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
O43169
CYB5B_HUMAN
MSGSMATAEASGSDGKGQEVETSVTYYRLEEVAKRNSLKELWLVIHGRVYDVTRFLNEHPGGEEVLLEQAGVDASESFEDVGHSSDAREMLKQYYIGDIHPSDLKPESGSKDPSKNDTCKSCWAYWILPIIGAVLLGFLYRYYTSESKSS
null
null
nitric oxide biosynthetic process [GO:0006809]; response to oxidative stress [GO:0006979]; xenobiotic metabolic process [GO:0006805]
endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; mitochondrial outer membrane [GO:0005741]; nitric-oxide synthase complex [GO:1903958]
enzyme activator activity [GO:0008047]; heme binding [GO:0020037]; metal ion binding [GO:0046872]
PF00173;
3.10.120.10;
Cytochrome b5 family
null
SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250|UniProtKB:P04166}.
null
null
null
null
null
FUNCTION: Cytochrome b5 is a membrane-bound hemoprotein functioning as an electron carrier for several membrane-bound oxygenases. {ECO:0000250}.
Homo sapiens (Human)
O43172
PRP4_HUMAN
MASSRASSTQATKTKAPDDLVAPVVKKPHIYYGSLEEKERERLAKGESGILGKDGLKAGIEAGNINITSGEVFEIEEHISERQAEVLAEFERRKRARQINVSTDDSEVKACLRALGEPITLFGEGPAERRERLRNILSVVGTDALKKTKKDDEKSKKSKEEYQQTWYHEGPNSLKVARLWIANYSLPRAMKRLEEARLHKEIPETTRTSQMQELHKSLRSLNNFCSQIGDDRPISYCHFSPNSKMLATACWSGLCKLWSVPDCNLLHTLRGHNTNVGAIVFHPKSTVSLDPKDVNLASCAADGSVKLWSLDSDEPVADIE...
null
null
mRNA splicing, via spliceosome [GO:0000398]; RNA processing [GO:0006396]; RNA splicing [GO:0008380]; RNA splicing, via transesterification reactions [GO:0000375]
Cajal body [GO:0015030]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spliceosomal complex [GO:0005681]; spliceosomal snRNP complex [GO:0097525]; U2-type precatalytic spliceosome [GO:0071005]; U4/U6 snRNP [GO:0071001]; U4/U6 x U5 tri-snRNP complex [GO:0046540]
U4 snRNA binding [GO:0030621]; U6 snRNA binding [GO:0017070]
PF08799;PF00400;
4.10.280.110;2.130.10.10;
null
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25383878, ECO:0000269|PubMed:26912367, ECO:0000269|PubMed:28781166, ECO:0000269|PubMed:9257651, ECO:0000269|PubMed:9328476, ECO:0000269|PubMed:9404889}. Nucleus speckle {ECO:0000305}.
null
null
null
null
null
FUNCTION: Plays a role in pre-mRNA splicing as component of the U4/U6-U5 tri-snRNP complex that is involved in spliceosome assembly, and as component of the precatalytic spliceosome (spliceosome B complex). {ECO:0000269|PubMed:25383878, ECO:0000269|PubMed:28781166}.
Homo sapiens (Human)
O43173
SIA8C_HUMAN
MRNCKMARVASVLGLVMLSVALLILSLISYVSLKKENIFTTPKYASPGAPRMYMFHAGFRSQFALKFLDPSFVPITNSLTQELQEKPSKWKFNRTAFLHQRQEILQHVDVIKNFSLTKNSVRIGQLMHYDYSSHKYVFSISNNFRSLLPDVSPIMNKHYNICAVVGNSGILTGSQCGQEIDKSDFVFRCNFAPTEAFQRDVGRKTNLTTFNPSILEKYYNNLLTIQDRNNFFLSLKKLDGAILWIPAFFFHTSATVTRTLVDFFVEHRGQLKVQLAWPGNIMQHVNRYWKNKHLSPKRLSTGILMYTLASAICEEIHLYG...
