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
O94855
SC24D_HUMAN
MSQQGYVATPPYSQPQPGIGLSPPHYGHYGDPSHTASPTGMMKPAGPLGATATRGMLPPGPPPPGPHQFGQNGAHATGHPPQRFPGPPPVNNVASSHAPYQPSAQSSYPGPISTSSVTQLGSQLSAMQINSYGSGMAPPSQGPPGPLSATSLQTPPRPPQPSILQPGSQVLPPPPTTLNGPGASPLPLPMYRPDGLSGPPPPNAQYQPPPLPGQTLGAGYPPQQANSGPQMAGAQLSYPGGFPGGPAQMAGPPQPQKKLDPDSIPSPIQVIENDRASRGGQVYATNTRGQIPPLVTTDCMIQDQGNASPRFIRCTTYCFP...
null
null
COPII-coated vesicle cargo loading [GO:0090110]; endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; in utero embryonic development [GO:0001701]; intracellular protein transport [GO:0006886]
COPII vesicle coat [GO:0030127]; cytosol [GO:0005829]; endoplasmic reticulum exit site [GO:0070971]; endoplasmic reticulum membrane [GO:0005789]; ER to Golgi transport vesicle membrane [GO:0012507]; intracellular membrane-bounded organelle [GO:0043231]
SNARE binding [GO:0000149]; zinc ion binding [GO:0008270]
PF00626;PF08033;PF04815;PF04811;PF04810;
2.60.40.1670;1.20.120.730;3.40.20.10;3.40.50.410;2.30.30.380;
SEC23/SEC24 family, SEC24 subfamily
null
SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000269|PubMed:10329445}; Peripheral membrane protein {ECO:0000250|UniProtKB:P53992}; Cytoplasmic side {ECO:0000250|UniProtKB:P53992}. Endoplasmic reticulum membrane {ECO:0000305|PubMed:10329445}; Peripheral membrane protein {ECO:0000250|UniP...
null
null
null
null
null
FUNCTION: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules for their transport to the...
Homo sapiens (Human)
O94856
NFASC_HUMAN
MARQPPPPWVHAAFLLCLLSLGGAIEIPMDPSIQNELTQPPTITKQSAKDHIVDPRDNILIECEAKGNPAPSFHWTRNSRFFNIAKDPRVSMRRRSGTLVIDFRSGGRPEEYEGEYQCFARNKFGTALSNRIRLQVSKSPLWPKENLDPVVVQEGAPLTLQCNPPPGLPSPVIFWMSSSMEPITQDKRVSQGHNGDLYFSNVMLQDMQTDYSCNARFHFTHTIQQKNPFTLKVLTTRGVAERTPSFMYPQGTASSQMVLRGMDLLLECIASGVPTPDIAWYKKGGDLPSDKAKFENFNKALRITNVSEEDSGEYFCLASN...
null
null
axon guidance [GO:0007411]; brain development [GO:0007420]; cell-cell adhesion [GO:0098609]; myelination [GO:0042552]; peripheral nervous system development [GO:0007422]
axon [GO:0030424]; axon initial segment [GO:0043194]; ficolin-1-rich granule membrane [GO:0101003]; focal adhesion [GO:0005925]; node of Ranvier [GO:0033268]; paranodal junction [GO:0033010]; plasma membrane [GO:0005886]
cell-cell adhesion mediator activity [GO:0098632]
PF13882;PF00041;PF07679;PF00047;PF13927;
2.60.40.10;
Immunoglobulin superfamily, L1/neurofascin/NgCAM family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:30850329}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 8]: Cell junction, paranodal septate junction {ECO:0000269|PubMed:30124836}.
null
null
null
null
null
FUNCTION: Cell adhesion, ankyrin-binding protein which may be involved in neurite extension, axonal guidance, synaptogenesis, myelination and neuron-glial cell interactions. {ECO:0000250}.
Homo sapiens (Human)
O94864
ST65G_HUMAN
MNLQRYWGEIPISSSQTNRSSFDLLPREFRLVEVHDPPLHQPSANKPKPPTMLDIPSEPCSLTIHTIQLIQHNRRLRNLIATAQAQNQQQTEGVKTEESEPLPSCPGSPPLPDDLLPLDCKNPNAPFQIRHSDPESDFYRGKGEPVTELSWHSCRQLLYQAVATILAHAGFDCANESVLETLTDVAHEYCLKFTKLLRFAVDREARLGQTPFPDVMEQVFHEVGIGSVLSLQKFWQHRIKDYHSYMLQISKQLSEEYERIVNPEKATEDAKPVKIKEEPVSDITFPVSEELEADLASGDQSLPMGVLGAQSERFPSNLEV...
null
null
maintenance of protein location in nucleus [GO:0051457]; positive regulation of DNA-templated transcription [GO:0045893]; regulation of DNA repair [GO:0006282]; regulation of RNA splicing [GO:0043484]
nucleoplasm [GO:0005654]; nucleus [GO:0005634]; SAGA complex [GO:0000124]
protein heterodimerization activity [GO:0046982]; transcription coactivator activity [GO:0003713]
PF07524;
1.10.20.10;
null
PTM: Sumoylated. {ECO:0000269|PubMed:15561718}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11564863}.
null
null
null
null
null
null
Homo sapiens (Human)
O94868
FCSD2_HUMAN
MQPPPRKVKVTQELKNIQVEQMTKLQAKHQAECDLLEDMRTFSQKKAAIEREYAQGMQKLASQYLKRDWPGVKADDRNDYRSMYPVWKSFLEGTMQVAQSRMNICENYKNFISEPARTVRSLKEQQLKRCVDQLTKIQTELQETVKDLAKGKKKYFETEQMAHAVREKADIEAKSKLSLFQSRISLQKASVKLKARRSECNSKATHARNDYLLTLAAANAHQDRYYQTDLVNIMKALDGNVYDHLKDYLIAFSRTELETCQAVQNTFQFLLENSSKVVRDYNLQLFLQENAVFHKPQPFQFQPCDSDTSRQLESETGTTE...
null
null
clathrin-dependent endocytosis [GO:0072583]; membrane organization [GO:0061024]; neuromuscular synaptic transmission [GO:0007274]; positive regulation of actin filament polymerization [GO:0030838]; positive regulation of Arp2/3 complex-mediated actin nucleation [GO:2000601]; protein transport [GO:0015031]; regulation o...
anchoring junction [GO:0070161]; clathrin-coated pit [GO:0005905]; neuromuscular junction [GO:0031594]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]; stereocilium shaft [GO:0120043]
phosphatidylinositol-3,4,5-trisphosphate binding [GO:0005547]; phosphatidylinositol-3,4-bisphosphate binding [GO:0043325]
PF00611;PF00018;PF14604;
1.20.1270.60;2.30.30.40;
null
PTM: Phosphorylated. Phosphorylation on a Ser residue is important for recruitment to the cell membrane and for its role in promoting endocytosis. {ECO:0000269|PubMed:30249660}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q3USJ8}. Cell junction {ECO:0000269|PubMed:14627983}. Membrane, clathrin-coated pit {ECO:0000269|PubMed:29887380, ECO:0000269|PubMed:30249660}. Cell membrane {ECO:0000269|PubMed:14627983, ECO:0000269|PubMed:29887380, ECO:0000269|PubMed:30249660}; Peripheral membran...
null
null
null
null
null
FUNCTION: Adapter protein that plays a role in endocytosis via clathrin-coated pits. Contributes to the internalization of cell surface receptors, such as integrin ITGB1 and transferrin receptor (PubMed:29887380). Promotes endocytosis of EGFR in cancer cells, and thereby contributes to the down-regulation of EGFR signa...
Homo sapiens (Human)
O94874
UFL1_HUMAN
MADAWEEIRRLAADFQRAQFAEATQRLSERNCIEIVNKLIAQKQLEVVHTLDGKEYITPAQISKEMRDELHVRGGRVNIVDLQQVINVDLIHIENRIGDIIKSEKHVQLVLGQLIDENYLDRLAEEVNDKLQESGQVTISELCKTYDLPGNFLTQALTQRLGRIISGHIDLDNRGVIFTEAFVARHKARIRGLFSAITRPTAVNSLISKYGFQEQLLYSVLEELVNSGRLRGTVVGGRQDKAVFVPDIYSRTQSTWVDSFFRQNGYLEFDALSRLGIPDAVSYIKKRYKTTQLLFLKAACVGQGLVDQVEASVEEAISSG...
2.3.2.-
null
DNA damage checkpoint signaling [GO:0000077]; DNA damage response [GO:0006974]; DNA repair [GO:0006281]; erythrocyte differentiation [GO:0030218]; hematopoietic stem cell differentiation [GO:0060218]; negative regulation of apoptotic process [GO:0043066]; negative regulation of IRE1-mediated unfolded protein response [...
cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; mitochondrial outer membrane [GO:0005741]; neuron projection [GO:0043005]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; site of double-strand break [GO:...
protein kinase binding [GO:0019901]; UFM1 ligase activity [GO:0061666]; UFM1 transferase activity [GO:0071568]
PF09743;
null
UFL1 family
PTM: Ubiquitinated, leading to its degradation by the proteasome (PubMed:20164180). Interaction with CDK5RAP3 protects both proteins against ubiquitination and degradation via the proteasome (PubMed:20164180). {ECO:0000269|PubMed:20164180}.; PTM: Phosphorylated at Ser-462 by ATM, enhancing protein ligase activity and p...
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:20018847, ECO:0000269|PubMed:20164180, ECO:0000269|PubMed:20228063, ECO:0000269|PubMed:32160526}. Cytoplasm, cytosol {ECO:0000269|PubMed:20228063, ECO:0000269|PubMed:30886146}. Nucleus {ECO:0000269|PubMed:30886146}. Chromosome {ECO:0000269|PubMed:...
null
null
null
null
null
FUNCTION: E3 protein ligase that mediates ufmylation, the covalent attachment of the ubiquitin-like modifier UFM1 to lysine residues on target proteins, and which plays a key role in reticulophagy (also called ER-phagy) induced in response to endoplasmic reticulum stress (PubMed:20018847, PubMed:20164180, PubMed:202280...
Homo sapiens (Human)
O94875
SRBS2_HUMAN
MSYYQRPFSPSAYSLPASLNSSIVMQHGTSLDSTDTYPQHAQSLDGTTSSSIPLYRSSEEEKRVTVIKAPHYPGIGPVDESGIPTAIRTTVDRPKDWYKTMFKQIHMVHKPDDDTDMYNTPYTYNAGLYNPPYSAQSHPAAKTQTYRPLSKSHSDNSPNAFKDASSPVPPPHVPPPVPPLRPRDRSSTEKHDWDPPDRKVDTRKFRSEPRSIFEYEPGKSSILQHERPASLYQSSIDRSLERPMSSASMASDFRKRRKSEPAVGPPRGLGDQSASRTSPGRVDLPGSSTTLTKSFTSSSPSSPSRAKGGDDSKICPSLCS...
null
null
cell growth involved in cardiac muscle cell development [GO:0061049]; Notch signaling pathway [GO:0007219]
actin cytoskeleton [GO:0015629]; apical plasma membrane [GO:0016324]; dendrite [GO:0030425]; focal adhesion [GO:0005925]; lamellipodium [GO:0030027]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; synapse [GO:0045202]; Z disc [GO:003001...
cytoskeletal anchor activity [GO:0008093]; identical protein binding [GO:0042802]; RNA binding [GO:0003723]; structural constituent of cytoskeleton [GO:0005200]; structural constituent of muscle [GO:0008307]
PF00018;PF14604;PF02208;
2.30.30.40;
null
PTM: Ubiquitinated by CBL. {ECO:0000269|PubMed:12475393}.; PTM: Dephosphorylated by PTPN12. {ECO:0000269|PubMed:18559503}.
SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:16125169, ECO:0000269|PubMed:9211900}. Apical cell membrane {ECO:0000269|PubMed:18559503}. Cell junction, focal adhesion {ECO:0000269|PubMed:18559503}. Cell projection, lamellipodium {ECO:0000269|PubMed:18559503}. Note=Found at the Z-disk sarcomere...
null
null
null
null
null
FUNCTION: Adapter protein that plays a role in the assembling of signaling complexes, being a link between ABL kinases and actin cytoskeleton. Can form complex with ABL1 and CBL, thus promoting ubiquitination and degradation of ABL1. May play a role in the regulation of pancreatic cell adhesion, possibly by acting on W...
Homo sapiens (Human)
O94876
TMCC1_HUMAN
MEPSGSEQLFEDPDPGGKSQDAEARKQTESEQKLSKMTHNALENINVIGQGLKHLFQHQRRRSSVSPHDVQQIQADPEPEMDLESQNACAEIDGVPTHPTALNRVLQQIRVPPKMKRGTSLHSRRGKPEAPKGSPQINRKSGQEMTAVMQSGRPRSSSTTDAPTSSAMMEIACAAAAAAAACLPGEEGTAERIERLEVSSLAQTSSAVASSTDGSIHTDSVDGTPDPQRTKAAIAHLQQKILKLTEQIKIAQTARDDNVAEYLKLANSADKQQAARIKQVFEKKNQKSAQTILQLQKKLEHYHRKLREVEQNGIPRQPKD...
null
null
endoplasmic reticulum organization [GO:0007029]; endosomal transport [GO:0016197]; endosome fission [GO:0140285]; endosome membrane tubulation [GO:0097750]; membrane fission [GO:0090148]
cytosol [GO:0005829]; endomembrane system [GO:0012505]; endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum-endosome membrane contact site [GO:0140284]; rough endoplasmic reticulum [GO:0005791]
identical protein binding [GO:0042802]
PF10267;
null
TEX28 family
null
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:24454821, ECO:0000269|PubMed:30220460}; Multi-pass membrane protein {ECO:0000255}. Note=Specifically localizes to contact sites between the endoplasmic reticulum and endosomes that are spatially and temporally linked to endosome fission. {ECO:0000...
null
null
null
null
null
FUNCTION: Endoplasmic reticulum membrane protein that promotes endoplasmic reticulum-associated endosome fission (PubMed:30220460). Localizes to contact sites between the endoplasmic reticulum and endosomes and acts by promoting recruitment of the endoplasmic reticulum to endosome tubules for fission (PubMed:30220460)....
Homo sapiens (Human)
O94880
PHF14_HUMAN
MDRSSKRRQVKPLAASLLEALDYDSSDDSDFKVGDASDSEGSGNGSEDASKDSGEGSCSDSEENILEEELNEDIKVKEEQLKNSAEEEVLSSEKQLIKMEKKEEEENGERPRKKKEKEKEKEKEKEKEKEREKEKEKATVSENVAASAAATTPATSPPAVNTSPSVPTTTTATEEQVSEPKKWNLRRNRPLLDFVSMEELNDMDDYDSEDDNDWRPTVVKRKGRSASQKEGSDGDNEDDEDEGSGSDEDENDEGNDEDHSSPASEGGCKKKKSKVLSRNSADDEELTNDSLTLSQSKSNEDSLILEKSQNWSSQKMDHIL...
null
null
germinal center B cell differentiation [GO:0002314]; lung alveolus development [GO:0048286]; mesenchymal cell proliferation [GO:0010463]; mesenchymal cell proliferation involved in lung development [GO:0060916]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of mesenchymal cell p...
chromatin [GO:0000785]; chromosome [GO:0005694]; cytoplasm [GO:0005737]; nucleus [GO:0005634]
histone binding [GO:0042393]; histone reader activity [GO:0140566]; zinc ion binding [GO:0008270]
PF00628;PF13831;PF13832;
2.30.30.1150;3.30.40.10;
null
null
SUBCELLULAR LOCATION: [Isoform 1]: Nucleus {ECO:0000269|PubMed:23688586}. Chromosome {ECO:0000269|PubMed:23688586}. Note=Mainly localized in the nucleus of interphase cells. In mitotic cells, colocalizes with condensed chromatin during metaphase and anaphase. {ECO:0000269|PubMed:23688586}.; SUBCELLULAR LOCATION: [Isofo...
null
null
null
null
null
FUNCTION: Histone-binding protein (PubMed:23688586). Binds preferentially to unmodified histone H3 but can also bind to a lesser extent to histone H3 trimethylated at 'Lys-9' (H3K9me3) as well as to histone H3 monomethylated at 'Lys-27' (H3K27ac) and trimethylated at 'Lys-27' (H3K27me3) (By similarity). Represses PDGFR...
Homo sapiens (Human)
O94885
SASH1_HUMAN
MEDAGAAGPGPEPEPEPEPEPEPAPEPEPEPKPGAGTSEAFSRLWTDVMGILDGSLGNIDDLAQQYADYYNTCFSDVCERMEELRKRRVSQDLEVEKPDASPTSLQLRSQIEESLGFCSAVSTPEVERKNPLHKSNSEDSSVGKGDWKKKNKYFWQNFRKNQKGIMRQTSKGEDVGYVASEITMSDEERIQLMMMVKEKMITIEEALARLKEYEAQHRQSAALDPADWPDGSYPTFDGSSNCNSREQSDDETEESVKFKRLHKLVNSTRRVRKKLIRVEEMKKPSTEGGEEHVFENSPVLDERSALYSGVHKKPLFFDGS...
null
null
positive regulation of angiogenesis [GO:0045766]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of JUN kinase activity [GO:0043507]; positive regulation of lipopolysaccharide-mediated signaling pathway [GO:0031666]; positive regulation of non-canonical NF-kappaB signal transduction...
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; protein-containing complex [GO:0032991]
G-protein alpha-subunit binding [GO:0001965]; mitogen-activated protein kinase kinase kinase binding [GO:0031435]; molecular adaptor activity [GO:0060090]; protein kinase binding [GO:0019901]
PF00536;PF07647;PF07653;PF12485;
2.30.30.40;1.10.150.50;
null
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23333244}.
null
null
null
null
null
FUNCTION: Is a positive regulator of NF-kappa-B signaling downstream of TLR4 activation. It acts as a scaffold molecule to assemble a molecular complex that includes TRAF6, MAP3K7, CHUK and IKBKB, thereby facilitating NF-kappa-B signaling activation (PubMed:23776175). Regulates TRAF6 and MAP3K7 ubiquitination (PubMed:2...
Homo sapiens (Human)
O94886
CSCL1_HUMAN
MMDSPFLELWQSKAVSIREQLGLGDRPNDSYCYNSAKNSTVLQGVTFGGIPTVLLIDVSCFLFLILVFSIIRRRFWDYGRIALVSEADSESRFQRLSSTSSSGQQDFENELGCCPWLTAIFRLHDDQILEWCGEDAIHYLSFQRHIIFLLVVVSFLSLCVILPVNLSGDLLDKDPYSFGRTTIANLQTDNDLLWLHTIFAVIYLFLTVGFMRHHTQSIKYKEENLVRRTLFITGLPRDARKETVESHFRDAYPTCEVVDVQLCYNVAKLIYLCKEKKKTEKSLTYYTNLQVKTGQRTLINPKPCGQFCCCEVLGCEWEDA...
null
null
null
centriolar satellite [GO:0034451]; extracellular exosome [GO:0070062]; intracellular membrane-bounded organelle [GO:0043231]; lysosomal membrane [GO:0005765]; plasma membrane [GO:0005886]; specific granule membrane [GO:0035579]; tertiary granule membrane [GO:0070821]
calcium-activated cation channel activity [GO:0005227]; mechanosensitive monoatomic ion channel activity [GO:0008381]; nucleic acid binding [GO:0003676]; osmolarity-sensing monoatomic cation channel activity [GO:1990760]
PF14703;PF02714;PF13967;
3.30.70.330;
CSC1 (TC 1.A.17) family
PTM: N-Glycosylated. {ECO:0000269|PubMed:37543036}.
SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:20957757}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:37543036}; Multi-pass membrane protein {ECO:0000255}.
null
null
null
null
null
FUNCTION: Acts as an osmosensitive calcium-permeable cation channel (PubMed:30382938, PubMed:31587869). Mechanosensitive ion channel that converts mechanical stimuli into a flow of ion (PubMed:30382938, PubMed:31587869, PubMed:37543036). {ECO:0000250|UniProtKB:Q91YT8, ECO:0000269|PubMed:30382938, ECO:0000269|PubMed:315...
Homo sapiens (Human)
O94887
FARP2_HUMAN
MGEIEGTYRVLQTAGMRLGAQTPVGVSTLEPGQTLLPRMQEKHLHLRVKLLDNTMEIFDIEPKCDGQVLLTQVWKRLNLVECDYFGMEFQNTQSYWIWLEPMKPIIRQIRRPKNVVLRLAVKFFPPDPGQLQEEYTRYLFALQLKRDLLEERLTCADTTAALLTSHLLQSEIGDYDETLDREHLKVNEYLPGQQHCLEKILEFHQKHVGQTPAESDFQVLEIARKLEMYGIRFHMASDREGTKIQLAVSHMGVLVFQGTTKINTFNWSKVRKLSFKRKRFLIKLHPEVHGPYQDTLEFLLGSRDECKNFWKICVEYHTFF...
null
null
actin cytoskeleton organization [GO:0030036]; cell adhesion [GO:0007155]; hair cycle process [GO:0022405]; neuron remodeling [GO:0016322]; osteoclast differentiation [GO:0030316]; podosome assembly [GO:0071800]; Rac protein signal transduction [GO:0016601]; regulation of integrin activation [GO:0033623]; semaphorin-ple...
cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]
cytoskeletal protein binding [GO:0008092]; guanyl-nucleotide exchange factor activity [GO:0005085]
PF08736;PF09380;PF00373;PF09379;PF00169;PF00621;
1.20.80.10;1.20.900.10;2.30.29.30;
null
null
null
null
null
null
null
null
FUNCTION: Functions as a guanine nucleotide exchange factor that activates RAC1. May have relatively low activity. Plays a role in the response to class 3 semaphorins and remodeling of the actin cytoskeleton. Plays a role in TNFSF11-mediated osteoclast differentiation, especially in podosome rearrangement and reorganiz...
Homo sapiens (Human)
O94888
UBXN7_HUMAN
MAAHGGSAASSALKGLIQQFTTITGASESVGKHMLEACNNNLEMAVTMFLDGGGIAEEPSTSSASVSTVRPHTEEEVRAPIPQKQEILVEPEPLFGAPKRRRPARSIFDGFRDFQTETIRQEQELRNGGAIDKKLTTLADLFRPPIDLMHKGSFETAKECGQMQNKWLMINIQNVQDFACQCLNRDVWSNEAVKNIIREHFIFWQVYHDSEEGQRYIQFYKLGDFPYVSILDPRTGQKLVEWHQLDVSSFLDQVTGFLGEHGQLDGLSSSPPKKCARSESLIDASEDSQLEAAIRASLQETHFDSTQTKQDSRSDEESES...
null
null
proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]
cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; VCP-NPL4-UFD1 AAA ATPase complex [GO:0034098]
RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; ubiquitin binding [GO:0043130]; ubiquitin protein ligase binding [GO:0031625]
PF13899;PF14555;PF00789;
1.10.8.10;3.40.30.10;
null
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22537386}.
null
null
null
null
null
FUNCTION: Ubiquitin-binding adapter that links a subset of NEDD8-associated cullin ring ligases (CRLs) to the segregase VCP/p97, to regulate turnover of their ubiquitination substrates. {ECO:0000269|PubMed:22537386}.
