHNVKQSGVDDMVLLPQITEDAIAANLRKRFMDDYIFTYIGSVLISVNPFKQMPYFTDREIDLYQGAAQYENPPHIYALTDNMYRNMLIDCENQCVIISGESGAGKTVAAKYIMGYISKVSGGGEKVQHVKDIILQSNPLLEAFGNAKTVRNNNSSRFGKYFEIQFSRGGEPDGGKISNFLLEKSRVVMQNENERNFHIYYQLLEGASQEQRQNLGLMTPDYYYYLNQSDTYQVDGTDDRSDFGETLSAMQVIGIPPSIQQLVLQLVAGILHLGNISFCEDGNYARVESVDLLAFPAYLLGIDSGRLQEK...
null
null
actin filament organization [GO:0007015]; endocytosis [GO:0006897]; vesicle transport along actin filament [GO:0030050]
actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; microvillus [GO:0005902]; plasma membrane [GO:0005886]; unconventional myosin complex [GO:0016461]; vesicle [GO:0031982]
actin binding [GO:0003779]; actin filament binding [GO:0051015]; ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; microfilament motor activity [GO:0000146]
PF00063;PF06017;PF00018;
1.10.10.820;1.20.5.4820;1.20.58.530;3.40.850.10;1.20.120.720;2.30.30.40;
TRAFAC class myosin-kinesin ATPase superfamily, Myosin family
null
null
null
null
null
null
null
FUNCTION: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments (By similarity). {ECO:0000250}.
Homo sapiens (Human)
O00161
SNP23_HUMAN
MDNLSSEEIQQRAHQITDESLESTRRILGLAIESQDAGIKTITMLDEQKEQLNRIEEGLDQINKDMRETEKTLTELNKCCGLCVCPCNRTKNFESGKAYKTTWGDGGENSPCNVVSKQPGPVTNGQLQQPTTGAASGGYIKRITNDAREDEMEENLTQVGSILGNLKDMALNIGNEIDAQNPQIKRITDKADTNRDRIDIANARAKKLIDS
null
null
exocytosis [GO:0006887]; histamine secretion by mast cell [GO:0002553]; membrane fusion [GO:0061025]; post-Golgi vesicle-mediated transport [GO:0006892]; protein transport [GO:0015031]; synaptic vesicle fusion to presynaptic active zone membrane [GO:0031629]; synaptic vesicle priming [GO:0016082]; vesicle targeting [GO...
adherens junction [GO:0005912]; azurophil granule [GO:0042582]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; mitochondrion [GO:0005739]; neuron projection [GO:0043005]; nucleoplasm [GO:0005654]; phagocytic vesicle membrane [GO:0030670]; plasma membrane [GO:0005886]; presynaps...
SNAP receptor activity [GO:0005484]; syntaxin binding [GO:0019905]; syntaxin-1 binding [GO:0017075]
PF00835;
1.20.5.110;
SNAP-25 family
null
SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. Cell membrane; Lipid-anchor. Synapse, synaptosome. Note=Mainly localized to the plasma membrane.
null
null
null
null
null
FUNCTION: Essential component of the high affinity receptor for the general membrane fusion machinery and an important regulator of transport vesicle docking and fusion.
Homo sapiens (Human)
O00165
HAX1_HUMAN
MSLFDLFRGFFGFPGPRSHRDPFFGGMTRDEDDDEEEEEEGGSWGRGNPRFHSPQHPPEEFGFGFSFSPGGGIRFHDNFGFDDLVRDFNSIFSDMGAWTLPSHPPELPGPESETPGERLREGQTLRDSMLKYPDSHQPRIFGGVLESDARSESPQPAPDWGSQRPFHRFDDVWPMDPHPRTREDNDLDSQVSQEGLGPVLQPQPKSYFKSISVTKITKPDGIVEERRTVVDSEGRTETTVTRHEADSSPRGDPESPRPPALDDAFSILDLFLGRWFRSR
null
null
cellular response to cytokine stimulus [GO:0071345]; granulocyte colony-stimulating factor signaling pathway [GO:0038158]; negative regulation of apoptotic process [GO:0043066]; positive regulation of granulocyte differentiation [GO:0030854]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positi...
actin cytoskeleton [GO:0015629]; apical plasma membrane [GO:0016324]; cell cortex [GO:0005938]; clathrin-coated vesicle [GO:0030136]; endoplasmic reticulum [GO:0005783]; lamellipodium [GO:0030027]; mitochondrial intermembrane space [GO:0005758]; mitochondrial matrix [GO:0005759]; mitochondrial outer membrane [GO:000574...
interleukin-1 binding [GO:0019966]; signaling adaptor activity [GO:0035591]
null
null
HAX1 family
PTM: Proteolytically cleaved by caspase-3 during apoptosis. {ECO:0000269|PubMed:18319618}.
SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:18971376, ECO:0000269|PubMed:9058808}. Endoplasmic reticulum {ECO:0000269|PubMed:18971376, ECO:0000269|PubMed:9058808}. Nucleus membrane {ECO:0000269|PubMed:9058808}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:O35387}. Cytoplasm, cell cortex {ECO:0000269|Pu...
null
null
null
null
null
FUNCTION: Recruits the Arp2/3 complex to the cell cortex and regulates reorganization of the cortical actin cytoskeleton via its interaction with KCNC3 and the Arp2/3 complex (PubMed:26997484). Slows down the rate of inactivation of KCNC3 channels (PubMed:26997484). Promotes GNA13-mediated cell migration. Involved in t...
Homo sapiens (Human)
O00167
EYA2_HUMAN
MVELVISPSLTVNSDCLDKLKFNRADAAVWTLSDRQGITKSAPLRVSQLFSRSCPRVLPRQPSTAMAAYGQTQYSAGIQQATPYTAYPPPAQAYGIPSYSIKTEDSLNHSPGQSGFLSYGSSFSTSPTGQSPYTYQMHGTTGFYQGGNGLGNAAGFGSVHQDYPSYPGFPQSQYPQYYGSSYNPPYVPASSICPSPLSTSTYVLQEASHNVPNQSSESLAGEYNTHNGPSTPAKEGDTDRPHRASDGKLRGRSKRSSDPSPAGDNEIERVFVWDLDETIIIFHSLLTGTFASRYGKDTTTSVRIGLMMEEMIFNLADTHL...
3.1.3.48
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:19858093}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:19858093};
cell differentiation [GO:0030154]; DNA repair [GO:0006281]; extrinsic apoptotic signaling pathway in absence of ligand [GO:0097192]; mesodermal cell fate specification [GO:0007501]; mitochondrial outer membrane permeabilization [GO:0097345]; negative regulation of extrinsic apoptotic signaling pathway in absence of lig...
cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
histone H2AXY142 phosphatase activity [GO:0140793]; magnesium ion binding [GO:0000287]; protein tyrosine phosphatase activity [GO:0004725]
PF00702;
3.40.50.12350;
HAD-like hydrolase superfamily, EYA family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10906137, ECO:0000269|PubMed:12500905}. Nucleus {ECO:0000269|PubMed:10906137, ECO:0000269|PubMed:12500905, ECO:0000269|PubMed:19497856}. Note=Retained in the cytoplasm via interaction with GNAZ and GNAI2 (PubMed:10906137). Interaction with SIX1, SIX2, SIX4 or SIX5 is ...
CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000269|PubMed:19351884};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.9 uM for H2AXY142ph {ECO:0000269|PubMed:19351884}; KM=80 uM for H2AXS139ph {ECO:0000269|PubMed:19351884};
null
null
null
FUNCTION: Functions both as protein phosphatase and as transcriptional coactivator for SIX1, and probably also for SIX2, SIX4 and SIX5 (PubMed:12500905, PubMed:23435380). Tyrosine phosphatase that dephosphorylates 'Tyr-142' of histone H2AX (H2AXY142ph) and promotes efficient DNA repair via the recruitment of DNA repair...
Homo sapiens (Human)
O00168
PLM_HUMAN
MASLGHILVFCVGLLTMAKAESPKEHDPFTYDYQSLQIGGLVIAGILFILGILIVLSRRCRCKFNQQQRTGEPDEEEGTFRSSIRRLSTRRR
null
null
chloride transport [GO:0006821]; muscle contraction [GO:0006936]; negative regulation of protein glutathionylation [GO:0010734]; positive regulation of sodium ion export across plasma membrane [GO:1903278]; potassium ion transport [GO:0006813]; regulation of cardiac muscle cell membrane potential [GO:0086036]; regulati...
apical plasma membrane [GO:0016324]; caveola [GO:0005901]; intercalated disc [GO:0014704]; plasma membrane [GO:0005886]; sarcolemma [GO:0042383]; sodium:potassium-exchanging ATPase complex [GO:0005890]; T-tubule [GO:0030315]
chloride channel activity [GO:0005254]; sodium channel regulator activity [GO:0017080]; transmembrane transporter binding [GO:0044325]
PF02038;
1.20.5.780;
FXYD family
PTM: Major plasma membrane substrate for cAMP-dependent protein kinase (PKA) and protein kinase C (PKC) in several different tissues (By similarity). Phosphorylated in response to insulin and adrenergic stimulation (By similarity). Phosphorylation at Ser-88 stimulates sodium/potassium-transporting ATPase activity while...
SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P56513}; Single-pass type I membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:O08589}; Single-pass type I membrane protein {ECO:0000255}. Membrane, caveola {ECO:0000250|UniProtKB:O08589}. Cell membrane, sarcolemma, T-tubule...
null
null
null
null
null
FUNCTION: Associates with and regulates the activity of the sodium/potassium-transporting ATPase (NKA) which transports Na(+) out of the cell and K(+) into the cell. Inhibits NKA activity in its unphosphorylated state and stimulates activity when phosphorylated. Reduces glutathionylation of the NKA beta-1 subunit ATP1B...
Homo sapiens (Human)
O00170
AIP_HUMAN
MADIIARLREDGIQKRVIQEGRGELPDFQDGTKATFHYRTLHSDDEGTVLDDSRARGKPMELIIGKKFKLPVWETIVCTMREGEIAQFLCDIKHVVLYPLVAKSLRNIAVGKDPLEGQRHCCGVAQMREHSSLGHADLDALQQNPQPLIFHMEMLKVESPGTYQQDPWAMTDEEKAKAVPLIHQEGNRLYREGHVKEAAAKYYDAIACLKNLQMKEQPGSPEWIQLDQQITPLLLNYCQCKLVVEEYYEVLDHCSSILNKYDDNVKAYFKRGKAHAAVWNAQEAQADFAKVLELDPALAPVVSRELRALEARIRQKDEED...
null
null
protein maturation by protein folding [GO:0022417]; protein targeting to mitochondrion [GO:0006626]; regulation of protein kinase A signaling [GO:0010738]; xenobiotic metabolic process [GO:0006805]
aryl hydrocarbon receptor complex [GO:0034751]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; nucleoplasm [GO:0005654]
aryl hydrocarbon receptor binding [GO:0017162]; GAF domain binding [GO:0036004]; peptidyl-prolyl cis-trans isomerase activity [GO:0003755]; transcription coactivator activity [GO:0003713]; unfolded protein binding [GO:0051082]
PF00254;
3.10.50.40;1.25.40.10;
null
null
SUBCELLULAR LOCATION: Cytoplasm.
null
null
null
null
null
FUNCTION: May play a positive role in AHR-mediated (aromatic hydrocarbon receptor) signaling, possibly by influencing its receptivity for ligand and/or its nuclear targeting.; FUNCTION: Cellular negative regulator of the hepatitis B virus (HBV) X protein.
Homo sapiens (Human)
O00175
CCL24_HUMAN
MAGLMTIVTSLLFLGVCAHHIIPTGSVVIPSPCCMFFVSKRIPENRVVSYQLSSRSTCLKAGVIFTTKKGQQFCGDPKQEWVQRYMKNLDAKQKKASPRARAVAVKGPVQRYPGNQTTC
null
null
cell-cell signaling [GO:0007267]; cellular response to interleukin-1 [GO:0071347]; cellular response to tumor necrosis factor [GO:0071356]; cellular response to type II interferon [GO:0071346]; chemokine-mediated signaling pathway [GO:0070098]; chemotaxis [GO:0006935]; cytoskeleton organization [GO:0007010]; eosinophil...
extracellular space [GO:0005615]
CCR chemokine receptor binding [GO:0048020]; CCR3 chemokine receptor binding [GO:0031728]; chemokine activity [GO:0008009]; receptor ligand activity [GO:0048018]
PF00048;
2.40.50.40;
Intercrine beta (chemokine CC) family
PTM: N-glycosylated. {ECO:0000269|PubMed:9104803}.
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9104803, ECO:0000269|PubMed:9365122}.
null
null
null
null
null
FUNCTION: Chemotactic for resting T-lymphocytes, and eosinophils (PubMed:9104803, PubMed:9365122). Has lower chemotactic activity for neutrophils but none for monocytes and activated lymphocytes (PubMed:9104803, PubMed:9365122). Is a strong suppressor of colony formation by a multipotential hematopoietic progenitor cel...
Homo sapiens (Human)
O00178
GTPB1_HUMAN
MATERSRSAMDSPVPASMFAPEPSSPGAARAAAAAARLHGGFDSDCSEDGEALNGEPELDLTSKLVLVSPTSEQYDSLLRQMWERMDEGCGETIYVIGQGSDGTEYGLSEADMEASYATVKSMAEQIEADVILLRERQEAGGRVRDYLVRKRVGDNDFLEVRVAVVGNVDAGKSTLLGVLTHGELDNGRGFARQKLFRHKHEIESGRTSSVGNDILGFDSEGNVVNKPDSHGGSLEWTKICEKSTKVITFIDLAGHEKYLKTTVFGMTGHLPDFCMLMVGSNAGIVGMTKEHLGLALALNVPVFVVVTKIDMCPANILQE...
null
null
cytoplasmic translation [GO:0002181]; GTP metabolic process [GO:0046039]; immune response [GO:0006955]; positive regulation of mRNA catabolic process [GO:0061014]; signal transduction [GO:0007165]; translational elongation [GO:0006414]
cytoplasmic exosome (RNase complex) [GO:0000177]; cytosol [GO:0005829]; membrane [GO:0016020]
alpha-aminoacyl-tRNA binding [GO:1904678]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; RNA binding [GO:0003723]; translation elongation factor activity [GO:0003746]; tRNA binding [GO:0000049]
PF00009;PF03144;
3.40.50.300;2.40.30.10;
TRAFAC class translation factor GTPase superfamily, Classic translation factor GTPase family, GTPBP1 subfamily
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
null
null
null
null
null
FUNCTION: Promotes degradation of target mRNA species. Plays a role in the regulation of circadian mRNA stability. Binds GTP and has GTPase activity (By similarity). {ECO:0000250}.
Homo sapiens (Human)
O00180
KCNK1_HUMAN
MLQSLAGSSCVRLVERHRSAWCFGFLVLGYLLYLVFGAVVFSSVELPYEDLLRQELRKLKRRFLEEHECLSEQQLEQFLGRVLEASNYGVSVLSNASGNWNWDFTSALFFASTVLSTTGYGHTVPLSDGGKAFCIIYSVIGIPFTLLFLTAVVQRITVHVTRRPVLYFHIRWGFSKQVVAIVHAVLLGFVTVSCFFFIPAAVFSVLEDDWNFLESFYFCFISLSTIGLGDYVPGEGYNQKFRELYKIGITCYLLLGLIAMLVVLETFCELHELKKFRKMFYVKKDKDEDQVHIIEHDQLSFSSITDQAAGMKEDQKQNEP...
null
null
potassium ion transmembrane transport [GO:0071805]; potassium ion transport [GO:0006813]; regulation of resting membrane potential [GO:0060075]; response to nicotine [GO:0035094]; sodium ion transmembrane transport [GO:0035725]; stabilization of membrane potential [GO:0030322]
apical plasma membrane [GO:0016324]; brush border membrane [GO:0031526]; dendrite [GO:0030425]; intracellular membrane-bounded organelle [GO:0043231]; inward rectifier potassium channel complex [GO:1902937]; membrane [GO:0016020]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; potassium channel complex [GO:0034...
identical protein binding [GO:0042802]; inward rectifier potassium channel activity [GO:0005242]; outward rectifier potassium channel activity [GO:0015271]; potassium channel activity [GO:0005267]; potassium ion leak channel activity [GO:0022841]; sodium channel activity [GO:0005272]
PF07885;
1.10.287.70;
Two pore domain potassium channel (TC 1.A.1.8) family
PTM: Sumoylation is controversial. Sumoylated by UBE2I (PubMed:15820677). Not sumoylated when expressed in xenopus oocytes or mammalian cells (PubMed:17693262). Sumoylation inactivates the channel, but does not interfere with expression at the cell membrane (PubMed:15820677). Sumoylation of a single subunit is sufficie...
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15820677, ECO:0000269|PubMed:17693262, ECO:0000269|PubMed:20498050, ECO:0000269|PubMed:21653227, ECO:0000269|PubMed:22282804, ECO:0000269|PubMed:22431633, ECO:0000269|PubMed:23169818, ECO:0000269|PubMed:25001086, ECO:0000269|PubMed:8605869, ECO:0000269|PubMed:8978...
null
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Note=Has a unit conductance of 34 pS. Both activation and channel closure are very rapid. Is not voltage-gated. The relationship between voltage and current is nearly linear. Has a mean open time of 0.3 msec at a membrane potential of -80 mV, and 1.9 msec at +80 mV (P...
null
null
null
FUNCTION: Ion channel that contributes to passive transmembrane potassium transport and to the regulation of the resting membrane potential in brain astrocytes, but also in kidney and in other tissues (PubMed:15820677, PubMed:21653227). Forms dimeric channels through which potassium ions pass in accordance with their e...
Homo sapiens (Human)
O00182
LEG9_HUMAN
MAFSGSQAPYLSPAVPFSGTIQGGLQDGLQITVNGTVLSSSGTRFAVNFQTGFSGNDIAFHFNPRFEDGGYVVCNTRQNGSWGPEERKTHMPFQKGMPFDLCFLVQSSDFKVMVNGILFVQYFHRVPFHRVDTISVNGSVQLSYISFQNPRTVPVQPAFSTVPFSQPVCFPPRPRGRRQKPPGVWPANPAPITQTVIHTVQSAPGQMFSTPAIPPMMYPHPAYPMPFITTILGGLYPSKSILLSGTVLPSAQRFHINLCSGNHIAFHLNPRFDENAVVRNTQIDNSWGSEERSLPRKMPFVRGQSFSVWILCEAHCLKVA...
null
null
cellular response to type II interferon [GO:0071346]; cellular response to virus [GO:0098586]; chemotaxis [GO:0006935]; ERK1 and ERK2 cascade [GO:0070371]; female pregnancy [GO:0007565]; inflammatory response [GO:0006954]; maternal process involved in female pregnancy [GO:0060135]; natural killer cell tolerance inducti...
collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular space [GO:0005615]; nucleus [GO:0005634]
carbohydrate binding [GO:0030246]; disaccharide binding [GO:0048030]; enzyme binding [GO:0019899]; galactose binding [GO:0005534]; galactoside binding [GO:0016936]
PF00337;
2.60.120.200;
null
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23242525}. Nucleus {ECO:0000269|PubMed:23242525}. Secreted {ECO:0000269|PubMed:23817958, ECO:0000269|PubMed:25578313}. Note=May also be secreted by a non-classical secretory pathway (By similarity). Secreted by mesenchymal stromal cells upon IFNG stimulation (PubMed:2...
null
null
null
null
null
FUNCTION: Binds galactosides (PubMed:18005988). Has high affinity for the Forssman pentasaccharide (PubMed:18005988). Ligand for HAVCR2/TIM3 (PubMed:16286920). Binding to HAVCR2 induces T-helper type 1 lymphocyte (Th1) death (PubMed:16286920). Also stimulates bactericidal activity in infected macrophages by causing mac...
Homo sapiens (Human)
O00186
STXB3_HUMAN
MAPPVAERGLKSVVWQKIKATVFDDCKKEGEWKIMLLDEFTTKLLASCCKMTDLLEEGITVVENIYKNREPVRQMKALYFITPTSKSVDCFLHDFASKSENKYKAAYIYFTDFCPDNLFNKIKASCSKSIRRCKEINISFIPHESQVYTLDVPDAFYYCYSPDPGNAKGKDAIMETMADQIVTVCATLDENPGVRYKSKPLDNASKLAQLVEKKLEDYYKIDEKSLIKGKTHSQLLIIDRGFDPVSTVLHELTFQAMAYDLLPIENDTYKYKTDGKEKEAILEEEDDLWVRIRHRHIAVVLEEIPKLMKEISSTKKATEG...
null
null
brain development [GO:0007420]; cellular response to type II interferon [GO:0071346]; insulin secretion [GO:0030073]; intracellular glucose homeostasis [GO:0001678]; intracellular protein transport [GO:0006886]; negative regulation of calcium ion-dependent exocytosis [GO:0045955]; negative regulation of glucose import ...
apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; phagocytic vesicle [GO:0045335]; plasma membrane [GO:0005886]; platelet alpha granule [GO:0031091]; presynapse [GO:0098793]; secretory granule [GO:0030141]; specific granule [GO:00425...
protein-containing complex binding [GO:0044877]; syntaxin binding [GO:0019905]; syntaxin-1 binding [GO:0017075]
PF00995;
1.25.40.60;3.40.50.1910;3.40.50.2060;
STXBP/unc-18/SEC1 family
PTM: Phosphorylated by PKC in platelets in response to thrombin stimulation; phosphorylation inhibits binding to STX4. {ECO:0000269|PubMed:10194441}.
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:10194441}. Cell membrane {ECO:0000269|PubMed:10194441}. Note=In platelets, predominantly cytosolic. Low amounts membrane-associated.
null
null
null
null
null
FUNCTION: Together with STX4 and VAMP2, may play a role in insulin-dependent movement of GLUT4 and in docking/fusion of intracellular GLUT4-containing vesicles with the cell surface in adipocytes. {ECO:0000250}.
Homo sapiens (Human)
O00187
MASP2_HUMAN
MRLLTLLGLLCGSVATPLGPKWPEPVFGRLASPGFPGEYANDQERRWTLTAPPGYRLRLYFTHFDLELSHLCEYDFVKLSSGAKVLATLCGQESTDTERAPGKDTFYSLGSSLDITFRSDYSNEKPFTGFEAFYAAEDIDECQVAPGEAPTCDHHCHNHLGGFYCSCRAGYVLHRNKRTCSALCSGQVFTQRSGELSSPEYPRPYPKLSSCTYSISLEEGFSVILDFVESFDVETHPETLCPYDFLKIQTDREEHGPFCGKTLPHRIETKSNTVTITFVTDESGDHTGWKIHYTSTAQPCPYPMAPPNGHVSPVQAKYIL...
3.4.21.104
null
complement activation, classical pathway [GO:0006958]; complement activation, lectin pathway [GO:0001867]; proteolysis [GO:0006508]
extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]
calcium ion binding [GO:0005509]; calcium-dependent protein binding [GO:0048306]; complement component C4b binding [GO:0001855]; identical protein binding [GO:0042802]; peptidase activity [GO:0008233]; serine-type endopeptidase activity [GO:0004252]
PF00431;PF07645;PF00084;PF00089;
2.10.70.10;2.10.25.10;2.60.120.290;2.40.10.10;
Peptidase S1 family
PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. {ECO:0000250}.; PTM: Activated by cleavage after Arg-444. The uncleaved zymogen is inactive towards synthetic substrates, but has sufficient activity to effect autocatalytic cleavage.
SUBCELLULAR LOCATION: Secreted.
CATALYTIC ACTIVITY: Reaction=Selective cleavage after Arg-223 in complement component C2 (-Ser-Leu-Gly-Arg-|-Lys-Ile-Gln-Ile) and after Arg-76 in complement component C4 (-Gly-Leu-Gln-Arg-|-Ala-Leu-Glu-Ile).; EC=3.4.21.104;
null
null
null
null
FUNCTION: Serum protease that plays an important role in the activation of the complement system via mannose-binding lectin. After activation by auto-catalytic cleavage it cleaves C2 and C4, leading to their activation and to the formation of C3 convertase. {ECO:0000269|PubMed:10946292}.