2.4.3.-; 2.4.3.8
null
ganglioside biosynthetic process [GO:0001574]; glycoprotein metabolic process [GO:0009100]; glycosphingolipid biosynthetic process [GO:0006688]; N-glycan processing [GO:0006491]; oligosaccharide metabolic process [GO:0009311]; protein glycosylation [GO:0006486]; sialylation [GO:0097503]
Golgi membrane [GO:0000139]
alpha-N-acetylneuraminate alpha-2,8-sialyltransferase activity [GO:0003828]; identical protein binding [GO:0042802]; sialic acid binding [GO:0033691]
PF00777;
3.90.1480.20;
Glycosyltransferase 29 family
PTM: Autopolysialylated. {ECO:0000269|PubMed:10766765}.
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305|PubMed:10766765}; Single-pass type II membrane protein {ECO:0000305}.
CATALYTIC ACTIVITY: Reaction=[N-acetyl-alpha-D-neuraminosyl-(2->8)](n) + CMP-N-acetyl-beta-neuraminate = [N-acetyl-alpha-D-neuraminosyl-(2->8)](n+1) + CMP + H(+); Xref=Rhea:RHEA:77367, Rhea:RHEA-COMP:14315, Rhea:RHEA-COMP:18878, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:139252; Evidence={ECO:...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=30 mM for N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl-(1->4)-beta-D-glucose (with a constant CMP-Neu5Ac concentration of 1 mM) {ECO:0000269|PubMed:26192331}; KM=2.6 mM for 3'-sialyl-N-acetyllactosamine-6-sulfate (with a constant CMP-Neu5Ac concentration of 1...
PATHWAY: Protein modification; protein glycosylation. {ECO:0000269|PubMed:9826427, ECO:0000305|PubMed:10766765, ECO:0000305|PubMed:26192331}.
null
null
FUNCTION: Catalyzes the transfer of sialic acid from a CMP-linked sialic acid donor onto a terminal alpha-2,3-, alpha-2,6-, or alpha-2,8-linked sialic acid of an acceptor, such as N-linked oligosaccharides of glycoproteins and glycolipids through alpha-2,8-linkages (PubMed:10766765, PubMed:26192331, PubMed:9826427). Fo...
Homo sapiens (Human)
O43174
CP26A_HUMAN
MGLPALLASALCTFVLPLLLFLAAIKLWDLYCVSGRDRSCALPLPPGTMGFPFFGETLQMVLQRRKFLQMKRRKYGFIYKTHLFGRPTVRVMGADNVRRILLGEHRLVSVHWPASVRTILGSGCLSNLHDSSHKQRKKVIMRAFSREALECYVPVITEEVGSSLEQWLSCGERGLLVYPEVKRLMFRIAMRILLGCEPQLAGDGDSEQQLVEAFEEMTRNLFSLPIDVPFSGLYRGMKARNLIHARIEQNIRAKICGLRASEAGQGCKDALQLLIEHSWERGERLDMQALKQSSTELLFGGHETTASAATSLITYLGLYP...
1.14.13.-
COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
kidney development [GO:0001822]; negative regulation of retinoic acid receptor signaling pathway [GO:0048387]; response to retinoic acid [GO:0032526]; response to vitamin A [GO:0033189]; retinoic acid catabolic process [GO:0034653]; retinoic acid metabolic process [GO:0042573]; sterol metabolic process [GO:0016125]; vi...
endoplasmic reticulum membrane [GO:0005789]
all-trans retinoic acid 18-hydroxylase activity [GO:0062183]; all-trans retinoic acid 4-hydrolase activity [GO:0062182]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, N...
PF00067;
1.10.630.10;
Cytochrome P450 family
null
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305|PubMed:9716180}; Peripheral membrane protein. Microsome membrane {ECO:0000269|PubMed:9716180}; Peripheral membrane protein.
CATALYTIC ACTIVITY: Reaction=all-trans-retinoate + O2 + reduced [NADPH--hemoprotein reductase] = all-trans-(4S)-hydroxyretinoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:51492, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=50.1 nM for all-trans-retinoate (4-hydroxylation) {ECO:0000269|PubMed:22020119}; KM=48.9 nM for all-trans-retinoate (18-hydroxylation) {ECO:0000269|PubMed:22020119}; KM=0.24 uM for tazarotenic acid (tazarotenic acid sulfoxide formation) {ECO:0000269|PubMed:26937021...
null
null
null
FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of retinoates (RAs), the active metabolites of vitamin A, and critical signaling molecules in animals (PubMed:22020119, PubMed:9228017, PubMed:9716180). RAs exist as at least four different isomers: all-trans-RA (atRA), 9-cis-RA, 13-cis-RA, and 9,13-d...