Homo sapiens (Human)
O94892
ZN432_HUMAN
MINAQELLTLEDVTVEFTWEEWQLLGPFQKDLYRDVMLEIYSNLLSMGYQVSKPDALSKLERGEEPWTMEDERHSRICPENNEVDDHLQDHLENQRMLKSVEQYHEHNAFGNTASQTKSLCLFRENHDTFELYIKTLKSNLSLVNQNKSCEINNSTKFSGDGKSFLHGNYEELYSAAKFSVSTKANSTKSQVSKHQRTHEIEKNHVCSECGKAFVKKSQLTDHERVHTGEKPYGCTLCAKVFSRKSRLNEHQRIHKREKSFICSECGKVFTMKSRLIEHQRTHTGEKPYICNECGKGFPGKRNLIVHQRNHTGEKSYICS...
null
null
DNA damage response [GO:0006974]; regulation of transcription by RNA polymerase II [GO:0006357]
nucleoplasm [GO:0005654]; nucleus [GO:0005634]
damaged DNA binding [GO:0003684]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; protein-macromolecule adaptor activity [GO:0030674]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
PF01352;PF00096;
6.10.140.140;3.30.160.60;
Krueppel C2H2-type zinc-finger protein family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:37823600}. Note=Excluded from nucleolus (PubMed:37823600). Responds to DNA damage by relocating to damage sites, this relocation is PAR-dependent (PubMed:37823600). {ECO:0000269|PubMed:37823600}.
null
null
null
null
null
FUNCTION: Homologous recombination repressor that functions as a poly(ADP-ribose) (PAR) reader regulating DNA damage response and PARP inhibition. Once recruited to DNA lesions via DNA-, in a PAR-dependent mechanism, stimulates PARP1 activity (PubMed:37823600). Binds preferentially ssDNA and inhibits EXO1-mediated rese...
Homo sapiens (Human)
O94898
LRIG2_HUMAN
MAPAPLGVPEEQLLGCRSRVLSRLLFIAQTALLLLPAAGAGLCPAPCSCRIPLLDCSRRKLPAPSWRALSGLLPPDTAILDFSHNRLSNWNISLESQTLQEVKMNYNELTEIPYFGEPTSNITLLSLVHNIIPEINAQALQFYPALESLDLSSNIISEIKTSSFPRMQLKYLNLSNNRITTLEAGCFDNLSSSLLVVKLNRNRMSMIPPKIFKLPHLQFLELKRNRIKIVEGLTFQGLDSLRSLKMQRNGISKLKDGAFFGLNNMEELELEHNNLTRVNKGWLYGLRMLQQLYVSQNAIERISPDAWEFCQRLSELDLSY...
null
null
innervation [GO:0060384]; membrane protein ectodomain proteolysis [GO:0006509]; negative regulation of axon regeneration [GO:0048681]; negative regulation of membrane protein ectodomain proteolysis [GO:0051045]; positive regulation of protein localization to cell surface [GO:2000010]; protein localization to cell surfa...
cytoplasm [GO:0005737]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; growth cone [GO:0030426]; intracellular vesicle [GO:0097708]; plasma membrane [GO:0005886]
signaling receptor binding [GO:0005102]
PF07679;PF13927;PF13855;PF01463;
2.60.40.10;3.80.10.10;
null
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15145052}; Single-pass type I membrane protein {ECO:0000269|PubMed:15145052}. Cytoplasm {ECO:0000269|PubMed:15145052}.
null
null
null
null
null
null
Homo sapiens (Human)
O94900
TOX_HUMAN
MDVRFYPPPAQPAAAPDAPCLGPSPCLDPYYCNKFDGENMYMSMTEPSQDYVPASQSYPGPSLESEDFNIPPITPPSLPDHSLVHLNEVESGYHSLCHPMNHNGLLPFHPQNMDLPEITVSNMLGQDGTLLSNSISVMPDIRNPEGTQYSSHPQMAAMRPRGQPADIRQQPGMMPHGQLTTINQSQLSAQLGLNMGGSNVPHNSPSPPGSKSATPSPSSSVHEDEGDDTSKINGGEKRPASDMGKKPKTPKKKKKKDPNEPQKPVSAYALFFRDTQAAIKGQNPNATFGEVSKIVASMWDGLGEEQKQVYKKKTEAAKKE...
null
null
CD4-positive, alpha-beta T cell lineage commitment [GO:0043373]; CD4-positive, CD25-positive, alpha-beta regulatory T cell lineage commitment [GO:0002362]; CD8-positive, alpha-beta T cell lineage commitment [GO:0043375]; cerebral cortex neuron differentiation [GO:0021895]; chromatin organization [GO:0006325]; leukocyte...
nucleus [GO:0005634]
chromatin DNA binding [GO:0031490]
PF00505;
1.10.30.10;
High motility group (HMG) box superfamily
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}.
null
null
null
null
null
FUNCTION: Transcriptional regulator with a major role in neural stem cell commitment and corticogenesis as well as in lymphoid cell development and lymphoid tissue organogenesis (By similarity). Binds to GC-rich DNA sequences in the proximity of transcription start sites and may alter chromatin structure, modifying acc...
Homo sapiens (Human)
O94901
SUN1_HUMAN
MDFSRLHMYSPPQCVPENTGYTYALSSSYSSDALDFETEHKLDPVFDSPRMSRRSLRLATTACTLGDGEAVGADSGTSSAVSLKNRAARTTKQRRSTNKSAFSINHVSRQVTSSGVSHGGTVSLQDAVTRRPPVLDESWIREQTTVDHFWGLDDDGDLKGGNKAAIQGNGDVGAAAATAHNGFSCSNCSMLSERKDVLTAHPAAPGPVSRVYSRDRNQKCYFLLQILRRIGAVGQAVSRTAWSALWLAVVAPGKAASGVFWWLGIGWYQFVTLISWLNVFLLTRCLRNICKFLVLLIPLFLLLAGLSLRGQGNFFSFLPV...
null
null
centrosome localization [GO:0051642]; homologous chromosome pairing at meiosis [GO:0007129]; meiotic attachment of telomere to nuclear envelope [GO:0070197]; nuclear matrix anchoring at nuclear membrane [GO:0090292]; nucleokinesis involved in cell motility in cerebral cortex radial glia guided migration [GO:0021817]; o...
chromosome, telomeric region [GO:0000781]; cytoplasm [GO:0005737]; intracellular membrane-bounded organelle [GO:0043231]; meiotic nuclear membrane microtubule tethering complex [GO:0034993]; nuclear envelope [GO:0005635]; nuclear inner membrane [GO:0005637]; nuclear membrane [GO:0031965]
cytoskeleton-nuclear membrane anchor activity [GO:0140444]; identical protein binding [GO:0042802]; lamin binding [GO:0005521]; protein-membrane adaptor activity [GO:0043495]
PF18580;PF09387;PF07738;
2.60.120.260;
null
PTM: The disulfide bond with KASH domain-containing nesprins is required for stability of the respective LINC complexes under tensile forces. {ECO:0000250|UniProtKB:Q9UH99}.
SUBCELLULAR LOCATION: Nucleus inner membrane {ECO:0000269|PubMed:12958361, ECO:0000269|PubMed:16445915, ECO:0000269|PubMed:17132086, ECO:0000269|PubMed:18845190, ECO:0000269|PubMed:19933576}; Single-pass type II membrane protein {ECO:0000269|PubMed:12958361, ECO:0000269|PubMed:16445915, ECO:0000269|PubMed:17132086, ECO...
null
null
null
null
null
FUNCTION: As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex involved in the connection between the nuclear lamina and the cytoskeleton (PubMed:18039933, PubMed:18396275). The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechani...
Homo sapiens (Human)
O94905
ERLN2_HUMAN
MAQLGAVVAVASSFFCASLFSAVHKIEEGHIGVYYRGGALLTSTSGPGFHLMLPFITSYKSVQTTLQTDEVKNVPCGTSGGVMIYFDRIEVVNFLVPNAVYDIVKNYTADYDKALIFNKIHHELNQFCSVHTLQEVYIELFDQIDENLKLALQQDLTSMAPGLVIQAVRVTKPNIPEAIRRNYELMESEKTKLLIAAQKQKVVEKEAETERKKALIEAEKVAQVAEITYGQKVMEKETEKKISEIEDAAFLAREKAKADAECYTAMKIAEANKLKLTPEYLQLMKYKAIASNSKIYFGKDIPNMFMDSAGSVSKQFEGLA...
null
null
cholesterol metabolic process [GO:0008203]; ERAD pathway [GO:0036503]; negative regulation of cholesterol biosynthetic process [GO:0045541]; negative regulation of fatty acid biosynthetic process [GO:0045717]; regulation of cholesterol biosynthetic process [GO:0045540]; SREBP signaling pathway [GO:0032933]
cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; membrane raft [GO:0045121]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]
cholesterol binding [GO:0015485]; ubiquitin protein ligase binding [GO:0031625]
PF01145;
3.30.479.30;
Band 7/mec-2 family
PTM: Deubiquitinated by USP25; leading to stabilization. {ECO:0000250|UniProtKB:O75477}.
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16835267, ECO:0000269|PubMed:17502376, ECO:0000269|PubMed:19240031}; Single-pass type II membrane protein {ECO:0000269|PubMed:16835267, ECO:0000269|PubMed:17502376, ECO:0000269|PubMed:19240031}. Note=Associated with lipid raft-like domains of the ...
null
null
null
null
null
FUNCTION: Component of the ERLIN1/ERLIN2 complex which mediates the endoplasmic reticulum-associated degradation (ERAD) of inositol 1,4,5-trisphosphate receptors (IP3Rs) such as ITPR1 (PubMed:17502376, PubMed:19240031). Promotes sterol-accelerated ERAD of HMGCR probably implicating an AMFR/gp78-containing ubiquitin lig...
Homo sapiens (Human)
O94906
PRP6_HUMAN
MNKKKKPFLGMPAPLGYVPGLGRGATGFTTRSDIGPARDANDPVDDRHAPPGKRTVGDQMKKNQAADDDDEDLNDTNYDEFNGYAGSLFSSGPYEKDDEEADAIYAALDKRMDERRKERREQREKEEIEKYRMERPKIQQQFSDLKRKLAEVTEEEWLSIPEVGDARNKRQRNPRYEKLTPVPDSFFAKHLQTGENHTSVDPRQTQFGGLNTPYPGGLNTPYPGGMTPGLMTPGTGELDMRKIGQARNTLMDMRLSQVSDSVSGQTVVDPKGYLTDLNSMIPTHGGDINDIKKARLLLKSVRETNPHHPPAWIASARLEE...
null
null
mRNA splicing, via spliceosome [GO:0000398]; positive regulation of miRNA metabolic process [GO:2000630]; positive regulation of primary miRNA processing [GO:2000636]; positive regulation of transcription by RNA polymerase II [GO:0045944]; RNA localization [GO:0006403]; RNA splicing [GO:0008380]; RNA splicing, via tran...
catalytic step 2 spliceosome [GO:0071013]; membrane [GO:0016020]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spliceosomal complex [GO:0005681]; U2-type precatalytic spliceosome [GO:0071005]; U4/U6 x U5 tri-snRNP complex [GO:0046540]; U5 snRNP [GO:0005682]
identical protein binding [GO:0042802]; protein-macromolecule adaptor activity [GO:0030674]; ribonucleoprotein complex binding [GO:0043021]; RNA binding [GO:0003723]
PF06424;PF13432;PF14559;
1.25.40.10;
null
PTM: Phosphorylated by PRP4K during spliceosome assembly. {ECO:0000269|PubMed:20118938}.
SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:10561546, ECO:0000269|PubMed:26912367, ECO:0000269|PubMed:28781166, ECO:0000269|PubMed:34023904}. Nucleus speckle {ECO:0000269|PubMed:21549338}. Note=Localized in splicing speckles. {ECO:0000269|PubMed:21549338}.
null
null
null
null
null
FUNCTION: Involved in pre-mRNA splicing as component of the U4/U6-U5 tri-snRNP complex, one of the building blocks of the spliceosome (PubMed:20118938, PubMed:21549338, PubMed:28781166). Enhances dihydrotestosterone-induced transactivation activity of AR, as well as dexamethasone-induced transactivation activity of NR3...
Homo sapiens (Human)
O94907
DKK1_HUMAN
MMALGAAGATRVFVAMVAAALGGHPLLGVSATLNSVLNSNAIKNLPPPLGGAAGHPGSAVSAAPGILYPGGNKYQTIDNYQPYPCAEDEECGTDEYCASPTRGGDAGVQICLACRKRRKRCMRHAMCCPGNYCKNGICVSSDQNHFRGEIEETITESFGNDHSTLDGYSRRTTLSSKMYHTKGQEGSVCLRSSDCASGLCCARHFWSKICKPVLKEGQVCTKHRRKGSHGLEIFQRCYCGEGLSCRIQKDHHQASNSSRLHTCQRH
null
null
canonical Wnt signaling pathway [GO:0060070]; cell morphogenesis [GO:0000902]; embryonic limb morphogenesis [GO:0030326]; endocardial cushion development [GO:0003197]; endoderm formation [GO:0001706]; face morphogenesis [GO:0060325]; forebrain development [GO:0030900]; hair follicle development [GO:0001942]; heart indu...
early endosome membrane [GO:0031901]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]
co-receptor binding [GO:0039706]; growth factor activity [GO:0008083]; low-density lipoprotein particle receptor binding [GO:0050750]; receptor antagonist activity [GO:0048019]
PF04706;PF21481;PF21479;
2.10.80.10;
Dickkopf family
null
SUBCELLULAR LOCATION: Secreted.
null
null
null
null
null
FUNCTION: Antagonizes canonical Wnt signaling by inhibiting LRP5/6 interaction with Wnt and by forming a ternary complex with the transmembrane protein KREMEN that promotes internalization of LRP5/6 (PubMed:22000856). DKKs play an important role in vertebrate development, where they locally inhibit Wnt regulated proces...
Homo sapiens (Human)
O94910
AGRL1_HUMAN
MARLAAVLWNLCVTAVLVTSATQGLSRAGLPFGLMRRELACEGYPIELRCPGSDVIMVENANYGRTDDKICDADPFQMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAFPDPCPGTYKYLEVQYDCVPYKVEQKVFVCPGTLQKVLEPTSTHESEHQSGAWCKDPLQAGDRIYVMPWIPYRTDTLTEYASWEDYVAARHTTTYRLPNRVDGTGFVVYDGAVFYNKERTRNIVKYDLRTRIKSGETVINTANYHDTSPYRWGGKTDIDLAVDENGLWVIYATEGNNGRLVVSQLNPYTLRFEGTWETGYDKRSASNAFM...
null
null
adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; calcium-mediated signaling using intracellular calcium source [GO:0035584]; cell surface receptor signaling pathway [GO:0007166]; G protein-coupled receptor signaling pathway [GO:0007186]; heterophilic cell-cell adhesion via plasma ...
axon [GO:0030424]; growth cone [GO:0030426]; membrane [GO:0016020]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; presynaptic membrane [GO:0042734]; synapse [GO:0045202]
carbohydrate binding [GO:0030246]; cell adhesion molecule binding [GO:0050839]; G protein-coupled receptor activity [GO:0004930]; latrotoxin receptor activity [GO:0016524]
PF00002;PF16489;PF02140;PF01825;PF02793;PF02354;PF02191;
1.25.40.610;2.60.120.740;2.60.220.50;4.10.1240.10;1.20.1070.10;
G-protein coupled receptor 2 family, Adhesion G-protein coupled receptor (ADGR) subfamily
PTM: Autoproteolytically cleaved into 2 subunits, an extracellular subunit and a seven-transmembrane subunit. This proteolytic processing takes place early in the biosynthetic pathway, either in the endoplasmic reticulum or in the early compartment of the Golgi apparatus (By similarity). {ECO:0000250|UniProtKB:O88917}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:35907405}; Multi-pass membrane protein. Cell projection, axon {ECO:0000250|UniProtKB:O88917}. Cell projection, growth cone {ECO:0000250|UniProtKB:O88917}. Synapse {ECO:0000250|UniProtKB:O88917}. Presynaptic cell membrane {ECO:0000250|UniProtKB:O88917}. Synapse, sy...
null
null
null
null
null
FUNCTION: Calcium-independent receptor of high affinity for alpha-latrotoxin, an excitatory neurotoxin present in black widow spider venom which triggers massive exocytosis from neurons and neuroendocrine cells (PubMed:35907405). Receptor for TENM2 that mediates heterophilic synaptic cell-cell contact and postsynaptic ...
Homo sapiens (Human)
O94911
ABCA8_HUMAN
MRKRKISVCQQTWALLCKNFLKKWRMKRESLMEWLNSLLLLLCLYIYPHSHQVNDFSSLLTMDLGRVDTFNESRFSVVYTPVTNTTQQIMNKVASTPFLAGKEVLGLPDEESIKEFTANYPEEIVRVTFTNTYSYHLKFLLGHGMPAKKEHKDHTAHCYETNEDVYCEVSVFWKEGFVALQAAINAAIIEITTNHSVMEELMSVTGKNMKMHSFIGQSGVITDLYLFSCIISFSSFIYYASVNVTRERKRMKALMTMMGLRDSAFWLSWGLLYAGFIFIMALFLALVIRSTQFIILSGFMVVFSLFLLYGLSLVALAFLM...
7.6.2.-
null
cholesterol efflux [GO:0033344]; cholesterol transport [GO:0030301]; lipid transport [GO:0006869]; positive regulation of cholesterol efflux [GO:0010875]; regulation of cholesterol efflux [GO:0010874]; sphingomyelin biosynthetic process [GO:0006686]; transmembrane transport [GO:0055085]; xenobiotic transport [GO:004290...
basolateral plasma membrane [GO:0016323]; endoplasmic reticulum [GO:0005783]; intracellular membrane-bounded organelle [GO:0043231]; mitochondrial inner membrane [GO:0005743]; plasma membrane [GO:0005886]
ABC-type transporter activity [GO:0140359]; ABC-type xenobiotic transporter activity [GO:0008559]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled transmembrane transporter activity [GO:0042626]; lipid transporter activity [GO:0005319]
PF12698;PF00005;
3.40.50.300;
ABC transporter superfamily, ABCA family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28882873, ECO:0000269|PubMed:29300488}; Multi-pass membrane protein {ECO:0000305}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q8K440}. Note=Predominantly expressed on the sinusoidal plasma membrane. {ECO:0000250|UniProtKB:Q8K440}.
CATALYTIC ACTIVITY: [Isoform 3]: Reaction=ATP + H2O + taurocholate(in) = ADP + H(+) + phosphate + taurocholate(out); Xref=Rhea:RHEA:50052, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36257, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000305|PubMed:29300488}; PhysiologicalDirection=lef...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=30.4 uM for estradiol-beta-glucuronide {ECO:0000269|PubMed:12379217}; KM=0.1 uM for LTC4 {ECO:0000269|PubMed:12379217}; KM=10.3 uM for taurochlorate {ECO:0000269|PubMed:12379217}; KM=5 uM for PAH {ECO:0000269|PubMed:12379217}; KM=0.5 uM for estrone sulfate {ECO:000...
null
null
null
FUNCTION: [Isoform 1]: Catalyzes ATP-dependent import of organic anions such as taurocholate and estrone sulfate (PubMed:12379217). In vitro, also imports ochratoxin A (PubMed:12379217). Also mediates cholesterol efflux independent of apolipoprotein, and plays a role in sphingomyelin production in oligodendrocytes (Pub...
Homo sapiens (Human)
O94913
PCF11_HUMAN
MSEQTPAEAGAAGAREDACRDYQSSLEDLTFNSKPHINMLTILAEENLPFAKEIVSLIEAQTAKAPSSEKLPVMYLMDSIVKNVGREYLTAFTKNLVATFICVFEKVDENTRKSLFKLRSTWDEIFPLKKLYALDVRVNSLDPAWPIKPLPPNVNTSSIHVNPKFLNKSPEEPSTPGTVVSSPSISTPPIVPDIQKNLTQEQLIRQQLLAKQKQLLELQQKKLELELEQAKAQLAVSLSVQQETSNLGPGSAPSKLHVSQIPPMAVKAPHQVPVQSEKSRPGPSLQIQDLKGTNRDPRLNRISQHSHGKDQSHRKEFLMN...
null
null
co-transcriptional mRNA 3'-end processing, cleavage and polyadenylation pathway [GO:0180010]; mRNA polyadenylation [GO:0006378]; termination of RNA polymerase II transcription [GO:0006369]
cytoplasm [GO:0005737]; mitochondrion [GO:0005739]; mRNA cleavage factor complex [GO:0005849]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
mRNA binding [GO:0003729]; RNA polymerase II complex binding [GO:0000993]
PF11526;PF04818;PF20827;PF20845;PF20844;
1.25.40.90;
null
PTM: Phosphorylation at Ser-120 and/or Thr-121 by WNK1 weakens its association with POLR2A/RNA polymerase II, promoting transcript release from the chromatin template and mRNA export to the cytoplasm. {ECO:0000269|PubMed:29196535}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:29196535}.
null
null
null
null
null
FUNCTION: Component of pre-mRNA cleavage complex II, which promotes transcription termination by RNA polymerase II. {ECO:0000269|PubMed:11060040, ECO:0000269|PubMed:29196535}.
Homo sapiens (Human)
O94915
FRYL_HUMAN
MSNITIDPDVKPGEYVIKSLFAEFAVQAEKKIEVVMAEPLEKLLSRSLQRGEDLQFDQLISSMSSVAEHCLPSLLRTLFDWYRRQNGTEDESYEYRPRSSTKSKGDEQQRERDYLLERRDLAVDFIFCLVLVEVLKQIPVHPVPDPLVHEVLNLAFKHFKHKEGYSGTNTGNVHIIADLYAEVIGVLAQSKFQAVRKKFVTELKELRQKEQSPHVVQSVISLIMGMKFFRVKMYPVEDFEASFQFMQECAQYFLEVKDKDIKHALAGLFVEILIPVAAAVKNEVNVPCLKNFVEMLYQTTFELSSRKKHSLALYPLITCL...
null
null
cell morphogenesis [GO:0000902]; neuron projection development [GO:0031175]
cell cortex [GO:0005938]; site of polarized growth [GO:0030427]
null
PF19421;PF14225;PF14228;PF14222;
null
Furry protein family
null
null
null
null
null
null
null
FUNCTION: Plays a key role in maintaining the integrity of polarized cell extensions during morphogenesis, regulates the actin cytoskeleton and plays a key role in patterning sensory neuron dendritic fields by promoting avoidance between homologous dendrites as well as by limiting dendritic branching (By similarity). M...