Homo sapiens (Human)
O00189
AP4M1_HUMAN
MISQFFILSSKGDPLIYKDFRGDSGGRDVAELFYRKLTGLPGDESPVVMHHHGRHFIHIRHSGLYLVVTTSENVSPFSLLELLSRLATLLGDYCGSLGEGTISRNVALVYELLDEVLDYGYVQTTSTEMLRNFIQTEAVVSKPFSLFDLSSVGLFGAETQQSKVAPSSAASRPVLSSRSDQSQKNEVFLDVVERLSVLIASNGSLLKVDVQGEIRLKSFLPSGSEMRIGLTEEFCVGKSELRGYGPGIRVDEVSFHSSVNLDEFESHRILRLQPPQGELTVMRYQLSDDLPSPLPFRLFPSVQWDRGSGRLQVYLKLRCD...
null
null
autophagosome assembly [GO:0000045]; Golgi to endosome transport [GO:0006895]; Golgi to lysosome transport [GO:0090160]; intracellular protein transport [GO:0006886]; post-Golgi vesicle-mediated transport [GO:0006892]; protein localization [GO:0008104]; protein localization to basolateral plasma membrane [GO:1903361]; ...
AP-4 adaptor complex [GO:0030124]; clathrin adaptor complex [GO:0030131]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; early endosome [GO:0005769]; endosome lumen [GO:0031904]; extracellular exosome [GO:0070062]; trans-Golgi network [GO:0005802]; trans-Golgi network membrane [GO:0032588]
protein domain specific binding [GO:0019904]; protein transmembrane transporter activity [GO:0008320]
PF00928;PF01217;
3.30.450.60;2.60.40.1170;
Adaptor complexes medium subunit family
null
SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:20230749, ECO:0000269|PubMed:29180427, ECO:0000269|PubMed:32073997}; Peripheral membrane protein {ECO:0000305|PubMed:32073997}. Early endosome {ECO:0000269|PubMed:20230749}. Note=Found in soma and dendritic shafts of neuronal cells....
null
null
null
null
null
FUNCTION: Component of the adaptor protein complex 4 (AP-4). Adaptor protein complexes are vesicle coat components involved both in vesicle formation and cargo selection. They control the vesicular transport of proteins in different trafficking pathways (PubMed:10066790, PubMed:10436028, PubMed:11139587, PubMed:1180216...
Homo sapiens (Human)
O00192
ARVC_HUMAN
MEDCNVHSAASILASVKEQEARFERLTRALEQERRHVALQLERAQQPGMVSGGMGSGQPLPMAWQQLVLQEQSPGSQASLATMPEAPDVLEETVTVEEDPGTPTSHVSIVTSEDGTTRRTETKVTKTVKTVTTRTVRQVPVGPDGLPLLDGGPPLGPFADGALDRHFLLRGGGPVATLSRAYLSSGGGFPEGPEPRDSPSYGSLSRGLGMRPPRAGPLGPGPGDGCFTLPGHREAFPVGPEPGPPGGRSLPERFQAEPYGLEDDTRSLAADDEGGPELEPDYGTATRRRPECGRGLHTRAYEDTADDGGELADERPAFPM...
null
null
cell adhesion [GO:0007155]; cell-cell adhesion [GO:0098609]; cell-cell junction assembly [GO:0007043]; mRNA processing [GO:0006397]; RNA splicing [GO:0008380]
adherens junction [GO:0005912]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
cadherin binding [GO:0045296]
PF00514;
1.25.10.10;
Beta-catenin family
null
SUBCELLULAR LOCATION: Cell junction, adherens junction {ECO:0000269|PubMed:10725230, ECO:0000269|PubMed:24644279, ECO:0000305|PubMed:30479852}. Nucleus {ECO:0000269|PubMed:10725230, ECO:0000269|PubMed:24644279}. Cytoplasm {ECO:0000269|PubMed:24644279}. Note=In heart, localizes at area composita, the mixed-type junction...
null
null
null
null
null
FUNCTION: Contributes to the regulation of alternative splicing of pre-mRNAs. {ECO:0000269|PubMed:24644279}.
Homo sapiens (Human)
O00194
RB27B_HUMAN
MTDGDYDYLIKLLALGDSGVGKTTFLYRYTDNKFNPKFITTVGIDFREKRVVYNAQGPNGSSGKAFKVHLQLWDTAGQERFRSLTTAFFRDAMGFLLMFDLTSQQSFLNVRNWMSQLQANAYCENPDIVLIGNKADLPDQREVNERQARELADKYGIPYFETSAATGQNVEKAVETLLDLIMKRMEQCVEKTQIPDTVNGGNSGNLDGEKPPEKKCIC
3.6.5.2
null
anterograde axonal protein transport [GO:0099641]; exocytosis [GO:0006887]; multivesicular body sorting pathway [GO:0071985]; positive regulation of exocytosis [GO:0045921]; synaptic vesicle endocytosis [GO:0048488]
apical plasma membrane [GO:0016324]; axon cytoplasm [GO:1904115]; exocytic vesicle [GO:0070382]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; Golgi stack [GO:0005795]; late endosome [GO:0005770]; melanosome [GO:0042470]; multivesicular body membrane [GO:0032585]; plasma membrane [GO:0005886]; plate...
G protein activity [GO:0003925]; GDP binding [GO:0019003]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; myosin V binding [GO:0031489]; protein domain specific binding [GO:0019904]
PF00071;
3.40.50.300;
Small GTPase superfamily, Rab family
null
SUBCELLULAR LOCATION: Membrane; Lipid-anchor. Late endosome {ECO:0000269|PubMed:30771381}.
CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence={ECO:0000305|PubMed:30771381}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000305|PubM...
null
null
null
null
FUNCTION: Small GTPase which cycles between active GTP-bound and inactive GDP-bound states. In its active state, binds to a variety of effector proteins to regulate homeostasis of late endocytic pathway, including endosomal positioning, maturation and secretion (PubMed:30771381). Plays a role in NTRK2/TRKB axonal anter...
Homo sapiens (Human)
O00198
HRK_HUMAN
MCPCPLHRGRGPPAVCACSAGRLGLRSSAAQLTAARLKALGDELHQRTMWRRRARSRRAPAPGALPTYWPWLCAAAQVAALAAWLLGRRNL
null
null
apoptotic process [GO:0006915]; positive regulation of apoptotic process [GO:0043065]; positive regulation of protein-containing complex assembly [GO:0031334]; positive regulation of release of cytochrome c from mitochondria [GO:0090200]
membrane [GO:0016020]; mitochondrion [GO:0005739]
null
PF15196;
null
null
null
SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. Mitochondrion.
null
null
null
null
null
FUNCTION: Promotes apoptosis. {ECO:0000269|PubMed:15031724, ECO:0000269|PubMed:9130713}.
Homo sapiens (Human)
O00203
AP3B1_HUMAN
MSSNSFPYNEQSGGGEATELGQEATSTISPSGAFGLFSSDLKKNEDLKQMLESNKDSAKLDAMKRIVGMIAKGKNASELFPAVVKNVASKNIEIKKLVYVYLVRYAEEQQDLALLSISTFQRALKDPNQLIRASALRVLSSIRVPIIVPIMMLAIKEASADLSPYVRKNAAHAIQKLYSLDPEQKEMLIEVIEKLLKDKSTLVAGSVVMAFEEVCPDRIDLIHKNYRKLCNLLVDVEEWGQVVIIHMLTRYARTQFVSPWKEGDELEDNGKNFYESDDDQKEKTDKKKKPYTMDPDHRLLIRNTKPLLQSRNAAVVMAVA...
null
null
anterograde axonal transport [GO:0008089]; anterograde synaptic vesicle transport [GO:0048490]; antigen processing and presentation, exogenous lipid antigen via MHC class Ib [GO:0048007]; blood coagulation [GO:0007596]; cell morphogenesis [GO:0000902]; clathrin-coated vesicle cargo loading, AP-3-mediated [GO:0035654]; ...
AP-3 adaptor complex [GO:0030123]; axon cytoplasm [GO:1904115]; clathrin adaptor complex [GO:0030131]; clathrin-coated vesicle membrane [GO:0030665]; early endosome [GO:0005769]; Golgi apparatus [GO:0005794]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; microvesicle [GO:1990742]; mitochondrion [GO:0005739]
GTP-dependent protein binding [GO:0030742]; protein phosphatase binding [GO:0019903]
PF01602;PF14796;PF14797;
1.25.10.10;
Adaptor complexes large subunit family
PTM: Phosphorylated on serine residues. {ECO:0000269|PubMed:9182526}.; PTM: Pyrophosphorylation by 5-diphosphoinositol pentakisphosphate (5-IP7) impairs interaction with KIF3A (PubMed:19934039). Serine pyrophosphorylation is achieved by Mg(2+)-dependent, but enzyme independent transfer of a beta-phosphate from a inosit...
SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000305|PubMed:9151686}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Golgi apparatus {ECO:0000305|PubMed:9151686}. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles located at the...
null
null
null
null
null
FUNCTION: Subunit of non-clathrin- and clathrin-associated adaptor protein complex 3 (AP-3) that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosoli...
Homo sapiens (Human)
O00204
ST2B1_HUMAN
MDGPAEPQIPGLWDTYEDDISEISQKLPGEYFRYKGVPFPVGLYSLESISLAENTQDVRDDDIFIITYPKSGTTWMIEIICLILKEGDPSWIRSVPIWERAPWCETIVGAFSLPDQYSPRLMSSHLPIQIFTKAFFSSKAKVIYMGRNPRDVVVSLYHYSKIAGQLKDPGTPDQFLRDFLKGEVQFGSWFDHIKGWLRMKGKDNFLFITYEELQQDLQGSVERICGFLGRPLGKEALGSVVAHSTFSAMKANTMSNYTLLPPSLLDHRRGAFLRKGVCGDWKNHFTVAQSEAFDRAYRKQMRGMPTFPWDEDPEEDGSPD...
2.8.2.2
null
3'-phosphoadenosine 5'-phosphosulfate metabolic process [GO:0050427]; cholesterol metabolic process [GO:0008203]; negative regulation of cell population proliferation [GO:0008285]; positive regulation of epidermal cell differentiation [GO:0045606]; steroid metabolic process [GO:0008202]; sulfation [GO:0051923]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; intracellular membrane-bounded organelle [GO:0043231]; nucleus [GO:0005634]
cholesterol binding [GO:0015485]; cholesterol sulfotransferase activity [GO:0051922]; nucleic acid binding [GO:0003676]; small molecule binding [GO:0036094]; steroid hormone binding [GO:1990239]; steroid sulfotransferase activity [GO:0050294]; sulfotransferase activity [GO:0008146]
PF00685;
3.40.50.300;
Sulfotransferase 1 family
PTM: Phosphorylated. {ECO:0000269|PubMed:16855051}.
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12923182, ECO:0000269|PubMed:16855051, ECO:0000269|PubMed:21855633, ECO:0000269|PubMed:28575648}. Microsome {ECO:0000269|PubMed:16855051, ECO:0000269|PubMed:21855633}. Nucleus {ECO:0000269|PubMed:16855051, ECO:0000269|PubMed:21855633}. Note=Phosphorylation of...
CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + an alcohol = adenosine 3',5'-bisphosphate + an alkyl sulfate + H(+); Xref=Rhea:RHEA:22552, ChEBI:CHEBI:15378, ChEBI:CHEBI:30879, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:83414; EC=2.8.2.2; Evidence={ECO:0000269|PubMed:12145317, ECO:0000269|PubMed:168550...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=23.5 uM for (24S)-hydroxycholesterol {ECO:0000269|PubMed:19589875}; KM=10.9 uM for DHEA (at 37 degrees Celsius, in the presence of 1 mM MgCl2) {ECO:0000269|PubMed:21855633}; KM=3.8 uM for DHEA (at 37 degrees Celsius, in the presence of 10 mM MgCl2) {ECO:0000269|Pub...
null
null
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. Retains 70% and 20% of activity when incubated at 42 degrees Celsius for 45 and 120 minutes, respectively. Activity is lost after 200 minutes incubation at 42 degrees Celsius. {ECO:0000269|PubMed:16855051, ECO:0000269|Pub...
FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation. Responsible for the sulfation of cholesterol (PubMed:12145317, PubMed:19589875). Catalyzes sulfation of the 3beta-hydroxyl groups of steroids, such as, pregnenolone and dehydroepiandros...
Homo sapiens (Human)
O00206
TLR4_HUMAN
MMSASRLAGTLIPAMAFLSCVRPESWEPCVEVVPNITYQCMELNFYKIPDNLPFSTKNLDLSFNPLRHLGSYSFFSFPELQVLDLSRCEIQTIEDGAYQSLSHLSTLILTGNPIQSLALGAFSGLSSLQKLVAVETNLASLENFPIGHLKTLKELNVAHNLIQSFKLPEYFSNLTNLEHLDLSSNKIQSIYCTDLRVLHQMPLLNLSLDLSLNPMNFIQPGAFKEIRLHKLTLRNNFDSLNVMKTCIQGLAGLEVHRLVLGEFRNEGNLEKFDKSALEGLCNLTIEEFRLAYLDYYLDDIIDLFNCLTNVSSFSLVSVTI...
null
null
astrocyte development [GO:0014002]; B cell proliferation involved in immune response [GO:0002322]; cellular response to amyloid-beta [GO:1904646]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to lipoteichoic acid [GO:0071223]; cellular response to mechanical stimulus [GO:0071260]; cellular re...
cell surface [GO:0009986]; cytoplasm [GO:0005737]; early endosome [GO:0005769]; endosome membrane [GO:0010008]; external side of plasma membrane [GO:0009897]; lipopolysaccharide receptor complex [GO:0046696]; perinuclear region of cytoplasm [GO:0048471]; phagocytic cup [GO:0001891]; plasma membrane [GO:0005886]; recept...
amyloid-beta binding [GO:0001540]; identical protein binding [GO:0042802]; lipopolysaccharide binding [GO:0001530]; lipopolysaccharide immune receptor activity [GO:0001875]; NAD+ nucleotidase, cyclic ADP-ribose generating [GO:0061809]; protein heterodimerization activity [GO:0046982]; signaling receptor activity [GO:00...
PF12799;PF13516;PF13855;PF01582;
3.80.10.10;3.40.50.10140;
Toll-like receptor family
PTM: N-glycosylated. Glycosylation of Asn-526 and Asn-575 seems to be necessary for the expression of TLR4 on the cell surface and the LPS-response. Likewise, mutants lacking two or more of the other N-glycosylation sites were deficient in interaction with LPS. {ECO:0000269|PubMed:11706042, ECO:0000269|PubMed:17803912,...
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11274165, ECO:0000269|PubMed:17098818, ECO:0000269|PubMed:20037584, ECO:0000269|PubMed:21393102, ECO:0000269|PubMed:27022195, ECO:0000269|PubMed:36232715, ECO:0000269|PubMed:36945827, ECO:0000269|PubMed:9237759}; Single-pass type I membrane protein {ECO:0000269|Pu...
null
null
null
null
null
FUNCTION: Transmembrane receptor that functions as a pattern recognition receptor recognizing pathogen- and damage-associated molecular patterns (PAMPs and DAMPs) to induce innate immune responses via downstream signaling pathways (PubMed:10835634, PubMed:15809303, PubMed:16622205, PubMed:17292937, PubMed:17478729, Pub...
Homo sapiens (Human)
O00212
RHOD_HUMAN
MTAAQAAGEEAPPGVRSVKVVLVGDGGCGKTSLLMVFADGAFPESYTPTVFERYMVNLQVKGKPVHLHIWDTAGQDDYDRLRPLFYPDASVLLLCFDVTSPNSFDNIFNRWYPEVNHFCKKVPIIVVGCKTDLRKDKSLVNKLRRNGLEPVTYHRGQEMARSVGAVAYLECSARLHDNVHAVFQEAAEVALSSRGRNFWRRITQGFCVVT
null
null
actin filament bundle assembly [GO:0051017]; actin filament organization [GO:0007015]; cell migration [GO:0016477]; focal adhesion assembly [GO:0048041]; lamellipodium assembly [GO:0030032]; positive regulation of cell adhesion [GO:0045785]; positive regulation of cell migration [GO:0030335]; regulation of actin cytosk...
cytosol [GO:0005829]; early endosome [GO:0005769]; endosome membrane [GO:0010008]; Golgi membrane [GO:0000139]; mitochondrial outer membrane [GO:0005741]; plasma membrane [GO:0005886]
GTP binding [GO:0005525]; GTPase activity [GO:0003924]; guanyl-nucleotide exchange factor activity [GO:0005085]; protein kinase binding [GO:0019901]
PF00071;
3.40.50.300;
Small GTPase superfamily, Rho family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Early endosome {ECO:0000269|PubMed:24102721}. Note=Colocalizes with RAB5 to early endosomes (By similarity). {ECO:0000250|UniProtKB:P97348}.
null
null
null
null
null
FUNCTION: Involved in endosome dynamics. May coordinate membrane transport with the function of the cytoskeleton. Involved in the internalization and trafficking of activated tyrosine kinase receptors such as PDGFRB. Participates in the reorganization of actin cytoskeleton; the function seems to involve WHAMM and inclu...
Homo sapiens (Human)
O00213
APBB1_HUMAN
MSVPSSLSQSAINANSHGGPALSLPLPLHAAHNQLLNAKLQATAVGPKDLRSAMGEGGGPEPGPANAKWLKEGQNQLRRAATAHRDQNRNVTLTLAEEASQEPEMAPLGPKGLIHLYSELELSAHNAANRGLRGPGLIISTQEQGPDEGEEKAAGEAEEEEEDDDDEEEEEDLSSPPGLPEPLESVEAPPRPQALTDGPREHSKSASLLFGMRNSAASDEDSSWATLSQGSPSYGSPEDTDSFWNPNAFETDSDLPAGWMRVQDTSGTYYWHIPTGTTQWEPPGRASPSQGSSPQEESQLTWTGFAHGEGFEDGEFWKDE...
null
null
apoptotic process [GO:0006915]; axonogenesis [GO:0007409]; chromatin organization [GO:0006325]; DNA damage response [GO:0006974]; negative regulation of cell cycle G1/S phase transition [GO:1902807]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of apoptotic process [GO:004...
cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; growth cone [GO:0030426]; lamellipodium [GO:0030027]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; synapse [GO:0045202]
amyloid-beta binding [GO:0001540]; chromatin binding [GO:0003682]; histone binding [GO:0042393]; low-density lipoprotein particle receptor binding [GO:0050750]; molecular adaptor activity [GO:0060090]; proline-rich region binding [GO:0070064]; transcription coactivator activity [GO:0003713]; ubiquitin protein ligase bi...
PF00640;PF00397;
2.20.70.10;2.30.29.30;
null
PTM: Phosphorylation at Ser-610 by SGK1 promotes its localization to the nucleus (By similarity). Phosphorylated following nuclear translocation (PubMed:15031292, PubMed:18922798). Phosphorylation at Tyr-547 by ABL1 enhances transcriptional activation activity and reduces the affinity for RASD1/DEXRAS1 (PubMed:15031292...
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18468999}. Cytoplasm {ECO:0000269|PubMed:18468999}. Nucleus {ECO:0000269|PubMed:15031292, ECO:0000269|PubMed:18468999, ECO:0000269|PubMed:18922798, ECO:0000269|PubMed:19343227}. Cell projection, growth cone {ECO:0000250|UniProtKB:P46933}. Nucleus speckle {ECO:0000...
null
null
null
null
null
FUNCTION: Transcription coregulator that can have both coactivator and corepressor functions (PubMed:15031292, PubMed:18468999, PubMed:18922798, PubMed:25342469, PubMed:33938178). Adapter protein that forms a transcriptionally active complex with the gamma-secretase-derived amyloid precursor protein (APP) intracellular...
Homo sapiens (Human)
O00214
LEG8_HUMAN
MMLSLNNLQNIIYNPVIPFVGTIPDQLDPGTLIVIRGHVPSDADRFQVDLQNGSSMKPRADVAFHFNPRFKRAGCIVCNTLINEKWGREEITYDTPFKREKSFEIVIMVLKDKFQVAVNGKHTLLYGHRIGPEKIDTLGIYGKVNIHSIGFSFSSDLQSTQASSLELTEISRENVPKSGTPQLRLPFAARLNTPMGPGRTVVVKGEVNANAKSFNVDLLAGKSKDIALHLNPRLNIKAFVRNSFLQESWGEEERNITSFPFSPGMYFEMIIYCDVREFKVAVNGVHSLEYKHRFKELSSIDTLEINGDIHLLEVRSW
null
null
cellular response to virus [GO:0098586]; lymphatic endothelial cell migration [GO:1904977]; xenophagy [GO:0098792]
cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; extracellular space [GO:0005615]; membrane [GO:0016020]
carbohydrate binding [GO:0030246]; integrin binding [GO:0005178]
PF00337;
2.60.120.200;
null
null
SUBCELLULAR LOCATION: Cytoplasmic vesicle {ECO:0000269|PubMed:22246324}. Cytoplasm, cytosol {ECO:0000269|PubMed:22246324}.
null
null
null
null
null
FUNCTION: Beta-galactoside-binding lectin that acts as a sensor of membrane damage caused by infection and restricts the proliferation of infecting pathogens by targeting them for autophagy (PubMed:22246324, PubMed:28077878). Detects membrane rupture by binding beta-galactoside ligands located on the lumenal side of th...
Homo sapiens (Human)
O00217
NDUS8_HUMAN
MRCLTTPMLLRALAQAARAGPPGGRSLHSSAVAATYKYVNMQDPEMDMKSVTDRAARTLLWTELFRGLGMTLSYLFREPATINYPFEKGPLSPRFRGEHALRRYPSGEERCIACKLCEAICPAQAITIEAEPRADGSRRTTRYDIDMTKCIYCGFCQEACPVDAIVEGPNFEFSTETHEELLYNKEKLLNNGDKWEAEIAANIQADYLYR
7.1.1.2
COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250|UniProtKB:Q56224}; Note=Binds 2 [4Fe-4S] cluster. {ECO:0000250|UniProtKB:Q56224};
aerobic respiration [GO:0009060]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; mitochondrial respiratory chain complex I assembly [GO:0032981]; proton motive force-driven mitochondrial ATP synthesis [GO:0042776]; response to oxidative stress [GO:0006979]
mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrial respiratory chain complex I [GO:0005747]; mitochondrion [GO:0005739]
4 iron, 4 sulfur cluster binding [GO:0051539]; metal ion binding [GO:0046872]; NADH dehydrogenase (ubiquinone) activity [GO:0008137]
PF12838;
3.30.70.3270;
Complex I 23 kDa subunit family
null
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305|PubMed:12611891, ECO:0000305|PubMed:9666055}; Peripheral membrane protein {ECO:0000250|UniProtKB:P42028}; Matrix side {ECO:0000250|UniProtKB:P42028}.
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:22499348};
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:22499348). Essential for the catalytic activity and assembly of complex I (PubMed:22499348). {...
Homo sapiens (Human)
O00219
HYAS3_HUMAN
MPVQLTTALRVVGTSLFALAVLGGILAAYVTGYQFIHTEKHYLSFGLYGAILGLHLLIQSLFAFLEHRRMRRAGQALKLPSPRRGSVALCIAAYQEDPDYLRKCLRSAQRISFPDLKVVMVVDGNRQEDAYMLDIFHEVLGGTEQAGFFVWRSNFHEAGEGETEASLQEGMDRVRDVVRASTFSCIMQKWGGKREVMYTAFKALGDSVDYIQVCDSDTVLDPACTIEMLRVLEEDPQVGGVGGDVQILNKYDSWISFLSSVRYWMAFNVERACQSYFGCVQCISGPLGMYRNSLLQQFLEDWYHQKFLGSKCSFGDDRHL...
2.4.1.212
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
carbohydrate metabolic process [GO:0005975]; extracellular matrix assembly [GO:0085029]; extracellular polysaccharide biosynthetic process [GO:0045226]; hyaluronan biosynthetic process [GO:0030213]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of hyaluranon cable assembly [GO:190...
early endosome [GO:0005769]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; hyaluranon cable [GO:0036117]; membrane [GO:0016020]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
hyaluronan synthase activity [GO:0050501]; identical protein binding [GO:0042802]
PF13641;
null
NodC/HAS family
PTM: O-GlcNAcylation increases the hyaluronan synthase activity, HAS3 stability and its plasma membrane residence. The concentration of UDP-GlcNAc controls the level of O-GlcNAc modification. {ECO:0000269|PubMed:26883802}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25795779, ECO:0000269|PubMed:26883802, ECO:0000269|PubMed:30394292}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:25795779}; Multi-pass membrane protein. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtK...