Homo sapiens (Human)
O43175
SERA_HUMAN
MAFANLRKVLISDSLDPCCRKILQDGGLQVVEKQNLSKEELIAELQDCEGLIVRSATKVTADVINAAEKLQVVGRAGTGVDNVDLEAATRKGILVMNTPNGNSLSAAELTCGMIMCLARQIPQATASMKDGKWERKKFMGTELNGKTLGILGLGRIGREVATRMQSFGMKTIGYDPIISPEVSASFGVQQLPLEEIWPLCDFITVHTPLLPSTTGLLNDNTFAQCKKGVRVVNCARGGIVDEGALLRALQSGQCAGAALDVFTEEPPRDRALVDHENVISCPHLGASTKEAQSRCGEEIAVQFVDMVKGKSLTGVVNAQA...
1.1.1.37; 1.1.1.399; 1.1.1.95
null
brain development [GO:0007420]; G1 to G0 transition [GO:0070314]; gamma-aminobutyric acid metabolic process [GO:0009448]; glial cell development [GO:0021782]; glutamine metabolic process [GO:0006541]; glycine metabolic process [GO:0006544]; L-serine biosynthetic process [GO:0006564]; neural tube development [GO:0021915...
cytosol [GO:0005829]; extracellular exosome [GO:0070062]
electron transfer activity [GO:0009055]; L-malate dehydrogenase activity [GO:0030060]; NAD binding [GO:0051287]; phosphoglycerate dehydrogenase activity [GO:0004617]
PF00389;PF02826;PF19304;
3.40.50.720;
D-isomer specific 2-hydroxyacid dehydrogenase family
null
null
CATALYTIC ACTIVITY: Reaction=(2R)-3-phosphoglycerate + NAD(+) = 3-phosphooxypyruvate + H(+) + NADH; Xref=Rhea:RHEA:12641, ChEBI:CHEBI:15378, ChEBI:CHEBI:18110, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58272; EC=1.1.1.95; Evidence={ECO:0000269|PubMed:11751922}; CATALYTIC ACTIVITY: Reaction=(R)-2-hydroxyglutarat...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=21.6 uM for 3-phosphonooxypyruvate {ECO:0000269|PubMed:19235232}; KM=0.26 mM for 3-phosphoglycerate {ECO:0000269|PubMed:25406093}; KM=6.5 mM for oxaloacetate {ECO:0000269|PubMed:25406093}; KM=10.1 mM for 2-oxoglutarate {ECO:0000269|PubMed:25406093}; KM=22 uM for NA...
PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 1/3.
null
null
FUNCTION: Catalyzes the reversible oxidation of 3-phospho-D-glycerate to 3-phosphonooxypyruvate, the first step of the phosphorylated L-serine biosynthesis pathway. Also catalyzes the reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate and the reversible oxidation of (S)-malate to oxaloacetate. {ECO:0000269|Pu...
Homo sapiens (Human)
O43181
NDUS4_HUMAN
MAAVSMSVVLRQTLWRRRAVAVAALSVSRVPTRSLRTSTWRLAQDQTQDTQLITVDEKLDITTLTGVPEEHIKTRKVRIFVPARNNMQSGVNNTKKWKMEFDTRERWENPLMGWASTADPLSNMVLTFSTKEDAVSFAEKNGWSYDIEERKVPKPKSKSYGANFSWNKRTRVSTK
null
null
aerobic respiration [GO:0009060]; brain development [GO:0007420]; cellular respiration [GO:0045333]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; mitochondrial respiratory chain complex I assembly [GO:0032981]; positive regulation of fibroblast proliferation [GO:0048146]; proton motive force-drive...
mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex I [GO:0005747]; mitochondrion [GO:0005739]
NADH dehydrogenase (ubiquinone) activity [GO:0008137]
PF04800;
3.30.160.190;
Complex I NDUFS4 subunit family
null
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:11181577, ECO:0000269|PubMed:12611891, ECO:0000269|PubMed:31206022}; Peripheral membrane protein {ECO:0000269|PubMed:12611891}; Matrix side {ECO:0000269|PubMed:12611891}. Note=The interaction with BCAP31 mediates mitochondria localization. {ECO:0000...