Homo sapiens (Human)
O94916
NFAT5_HUMAN
MPSDFISLLSADLDLESPKSLYSRESVYDLLPKELQLPPSRETSVASMSQTSGGEAGSPPPAVVAADASSAPSSSSMGGACSSFTTSSSPTIYSTSVTDSKAMQVESCSSAVGVSNRGVSEKQLTSNTVQQHPSTPKRHTVLYISPPPEDLLDNSRMSCQDEGCGLESEQSCSMWMEDSPSNFSNMSTSSYNDNTEVPRKSRKRNPKQRPGVKRRDCEESNMDIFDADSAKAPHYVLSQLTTDNKGNSKAGNGTLENQKGTGVKKSPMLCGQYPVKSEGKELKIVVQPETQHRARYLTEGSRGSVKDRTQQGFPTVKLEG...
null
null
calcineurin-NFAT signaling cascade [GO:0033173]; cellular hyperosmotic response [GO:0071474]; cellular response to cytokine stimulus [GO:0071345]; DNA damage response [GO:0006974]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of gene expression [GO:0010628]; positive ...
chromatin [GO:0000785]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667]
chromatin binding [GO:0003682]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA...
PF16179;PF00554;
2.60.40.10;2.60.40.340;
null
PTM: Phosphorylated (PubMed:10377394). Phosphorylated at Thr-135 by CDK5 in response to osmotic stress; this phosphorylation mediates its rapid nuclear localization (PubMed:21209322). {ECO:0000269|PubMed:10377394, ECO:0000269|PubMed:21209322}.; PTM: Poly-ADP-ribosylated by PARP1 in response to DNA damage, promoting rec...
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10377394}. Cytoplasm {ECO:0000250|UniProtKB:Q9WV30}. Chromosome {ECO:0000269|PubMed:34049076}. Note=Nuclear distribution increases under hypertonic conditions (By similarity). Recruited to sites of R-loop-associated DNA damage following poly-ADP-ribosylation by PARP1 (P...
null
null
null
null
null
FUNCTION: Transcription factor involved, among others, in the transcriptional regulation of osmoprotective and inflammatory genes. Binds the DNA consensus sequence 5'-[ACT][AG]TGGAAA[CAT]A[TA][ATC][CA][ATG][GT][GAC][CG][CT]-3' (PubMed:10377394). Mediates the transcriptional response to hypertonicity (PubMed:10051678). ...
Homo sapiens (Human)
O94919
ENDD1_HUMAN
MGTARWLALGSLFALAGLLEGRLVGEEEAGFGECDKFFYAGTPPAGLAADSHVKICQRAEGAERFATLYSTRDRIPVYSAFRAPRPAPGGAEQRWLVEPQIDDPNSNLEEAINEAEAITSVNSLGSKQALNTDYLDSDYQRGQLYPFSLSSDVQVATFTLTNSAPMTQSFQERWYVNLHSLMDRALTPQCGSGEDLYILTGTVPSDYRVKDKVAVPEFVWLAACCAVPGGGWAMGFVKHTRDSDIIEDVMVKDLQKLLPFNPQLFQNNCGETEQDTEKMKKILEVVNQIQDEERMVQSQKSSSPLSSTRSKRSTLLPPEA...
3.1.30.-
null
innate immune response [GO:0045087]
cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; membrane [GO:0016020]
endonuclease activity [GO:0004519]; metal ion binding [GO:0046872]; nucleic acid binding [GO:0003676]
PF01223;
3.40.570.10;
DNA/RNA non-specific endonuclease family
null
SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
null
null
null
null
null
FUNCTION: May act as a DNase and a RNase. Plays a role in the modulation of innate immune signaling through the cGAS-STING pathway by interacting with RNF26. {ECO:0000269|PubMed:32614325}.
Homo sapiens (Human)
O94921
CDK14_HUMAN
MCDLIEPQPAEKIGKMKKLRRTLSESFSRIALKKDDTTFDEICVTKMSTRNCQGMDSVIKPLDTIPEDKKVRVQRTQSTFDPFEKPANQVKRVHSENNACINFKTSSTGKESPKVRRHSSPSSPTSPKFGKADSYEKLEKLGEGSYATVYKGKSKVNGKLVALKVIRLQEEEGTPFTAIREASLLKGLKHANIVLLHDIIHTKETLTLVFEYVHTDLCQYMDKHPGGLHPDNVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLARAKSVPSHTYSNEVVTLWYRPPDVLLGSTEYSTCLDMWGVGC...
2.7.11.22
null
cell division [GO:0051301]; G2/M transition of mitotic cell cycle [GO:0000086]; phosphorylation [GO:0016310]; regulation of canonical Wnt signaling pathway [GO:0060828]; Wnt signaling pathway [GO:0016055]
cyclin-dependent protein kinase holoenzyme complex [GO:0000307]; cytoplasm [GO:0005737]; cytoplasmic cyclin-dependent protein kinase holoenzyme complex [GO:0000308]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
ATP binding [GO:0005524]; cyclin binding [GO:0030332]; cyclin-dependent protein serine/threonine kinase activity [GO:0004693]; protein serine kinase activity [GO:0106310]
PF00069;
1.10.510.10;
Protein kinase superfamily, CMGC Ser/Thr protein kinase family, CDC2/CDKX subfamily
null
SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. Cytoplasm. Nucleus. Note=Recruited to the cell membrane by CCNY.
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=2.7.11.22; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[p...
null
null
null
null
FUNCTION: Serine/threonine-protein kinase involved in the control of the eukaryotic cell cycle, whose activity is controlled by an associated cyclin. Acts as a cell-cycle regulator of Wnt signaling pathway during G2/M phase by mediating the phosphorylation of LRP6 at 'Ser-1490', leading to the activation of the Wnt sig...
Homo sapiens (Human)
O94923
GLCE_HUMAN
MRCLAARVNYKTLIIICALFTLVTVLLWNKCSSDKAIQFPRRSSSGFRVDGFEKRAAASESNNYMNHVAKQQSEEAFPQEQQKAPPVVGGFNSNVGSKVLGLKYEEIDCLINDEHTIKGRREGNEVFLPFTWVEKYFDVYGKVVQYDGYDRFEFSHSYSKVYAQRAPYHPDGVFMSFEGYNVEVRDRVKCISGVEGVPLSTQWGPQGYFYPIQIAQYGLSHYSKNLTEKPPHIEVYETAEDRDKNKPNDWTVPKGCFMANVADKSRFTNVKQFIAPETSEGVSLQLGNTKDFIISFDLKFLTNGSVSVVLETTEKNQLFT...
5.1.3.17
null
heparan sulfate proteoglycan biosynthetic process [GO:0015012]; heparin biosynthetic process [GO:0030210]; negative regulation of cell projection organization [GO:0031345]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of SMAD protein signal transduction [GO:0060391]
Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]
calcium ion binding [GO:0005509]; heparosan-N-sulfate-glucuronate 5-epimerase activity [GO:0047464]; protein homodimerization activity [GO:0042803]; racemase and epimerase activity, acting on carbohydrates and derivatives [GO:0016857]
PF06662;PF21174;
null
D-glucuronyl C5-epimerase family
null
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9EPS3}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9EPS3}.
CATALYTIC ACTIVITY: Reaction=[heparosan-N-sulfate](n) = [heparan-N-sulfate](n); Xref=Rhea:RHEA:20197, Rhea:RHEA-COMP:9556, Rhea:RHEA-COMP:9557, ChEBI:CHEBI:58041, ChEBI:CHEBI:58287; EC=5.1.3.17; Evidence={ECO:0000269|PubMed:20118238, ECO:0000269|PubMed:22528493, ECO:0000269|PubMed:30872481};
null
PATHWAY: Glycan metabolism; heparan sulfate biosynthesis. {ECO:0000305|PubMed:22528493, ECO:0000305|PubMed:30872481}.; PATHWAY: Glycan metabolism; heparin biosynthesis. {ECO:0000305}.
null
null
FUNCTION: Converts D-glucuronic acid residues adjacent to N-sulfate sugar residues to L-iduronic acid residues, both in maturing heparan sulfate (HS) and heparin chains. This is important for further modifications that determine the specificity of interactions between these glycosaminoglycans and proteins. {ECO:0000269...
Homo sapiens (Human)
O94925
GLSK_HUMAN
MMRLRGSGMLRDLLLRSPAGVSATLRRAQPLVTLCRRPRGGGRPAAGPAAAARLHPWWGGGGWPAEPLARGLSSSPSEILQELGKGSTHPQPGVSPPAAPAAPGPKDGPGETDAFGNSEGKELVASGENKIKQGLLPSLEDLLFYTIAEGQEKIPVHKFITALKSTGLRTSDPRLKECMDMLRLTLQTTSDGVMLDKDLFKKCVQSNIVLLTQAFRRKFVIPDFMSFTSHIDELYESAKKQSGGKVADYIPQLAKFSPDLWGVSVCTVDGQRHSTGDTKVPFCLQSCVKPLKYAIAVNDLGTEYVHRYVGKEPSGLRFNK...
3.5.1.2
null
chemical synaptic transmission [GO:0007268]; glutamate biosynthetic process [GO:0006537]; glutamine catabolic process [GO:0006543]; intracellular glutamate homeostasis [GO:0090461]; protein homotetramerization [GO:0051289]; regulation of respiratory gaseous exchange by nervous system process [GO:0002087]; suckling beha...
cytosol [GO:0005829]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; synapse [GO:0045202]
glutaminase activity [GO:0004359]
PF12796;PF17959;PF04960;
1.10.238.210;1.25.40.20;3.40.710.10;
Glutaminase family
PTM: Synthesized as a 74-kDa cytosolic precursor which is proteolytically processed by the mitochondrial-processing peptidase (MPP) via a 72-kDa intermediate to yield the mature mitochondrial 68- and 65-kDa subunits. {ECO:0000250|UniProtKB:P13264}.
SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion {ECO:0000250|UniProtKB:P13264}. Cytoplasm, cytosol {ECO:0000269|PubMed:22228304}. Note=The 74-kDa cytosolic precursor is translocated into the mitochondria and processed via a 72-kDa intermediate to yield the mature 68- and 65-kDa subunits. {ECO:0000250|UniProtKB:P13264}...
CATALYTIC ACTIVITY: Reaction=H2O + L-glutamine = L-glutamate + NH4(+); Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=3.5.1.2; Evidence={ECO:0000269|PubMed:22049910, ECO:0000269|PubMed:22538822, ECO:0000269|PubMed:24451979, ECO:0000269|PubMed:26988803, ECO:0000269|P...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.9 mM for glutamine (isoform 1) {ECO:0000269|PubMed:22049910}; KM=1.4 mM for glutamine (isoform 3) {ECO:0000269|PubMed:22049910};
null
null
null
FUNCTION: Catalyzes the first reaction in the primary pathway for the renal catabolism of glutamine. Plays a role in maintaining acid-base homeostasis. Regulates the levels of the neurotransmitter glutamate, the main excitatory neurotransmitter in the brain (PubMed:30239721, PubMed:30575854, PubMed:30970188). {ECO:0000...
Homo sapiens (Human)
O94927
HAUS5_HUMAN
MELAQEARELGCWAVEEMGVPVAARAPESTLRRLCLGQGADIWAYILQHVHSQRTVKKIRGNLLWYGHQDSPQVRRKLELEAAVTRLRAEIQELDQSLELMERDTEAQDTAMEQARQHTQDTQRRALLLRAQAGAMRRQQHTLRDPMQRLQNQLRRLQDMERKAKVDVTFGSLTSAALGLEPVVLRDVRTACTLRAQFLQNLLLPQAKRGSLPTPHDDHFGTSYQQWLSSVETLLTNHPPGHVLAALEHLAAEREAEIRSLCSGDGLGDTEISRPQAPDQSDSSQTLPSMVHLIQEGWRTVGVLVSQRSTLLKERQVLTQ...
null
null
cell division [GO:0051301]; centrosome cycle [GO:0007098]; regulation of microtubule nucleation [GO:0010968]; spindle assembly [GO:0051225]
centrosome [GO:0005813]; cytosol [GO:0005829]; HAUS complex [GO:0070652]; mitotic spindle microtubule [GO:1990498]
null
PF14817;
null
HAUS5 family
null
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:19369198, ECO:0000269|PubMed:19427217}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:19369198, ECO:0000269|PubMed:19427217, ECO:0000269|PubMed:30723163}. Note=Localizes to interphase centrosomes and to m...
null
null
null
null
null
FUNCTION: Contributes to mitotic spindle assembly, maintenance of centrosome integrity and completion of cytokinesis as part of the HAUS augmin-like complex. {ECO:0000269|PubMed:19369198, ECO:0000269|PubMed:19427217}.
Homo sapiens (Human)
O94929
ABLM3_HUMAN
MNTSIPYQQNPYNPRGSSNVIQCYRCGDTCKGEVVRVHNNHFHIRCFTCQVCGCGLAQSGFFFKNQEYICTQDYQQLYGTRCDSCRDFITGEVISALGRTYHPKCFVCSLCRKPFPIGDKVTFSGKECVCQTCSQSMASSKPIKIRGPSHCAGCKEEIKHGQSLLALDKQWHVSCFKCQTCSVILTGEYISKDGVPYCESDYHAQFGIKCETCDRYISGRVLEAGGKHYHPTCARCVRCHQMFTEGEEMYLTGSEVWHPICKQAARAEKKLKHRRTSETSISPPGSSIGSPNRVICAKVDNEILNYKDLAALPKVKSIYE...
null
null
cilium assembly [GO:0060271]; cytoskeleton organization [GO:0007010]; lamellipodium assembly [GO:0030032]; positive regulation of protein targeting to mitochondrion [GO:1903955]; positive regulation of transcription by RNA polymerase II [GO:0045944]; transcription by RNA polymerase II [GO:0006366]
actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; glutamatergic synapse [GO:0098978]; lamellipodium [GO:0030027]; stress fiber [GO:0001725]
actin filament binding [GO:0051015]; metal ion binding [GO:0046872]
PF16182;PF00412;PF02209;
2.10.110.10;1.10.950.10;
null
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
null
null
null
null
null
FUNCTION: May act as scaffold protein. May stimulate ABRA activity and ABRA-dependent SRF transcriptional activity. {ECO:0000269|PubMed:17194709}.
Homo sapiens (Human)
O94933
SLIK3_HUMAN
MKPSIAEMLHRGRMLWIILLSTIALGWTTPIPLIEDSEEIDEPCFDPCYCEVKESLFHIHCDSKGFTNISQITEFWSRPFKLYLQRNSMRKLYTNSFLHLNNAVSINLGNNALQDIQTGAFNGLKILKRLYLHENKLDVFRNDTFLGLESLEYLQADYNVIKRIESGAFRNLSKLRVLILNDNLIPMLPTNLFKAVSLTHLDLRGNRLKVLFYRGMLDHIGRSLMELQLEENPWNCTCEIVQLKSWLERIPYTALVGDITCETPFHFHGKDLREIRKTELCPLLSDSEVEASLGIPHSSSSKENAWPTKPSSMLSSVHFT...
null
null
axonogenesis [GO:0007409]; gephyrin clustering involved in postsynaptic density assembly [GO:0097116]; neurotransmitter-gated ion channel clustering [GO:0072578]; positive regulation of synapse assembly [GO:0051965]; regulation of presynapse assembly [GO:1905606]; synaptic membrane adhesion [GO:0099560]; synaptic trans...
cell surface [GO:0009986]; GABA-ergic synapse [GO:0098982]; plasma membrane [GO:0005886]; postsynaptic density membrane [GO:0098839]; postsynaptic specialization membrane [GO:0099634]
null
PF13855;
3.80.10.10;
SLITRK family
null
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
null
null
null
null
null
FUNCTION: Suppresses neurite outgrowth. {ECO:0000250}.
Homo sapiens (Human)
O94941
RNF37_HUMAN
MVINLCLPQFRPRIHCNKISADGYEVENLISEDLTKRSHGFRTEYFIKPPVYVTVSFPFNVEICRINIDLTAGGGQNVTGLEMYTSASSSRVSWNTPQCRTLGPAEPSVPDKEAFTLVGKVLLKNQSQVVFSHRGFKARPPFGAMEATLPSPAVVAQELWNKGALSLSHVAHLRICITHVTGGGIPCIKRLEVWGQPAKTCSQEVIDSILLVTSENLPQDVALQAPALPMESDCDPGDQPESQQAPSSLQKLAEIIQDVPEEFLDPITLEIMPCPMLLPSGKVIDQSTLEKCNRSEATWGRVPSDPFTGVAFTPHSQPLP...
2.3.2.27
null
protein polyubiquitination [GO:0000209]
focal adhesion [GO:0005925]; nuclear body [GO:0016604]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
metal ion binding [GO:0046872]; ubiquitin protein ligase binding [GO:0031625]; ubiquitin-ubiquitin ligase activity [GO:0034450]
PF19318;PF04564;PF14634;
3.30.40.10;
null
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11274149, ECO:0000269|PubMed:11435423}. Note=Enriched in nuclear bodies. {ECO:0000269|PubMed:11274149}.
CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q925F4};
null
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:Q925F4}.
null
null
FUNCTION: May have a ubiquitin-protein ligase activity acting as an E3 ubiquitin-protein ligase or as a ubiquitin-ubiquitin ligase promoting elongation of ubiquitin chains on substrates. {ECO:0000250|UniProtKB:Q925F4}.
Homo sapiens (Human)
O94953
KDM4B_HUMAN
MGSEDHGAQNPSCKIMTFRPTMEEFKDFNKYVAYIESQGAHRAGLAKIIPPKEWKPRQTYDDIDDVVIPAPIQQVVTGQSGLFTQYNIQKKAMTVGEYRRLANSEKYCTPRHQDFDDLERKYWKNLTFVSPIYGADISGSLYDDDVAQWNIGSLRTILDMVERECGTIIEGVNTPYLYFGMWKTTFAWHTEDMDLYSINYLHFGEPKSWYAIPPEHGKRLERLAIGFFPGSSQGCDAFLRHKMTLISPIILKKYGIPFSRITQEAGEFMITFPYGYHAGFNHGFNCAESTNFATLRWIDYGKVATQCTCRKDMVKISMDV...
1.14.11.66
COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250};
brain development [GO:0007420]; chromatin remodeling [GO:0006338]; regulation of gene expression [GO:0010468]
chromatin [GO:0000785]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
histone demethylase activity [GO:0032452]; histone H3K36 demethylase activity [GO:0051864]; histone H3K9 demethylase activity [GO:0032454]; histone H3K9me2/H3K9me3 demethylase activity [GO:0140684]; metal ion binding [GO:0046872]
PF02373;PF02375;PF13831;PF18104;PF13832;
2.30.30.140;3.10.330.70;2.60.120.650;3.30.40.10;
JHDM3 histone demethylase family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00537, ECO:0000269|PubMed:15927959}.
CATALYTIC ACTIVITY: Reaction=2 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(9)-[histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + N(6)-methyl-L-lysyl(9)-[histone H3] + 2 succinate; Xref=Rhea:RHEA:60200, Rhea:RHEA-COMP:15538, Rhea:RHEA-COMP:15542, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:168...
null
null
null
null
FUNCTION: Histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27', H3 'Lys-36' nor H4 'Lys-20'. Only able to demethylate trimethylated H3 'Lys-9', with a weaker activity than KDM4A, KDM4C and KDM4D. Demethylat...
Homo sapiens (Human)
O94955
RHBT3_HUMAN
MSIHIVALGNEGDTFHQDNRPSGLIRTYLGRSPLVSGDESSLLLNAASTVARPVFTEYQASAFGNVKLVVHDCPVWDIFDSDWYTSRNLIGGADIIVIKYNVNDKFSFHEVKDNYIPVIKRALNSVPVIIAAVGTRQNEELPCTCPLCTSDRGSCVSTTEGIQLAKELGATYLELHSLDDFYIGKYFGGVLEYFMIQALNQKTSEKMKKRKMSNSFHGIRPPQLEQPEKMPVLKAEASHYNSDLNNLLFCCQCVDVVFYNPNLKKVVEAHKIVLCAVSHVFMLLFNVKSPTDIQDSSIIRTTQDLFAINRDTAFPGASHE...
3.6.1.-
null
male gonad development [GO:0008584]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; regulation of proteolysis [GO:0030162]; retrograde transport, endosome to Golgi [GO:0042147]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleus [GO:0005634]; trans-Golgi network membrane [GO:0032588]
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; GTPase activity [GO:0003924]; small GTPase binding [GO:0031267]; ubiquitin protein ligase binding [GO:0031625]
PF00651;PF00071;
3.40.50.300;
null
null
SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:19490898}.
null
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=48 uM for ATP {ECO:0000269|PubMed:19490898};
null
null
null
FUNCTION: Rab9-regulated ATPase required for endosome to Golgi transport. Involved in transport vesicle docking at the Golgi complex, possibly by participating in release M6PRBP1/TIP47 from vesicles to permit their efficient docking and fusion at the Golgi. Specifically binds Rab9, but not other Rab proteins. Has low i...
Homo sapiens (Human)
O94956
SO2B1_HUMAN
MGPRIGPAGEVPQVPDKETKATMGTENTPGGKASPDPQDVRPSVFHNIKLFVLCHSLLQLAQLMISGYLKSSISTVEKRFGLSSQTSGLLASFNEVGNTALIVFVSYFGSRVHRPRMIGYGAILVALAGLLMTLPHFISEPYRYDNTSPEDMPQDFKASLCLPTTSAPASAPSNGNCSSYTETQHLSVVGIMFVAQTLLGVGGVPIQPFGISYIDDFAHNSNSPLYLGILFAVTMMGPGLAFGLGSLMLRLYVDINQMPEGGISLTIKDPRWVGAWWLGFLIAAGAVALAAIPYFFFPKEMPKEKRELQFRRKVLAVTDS...
null
null
bile acid and bile salt transport [GO:0015721]; heme catabolic process [GO:0042167]; monoatomic ion transport [GO:0006811]; organic anion transport [GO:0015711]; sodium-independent organic anion transport [GO:0043252]; transmembrane transport [GO:0055085]; transport across blood-brain barrier [GO:0150104]; xenobiotic m...
apical plasma membrane [GO:0016324]; basal plasma membrane [GO:0009925]; basolateral plasma membrane [GO:0016323]; plasma membrane [GO:0005886]
bile acid transmembrane transporter activity [GO:0015125]; organic anion transmembrane transporter activity [GO:0008514]; prostaglandin transmembrane transporter activity [GO:0015132]; sodium-independent organic anion transmembrane transporter activity [GO:0015347]; transmembrane transporter activity [GO:0022857]
PF03137;
1.20.1250.20;
Organo anion transporter (TC 2.A.60) family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25132355}; Multi-pass membrane protein {ECO:0000305}. Basal cell membrane {ECO:0000269|PubMed:11159893, ECO:0000269|PubMed:11932330, ECO:0000269|PubMed:12409283, ECO:0000269|PubMed:35307651}; Multi-pass membrane protein {ECO:0000305}. Basolateral cell membrane {EC...