CATALYTIC ACTIVITY: Reaction=[hyaluronan](n) + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N-acetyl-beta-D-glucosaminyl-(1->4)-[hyaluronan](n) + UDP; Xref=Rhea:RHEA:20465, Rhea:RHEA-COMP:12583, Rhea:RHEA-COMP:12585, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:132153, ChEBI:CHEBI:132154; EC=2.4.1....
null
PATHWAY: Glycan biosynthesis; hyaluronan biosynthesis. {ECO:0000269|PubMed:23303191}.
null
null
FUNCTION: Catalyzes the addition of GlcNAc or GlcUA monosaccharides to the nascent hyaluronan polymer. Therefore, it is essential to hyaluronan synthesis a major component of most extracellular matrices that has a structural role in tissues architectures and regulates cell adhesion, migration and differentiation. This ...
Homo sapiens (Human)
O00220
TR10A_HUMAN
MAPPPARVHLGAFLAVTPNPGSAASGTEAAAATPSKVWGSSAGRIEPRGGGRGALPTSMGQHGPSARARAGRAPGPRPAREASPRLRVHKTFKFVVVGVLLQVVPSSAATIKLHDQSIGTQQWEHSPLGELCPPGSHRSEHPGACNRCTEGVGYTNASNNLFACLPCTACKSDEEERSPCTTTRNTACQCKPGTFRNDNSAEMCRKCSRGCPRGMVKVKDCTPWSDIECVHKESGNGHNIWVILVVTLVVPLLLVAVLIVCCCIGSGCGGDPKCMDRVCFWRLGLLRGPGAEDNAHNEILSNADSLSTFVSEQQMESQEP...
null
null
activation of NF-kappaB-inducing kinase activity [GO:0007250]; apoptotic process [GO:0006915]; cellular response to mechanical stimulus [GO:0071260]; extrinsic apoptotic signaling pathway [GO:0097191]; extrinsic apoptotic signaling pathway via death domain receptors [GO:0008625]; positive regulation of apoptotic proces...
cell surface [GO:0009986]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; membrane raft [GO:0045121]; plasma membrane [GO:0005886]
death receptor activity [GO:0005035]; identical protein binding [GO:0042802]; protease binding [GO:0002020]; signaling receptor activity [GO:0038023]; TRAIL binding [GO:0045569]
PF00531;PF00020;
1.10.533.10;2.10.50.10;
null
PTM: Palmitoylated (PubMed:19090789). Palmitoylation of TNFRSF10A is required for its association with lipid rafts, oligomerization and function in TRAIL-induced cell death (PubMed:19090789). Palmitoylated by ZDHHC3 (Probable). {ECO:0000269|PubMed:19090789, ECO:0000305|PubMed:22240897}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22240897}; Single-pass type I membrane protein {ECO:0000255}. Membrane raft {ECO:0000269|PubMed:19090789, ECO:0000269|PubMed:22240897}. Cytoplasm, cytosol {ECO:0000269|PubMed:22240897}. Note=Palmitoylation is required for association with membranes. {ECO:0000269|P...
null
null
null
null
null
FUNCTION: Receptor for the cytotoxic ligand TNFSF10/TRAIL (PubMed:26457518). The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cyst...
Homo sapiens (Human)
O00221
IKBE_HUMAN
MNQRRSESRPGNHRLQAYAEPGKGDSGGAGPLSGSARRGRGGGGAIRVRRPCWSGGAGRGGGPAWAVRLPTVTAGWTWPALRTLSSLRAGPSEPHSPGRRPPRAGRPLCQADPQPGKAARRSLEPDPAQTGPRPARAAGMSEARKGPDEAEESQYDSGIESLRSLRSLPESTSAPASGPSDGSPQPCTHPPGPVKEPQEKEDADGERADSTYGSSSLTYTLSLLGGPEAEDPAPRLPLPHVGALSPQQLEALTYISEDGDTLVHLAVIHEAPAVLLCCLALLPQEVLDIQNNLYQTALHLAVHLDQPGAVRALVLKGASR...
null
null
cellular response to tumor necrosis factor [GO:0071356]; cytoplasmic sequestering of transcription factor [GO:0042994]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; fibrillar center [GO:0001650]; nucleoplasm [GO:0005654]
NF-kappaB binding [GO:0051059]
PF12796;
1.25.40.20;
NF-kappa-B inhibitor family
PTM: Serine phosphorylated; followed by proteasome-dependent degradation.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
null
null
null
null
null
FUNCTION: Inhibits NF-kappa-B by complexing with and trapping it in the cytoplasm. Inhibits DNA-binding of NF-kappa-B p50-p65 and p50-c-Rel complexes. {ECO:0000269|PubMed:9315679}.
Homo sapiens (Human)
O00222
GRM8_HUMAN
MVCEGKRSASCPCFFLLTAKFYWILTMMQRTHSQEYAHSIRVDGDIILGGLFPVHAKGERGVPCGELKKEKGIHRLEAMLYAIDQINKDPDLLSNITLGVRILDTCSRDTYALEQSLTFVQALIEKDASDVKCANGDPPIFTKPDKISGVIGAAASSVSIMVANILRLFKIPQISYASTAPELSDNTRYDFFSRVVPPDSYQAQAMVDIVTALGWNYVSTLASEGNYGESGVEAFTQISREIGGVCIAQSQKIPREPRPGEFEKIIKRLLETPNARAVIMFANEDDIRRILEAAKKLNQSGHFLWIGSDSWGSKIAPVYQ...
null
null
adenylate cyclase-inhibiting G protein-coupled glutamate receptor signaling pathway [GO:0007196]; adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway [GO:0007193]; G protein-coupled glutamate receptor signaling pathway [GO:0007216]; regulation of synaptic transmission, glutamatergic [GO:0051966]; ...
plasma membrane [GO:0005886]
G protein-coupled receptor activity [GO:0004930]; glutamate receptor activity [GO:0008066]; group III metabotropic glutamate receptor activity [GO:0001642]
PF00003;PF01094;PF07562;
3.40.50.2300;2.10.50.30;
G-protein coupled receptor 3 family
null
SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
null
null
null
null
null
FUNCTION: G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity. {ECO:0000269|PubMed:...
Homo sapiens (Human)
O00231
PSD11_HUMAN
MAAAAVVEFQRAQSLLSTDREASIDILHSIVKRDIQENDEEAVQVKEQSILELGSLLAKTGQAAELGGLLKYVRPFLNSISKAKAARLVRSLLDLFLDMEAATGQEVELCLECIEWAKSEKRTFLRQALEARLVSLYFDTKRYQEALHLGSQLLRELKKMDDKALLVEVQLLESKTYHALSNLPKARAALTSARTTANAIYCPPKLQATLDMQSGIIHAAEEKDWKTAYSYFYEAFEGYDSIDSPKAITSLKYMLLCKIMLNTPEDVQALVSGKLALRYAGRQTEALKCVAQASKNRSLADFEKALTDYRAELRDDPIIS...
null
null
proteasome assembly [GO:0043248]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; stem cell differentiation [GO:0048863]; ubiquitin-dependent protein catabolic process [GO:0006511]
cytosol [GO:0005829]; extracellular region [GO:0005576]; ficolin-1-rich granule lumen [GO:1904813]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; proteasome accessory complex [GO:0022624]; proteasome complex [GO:0000502]; proteasome regulatory particle, lid subcomplex [GO:0008541]; secretory gr...
structural molecule activity [GO:0005198]
PF01399;PF18503;PF18055;
1.25.40.570;
Proteasome subunit S9 family
PTM: Phosphorylated by AMPK. {ECO:0000269|PubMed:19616115}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}.
null
null
null
null
null
FUNCTION: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose ...
Homo sapiens (Human)
O00232
PSD12_HUMAN
MADGGSERADGRIVKMEVDYSATVDQRLPECAKLAKEGRLQEVIETLLSLEKQTRTASDMVSTSRILVAVVKMCYEAKEWDLLNENIMLLSKRRSQLKQAVAKMVQQCCTYVEEITDLPIKLRLIDTLRMVTEGKIYVEIERARLTKTLATIKEQNGDVKEAASILQELQVETYGSMEKKERVEFILEQMRLCLAVKDYIRTQIISKKINTKFFQEENTEKLKLKYYNLMIQLDQHEGSYLSICKHYRAIYDTPCIQAESEKWQQALKSVVLYVILAPFDNEQSDLVHRISGDKKLEEIPKYKDLLKLFTTMELMRWSTL...
null
null
proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; ficolin-1-rich granule lumen [GO:1904813]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; proteasome accessory complex [GO:0022624]; proteasome complex [GO:0000502]; proteasome regulatory particle [GO:...
null
PF01399;PF18098;
1.10.10.10;
Proteasome subunit p55 family
null
null
null
null
null
null
null
FUNCTION: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose ...
Homo sapiens (Human)
O00233
PSMD9_HUMAN
MSDEEARQSGGSSQAGVVTVSDVQELMRRKEEIEAQIKANYDVLESQKGIGMNEPLVDCEGYPRSDVDLYQVRTARHNIICLQNDHKAVMKQVEEALHQLHARDKEKQARDMAEAHKEAMSRKLGQSESQGPPRAFAKVNSISPGSPASIAGLQVDDEIVEFGSVNTQNFQSLHNIGSVVQHSEGKPLNVTVIRRGEKHQLRLVPTRWAGKGLLGCNIIPLQR
null
null
negative regulation of insulin secretion [GO:0046676]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of insulin secretion [GO:0032024]; proteasome regulatory particle assembly [GO:0070682]; ubiquitin-dependent protein catabolic process [GO:0006511]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; proteasome regulatory particle [GO:0005838]
bHLH transcription factor binding [GO:0043425]; transcription coactivator activity [GO:0003713]
PF18265;PF17820;
2.30.42.10;6.10.140.1710;
Proteasome subunit p27 family
null
null
null
null
null
null
null
FUNCTION: Acts as a chaperone during the assembly of the 26S proteasome, specifically of the base subcomplex of the PA700/19S regulatory complex (RC). During the base subcomplex assembly is part of an intermediate PSMD9:PSMC6:PSMC3 module, also known as modulator trimer complex; PSMD9 is released during the further bas...
Homo sapiens (Human)
O00237
RN103_HUMAN
MWLKLFFLLLYFLVLFVLARFFEAIVWYETGIFATQLVDPVALSFKKLKTILECRGLGYSGLPEKKDVRELVEKSGDLMEGELYSALKEEEASESVSSTNFSGEMHFYELVEDTKDGIWLVQVIANDRSPLVGKIHWEKMVKKVSRFGIRTGTFNCSSDPRYCRRRGWVRSTLIMSVPQTSTSKGKVMLKEYSGRKIEVEHIFKWITAHAASRIKTIYNAEHLKEEWNKSDQYWLKIYLFANLDQPPAFFSALSIKFTGRVEFIFVNVENWDNKSYMTDIGIYNMPSYILRTPEGIYRYGNHTGEFISLQAMDSFLRSLQ...
2.3.2.27
null
central nervous system development [GO:0007417]; ERAD pathway [GO:0036503]; protein ubiquitination [GO:0016567]
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]
metal ion binding [GO:0046872]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]
PF13639;
3.30.40.10;
null
null
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18675248}; Multi-pass membrane protein {ECO:0000269|PubMed:18675248}.
CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27;
null
PATHWAY: Protein modification; protein ubiquitination.
null
null
FUNCTION: Acts as an E2-dependent E3 ubiquitin-protein ligase, probably involved in the ER-associated protein degradation pathway. {ECO:0000269|PubMed:10500182, ECO:0000269|PubMed:18675248}.
Homo sapiens (Human)
O00238
BMR1B_HUMAN
MLLRSAGKLNVGTKKEDGESTAPTPRPKVLRCKCHHHCPEDSVNNICSTDGYCFTMIEEDDSGLPVVTSGCLGLEGSDFQCRDTPIPHQRRSIECCTERNECNKDLHPTLPPLKNRDFVDGPIHHRALLISVTVCSLLLVLIILFCYFRYKRQETRPRYSIGLEQDETYIPPGESLRDLIEQSQSSGSGSGLPLLVQRTIAKQIQMVKQIGKGRYGEVWMGKWRGEKVAVKVFFTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTGSWTQLYLITDYHENGSLYDYLKSTTLDAKSMLKLAYSSVSGLCHLHTEIF...
2.7.11.30
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
BMP signaling pathway [GO:0030509]; cartilage condensation [GO:0001502]; cellular response to BMP stimulus [GO:0071773]; cellular response to growth factor stimulus [GO:0071363]; central nervous system neuron differentiation [GO:0021953]; chondrocyte development [GO:0002063]; dorsal/ventral pattern formation [GO:000995...
dendrite [GO:0030425]; HFE-transferrin receptor complex [GO:1990712]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]
ATP binding [GO:0005524]; BMP binding [GO:0036122]; BMP receptor activity [GO:0098821]; metal ion binding [GO:0046872]; protein serine/threonine kinase activity [GO:0004674]; SMAD binding [GO:0046332]; transforming growth factor beta receptor activity, type I [GO:0005025]; transmembrane receptor protein serine/threonin...
PF01064;PF07714;PF08515;
2.10.60.10;1.10.510.10;
Protein kinase superfamily, TKL Ser/Thr protein kinase family, TGFB receptor subfamily
PTM: Autophosphorylated. {ECO:0000250|UniProtKB:P36898}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P36898}; Single-pass type I membrane protein {ECO:0000255}.
CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[receptor-protein] = ADP + H(+) + O-phospho-L-threonyl-[receptor-protein]; Xref=Rhea:RHEA:44880, Rhea:RHEA-COMP:11024, Rhea:RHEA-COMP:11025, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.30; Evidence={ECO:0000250|U...
null
null
null
null
FUNCTION: On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for BMP7/OP-1 and GDF5. Positivel...
Homo sapiens (Human)
O00241
SIRB1_HUMAN
MPVPASWPHLPSPFLLMTLLLGRLTGVAGEDELQVIQPEKSVSVAAGESATLRCAMTSLIPVGPIMWFRGAGAGRELIYNQKEGHFPRVTTVSELTKRNNLDFSISISNITPADAGTYYCVKFRKGSPDDVEFKSGAGTELSVRAKPSAPVVSGPAVRATPEHTVSFTCESHGFSPRDITLKWFKNGNELSDFQTNVDPAGDSVSYSIHSTARVVLTRGDVHSQVICEIAHITLQGDPLRGTANLSEAIRVPPTLEVTQQPMRAENQANVTCQVSNFYPRGLQLTWLENGNVSRTETASTLIENKDGTYNWMSWLLVNTC...
null
null
cell surface receptor signaling pathway [GO:0007166]; positive regulation of phagocytosis [GO:0050766]; positive regulation of T cell activation [GO:0050870]; signal transduction [GO:0007165]
cell surface [GO:0009986]; plasma membrane [GO:0005886]; secretory granule membrane [GO:0030667]
null
PF07654;PF07686;
2.60.40.10;
null
PTM: N-glycosylated. {ECO:0000269|PubMed:10604985, ECO:0000269|PubMed:16335952}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10604985}; Single-pass type I membrane protein {ECO:0000255}.
null
null
null
null
null
FUNCTION: Immunoglobulin-like cell surface receptor involved in the negative regulation of receptor tyrosine kinase-coupled signaling processes. Participates also in the recruitment of tyrosine kinase SYK. Triggers activation of myeloid cells when associated with TYROBP (PubMed:10604985). {ECO:0000269|PubMed:10604985}.
Homo sapiens (Human)
O00244
ATOX1_HUMAN
MPKHEFSVDMTCGGCAEAVSRVLNKLGGVKYDIDLPNKKVCIESEHSMDTLLATLKKTGKTVSYLGLE
null
null
copper ion transport [GO:0006825]; intracellular copper ion homeostasis [GO:0006878]; response to oxidative stress [GO:0006979]
cytosol [GO:0005829]
copper chaperone activity [GO:0016531]; copper ion binding [GO:0005507]; copper-dependent protein binding [GO:0032767]; cuprous ion binding [GO:1903136]; metallochaperone activity [GO:0016530]
PF00403;
3.30.70.100;
ATX1 family
null
null
null
null
null
null
null
FUNCTION: Binds and deliver cytosolic copper to the copper ATPase proteins. May be important in cellular antioxidant defense.
Homo sapiens (Human)
O00253
AGRP_HUMAN
MLTAAVLSCALLLALPATRGAQMGLAPMEGIRRPDQALLPELPGLGLRAPLKKTTAEQAEEDLLQEAQALAEVLDLQDREPRSSRRCVRLHESCLGQQVPCCDPCATCYCRFFNAFCYCRKLGTAMNPCSRT
null
null
adult feeding behavior [GO:0008343]; circadian rhythm [GO:0007623]; eating behavior [GO:0042755]; feeding behavior [GO:0007631]; hormone-mediated signaling pathway [GO:0009755]; long-day photoperiodism [GO:0048571]; maternal process involved in female pregnancy [GO:0060135]; neuropeptide signaling pathway [GO:0007218];...
extracellular space [GO:0005615]; Golgi lumen [GO:0005796]; neuronal cell body [GO:0043025]
neuropeptide hormone activity [GO:0005184]; signaling receptor binding [GO:0005102]; type 1 melanocortin receptor binding [GO:0070996]
PF05039;
4.10.760.10;
null
null
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15927146}. Golgi apparatus lumen {ECO:0000269|PubMed:15927146}.
null
null
null
null
null
FUNCTION: Plays a role in weight homeostasis. Involved in the control of feeding behavior through the central melanocortin system. Acts as alpha melanocyte-stimulating hormone antagonist by inhibiting cAMP production mediated by stimulation of melanocortin receptors within the hypothalamus and adrenal gland. Has very l...
Homo sapiens (Human)
O00254
PAR3_HUMAN
MKALIFAAAGLLLLLPTFCQSGMENDTNNLAKPTLPIKTFRGAPPNSFEEFPFSALEGWTGATITVKIKCPEESASHLHVKNATMGYLTSSLSTKLIPAIYLLVFVVGVPANAVTLWMLFFRTRSICTTVFYTNLAIADFLFCVTLPFKIAYHLNGNNWVFGEVLCRATTVIFYGNMYCSILLLACISINRYLAIVHPFTYRGLPKHTYALVTCGLVWATVFLYMLPFFILKQEYYLVQPDITTCHDVHNTCESSSPFQLYYFISLAFFGFLIPFVLIIYCYAAIIRTLNAYDHRWLWYVKASLLILVIFTICFAPSNII...
null
null
blood coagulation [GO:0007596]; ligand-gated ion channel signaling pathway [GO:1990806]; platelet activation [GO:0030168]; positive regulation of insulin secretion [GO:0032024]; positive regulation of Rho protein signal transduction [GO:0035025]; response to wounding [GO:0009611]
apical plasma membrane [GO:0016324]; extracellular region [GO:0005576]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]
G protein-coupled receptor activity [GO:0004930]; phosphatidylinositol phospholipase C activity [GO:0004435]; receptor ligand activity [GO:0048018]; thrombin-activated receptor activity [GO:0015057]
PF00001;
1.20.1070.10;
G-protein coupled receptor 1 family
PTM: A proteolytic cleavage generates a new N-terminus that functions as a tethered ligand.
SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
null
null
null
null
null
FUNCTION: Receptor for activated thrombin coupled to G proteins that stimulate phosphoinositide hydrolysis. {ECO:0000269|PubMed:10079109}.
Homo sapiens (Human)
O00255
MEN1_HUMAN
MGLKAAQKTLFPLRSIDDVVRLFAAELGREEPDLVLLSLVLGFVEHFLAVNRVIPTNVPELTFQPSPAPDPPGGLTYFPVADLSIIAALYARFTAQIRGAVDLSLYPREGGVSSRELVKKVSDVIWNSLSRSYFKDRAHIQSLFSFITGTKLDSSGVAFAVVGACQALGLRDVHLALSEDHAWVVFGPNGEQTAEVTWHGKGNEDRRGQTVNAGVAERSWLYLKGSYMRCDRKMEVAFMVCAINPSIDLHTDSLELLQLQQKLLWLLYDLGHLERYPMALGNLADLEELEPTPGRPDPLTLYHKGIASAKTYYRDEHIYP...
null
null
DNA damage response [GO:0006974]; DNA repair [GO:0006281]; MAPK cascade [GO:0000165]; negative regulation of cell cycle [GO:0045786]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of cyclin-dependent protein serine/threonine kinase activity [GO:0045736]; negative regulation of D...
chromatin [GO:0000785]; chromosome, telomeric region [GO:0000781]; cleavage furrow [GO:0032154]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum lumen [GO:0005788]; histone methyltransferase complex [GO:0035097]; MLL1 complex [GO:0071339]; MLL1/2 complex [GO:0044665]; nuclear matrix [GO:0016363]; nu...
chromatin binding [GO:0003682]; double-stranded DNA binding [GO:0003690]; four-way junction DNA binding [GO:0000400]; phosphoprotein binding [GO:0051219]; protein-macromolecule adaptor activity [GO:0030674]; R-SMAD binding [GO:0070412]; transcription cis-regulatory region binding [GO:0000976]; Y-form DNA binding [GO:00...
PF05053;
null
null
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12874027}. Note=Concentrated in nuclear body-like structures. Relocates to the nuclear matrix upon gamma irradiation.
null
null
null
null
null
FUNCTION: Essential component of a MLL/SET1 histone methyltransferase (HMT) complex, a complex that specifically methylates 'Lys-4' of histone H3 (H3K4). Functions as a transcriptional regulator. Binds to the TERT promoter and represses telomerase expression. Plays a role in TGFB1-mediated inhibition of cell-proliferat...
Homo sapiens (Human)
O00257
CBX4_HUMAN
MELPAVGEHVFAVESIEKKRIRKGRVEYLVKWRGWSPKYNTWEPEENILDPRLLIAFQNRERQEQLMGYRKRGPKPKPLVVQVPTFARRSNVLTGLQDSSTDNRAKLDLGAQGKGQGHQYELNSKKHHQYQPHSKERAGKPPPPGKSGKYYYQLNSKKHHPYQPDPKMYDLQYQGGHKEAPSPTCPDLGAKSHPPDKWAQGAGAKGYLGAVKPLAGAAGAPGKGSEKGPPNGMMPAPKEAVTGNGIGGKMKIVKNKNKNGRIVIVMSKYMENGMQAVKIKSGEVAEGEARSPSHKKRAADERHPPADRTFKKAAGAEEKK...
2.3.2.-
null
chromatin organization [GO:0006325]; negative regulation of apoptotic process [GO:0043066]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of transcription by RNA polymerase II [GO:0000122]; protein sumoylation [GO:0016925]
nuclear body [GO:0016604]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PcG protein complex [GO:0031519]; PRC1 complex [GO:0035102]
chromatin binding [GO:0003682]; enzyme binding [GO:0019899]; methylated histone binding [GO:0035064]; phosphoprotein binding [GO:0051219]; single-stranded RNA binding [GO:0003727]; SUMO binding [GO:0032183]; SUMO ligase activity [GO:0061665]; SUMO transferase activity [GO:0019789]; transcription cis-regulatory region b...
PF17218;PF00385;
2.40.50.40;
null
PTM: Ubiquitinated. Ubiquitination regulates the function of the Polycomb group (PcG) multiprotein PRC1-like complex. Deubiquitinated by USP26. {ECO:0000269|PubMed:28839133}.; PTM: Phosphorylated on Thr-497 by HIPK2 upon DNA damage. This phosphorylation stimulates E3 SUMO-protein ligase activity and promotes sumoylatio...
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12679040, ECO:0000269|PubMed:17018294, ECO:0000269|PubMed:18927235, ECO:0000269|PubMed:21282530}. Nucleus speckle {ECO:0000269|PubMed:19266028}. Note=Localization to nuclear polycomb bodies is required for ZNF131 sumoylation (PubMed:22467880). Localized in distinct foci...
null
null
PATHWAY: Protein modification; protein sumoylation.
null
null
FUNCTION: E3 SUMO-protein ligase which facilitates SUMO1 conjugation by UBE2I (PubMed:12679040). Involved in the sumoylation of HNRNPK, a p53/TP53 transcriptional coactivator, hence indirectly regulates p53/TP53 transcriptional activation resulting in p21/CDKN1A expression. Monosumoylates ZNF131 (PubMed:22825850). {ECO...