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)
O43182
RHG06_HUMAN
MSAQSLLHSVFSCSSPASSSAASAKGFSKRKLRQTRSLDPALIGGCGSDEAGAEGSARGATAGRLYSPSLPAESLGPRLASSSRGPPPRATRLPPPGPLCSSFSTPSTPQEKSPSGSFHFDYEVPLGRGGLKKSMAWDLPSVLAGPASSRSASSILCSSGGGPNGIFASPRRWLQQRKFQSPPDSRGHPYVVWKSEGDFTWNSMSGRSVRLRSVPIQSLSELERARLQEVAFYQLQQDCDLSCQITIPKDGQKRKKSLRKKLDSLGKEKNKDKEFIPQAFGMPLSQVIANDRAYKLKQDLQRDEQKDASDFVASLLPFGN...
null
null
actin filament polymerization [GO:0030041]; activation of phospholipase C activity [GO:0007202]; focal adhesion assembly [GO:0048041]; negative regulation of focal adhesion assembly [GO:0051895]; negative regulation of stress fiber assembly [GO:0051497]; positive regulation of phospholipase activity [GO:0010518]; regul...
actin cytoskeleton [GO:0015629]; actin filament [GO:0005884]; cytoplasm [GO:0005737]; cytosol [GO:0005829]
GTPase activator activity [GO:0005096]; phospholipase activator activity [GO:0016004]; phospholipase binding [GO:0043274]; SH3 domain binding [GO:0017124]
PF00620;
1.10.555.10;
null
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10699171}.
null
null
null
null
null
FUNCTION: GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. Could regulate the interactions of signaling molecules with the actin cytoskeleton. Promotes continuous elongation of cytoplasmic processes during cell motility and simultaneous retraction of the cell body changing th...
Homo sapiens (Human)
O43184
ADA12_HUMAN
MAARPLPVSPARALLLALAGALLAPCEARGVSLWNQGRADEVVSASVGSGDLWIPVKSFDSKNHPEVLNIRLQRESKELIINLERNEGLIASSFTETHYLQDGTDVSLARNYTVILGHCYYHGHVRGYSDSAVSLSTCSGLRGLIVFENESYVLEPMKSATNRYKLFPAKKLKSVRGSCGSHHNTPNLAAKNVFPPPSQTWARRHKRETLKATKYVELVIVADNREFQRQGKDLEKVKQRLIEIANHVDKFYRPLNIRIVLVGVEVWNDMDKCSVSQDPFTSLHEFLDWRKMKLLPRKSHDNAQLVSGVYFQGTTIGMAP...
3.4.24.-
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 zinc ion per subunit.;
cell adhesion [GO:0007155]; myoblast fusion [GO:0007520]; positive regulation of angiogenesis [GO:0045766]; proteolysis [GO:0006508]
extracellular region [GO:0005576]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]
metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; metallopeptidase activity [GO:0008237]; SH3 domain binding [GO:0017124]
PF08516;PF00200;PF01562;PF01421;
3.40.390.10;4.10.70.10;
null
PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}.
SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted.; SUBCELLULAR LOCATION: [Isoform 3]: Secreted {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 4]: Secreted {ECO:0000305}.
null
null
null
null
null
FUNCTION: Involved in skeletal muscle regeneration, specifically at the onset of cell fusion. Also involved in macrophage-derived giant cells (MGC) and osteoclast formation from mononuclear precursors (By similarity). {ECO:0000250}.