CATALYTIC ACTIVITY: Reaction=dehydroepiandrosterone 3-sulfate(out) = dehydroepiandrosterone 3-sulfate(in); Xref=Rhea:RHEA:71839, ChEBI:CHEBI:57905; Evidence={ECO:0000305|PubMed:11159893, ECO:0000305|PubMed:14610227, ECO:0000305|PubMed:16908597, ECO:0000305|PubMed:18501590, ECO:0000305|PubMed:23531488, ECO:0000305|PubMe...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=13.1 uM for estrone 3-sulfate (at pH 5.0) {ECO:0000269|PubMed:14610227}; KM=9.36 uM for estrone-3-sulfate (at pH 6.5) {ECO:0000269|PubMed:19129463}; KM=35 uM for estrone 3-sulfate (at pH 7.2) {ECO:0000269|PubMed:11932330}; KM=14 uM for estrone 3-sulfate (at pH 7.3)...
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is around 5.0 with estrone 3-sulfate, dehydroepiandrosterone sulfate and taurocholate as substrates (PubMed:12724351, PubMed:14610227, PubMed:20507927, PubMed:22201122). The high-affinity site for estrone 3-sulfate binding is pH-dependent with increased transpor...
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius with estrone 3-sulfate as substrate. {ECO:0000269|PubMed:11932330};
FUNCTION: Mediates the Na(+)-independent transport of steroid sulfate conjugates and other specific organic anions (PubMed:10873595, PubMed:11159893, PubMed:11932330, PubMed:12724351, PubMed:14610227, PubMed:16908597, PubMed:18501590, PubMed:20507927, PubMed:22201122, PubMed:23531488, PubMed:25132355, PubMed:26383540, ...
Homo sapiens (Human)
O94964
MTCL2_HUMAN
MEAPAAEPPVRGCGPQPAPAPAPAPERKKSHRAPSPARPKDVAGWSLAKGRRGPGPGSAVACSAAFSSRPDKKGRAVAPGARGAGVRVAGVRTGVRAKGRPRSGAGPRPPPPPPSLTDSSSEVSDCASEEARLLGLELALSSDAESAAGGPAGVRTGQPAQPAPSAQQPPRPPASPDEPSVAASSVGSSRLPLSASLAFSDLTEEMLDCGPSGLVRELEELRSENDYLKDEIEELRAEMLEMRDVYMEEDVYQLQELRQQLDQASKTCRILQYRLRKAERRSLRAAQTGQVDGELIRGLEQDVKVSKDISMRLHKELEVV...
null
null
cell division [GO:0051301]; chromosome segregation [GO:0007059]; insulin receptor signaling pathway [GO:0008286]; negative regulation of gluconeogenesis [GO:0045721]; regulation of autophagy [GO:0010506]
extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; Golgi membrane [GO:0000139]; microtubule [GO:0005874]; midbody [GO:0030496]
null
PF14818;PF11365;
null
MTCL family
PTM: Proteolytically cleaved in primary hepatocytes into a C-terminal 80 kDa form (By similarity). Proteolytically cleaved into a C-terminal SOGA 25 kDa form that is detected in plasma. {ECO:0000250|UniProtKB:E1U8D0, ECO:0000269|PubMed:20813965}.; PTM: Phosphorylated during mitosis in a CDK1-dependent manner. {ECO:0000...
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:33587225}. Golgi apparatus membrane {ECO:0000250|UniProtKB:E1U8D0}. Midbody {ECO:0000269|PubMed:33587225}. Note=Associates with microtubules during late mitosis and interphase. {ECO:0000269|PubMed:33587225}.; SUBCELLULAR LOCATION: [C-terminal 80 kDa form...
null
null
null
null
null
FUNCTION: Microtubule-associated factor that enables integration of the centrosomal and Golgi-associated microtubules on the Golgi membrane, supporting directional migration. Preferentially acts on the perinuclear microtubules accumulated around the Golgi. Associates with the Golgi membrane through the N-terminal coile...
Homo sapiens (Human)
O94966
UBP19_HUMAN
MSGGASATGPRRGPPGLEDTTSKKKQKDRANQESKDGDPRKETGSRYVAQAGLEPLASGDPSASASHAAGITGSRHRTRLFFPSSSGSASTPQEEQTKEGACEDPHDLLATPTPELLLDWRQSAEEVIVKLRVGVGPLQLEDVDAAFTDTDCVVRFAGGQQWGGVFYAEIKSSCAKVQTRKGSLLHLTLPKKVPMLTWPSLLVEADEQLCIPPLNSQTCLLGSEENLAPLAGEKAVPPGNDPVSPAMVRSRNPGKDDCAKEEMAVAADAATLVDEPESMVNLAFVKNDSYEKGPDSVVVHVYVKEICRDTSRVLFREQDF...
3.4.19.12
null
ERAD pathway [GO:0036503]; negative regulation of skeletal muscle tissue development [GO:0048642]; positive regulation of cell cycle process [GO:0090068]; protein deubiquitination [GO:0016579]; protein stabilization [GO:0050821]; regulation of cellular response to hypoxia [GO:1900037]; regulation of ERAD pathway [GO:19...
cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]
cysteine-type deubiquitinase activity [GO:0004843]; Hsp90 protein binding [GO:0051879]; metal ion binding [GO:0046872]
PF04969;PF00443;PF16602;PF01753;
2.60.40.790;6.10.140.2220;3.90.70.10;
Peptidase C19 family
null
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19465887}; Single-pass membrane protein {ECO:0000269|PubMed:19465887}.
CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12;
null
null
null
null
FUNCTION: Deubiquitinating enzyme that regulates the degradation of various proteins. Deubiquitinates and prevents proteasomal degradation of RNF123 which in turn stimulates CDKN1B ubiquitin-dependent degradation thereby playing a role in cell proliferation. Involved in decreased protein synthesis in atrophying skeleta...
Homo sapiens (Human)
O94967
WDR47_HUMAN
MTAEETVNVKEVEIIKLILDFLNSKKLHISMLALEKESGVINGLFSDDMLFLRQLILDGQWDEVLQFIQPLECMEKFDKKRFRYIILKQKFLEALCVNNAMSAEDEPQHLEFTMQEAVQCLHALEEYCPSKDDYSKLCLLLTLPRLTNHAEFKDWNPSTARVHCFEEACVMVAEFIPADRKLSEAGFKASNNRLFQLVMKGLLYECCVEFCQSKATGEEITESEVLLGIDLLCGNGCDDLDLSLLSWLQNLPSSVFSCAFEQKMLNIHVDKLLKPTKAAYADLLTPLISKLSPYPSSPMRRPQSADAYMTRSLNPALDGL...
null
null
adult locomotory behavior [GO:0008344]; anterior commissure morphogenesis [GO:0021960]; autophagy [GO:0006914]; cerebral cortex radial glia-guided migration [GO:0021801]; corpus callosum development [GO:0022038]; detection of hot stimulus involved in thermoception [GO:0120168]; microtubule cytoskeleton organization [GO...
cytoplasm [GO:0005737]; dendrite [GO:0030425]; growth cone [GO:0030426]; microtubule [GO:0005874]; neuronal cell body [GO:0043025]
null
PF17814;PF00400;
2.130.10.10;
null
null
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Note=Localization along microtubules is mediated by MAP1S. {ECO:0000250}.
null
null
null
null
null
null
Homo sapiens (Human)
O94972
TRI37_HUMAN
MDEQSVESIAEVFRCFICMEKLRDARLCPHCSKLCCFSCIRRWLTEQRAQCPHCRAPLQLRELVNCRWAEEVTQQLDTLQLCSLTKHEENEKDKCENHHEKLSVFCWTCKKCICHQCALWGGMHGGHTFKPLAEIYEQHVTKVNEEVAKLRRRLMELISLVQEVERNVEAVRNAKDERVREIRNAVEMMIARLDTQLKNKLITLMGQKTSLTQETELLESLLQEVEHQLRSCSKSELISKSSEILMMFQQVHRKPMASFVTTPVPPDFTSELVPSYDSATFVLENFSTLRQRADPVYSPPLQVSGLCWRLKVYPDGNGVV...
2.3.2.27
null
aggresome assembly [GO:0070842]; negative regulation of centriole replication [GO:0046600]; negative regulation of gene expression, epigenetic [GO:0045814]; negative regulation of NF-kappaB transcription factor activity [GO:0032088]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regul...
aggresome [GO:0016235]; chromosome [GO:0005694]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; perinuclear region of cytoplasm [GO:0048471]; peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777]
chromatin binding [GO:0003682]; histone H2AK119 ubiquitin ligase activity [GO:0140862]; protein homodimerization activity [GO:0042803]; transcription coactivator activity [GO:0003713]; tumor necrosis factor receptor binding [GO:0005164]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin protein ligase binding [...
PF00917;PF00643;
3.30.160.60;3.30.40.10;
TRIM/RBCC family
PTM: Auto-ubiquitinated. {ECO:0000269|PubMed:15885686}.
SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:25470042}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:15885686}. Peroxisome membrane {ECO:0000269|PubMed:11938494, ECO:0000269|PubMed:28724525}; Peripheral membrane protein {ECO:0000269|PubMed:28724525}. Note=Found in vesicles of the peroxisome. Aggregates as ...
CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000269|PubMed:15885686, ECO:0000269|PubMed:28724525};
null
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:15885686, ECO:0000269|PubMed:25470042, ECO:0000269|PubMed:28724525}.
null
null
FUNCTION: E3 ubiquitin-protein ligase required to prevent centriole reduplication (PubMed:15885686, PubMed:23769972). Probably acts by ubiquitinating positive regulators of centriole reduplication (PubMed:23769972). Mediates monoubiquitination of 'Lys-119' of histone H2A (H2AK119Ub), a specific tag for epigenetic trans...
Homo sapiens (Human)
O94973
AP2A2_HUMAN
MPAVSKGDGMRGLAVFISDIRNCKSKEAEIKRINKELANIRSKFKGDKALDGYSKKKYVCKLLFIFLLGHDIDFGHMEAVNLLSSNRYTEKQIGYLFISVLVNSNSELIRLINNAIKNDLASRNPTFMGLALHCIASVGSREMAEAFAGEIPKVLVAGDTMDSVKQSAALCLLRLYRTSPDLVPMGDWTSRVVHLLNDQHLGVVTAATSLITTLAQKNPEEFKTSVSLAVSRLSRIVTSASTDLQDYTYYFVPAPWLSVKLLRLLQCYPPPDPAVRGRLTECLETILNKAQEPPKSKKVQHSNAKNAVLFEAISLIIHHD...
null
null
clathrin-dependent endocytosis [GO:0072583]; intracellular protein transport [GO:0006886]; postsynaptic neurotransmitter receptor internalization [GO:0098884]; vesicle-mediated transport [GO:0016192]
AP-2 adaptor complex [GO:0030122]; clathrin-coated endocytic vesicle [GO:0045334]; clathrin-coated endocytic vesicle membrane [GO:0030669]; cytoplasmic side of plasma membrane [GO:0009898]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; endocytic vesicle membrane [GO:0030666]; endolysosome membrane [GO:0036020...
clathrin adaptor activity [GO:0035615]; disordered domain specific binding [GO:0097718]; lipid binding [GO:0008289]; protein kinase binding [GO:0019901]
PF01602;PF02296;PF02883;
2.60.40.1230;1.25.10.10;3.30.310.10;
Adaptor complexes large subunit family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P17427}; Peripheral membrane protein {ECO:0000250|UniProtKB:P17427}; Cytoplasmic side {ECO:0000250|UniProtKB:P17427}. Membrane, coated pit {ECO:0000250|UniProtKB:P17427}; Peripheral membrane protein {ECO:0000250|UniProtKB:P17427}; Cytoplasmic side {ECO:0000250|...
null
null
null
null
null
FUNCTION: Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved i...
Homo sapiens (Human)
O94979
SC31A_HUMAN
MKLKEVDRTAMQAWSPAQNHPIYLATGTSAQQLDATFSTNASLEIFELDLSDPSLDMKSCATFSSSHRYHKLIWGPYKMDSKGDVSGVLIAGGENGNIILYDPSKIIAGDKEVVIAQNDKHTGPVRALDVNIFQTNLVASGANESEIYIWDLNNFATPMTPGAKTQPPEDISCIAWNRQVQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMHCSGLAWHPDVATQMVLASEDDRLPVIQMWDLRFASSPLRVLENHARGILAIAWSMADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLS...
null
null
COPII-coated vesicle cargo loading [GO:0090110]; endoplasmic reticulum organization [GO:0007029]; endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; intracellular protein transport [GO:0006886]; response to calcium ion [GO:0051592]
COPII vesicle coat [GO:0030127]; COPII-coated ER to Golgi transport vesicle [GO:0030134]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum exit site [GO:0070971]; endoplasmic reticulum membrane [GO:0005789]; ER to Golgi transport vesicle membrane [GO:0012507]; intr...
calcium-dependent protein binding [GO:0048306]; structural molecule activity [GO:0005198]
PF12931;
1.25.40.1030;1.20.940.10;2.130.10.10;
WD repeat SEC31 family
PTM: Monoubiquitinated by the BCR(KLHL12) E3 ubiquitin ligase complex, leading to regulate the size of COPII coats. {ECO:0000269|PubMed:22358839, ECO:0000269|PubMed:27565346}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000269|PubMed:10788476, ECO:0000269|PubMed:16957052, ECO:0000269|PubMed:22358839, ECO:0000269|PubMed:27716508}; Peripheral membrane protein; Cytoplasmic side. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral ...
null
null
null
null
null
FUNCTION: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER) (PubMed:10788476). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules (By simi...
Homo sapiens (Human)
O94983
CMTA2_HUMAN
MNTKDTTEVAENSHHLKIFLPKKLLECLPRCPLLPPERLRWNTNEEIASYLITFEKHDEWLSCAPKTRPQNGSIILYNRKKVKYRKDGYLWKKRKDGKTTREDHMKLKVQGMECLYGCYVHSSIVPTFHRRCYWLLQNPDIVLVHYLNVPALEDCGKGCSPIFCSISSDRREWLKWSREELLGQLKPMFHGIKWSCGNGTEEFSVEHLVQQILDTHPTKPAPRTHACLCSGGLGSGSLTHKCSSTKHRIISPKVEPRALTLTSIPHAHPPEPPPLIAPLPPELPKAHTSPSSSSSSSSSGFAEPLEIRPSPPTSRGGSSR...
null
null
cardiac muscle hypertrophy in response to stress [GO:0014898]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]
chromatin [GO:0000785]; nucleus [GO:0005634]
chromatin binding [GO:0003682]; double-stranded DNA binding [GO:0003690]; histone deacetylase binding [GO:0042826]; sequence-specific DNA binding [GO:0043565]; transcription coactivator activity [GO:0003713]; transcription coregulator activity [GO:0003712]
PF03859;PF01833;
1.20.5.190;1.25.40.20;2.60.40.10;
CAMTA family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:11925432}.
null
null
null
null
null
FUNCTION: Transcription activator. May act as tumor suppressor. {ECO:0000269|PubMed:11925432}.
Homo sapiens (Human)
O94985
CSTN1_HUMAN
MLRRPAPALAPAARLLLAGLLCGGGVWAARVNKHKPWLEPTYHGIVTENDNTVLLDPPLIALDKDAPLRFAESFEVTVTKEGEICGFKIHGQNVPFDAVVVDKSTGEGVIRSKEKLDCELQKDYSFTIQAYDCGKGPDGTNVKKSHKATVHIQVNDVNEYAPVFKEKSYKATVIEGKQYDSILRVEAVDADCSPQFSQICSYEIITPDVPFTVDKDGYIKNTEKLNYGKEHQYKLTVTAYDCGKKRATEDVLVKISIKPTCTPGWQGWNNRIEYEPGTGALAVFPNIHLETCDEPVASVQATVELETSHIGKGCDRDTYS...
null
null
cell adhesion [GO:0007155]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; neurotransmitter receptor transport to postsynaptic membrane [GO:0098969]; positive regulation of synapse assembly [GO:0051965]; positive regulation of synaptic transmission [GO:0050806]; regulation of cell growth ...
cell surface [GO:0009986]; endoplasmic reticulum membrane [GO:0005789]; extracellular region [GO:0005576]; glutamatergic synapse [GO:0098978]; Golgi membrane [GO:0000139]; neuron projection [GO:0043005]; nucleus [GO:0005634]; postsynaptic density [GO:0014069]; postsynaptic endosome [GO:0098845]; postsynaptic membrane [...
amyloid-beta binding [GO:0001540]; calcium ion binding [GO:0005509]; kinesin binding [GO:0019894]; X11-like protein binding [GO:0042988]
PF00028;PF19699;PF13385;
2.60.120.200;2.60.40.60;
Calsyntenin family
PTM: Proteolytically processed under normal cellular conditions (PubMed:15037614). A primary zeta-cleavage generates a large extracellular (soluble) N-terminal domain (sAlc) and a short C-terminal transmembrane fragment (CTF1) (PubMed:15037614). A secondary cleavage catalyzed by presenilin gamma-secretase within the tr...
SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q9EPL2}; Single-pass type I membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:17332754}; Single-pass type I membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:17332754, ECO:0000269|PubMed:2...
null
null
null
null
null
FUNCTION: Postsynaptic adhesion molecule that binds to presynaptic neurexins to mediate both excitatory and inhibitory synapse formation (By similarity). Promotes synapse development by acting as a cell adhesion molecule at the postsynaptic membrane, which associates with neurexin-alpha at the presynaptic membrane (By ...
Homo sapiens (Human)
O94986
CE152_HUMAN
MSLDFGSVALPVQNEDEEYDEEDYEREKELQQLLTDLPHDMLDDDLSSPELQYSDCSEDGTDGQPHHPEQLEMSWNEQMLPKSQSVNGYNEIQSLYAGEKCGNVWEENRSKTEDRHPVYHPEEGGDEGGSGYSPPSKCEQTDLYHLPENFRPYTNGQKQEFNNQATNVIKFSDPQWNHFQGPSCQGLEPYNKVTYKPYQSSAQNNGSPAQEITGSDTFEGLQQQFLGANENSAENMQIIQLQVLNKAKERQLENLIEKLNESERQIRYLNHQLVIIKDEKDGLTLSLRESQKLFQNGKEREIQLEAQIKALETQIQALKV...
null
null
cell projection organization [GO:0030030]; centriole replication [GO:0007099]; centrosome duplication [GO:0051298]; de novo centriole assembly involved in multi-ciliated epithelial cell differentiation [GO:0098535]
centriole [GO:0005814]; centrosome [GO:0005813]; cytosol [GO:0005829]; deuterosome [GO:0098536]; nucleoplasm [GO:0005654]; pericentriolar material [GO:0000242]; procentriole [GO:0120098]; procentriole replication complex [GO:0120099]
protein kinase binding [GO:0019901]
null
null
CEP152 family
null
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:20598275, ECO:0000269|PubMed:21059844, ECO:0000269|PubMed:21131973, ECO:0000269|PubMed:21983783, ECO:0000269|PubMed:26297806, ECO:0000269|PubMed:30804208}. Cytoplasm, cytoskeleton, m...
null
null
null
null
null
FUNCTION: Necessary for centrosome duplication; the function seems also to involve CEP63, CDK5RAP2 and WDR62 through a stepwise assembled complex at the centrosome that recruits CDK2 required for centriole duplication (PubMed:26297806). Acts as a molecular scaffold facilitating the interaction of PLK4 and CENPJ, 2 mole...
Homo sapiens (Human)
O94989
ARHGF_HUMAN
MSAQSLPAATPPTQKPPRIIRPRPPSRSRAAQSPGPPHNGSSPQELPRNSNDAPTPMCTPIFWEPPAASLKPPALLPPSASRASLDSQTSPDSPSSTPTPSPVSRRSASPEPAPRSPVPPPKPSGSPCTPLLPMAGVLAQNGSASAPGTVRRLAGRFEGGAEGRAQDADAPEPGLQARADVNGEREAPLTGSGSQENGAPDAGLACPPCCPCVCHTTRPGLELRWVPVGGYEEVPRVPRRASPLRTSRSRPHPPSIGHPAVVLTSYRSTAERKLLPLLKPPKPTRVRQDATIFGDPPQPDLDLLSEDGIQTGDSPDEAPQ...
null
null
negative regulation of synapse maturation [GO:2000297]; positive regulation of stress fiber assembly [GO:0051496]; regulation of catalytic activity [GO:0050790]; regulation of postsynapse assembly [GO:0150052]; regulation of small GTPase mediated signal transduction [GO:0051056]; retina vasculature morphogenesis in cam...
cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; glutamatergic synapse [GO:0098978]; postsynapse [GO:0098794]
GTPase activator activity [GO:0005096]; guanyl-nucleotide exchange factor activity [GO:0005085]
PF00621;
1.20.900.10;2.30.29.30;
null
PTM: Phosphorylated on tyrosine residues upon EFNA1 stimulation. EPHB2-dependent phosphorylation at Tyr-353 triggers UBE3A-mediated ubiquitination (By similarity). {ECO:0000250}.; PTM: Ubiquitinated; UBE3A-mediated ubiquitination and degradation by the proteasome promotes EFNB1-dependent synapse formation. {ECO:0000250...
SUBCELLULAR LOCATION: Cell projection, dendrite {ECO:0000250}. Note=Expressed exclusively in dendrites of the developing hippocampus. {ECO:0000250}.
null
null
null
null
null
FUNCTION: Specific GEF for RhoA activation. Does not activate RAC1 or CDC42. Regulates vascular smooth muscle contractility. Negatively regulates excitatory synapse development by suppressing the synapse-promoting activity of EPHB2. {ECO:0000269|PubMed:12775584}.
Homo sapiens (Human)
O94991
SLIK5_HUMAN
MHTCCPPVTLEQDLHRKMHSWMLQTLAFAVTSLVLSCAETIDYYGEICDNACPCEEKDGILTVSCENRGIISLSEISPPRFPIYHLLLSGNLLNRLYPNEFVNYTGASILHLGSNVIQDIETGAFHGLRGLRRLHLNNNKLELLRDDTFLGLENLEYLQVDYNYISVIEPNAFGKLHLLQVLILNDNLLSSLPNNLFRFVPLTHLDLRGNRLKLLPYVGLLQHMDKVVELQLEENPWNCSCELISLKDWLDSISYSALVGDVVCETPFRLHGRDLDEVSKQELCPRRLISDYEMRPQTPLSTTGYLHTTPASVNSVATSS...
null
null
adult behavior [GO:0030534]; axonogenesis [GO:0007409]; chemical synaptic transmission [GO:0007268]; circulatory system development [GO:0072359]; dendrite morphogenesis [GO:0048813]; grooming behavior [GO:0007625]; positive regulation of synapse assembly [GO:0051965]; regulation of presynapse assembly [GO:1905606]; res...
plasma membrane [GO:0005886]; receptor complex [GO:0043235]; synapse [GO:0045202]
null
PF13855;
3.80.10.10;
SLITRK family
null
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
null
null
null
null
null
FUNCTION: Suppresses neurite outgrowth. {ECO:0000250}.