Homo sapiens (Human)
O00258
GET1_HUMAN
MSSAAADHWAWLLVLSFVFGCNVLRILLPSFSSFMSRVLQKDAEQESQMRAEIQDMKQELSTVNMMDEFARYARLERKINKMTDKLKTHVKARTAQLAKIKWVISVAFYVLQAALMISLIWKYYSVPVAVVPSKWITPLDRLVAFPTRVAGGVGITCWILVCNKVVAIVLHPFS
null
null
protein insertion into ER membrane [GO:0045048]; protein stabilization [GO:0050821]; tail-anchored membrane protein insertion into ER membrane [GO:0071816]
endoplasmic reticulum membrane [GO:0005789]; GET complex [GO:0043529]; nucleus [GO:0005634]
protein-membrane adaptor activity [GO:0043495]
PF04420;
1.10.287.660;
WRB/GET1 family
null
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21444755}; Multi-pass membrane protein {ECO:0000255}.
null
null
null
null
null
FUNCTION: Required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum (ER) (PubMed:21444755, PubMed:23041287, PubMed:24392163, PubMed:27226539). Together with CAMLG/GET2, acts as a membrane receptor for soluble GET3/TRC40, which recognizes and selectively binds the transmemb...
Homo sapiens (Human)
O00264
PGRC1_HUMAN
MAAEDVVATGADPSDLESGGLLHEIFTSPLNLLLLGLCIFLLYKIVRGDQPAASGDSDDDEPPPLPRLKRRDFTPAELRRFDGVQDPRILMAINGKVFDVTKGRKFYGPEGPYGVFAGRDASRGLATFCLDKEALKDEYDDLSDLTAAQQETLSDWESQFTFKYHHVGKLLKEGEEPTVYSDEEEPKDESARKND
null
null
heme biosynthetic process [GO:0006783]; positive regulation of lipoprotein transport [GO:0140077]; positive regulation of protein localization to plasma membrane [GO:1903078]
cell body [GO:0044297]; endomembrane system [GO:0012505]; endoplasmic reticulum [GO:0005783]; extracellular region [GO:0005576]; membrane [GO:0016020]; mitochondrial outer membrane [GO:0005741]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; smooth endoplasmic reticulum m...
amyloid-beta binding [GO:0001540]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; steroid binding [GO:0005496]
PF00173;
3.10.120.10;
Cytochrome b5 family, MAPR subfamily
PTM: O-glycosylated; contains chondroitin sulfate attached to Ser-54. Ser-54 is in the cytoplasmic domain but the glycosylated form was detected in urine, suggesting that the membrane-bound form is cleaved, allowing for production of a secreted form which is glycosylated. {ECO:0000269|PubMed:36213313, ECO:0000269|PubMe...
SUBCELLULAR LOCATION: Microsome membrane {ECO:0000250|UniProtKB:Q95250}; Single-pass membrane protein {ECO:0000255}. Smooth endoplasmic reticulum membrane {ECO:0000303|PubMed:28396637}; Single-pass membrane protein {ECO:0000255}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:O55022}; Single-pass membrane protein ...
null
null
null
null
null
FUNCTION: Component of a progesterone-binding protein complex (PubMed:28396637). Binds progesterone (PubMed:25675345). Has many reported cellular functions (heme homeostasis, interaction with CYPs). Required for the maintenance of uterine histoarchitecture and normal female reproductive lifespan (By similarity). Intrac...
Homo sapiens (Human)
O00267
SPT5H_HUMAN
MSDSEDSNFSEEEDSERSSDGEEAEVDEERRSAAGSEKEEEPEDEEEEEEEEEYDEEEEEEDDDRPPKKPRHGGFILDEADVDDEYEDEDQWEDGAEDILEKEEIEASNIDNVVLDEDRSGARRLQNLWRDQREEELGEYYMKKYAKSSVGETVYGGSDELSDDITQQQLLPGVKDPNLWTVKCKIGEERATAISLMRKFIAYQFTDTPLQIKSVVAPEHVKGYIYVEAYKQTHVKQAIEGVGNLRLGYWNQQMVPIKEMTDVLKVVKEVANLKPKSWVRLKRGIYKDDIAQVDYVEPSQNTISLKMIPRIDYDRIKARM...
null
null
negative regulation of DNA-templated transcription, elongation [GO:0032785]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of DNA-templated transcription, elongation [GO:0032786]; positive regulation of macroautophagy [GO:0016239]; positive regulation of transcription by RN...
DSIF complex [GO:0032044]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
chromatin binding [GO:0003682]; enzyme binding [GO:0019899]; mRNA binding [GO:0003729]; protein heterodimerization activity [GO:0046982]; RNA binding [GO:0003723]
PF00467;PF03439;PF11942;
2.30.30.30;3.30.70.940;
SPT5 family
PTM: Methylated by PRMT1/HRMT1L2 and PRMT5/SKB1. Methylation negatively regulates interaction with P-TEFb and RNA polymerase II. {ECO:0000269|PubMed:12718890}.; PTM: Phosphorylated by CDK7 and CDK9. Phosphorylation by P-TEFb alleviates transcriptional pausing and can stimulate transcriptional elongation from the HIV-1 ...
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10075709}.
null
null
null
null
null
FUNCTION: Component of the DRB sensitivity-inducing factor complex (DSIF complex), which regulates mRNA processing and transcription elongation by RNA polymerase II. DSIF positively regulates mRNA capping by stimulating the mRNA guanylyltransferase activity of RNGTT/CAP1A. DSIF also acts cooperatively with the negative...
Homo sapiens (Human)
O00268
TAF4_HUMAN
MAAGSDLLDEVFFNSEVDEKVVSDLVGSLESQLAASAAHHHHLAPRTPEVRAAAAGALGNHVVSGSPAGAAGAGPAAPAEGAPGAAPEPPPAGRARPGGGGPQRPGPPSPRRPLVPAGPAPPAAKLRPPPEGSAGSCAPVPAAAAVAAGPEPAPAGPAKPAGPAALAARAGPGPGPGPGPGPGPGPGKPAGPGAAQTLNGSAALLNSHHAAAPAVSLVNNGPAALLPLPKPAAPGTVIQTPPFVGAAAPPAPAAPSPPAAPAPAAPAAAPPPPPPAPATLARPPGHPAGPPTAAPAVPPPAAAQNGGSAGAAPAPAPAAG...
null
null
DNA-templated transcription initiation [GO:0006352]; mRNA transcription by RNA polymerase II [GO:0042789]; ovarian follicle development [GO:0001541]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of transcription initiation by RNA polymerase II [GO:0060261]; regulation of DNA repa...
chromatin [GO:0000785]; cytosol [GO:0005829]; male germ cell nucleus [GO:0001673]; MLL1 complex [GO:0071339]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; transcription factor TFIID complex [GO:0005669]; transcription factor TFTC complex [GO:0033276]
aryl hydrocarbon receptor binding [GO:0017162]; DNA binding [GO:0003677]; protein heterodimerization activity [GO:0046982]; RNA polymerase II general transcription initiation factor activity [GO:0016251]
PF05236;PF07531;
1.10.20.10;1.20.120.1110;
TAF4 family
null
SUBCELLULAR LOCATION: Nucleus.
null
null
null
null
null
FUNCTION: The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription (PubMed:33795473). TFIID recognizes and binds promoters with or without a TATA box via its subunit TBP, a TATA-box-binding protein, and promotes assembly of the pre-initiatio...
Homo sapiens (Human)
O00270
GPR31_HUMAN
MPFPNCSAPSTVVATAVGVLLGLECGLGLLGNAVALWTFLFRVRVWKPYAVYLLNLALADLLLAACLPFLAAFYLSLQAWHLGRVGCWALHFLLDLSRSVGMAFLAAVALDRYLRVVHPRLKVNLLSPQAALGVSGLVWLLMVALTCPGLLISEAAQNSTRCHSFYSRADGSFSIIWQEALSCLQFVLPFGLIVFCNAGIIRALQKRLREPEKQPKLQRAQALVTLVVVLFALCFLPCFLARVLMHIFQNLGSCRALCAVAHTSDVTGSLTYLHSVLNPVVYCFSSPTFRSSYRRVFHTLRGKGQAAEPPDFNPRDSYS
null
null
G protein-coupled receptor signaling pathway [GO:0007186]; lipid metabolic process [GO:0006629]; negative regulation of inflammatory response [GO:0050728]; positive regulation of immune response [GO:0050778]; response to acidic pH [GO:0010447]; response to ischemia [GO:0002931]; response to molecule of bacterial origin...
plasma membrane [GO:0005886]
arachidonic acid binding [GO:0050544]; bioactive lipid receptor activity [GO:0045125]; G protein-coupled receptor activity [GO:0004930]
PF00001;
1.20.1070.10;
G-protein coupled receptor 1 family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21712392, ECO:0000269|PubMed:28619714, ECO:0000269|PubMed:31119277}; Multi-pass membrane protein {ECO:0000255}.
null
null
null
null
null
FUNCTION: High-affinity receptor for 12-(S)-hydroxy-5,8,10,14-eicosatetraenoic acid (12-S-HETE), with much lower affinities for other HETE isomers (PubMed:21712392, PubMed:29227475). 12-S-HETE is a eicosanoid, a 12-lipoxygenase (ALOX12) metabolite of arachidonic acid, involved in many physiologic and pathologic process...
Homo sapiens (Human)
O00273
DFFA_HUMAN
MEVTGDAGVPESGEIRTLKPCLLRRNYSREQHGVAASCLEDLRSKACDILAIDKSLTPVTLVLAEDGTIVDDDDYFLCLPSNTKFVALASNEKWAYNNSDGGTAWISQESFDVDETDSGAGLKWKNVARQLKEDLSSIILLSEEDLQMLVDAPCSDLAQELRQSCATVQRLQHTLQQVLDQREEVRQSKQLLQLYLQALEKEGSLLSKQEESKAAFGEEVDAVDTGISRETSSDVALASHILTALREKQAPELSLSSQDLELVTKEDPKALAVALNWDIKKTETVQEACERELALRLQQTQSLHSLRSISASKASPPGDL...
null
null
apoptotic DNA fragmentation [GO:0006309]; chaperone-mediated protein folding [GO:0061077]; negative regulation of apoptotic DNA fragmentation [GO:1902511]; negative regulation of deoxyribonuclease activity [GO:0032076]; negative regulation of execution phase of apoptosis [GO:1900118]; positive regulation of apoptotic p...
chromatin [GO:0000785]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]
deoxyribonuclease inhibitor activity [GO:0060703]; protein domain specific binding [GO:0019904]; protein folding chaperone [GO:0044183]
PF02017;PF09033;
3.10.20.10;1.10.1490.10;
null
PTM: Caspase-3 cleaves DFF45 at 2 sites to generate an active factor.
SUBCELLULAR LOCATION: Cytoplasm.
null
null
null
null
null
FUNCTION: Inhibitor of the caspase-activated DNase (DFF40).
Homo sapiens (Human)
O00287
RFXAP_HUMAN
MEAQGVAEGAGPGAASGVPHPAALAPAAAPTLAPASVAAAASQFTLLVMQPCAGQDEAAAPGGSVGAGKPVRYLCEGAGDGEEEAGEDEADLLDTSDPPGGGESAASLEDLEDEETHSGGEGSSGGARRRGSGGGSMSKTCTYEGCSETTSQVAKQRKPWMCKKHRNKMYKDKYKKKKSDQALNCGGTASTGSAGNVKLEESADNILSIVKQRTGSFGDRPARPTLLEQVLNQKRLSLLRSPEVVQFLQKQQQLLNQQVLEQRQQQFPGTSM
null
null
positive regulation of MHC class II biosynthetic process [GO:0045348]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]
nuclear speck [GO:0016607]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575]
DNA binding [GO:0003677]
PF15289;
6.10.290.30;
null
PTM: Phosphorylated.
SUBCELLULAR LOCATION: Nucleus.
null
null
null
null
null
FUNCTION: Part of the RFX complex that binds to the X-box of MHC II promoters.
Homo sapiens (Human)
O00291
HIP1_HUMAN
MDRMASSMKQVPNPLPKVLSRRGVGAGLEAAERESFERTQTVSINKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVLKDSLRYRNELSDMSRMWGHLSEGYGQLCSIYLKLLRTKMEYHTKNPRFPGNLQMSDRQLDEAGESDVNNFFQLTVEMFDYLECELNLFQTVFNSLDMSRSVSVTAAGQCRLAPLIQVILDCSHLYDYTVKLLFKLHSCLPADTLQGHRDRFMEQFTKLKDLFYRSSNLQYFKRLIQIPQLPENPPNFLRASALSEHISPVVVIPAEASS...
null
null
actin filament organization [GO:0007015]; activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; apoptotic process [GO:0006915]; apoptotic signaling pathway [GO:0097190]; cell differentiation [GO:0030154]; clathrin coat assembly [GO:0048268]; endocytosis [GO:0006897]; neurotransm...
clathrin-coated vesicle [GO:0030136]; clathrin-coated vesicle membrane [GO:0030665]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; glutamatergic synapse [GO:0098978]; Golgi apparatus [GO:0005794]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; nucleus [GO:000563...
actin filament binding [GO:0051015]; AP-2 adaptor complex binding [GO:0035612]; clathrin adaptor activity [GO:0035615]; clathrin binding [GO:0030276]; clathrin light chain binding [GO:0032051]; epidermal growth factor receptor binding [GO:0005154]; glutamate receptor binding [GO:0035254]; phosphatidylinositol binding [...
PF07651;PF16515;PF01608;
1.20.5.1700;1.25.40.90;6.10.250.920;1.20.1410.10;
SLA2 family
null
SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Endomembrane system. Cytoplasmic vesicle, clathrin-coated vesicle membrane. Note=Shuttles between cytoplasm and nucleus. Nuclear translocation can be induced by AR.
null
null
null
null
null
FUNCTION: Plays a role in clathrin-mediated endocytosis and trafficking (PubMed:11532990, PubMed:11577110, PubMed:11889126). Involved in regulating AMPA receptor trafficking in the central nervous system in an NMDA-dependent manner (By similarity). Regulates presynaptic nerve terminal activity (By similarity). Enhances...
Homo sapiens (Human)
O00292
LFTY2_HUMAN
MWPLWLCWALWVLPLAGPGAALTEEQLLGSLLRQLQLSEVPVLDRADMEKLVIPAHVRAQYVVLLRRSHGDRSRGKRFSQSFREVAGRFLASEASTHLLVFGMEQRLPPNSELVQAVLRLFQEPVPKAALHRHGRLSPRSAQARVTVEWLRVRDDGSNRTSLIDSRLVSVHESGWKAFDVTEAVNFWQQLSRPRQPLLLQVSVQREHLGPLASGAHKLVRFASQGAPAGLGEPQLELHTLDLRDYGAQGDCDPEAPMTEGTRCCRQEMYIDLQGMKWAKNWVLEPPGFLAYECVGTCQQPPEALAFNWPFLGPRQCIASE...
null
null
anterior/posterior axis specification [GO:0009948]
collagen-containing extracellular matrix [GO:0062023]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; platelet alpha granule lumen [GO:0031093]
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 (L-R) asymmetry determination of organ systems in mammals. May play a role in endometrial bleeding.
Homo sapiens (Human)
O00294
TULP1_HUMAN
MPLRDETLREVWASDSGHEEESLSPEAPRRPKQRPAPAQRLRKKRTEAPESPCPTGSKPRKPGAGRTGRPREEPSPDPAQARAPQTVYARFLRDPEAKKRDPRETFLVARAPDAEDEEEEEEEDEEDEEEEAEEKKEKILLPPKKPLREKSSADLKERRAKAQGPRGDLGSPDPPPKPLRVRNKEAPAGEGTKMRKTKKKGSGEADKDPSGSPASARKSPAAMFLVGEGSPDKKALKKKGTPKGARKEEEEEEEAATVIKKSNQKGKAKGKGKKKAKEERAPSPPVEVDEPREFVLRPAPQGRTVRCRLTRDKKGMDRGM...
null
null
dendrite development [GO:0016358]; detection of light stimulus involved in visual perception [GO:0050908]; eye photoreceptor cell development [GO:0042462]; phagocytosis, recognition [GO:0006910]; photoreceptor cell maintenance [GO:0045494]; positive regulation of phagocytosis [GO:0050766]; protein localization to ciliu...
axon terminus [GO:0043679]; cell projection [GO:0042995]; cilium [GO:0005929]; cytosol [GO:0005829]; extracellular region [GO:0005576]; photoreceptor inner segment [GO:0001917]; photoreceptor outer segment [GO:0001750]; plasma membrane [GO:0005886]; synapse [GO:0045202]
actin filament binding [GO:0051015]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]
PF01167;
null
TUB family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16303976}. Cell membrane {ECO:0000269|PubMed:16303976}; Peripheral membrane protein {ECO:0000269|PubMed:16303976}; Cytoplasmic side {ECO:0000269|PubMed:16303976}. Secreted {ECO:0000250}. Synapse {ECO:0000250}. Note=Detected at synapses between photoreceptor cells and ...
null
null
null
null
null
FUNCTION: Required for normal development of photoreceptor synapses. Required for normal photoreceptor function and for long-term survival of photoreceptor cells. Interacts with cytoskeleton proteins and may play a role in protein transport in photoreceptor cells (By similarity). Binds lipids, especially phosphatidylin...
Homo sapiens (Human)
O00299
CLIC1_HUMAN
MAEEQPQVELFVKAGSDGAKIGNCPFSQRLFMVLWLKGVTFNVTTVDTKRRTETVQKLCPGGQLPFLLYGTEVHTDTNKIEEFLEAVLCPPRYPKLAALNPESNTAGLDIFAKFSAYIKNSNPALNDNLEKGLLKALKVLDNYLTSPLPEEVDETSAEDEGVSQRKFLDGNELTLADCNLLPKLHIVQVVCKKYRGFTIPEAFRGVHRYLSNAYAREEFASTCPDDEEIELAYEQVAKALK
null
null
chloride transport [GO:0006821]; platelet aggregation [GO:0070527]; positive regulation of osteoblast differentiation [GO:0045669]; regulation of mitochondrial membrane potential [GO:0051881]; signal transduction [GO:0007165]
blood microparticle [GO:0072562]; brush border [GO:0005903]; chloride channel complex [GO:0034707]; cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; membrane [GO:0016020]; mitochondrion [GO:0005739]; nuclear envelope [GO:0005635]; nuclear ...
cadherin binding [GO:0045296]; chloride channel activity [GO:0005254]
PF13410;PF13409;
1.20.1050.10;3.40.30.10;
Chloride channel CLIC family
PTM: Hydrogen peroxide treatment causes a conformation change, leading to dimerization and formation of an intramolecular disulfide bond between Cys-24 and Cys-59.
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12681486, ECO:0000269|PubMed:9139710}. Nucleus membrane {ECO:0000269|PubMed:9139710}; Single-pass membrane protein {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:10793131, ECO:0000269|PubMed:11551966, ECO:0000269|PubMed:12681486, ECO:0000269|PubMed:9139710, ECO:0000305|Pu...
CATALYTIC ACTIVITY: Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823, ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:11195932, ECO:0000269|PubMed:11551966, ECO:0000269|PubMed:11978800, ECO:0000269|PubMed:14613939, ECO:0000269|PubMed:9139710};
null
null
null
null
FUNCTION: Can insert into membranes and form chloride ion channels. Channel activity depends on the pH. Membrane insertion seems to be redox-regulated and may occur only under oxydizing conditions. Involved in regulation of the cell cycle. {ECO:0000269|PubMed:10834939, ECO:0000269|PubMed:11195932, ECO:0000269|PubMed:11...
Homo sapiens (Human)
O00300
TR11B_HUMAN
MNNLLCCALVFLDISIKWTTQETFPPKYLHYDEETSHQLLCDKCPPGTYLKQHCTAKWKTVCAPCPDHYYTDSWHTSDECLYCSPVCKELQYVKQECNRTHNRVCECKEGRYLEIEFCLKHRSCPPGFGVVQAGTPERNTVCKRCPDGFFSNETSSKAPCRKHTNCSVFGLLLTQKGNATHDNICSGNSESTQKCGIDVTLCEEAFFRFAVPTKFTPNWLSVLVDNLPGTKVNAESVERIKRQHSSQEQTFQLLKLWKHQNKDQDIVKKIIQDIDLCENSVQRHIGHANLTFEQLRSLMESLPGKKVGAEDIEKTIKACK...
null
null
apoptotic process [GO:0006915]; extracellular matrix organization [GO:0030198]; negative regulation of bone resorption [GO:0045779]; negative regulation of odontogenesis of dentin-containing tooth [GO:0042489]; negative regulation of osteoclast differentiation [GO:0045671]; negative regulation of tumor necrosis factor-...
extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]
cytokine activity [GO:0005125]; heparan sulfate binding [GO:1904399]; signaling receptor activity [GO:0038023]
PF00531;PF00020;
1.10.533.10;2.10.50.10;
null
PTM: N-glycosylated. Contains sialic acid residues. {ECO:0000269|PubMed:22664871}.; PTM: The N-terminus is blocked.
SUBCELLULAR LOCATION: Secreted.
null
null
null
null
null
FUNCTION: Acts as a decoy receptor for TNFSF11/RANKL and thereby neutralizes its function in osteoclastogenesis. Inhibits the activation of osteoclasts and promotes osteoclast apoptosis in vitro. Bone homeostasis seems to depend on the local ratio between TNFSF11 and TNFRSF11B. May also play a role in preventing arteri...
Homo sapiens (Human)
O00303
EIF3F_HUMAN
MATPAVPVSAPPATPTPVPAAAPASVPAPTPAPAAAPVPAAAPASSSDPAAAAAATAAPGQTPASAQAPAQTPAPALPGPALPGPFPGGRVVRLHPVILASIVDSYERRNEGAARVIGTLLGTVDKHSVEVTNCFSVPHNESEDEVAVDMEFAKNMYELHKKVSPNELILGWYATGHDITEHSVLIHEYYSREAPNPIHLTVDTSLQNGRMSIKAYVSTLMGVPGRTMGVMFTPLTVKYAYYDTERIGVDLIMKTCFSPNRVIGLSSDLQQVGGASARIQDALSTVLQYAEDVLSGKVSADNTVGRFLMSLVNQVPKIVP...
3.4.19.12
null
formation of cytoplasmic translation initiation complex [GO:0001732]; IRES-dependent viral translational initiation [GO:0075522]; protein deubiquitination [GO:0016579]; proteolysis [GO:0006508]; translational initiation [GO:0006413]
cytosol [GO:0005829]; eukaryotic 43S preinitiation complex [GO:0016282]; eukaryotic 48S preinitiation complex [GO:0033290]; eukaryotic translation initiation factor 3 complex [GO:0005852]; eukaryotic translation initiation factor 3 complex, eIF3m [GO:0071541]; membrane [GO:0016020]; synapse [GO:0045202]
cysteine-type deubiquitinase activity [GO:0004843]; identical protein binding [GO:0042802]; metal-dependent deubiquitinase activity [GO:0140492]; translation initiation factor activity [GO:0003743]; translation initiation factor binding [GO:0031369]
PF01398;PF13012;
3.40.140.10;
EIF-3 subunit F family
PTM: Phosphorylation is enhanced upon serum stimulation. Phosphorylated during apoptosis by caspase-processed CDK11. {ECO:0000269|PubMed:12446680, ECO:0000269|PubMed:17322308}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03005}.
CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000269|PubMed:21124883};
null
null
null
null
FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis (PubMed:17581632, PubMed:25849773, PubMed:27462815). The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-...