Homo sapiens (Human)
O94992
HEXI1_HUMAN
MAEPFLSEYQHQPQTSNCTGAAAVQEELNPERPPGAEERVPEEDSRWQSRAFPQLGGRPGPEGEGSLESQPPPLQTQACPESSCLREGEKGQNGDDSSAGGDFPPPAEVEPTPEAELLAQPCHDSEASKLGAPAAGGEEEWGQQQRQLGKKKHRRRPSKKKRHWKPYYKLTWEEKKKFDEKQSLRASRIRAEMFAKGQPVAPYNTTQFLMDDHDQEEPDLKTGLYSKRAAAKSDDTSDDDFMEEGGEEDGGSDGMGGDGSEFLQRDFSETYERYHTESLQNMSKQELIKEYLELEKCLSRMEDENNRLRLESKRLGGDDA...
null
null
activation of innate immune response [GO:0002218]; heart development [GO:0007507]; innate immune response [GO:0045087]; negative regulation of cyclin-dependent protein serine/threonine kinase activity [GO:0045736]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of transcription by ...
7SK snRNP [GO:0120259]; cytoplasm [GO:0005737]; intracellular membrane-bounded organelle [GO:0043231]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
7SK snRNA binding [GO:0097322]; cyclin-dependent protein serine/threonine kinase inhibitor activity [GO:0004861]; identical protein binding [GO:0042802]; P-TEFb complex binding [GO:0106140]; protein kinase inhibitor activity [GO:0004860]; snRNA binding [GO:0017069]
PF15313;
6.10.250.2910;
HEXIM family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12581153, ECO:0000269|PubMed:12832472, ECO:0000269|PubMed:12941847, ECO:0000269|PubMed:16362050, ECO:0000269|PubMed:17395637}. Cytoplasm {ECO:0000269|PubMed:12581153, ECO:0000269|PubMed:17395637}. Note=Binds alpha-importin and is mostly nuclear (PubMed:16362050).
null
null
null
null
null
FUNCTION: Transcriptional regulator which functions as a general RNA polymerase II transcription inhibitor (PubMed:14580347, PubMed:15201869, PubMed:15713661). Core component of the 7SK RNP complex: in cooperation with 7SK snRNA sequesters P-TEFb in a large inactive 7SK snRNP complex preventing RNA polymerase II phosph...
Homo sapiens (Human)
O94993
SOX30_HUMAN
MERARPEPPPQPRPLRPAPPPLPVEGTSFWAAAMEPPPSSPTLSAAASATLASSCGEAVASGLQPAVRRLLQVKPEQVLLLPQPQAQNEEAAASSAQARLLQFRPDLRLLQPPTASDGATSRPELHPVQPLALHVKAKKQKLGPSLDQSVGPRGAVETGPRASRVVKLEGPGPALGYFRGDEKGKLEAEEVMRDSMQGGAGKSPAAIREGVIKTEEPERLLEDCRLGAEPASNGLVHGSAEVILAPTSGAFGPHQQDLRIPLTLHTVPPGARIQFQGAPPSELIRLTKVPLTPVPTKMQSLLEPSVKIETKDVPLTVLPS...
null
null
negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of Wnt signaling pathway [GO:0030178]; positive regulation of transcription by RNA polymerase II [GO:0045944]; proacrosomal vesicle fusion [GO:0120211]; regulation of transcription by RNA polymerase II [GO:0006357]; response to ...
chromatin [GO:0000785]; chromocenter [GO:0010369]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
beta-catenin binding [GO:0008013]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; RNA polymerase II cis-regul...
PF00505;
1.10.30.10;
null
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10359848, ECO:0000269|PubMed:29739711}. Cytoplasm {ECO:0000269|PubMed:29739711}. Note=Enriched at the chromocenter. {ECO:0000250|UniProtKB:Q8CGW4}.
null
null
null
null
null
FUNCTION: Acts both as a transcriptional activator and a repressor (PubMed:10359848, PubMed:29739711). Binds to the DNA sequence 5'-ACAAT-3' and shows a preference for guanine residues surrounding this core motif (PubMed:10359848). Binds to its own promoter and activates its own transcription (By similarity). Required ...
Homo sapiens (Human)
O95045
UPP2_HUMAN
MASVIPASNRSMRSDRNTYVGKRFVHVKNPYLDLMDEDILYHLDLGTKTHNLPAMFGDVKFVCVGGSPNRMKAFALFMHKELGFEEAEEDIKDICAGTDRYCMYKTGPVLAISHGMGIPSISIMLHELIKLLHHARCCDVTIIRIGTSGGIGIAPGTVVITDIAVDSFFKPRFEQVILDNIVTRSTELDKELSEELFNCSKEIPNFPTLVGHTMCTYDFYEGQGRLDGALCSFSREKKLDYLKRAFKAGVRNIEMESTVFAAMCGLCGLKAAVVCVTLLDRLDCDQINLPHDVLVEYQQRPQLLISNFIRRRLGLCD
2.4.2.3
null
dCMP catabolic process [GO:0006249]; nucleoside metabolic process [GO:0009116]; UMP salvage [GO:0044206]; uridine catabolic process [GO:0006218]; uridine metabolic process [GO:0046108]
cytosol [GO:0005829]; type III intermediate filament [GO:0045098]
deoxyuridine phosphorylase activity [GO:0047847]; identical protein binding [GO:0042802]; uridine phosphorylase activity [GO:0004850]
PF01048;
3.40.50.1580;
PNP/UDP phosphorylase family
null
null
CATALYTIC ACTIVITY: Reaction=phosphate + uridine = alpha-D-ribose 1-phosphate + uracil; Xref=Rhea:RHEA:24388, ChEBI:CHEBI:16704, ChEBI:CHEBI:17568, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; EC=2.4.2.3; Evidence={ECO:0000269|PubMed:12849978, ECO:0000269|PubMed:21855639}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=76 uM for uridine {ECO:0000269|PubMed:12849978}; KM=300 uM for deoxyuridine {ECO:0000269|PubMed:12849978}; KM=73 uM for thymidine {ECO:0000269|PubMed:12849978}; KM=24 uM for 5-fluorouridine {ECO:0000269|PubMed:12849978}; KM=427 uM for 5-fluoro-2(')-deoxyuridine {EC...
PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway; uracil from uridine (phosphorylase route): step 1/1. {ECO:0000269|PubMed:12849978}.
null
null
FUNCTION: Catalyzes the reversible phosphorylytic cleavage of uridine to uracil and ribose-1-phosphate which can then be utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis (PubMed:12849978, PubMed:21855639). Shows broad substrate specificity and can also accept deoxyurid...
Homo sapiens (Human)
O95047
OR2A4_HUMAN
MGDNITSIREFLLLGFPVGPRIQMLLFGLFSLFYVFTLLGNGTILGLISLDSRLHAPMYFFLSHLAVVDIAYACNTVPRMLVNLLHPAKPISFAGRMMQTFLFSTFAVTECLLLVVMSYDLYVAICHPLRYLAIMTWRVCITLAVTSWTTGVLLSLIHLVLLLPLPFCRPQKIYHFFCEILAVLKLACADTHINENMVLAGAISGLVGPLSTIVVSYMCILCAILQIQSREVQRKAFRTCFSHLCVIGLVYGTAIIMYVGPRYGNPKEQKKYLLLFHSLFNPMLNPLICSLRNSEVKNTLKRVLGVERAL
null
null
detection of chemical stimulus involved in sensory perception of smell [GO:0050911]; positive regulation of cytokinesis [GO:0032467]; regulation of actin cytoskeleton organization [GO:0032956]
cleavage furrow [GO:0032154]; Flemming body [GO:0090543]; mitotic spindle midzone [GO:1990023]; mitotic spindle pole [GO:0097431]; recycling endosome [GO:0055037]
G protein-coupled receptor activity [GO:0004930]; odorant binding [GO:0005549]; olfactory receptor activity [GO:0004984]
PF13853;
1.20.1070.10;
G-protein coupled receptor 1 family
null
SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
null
null
null
null
null
FUNCTION: Odorant receptor. {ECO:0000305}.
Homo sapiens (Human)
O95049
ZO3_HUMAN
MEELTIWEQHTATLSKDPRRGFGIAISGGRDRPGGSMVVSDVVPGGPAEGRLQTGDHIVMVNGVSMENATSAFAIQILKTCTKMANITVKRPRRIHLPATKASPSSPGRQDSDEDDGPQRVEEVDQGRGYDGDSSSGSGRSWDERSRRPRPGRRGRAGSHGRRSPGGGSEANGLALVSGFKRLPRQDVQMKPVKSVLVKRRDSEEFGVKLGSQIFIKHITDSGLAARHRGLQEGDLILQINGVSSQNLSLNDTRRLIEKSEGKLSLLVLRDRGQFLVNIPPAVSDSDSSPLEDISDLASELSQAPPSHIPPPPRHAQRSP...
null
null
cell-cell adhesion [GO:0098609]; cell-cell junction organization [GO:0045216]; establishment of endothelial intestinal barrier [GO:0090557]; maintenance of blood-brain barrier [GO:0035633]; positive regulation of blood-brain barrier permeability [GO:1905605]; protein localization to cell-cell junction [GO:0150105]
bicellular tight junction [GO:0005923]; cell junction [GO:0030054]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
cell adhesion molecule binding [GO:0050839]
PF00625;PF00595;PF07653;
2.30.42.10;3.40.50.300;2.30.30.40;
MAGUK family
PTM: Phosphorylated (By similarity). {ECO:0000250|UniProtKB:O62683}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21411630}; Peripheral membrane protein {ECO:0000269|PubMed:21411630}; Cytoplasmic side {ECO:0000269|PubMed:21411630}. Cell junction, tight junction {ECO:0000269|PubMed:21411630, ECO:0000269|PubMed:23608536}. Nucleus {ECO:0000269|PubMed:23608536}. Note=Exhibits pre...
null
null
null
null
null
FUNCTION: TJP1, TJP2, and TJP3 are closely related scaffolding proteins that link tight junction (TJ) transmembrane proteins such as claudins, junctional adhesion molecules, and occludin to the actin cytoskeleton (PubMed:16129888). The tight junction acts to limit movement of substances through the paracellular space a...
Homo sapiens (Human)
O95050
INMT_HUMAN
MKGGFTGGDEYQKHFLPRDYLATYYSFDGSPSPEAEMLKFNLECLHKTFGPGGLQGDTLIDIGSGPTIYQVLAACDSFQDITLSDFTDRNREELEKWLKKEPGAYDWTPAVKFACELEGNSGRWEEKEEKLRAAVKRVLKCDVHLGNPLAPAVLPLADCVLTLLAMECACCSLDAYRAALCNLASLLKPGGHLVTTVTLRLPSYMVGKREFSCVALEKEEVEQAVLDAGFDIEQLLHSPQSYSVTNAANNGVCFIVARKKPGP
2.1.1.49; 2.1.1.96
null
amine metabolic process [GO:0009308]; methylation [GO:0032259]; response to toxic substance [GO:0009636]
cytosol [GO:0005829]
amine N-methyltransferase activity [GO:0030748]; N-methyltransferase activity [GO:0008170]; S-adenosyl-L-methionine:beta-alanine N-methyltransferase activity [GO:0102707]; thioether S-methyltransferase activity [GO:0004790]
PF01234;
3.40.50.150;
Class I-like SAM-binding methyltransferase superfamily, NNMT/PNMT/TEMT family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=a tertiary amine + S-adenosyl-L-methionine = a methylated tertiary amine + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:53928, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:137982, ChEBI:CHEBI:137983; EC=2.1.1.49; Evidence={ECO:0000269|PubMed:10552930}; CATALYTIC ...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.9 mM for tryptamine {ECO:0000269|PubMed:10552930};
null
null
null
FUNCTION: Functions as a thioether S-methyltransferase and is active with a variety of thioethers and the corresponding selenium and tellurium compounds, including 3-methylthiopropionaldehyde, dimethyl selenide, dimethyl telluride, 2-methylthioethylamine, 2-methylthioethanol, methyl-n-propyl sulfide and diethyl sulfide...
Homo sapiens (Human)
O95057
DIRA1_HUMAN
MPEQSNDYRVVVFGAGGVGKSSLVLRFVKGTFRDTYIPTIEDTYRQVISCDKSVCTLQITDTTGSHQFPAMQRLSISKGHAFILVFSVTSKQSLEELGPIYKLIVQIKGSVEDIPVMLVGNKCDETQREVDTREAQAVAQEWKCAFMETSAKMNYNVKELFQELLTLETRRNMSLNIDGKRSGKQKRTDRVKGKCTLM
null
null
signal transduction [GO:0007165]
plasma membrane [GO:0005886]
GDP binding [GO:0019003]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]
PF00071;
3.40.50.300;
Small GTPase superfamily, Di-Ras family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
null
null
null
null
null
FUNCTION: Displays low GTPase activity and exists predominantly in the GTP-bound form. {ECO:0000269|PubMed:12194967}.
Homo sapiens (Human)
O95059
RPP14_HUMAN
MPAPAATYERVVYKNPSEYHYMKVCLEFQDCGVGLNAAQFKQLLISAVKDLFGEVDAALPLDILTYEEKTLSAILRICSSGLVKLWSSLTLLGSYKGKKCAFRVIQVSPFLLALSGNSRELVLD
null
null
tRNA 5'-leader removal [GO:0001682]
multimeric ribonuclease P complex [GO:0030681]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]
ribonuclease P activity [GO:0004526]; ribonuclease P RNA binding [GO:0033204]
PF01900;
3.30.70.3250;
Eukaryotic/archaeal RNase P protein component 2 family
null
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:10444065, ECO:0000305}.
null
null
null
null
null
FUNCTION: Component of ribonuclease P, a ribonucleoprotein complex that generates mature tRNA molecules by cleaving their 5'-ends. {ECO:0000269|PubMed:10024167, ECO:0000269|PubMed:30454648}.
Homo sapiens (Human)
O95067
CCNB2_HUMAN
MALLRRPTVSSDLENIDTGVNSKVKSHVTIRRTVLEEIGNRVTTRAAQVAKKAQNTKVPVQPTKTTNVNKQLKPTASVKPVQMEKLAPKGPSPTPEDVSMKEENLCQAFSDALLCKIEDIDNEDWENPQLCSDYVKDIYQYLRQLEVLQSINPHFLDGRDINGRMRAILVDWLVQVHSKFRLLQETLYMCVGIMDRFLQVQPVSRKKLQLVGITALLLASKYEEMFSPNIEDFVYITDNAYTSSQIREMETLILKELKFELGRPLPLHFLRRASKAGEVDVEQHTLAKYLMELTLIDYDMVHYHPSKVAAAASCLSQKVL...
null
null
cell division [GO:0051301]; G2/MI transition of meiotic cell cycle [GO:0008315]; in utero embryonic development [GO:0001701]; mitotic cell cycle phase transition [GO:0044772]; regulation of growth [GO:0040008]; spindle assembly involved in female meiosis I [GO:0007057]; T cell homeostasis [GO:0043029]; thymus developme...
centrosome [GO:0005813]; cyclin-dependent protein kinase holoenzyme complex [GO:0000307]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; microtubule cytoskeleton [GO:0015630]; nucleus [GO:0005634]
cadherin binding [GO:0045296]; cyclin-dependent protein serine/threonine kinase regulator activity [GO:0016538]
PF02984;PF00134;
1.10.472.10;
Cyclin family, Cyclin AB subfamily
null
null
null
null
null
null
null
FUNCTION: Essential for the control of the cell cycle at the G2/M (mitosis) transition.
Homo sapiens (Human)
O95069
KCNK2_HUMAN
MLPSASRERPGYRAGVAAPDLLDPKSAAQNSKPRLSFSTKPTVLASRVESDTTINVMKWKTVSTIFLVVVLYLIIGATVFKALEQPHEISQRTTIVIQKQTFISQHSCVNSTELDELIQQIVAAINAGIIPLGNTSNQISHWDLGSSFFFAGTVITTIGFGNISPRTEGGKIFCIIYALLGIPLFGFLLAGVGDQLGTIFGKGIAKVEDTFIKWNVSQTKIRIISTIIFILFGCVLFVALPAIIFKHIEGWSALDAIYFVVITLTTIGFGDYVAGGSDIEYLDFYKPVVWFWILVGLAYFAAVLSMIGDWLRVISKKTKE...
null
null
cardiac ventricle development [GO:0003231]; cellular response to hypoxia [GO:0071456]; cochlea development [GO:0090102]; G protein-coupled receptor signaling pathway [GO:0007186]; memory [GO:0007613]; negative regulation of cardiac muscle cell proliferation [GO:0060044]; negative regulation of DNA biosynthetic process ...
apical plasma membrane [GO:0016324]; astrocyte projection [GO:0097449]; calyx of Held [GO:0044305]; cell surface [GO:0009986]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; voltage-gated potassium channel complex [GO:00080...
outward rectifier potassium channel activity [GO:0015271]; potassium channel inhibitor activity [GO:0019870]; potassium ion leak channel activity [GO:0022841]
PF07885;
1.10.287.70;
Two pore domain potassium channel (TC 1.A.1.8) family
PTM: Phosphorylation at Ser-348 controls the reversible conversion from a leak channel to a voltage-dependent channel. {ECO:0000269|PubMed:11319556}.
SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:23169818}; Multi-pass membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000269|PubMed:10784345}; Multi-pass membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 4]: Endoplasmic reticulum membrane {ECO:0...
null
null
null
null
null
FUNCTION: Ion channel that contributes to passive transmembrane potassium transport (PubMed:23169818). Reversibly converts between a voltage-insensitive potassium leak channel and a voltage-dependent outward rectifying potassium channel in a phosphorylation-dependent manner (PubMed:11319556). In astrocytes, forms mostl...
Homo sapiens (Human)
O95070
YIF1A_HUMAN
MAYHSGYGAHGSKHRARAAPDPPPLFDDTSGGYSSQPGGYPATGADVAFSVNHLLGDPMANVAMAYGSSIASHGKDMVHKELHRFVSVSKLKYFFAVDTAYVAKKLGLLVFPYTHQNWEVQYSRDAPLPPRQDLNAPDLYIPTMAFITYVLLAGMALGIQKRFSPEVLGLCASTALVWVVMEVLALLLGLYLATVRSDLSTFHLLAYSGYKYVGMILSVLTGLLFGSDGYYVALAWTSSALMYFIVRSLRTAALGPDSMGGPVPRQRLQLYLTLGAAAFQPLIIYWLTFHLVR
null
null
endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; protein transport [GO:0015031]
COPII-coated ER to Golgi transport vesicle [GO:0030134]; endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; intracellular me...
null
PF03878;
null
YIF1 family
null
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15308636}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:15308636, ECO:0000269|PubMed:15990086, ECO:0000269|PubMed:26077767}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum-Golgi intermed...
null
null
null
null
null
FUNCTION: Possible role in transport between endoplasmic reticulum and Golgi. {ECO:0000269|PubMed:15990086}.
Homo sapiens (Human)
O95071
UBR5_HUMAN
MTSIHFVVHPLPGTEDQLNDRLREVSEKLNKYNLNSHPPLNVLEQATIKQCVVGPNHAAFLLEDGRVCRIGFSVQPDRLELGKPDNNDGSKLNSNSGAGRTSRPGRTSDSPWFLSGSETLGRLAGNTLGSRWSSGVGGSGGGSSGRSSAGARDSRRQTRVIRTGRDRGSGLLGSQPQPVIPASVIPEELISQAQVVLQGKSRSVIIRELQRTNLDVNLAVNNLLSRDDEDGDDGDDTASESYLPGEDLMSLLDADIHSAHPSVIIDADAMFSEDISYFGYPSFRRSSLSRLGSSRVLLLPLERDSELLRERESVLRLRER...
2.3.2.26
null
DNA damage response [GO:0006974]; DNA repair [GO:0006281]; DNA repair-dependent chromatin remodeling [GO:0140861]; heterochromatin boundary formation [GO:0033696]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of gene expression [GO:0010628]; positive regulation of protein imp...
cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; protein-containing complex [GO:0032991]
RNA binding [GO:0003723]; ubiquitin binding [GO:0043130]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-ubiquitin ligase activity [GO:0034450]; zinc ion binding [GO:0008270]
PF11547;PF00632;PF00658;
1.10.1900.10;1.10.8.10;3.30.2160.10;3.30.2410.10;3.90.1750.10;2.130.10.30;
null
null
SUBCELLULAR LOCATION: Nucleus.
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;
null
PATHWAY: Protein modification; protein ubiquitination.
null
null
FUNCTION: E3 ubiquitin-protein ligase which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation (By similarity). Involved in maturation and/or transc...
Homo sapiens (Human)
O95072
REC8_HUMAN
MFYYPNVLQRHTGCFATIWLAATRGSRLVKREYLRVNVVKTCEEILNYVLVRVQPPQPGLPRPRFSLYLSAQLQIGVIRVYSQQCQYLVEDIQHILERLHRAQLQIRIDMETELPSLLLPNHLAMMETLEDAPDPFFGMMSVDPRLPSPFDIPQIRHLLEAAIPERVEEIPPEVPTEPREPERIPVTVLPPEAITILEAEPIRMLEIEGERELPEVSRRELDLLIAEEEEAILLEIPRLPPPAPAEVEGIGEALGPEELRLTGWEPGALLMEVTPPEELRLPAPPSPERRPPVPPPPRRRRRRRLLFWDKETQISPEKFQ...
null
null
double-strand break repair [GO:0006302]; fertilization [GO:0009566]; male meiosis I [GO:0007141]; meiotic cell cycle [GO:0051321]; meiotic sister chromatid cohesion [GO:0051177]; oocyte maturation [GO:0001556]; reciprocal meiotic recombination [GO:0007131]; replication-born double-strand break repair via sister chromat...
cohesin complex [GO:0008278]; kinetochore [GO:0000776]; lateral element [GO:0000800]; male germ cell nucleus [GO:0001673]; meiotic cohesin complex [GO:0030893]; nucleus [GO:0005634]
chromatin binding [GO:0003682]
PF04824;PF04825;
1.10.10.580;
Rad21 family
PTM: Phosphorylated. {ECO:0000250}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6AYJ4}. Chromosome {ECO:0000250|UniProtKB:Q6AYJ4}. Chromosome, centromere {ECO:0000250|UniProtKB:Q6AYJ4}. Note=In meiotic chromosomes, localized along axial elements in prophase from the leptotene to diplotene stages. At later prophase stages, diakinesis and metapha...
null
null
null
null
null
FUNCTION: Required during meiosis for separation of sister chromatids and homologous chromosomes. Proteolytic cleavage of REC8 on chromosome arms by separin during anaphase I allows for homologous chromosome separation in meiosis I and cleavage of REC8 on centromeres during anaphase II allows for sister chromatid separ...
Homo sapiens (Human)
O95073
FSBP_HUMAN
MVGKARSSNFTLSEKLDLLKLVKPYVKILEEHTNKHSVIVEKNRCWDIIAVNYNAIGVDRPPRTAQGLRTLYKRLKEYAKQELLQQKETQSDFKSNISEPTKKVMEMIPQISSFCLVRDRNHIQSANLDEEAQAGTSSLQVMLDHHPVAITVEVKQEEDIKPPPPLVLNSQQSDTLEQREEHELVHVMERSLSPSLSSVDMRMTSSPSSIPRRDDFFRHESGEHFRSLLGYDPQILQMLKEEHQIILENQKNFGLYVQEKRDGLKRRQQLEEELLRAKIEVEKLKAIRLRHDLPEYNSL
null
null
null
nucleoplasm [GO:0005654]; nucleus [GO:0005634]
identical protein binding [GO:0042802]
PF13873;
null
null
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20531236}.
null
null
null
null
null
FUNCTION: Transcriptional repressor that down-regulates the expression of the fibrinogen gamma chain. Represses transcription of GSK3B gene promoter via its interaction with APBA1. {ECO:0000269|PubMed:20531236}.
Homo sapiens (Human)
O95096
NKX22_HUMAN
MSLTNTKTGFSVKDILDLPDTNDEEGSVAEGPEEENEGPEPAKRAGPLGQGALDAVQSLPLKNPFYDSSDNPYTRWLASTEGLQYSLHGLAAGAPPQDSSSKSPEPSADESPDNDKETPGGGGDAGKKRKRRVLFSKAQTYELERRFRQQRYLSAPEREHLASLIRLTPTQVKIWFQNHRYKMKRARAEKGMEVTPLPSPRRVAVPVLVRDGKPCHALKAQDLAAATFQAGIPFSAYSAQSLQHMQYNAQYSSASTPQYPTAHPLVQAQQWTW
null
null
astrocyte differentiation [GO:0048708]; brain development [GO:0007420]; cell differentiation [GO:0030154]; digestive tract development [GO:0048565]; negative regulation of neuron differentiation [GO:0045665]; neuroendocrine cell differentiation [GO:0061101]; neuron fate specification [GO:0048665]; oligodendrocyte devel...
chromatin [GO:0000785]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
cis-regulatory region sequence-specific DNA binding [GO:0000987]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
PF00046;
1.10.10.60;
NK-2 homeobox family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
null
null
null
null
null
FUNCTION: Transcriptional activator involved in the development of insulin-producting beta cells in the endocrine pancreas (By similarity). May also be involved in specifying diencephalic neuromeric boundaries, and in controlling the expression of genes that play a role in axonal guidance. Binds to elements within the ...
Homo sapiens (Human)
O95104
SCAF4_HUMAN
MDAVNAFNQELFSLMDMKPPISRAKMILITKAAIKAIKLYKHVVQIVEKFIKKCKPEYKVPGLYVIDSIVRQSRHQFGTDKDVFGPRFSKNITATFQYLYLCPSEDKSKIVRVLNLWQKNGVFKIEIIQPLLDMAAGTSNAAPVAENVTNNEGSPPPPVKVSSEPPTQATPNSVPAVPQLPSSDAFAAVAQLFQTTQGQQLQQILQTFQQPPKPQSPALDNAVMAQVQAITAQLKTTPTQPSEQKAAFPPPEQKTAFDKKLLDRFDYDDEPEAVEESKKEDTTAVTTTAPAAAVPPAPTATVPAAAAPAAASPPPPQAPF...
null
null
negative regulation of termination of RNA polymerase II transcription, poly(A)-coupled [GO:2000805]
nucleoplasm [GO:0005654]; nucleus [GO:0005634]
RNA binding [GO:0003723]; RNA polymerase II C-terminal domain phosphoserine binding [GO:1990269]
PF04818;PF00076;
1.25.40.90;3.30.70.330;
null
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:31104839}.
null
null
null
null
null
FUNCTION: Anti-terminator protein required to prevent early mRNA termination during transcription (PubMed:31104839). Together with SCAF8, acts by suppressing the use of early, alternative poly(A) sites, thereby preventing the accumulation of non-functional truncated proteins (PubMed:31104839). Mechanistically, associat...
Homo sapiens (Human)
O95125
ZN202_HUMAN
MATAVEPEDQDLWEEEGILMVKLEDDFTCRPESVLQRDDPVLETSHQNFRRFRYQEAASPREALIRLRELCHQWLRPERRTKEQILELLVLEQFLTVLPGELQSWVRGQRPESGEEAVTLVEGLQKQPRRPRRWVTVHVHGQEVLSEETVHLGVEPESPNELQDPVQSSTPEQSPEETTQSPDLGAPAEQRPHQEEELQTLQESEVPVPEDPDLPAERSSGDSEMVALLTALSQGLVTFKDVAVCFSQDQWSDLDPTQKEFYGEYVLEEDCGIVVSLSFPIPRPDEISQVREEEPWVPDIQEPQETQEPEILSFTYTGDR...
null
null
lipid metabolic process [GO:0006629]; negative regulation of transcription by RNA polymerase II [GO:0000122]; regulation of transcription by RNA polymerase II [GO:0006357]
chromosome [GO:0005694]; nuclear body [GO:0016604]; nucleolus [GO:0005730]
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
PF01352;PF02023;PF00096;
6.10.140.140;3.30.160.60;1.10.4020.10;
null
null
SUBCELLULAR LOCATION: Nucleus.
null
null
null
null
null
FUNCTION: Transcriptional repressor that binds to elements found predominantly in genes that participate in lipid metabolism. Among its targets are structural components of lipoprotein particles (apolipoproteins AIV, CIII, and E), enzymes involved in lipid processing (lipoprotein lipase, lecithin cholesteryl ester tran...
Homo sapiens (Human)
O95136
S1PR2_HUMAN
MGSLYSEYLNPNKVQEHYNYTKETLETQETTSRQVASAFIVILCCAIVVENLLVLIAVARNSKFHSAMYLFLGNLAASDLLAGVAFVANTLLSGSVTLRLTPVQWFAREGSAFITLSASVFSLLAIAIERHVAIAKVKLYGSDKSCRMLLLIGASWLISLVLGGLPILGWNCLGHLEACSTVLPLYAKHYVLCVVTIFSIILLAIVALYVRIYCVVRSSHADMAAPQTLALLKTVTIVLGVFIVCWLPAFSILLLDYACPVHSCPILYKAHYFFAVSTLNSLLNPVIYTWRSRDLRREVLRPLQCWRPGVGVQGRRRGGT...
null
null
actin cytoskeleton organization [GO:0030036]; adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; excitatory postsynaptic potential [GO:0060079]; filopodium assembly [GO:0046847]; G protein-coupled receptor signaling pathway [GO:0007186]; negative regulation of excitatory postsynapti...
cytoplasm [GO:0005737]; plasma membrane [GO:0005886]; postsynapse [GO:0098794]
G protein-coupled peptide receptor activity [GO:0008528]; G protein-coupled receptor activity [GO:0004930]; G protein-coupled receptor binding [GO:0001664]; integrin binding [GO:0005178]; lipid binding [GO:0008289]; sphingosine-1-phosphate receptor activity [GO:0038036]
PF00001;
1.20.1070.10;
G-protein coupled receptor 1 family
null
SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
null
null
null
null
null
FUNCTION: Receptor for the lysosphingolipid sphingosine 1-phosphate (S1P) (PubMed:10617617). S1P is a bioactive lysophospholipid that elicits diverse physiological effects on most types of cells and tissues (PubMed:10617617). When expressed in rat HTC4 hepatoma cells, is capable of mediating S1P-induced cell proliferat...
Homo sapiens (Human)
O95139
NDUB6_HUMAN
MTGYTPDEKLRLQQLRELRRRWLKDQELSPREPVLPPQKMGPMEKFWNKFLENKSPWRKMVHGVYKKSIFVFTHVLVPVWIIHYYMKYHVSEKPYGIVEKKSRIFPGDTILETGEVIPPMKEFPDQHH
null
null
aerobic respiration [GO:0009060]; mitochondrial ATP synthesis coupled electron transport [GO:0042775]; 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]
mitochondrial inner membrane [GO:0005743]; mitochondrial membrane [GO:0031966]; mitochondrial respiratory chain complex I [GO:0005747]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]
NADH dehydrogenase (ubiquinone) activity [GO:0008137]
PF09782;
null
Complex I NDUFB6 subunit family
null
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305|PubMed:12611891}; Single-pass membrane protein {ECO:0000255}; Matrix side {ECO:0000305}.
null
null
null
null
null
FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. ...
Homo sapiens (Human)
O95140
MFN2_HUMAN
MSLLFSRCNSIVTVKKNKRHMAEVNASPLKHFVTAKKKINGIFEQLGAYIQESATFLEDTYRNAELDPVTTEEQVLDVKGYLSKVRGISEVLARRHMKVAFFGRTSNGKSTVINAMLWDKVLPSGIGHTTNCFLRVEGTDGHEAFLLTEGSEEKRSAKTVNQLAHALHQDKQLHAGSLVSVMWPNSKCPLLKDDLVLMDSPGIDVTTELDSWIDKFCLDADVFVLVANSESTLMQTEKHFFHKVSERLSRPNIFILNNRWDASASEPEYMEEVRRQHMERCTSFLVDELGVVDRSQAGDRIFFVSAKEVLNARIQKAQGM...
3.6.5.-
null
aerobic respiration [GO:0009060]; apoptotic process [GO:0006915]; blastocyst formation [GO:0001825]; camera-type eye morphogenesis [GO:0048593]; mitochondrial fusion [GO:0008053]; mitochondrial membrane organization [GO:0007006]; mitochondrion localization [GO:0051646]; negative regulation of Ras protein signal transdu...
cytosol [GO:0005829]; microtubule cytoskeleton [GO:0015630]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]
GTP binding [GO:0005525]; GTPase activity [GO:0003924]; ubiquitin protein ligase binding [GO:0031625]
PF00350;PF04799;
1.20.5.110;3.40.50.300;
TRAFAC class dynamin-like GTPase superfamily, Dynamin/Fzo/YdjA family, Mitofusin subfamily
PTM: Phosphorylated by PINK1. {ECO:0000269|PubMed:23620051}.; PTM: Ubiquitinated by non-degradative ubiquitin by PRKN, promoting mitochondrial fusion; deubiquitination by USP30 inhibits mitochondrial fusion (PubMed:23620051). Ubiquitinated by HUWE1 when dietary stearate (C18:0) levels are low; ubiquitination inhibits m...
SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:11181170, ECO:0000269|PubMed:11950885, ECO:0000269|PubMed:12499352, ECO:0000269|PubMed:23620051, ECO:0000269|PubMed:26214738}; Multi-pass membrane protein {ECO:0000269|PubMed:11181170, ECO:0000269|PubMed:11950885, ECO:0000269|PubMed:12499352, ECO:00...
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; Evidence={ECO:0000269|PubMed:28114303}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000269|PubMed:28114303}...
null
null
null
null
FUNCTION: Mitochondrial outer membrane GTPase that mediates mitochondrial clustering and fusion (PubMed:11181170, PubMed:11950885, PubMed:19889647, PubMed:26214738, PubMed:28114303). Mitochondria are highly dynamic organelles, and their morphology is determined by the equilibrium between mitochondrial fusion and fissio...
Homo sapiens (Human)
O95147
DUS14_HUMAN
MSSRGHSTLPRTLMAPRMISEGDIGGIAQITSSLFLGRGSVASNRHLLQARGITCIVNATIEIPNFNWPQFEYVKVPLADMPHAPIGLYFDTVADKIHSVSRKHGATLVHCAAGVSRSATLCIAYLMKFHNVCLLEAYNWVKARRPVIRPNVGFWRQLIDYERQLFGKSTVKMVQTPYGIVPDVYEKESRHLMPYWGI
3.1.3.16; 3.1.3.48
null
dephosphorylation [GO:0016311]
cytoplasm [GO:0005737]
MAP kinase tyrosine/serine/threonine phosphatase activity [GO:0017017]; myosin phosphatase activity [GO:0017018]; protein tyrosine phosphatase activity [GO:0004725]; RNA binding [GO:0003723]
PF00782;
3.90.190.10;
Protein-tyrosine phosphatase family, Non-receptor class dual specificity subfamily
null
null
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:0000255|PROSITE-ProRule:PRU10044}; CATALYTIC ACTIVI...
null
null
null
null
FUNCTION: Involved in the inactivation of MAP kinases. Dephosphorylates ERK, JNK and p38 MAP-kinases. Plays a negative role in TCR signaling by dephosphorylating MAP3K7 adapter TAB1 leading to its inactivation (PubMed:24403530). {ECO:0000269|PubMed:24403530}.
Homo sapiens (Human)
O95149
SPN1_HUMAN
MEELSQALASSFSVSQDLNSTAAPHPRLSQYKSKYSSLEQSERRRRLLELQKSKRLDYVNHARRLAEDDWTGMESEEENKKDDEEMDIDTVKKLPKHYANQLMLSEWLIDVPSDLGQEWIVVVCPVGKRALIVASRGSTSAYTKSGYCVNRFSSLLPGGNRRNSTAKDYTILDCIYNEVNQTYYVLDVMCWRGHPFYDCQTDFRFYWMHSKLPEEEGLGEKTKLNPFKFVGLKNFPCTPESLCDVLSMDFPFEVDGLLFYHKQTHYSPGSTPLVGWLRPYMVSDVLGVAVPAGPLTTKPDYAGHQLQQIMEHKKSQKEGM...
null
null
protein import into nucleus [GO:0006606]; RNA import into nucleus [GO:0006404]; snRNA import into nucleus [GO:0061015]
cytosol [GO:0005829]; NLS-dependent protein nuclear import complex [GO:0042564]; nuclear pore [GO:0005643]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]
nuclear import signal receptor activity [GO:0061608]; RNA cap binding [GO:0000339]
PF11538;
3.30.470.30;
Snurportin family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10209022, ECO:0000269|PubMed:15920472}. Cytoplasm {ECO:0000269|PubMed:12095920, ECO:0000269|PubMed:9670026, ECO:0000305|PubMed:10209022}. Note=Nucleoplasmic shuttling protein. Its nuclear import involves the nucleocytoplasmic transport receptor importin beta (PubMed:102...
null
null
null
null
null
FUNCTION: Functions as an U snRNP-specific nuclear import adapter. Involved in the trimethylguanosine (m3G)-cap-dependent nuclear import of U snRNPs. Binds specifically to the terminal m3G-cap U snRNAs. {ECO:0000269|PubMed:10209022, ECO:0000269|PubMed:15920472, ECO:0000269|PubMed:16030253, ECO:0000269|PubMed:9670026}.
Homo sapiens (Human)
O95150
TNF15_HUMAN
MAEDLGLSFGETASVEMLPEHGSCRPKARSSSARWALTCCLVLLPFLAGLTTYLLVSQLRAQGEACVQFQALKGQEFAPSHQQVYAPLRADGDKPRAHLTVVRQTPTQHFKNQFPALHWEHELGLAFTKNRMNYTNKFLLIPESGDYFIYSQVTFRGMTSECSEIRQAGRPNKPDSITVVITKVTDSYPEPTQLLMGTKSVCEVGSNWFQPIYLGAMFSLQEGDKLMVNVSDISLVDYTKEDKTFFGAFLL
null
null
activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; activation of NF-kappaB-inducing kinase activity [GO:0007250]; immune response [GO:0006955]; signal transduction [GO:0007165]
extracellular space [GO:0005615]; membrane [GO:0016020]; plasma membrane [GO:0005886]
cytokine activity [GO:0005125]; signaling receptor binding [GO:0005102]; tumor necrosis factor receptor binding [GO:0005164]
PF00229;
2.60.120.40;
Tumor necrosis factor family
null
SUBCELLULAR LOCATION: Membrane {ECO:0000305|PubMed:11911831, ECO:0000305|PubMed:11923219}; Single-pass type II membrane protein {ECO:0000305|PubMed:11911831, ECO:0000305|PubMed:11923219}.; SUBCELLULAR LOCATION: [Tumor necrosis factor ligand superfamily member 15, secreted form]: Secreted.
null
null
null
null
null
FUNCTION: Receptor for TNFRSF25 and TNFRSF6B. Mediates activation of NF-kappa-B. Inhibits vascular endothelial growth and angiogenesis (in vitro). Promotes activation of caspases and apoptosis. {ECO:0000269|PubMed:10597252, ECO:0000269|PubMed:11911831, ECO:0000269|PubMed:11923219, ECO:0000269|PubMed:9872942}.
Homo sapiens (Human)
O95153
RIMB1_HUMAN
MEQLTTLPRPGDPGAMEPWALPTWHSWTPGRGGEPSSAAPSIADTPPAALQLQELRSEESSKPKGDGSSRPVGGTDPEGAEACLPSLGQQASSSGPACQRPEDEEVEAFLKAKLNMSFGDRPNLELLRALGELRQRCAILKEENQMLRKSSFPETEEKVRRLKRKNAELAVIAKRLEERARKLQETNLRVVSAPLPRPGTSLELCRKALARQRARDLSETASALLAKDKQIAALQRECRELQARLTLVGKEGPQWLHVRDFDRLLRESQREVLRLQRQIALRNQRETLPLPPSWPPGPALQARAGAPAPGAPGEATPQED...
null
null
regulation of neurotransmitter secretion [GO:0046928]
calyx of Held [GO:0044305]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; glutamatergic synapse [GO:0098978]; mitochondrion [GO:0005739]
benzodiazepine receptor binding [GO:0030156]; voltage-gated calcium channel activity involved in regulation of presynaptic cytosolic calcium levels [GO:0099626]
PF07653;PF14604;
2.60.40.10;2.30.30.40;
RIMBP family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9915832}. Mitochondrion {ECO:0000269|PubMed:9915832}. Note=Preferentially expressed in the mitochondria in the presence of TSPO.
null
null
null
null
null
FUNCTION: Required for synaptic transmission regulation (PubMed:33539324). It probably controls the recruitement of voltage-gated calcium channels to the presynaptic membrane, and modulates neurotransmitter release. {ECO:0000269|PubMed:33539324}.
Homo sapiens (Human)
O95154
ARK73_HUMAN
MSRQLSRARPATVLGAMEMGRRMDAPTSAAVTRAFLERGHTEIDTAFVYSEGQSETILGGLGLRLGGSDCRVKIDTKAIPLFGNSLKPDSLRFQLETSLKRLQCPRVDLFYLHMPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKSNGWILPTVYQGMYNAITRQVETELFPCLRHFGLRFYAFNPLAGGLLTGKYKYEDKNGKQPVGRFFGNTWAEMYRNRYWKEHHFEGIALVEKALQAAYGASAPSMTSATLRWMYHHSQLQGAHGDAVILGMSSLEQLEQNLAAAEEGPLEPAVVDAFNQAWH...
1.-.-.-
null
cellular aldehyde metabolic process [GO:0006081]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]
aldo-keto reductase (NADP) activity [GO:0004033]; electron transfer activity [GO:0009055]; identical protein binding [GO:0042802]
PF00248;
3.20.20.100;
Aldo/keto reductase family, Aldo/keto reductase 2 subfamily
null
SUBCELLULAR LOCATION: Cytoplasm.
null
null
null
null
null
FUNCTION: Can reduce the dialdehyde protein-binding form of aflatoxin B1 (AFB1) to the non-binding AFB1 dialcohol. May be involved in protection of liver against the toxic and carcinogenic effects of AFB1, a potent hepatocarcinogen. {ECO:0000269|PubMed:18416522}.
Homo sapiens (Human)
O95155
UBE4B_HUMAN
MEELSADEIRRRRLARLAGGQTSQPTTPLTSPQRENPPGPPIAASAPGPSQSLGLNVHNMTPATSPIGASGVAHRSQSSEGVSSLSSSPSNSLETQSQSLSRSQSMDIDGVSCEKSMSQVDVDSGIENMEVDENDRREKRSLSDKEPSSGPEVSEEQALQLVCKIFRVSWKDRDRDVIFLSSLSAQFKQNPKEVFSDFKDLIGQILMEVLMMSTQTRDENPFASLTATSQPIAAAARSPDRNLLLNTGSNPGTSPMFCSVASFGASSLSSLYESSPAPTPSFWSSVPVMGPSLASPSRAASQLAVPSTPLSPHSAASGTA...
2.3.2.27
null
ERAD pathway [GO:0036503]; granzyme-mediated apoptotic signaling pathway [GO:0008626]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein polyubiquitination [GO:0000209]; response to UV [GO:0009411]; ubiquitin-dependent protein catabolic process [GO:0006511]
cytoplasm [GO:0005737]; nucleus [GO:0005634]; ubiquitin ligase complex [GO:0000151]
enzyme binding [GO:0019899]; ubiquitin-ubiquitin ligase activity [GO:0034450]
PF04564;PF10408;
3.30.40.10;
Ubiquitin conjugation factor E4 family
PTM: Proteolytically cleaved by caspases during apoptosis. Cleaved efficiently at Asp-123 by caspase-6 and granzyme B. Cleaved with approximately 10-fold less efficiency at Asp-109 by caspase-3 and caspase-7. {ECO:0000269|PubMed:11802788}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17369820}. Nucleus {ECO:0000250|UniProtKB:Q9ES00}.
CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q9ES00};
null
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:Q9ES00}.
null
null
FUNCTION: Ubiquitin-protein ligase that probably functions as an E3 ligase in conjunction with specific E1 and E2 ligases (By similarity). May also function as an E4 ligase mediating the assembly of polyubiquitin chains on substrates ubiquitinated by another E3 ubiquitin ligase (By similarity). May regulate myosin asse...
Homo sapiens (Human)
O95159
ZFPL1_HUMAN
MGLCKCPKRKVTNLFCFEHRVNVCEHCLVANHAKCIVQSYLQWLQDSDYNPNCRLCNIPLASRETTRLVCYDLFHWACLNERAAQLPRNTAPAGYQCPSCNGPIFPPTNLAGPVASALREKLATVNWARAGLGLPLIDEVVSPEPEPLNTSDFSDWSSFNASSTPGPEEVDSASAAPAFYSQAPRPPASPGRPEQHTVIHMGNPEPLTHAPRKVYDTRDDDRTPGLHGDCDDDKYRRRPALGWLARLLRSRAGSRKRPLTLLQRAGLLLLLGLLGFLALLALMSRLGRAAADSDPNLDPLMNPHIRVGPS
null
null
regulation of DNA-templated transcription [GO:0006355]; vesicle-mediated transport [GO:0016192]
Golgi apparatus [GO:0005794]; membrane [GO:0016020]; nucleus [GO:0005634]
DNA binding [GO:0003677]; zinc ion binding [GO:0008270]
null
3.30.40.10;
ZFPL1 family
PTM: Phosphorylated. {ECO:0000269|PubMed:18323775}.
SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane {ECO:0000269|PubMed:18323775}; Single-pass membrane protein {ECO:0000269|PubMed:18323775}.
null
null
null
null
null
FUNCTION: Required for cis-Golgi integrity and efficient ER to Golgi transport. Involved in the maintenance of the integrity of the cis-Golgi, possibly via its interaction with GOLGA2/GM130. {ECO:0000269|PubMed:18323775}.