Homo sapiens (Human)
O00305
CACB4_HUMAN
MSSSSYAKNGTADGPHSPTSQVARGTTTRRSRLKRSDGSTTSTSFILRQGSADSYTSRPSDSDVSLEEDREAIRQEREQQAAIQLERAKSKPVAFAVKTNVSYCGALDEDVPVPSTAISFDAKDFLHIKEKYNNDWWIGRLVKEGCEIGFIPSPLRLENIRIQQEQKRGRFHGGKSSGNSSSSLGEMVSGTFRATPTSTAKQKQKVTEHIPPYDVVPSMRPVVLVGPSLKGYEVTDMMQKALFDFLKHRFDGRISITRVTADISLAKRSVLNNPSKRAIIERSNTRSSLAEVQSEIERIFELARSLQLVVLDADTINHPA...
null
null
adult walking behavior [GO:0007628]; cAMP metabolic process [GO:0046058]; cellular response to leukemia inhibitory factor [GO:1990830]; chemical synaptic transmission [GO:0007268]; detection of light stimulus involved in visual perception [GO:0050908]; gamma-aminobutyric acid secretion [GO:0014051]; gamma-aminobutyric ...
cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; glutamatergic synapse [GO:0098978]; nuclear speck [GO:0016607]; plasma membrane [GO:0005886]; presynapse [GO:0098793]; synapse [GO:0045202]; voltage-gated calcium channel complex [GO:0005891]
protein kinase binding [GO:0019901]; voltage-gated calcium channel activity involved in regulation of presynaptic cytosolic calcium levels [GO:0099626]
PF00625;PF12052;
3.40.50.300;2.30.30.40;
Calcium channel beta subunit family
null
null
null
null
null
null
null
FUNCTION: The beta subunit of voltage-dependent calcium channels contributes to the function of the calcium channel by increasing peak calcium current, shifting the voltage dependencies of activation and inactivation, modulating G protein inhibition and controlling the alpha-1 subunit membrane targeting. {ECO:0000269|P...
Homo sapiens (Human)
O00308
WWP2_HUMAN
MASASSSRAGVALPFEKSQLTLKVVSAKPKVHNRQPRINSYVEVAVDGLPSETKKTGKRIGSSELLWNEIIILNVTAQSHLDLKVWSCHTLRNELLGTASVNLSNVLKNNGGKMENMQLTLNLQTENKGSVVSGGELTIFLDGPTVDLGNVPNGSALTDGSQLPSRDSSGTAVAPENRHQPPSTNCFGGRSRTHRHSGASARTTPATGEQSPGARSRHRQPVKNSGHSGLANGTVNDEPTTATDPEEPSVVGVTSPPAAPLSVTPNPNTTSLPAPATPAEGEEPSTSGTQQLPAAAQAPDALPAGWEQRELPNGRVYYVD...
2.3.2.26
null
extracellular transport [GO:0006858]; negative regulation of DNA-binding transcription factor activity [GO:0043433]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of gene expression [GO:0010629]; negative regulation of Notch signaling pathway [GO:0045746]; negative regulation of p...
cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; nucleus [GO:0005634]; ubiquitin ligase complex [GO:0000151]
RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; transcription factor binding [GO:0008134]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]
PF00632;PF00397;
2.20.70.10;2.60.40.150;3.30.2160.10;3.30.2410.10;3.90.1750.10;
null
PTM: Autoubiquitinated. Ubiquitinated by the SCF(FBXL15) complex, leading to its degradation by the proteasome. {ECO:0000269|PubMed:19343052, ECO:0000269|PubMed:21572392}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19274063, ECO:0000269|PubMed:20858735}.
CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.26; Evidence={ECO:0000269|PubMed:19274063, ECO:0000269|PubMed:19651900};
null
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:19274063, ECO:0000269|PubMed:19651900}.
null
null
FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Polyubiquitinates POU5F1 by 'Lys-63'-linked conjugation and promotes it to proteasomal degradation; in embryonic stem cells (...
Homo sapiens (Human)
O00311
CDC7_HUMAN
MEASLGIQMDEPMAFSPQRDRFQAEGSLKKNEQNFKLAGVKKDIEKLYEAVPQLSNVFKIEDKIGEGTFSSVYLATAQLQVGPEEKIALKHLIPTSHPIRIAAELQCLTVAGGQDNVMGVKYCFRKNDHVVIAMPYLEHESFLDILNSLSFQEVREYMLNLFKALKRIHQFGIVHRDVKPSNFLYNRRLKKYALVDFGLAQGTHDTKIELLKFVQSEAQQERCSQNKSHIITGNKIPLSGPVPKELDQQSTTKASVKRPYTNAQIQIKQGKDGKEGSVGLSVQRSVFGERNFNIHSSISHESPAVKLMKQSKTVDVLSRK...
2.7.11.1
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
cell cycle phase transition [GO:0044770]; cell division [GO:0051301]; double-strand break repair via break-induced replication [GO:0000727]; G1/S transition of mitotic cell cycle [GO:0000082]; mitotic DNA damage checkpoint signaling [GO:0044773]; phosphorylation [GO:0016310]; positive regulation of cell population prol...
cytoplasm [GO:0005737]; intercellular bridge [GO:0045171]; mitotic spindle [GO:0072686]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
ATP binding [GO:0005524]; kinase activity [GO:0016301]; metal ion binding [GO:0046872]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
PF00069;
1.10.510.10;
Protein kinase superfamily, Ser/Thr protein kinase family, CDC7 subfamily
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:27401717}.
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:27401717}; Physiolog...
null
null
null
null
FUNCTION: Kinase involved in initiation of DNA replication. Phosphorylates critical substrates that regulate the G1/S phase transition and initiation of DNA replication, such as MCM proteins and CLASPIN. {ECO:0000269|PubMed:12065429, ECO:0000269|PubMed:27401717}.
Homo sapiens (Human)
O00322
UPK1A_HUMAN
MASAAAAEAEKGSPVVVGLLVVGNIIILLSGLSLFAETIWVTADQYRVYPLMGVSGKDDVFAGAWIAIFCGFSFFMVASFGVGAALCRRRSMVLTYLVLMLIVYIFECASCITSYTHRDYMVSNPSLITKQMLTFYSADTDQGQELTRLWDRVMIEQECCGTSGPMDWVNFTSAFRAATPEVVFPWPPLCCRRTGNFIPLNEEGCRLGHMDYLFTKGCFEHIGHAIDSYTWGISWFGFAILMWTLPVMLIAMYFYTML
null
null
epithelial cell differentiation [GO:0030855]
apical plasma membrane urothelial plaque [GO:0120001]; cell surface [GO:0009986]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]
null
PF00335;
1.10.1450.10;
Tetraspanin (TM4SF) family
null
SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
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 normal bladder epithelial physiology, possibly in regulating membrane permeability of superficial umbrella cells or in stabilizing the apica...
Homo sapiens (Human)
O00327
BMAL1_HUMAN
MADQRMDISSTISDFMSPGPTDLLSSSLGTSGVDCNRKRKGSSTDYQESMDTDKDDPHGRLEYTEHQGRIKNAREAHSQIEKRRRDKMNSFIDELASLVPTCNAMSRKLDKLTVLRMAVQHMKTLRGATNPYTEANYKPTFLSDDELKHLILRAADGFLFVVGCDRGKILFVSESVFKILNYSQNDLIGQSLFDYLHPKDIAKVKEQLSSSDTAPRERLIDAKTGLPVKTDITPGPSRLCSGARRSFFCRMKCNRPSVKVEDKDFPSTCSKKKADRKSFCTIHSTGYLKSWPPTKMGLDEDNEPDNEGCNLSCLVAIGRL...
null
null
circadian regulation of gene expression [GO:0032922]; circadian rhythm [GO:0007623]; negative regulation of cold-induced thermogenesis [GO:0120163]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of fat cell differentiation [GO:0045599]; negative regulation of glucocorticoid recept...
aryl hydrocarbon receptor complex [GO:0034751]; chromatin [GO:0000785]; chromatoid body [GO:0033391]; CLOCK-BMAL transcription complex [GO:1990513]; intracellular membrane-bounded organelle [GO:0043231]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PML body [GO:0016605]
aryl hydrocarbon receptor binding [GO:0017162]; DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription factor binding [GO:0140297]; E-box binding [GO:0070888]; Hsp90 protein binding [GO:0051879]; protein dimerization activity [GO:0046983];...
PF00010;PF00989;PF14598;
4.10.280.10;3.30.450.20;
null
PTM: Ubiquitinated, leading to its proteasomal degradation (PubMed:24728990). Deubiquitinated by USP9X (PubMed:29626158). {ECO:0000269|PubMed:24728990, ECO:0000269|PubMed:29626158}.; PTM: O-glycosylated; contains O-GlcNAc. O-glycosylation by OGT prevents protein degradation by inhibiting ubiquitination. It also stabili...
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:24005054}. Cytoplasm {ECO:0000250|UniProtKB:Q9WTL8}. Nucleus, PML body {ECO:0000250|UniProtKB:Q9WTL8}. Note=Shuttles between the nucleus and the cytoplasm and this nucleocytoplasmic shuttling is essential for the nuclear accumulatio...
null
null
null
null
null
FUNCTION: Transcriptional activator which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism a...
Homo sapiens (Human)
O00329
PK3CD_HUMAN
MPPGVDCPMEFWTKEENQSVVVDFLLPTGVYLNFPVSRNANLSTIKQLLWHRAQYEPLFHMLSGPEAYVFTCINQTAEQQELEDEQRRLCDVQPFLPVLRLVAREGDRVKKLINSQISLLIGKGLHEFDSLCDPEVNDFRAKMCQFCEEAAARRQQLGWEAWLQYSFPLQLEPSAQTWGPGTLRLPNRALLVNVKFEGSEESFTFQVSTKDVPLALMACALRKKATVFRQPLVEQPEDYTLQVNGRHEYLYGSYPLCQFQYICSCLHSGLTPHLTMVHSSSILAMRDEQSNPAPQVQKPRAKPPPIPAKKPSSVSLWSLE...
2.7.1.137; 2.7.1.153
null
adaptive immune response [GO:0002250]; B cell activation [GO:0042113]; B cell chemotaxis [GO:0035754]; B cell differentiation [GO:0030183]; B cell receptor signaling pathway [GO:0050853]; immune response [GO:0006955]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; mast cell chemotaxis [GO:0002...
cytoplasm [GO:0005737]; cytosol [GO:0005829]; phosphatidylinositol 3-kinase complex [GO:0005942]; phosphatidylinositol 3-kinase complex, class IA [GO:0005943]; plasma membrane [GO:0005886]
1-phosphatidylinositol-3-kinase activity [GO:0016303]; 1-phosphatidylinositol-4,5-bisphosphate 3-kinase activity [GO:0046934]; 1-phosphatidylinositol-4-phosphate 3-kinase activity [GO:0035005]; ATP binding [GO:0005524]; kinase activity [GO:0016301]
PF00454;PF00792;PF02192;PF00794;PF00613;
3.10.20.770;2.60.40.150;1.10.1070.11;1.25.40.70;
PI3/PI4-kinase family
PTM: Autophosphorylation on Ser-1039 results in the almost complete inactivation of the lipid kinase activity. {ECO:0000269|PubMed:10064595}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22020336}.
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-trisphosphate) + ADP + H(+); Xref=Rhea:RHEA:21292, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57836, ChEBI:CHEBI:58456, ChEBI:CHEBI:456216; EC=2.7.1.1...
null
PATHWAY: Phospholipid metabolism; phosphatidylinositol phosphate biosynthesis. {ECO:0000305|PubMed:15135396, ECO:0000305|PubMed:9113989}.
null
null
FUNCTION: Phosphoinositide-3-kinase (PI3K) phosphorylates phosphatidylinositol (PI) and its phosphorylated derivatives at position 3 of the inositol ring to produce 3-phosphoinositides (PubMed:9235916). Uses ATP and PtdIns(4,5)P2 (phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphospha...
Homo sapiens (Human)
O00330
ODPX_HUMAN
MAASWRLGCDPRLLRYLVGFPGRRSVGLVKGALGWSVSRGANWRWFHSTQWLRGDPIKILMPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKNIRLGSLIGLIVEEGEDWKHVEIPKDVGPPPPVSKPSEPRPSPEPQISIPVKKEHIPGTLRFRLSPAARNILEKHSLDASQGTATGPRGIFTKEDALKLVQLKQTGKITESRPTPAPTATPTAPSPLQATAGPSYPRPVIPPVSTPGQPNAVGTFTEIPASNIRRVIAKRLTESKSTVPHAYATADCDLGAVLKVRQDLV...
null
null
acetyl-CoA biosynthetic process from pyruvate [GO:0006086]
mitochondrial matrix [GO:0005759]; mitochondrial pyruvate dehydrogenase complex [GO:0005967]; mitochondrion [GO:0005739]; pyruvate dehydrogenase complex [GO:0045254]
acyltransferase activity [GO:0016746]
PF00198;PF00364;PF02817;
2.40.50.100;3.30.559.10;4.10.320.10;
2-oxoacid dehydrogenase family
PTM: Delipoylated at Lys-97 by SIRT4, delipoylation decreases the PHD complex activity. {ECO:0000269|PubMed:25525879}.
SUBCELLULAR LOCATION: Mitochondrion matrix.
null
null
null
null
null
FUNCTION: Required for anchoring dihydrolipoamide dehydrogenase (E3) to the dihydrolipoamide transacetylase (E2) core of the pyruvate dehydrogenase complexes of eukaryotes. This specific binding is essential for a functional PDH complex.
Homo sapiens (Human)
O00337
S28A1_HUMAN
MENDPSRRRESISLTPVAKGLENMGADFLESLEEGQLPRSDLSPAEIRSSWSEAAPKPFSRWRNLQPALRARSFCREHMQLFRWIGTGLLCTGLSAFLLVACLLDFQRALALFVLTCVVLTFLGHRLLKRLLGPKLRRFLKPQGHPRLLLWFKRGLALAAFLGLVLWLSLDTSQRPEQLVSFAGICVFVALLFACSKHHCAVSWRAVSWGLGLQFVLGLLVIRTEPGFIAFEWLGEQIRIFLSYTKAGSSFVFGEALVKDVFAFQVLPIIVFFSCVISVLYHVGLMQWVILKIAWLMQVTMGTTATETLSVAGNIFVSQT...
null
null
azole transmembrane transport [GO:0045117]; cytidine transport [GO:0015861]; nucleoside import across plasma membrane [GO:0180015]; nucleoside transmembrane transport [GO:1901642]; purine nucleobase transmembrane transport [GO:1904823]; pyrimidine nucleobase transport [GO:0015855]; pyrimidine-containing compound transm...
apical plasma membrane [GO:0016324]; brush border membrane [GO:0031526]; cytosol [GO:0005829]; nuclear speck [GO:0016607]; plasma membrane [GO:0005886]
azole transmembrane transporter activity [GO:1901474]; cytidine transmembrane transporter activity [GO:0015212]; nucleoside:sodium symporter activity [GO:0005415]; purine nucleobase transmembrane transporter activity [GO:0005345]; pyrimidine- and adenosine-specific:sodium symporter activity [GO:0015389]; uridine transm...
PF07670;PF07662;PF01773;
null
Concentrative nucleoside transporter (CNT) (TC 2.A.41) family
PTM: N-glycosylated. N-glycosylation is required for localization to the plasma membrane and the transporter activity. {ECO:0000269|PubMed:30658162}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21998139}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q62674}. Apical cell membrane {ECO:0000269|PubMed:21998139}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q62674}.
CATALYTIC ACTIVITY: Reaction=Na(+)(out) + uridine(out) = Na(+)(in) + uridine(in); Xref=Rhea:RHEA:69887, ChEBI:CHEBI:16704, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:10455109, ECO:0000269|PubMed:14701834, ECO:0000269|PubMed:21795683, ECO:0000269|PubMed:21998139, ECO:0000269|PubMed:32126230, ECO:0000269|PubMed:9124...
null
null
null
null
FUNCTION: Sodium and pyrimidine nucleoside symporter of the plasma membrane that imports uridine, thymidine and cytidine into cells by coupling their transport to the transmembrane sodium electrochemical gradient. Also transports adenosine, an atypical substrate transported with high apparent affinity, but low maximum ...
Homo sapiens (Human)
O00338
ST1C2_HUMAN
MALTSDLGKQIKLKEVEGTLLQPATVDNWSQIQSFEAKPDDLLICTYPKAGTTWIQEIVDMIEQNGDVEKCQRAIIQHRHPFIEWARPPQPSGVEKAKAMPSPRILKTHLSTQLLPPSFWENNCKFLYVARNAKDCMVSYYHFQRMNHMLPDPGTWEEYFETFINGKVVWGSWFDHVKGWWEMKDRHQILFLFYEDIKRDPKHEIRKVMQFMGKKVDETVLDKIVQETSFEKMKENPMTNRSTVSKSILDQSISSFMRKGTVGDWKNHFTVAQNERFDEIYRRKMEGTSINFCMEL
2.8.2.1
null
amine metabolic process [GO:0009308]; sulfation [GO:0051923]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; lysosome [GO:0005764]
aryl sulfotransferase activity [GO:0004062]; sulfotransferase activity [GO:0008146]
PF00685;
3.40.50.300;
Sulfotransferase 1 family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O46503}. Lysosome {ECO:0000250|UniProtKB:Q9WUW8}.
CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + a phenol = adenosine 3',5'-bisphosphate + an aryl sulfate + H(+); Xref=Rhea:RHEA:12164, ChEBI:CHEBI:15378, ChEBI:CHEBI:33853, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:140317; EC=2.8.2.1; Evidence={ECO:0000269|PubMed:10481272, ECO:0000269|PubMed:10783263...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=13.3 mM for p-nitrophenol {ECO:0000269|PubMed:10481272}; Vmax=0.005 nmol/min/mg enzyme with p-nitrophenol as substrate {ECO:0000269|PubMed:10481272};
null
null
null
FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of phenolic compounds. Does not sulfonate steroids, dopamine, acetaminophen, or alpha-naphthol (PubMed:10481272, PubMed:10783263, PubMed:9852044). Catalyzes the sulfonation of the carcin...
Homo sapiens (Human)
O00339
MATN2_HUMAN
MEKMLAGCFLLILGQIVLLPAEARERSRGRSISRGRHARTHPQTALLESSCENKRADLVFIIDSSRSVNTHDYAKVKEFIVDILQFLDIGPDVTRVGLLQYGSTVKNEFSLKTFKRKSEVERAVKRMRHLSTGTMTGLAIQYALNIAFSEAEGARPLRENVPRVIMIVTDGRPQDSVAEVAAKARDTGILIFAIGVGQVDFNTLKSIGSEPHEDHVFLVANFSQIETLTSVFQKKLCTAHMCSTLEHNCAHFCINIPGSYVCRCKQGYILNSDQTTCRIQDLCAMEDHNCEQLCVNVPGSFVCQCYSGYALAEDGKRCVA...
null
null
axon guidance [GO:0007411]; dendrite regeneration [GO:0031104]; extracellular matrix organization [GO:0030198]; glial cell migration [GO:0008347]; neuron migration [GO:0001764]; response to axon injury [GO:0048678]
basement membrane [GO:0005604]; collagen-containing extracellular matrix [GO:0062023]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; matrilin complex [GO:0120216]
calcium ion binding [GO:0005509]; extracellular matrix structural constituent [GO:0005201]
PF12662;PF07645;PF14670;PF10393;PF00092;
1.20.5.30;2.10.25.10;3.40.50.410;
null
null
SUBCELLULAR LOCATION: Secreted.
null
null
null
null
null
FUNCTION: Involved in matrix assembly. {ECO:0000250}.
Homo sapiens (Human)
O00341
EAA5_HUMAN
MVPHAILARGRDVCRRNGLLILSVLSVIVGCLLGFFLRTRRLSPQEISYFQFPGELLMRMLKMMILPLVVSSLMSGLASLDAKTSSRLGVLTVAYYLWTTFMAVIVGIFMVSIIHPGSAAQKETTEQSGKPIMSSADALLDLIRNMFPANLVEATFKQYRTKTTPVVKSPKVAPEEAPPRRILIYGVQEENGSHVQNFALDLTPPPEVVYKSEPGTSDGMNVLGIVFFSATMGIMLGRMGDSGAPLVSFCQCLNESVMKIVAVAVWYFPFGIVFLIAGKILEMDDPRAVGKKLGFYSVTVVCGLVLHGLFILPLLYFFIT...
null
null
chloride transmembrane transport [GO:1902476]; dicarboxylic acid transport [GO:0006835]; L-glutamate transmembrane transport [GO:0015813]; monoatomic ion transport [GO:0006811]; neurotransmitter transport [GO:0006836]; neurotransmitter uptake [GO:0001504]
plasma membrane [GO:0005886]; postsynapse [GO:0098794]; synaptic membrane [GO:0097060]
extracellularly glutamate-gated chloride channel activity [GO:0008068]; glutamate:sodium symporter activity [GO:0015501]; high-affinity L-glutamate transmembrane transporter activity [GO:0005314]; L-glutamate transmembrane transporter activity [GO:0005313]; neutral L-amino acid transmembrane transporter activity [GO:00...
PF00375;
1.10.3860.10;
Dicarboxylate/amino acid:cation symporter (DAACS) (TC 2.A.23) family, SLC1A7 subfamily
null
SUBCELLULAR LOCATION: Photoreceptor inner segment membrane {ECO:0000250|UniProtKB:Q8JZR4}; Multi-pass membrane protein {ECO:0000255}. Synaptic cell membrane {ECO:0000250|UniProtKB:Q8JZR4}; Multi-pass membrane protein {ECO:0000255}. Note=Located in both cone and rod photoreceptor terminals and in axon terminals of rod b...
CATALYTIC ACTIVITY: Reaction=H(+)(out) + K(+)(in) + L-glutamate(out) + 3 Na(+)(out) = H(+)(in) + K(+)(out) + L-glutamate(in) + 3 Na(+)(in); Xref=Rhea:RHEA:70699, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:29103, ChEBI:CHEBI:29985; Evidence={ECO:0000269|PubMed:9108121}; CATALYTIC ACTIVITY: Reaction=H(+)(out) + K(...
null
null
null
null
FUNCTION: Sodium-dependent, high-affinity amino acid transporter that mediates the uptake of L-glutamate and also L-aspartate and D-aspartate. Functions as a symporter that transports one amino acid molecule together with two or three Na(+) ions and one proton, in parallel with the counter-transport of one K(+) ion (Pu...
Homo sapiens (Human)
O00358
FOXE1_HUMAN
MTAESGPPPPQPEVLATVKEERGETAAGAGVPGEATGRGAGGRRRKRPLQRGKPPYSYIALIAMAIAHAPERRLTLGGIYKFITERFPFYRDNPKKWQNSIRHNLTLNDCFLKIPREAGRPGKGNYWALDPNAEDMFESGSFLRRRKRFKRSDLSTYPAYMHDAAAAAAAAAAAAAAAAIFPGAVPAARPPYPGAVYAGYAPPSLAAPPPVYYPAASPGPCRVFGLVPERPLSPELGPAPSGPGGSCAFASAGAPATTTGYQPAGCTGARPANPSAYAAAYAGPDGAYPQGAGSAIFAAAGRLAGPASPPAGGSSGGVET...
null
null
anatomical structure morphogenesis [GO:0009653]; cell differentiation [GO:0030154]; cell migration [GO:0016477]; chordate pharynx development [GO:0160093]; cranial skeletal system development [GO:1904888]; embryonic organ morphogenesis [GO:0048562]; hair follicle morphogenesis [GO:0031069]; hard palate development [GO:...
chromatin [GO:0000785]; nucleus [GO:0005634]
DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]; sequence-specific double-stranded DNA binding [GO:19...
PF00250;
1.10.10.10;
null
PTM: Phosphorylated. {ECO:0000250}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21177256}.
null
null
null
null
null
FUNCTION: Transcription factor that binds consensus sites on a variety of gene promoters and activate their transcription. Involved in proper palate formation, most probably through the expression of MSX1 and TGFB3 genes which are direct targets of this transcription factor. Also implicated in thyroid gland morphogenes...
Homo sapiens (Human)
O00370
LORF2_HUMAN
MTGSNSHITILTLNVNGLNSPIKRHRLASWIKSQDPSVCCIQETHLTCRDTHRLKIKGWRKIYQANGKQKKAGVAILVSDKTDFKPTKIKRDKEGHYIMVKGSIQQEELTILNIYAPNTGAPRFIKQVLSDLQRDLDSHTLIMGDFNTPLSILDRSTRQKVNKDTQELNSALHQTDLIDIYRTLHPKSTEYTFFSAPHHTYSKIDHIVGSKALLSKCKRTEIITNYLSDHSAIKLELRIKNLTQSRSTTWKLNNLLLNDYWVHNEMKAEIKMFFETNENKDTTYQNLWDAFKAVCRGKFIALNAYKRKQERSKIDTLTSQ...