Homo sapiens (Human)
O95163
ELP1_HUMAN
MRNLKLFRTLEFRDIQGPGNPQCFSLRTEQGTVLIGSEHGLIEVDPVSREVKNEVSLVAEGFLPEDGSGRIVGVQDLLDQESVCVATASGDVILCSLSTQQLECVGSVASGISVMSWSPDQELVLLATGQQTLIMMTKDFEPILEQQIHQDDFGESKFITVGWGRKETQFHGSEGRQAAFQMQMHESALPWDDHRPQVTWRGDGQFFAVSVVCPETGARKVRVWNREFALQSTSEPVAGLGPALAWKPSGSLIASTQDKPNQQDIVFFEKNGLLHGHFTLPFLKDEVKVNDLLWNADSSVLAVWLEDLQREESSIPKTCV...
null
null
regulation of translation [GO:0006417]; tRNA wobble base 5-methoxycarbonylmethyl-2-thiouridinylation [GO:0002926]; tRNA wobble uridine modification [GO:0002098]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; elongator holoenzyme complex [GO:0033588]; nucleus [GO:0005634]
protein self-association [GO:0043621]; tRNA binding [GO:0000049]
PF04762;
2.130.10.10;
ELP1/IKA1 family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11714725, ECO:0000269|PubMed:11818576, ECO:0000269|PubMed:22854966}. Nucleus {ECO:0000269|PubMed:11714725, ECO:0000269|PubMed:11818576}.
null
null
PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis. {ECO:0000303|PubMed:29332244}.
null
null
FUNCTION: Component of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine) (PubMed:29332244). The elongator complex catalyzes the formation of carboxymethyluridi...
Homo sapiens (Human)
O95166
GBRAP_HUMAN
MKFVYKEEHPFEKRRSEGEKIRKKYPDRVPVIVEKAPKARIGDLDKKKYLVPSDLTVGQFYFLIRKRIHLRAEDALFFFVNNVIPPTSATMGQLYQEHHEEDFFLYIAYSDESVYGL
null
null
autophagosome assembly [GO:0000045]; autophagosome maturation [GO:0097352]; cellular response to nitrogen starvation [GO:0006995]; chemical synaptic transmission [GO:0007268]; extrinsic apoptotic signaling pathway via death domain receptors [GO:0008625]; microtubule cytoskeleton organization [GO:0000226]; positive regu...
actin cytoskeleton [GO:0015629]; autophagosome [GO:0005776]; autophagosome membrane [GO:0000421]; axoneme [GO:0005930]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; Golgi membrane [GO:0000139]; lysosome [GO:0005764]; microtubule [GO:0005874]; microtubule associated complex [GO:0005875]; plasma membrane [GO:0...
beta-tubulin binding [GO:0048487]; GABA receptor binding [GO:0050811]; microtubule binding [GO:0008017]; phosphatidylethanolamine binding [GO:0008429]; ubiquitin protein ligase binding [GO:0031625]
PF02991;
null
ATG8 family
PTM: The precursor molecule is cleaved by ATG4 (ATG4A, ATG4B, ATG4C or ATG4D) to expose the glycine at the C-terminus and form the cytosolic form, GABARAP-I (PubMed:15169837, PubMed:20818167, PubMed:30661429). The processed form is then activated by APG7L/ATG7, transferred to ATG3 and conjugated to phosphatidylethanola...
SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome membrane {ECO:0000269|PubMed:12507496, ECO:0000269|PubMed:15169837, ECO:0000269|PubMed:17580304, ECO:0000269|PubMed:19056683}. Endomembrane system {ECO:0000250|UniProtKB:P60517}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P60517}. Golgi apparatus membrane {EC...
null
null
null
null
null
FUNCTION: Ubiquitin-like modifier that plays a role in intracellular transport of GABA(A) receptors and its interaction with the cytoskeleton (PubMed:9892355). Involved in autophagy: while LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autopha...
Homo sapiens (Human)
O95167
NDUA3_HUMAN
MAARVGAFLKNAWDKEPVLVVSFVVGGLAVILPPLSPYFKYSVMINKATPYNYPVPVRDDGNMPDVPSHPQDPQGPSLEWLKKL
null
null
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]
mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex I [GO:0005747]; mitochondrion [GO:0005739]
NADH dehydrogenase (ubiquinone) activity [GO:0008137]
PF14987;
null
Complex I NDUFA3 subunit family
null
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305|PubMed:12611891}; Single-pass membrane protein {ECO:0000255}.
null
null
null
null
null
FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. ...
Homo sapiens (Human)
O95168
NDUB4_HUMAN
MSFPKYKPSSLRTLPETLDPAEYNISPETRRAQAERLAIRAQLKREYLLQYNDPNRRGLIENPALLRWAYARTINVYPNFRPTPKNSLMGALCGFGPLIFIYYIIKTERDRKEKLIQEGKLDRTFHLSY
null
null
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 respiratory chain complex I [GO:0005747]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]
NADH dehydrogenase (ubiquinone) activity [GO:0008137]
PF07225;
null
Complex I NDUFB4 subunit family
null
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305|PubMed:12611891}; Single-pass membrane protein {ECO:0000255}; Matrix side {ECO:0000305}.
null
null
null
null
null
FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. ...
Homo sapiens (Human)
O95169
NDUB8_HUMAN
MAVARAGVLGVQWLQRASRNVMPLGARTASHMTKDMFPGPYPRTPEERAAAAKKYNMRVEDYEPYPDDGMGYGDYPKLPDRSQHERDPWYSWDQPGLRLNWGEPMHWHLDMYNRNRVDTSPTPVSWHVMCMQLFGFLAFMIFMCWVGDVYPVYQPVGPKQYPYNNLYLERGGDPSKEPERVVHYEI
null
null
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]
endoplasmic reticulum [GO:0005783]; mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrial respiratory chain complex I [GO:0005747]; mitochondrion [GO:0005739]
NADH dehydrogenase (ubiquinone) activity [GO:0008137]
PF05821;
null
Complex I NDUFB8 subunit family
null
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305|PubMed:12611891}; Single-pass membrane protein {ECO:0000255}; Matrix side {ECO:0000305}.
null
null
null
null
null
FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. ...
Homo sapiens (Human)
O95171
SCEL_HUMAN
MSNVTLRKMSPTGNEMKSTTQGTTRKQQDFHEVNKRRTFLQDNSWIKKRPEEEKDENYGRVVLNRHNSHDALDRKVNERDVPKATISRYSSDDTLDRISDRNDAAKTYKANTLDNQLTNRSMSMFRSLEVTKLQPGGSLNANTSNTIASTSATTPVKKKRQSWFPPPPPGYNASSSTGTRRREPGVHPPIPPKPSSPVSSPNQLRQDNRQIHPPKPGVYTETNRSAERNIRSQDLDNIVKVATSLQRSDKGEELDNLIKMNKSLNRNQGLDSLFRANPKVEEREKRAKSLESLIYMSTRTDKDGKGIQSLGSPIKVNQRT...
null
null
embryo development ending in birth or egg hatching [GO:0009792]; epidermis development [GO:0008544]; keratinocyte differentiation [GO:0030216]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; response to mechanical stimulus [GO:0009612]
cornified envelope [GO:0001533]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; perinuclear region of cytoplasm [GO:0048471]
metal ion binding [GO:0046872]
null
2.10.110.10;
null
null
SUBCELLULAR LOCATION: Cytoplasm. Membrane. Note=May become cross-linked to membrane proteins by transglutaminase.
null
null
null
null
null
FUNCTION: May function in the assembly or regulation of proteins in the cornified envelope. The LIM domain may be involved in homotypic or heterotypic associations and may function to localize sciellin to the cornified envelope.
Homo sapiens (Human)
O95180
CAC1H_HUMAN
MTEGARAADEVRVPLGAPPPGPAALVGASPESPGAPGREAERGSELGVSPSESPAAERGAELGADEEQRVPYPALAATVFFCLGQTTRPRSWCLRLVCNPWFEHVSMLVIMLNCVTLGMFRPCEDVECGSERCNILEAFDAFIFAFFAVEMVIKMVALGLFGQKCYLGDTWNRLDFFIVVAGMMEYSLDGHNVSLSAIRTVRVLRPLRAINRVPSMRILVTLLLDTLPMLGNVLLLCFFVFFIFGIVGVQLWAGLLRNRCFLDSAFVRNNNLTFLRPYYQTEEGEENPFICSSRRDNGMQKCSHIPGRRELRMPCTLGWE...
null
null
aldosterone biosynthetic process [GO:0032342]; calcium ion import [GO:0070509]; calcium ion import across plasma membrane [GO:0098703]; cellular response to hormone stimulus [GO:0032870]; cellular response to potassium ion [GO:0035865]; cortisol biosynthetic process [GO:0034651]; inorganic cation transmembrane transpor...
membrane [GO:0016020]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; voltage-gated calcium channel complex [GO:0005891]; voltage-gated sodium channel complex [GO:0001518]
high voltage-gated calcium channel activity [GO:0008331]; low voltage-gated calcium channel activity [GO:0008332]; metal ion binding [GO:0046872]; scaffold protein binding [GO:0097110]; voltage-gated monoatomic ion channel activity [GO:0005244]; voltage-gated sodium channel activity [GO:0005248]
PF00520;
1.10.287.70;1.20.120.350;
Calcium channel alpha-1 subunit (TC 1.A.1.11) family, CACNA1H subfamily
PTM: In response to raising of intracellular calcium, the T-type channels are activated by CaM-kinase II.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25907736, ECO:0000269|PubMed:27149520, ECO:0000269|PubMed:27729216, ECO:0000269|PubMed:9670923, ECO:0000269|PubMed:9930755}; Multi-pass membrane protein {ECO:0000305}. Note=Interaction with STAC increases expression at the cell membrane. {ECO:0000269|PubMed:271495...
null
null
null
null
null
FUNCTION: Voltage-sensitive calcium channel that gives rise to T-type calcium currents. T-type calcium channels belong to the 'low-voltage activated (LVA)' group. A particularity of this type of channel is an opening at quite negative potentials, and a voltage-dependent inactivation (PubMed:27149520, PubMed:9670923, Pu...
Homo sapiens (Human)
O95182
NDUA7_HUMAN
MASATRLIQRLRNWASGHDLQGKLQLRYQEISKRTQPPPKLPVGPSHKLSNNYYCTRDGRRESVPPSIIMSSQKALVSGKPAESSAVAATEKKAVTPAPPIKRWELSSDQPYL
null
null
aerobic respiration [GO:0009060]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; mitochondrial translation [GO:0032543]; proton motive force-driven mitochondrial ATP synthesis [GO:0042776]
mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex I [GO:0005747]; mitochondrial ribosome [GO:0005761]; mitochondrion [GO:0005739]
NADH dehydrogenase (ubiquinone) activity [GO:0008137]; structural constituent of ribosome [GO:0003735]
PF07347;
null
Complex I NDUFA7 subunit family
null
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305|PubMed:12611891}; Peripheral membrane protein {ECO:0000305}; Matrix side {ECO:0000305}.
null
null
null
null
null
FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. ...
Homo sapiens (Human)
O95183
VAMP5_HUMAN
MAGIELERCQQQANEVTEIMRNNFGKVLERGVKLAELQQRSDQLLDMSSTFNKTTQNLAQKKCWENIRYRICVGLVVVGVLLIILIVLLVVFLPQSSDSSSAPRTQDAGIASGPGN
null
null
cell differentiation [GO:0030154]; Golgi to plasma membrane protein transport [GO:0043001]; muscle organ development [GO:0007517]; skeletal muscle tissue development [GO:0007519]
cell surface [GO:0009986]; cytoplasmic vesicle membrane [GO:0030659]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; intercalated disc [GO:0014704]; late endosome [GO:0005770]; organelle membrane [GO:0031090]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]
null
PF00957;
1.20.5.110;
Synaptobrevin family
PTM: (Microbial infection) Targeted and hydrolyzed by C.botulinum neurotoxin type X (BoNT/X) which hydrolyzes the 40-Arg-|-Ser-41 bond and probably inhibits neurotransmitter release (PubMed:28770820). It remains unknown whether BoNT/X is ever produced, or what organisms it targets. {ECO:0000269|PubMed:28770820}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}. Endomembrane system {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}. Golgi apparatus, trans-Golgi network membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}. Note=Associated w...
null
null
null
null
null
FUNCTION: May participate in trafficking events that are associated with myogenesis, such as myoblast fusion and/or GLUT4 trafficking.
Homo sapiens (Human)
O95185
UNC5C_HUMAN
MRKGLRATAARCGLGLGYLLQMLVLPALALLSASGTGSAAQDDDFFHELPETFPSDPPEPLPHFLIEPEEAYIVKNKPVNLYCKASPATQIYFKCNSEWVHQKDHIVDERVDETSGLIVREVSIEISRQQVEELFGPEDYWCQCVAWSSAGTTKSRKAYVRIAYLRKTFEQEPLGKEVSLEQEVLLQCRPPEGIPVAEVEWLKNEDIIDPVEDRNFYITIDHNLIIKQARLSDTANYTCVAKNIVAKRKSTTATVIVYVNGGWSTWTEWSVCNSRCGRGYQKRTRTCTNPAPLNGGAFCEGQSVQKIACTTLCPVDGRWT...
null
null
anterior/posterior axon guidance [GO:0033564]; apoptotic process [GO:0006915]; axon guidance [GO:0007411]; brain development [GO:0007420]; chemorepulsion of axon [GO:0061643]; dorsal root ganglion development [GO:1990791]; ectopic germ cell programmed cell death [GO:0035234]; positive regulation of apoptotic process [G...
cell surface [GO:0009986]; dendrite [GO:0030425]; filopodium [GO:0030175]; growth cone [GO:0030426]; lamellipodium [GO:0030027]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; synapse [GO:0045202]
netrin receptor activity [GO:0005042]; netrin receptor activity involved in chemorepulsion [GO:0005043]; protein kinase binding [GO:0019901]; tubulin binding [GO:0015631]
PF00531;PF07679;PF00090;PF17217;PF00791;
2.60.220.30;1.10.533.10;2.60.40.10;2.20.100.10;
Unc-5 family
PTM: Proteolytically cleaved by caspases during apoptosis. The cleavage does not take place when the receptor is associated with netrin ligand. Its cleavage by caspases is required to induce apoptosis. {ECO:0000250|UniProtKB:Q761X5}.; PTM: Phosphorylated on different cytoplasmic tyrosine residues. Phosphorylation of Ty...
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25419706}; Single-pass type I membrane protein {ECO:0000255}. Cell surface {ECO:0000269|PubMed:25419706}. Synapse, synaptosome {ECO:0000250|UniProtKB:Q761X5}. Cell projection, axon {ECO:0000250|UniProtKB:O08747}. Cell projection, dendrite {ECO:0000250|UniProtKB:O0...
null
null
null
null
null
FUNCTION: Receptor for netrin required for axon guidance (By similarity). Mediates axon repulsion of neuronal growth cones in the developing nervous system upon ligand binding (By similarity). NTN1/Netrin-1 binding might cause dissociation of UNC5C from polymerized TUBB3 in microtubules and thereby lead to increased mi...
Homo sapiens (Human)
O95196
CSPG5_HUMAN
MGRAGGGGPGRGPPPLLLFLGAALVLASGAVPAREAGSAVEAEELVKGSPAWEPPANDTREEAGPPAAGEDEASWTAPGGELAGPEEVLQESAAVTGTAWLEADSPGLGGVTAEAGSGDAQALPATLQAPHEVLGQSIMPPAIPEATEASGPPSPTPGDKLSPASELPKESPLEVWLNLGGSTPDPQGPELTYPFQGTLEPQPASDIIDIDYFEGLDGEGRGADLGSFPGSPGTSENHPDTEGETPSWSLLDLYDDFTPFDESDFYPTTSFYDDLDEEEEEEEDDKDAVGGGDLEDENELLVPTGKPGLGPGTGQPTSRW...
null
null
axon regeneration [GO:0031103]; cell projection morphogenesis [GO:0048858]; cytoskeleton organization [GO:0007010]; glial cell projection elongation [GO:0106091]; intracellular transport [GO:0046907]; nervous system development [GO:0007399]; positive regulation of substrate adhesion-dependent cell spreading [GO:1900026...
cell surface [GO:0009986]; endoplasmic reticulum membrane [GO:0005789]; extracellular region [GO:0005576]; GABA-ergic synapse [GO:0098982]; glutamatergic synapse [GO:0098978]; Golgi apparatus [GO:0005794]; Golgi lumen [GO:0005796]; Golgi membrane [GO:0000139]; Golgi-associated vesicle membrane [GO:0030660]; lysosomal l...
growth factor activity [GO:0008083]
PF06566;PF06567;
null
null
PTM: N-glycosylated. {ECO:0000250}.; PTM: O-glycosylated; contains chondroitin sulfate glycans (PubMed:25326458). Part-time proteoglycan, expressed in part as a proteoglycan exhibiting chondroitin sulfate glycans and in part as a non-proteoglycan form (By similarity). The relative amount of both forms depends on tissue...
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9ERQ6}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9ERQ6}. Synaptic cell membrane {ECO:0000250|UniProtKB:Q71M36}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q71M36}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q71M36}...
null
null
null
null
null
FUNCTION: May function as a growth and differentiation factor involved in neuritogenesis. May induce ERBB3 activation. {ECO:0000269|PubMed:15358134}.
Homo sapiens (Human)
O95197
RTN3_HUMAN
MAEPSAATQSHSISSSSFGAEPSAPGGGGSPGACPALGTKSCSSSCADSFVSSSSSQPVSLFSTSQEGLSSLCSDEPSSEIMTSSFLSSSEIHNTGLTILHGEKSHVLGSQPILAKEGKDHLDLLDMKKMEKPQGTSNNVSDSSVSLAAGVHCDRPSIPASFPEHPAFLSKKIGQVEEQIDKETKNPNGVSSREAKTALDADDRFTLLTAQKPPTEYSKVEGIYTYSLSPSKVSGDDVIEKDSPESPFEVIIDKAAFDKEFKDSYKESTDDFGSWSVHTDKESSEDISETNDKLFPLRNKEAGRYPMSALLSRQFSHTNA...
null
null
apoptotic process [GO:0006915]; brain development [GO:0007420]; endoplasmic reticulum tubular network formation [GO:0071787]; endoplasmic reticulum tubular network organization [GO:0071786]; negative regulation of amyloid-beta formation [GO:1902430]; neuron differentiation [GO:0030182]; vesicle-mediated transport [GO:0...
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]
null
PF02453;
1.20.5.2480;
null
null
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12811824, ECO:0000269|PubMed:15286784, ECO:0000269|PubMed:16054885, ECO:0000269|PubMed:16979658, ECO:0000269|PubMed:17031492, ECO:0000269|PubMed:17182608, ECO:0000269|PubMed:17191123, ECO:0000269|PubMed:24262037, ECO:0000269|PubMed:29117567, ECO:0...
null
null
null
null
null
FUNCTION: May be involved in membrane trafficking in the early secretory pathway. Inhibits BACE1 activity and amyloid precursor protein processing. May induce caspase-8 cascade and apoptosis. May favor BCL2 translocation to the mitochondria upon endoplasmic reticulum stress. Induces the formation of endoplasmic reticul...
Homo sapiens (Human)
O95198
KLHL2_HUMAN
METPPLPPACTKQGHQKPLDSKDDNTEKHCPVTVNPWHMKKAFKVMNELRSQNLLCDVTIVAEDMEISAHRVVLAACSPYFHAMFTGEMSESRAKRVRIKEVDGWTLRMLIDYVYTAEIQVTEENVQVLLPAAGLLQLQDVKKTCCEFLESQLHPVNCLGIRAFADMHACTDLLNKANTYAEQHFADVVLSEEFLNLGIEQVCSLISSDKLTISSEEKVFEAVIAWVNHDKDVRQEFMARLMEHVRLPLLPREYLVQRVEEEALVKNSSACKDYLIEAMKYHLLPTEQRILMKSVRTRLRTPMNLPKLMVVVGGQAPKAI...
null
null
protein ubiquitination [GO:0016567]
actin cytoskeleton [GO:0015629]; Cul3-RING ubiquitin ligase complex [GO:0031463]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; lamellipodium [GO:0030027]; ruffle [GO:0001726]
actin binding [GO:0003779]; identical protein binding [GO:0042802]; ubiquitin ligase-substrate adaptor activity [GO:1990756]
PF07707;PF00651;PF01344;
1.25.40.420;2.120.10.80;
null
null
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10397770, ECO:0000269|PubMed:15715669}. Cell projection, ruffle {ECO:0000250|UniProtKB:Q8JZP3}. Cell projection {ECO:0000269|PubMed:15715669}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:F1LZF0}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8JZP3...
null
null
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:23838290}.
null
null
FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that mediates the ubiquitination of target proteins, such as NPTXR, WNK1, WNK3 and WNK4, leading most often to their proteasomal degradation (PubMed:23838290). The BCR(KLHL2) complex catalyzes ubiquitination and degradation of NPT...
Homo sapiens (Human)
O95201
RHIT_HUMAN
MSADGGGIQDTQDKETPPEVPDRGHPHQEMPSKLGEAVPSGDTQESLHIKMEPEEPHSEGASQEDGAQGAWGWAPLSHGSKEKALFLPGGALPSPRIPVLSREGRTRDRQMAAALLTAWSQMPVTFEDVALYLSREEWGRLDHTQQNFYRDVLQKKNGLSLGFPFSRPFWAPQAHGKGEASGSSRQAGDEKEWRGACTGAVEVGQRVQTSSVAALGNVKPFRTRAGRVQWGVPQCAQEAACGRSSGPAKDSGQPAEPDRTPDAAPPDPSPTEPQEYRVPEKPNEEEKGAPESGEEGLAPDSEVGRKSYRCEQCGKGFSWH...
null
null
negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of hydrogen peroxide biosynthetic process [GO:0010729]; positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway [GO:1901030]; regulation of DNA-templated transcription [GO:000...
mitochondrion [GO:0005739]; nucleus [GO:0005634]
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; zinc ion binding [GO:0008270]
PF01352;PF00096;
6.10.140.140;3.30.160.60;
Krueppel C2H2-type zinc-finger protein family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
null
null
null
null
null
FUNCTION: Transcriptional repressor involved in regulating MPV17L expression (PubMed:22306510). By regulating MPV17L expression, contributes to the regulation of genes involved in H(2)O(2) metabolism and the mitochondrial apoptotic cascade (PubMed:22306510). {ECO:0000269|PubMed:22306510}.