2.7.7.49; 3.1.21.-
null
DNA recombination [GO:0006310]; nucleic acid metabolic process [GO:0090304]; retrotransposition [GO:0032197]
null
metal ion binding [GO:0046872]; RNA binding [GO:0003723]; RNA-directed DNA polymerase activity [GO:0003964]; type II site-specific deoxyribonuclease activity [GO:0009036]
PF03372;PF00078;
3.60.10.10;
null
null
null
CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.49; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405, ECO:0000269|PubMed:9140393};
null
null
null
null
FUNCTION: Has reverse transcriptase activity required for target-primed reverse transcription of the LINE-1 element mRNA, a crucial step in LINE-1 retrotransposition (PubMed:7516468, PubMed:9140393). Also has endonuclease activity that allows the introduction of nicks in the chromosomal target DNA (PubMed:17626046, Pub...
Homo sapiens (Human)
O00391
QSOX1_HUMAN
MRRCNSGSGPPPSLLLLLLWLLAVPGANAAPRSALYSPSDPLTLLQADTVRGAVLGSRSAWAVEFFASWCGHCIAFAPTWKALAEDVKAWRPALYLAALDCAEETNSAVCRDFNIPGFPTVRFFKAFTKNGSGAVFPVAGADVQTLRERLIDALESHHDTWPPACPPLEPAKLEEIDGFFARNNEEYLALIFEKGGSYLGREVALDLSQHKGVAVRRVLNTEANVVRKFGVTDFPSCYLLFRNGSVSRVPVLMESRSFYTAYLQRLSGLTREAAQTTVAPTTANKIAPTVWKLADRSKIYMADLESALHYILRIEVGRFP...
1.8.3.2
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:18393449, ECO:0000269|PubMed:20211621}; Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:18393449, ECO:0000269|PubMed:20211621};
extracellular matrix assembly [GO:0085029]; negative regulation of macroautophagy [GO:0016242]; protein folding [GO:0006457]
endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; intercellular bridge [GO:0045171]; intracellular membrane-bounded organelle [GO:0043231]; platelet alpha granule l...
FAD binding [GO:0071949]; flavin-dependent sulfhydryl oxidase activity [GO:0016971]; protein disulfide isomerase activity [GO:0003756]
PF04777;PF18371;PF18108;PF00085;
1.20.120.310;3.40.30.10;1.20.120.1960;
Quiescin-sulfhydryl oxidase (QSOX) family
PTM: N-glycosylated (PubMed:17331072, PubMed:29757379). O-glycosylated on Thr and Ser residues (PubMed:29757379). {ECO:0000269|PubMed:17331072, ECO:0000269|PubMed:29757379}.
SUBCELLULAR LOCATION: [Isoform 1]: Golgi apparatus membrane {ECO:0000269|PubMed:17331072, ECO:0000269|PubMed:23704371}; Single-pass membrane protein {ECO:0000305|PubMed:17331072}. Secreted {ECO:0000269|PubMed:29757379}. Note=A small proportion is secreted, probably via a proteolytic cleavage that removes the membrane a...
CATALYTIC ACTIVITY: Reaction=O2 + 2 R'C(R)SH = H2O2 + R'C(R)S-S(R)CR'; Xref=Rhea:RHEA:17357, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16520, ChEBI:CHEBI:17412; EC=1.8.3.2; Evidence={ECO:0000269|PubMed:18393449, ECO:0000269|PubMed:22801504, ECO:0000269|PubMed:23704371, ECO:0000269|PubMed:23867277, ECO:0000269|P...
null
null
null
null
FUNCTION: Catalyzes the oxidation of sulfhydryl groups in peptide and protein thiols to disulfides with the reduction of oxygen to hydrogen peroxide (PubMed:17331072, PubMed:18393449, PubMed:23704371, PubMed:23867277, PubMed:30367560). Plays a role in disulfide bond formation in a variety of extracellular proteins (Pub...
Homo sapiens (Human)
O00399
DCTN6_HUMAN
MAEKTQKSVKIAPGAVVCVESEIRGDVTIGPRTVIHPKARIIAEAGPIVIGEGNLIEEQALIINAYPDNITPDTEDPEPKPMIIGTNNVFEVGCYSQAMKMGDNNVIESKAYVGRNVILTSGCIIGACCNLNTFEVIPENTVIYGADCLRRVQTERPQPQTLQLDFLMKILPNYHHLKKTMKGSSTPVKN
null
null
mitotic spindle organization [GO:0007052]
centrosome [GO:0005813]; cytosol [GO:0005829]; dynactin complex [GO:0005869]; kinetochore [GO:0000776]
dynein complex binding [GO:0070840]
null
2.160.10.10;
Dynactin subunits 5/6 family, Dynactin subunit 6 subfamily
PTM: Phosphorylation at Thr-186 by CDK1 during mitotic prometaphase creates a binding site for PLK1 that facilitates its recruitment to kinetochores. {ECO:0000269|PubMed:23455152}.
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:D0G6S1}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:23455152}.
null
null
null
null
null
FUNCTION: Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules. {ECO:0000269|PubMed:23455152}.
Homo sapiens (Human)
O00400
ACATN_HUMAN
MSPTISHKDSSRQRRPGNFSHSLDMKSGPLPPGGWDDSHLDSAGREGDREALLGDTGTGDFLKAPQSFRAELSSILLLLFLYVLQGIPLGLAGSIPLILQSKNVSYTDQAFFSFVFWPFSLKLLWAPLVDAVYVKNFGRRKSWLVPTQYILGLFMIYLSTQVDRLLGNTDDRTPDVIALTVAFFLFEFLAATQDIAVDGWALTMLSRENVGYASTCNSVGQTAGYFLGNVLFLALESADFCNKYLRFQPQPRGIVTLSDFLFFWGTVFLITTTLVALLKKENEVSVVKEETQGITDTYKLLFAIIKMPAVLTFCLLILTA...
null
null
acetyl-CoA transmembrane transport [GO:0035348]; transmembrane transport [GO:0055085]
endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; membrane [GO:0016020]; plasma membrane [GO:0005886]
acetyl-CoA transmembrane transporter activity [GO:0008521]; protein homodimerization activity [GO:0042803]
PF13000;
1.20.1250.20;
SLC33A transporter family
null
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:20826464, ECO:0000269|PubMed:24828632}; Multi-pass membrane protein {ECO:0000255}.
CATALYTIC ACTIVITY: Reaction=acetyl-CoA(in) = acetyl-CoA(out); Xref=Rhea:RHEA:75039, ChEBI:CHEBI:57288; Evidence={ECO:0000269|PubMed:20826464, ECO:0000269|PubMed:24828632}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75040; Evidence={ECO:0000269|PubMed:20826464, ECO:0000269|PubMed:24828632};
null
null
null
null
FUNCTION: Acetyl-CoA transporter that mediates active acetyl-CoA import through the endoplasmic reticulum (ER) membrane into the ER lumen where specific ER-based acetyl-CoA:lysine acetyltransferases are responsible for the acetylation of ER-based protein substrates, such as BACE1 (PubMed:20826464, PubMed:24828632). Nec...
Homo sapiens (Human)
O00401
WASL_HUMAN
MSSVQQQPPPPRRVTNVGSLLLTPQENESLFTFLGKKCVTMSSAVVQLYAADRNCMWSKKCSGVACLVKDNPQRSYFLRIFDIKDGKLLWEQELYNNFVYNSPRGYFHTFAGDTCQVALNFANEEEAKKFRKAVTDLLGRRQRKSEKRRDPPNGPNLPMATVDIKNPEITTNRFYGPQVNNISHTKEKKKGKAKKKRLTKADIGTPSNFQHIGHVGWDPNTGFDLNNLDPELKNLFDMCGISEAQLKDRETSKVIYDFIEKTGGVEAVKNELRRQAPPPPPPSRGGPPPPPPPPHNSGPPPPPARGRGAPPPPPSRAPTA...
null
null
actin filament polymerization [GO:0030041]; actin polymerization or depolymerization [GO:0008154]; cell division [GO:0051301]; dendritic spine morphogenesis [GO:0060997]; negative regulation of lymphocyte migration [GO:2000402]; negative regulation of membrane tubulation [GO:1903526]; positive regulation of clathrin-de...
actin cap [GO:0030478]; actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; endocytic vesicle membrane [GO:0030666]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; glutamatergic synapse [GO:0098978]; lamellipodium [GO:0030027...
actin binding [GO:0003779]; GTPase regulator activity [GO:0030695]; microtubule binding [GO:0008017]
PF00786;PF00568;PF02205;
3.90.810.10;2.30.29.30;
null
PTM: Phosphorylation at Ser-242, Tyr-256, Ser-484 and Ser-485 enhances actin polymerization activity. {ECO:0000269|PubMed:16257963}.
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9422512}. Nucleus {ECO:0000269|PubMed:16767080}. Cytoplasm {ECO:0000250|UniProtKB:Q91YD9}. Note=Preferentially localized in the cytoplasm when phosphorylated and in the nucleus when unphosphorylated (By similarity). Exported from the nucleus by an nuclea...
null
null
null
null
null
FUNCTION: Regulates actin polymerization by stimulating the actin-nucleating activity of the Arp2/3 complex (PubMed:16767080, PubMed:19366662, PubMed:19487689, PubMed:22847007, PubMed:22921828, PubMed:9422512). Involved in various processes, such as mitosis and cytokinesis, via its role in the regulation of actin polym...
Homo sapiens (Human)
O00408
PDE2A_HUMAN
MGQACGHSILCRSQQYPAARPAEPRGQQVFLKPDEPPPPPQPCADSLQDALLSLGSVIDISGLQRAVKEALSAVLPRVETVYTYLLDGESQLVCEDPPHELPQEGKVREAIISQKRLGCNGLGFSDLPGKPLARLVAPLAPDTQVLVMPLADKEAGAVAAVILVHCGQLSDNEEWSLQAVEKHTLVALRRVQVLQQRGPREAPRAVQNPPEGTAEDQKGGAAYTDRDRKILQLCGELYDLDASSLQLKVLQYLQQETRASRCCLLLVSEDNLQLSCKVIGDKVLGEEVSFPLTGCLGQVVEDKKSIQLKDLTSEDVQQLQ...
3.1.4.17
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:15938621, ECO:0000269|PubMed:19828435, ECO:0000269|PubMed:23899287}; Note=Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions. {ECO:0000269|PubMed:15938621, ECO:0000269|PubMed:19828435, ECO:0000269|PubMed:238992...
adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway [GO:0007193]; aorta development [GO:0035904]; cAMP-mediated signaling [GO:0019933]; cellular response to 2,3,7,8-tetrachlorodibenzodioxine [GO:1904613]; cellular response to cAMP [GO:0071320]; cellular response to cGMP [GO:0071321]; cellular resp...
cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrial outer membrane [GO:0005741]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO...
3',5'-cyclic-AMP phosphodiesterase activity [GO:0004115]; 3',5'-cyclic-GMP phosphodiesterase activity [GO:0047555]; cAMP binding [GO:0030552]; cGMP binding [GO:0030553]; cGMP-stimulated cyclic-nucleotide phosphodiesterase activity [GO:0004118]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287];...
PF01590;PF00233;
3.30.450.40;1.10.1300.10;
Cyclic nucleotide phosphodiesterase family, PDE2 subfamily
null
SUBCELLULAR LOCATION: [Isoform PDE2A3]: Cell membrane {ECO:0000269|PubMed:19632989, ECO:0000269|PubMed:28463107}; Lipid-anchor {ECO:0000269|PubMed:19632989}.; SUBCELLULAR LOCATION: [Isoform PDE2A2]: Mitochondrion matrix {ECO:0000250|UniProtKB:Q922S4}. Mitochondrion inner membrane {ECO:0000269|PubMed:28463107}. Mitochon...
CATALYTIC ACTIVITY: Reaction=a nucleoside 3',5'-cyclic phosphate + H2O = a nucleoside 5'-phosphate + H(+); Xref=Rhea:RHEA:14653, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57867, ChEBI:CHEBI:58464; EC=3.1.4.17; Evidence={ECO:0000269|PubMed:15938621, ECO:0000269|PubMed:29392776, ECO:0000269|PubMed:9210593}; Physi...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=43.7 uM for 3',5'-cyclic GMP {ECO:0000269|PubMed:15938621}; KM=32 uM for 3',5'-cyclic AMP {ECO:0000269|PubMed:15938621}; Vmax=20.5 nmol/min/mg enzyme for 3',5'-cyclic AMP {ECO:0000269|PubMed:9210593}; Vmax=28.5 nmol/min/mg enzyme for 3',5'-cyclic GMP {ECO:0000269|P...
null
null
null
FUNCTION: cGMP-activated cyclic nucleotide phosphodiesterase with a dual-specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes (PubMed:15938621, PubMed:29392776, PubMed:9210593). Has a higher efficiency with cGMP compared to cAMP (PubMed:15938621). Plays...
Homo sapiens (Human)
O00409
FOXN3_HUMAN
MGPVMPPSKKPESSGISVSSGLSQCYGGSGFSKALQEDDDLDFSLPDIRLEEGAMEDEELTNLNWLHESKNLLKSFGESVLRSVSPVQDLDDDTPPSPAHSDMPYDARQNPNCKPPYSFSCLIFMAIEDSPTKRLPVKDIYNWILEHFPYFANAPTGWKNSVRHNLSLNKCFKKVDKERSQSIGKGSLWCIDPEYRQNLIQALKKTPYHPHPHVFNTPPTCPQAYQSTSGPPIWPGSTFFKRNGALLQDPDIDAASAMMLLNTPPEIQAGFPPGVIQNGARVLSRGLFPGVRPLPITPIGVTAAMRNGITSCRMRTESEP...
null
null
craniofacial suture morphogenesis [GO:0097094]; mitotic G2 DNA damage checkpoint signaling [GO:0007095]; negative regulation of DNA-templated transcription [GO:0045892]; regulation of DNA-templated transcription [GO:0006355]
chromatin [GO:0000785]; nucleus [GO:0005634]
cis-regulatory region sequence-specific DNA binding [GO:0000987]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]
PF00250;
1.10.10.10;
null
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
null
null
null
null
null
FUNCTION: Acts as a transcriptional repressor. May be involved in DNA damage-inducible cell cycle arrests (checkpoints). {ECO:0000269|PubMed:16102918}.
Homo sapiens (Human)
O00410
IPO5_HUMAN
MAAAAAEQQQFYLLLGNLLSPDNVVRKQAEETYENIPGQSKITFLLQAIRNTTAAEEARQMAAVLLRRLLSSAFDEVYPALPSDVQTAIKSELLMIIQMETQSSMRKKVCDIAAELARNLIDEDGNNQWPEGLKFLFDSVSSQNVGLREAALHIFWNFPGIFGNQQQHYLDVIKRMLVQCMQDQEHPSIRTLSARATAAFILANEHNVALFKHFADLLPGFLQAVNDSCYQNDDSVLKSLVEIADTVPKYLRPHLEATLQLSLKLCGDTSLNNMQRQLALEVIVTLSETAAAMLRKHTNIVAQTIPQMLAMMVDLEEDED...
null
null
cellular response to amino acid stimulus [GO:0071230]; cytoplasmic pattern recognition receptor signaling pathway [GO:0002753]; negative regulation of cyclin-dependent protein serine/threonine kinase activity [GO:0045736]; NLS-bearing protein import into nucleus [GO:0006607]; positive regulation of protein import into ...
cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; nuclear membrane [GO:0031965]; nuclear pore [GO:0005643]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
GTPase inhibitor activity [GO:0005095]; nuclear import signal receptor activity [GO:0061608]; nuclear localization sequence binding [GO:0008139]; RNA binding [GO:0003723]; small GTPase binding [GO:0031267]
PF02985;PF13513;PF18808;PF18816;PF18829;
1.25.10.10;
Importin beta family, Importin beta-3 subfamily
null
SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Nucleus, nucleolus. Note=Nucleus; nuclear rim. Found particularly in the nuclear rim and nucleolus.
null
null
null
null
null
FUNCTION: Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. Is thought to mediate docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to nucleoporin and the complex is subsequently tra...
Homo sapiens (Human)
O00411
RPOM_HUMAN
MSALCWGRGAAGLKRALRPCGRPGLPGKEGTAGGVCGPRRSSSASPQEQDQDRRKDWGHVELLEVLQARVRQLQAESVSEVVVNRVDVARLPECGSGDGSLQPPRKVQMGAKDATPVPCGRWAKILEKDKRTQQMRMQRLKAKLQMPFQSGEFKALTRRLQVEPRLLSKQMAGCLEDCTRQAPESPWEEQLARLLQEAPGKLSLDVEQAPSGQHSQAQLSGQQQRLLAFFKCCLLTDQLPLAHHLLVVHHGQRQKRKLLTLDMYNAVMLGWARQGAFKELVYVLFMVKDAGLTPDLLSYAAALQCMGRQDQDAGTIERCL...
2.7.7.6
null
mitochondrial transcription [GO:0006390]; transcription initiation at mitochondrial promoter [GO:0006391]
mitochondrial DNA-directed RNA polymerase complex [GO:0034245]; mitochondrial matrix [GO:0005759]; mitochondrial nucleoid [GO:0042645]; mitochondrion [GO:0005739]; protein-containing complex [GO:0032991]
3'-5'-RNA exonuclease activity [GO:0000175]; DNA primase activity [GO:0003896]; DNA-directed 5'-3' RNA polymerase activity [GO:0003899]; mitochondrial promoter sequence-specific DNA binding [GO:0001018]; RNA binding [GO:0003723]; sequence-specific DNA binding [GO:0043565]
PF00940;PF14700;
1.10.287.280;1.10.150.20;1.10.1320.10;1.25.40.10;
Phage and mitochondrial RNA polymerase family
null
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:23283301, ECO:0000269|PubMed:29445193}.
CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.6; Evidence={ECO:0000255|PROSITE-ProRule:PRU10031, ECO:0000255|PROSITE-ProRule:PRU10032};
null
null
null
null
FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of mitochondrial DNA into RNA using the four ribonucleoside triphosphates as substrates (PubMed:21278163, PubMed:33602924). Component of the mitochondrial transcription initiation complex, composed at least of TFB2M, TFAM and POLRMT that is required for...
Homo sapiens (Human)
O00418
EF2K_HUMAN
MADEDLIFRLEGVDGGQSPRAGHDGDSDGDSDDEEGYFICPITDDPSSNQNVNSKVNKYYSNLTKSERYSSSGSPANSFHFKEAWKHAIQKAKHMPDPWAEFHLEDIATERATRHRYNAVTGEWLDDEVLIKMASQPFGRGAMRECFRTKKLSNFLHAQQWKGASNYVAKRYIEPVDRDVYFEDVRLQMEAKLWGEEYNRHKPPKQVDIMQMCIIELKDRPGKPLFHLEHYIEGKYIKYNSNSGFVRDDNIRLTPQAFSHFTFERSGHQLIVVDIQGVGDLYTDPQIHTETGTDFGDGNLGVRGMALFFYSHACNRICES...
2.7.11.20
null
cellular response to anoxia [GO:0071454]; cellular response to brain-derived neurotrophic factor stimulus [GO:1990416]; cellular response to calcium ion [GO:0071277]; cellular response to cAMP [GO:0071320]; cellular response to insulin stimulus [GO:0032869]; myosin II filament disassembly [GO:0031037]; negative regulat...
actomyosin contractile ring [GO:0005826]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendritic spine [GO:0043197]; glutamatergic synapse [GO:0098978]; postsynaptic density [GO:0014069]
ATP binding [GO:0005524]; calcium ion binding [GO:0005509]; calmodulin binding [GO:0005516]; elongation factor-2 kinase activity [GO:0004686]; myosin heavy chain kinase activity [GO:0016905]; protein kinase activity [GO:0004672]; translation factor activity, RNA binding [GO:0008135]
PF02816;
3.20.200.10;1.25.40.10;
Protein kinase superfamily, Alpha-type protein kinase family
PTM: Autophosphorylated at multiple residues, Thr-348 being the major site. Phosphorylated by AMP-activated protein kinase AMPK at Ser-398 leading to EEF2K activation and protein synthesis inhibition. Phosphorylated by TRPM7 at Ser-78 resulting in improved protein stability, higher EE2F phosphorylated and subsequently ...
null
CATALYTIC ACTIVITY: Reaction=[translation elongation factor 2] + ATP = [translation elongation factor 2]-phosphate + ADP + H(+); Xref=Rhea:RHEA:21436, Rhea:RHEA-COMP:11268, Rhea:RHEA-COMP:11269, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546, ChEBI:CHEBI:456216; EC=2.7.11.20; Evidence={ECO:0...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.2 uM for EEF2 {ECO:0000269|PubMed:11015200}; Vmax=4 nmol/min/mg enzyme {ECO:0000269|PubMed:11015200};
null
null
null
FUNCTION: Threonine kinase that regulates protein synthesis by controlling the rate of peptide chain elongation. Upon activation by a variety of upstream kinases including AMPK or TRPM7, phosphorylates the elongation factor EEF2 at a single site, renders it unable to bind ribosomes and thus inactive. In turn, the rate ...
Homo sapiens (Human)
O00421
CCRL2_HUMAN
MANYTLAPEDEYDVLIEGELESDEAEQCDKYDAQALSAQLVPSLCSAVFVIGVLDNLLVVLILVKYKGLKRVENIYLLNLAVSNLCFLLTLPFWAHAGGDPMCKILIGLYFVGLYSETFFNCLLTVQRYLVFLHKGNFFSARRRVPCGIITSVLAWVTAILATLPEFVVYKPQMEDQKYKCAFSRTPFLPADETFWKHFLTLKMNISVLVLPLFIFTFLYVQMRKTLRFREQRYSLFKLVFAIMVVFLLMWAPYNIAFFLSTFKEHFSLSDCKSSYNLDKSVHITKLIATTHCCINPLLYAFLDGTFSKYLCRCFHLRSN...
null
null
calcium-mediated signaling [GO:0019722]; cell chemotaxis [GO:0060326]; chemotaxis [GO:0006935]; G protein-coupled receptor signaling pathway [GO:0007186]; immune response [GO:0006955]; inflammatory response [GO:0006954]; positive regulation of cytosolic calcium ion concentration [GO:0007204]
cytoplasm [GO:0005737]; external side of plasma membrane [GO:0009897]; plasma membrane [GO:0005886]
C-C chemokine binding [GO:0019957]; C-C chemokine receptor activity [GO:0016493]; CCR chemokine receptor binding [GO:0048020]; chemokine receptor activity [GO:0004950]; chemokine receptor binding [GO:0042379]
PF00001;
1.20.1070.10;
G-protein coupled receptor 1 family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18397265, ECO:0000269|PubMed:20002784}; Multi-pass membrane protein {ECO:0000269|PubMed:18397265, ECO:0000269|PubMed:20002784}.
null
null
null
null
null
FUNCTION: Receptor for CCL19 and chemerin/RARRES2. Does not appear to be a signaling receptor, but may have a role in modulating chemokine-triggered immune responses by capturing and internalizing CCL19 or by presenting RARRES2 ligand to CMKLR1, a functional signaling receptors. Plays a critical role for the developmen...
Homo sapiens (Human)
O00422
SAP18_HUMAN
MAVESRVTQEEIKKEPEKPIDREKTCPLLLRVFTTNNGRHHRMDEFSRGNVPSSELQIYTWMDATLKELTSLVKEVYPEARKKGTHFNFAIVFTDVKRPGYRVKEIGSTMSGRKGTDDSMTLQSQKFQIGDYLDIAITPPNRAPPPSGRMRPY
null
null
mRNA processing [GO:0006397]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of mRNA splicing, via spliceosome [GO:0048025]; positive regulation of apoptotic process [GO:0043065]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; regulation of transcription by ...
ASAP complex [GO:0061574]; cytosol [GO:0005829]; histone deacetylase complex [GO:0000118]; nuclear body [GO:0016604]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
RNA binding [GO:0003723]; transcription corepressor activity [GO:0003714]
PF06487;
3.10.20.550;
SAP18 family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16314458}. Cytoplasm {ECO:0000269|PubMed:16314458}. Nucleus speckle {ECO:0000269|PubMed:20966198}. Note=Shuttles between the nucleus and the cytoplasm (PubMed:16314458). Colocalizes with ACIN1 and SRSF2 in nuclear speckles (PubMed:20966198). {ECO:0000269|PubMed:16314458...
null
null
null
null
null
FUNCTION: Component of the SIN3-repressing complex. Enhances the ability of SIN3-HDAC1-mediated transcriptional repression. When tethered to the promoter, it can direct the formation of a repressive complex to core histone proteins. Auxiliary component of the splicing-dependent multiprotein exon junction complex (EJC) ...