Homo sapiens (Human)
O95202
LETM1_HUMAN
MASILLRSCRGRAPARLPPPPRYTVPRGSPGDPAHLSCASTLGLRNCLNVPFGCCTPIHPVYTSSRGDHLGCWALRPECLRIVSRAPWTSTSVGFVAVGPQCLPVRGWHSSRPVRDDSVVEKSLKSLKDKNKKLEEGGPVYSPPAEVVVKKSLGQRVLDELKHYYHGFRLLWIDTKIAARMLWRILNGHSLTRRERRQFLRICADLFRLVPFLVFVVVPFMEFLLPVAVKLFPNMLPSTFETQSLKEERLKKELRVKLELAKFLQDTIEEMALKNKAAKGSATKDFSVFFQKIRETGERPSNEEIMRFSKLFEDELTLDN...
null
null
calcium export from the mitochondrion [GO:0099093]; calcium ion transport [GO:0006816]; cristae formation [GO:0042407]; inner mitochondrial membrane organization [GO:0007007]; mitochondrial calcium ion homeostasis [GO:0051560]; mitochondrial calcium ion transmembrane transport [GO:0006851]; mitochondrial potassium ion ...
mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]
calcium ion binding [GO:0005509]; calcium:proton antiporter activity [GO:0015369]; ribosome binding [GO:0043022]
PF07766;
1.10.238.10;
LETM1 family
PTM: PINK1-mediated phosphorylation at Thr-192, positively regulates its mitochondrial calcium transport activity. {ECO:0000269|PubMed:29123128}.
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:14706454, ECO:0000269|PubMed:15138253, ECO:0000269|PubMed:18628306, ECO:0000269|PubMed:19797662, ECO:0000269|PubMed:32139798}; Single-pass membrane protein {ECO:0000255}.
CATALYTIC ACTIVITY: Reaction=Ca(2+)(in) + 2 H(+)(out) = Ca(2+)(out) + 2 H(+)(in); Xref=Rhea:RHEA:72199, ChEBI:CHEBI:15378, ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:19797662, ECO:0000269|PubMed:24344246, ECO:0000269|PubMed:29123128}; CATALYTIC ACTIVITY: Reaction=H(+)(out) + K(+)(in) = H(+)(in) + K(+)(out); Xref=R...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=27 uM for calcium transport {ECO:0000269|PubMed:24344246}; Vmax=21 pmol/sec/ug enzyme for calcium transport {ECO:0000269|PubMed:24344246};
null
null
null
FUNCTION: Plays an important role in maintenance of mitochondrial morphology and in mediating either calcium or potassium/proton antiport (PubMed:18628306, PubMed:19797662, PubMed:24344246, PubMed:24898248, PubMed:29123128, PubMed:32139798, PubMed:36055214, PubMed:36321428). Mediates proton-dependent calcium efflux fro...
Homo sapiens (Human)
O95206
PCDH8_HUMAN
MSPVRRWGSPCLFPLQLFSLCWVLSVAQSKTVRYSTFEEDAPGTVIGTLAEDLHMKVSGDTSFRLMKQFNSSLLRVREGDGQLTVGDAGLDRERLCGQAPQCVLAFDVVSFSQEQFRLVHVEVEVRDVNDHAPRFPRAQIPVEVSEGAAVGTRIPLEVPVDEDVGANGLQTVRLAEPHSPFRVELQTRADGAQCADLVLLQELDRESQAAYSLELVAQDGGRPPRSATAALSVRVLDANDHSPAFPQGAVAEVELAEDAPVGSLLLDLDAADPDEGPNGDVVFAFGARTPPEARRLFRLDPRSGRLTLAGPVDYERQDTY...
null
null
cell adhesion [GO:0007155]; cell-cell signaling [GO:0007267]; chemical synaptic transmission [GO:0007268]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; modulation of chemical synaptic transmission [GO:0050804]; morphogenesis of embryonic epithelium [GO:0016331]; regulation of synaptic m...
dendrite [GO:0030425]; glutamatergic synapse [GO:0098978]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; presynaptic membrane [GO:0042734]; Schaffer collateral - CA1 synapse [GO:0098685]
calcium ion binding [GO:0005509]
PF00028;PF08266;
2.60.40.60;
null
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Presynaptic cell membrane. Postsynaptic cell membrane. Note=Also expressed in neuronal cell bodies. Localized to excitatory, but not with inhibitory, synapses. {ECO:0000250}.
null
null
null
null
null
FUNCTION: Calcium-dependent cell-adhesion protein (By similarity). May play a role in activity-induced synaptic reorganization underlying long term memory (By similarity). Could be involved in CDH2 internalization through TAOK2/p38 MAPK pathway. In hippocampal neurons, may play a role in the down-regulation of dendriti...
Homo sapiens (Human)
O95208
EPN2_HUMAN
MTTSSIRRQMKNIVNNYSEAEIKVREATSNDPWGPSSSLMTEIADLTYNVVAFSEIMSMVWKRLNDHGKNWRHVYKALTLLDYLIKTGSERVAQQCRENIFAIQTLKDFQYIDRDGKDQGINVREKSKQLVALLKDEERLKAERAQALKTKERMAQVATGMGSNQITFGRGSSQPNLSTSHSEQEYGKAGGSPASYHGSPEASLCPQHRTGAPLGQSEELQPLSQRHPFLPHLGLASRPNGDWSQPCLTCDRAARATSPRVSSELEQARPQTSGEEELQLQLALAMSREVAEQEERLRRGDDLRLQMALEESRRDTVKIP...
null
null
endocytosis [GO:0006897]; negative regulation of sprouting angiogenesis [GO:1903671]; negative regulation of vascular endothelial growth factor receptor signaling pathway [GO:0030948]; positive regulation of Notch signaling pathway [GO:0045747]
clathrin vesicle coat [GO:0030125]; cytosol [GO:0005829]; endosome [GO:0005768]; intracellular membrane-bounded organelle [GO:0043231]; plasma membrane [GO:0005886]
cadherin binding [GO:0045296]; clathrin binding [GO:0030276]; phospholipid binding [GO:0005543]
PF01417;
1.25.40.90;
Epsin family
PTM: Ubiquitinated. {ECO:0000250}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10567358}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000269|PubMed:10567358}. Note=In punctate structures throughout the cell, associated with clathrin-coated vesicles, and particularly concentrated in the region of the Golgi complex.
null
null
null
null
null
FUNCTION: Plays a role in the formation of clathrin-coated invaginations and endocytosis. {ECO:0000269|PubMed:10567358}.
Homo sapiens (Human)
O95210
STBD1_HUMAN
MGAVWSALLVGGGLAGALFVWLLRGGPGDTGKDGDAEQEKDAPLGGAAIPGGHQSGSSGLSPGPSGQELVTKPEHLQESNGHLISKTKDLGKLQAASWRLQNPSREVCDNSREHVPSGQFPDTEAPATSETSNSRSYSEVSRNESLESPMGEWGFQKGQEISAKAATCFAEKLPSSNLLKNRAKEEMSLSDLNSQDRVDHEEWEMVPRHSSWGDVGVGGSLKAPVLNLNQGMDNGRSTLVEARGQQVHGKMERVAVMPAGSQQVSVRFQVHYVTSTDVQFIAVTGDHECLGRWNTYIPLHYNKDGFWSHSIFLPADTVVE...
null
null
glycogen catabolic process [GO:0005980]; glycophagy [GO:0061723]; intracellular transport [GO:0046907]; substrate localization to autophagosome [GO:0061753]
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; ficolin-1-rich granule membrane [GO:0101003]; membrane [GO:0016020]; perinuclear region of cytoplasm [GO:0048471]; phagophore assembly site membrane [GO:0034045]; plasma membrane [GO:0005886]; T-tubule [GO:0030315]; tertiary granule membra...
cargo receptor activity [GO:0038024]; enzyme binding [GO:0019899]; glycogen binding [GO:2001069]; polysaccharide binding [GO:0030247]; starch binding [GO:2001070]
PF00686;
2.60.40.10;
null
PTM: Ubiquitinated, which leads to proteasomal degradation. {ECO:0000269|PubMed:24837458}.
SUBCELLULAR LOCATION: Preautophagosomal structure membrane {ECO:0000269|PubMed:20810658, ECO:0000305|PubMed:21893048}; Single-pass type III membrane protein {ECO:0000305|PubMed:9794794}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:24837458}; Single-pass type III membrane protein {ECO:0000305|PubMed:9794794}. Cel...
null
null
null
null
null
FUNCTION: Acts as a cargo receptor for glycogen. Delivers its cargo to an autophagic pathway called glycophagy, resulting in the transport of glycogen to lysosomes. {ECO:0000269|PubMed:20810658, ECO:0000269|PubMed:21893048, ECO:0000269|PubMed:24837458}.
Homo sapiens (Human)
O95214
LERL1_HUMAN
MAGIKALISLSFGGAIGLMFLMLGCALPIYNKYWPLFVLFFYILSPIPYCIARRLVDDTDAMSNACKELAIFLTTGIVVSAFGLPIVFARAHLIEWGACALVLTGNTVIFATILGFFLVFGSNDDFSWQQW
null
null
late endosome to vacuole transport via multivesicular body sorting pathway [GO:0032511]; negative regulation of growth hormone receptor signaling pathway [GO:0060400]
endosome [GO:0005768]; membrane [GO:0016020]
identical protein binding [GO:0042802]
PF04133;
null
OB-RGRP/VPS55 family
null
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
null
null
null
null
null
FUNCTION: Negatively regulates growth hormone (GH) receptor cell surface expression in liver. May play a role in liver resistance to GH during periods of reduced nutrient availability. {ECO:0000269|PubMed:19907080}.
Homo sapiens (Human)
O95218
ZRAB2_HUMAN
MSTKNFRVSDGDWICPDKKCGNVNFARRTSCNRCGREKTTEAKMMKAGGTEIGKTLAEKSRGLFSANDWQCKTCSNVNWARRSECNMCNTPKYAKLEERTGYGGGFNERENVEYIEREESDGEYDEFGRKKKKYRGKAVGPASILKEVEDKESEGEEEDEDEDLSKYKLDEDEDEDDADLSKYNLDASEEEDSNKKKSNRRSRSKSRSSHSRSSSRSSSPSSSRSRSRSRSRSSSSSQSRSRSSSRERSRSRGSKSRSSSRSHRGSSSPRKRSYSSSSSSPERNRKRSRSRSSSSGDRKKRRTRSRSPERRHRSSSGSSH...
null
null
mRNA processing [GO:0006397]; RNA splicing [GO:0008380]
nucleoplasm [GO:0005654]
lipopolysaccharide binding [GO:0001530]; metal ion binding [GO:0046872]; RNA binding [GO:0003723]
PF00641;
4.10.1060.10;
ZRANB2 family
PTM: Isoform 2 is phosphorylated on Ser-310 upon DNA damage, probably by ATM or ATR.
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11448987}.
null
null
null
null
null
FUNCTION: Splice factor required for alternative splicing of TRA2B/SFRS10 transcripts. May interfere with constitutive 5'-splice site selection. {ECO:0000269|PubMed:11448987}.
Homo sapiens (Human)
O95219
SNX4_HUMAN
MEQAPPDPERQLQPAPLEPLGSPDAGLGAAVGKEAEGAGEESSGVDTMTHNNFWLKKIEISVSEAEKRTGRNAMNMQETYTAYLIETRSVEHTDGQSVLTDSLWRRYSEFELLRSYLLVYYPHIVVPPLPEKRAEFVWHKLSADNMDPDFVERRRIGLENFLLRIASHPILCRDKIFYLFLTQEGNWKETVNETGFQLKADSRLKALNATFRVKNPDKRFTDLKHYSDELQSVISHLLRVRARVADRLYGVYKVHGNYGRVFSEWSAIEKEMGDGLQSAGHHMDVYASSIDDILEDEEHYADQLKEYLFYAEALRAVCRK...
null
null
endocytic recycling [GO:0032456]; positive regulation of autophagosome assembly [GO:2000786]; positive regulation of histamine secretion by mast cell [GO:1903595]; protein transport [GO:0015031]
cytoplasm [GO:0005737]; cytoplasmic dynein complex [GO:0005868]; early endosome [GO:0005769]; early endosome membrane [GO:0031901]; membrane [GO:0016020]; plasma membrane [GO:0005886]; presynaptic endosome [GO:0098830]; protein-containing complex [GO:0032991]; SNARE complex [GO:0031201]
epidermal growth factor receptor binding [GO:0005154]; insulin receptor binding [GO:0005158]; leptin receptor binding [GO:1990460]; phosphatidylinositol binding [GO:0035091]; phosphatidylinositol-3-phosphate binding [GO:0032266]; transferrin receptor binding [GO:1990459]
PF00787;
1.20.1270.60;3.30.1520.10;
Sorting nexin family
null
SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000269|PubMed:17994011, ECO:0000269|PubMed:32513819, ECO:0000269|PubMed:33468622}; Peripheral membrane protein {ECO:0000269|PubMed:17994011}; Cytoplasmic side {ECO:0000269|PubMed:17994011}. Note=Also detected on a juxtanuclear endocytic recycling compartment (ERC). {E...
null
null
null
null
null
FUNCTION: Involved in the regulation of endocytosis and in several stages of intracellular trafficking (PubMed:12668730, PubMed:17994011, PubMed:32513819, PubMed:33468622). Plays a role in recycling endocytosed transferrin receptor and prevent its degradation (PubMed:17994011). Involved in autophagosome assembly by reg...
Homo sapiens (Human)
O95229
ZWINT_HUMAN
MEAAETEAEAAALEVLAEVAGILEPVGLQEEAELPAKILVEFVVDSQKKDKLLCSQLQVADFLQNILAQEDTAKGLDPLASEDTSRQKAIAAKEQWKELKATYREHVEAIKIGLTKALTQMEEAQRKRTQLREAFEQLQAKKQMAMEKRRAVQNQWQLQQEKHLQHLAEVSAEVRERKTGTQQELDRVFQKLGNLKQQAEQERDKLQRYQTFLQLLYTLQGKLLFPEAEAEAENLPDDKPQQPTRPQEQSTGDTMGRDPGVSFKAVGLQPAGDVNLP
null
null
cell division [GO:0051301]; establishment of localization in cell [GO:0051649]; homologous chromosome orientation in meiotic metaphase I [GO:0031619]; mitotic sister chromatid segregation [GO:0000070]; mitotic spindle assembly checkpoint signaling [GO:0007094]; regulation of meiosis I spindle assembly checkpoint [GO:19...
cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; kinetochore [GO:0000776]; Knl1/Spc105 complex [GO:0180019]; nuclear body [GO:0016604]; nucleoplasm [GO:0005654]
null
PF15556;
null
null
null
SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere, kinetochore. Note=Localizes to kinetochores from late prophase to anaphase.
null
null
null
null
null
FUNCTION: Part of the MIS12 complex, which is required for kinetochore formation and spindle checkpoint activity. Required to target ZW10 to the kinetochore at prometaphase. {ECO:0000269|PubMed:15094189, ECO:0000269|PubMed:15485811, ECO:0000269|PubMed:15824131, ECO:0000269|PubMed:16732327}.
Homo sapiens (Human)
O95231
VENTX_HUMAN
MRLSSSPPRGPQQLSSFGSVDWLSQSSCSGPTHTPRPADFSLGSLPGPGQTSGAREPPQAVSIKEAAGSSNLPAPERTMAGLSKEPNTLRAPRVRTAFTMEQVRTLEGVFQHHQYLSPLERKRLAREMQLSEVQIKTWFQNRRMKHKRQMQDPQLHSPFSGSLHAPPAFYSTSSGLANGLQLLCPWAPLSGPQALMLPPGSFWGLCQVAQEALASAGASCCGQPLASHPPTPGRPSLGPALSTGPRGLCAMPQTGDAF
null
null
positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]
chromatin [GO:0000785]; nucleoplasm [GO:0005654]
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]; sequence-specific dou...
PF00046;
1.10.10.60;
null
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
null
null
null
null
null
FUNCTION: May be involved in ventralization.
Homo sapiens (Human)
O95232
LC7L3_HUMAN
MISAAQLLDELMGRDRNLAPDEKRSNVRWDHESVCKYYLCGFCPAELFTNTRSDLGPCEKIHDENLRKQYEKSSRFMKVGYERDFLRYLQSLLAEVERRIRRGHARLALSQNQQSSGAAGPTGKNEEKIQVLTDKIDVLLQQIEELGSEGKVEEAQGMMKLVEQLKEERELLRSTTSTIESFAAQEKQMEVCEVCGAFLIVGDAQSRVDDHLMGKQHMGYAKIKATVEELKEKLRKRTEEPDRDERLKKEKQEREEREKEREREREERERKRRREEEEREKERARDRERRKRSRSRSRHSSRTSDRRCSRSRDHKRSRSR...
null
null
mRNA splice site recognition [GO:0006376]; RNA splicing [GO:0008380]
nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; U1 snRNP [GO:0005685]; U2-type prespliceosome [GO:0071004]
DNA binding [GO:0003677]; mRNA binding [GO:0003729]; RNA binding [GO:0003723]
PF03194;
null
Luc7 family
PTM: Phosphorylated in vitro by SRPK1, SRPK2 and CLK1. {ECO:0000269|PubMed:12565863}.
SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:10631324, ECO:0000269|PubMed:12565863}. Note=The subnuclear localization is affected by cisplatin.
null
null
null
null
null
FUNCTION: Binds cAMP regulatory element DNA sequence. May play a role in RNA splicing. {ECO:0000269|PubMed:16462885}.
Homo sapiens (Human)
O95235
KI20A_HUMAN
MSQGILSPPAGLLSDDDVVVSPMFESTAADLGSVVRKNLLSDCSVVSTSLEDKQQVPSEDSMEKVKVYLRVRPLLPSELERQEDQGCVRIENVETLVLQAPKDSFALKSNERGIGQATHRFTFSQIFGPEVGQASFFNLTVKEMVKDVLKGQNWLIYTYGVTNSGKTHTIQGTIKDGGILPRSLALIFNSLQGQLHPTPDLKPLLSNEVIWLDSKQIRQEEMKKLSLLNGGLQEEELSTSLKRSVYIESRIGTSTSFDSGIAGLSSISQCTSSSQLDETSHRWAQPDTAPLPVPANIRFSIWISFFEIYNELLYDLLEPP...
null
null
microtubule bundle formation [GO:0001578]; microtubule-based movement [GO:0007018]; midbody abscission [GO:0061952]; mitotic cytokinesis [GO:0000281]; protein transport [GO:0015031]; regulation of cytokinesis [GO:0032465]
Golgi apparatus [GO:0005794]; intercellular bridge [GO:0045171]; kinesin complex [GO:0005871]; microtubule [GO:0005874]; midbody [GO:0030496]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spindle [GO:0005819]
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; microtubule binding [GO:0008017]; microtubule motor activity [GO:0003777]; protein kinase binding [GO:0019901]
PF00225;
3.40.850.10;
TRAFAC class myosin-kinesin ATPase superfamily, Kinesin family
PTM: Phosphorylated by PLK1 at Ser-528 during mitosis, creating a docking site for PLK1 and recruiting PLK1 at central spindle. {ECO:0000269|PubMed:12939256}.
SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:12939256, ECO:0000269|PubMed:29357359}. Note=Localizes to the spindle midzone during anaphase and telophase. {ECO:0000269|PubMed:29357359}.
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FUNCTION: Mitotic kinesin required for chromosome passenger complex (CPC)-mediated cytokinesis. Following phosphorylation by PLK1, involved in recruitment of PLK1 to the central spindle. Interacts with guanosine triphosphate (GTP)-bound forms of RAB6A and RAB6B. May act as a motor required for the retrograde RAB6 regul...
Homo sapiens (Human)
O95236
APOL3_HUMAN
MGLGQGWGWEASCFACLIRSCCQVVTFTFPFGFQGISQSLENVSGYYADARLEVGSTQLRTAGSCSHSFKRSFLEKKRFTEEATKYFRERVSPVHLQILLTNNEAWKRFVTAAELPRDEADALYEALKKLRTYAAIEDEYVQQKDEQFREWFLKEFPQVKRKIQESIEKLRALANGIEEVHRGCTISNVVSSSTGAASGIMSLAGLVLAPFTAGTSLALTAAGVGLGAASAVTGITTSIVEHSYTSSAEAEASRLTATSIDRLKVFKEVMRDITPNLLSLLNNYYEATQTIGSEIRAIRQARARARLPVTTWRISAGSGG...
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inflammatory response [GO:0006954]; lipoprotein metabolic process [GO:0042157]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]
cytoplasm [GO:0005737]; extracellular region [GO:0005576]; membrane [GO:0016020]
lipid binding [GO:0008289]; lipid transporter activity [GO:0005319]
PF05461;
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Apolipoprotein L family
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SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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FUNCTION: May affect the movement of lipids in the cytoplasm or allow the binding of lipids to organelles.
Homo sapiens (Human)
O95237
LRAT_HUMAN
MKNPMLEVVSLLLEKLLLISNFTLFSSGAAGEDKGRNSFYETSSFHRGDVLEVPRTHLTHYGIYLGDNRVAHMMPDILLALTDDMGRTQKVVSNKRLILGVIVKVASIRVDTVEDFAYGANILVNHLDESLQKKALLNEEVARRAEKLLGFTPYSLLWNNCEHFVTYCRYGTPISPQSDKFCETVKIIIRDQRSVLASAVLGLASIVCTGLVSYTTLPAIFIPFFLWMAG
2.3.1.135
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cellular response to leukemia inhibitory factor [GO:1990830]; positive regulation of lipid transport [GO:0032370]; response to bacterium [GO:0009617]; response to retinoic acid [GO:0032526]; response to vitamin A [GO:0033189]; retinoid metabolic process [GO:0001523]; retinol metabolic process [GO:0042572]; visual perce...
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; multivesicular body [GO:0005771]; perinuclear region of cytoplasm [GO:0048471]; rough endoplasmic reticulum [GO:0005791]
acyltransferase activity [GO:0016746]; lecithin:11-cis retinol acyltransferase activity [GO:0102279]; O-palmitoyltransferase activity [GO:0016416]; phosphatidylcholine-retinol O-acyltransferase activity [GO:0047173]; retinoic acid binding [GO:0001972]; retinol binding [GO:0019841]
PF04970;
3.90.1720.10;
H-rev107 family
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SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Rough endoplasmic reticulum {ECO:0000250}. Endosome, multivesicular body {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Present in the rough endoplasmic reticulum and multivesicular body in ...
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + all-trans-retinol--[retinol-binding protein] = a 2-acyl-sn-glycero-3-phosphocholine + an all-trans-retinyl ester + apo--[retinol-binding protein]; Xref=Rhea:RHEA:17469, Rhea:RHEA-COMP:14426, Rhea:RHEA-COMP:14428, ChEBI:CHEBI:17336, ChEBI:CHEBI:5764...
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PATHWAY: Cofactor metabolism; retinol metabolism.
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FUNCTION: Transfers the acyl group from the sn-1 position of phosphatidylcholine to all-trans retinol, producing all-trans retinyl esters (PubMed:9920938). Retinyl esters are storage forms of vitamin A (Probable). LRAT plays a critical role in vision (Probable). It provides the all-trans retinyl ester substrates for th...
Homo sapiens (Human)