Homo sapiens (Human)
O00423
EMAL1_HUMAN
MEDGFSSYSSLYDTSSLLQFCNDDSASAASSMEVTDRIASLEQRVQMQEDDIQLLKSALADVVRRLNITEEQQAVLNRKGPTKARPLMQTLPLRTTVNNGTVLPKKPTGSLPSPSGVRKETAVPATKSNIKRTSSSERVSPGGRRESNGDSRGNRNRTGSTSSSSSGKKNSESKPKEPVFSAEEGYVKMFLRGRPVTMYMPKDQVDSYSLEAKVELPTKRLKLEWVYGYRGRDCRNNLYLLPTGETVYFIASVVVLYNVEEQLQRHYAGHNDDVKCLAVHPDRITIATGQVAGTSKDGKQLPPHVRIWDSVTLNTLHVIG...
null
null
brain development [GO:0007420]; hematopoietic progenitor cell differentiation [GO:0002244]; microtubule cytoskeleton organization [GO:0000226]; mitotic spindle organization [GO:0007052]; neuroblast proliferation [GO:0007405]
cytosol [GO:0005829]; microtubule [GO:0005874]; microtubule associated complex [GO:0005875]; mitotic spindle midzone [GO:1990023]; mitotic spindle pole [GO:0097431]; perinuclear region of cytoplasm [GO:0048471]
calcium ion binding [GO:0005509]; microtubule binding [GO:0008017]; tubulin binding [GO:0015631]
PF03451;PF00400;
2.130.10.10;
WD repeat EMAP family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q05BC3}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q05BC3}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:24859200, ECO:0000269|PubMed:25740311}. Note=Detected in cytoplasmic punctae. Co-localizes with microtubules (PubMed:24859200, PubMed:25740311). Enric...
null
null
null
null
null
FUNCTION: Modulates the assembly and organization of the microtubule cytoskeleton, and probably plays a role in regulating the orientation of the mitotic spindle and the orientation of the plane of cell division. Required for normal proliferation of neuronal progenitor cells in the developing brain and for normal brain...
Homo sapiens (Human)
O00425
IF2B3_HUMAN
MNKLYIGNLSENAAPSDLESIFKDAKIPVSGPFLVKTGYAFVDCPDESWALKAIEALSGKIELHGKPIEVEHSVPKRQRIRKLQIRNIPPHLQWEVLDSLLVQYGVVESCEQVNTDSETAVVNVTYSSKDQARQALDKLNGFQLENFTLKVAYIPDEMAAQQNPLQQPRGRRGLGQRGSSRQGSPGSVSKQKPCDLPLRLLVPTQFVGAIIGKEGATIRNITKQTQSKIDVHRKENAGAAEKSITILSTPEGTSAACKSILEIMHKEAQDIKFTEEIPLKILAHNNFVGRLIGKEGRNLKKIEQDTDTKITISPLQELTL...
null
null
anatomical structure morphogenesis [GO:0009653]; CRD-mediated mRNA stabilization [GO:0070934]; mRNA transport [GO:0051028]; negative regulation of translation [GO:0017148]; nervous system development [GO:0007399]; regulation of cytokine production [GO:0001817]; regulation of gene expression [GO:0010468]; translation [G...
cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829]; nucleus [GO:0005634]; P-body [GO:0000932]
mRNA 3'-UTR binding [GO:0003730]; mRNA 5'-UTR binding [GO:0048027]; N6-methyladenosine-containing RNA reader activity [GO:1990247]; RNA binding [GO:0003723]; translation regulator activity [GO:0045182]
PF00013;PF00076;
3.30.310.210;3.30.70.330;3.30.1370.10;
RRM IMP/VICKZ family
null
SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasm, P-body {ECO:0000269|PubMed:29476152}. Cytoplasm, Stress granule {ECO:0000269|PubMed:29476152}. Note=Found in lamellipodia of the leading edge, in the perinuclear region, and beneath the plasma membrane. The subcytoplasmic localization is cell specific and regulated b...
null
null
null
null
null
FUNCTION: RNA-binding factor that may recruit target transcripts to cytoplasmic protein-RNA complexes (mRNPs). This transcript 'caging' into mRNPs allows mRNA transport and transient storage. It also modulates the rate and location at which target transcripts encounter the translational apparatus and shields them from ...
Homo sapiens (Human)
O00429
DNM1L_HUMAN
MEALIPVINKLQDVFNTVGADIIQLPQIVVVGTQSSGKSSVLESLVGRDLLPRGTGIVTRRPLILQLVHVSQEDKRKTTGEENGVEAEEWGKFLHTKNKLYTDFDEIRQEIENETERISGNNKGVSPEPIHLKIFSPNVVNLTLVDLPGMTKVPVGDQPKDIELQIRELILRFISNPNSIILAVTAANTDMATSEALKISREVDPDGRRTLAVITKLDLMDAGTDAMDVLMGRVIPVKLGIIGVVNRSQLDINNKKSVTDSIRDEYAFLQKKYPSLANRNGTKYLARTLNRLLMHHIRDCLPELKTRINVLAAQYQSLLN...
3.6.5.5
null
calcium ion transport [GO:0006816]; endocytosis [GO:0006897]; heart contraction [GO:0060047]; intracellular distribution of mitochondria [GO:0048312]; membrane fusion [GO:0061025]; mitochondrial fission [GO:0000266]; mitochondrial fragmentation involved in apoptotic process [GO:0043653]; mitochondrial membrane fission ...
brush border [GO:0005903]; clathrin-coated pit [GO:0005905]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; microtubule [GO:0005874]...
GTP binding [GO:0005525]; GTP-dependent protein binding [GO:0030742]; GTPase activator activity [GO:0005096]; GTPase activity [GO:0003924]; identical protein binding [GO:0042802]; lipid binding [GO:0008289]; microtubule binding [GO:0008017]; protein homodimerization activity [GO:0042803]; small GTPase binding [GO:00312...
PF01031;PF00350;PF02212;
1.20.120.1240;3.40.50.300;
TRAFAC class dynamin-like GTPase superfamily, Dynamin/Fzo/YdjA family
PTM: Phosphorylation/dephosphorylation events on two sites near the GED domain regulate mitochondrial fission (PubMed:17301055, PubMed:17553808, PubMed:18695047, PubMed:18838687, PubMed:23283981, PubMed:29478834, PubMed:33850055). Phosphorylation on Ser-637 by CAMK1 and PKA inhibits the GTPase activity, leading to a de...
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:11514614, ECO:0000269|PubMed:12618434, ECO:0000269|PubMed:9786947}. Golgi apparatus {ECO:0000269|PubMed:20688057, ECO:0000269|PubMed:9348079, ECO:0000269|PubMed:9570752}. Endomembrane system {ECO:0000269|PubMed:11514614, ECO:0000269|PubMed:9348079, ECO:000026...
CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.5; Evidence={ECO:0000269|PubMed:23977156, ECO:0000269|PubMed:9422767};
null
null
null
null
FUNCTION: Functions in mitochondrial and peroxisomal division (PubMed:11514614, PubMed:12499366, PubMed:17301055, PubMed:17460227, PubMed:17553808, PubMed:18695047, PubMed:18838687, PubMed:19342591, PubMed:19411255, PubMed:19638400, PubMed:23283981, PubMed:23530241, PubMed:23921378, PubMed:26992161, PubMed:27145208, Pu...
Homo sapiens (Human)
O00442
RTCA_HUMAN
MAGPRVEVDGSIMEGGGQILRVSTALSCLLGLPLRVQKIRAGRSTPGLRPQHLSGLEMIRDLCDGQLEGAEIGSTEITFTPEKIKGGIHTADTKTAGSVCLLMQVSMPCVLFAASPSELHLKGGTNAEMAPQIDYTVMVFKPIVEKFGFIFNCDIKTRGYYPKGGGEVIVRMSPVKQLNPINLTERGCVTKIYGRAFVAGVLPFKVAKDMAAAAVRCIRKEIRDLYVNIQPVQEPKDQAFGNGNGIIIIAETSTGCLFAGSSLGKRGVNADKVGIEAAEMLLANLRHGGTVDEYLQDQLIVFMALANGVSRIKTGPVTLH...
6.5.1.4
null
negative regulation of optical nerve axon regeneration [GO:1905592]; RNA processing [GO:0006396]
nucleoplasm [GO:0005654]; nucleus [GO:0005634]
ATP binding [GO:0005524]; RNA binding [GO:0003723]; RNA-3'-phosphate cyclase activity [GO:0003963]
PF01137;PF05189;
3.65.10.20;3.30.360.20;
RNA 3'-terminal cyclase family, Type 1 subfamily
null
SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:9184239}.
CATALYTIC ACTIVITY: Reaction=a 3'-end 3'-phospho-ribonucleotide-RNA + ATP = a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + AMP + diphosphate; Xref=Rhea:RHEA:23976, Rhea:RHEA-COMP:10463, Rhea:RHEA-COMP:10464, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:83062, ChEBI:CHEBI:83064, ChEBI:CHEBI:456215; EC=6.5.1.4; Ev...
null
null
null
null
FUNCTION: Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA (PubMed:9184239). The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydro...
Homo sapiens (Human)
O00443
P3C2A_HUMAN
MAQISSNSGFKECPSSHPEPTRAKDVDKEEALQMEAEALAKLQKDRQVTDNQRGFELSSSTRKKAQVYNKQDYDLMVFPESDSQKRALDIDVEKLTQAELEKLLLDDSFETKKTPVLPVTPILSPSFSAQLYFRPTIQRGQWPPGLPGPSTYALPSIYPSTYSKQAAFQNGFNPRMPTFPSTEPIYLSLPGQSPYFSYPLTPATPFHPQGSLPIYRPVVSTDMAKLFDKIASTSEFLKNGKARTDLEITDSKVSNLQVSPKSEDISKFDWLDLDPLSKPKVDNVEVLDHEEEKNVSSLLAKDPWDAVLLEERSTANCHLE...
2.7.1.137; 2.7.1.153; 2.7.1.154
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:10805725, ECO:0000269|PubMed:9337861}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:10805725, ECO:0000269|PubMed:9337861}; Note=Ca(2+) or Mg(2+). Mn(2+) cannot be used. {ECO:0000269|PubMed:10805725, ECO:0000269|PubMed:93378...
cell migration [GO:0016477]; clathrin coat assembly [GO:0048268]; endocytosis [GO:0006897]; epidermal growth factor receptor signaling pathway [GO:0007173]; exocytosis [GO:0006887]; insulin receptor signaling pathway [GO:0008286]; membrane organization [GO:0061024]; phosphatidylinositol biosynthetic process [GO:0006661...
clathrin-coated vesicle [GO:0030136]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; phosphatidylinositol 3-kinase complex [GO:0005942]; plasma membrane [GO:0005886]; trans-Golgi ne...
1-phosphatidylinositol-3-kinase activity [GO:0016303]; 1-phosphatidylinositol-4,5-bisphosphate 3-kinase activity [GO:0046934]; 1-phosphatidylinositol-4-phosphate 3-kinase activity [GO:0035005]; ATP binding [GO:0005524]; clathrin binding [GO:0030276]; phosphatidylinositol binding [GO:0035091]
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
PTM: Phosphorylated upon insulin stimulation; which may lead to enzyme activation (By similarity). Phosphorylated on Ser-259 during mitosis and upon UV irradiation; which does not change enzymatic activity but leads to proteasomal degradation. Ser-259 phosphorylation may be mediated by CDK1 or JNK, depending on the phy...
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10766823, ECO:0000269|PubMed:11239472, ECO:0000269|PubMed:17038310}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000269|PubMed:10766823, ECO:0000269|PubMed:11239472}. Nucleus {ECO:0000269|PubMed:11606566}. Cytoplasm {ECO:0000269|PubMed:11606566, ECO:0000269...
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...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=122 uM for PtdIns (in the absence of phosphatidylserine) {ECO:0000269|PubMed:9337861}; KM=64 uM for PtdIns (in the presence of phosphatidylserine) {ECO:0000269|PubMed:9337861}; KM=25 uM for PtdIns4P (in the presence of phosphatidylserine) {ECO:0000269|PubMed:933786...
null
null
null
FUNCTION: Generates phosphatidylinositol 3-phosphate (PtdIns3P) and phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) that act as second messengers. Has a role in several intracellular trafficking events. Functions in insulin signaling and secretion. Required for translocation of the glucose transporter SLC2A4/GLUT...
Homo sapiens (Human)
O00444
PLK4_HUMAN
MATCIGEKIEDFKVGNLLGKGSFAGVYRAESIHTGLEVAIKMIDKKAMYKAGMVQRVQNEVKIHCQLKHPSILELYNYFEDSNYVYLVLEMCHNGEMNRYLKNRVKPFSENEARHFMHQIITGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLATQLKMPHEKHYTLCGTPNYISPEIATRSAHGLESDVWSLGCMFYTLLIGRPPFDTDTVKNTLNKVVLADYEMPSFLSIEAKDLIHQLLRRNPADRLSLSSVLDHPFMSRNSSTKSKDLGTVEDSIDSGHATISTAITASSSTSISGSLFDKRRLLIGQPLPN...
2.7.11.21
null
centriole replication [GO:0007099]; cilium assembly [GO:0060271]; de novo centriole assembly involved in multi-ciliated epithelial cell differentiation [GO:0098535]; mitotic spindle organization [GO:0007052]; positive regulation of centriole replication [GO:0046601]; protein phosphorylation [GO:0006468]; trophoblast gi...
centriole [GO:0005814]; centrosome [GO:0005813]; cleavage furrow [GO:0032154]; cytosol [GO:0005829]; deuterosome [GO:0098536]; kinetochore [GO:0000776]; nucleolus [GO:0005730]; procentriole [GO:0120098]; procentriole replication complex [GO:0120099]; spindle pole [GO:0000922]; XY body [GO:0001741]
ATP binding [GO:0005524]; identical protein binding [GO:0042802]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
PF00069;PF18190;PF18409;
2.40.50.930;3.30.1120.120;3.30.1120.130;1.10.510.10;
Protein kinase superfamily, Ser/Thr protein kinase family, CDC5/Polo subfamily
PTM: Acetylation by KAT2A and KAT2B impairs kinase activity by shifting the kinase to an inactive conformation. {ECO:0000269|PubMed:27796307}.; PTM: Ubiquitinated; leading to its degradation by the proteasome. {ECO:0000250}.; PTM: Tyrosine-phosphorylated by TEC. {ECO:0000269|PubMed:11489907}.
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:22020124, ECO:0000269|PubMed:27246242, ECO:0000269|PubMed:27796307}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q64702}. Cleavage furrow {ECO:0000250|UniProtKB:Q64702}. Cytoplasm, cytoskeleton, microtu...
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=2.7.11.21; Evidence={ECO:0000269|PubMed:16244668, ECO:00002...
null
null
null
null
FUNCTION: Serine/threonine-protein kinase that plays a central role in centriole duplication. Able to trigger procentriole formation on the surface of the parental centriole cylinder, leading to the recruitment of centriole biogenesis proteins such as SASS6, CENPJ/CPAP, CCP110, CEP135 and gamma-tubulin. When overexpres...
Homo sapiens (Human)
O00445
SYT5_HUMAN
MFPEPPTPGPPSPDTPPDSSRISHGPVPPWALATIVLVSGLLIFSCCFCLYRKSCRRRTGKKSQAQAQVHLQEVKGLGQSYIDKVQPEVEELEPAPSGPGQQVADKHELGRLQYSLDYDFQSGQLLVGILQAMGLAALDLGGSSDPYVRVYLLPDKRRRYETKVHRQTLNPHFGETFAFKVPYVELGGRVLVMAVYDFDRFSRNDAIGEVRVPMSSVDLGRPVQAWRELQAAPREEQEKLGDICFSLRYVPTAGKLTVIVLEAKNLKKMDVGGLSDPYVKVHLLQGGKKVRKKKTTIKKNTLNPYYNEAFSFEVPCDQVQ...
null
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00041, ECO:0000269|PubMed:27793683}; Note=Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2 domains. {ECO:0000269|PubMed:15057824};
calcium ion-regulated exocytosis of neurotransmitter [GO:0048791]; cellular response to calcium ion [GO:0071277]; chemical synaptic transmission [GO:0007268]; regulation of calcium ion-dependent exocytosis [GO:0017158]; regulation of dopamine secretion [GO:0014059]; synaptic vesicle endocytosis [GO:0048488]
axon [GO:0030424]; dense core granule [GO:0031045]; exocytic vesicle [GO:0070382]; neuronal cell body [GO:0043025]; neuronal dense core vesicle membrane [GO:0099012]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; proximal neuron projection [GO:1990769]; recycling endosome membrane [GO:0055...
calcium ion binding [GO:0005509]; calcium-dependent phospholipid binding [GO:0005544]; clathrin binding [GO:0030276]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; phosphatidylserine binding [GO:0001786]; protein heterodimerization activity [GO:0046982]; syntaxin binding [GO:0019905]
PF00168;
2.60.40.150;
Synaptotagmin family
null
SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Recycling endosome membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Note=In mast cells, localizes to the endocytic recycling compartment. {ECO:0000250}.
null
null
null
null
null
FUNCTION: May be involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain or may serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. Regulates the Ca(2+)-dependent secretion of norepinephrine in PC12 cells. Required for export fro...
Homo sapiens (Human)
O00451
GFRA2_HUMAN
MILANVFCLFFFLDETLRSLASPSSLQGPELHGWRPPVDCVRANELCAAESNCSSRYRTLRQCLAGRDRNTMLANKECQAALEVLQESPLYDCRCKRGMKKELQCLQIYWSIHLGLTEGEEFYEASPYEPVTSRLSDIFRLASIFSGTGADPVVSAKSNHCLDAAKACNLNDNCKKLRSSYISICNREISPTERCNRRKCHKALRQFFDRVPSEYTYRMLFCSCQDQACAERRRQTILPSCSYEDKEKPNCLDLRGVCRTDHLCRSRLADFHANCRASYQTVTSCPADNYQACLGSYAGMIGFDMTPNYVDSSPTGIVVS...
null
null
glial cell-derived neurotrophic factor receptor signaling pathway [GO:0035860]; nervous system development [GO:0007399]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]
external side of plasma membrane [GO:0009897]; extrinsic component of membrane [GO:0019898]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]
glial cell-derived neurotrophic factor receptor activity [GO:0016167]; heparan sulfate binding [GO:1904399]
PF02351;
1.10.220.110;
GDNFR family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O08842}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:O08842}.
null
null
null
null
null
FUNCTION: Receptor for neurturin (NRTN), a growth factor that supports the survival of sympathetic neurons (PubMed:10829012, PubMed:29414779, PubMed:31535977, PubMed:9182803). NRTN-binding leads to autophosphorylation and activation of the RET receptor (PubMed:31535977). Also able to mediate GDNF signaling through the ...
Homo sapiens (Human)
O00453
LST1_HUMAN
MLSRNDDICIYGGLGLGGLLLLAVVLLSACLCWLHRRVKRLERSWAQGSSEQELHYASLQRLPVPSSEGPDLRGRDKRGTKEDPRADYACIAENKPT
null
null
anatomical structure morphogenesis [GO:0009653]; cell morphogenesis [GO:0000902]; dendrite development [GO:0016358]; immune response [GO:0006955]; negative regulation of lymphocyte proliferation [GO:0050672]; regulation of cell shape [GO:0008360]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; membrane [GO:0016020]; plasma membrane [GO:0005886]
null
PF05083;
null
LST1 family
null
SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. Golgi apparatus membrane; Single-pass membrane protein. Endomembrane system; Single-pass membrane protein. Note=Also detected in a perinuclear region corresponding to the localization of the Golgi apparatus and throughout the cytoplasm.
null
null
null
null
null
FUNCTION: Possible role in modulating immune responses. Induces morphological changes including production of filopodia and microspikes when overexpressed in a variety of cell types and may be involved in dendritic cell maturation. Isoform 1 and isoform 2 have an inhibitory effect on lymphocyte proliferation. {ECO:0000...
Homo sapiens (Human)
O00459
P85B_HUMAN
MAGPEGFQYRALYPFRRERPEDLELLPGDVLVVSRAALQALGVAEGGERCPQSVGWMPGLNERTRQRGDFPGTYVEFLGPVALARPGPRPRGPRPLPARPRDGAPEPGLTLPDLPEQFSPPDVAPPLLVKLVEAIERTGLDSESHYRPELPAPRTDWSLSDVDQWDTAALADGIKSFLLALPAPLVTPEASAEARRALREAAGPVGPALEPPTLPLHRALTLRFLLQHLGRVASRAPALGPAVRALGATFGPLLLRAPPPPSSPPPGGAPDGSEPSPDFPALLVEKLLQEHLEEQEVAPPALPPKPPKAKPASTVLANGG...
null
null
B cell differentiation [GO:0030183]; cellular response to insulin stimulus [GO:0032869]; immune response [GO:0006955]; insulin receptor signaling pathway [GO:0008286]; intracellular glucose homeostasis [GO:0001678]; negative regulation of MAPK cascade [GO:0043409]; phosphatidylinositol 3-kinase/protein kinase B signal ...
cytosol [GO:0005829]; focal adhesion [GO:0005925]; nucleus [GO:0005634]; phosphatidylinositol 3-kinase complex [GO:0005942]; phosphatidylinositol 3-kinase complex, class IA [GO:0005943]
1-phosphatidylinositol-3-kinase regulator activity [GO:0046935]; phosphatidylinositol 3-kinase regulatory subunit binding [GO:0036312]; phosphotyrosine residue binding [GO:0001784]; protein heterodimerization activity [GO:0046982]; protein phosphatase binding [GO:0019903]; receptor tyrosine kinase binding [GO:0030971]
PF16454;PF00620;PF00017;
1.10.287.1490;1.10.555.10;3.30.505.10;2.30.30.40;
PI3K p85 subunit family
PTM: Phosphorylated in response to signaling from activated receptor-type protein kinases (PubMed:19690332, PubMed:20068231). Dephosphorylated by PTPRJ (PubMed:18348712). Dephosphorylated at Tyr-655 by PTPN13. Phosphorylation of Tyr-655 impairs while its dephosphorylation promotes interaction with FBXL2 and SCF(FBXL2)-...
null
null
null
null
null
null
FUNCTION: Regulatory subunit of phosphoinositide-3-kinase (PI3K), a kinase that phosphorylates PtdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, a...
Homo sapiens (Human)
O00461
GOLI4_HUMAN
MGNGMCSRKQKRIFQTLLLLTVVFGFLYGAMLYYELQTQLRKAEAVALKYQQHQESLSAQLQVVYEHRSRLEKSLQKERLEHKKAKEDFLVYKLEAQETLNKGRQDSNSRYSALNVQHQMLKSQHEELKKQHSDLEEEHRKQGEDFSRTFNDHKQKYLQLQQEKEQELSKLKETVYNLREENRQLRKAHQDIHTQLQDVKQQHKNLLSEHEQLVVTLEDHKSALAAAQTQVAEYKQLKDTLNRIPSLRKPDPAEQQNVTQVAHSPQGYNTAREKPTREVQEVSRNNDVWQNHEAVPGRAEDTKLYAPTHKEAEFQAPPEP...
null
null
null
cis-Golgi network [GO:0005801]; endocytic vesicle [GO:0030139]; endosome membrane [GO:0010008]; Golgi apparatus [GO:0005794]; Golgi cisterna membrane [GO:0032580]; Golgi lumen [GO:0005796]; Golgi membrane [GO:0000139]; membrane [GO:0016020]; transport vesicle [GO:0030133]
null
null
null
GOLIM4 family
PTM: Phosphorylated probably by c-AMP-dependent kinases in its lumenal part. {ECO:0000269|PubMed:9201717}.; PTM: O-glycosylated; modified by sialic acid residues. {ECO:0000250}.; PTM: N-glycosylated; N-glycans are probably of the complex type and modified by sialic acid residues. {ECO:0000269|PubMed:9201717}.
SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein. Endosome membrane; Single-pass type II membrane protein. Membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Note=Localizes to cis and medial Golgi cisternae. Probably cycles between early Golgi and distal compartments li...
null
null
null
null
null
FUNCTION: Plays a role in endosome to Golgi protein trafficking; mediates protein transport along the late endosome-bypass pathway from the early endosome to the Golgi. {ECO:0000269|PubMed:15331763}.
Homo sapiens (Human)
O00462
MANBA_HUMAN
MRLHLLLLLALCGAGTTAAELSYSLRGNWSICNGNGSLELPGAVPGCVHSALFQQGLIQDSYYRFNDLNYRWVSLDNWTYSKEFKIPFEISKWQKVNLILEGVDTVSKILFNEVTIGETDNMFNRYSFDITNVVRDVNSIELRFQSAVLYAAQQSKAHTRYQVPPDCPPLVQKGECHVNFVRKEQCSFSWDWGPSFPTQGIWKDVRIEAYNICHLNYFTFSPIYDKSAQEWNLEIESTFDVVSSKPVGGQVIVAIPKLQTQQTYSIELQPGKRIVELFVNISKNITVETWWPHGHGNQTGYNMTVLFELDGGLNIEKSAK...
3.2.1.25
null
glycoprotein catabolic process [GO:0006516]; oligosaccharide catabolic process [GO:0009313]; protein modification process [GO:0036211]
azurophil granule membrane [GO:0035577]; lysosomal lumen [GO:0043202]; plasma membrane [GO:0005886]
beta-mannosidase activity [GO:0004567]; mannose binding [GO:0005537]
PF02836;PF17753;PF17786;
2.60.120.260;3.20.20.80;2.60.40.10;
Glycosyl hydrolase 2 family
null
SUBCELLULAR LOCATION: Lysosome {ECO:0000305}.
CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal, non-reducing beta-D-mannose residues in beta-D-mannosides.; EC=3.2.1.25; Evidence={ECO:0000305|PubMed:12890191, ECO:0000305|PubMed:16904924, ECO:0000305|PubMed:18565776, ECO:0000305|PubMed:30552791};
null
PATHWAY: Glycan metabolism; N-glycan degradation. {ECO:0000269|PubMed:12890191, ECO:0000269|PubMed:30552791}.
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.5-5. {ECO:0000269|PubMed:30552791};
null
FUNCTION: Exoglycosidase that cleaves the single beta-linked mannose residue from the non-reducing end of all N-linked glycoprotein oligosaccharides. {ECO:0000305|PubMed:12890191, ECO:0000305|PubMed:30552791}.
Homo sapiens (Human)
O00463
TRAF5_HUMAN
MAYSEEHKGMPCGFIRQNSGNSISLDFEPSIEYQFVERLEERYKCAFCHSVLHNPHQTGCGHRFCQHCILSLRELNTVPICPVDKEVIKSQEVFKDNCCKREVLNLYVYCSNAPGCNAKVILGRYQDHLQQCLFQPVQCSNEKCREPVLRKDLKEHLSASCQFRKEKCLYCKKDVVVINLQNHEENLCPEYPVFCPNNCAKIILKTEVDEHLAVCPEAEQDCPFKHYGCAVTDKRRNLQQHEHSALREHMRLVLEKNVQLEEQISDLHKSLEQKESKIQQLAETIKKLEKEFKQFAQLFGKNGSFLPNIQVFASHIDKSA...
null
null
apoptotic process [GO:0006915]; interleukin-17-mediated signaling pathway [GO:0097400]; mRNA stabilization [GO:0048255]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of DNA-binding transcription factor...
CD40 receptor complex [GO:0035631]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]
identical protein binding [GO:0042802]; thioesterase binding [GO:0031996]; tumor necrosis factor receptor binding [GO:0005164]; ubiquitin protein ligase binding [GO:0031625]; zinc ion binding [GO:0008270]
PF21355;PF21363;PF02176;
3.30.40.10;
TNF receptor-associated factor family, A subfamily
PTM: Ubiquitinated at Lys-318 by the SCF(FBXL2) complex, leading to its degradation by the proteasome. {ECO:0000250|UniProtKB:P70191}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:15121867}. Cytoplasm, cytosol {ECO:0000269|PubMed:15121867}.
null
null
null
null
null
FUNCTION: Adapter protein and signal transducer that links members of the tumor necrosis factor receptor family to different signaling pathways by association with the receptor cytoplasmic domain and kinases. Mediates activation of NF-kappa-B and probably JNK. Seems to be involved in apoptosis. Plays a role in mediatin...
Homo sapiens (Human)
O00468
AGRIN_HUMAN
MAGRSHPGPLRPLLPLLVVAACVLPGAGGTCPERALERREEEANVVLTGTVEEILNVDPVQHTYSCKVRVWRYLKGKDLVARESLLDGGNKVVISGFGDPLICDNQVSTGDTRIFFVNPAPPYLWPAHKNELMLNSSLMRITLRNLEEVEFCVEDKPGTHFTPVPPTPPDACRGMLCGFGAVCEPNAEGPGRASCVCKKSPCPSVVAPVCGSDASTYSNECELQRAQCSQQRRIRLLSRGPCGSRDPCSNVTCSFGSTCARSADGLTASCLCPATCRGAPEGTVCGSDGADYPGECQLLRRACARQENVFKKFDGPCDPC...
null
null
clustering of voltage-gated sodium channels [GO:0045162]; G protein-coupled acetylcholine receptor signaling pathway [GO:0007213]; neuromuscular junction development [GO:0007528]; positive regulation of filopodium assembly [GO:0051491]; positive regulation of GTPase activity [GO:0043547]; positive regulation of synapti...
basement membrane [GO:0005604]; collagen-containing extracellular matrix [GO:0062023]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; Golgi lumen [GO:0005796]; lysosomal lumen [GO:0043202]; plasma membrane [GO:0005886]; synapse [GO:0045202]
calcium ion binding [GO:0005509]; chondroitin sulfate binding [GO:0035374]; dystroglycan binding [GO:0002162]; heparan sulfate proteoglycan binding [GO:0043395]; laminin binding [GO:0043236]; sialic acid binding [GO:0033691]; structural constituent of cytoskeleton [GO:0005200]
PF00008;PF00050;PF07648;PF00053;PF00054;PF03146;PF01390;
2.40.50.120;2.60.120.200;3.30.60.30;2.10.25.10;3.30.70.960;
null
PTM: Contains heparan and chondroitin sulfate chains and alpha-dystroglycan as well as N-linked and O-linked oligosaccharides. Glycosaminoglycans (GAGs), present in the N-terminal 110 kDa fragment, are required for induction of filopodia in hippocampal neurons. The first cluster (Gly/Ser-rich) for GAG attachment contai...
SUBCELLULAR LOCATION: [Isoform 1]: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:20551380}. Note=Synaptic basal lamina at the neuromuscular junction. {ECO:0000250|UniProtKB:P31696}.; SUBCELLULAR LOCATION: [Isoform 2]: Synapse {ECO:0000250|UniProtKB:A2ASQ1}. Cell membrane {ECO:0000250|UniProtKB...
null
null
null
null
null
FUNCTION: [Isoform 1]: Heparan sulfate basal lamina glycoprotein that plays a central role in the formation and the maintenance of the neuromuscular junction (NMJ) and directs key events in postsynaptic differentiation. Component of the AGRN-LRP4 receptor complex that induces the phosphorylation and activation of MUSK....
Homo sapiens (Human)
O00469
PLOD2_HUMAN
MGGCTVKPQLLLLALVLHPWNPCLGADSEKPSSIPTDKLLVITVATKESDGFHRFMQSAKYFNYTVKVLGQGEEWRGGDGINSIGGGQKVRLMKEVMEHYADQDDLVVMFTECFDVIFAGGPEEVLKKFQKANHKVVFAADGILWPDKRLADKYPVVHIGKRYLNSGGFIGYAPYVNRIVQQWNLQDNDDDQLFYTKVYIDPLKREAINITLDHKCKIFQTLNGAVDEVVLKFENGKARAKNTFYETLPVAINGNGPTKILLNYFGNYVPNSWTQDNGCTLCEFDTVDLSAVDVHPNVSIGVFIEQPTPFLPRFLDILLT...
1.14.11.4
COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250|UniProtKB:P24802}; COFACTOR: Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000250|UniProtKB:P24802};
hydroxylysine biosynthetic process [GO:0046947]; peptidyl-lysine hydroxylation [GO:0017185]; protein modification process [GO:0036211]; response to hypoxia [GO:0001666]
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; rough endoplasmic reticulum membrane [GO:0030867]
iron ion binding [GO:0005506]; L-ascorbic acid binding [GO:0031418]; procollagen-lysine 5-dioxygenase activity [GO:0008475]
PF03171;
2.60.120.620;
null
null
SUBCELLULAR LOCATION: Rough endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side.
CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-lysyl-[collagen] + O2 = (5R)-5-hydroxy-L-lysyl-[collagen] + CO2 + succinate; Xref=Rhea:RHEA:16569, Rhea:RHEA-COMP:12751, Rhea:RHEA-COMP:12752, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:29969, ChEBI:CHEBI:30031, ChEBI:CHEBI:133442; EC=1.14.11.4; ...
null
null
null
null
FUNCTION: Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links. {ECO:0000250|UniProtKB:P24802}.
Homo sapiens (Human)
O00470
MEIS1_HUMAN
MAQRYDDLPHYGGMDGVGIPSTMYGDPHAARSMQPVHHLNHGPPLHSHQYPHTAHTNAMAPSMGSSVNDALKRDKDAIYGHPLFPLLALIFEKCELATCTPREPGVAGGDVCSSESFNEDIAVFAKQIRAEKPLFSSNPELDNLMIQAIQVLRFHLLELEKVHELCDNFCHRYISCLKGKMPIDLVIDDREGGSKSDSEDITRSANLTDQPSWNRDHDDTASTRSGGTPGPSSGGHTSHSGDNSSEQGDGLDNSVASPSTGDDDDPDKDKKRHKKRGIFPKVATNIMRAWLFQHLTHPYPSEEQKKQLAQDTGLTILQVN...
null
null
angiogenesis [GO:0001525]; animal organ morphogenesis [GO:0009887]; brain development [GO:0007420]; cell growth involved in cardiac muscle cell development [GO:0061049]; definitive hemopoiesis [GO:0060216]; embryonic pattern specification [GO:0009880]; eye development [GO:0001654]; hemopoiesis [GO:0030097]; lens morpho...
chromatin [GO:0000785]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667]
chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
PF05920;PF16493;
1.10.10.60;
TALE/MEIS homeobox family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
null
null
null
null
null
FUNCTION: Acts as a transcriptional regulator of PAX6. Acts as a transcriptional activator of PF4 in complex with PBX1 or PBX2. Required for hematopoiesis, megakaryocyte lineage development and vascular patterning. May function as a cofactor for HOXA7 and HOXA9 in the induction of myeloid leukemias. {ECO:0000269|PubMed...
Homo sapiens (Human)
O00471
EXOC5_HUMAN
MATTAELFEEPFVADEYIERLVWRTPGGGSRGGPEAFDPKRLLEEFVNHIQELQIMDERIQRKVEKLEQQCQKEAKEFAKKVQELQKSNQVAFQHFQELDEHISYVATKVCHLGDQLEGVNTPRQRAVEAQKLMKYFNEFLDGELKSDVFTNSEKIKEAADIIQKLHLIAQELPFDRFSEVKSKIASKYHDLECQLIQEFTSAQRRGEISRMREVAAVLLHFKGYSHCVDVYIKQCQEGAYLRNDIFEDAGILCQRVNKQVGDIFSNPETVLAKLIQNVFEIKLQSFVKEQLEECRKSDAEQYLKNLYDLYTRTTNLSSK...
null
null
epithelial cell apoptotic process [GO:1904019]; establishment of planar polarity [GO:0001736]; exocytosis [GO:0006887]; Golgi to plasma membrane transport [GO:0006893]; membrane fission [GO:0090148]; mitotic cytokinesis [GO:0000281]; non-motile cilium assembly [GO:1905515]; post-Golgi vesicle-mediated transport [GO:000...
cytoplasm [GO:0005737]; cytosol [GO:0005829]; exocyst [GO:0000145]; midbody [GO:0030496]
small GTPase binding [GO:0031267]
PF07393;PF20667;
null
SEC10 family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9119050}. Midbody {ECO:0000269|PubMed:18756269}. Note=Localization at the midbody requires the presence of RALA, EXOC2 and EXOC3. {ECO:0000269|PubMed:18756269}.
null
null
null
null
null
FUNCTION: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.
Homo sapiens (Human)
O00472
ELL2_HUMAN
MAAGGTGGLREEQRYGLSCGRLGQDNITVLHVKLTETAIRALETYQSHKNLIPFRPSIQFQGLHGLVKIPKNDPLNEVHNFNFYLSNVGKDNPQGSFDCIQQTFSSSGASQLNCLGFIQDKITVCATNDSYQMTRERMTQAEEESRNRSTKVIKPGGPYVGKRVQIRKAPQAVSDTVPERKRSTPMNPANTIRKTHSSSTISQRPYRDRVIHLLALKAYKKPELLARLQKDGVNQKDKNSLGAILQQVANLNSKDLSYTLKDYVFKELQRDWPGYSEIDRRSLESVLSRKLNPSQNAAGTSRSESPVCSSRDAVSSPQKR...
null
null
positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; snRNA transcription by RNA polymerase II [GO:0042795]; transcription elongation by RNA polymerase II [GO:0006368]
nucleoplasm [GO:0005654]; transcription elongation factor complex [GO:0008023]
cis-regulatory region sequence-specific DNA binding [GO:0000987]
PF10390;PF07303;
6.10.140.340;1.10.10.2670;
ELL/occludin family
PTM: Ubiquitinated by SIAH1, leading to its degradation by the proteasome. Interaction with AFF4 stabilizes ELL2 and prevents ELL2 ubiquitination. {ECO:0000269|PubMed:22483617}.
SUBCELLULAR LOCATION: Nucleus.
null
null
null
null
null
FUNCTION: Elongation factor component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA. Component of the little elongation complex (LEC), a complex required to re...
Homo sapiens (Human)
O00476
NPT4_HUMAN
MATKTELSPTARESKNAQDMQVDETLIPRKVPSLCSARYGIALVLHFCNFTTIAQNVIMNITMVAMVNSTSPQSQLNDSSEVLPVDSFGGLSKAPKSLPAKSSILGGQFAIWEKWGPPQERSRLCSIALSGMLLGCFTAILIGGFISETLGWPFVFYIFGGVGCVCCLLWFVVIYDDPVSYPWISTSEKEYIISSLKQQVGSSKQPLPIKAMLRSLPIWSICLGCFSHQWLVSTMVVYIPTYISSVYHVNIRDNGLLSALPFIVAWVIGMVGGYLADFLLTKKFRLITVRKIATILGSLPSSALIVSLPYLNSGYITATA...
null
null
glucose-6-phosphate transport [GO:0015760]; monoatomic anion transport [GO:0006820]; monoatomic ion transmembrane transport [GO:0034220]; organic anion transport [GO:0015711]; phosphate ion transport [GO:0006817]; sodium ion transport [GO:0006814]; urate metabolic process [GO:0046415]; urate transport [GO:0015747]; xen...
apical plasma membrane [GO:0016324]; brush border membrane [GO:0031526]; cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]
efflux transmembrane transporter activity [GO:0015562]; organic anion transmembrane transporter activity [GO:0008514]; sodium:phosphate symporter activity [GO:0005436]; toxin transmembrane transporter activity [GO:0019534]; urate transmembrane transporter activity [GO:0015143]; voltage-gated monoatomic anion channel ac...
PF07690;
1.20.1250.20;
Major facilitator superfamily, Sodium/anion cotransporter family
null
SUBCELLULAR LOCATION: [Isoform 1]: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15505377}; Multi-pass membrane protein {ECO:0000269|PubMed:15505377}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000269|PubMed:20810651}; Multi-pass membrane protein {ECO:0000269|PubMed:20810651}.
CATALYTIC ACTIVITY: [Isoform 2]: Reaction=Na(+)(out) + urate(in) = Na(+)(in) + urate(out); Xref=Rhea:RHEA:72383, ChEBI:CHEBI:17775, ChEBI:CHEBI:29101; Evidence={ECO:0000305|PubMed:20810651};
null
null
null
null
FUNCTION: [Isoform 2]: Transports organic anions in a voltage-driven, multispecific, manner, on the apical side of renal proximal tubule (PubMed:20810651). In particular, participates in the secretion of urate from the cell into the lumen (PubMed:20810651). Urate is the end product of purine metabolism (PubMed:20810651...
Homo sapiens (Human)
O00478
BT3A3_HUMAN
MKMASSLAFLLLNFHVSLFLVQLLTPCSAQFSVLGPSGPILAMVGEDADLPCHLFPTMSAETMELRWVSSSLRQVVNVYADGKEVEDRQSAPYRGRTSILRDGITAGKAALRIHNVTASDSGKYLCYFQDGDFYEKALVELKVAALGSDLHIEVKGYEDGGIHLECRSTGWYPQPQIKWSDTKGENIPAVEAPVVADGVGLYAVAASVIMRGSSGGGVSCIIRNSLLGLEKTASISIADPFFRSAQPWIAALAGTLPISLLLLAGASYFLWRQQKEKIALSRETEREREMKEMGYAATEQEISLREKLQEELKWRKIQYM...
null
null
regulation of cytokine production [GO:0001817]; T cell mediated immunity [GO:0002456]; T cell receptor signaling pathway [GO:0050852]
external side of plasma membrane [GO:0009897]; membrane [GO:0016020]; plasma membrane [GO:0005886]
signaling receptor binding [GO:0005102]
PF13765;PF00622;PF07686;
2.60.120.920;2.60.40.10;
Immunoglobulin superfamily, BTN/MOG family
PTM: N-glycosylated. {ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:20610803}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21918970, ECO:0000269|PubMed:22767497}; Single-pass type I membrane protein {ECO:0000269|PubMed:21918970, ECO:0000269|PubMed:22767497}.
null
null
null
null
null
FUNCTION: Plays a role in T-cell responses in the adaptive immune response. {ECO:0000269|PubMed:22767497}.
Homo sapiens (Human)
O00481
BT3A1_HUMAN
MKMASFLAFLLLNFRVCLLLLQLLMPHSAQFSVLGPSGPILAMVGEDADLPCHLFPTMSAETMELKWVSSSLRQVVNVYADGKEVEDRQSAPYRGRTSILRDGITAGKAALRIHNVTASDSGKYLCYFQDGDFYEKALVELKVAALGSDLHVDVKGYKDGGIHLECRSTGWYPQPQIQWSNNKGENIPTVEAPVVADGVGLYAVAASVIMRGSSGEGVSCTIRSSLLGLEKTASISIADPFFRSAQRWIAALAGTLPVLLLLLGGAGYFLWQQQEEKKTQFRKKKREQELREMAWSTMKQEQSTRVKLLEELRWRSIQYA...
null
null
activated T cell proliferation [GO:0050798]; adaptive immune response [GO:0002250]; positive regulation of cytokine production [GO:0001819]; positive regulation of type II interferon production [GO:0032729]; regulation of cytokine production [GO:0001817]; T cell receptor signaling pathway [GO:0050852]
external side of plasma membrane [GO:0009897]; plasma membrane [GO:0005886]
signaling receptor binding [GO:0005102]
PF13765;PF00622;PF07686;
2.60.120.920;2.60.40.10;
Immunoglobulin superfamily, BTN/MOG family
PTM: N-glycosylated. {ECO:0000269|PubMed:20610803, ECO:0000269|PubMed:22846996}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21113407, ECO:0000269|PubMed:21918970, ECO:0000269|PubMed:22767497}; Single-pass type I membrane protein {ECO:0000269|PubMed:21113407, ECO:0000269|PubMed:21918970, ECO:0000269|PubMed:22767497}.
null
null
null
null
null
FUNCTION: Plays a role in T-cell activation and in the adaptive immune response. Regulates the proliferation of activated T-cells. Regulates the release of cytokines and IFNG by activated T-cells. Mediates the response of T-cells toward infected and transformed cells that are characterized by high levels of phosphoryla...
Homo sapiens (Human)
O00482
NR5A2_HUMAN
MSSNSDTGDLQESLKHGLTPIGAGLPDRHGSPIPARGRLVMLPKVETEALGLARSHGEQGQMPENMQVSQFKMVNYSYDEDLEELCPVCGDKVSGYHYGLLTCESCKGFFKRTVQNNKRYTCIENQNCQIDKTQRKRCPYCRFQKCLSVGMKLEAVRADRMRGGRNKFGPMYKRDRALKQQKKALIRANGLKLEAMSQVIQAMPSDLTISSAIQNIHSASKGLPLNHAALPPTDYDRSPFVTSPISMTMPPHGSLQGYQTYGHFPSRAIKSEYPDPYTSSPESIMGYSYMDSYQTSSPASIPHLILELLKCEPDEPQVQA...
null
null
acinar cell differentiation [GO:0090425]; bile acid metabolic process [GO:0008206]; calcineurin-mediated signaling [GO:0097720]; cellular response to leukemia inhibitory factor [GO:1990830]; cholesterol homeostasis [GO:0042632]; embryo development ending in birth or egg hatching [GO:0009792]; homeostatic process [GO:00...
chromatin [GO:0000785]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575]
chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; nuclear receptor activity [GO:00048...
PF00104;PF00105;
3.30.50.10;1.10.565.10;
Nuclear hormone receptor family, NR5 subfamily
PTM: Sumoylated by SUMO1 at Lys-270 during the hepatic acute phase response, leading to promote interaction with GPS2 and prevent N-Cor corepressor complex dissociation. {ECO:0000269|PubMed:20159957}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
null
null
null
null
null
FUNCTION: Nuclear receptor that acts as a key metabolic sensor by regulating the expression of genes involved in bile acid synthesis, cholesterol homeostasis and triglyceride synthesis. Together with the oxysterol receptors NR1H3/LXR-alpha and NR1H2/LXR-beta, acts as an essential transcriptional regulator of lipid meta...
Homo sapiens (Human)
O00483
NDUA4_HUMAN
MLRQIIGQAKKHPSLIPLFVFIGTGATGATLYLLRLALFNPDVCWDRNNPEPWNKLGPNDQYKFYSVNVDYSKLKKERPDF
null
null
cellular respiration [GO:0045333]; mitochondrial electron transport, cytochrome c to oxygen [GO:0006123]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; positive regulation of cytochrome-c oxidase activity [GO:1904960]
mitochondrial inner membrane [GO:0005743]; mitochondrial membrane [GO:0031966]; mitochondrial respiratory chain complex I [GO:0005747]; mitochondrial respiratory chain complex IV [GO:0005751]; mitochondrion [GO:0005739]
NADH dehydrogenase (ubiquinone) activity [GO:0008137]; protein-containing complex binding [GO:0044877]
PF06522;
null
Complex IV NDUFA4 subunit family
null
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:23746447, ECO:0000269|PubMed:30030519}; Single-pass membrane protein {ECO:0000269|PubMed:30030519}.
null
null
null
null
null
FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, comple...
Homo sapiens (Human)
O00487
PSDE_HUMAN
MDRLLRLGGGMPGLGQGPPTDAPAVDTAEQVYISSLALLKMLKHGRAGVPMEVMGLMLGEFVDDYTVRVIDVFAMPQSGTGVSVEAVDPVFQAKMLDMLKQTGRPEMVVGWYHSHPGFGCWLSGVDINTQQSFEALSERAVAVVVDPIQSVKGKVVIDAFRLINANMMVLGHEPRQTTSNLGHLNKPSIQALIHGLNRHYYSITINYRKNELEQKMLLNLHKKSWMEGLTLQDYSEHCKHNESVVKEMLELAKNYNKAVEEEDKMTPEQLAIKNVGKQDPKRHLEEHVDVLMTSNIVQCLAAMLDTVVFK
3.4.19.-
null
double-strand break repair via homologous recombination [GO:0000724]; double-strand break repair via nonhomologous end joining [GO:0006303]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein K63-linked deubiquitination [GO:0070536]; regulation of proteasomal protein catabolic proce...
cytosol [GO:0005829]; cytosolic proteasome complex [GO:0031597]; extracellular region [GO:0005576]; ficolin-1-rich granule lumen [GO:1904813]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; proteasome accessory complex [GO:0022624]; proteasome complex [GO:0000502]; proteasome regulatory particle, lid subcomplex [GO:00...
endopeptidase activator activity [GO:0061133]; K63-linked deubiquitinase activity [GO:0061578]; metal ion binding [GO:0046872]; metal-dependent deubiquitinase activity [GO:0140492]; metallopeptidase activity [GO:0008237]; proteasome binding [GO:0070628]
PF01398;
3.40.140.10;
Peptidase M67A family, PSMD14 subfamily
null
null
null
null
null
null
null
FUNCTION: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose ...
Homo sapiens (Human)