Homo sapiens (Human)
O43186
CRX_HUMAN
MMAYMNPGPHYSVNALALSGPSVDLMHQAVPYPSAPRKQRRERTTFTRSQLEELEALFAKTQYPDVYAREEVALKINLPESRVQVWFKNRRAKCRQQRQQQKQQQQPPGGQAKARPAKRKAGTSPRPSTDVCPDPLGISDSYSPPLPGPSGSPTTAVATVSIWSPASESPLPEAQRAGLVASGPSLTSAPYAMTYAPASAFCSSPSAYGSPSSYFSGLDPYLSPMVPQLGGPALSPLSGPSVGPSLAQSPTSLSGQSYGAYSPVDSLEFKDPTGTWKFTYNPMDPLDYKDQSAWKFQIL
null
null
animal organ morphogenesis [GO:0009887]; cell differentiation [GO:0030154]; nervous system development [GO:0007399]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of DNA-templated transcription [GO:0006355]; regulation of transcription by RNA polymerase II [GO:0006357]; response to ...
chromatin [GO:0000785]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575]
DNA-binding transcription activator activity [GO:0001216]; 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]; leucine zipper domain binding [GO:...
PF00046;PF03529;
1.10.10.60;
Paired homeobox family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
null
null
null
null
null
FUNCTION: Transcription factor that binds and transactivates the sequence 5'-TAATC[CA]-3' which is found upstream of several photoreceptor-specific genes, including the opsin genes. Acts synergistically with other transcription factors, such as NRL, RORB and RAX, to regulate photoreceptor cell-specific gene transcripti...
Homo sapiens (Human)
O43187
IRAK2_HUMAN
MACYIYQLPSWVLDDLCRNMDALSEWDWMEFASYVITDLTQLRKIKSMERVQGVSITRELLWWWGMRQATVQQLVDLLCRLELYRAAQIILNWKPAPEIRCPIPAFPDSVKPEKPLAASVRKAEDEQEEGQPVRMATFPGPGSSPARAHQPAFLQPPEEDAPHSLRSDLPTSSDSKDFSTSIPKQEKLLSLAGDSLFWSEADVVQATDDFNQNRKISQGTFADVYRGHRHGKPFVFKKLRETACSSPGSIERFFQAELQICLRCCHPNVLPVLGFCAARQFHSFIYPYMANGSLQDRLQGQGGSDPLPWPQRVSICSGLL...
null
null
canonical NF-kappaB signal transduction [GO:0007249]; cellular response to lipopolysaccharide [GO:0071222]; inflammatory response [GO:0006954]; interleukin-1-mediated signaling pathway [GO:0070498]; intracellular signal transduction [GO:0035556]; lipopolysaccharide-mediated signaling pathway [GO:0031663]; MyD88-depende...
cytoplasm [GO:0005737]; cytosol [GO:0005829]; endosome membrane [GO:0010008]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
ATP binding [GO:0005524]; molecular adaptor activity [GO:0060090]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; protein kinase activity [GO:0004672]; signaling adaptor activity [GO:0035591]
PF00531;PF00069;
1.10.533.10;1.10.510.10;
Protein kinase superfamily, TKL Ser/Thr protein kinase family, Pelle subfamily
null
null
null
null
null
null
null
FUNCTION: Binds to the IL-1 type I receptor following IL-1 engagement, triggering intracellular signaling cascades leading to transcriptional up-regulation and mRNA stabilization. {ECO:0000269|PubMed:10383454, ECO:0000269|PubMed:9374458}.
Homo sapiens (Human)
O43189
PHF1_HUMAN
MAQPPRLSRSGASSLWDPASPAPTSGPRPRLWEGQDVLARWTDGLLYLGTIKKVDSAREVCLVQFEDDSQFLVLWKDISPAALPGEELLCCVCRSETVVPGNRLVSCEKCRHAYHQDCHVPRAPAPGEGEGTSWVCRQCVFAIATKRGGALKKGPYARAMLGMKLSLPYGLKGLDWDAGHLSNRQQSYCYCGGPGEWNLKMLQCRSCLQWFHEACTQCLSKPLLYGDRFYEFECCVCRGGPEKVRRLQLRWVDVAHLVLYHLSVCCKKKYFDFDREILPFTSENWDSLLLGELSDTPKGERSSRLLSALNSHKDRFISGR...
null
null
chromatin organization [GO:0006325]; DNA repair-dependent chromatin remodeling [GO:0140861]; regulation of DNA-templated transcription [GO:0006355]
centrosome [GO:0005813]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; site of double-strand break [GO:0035861]
chromatin binding [GO:0003682]; DNA binding [GO:0003677]; histone methyltransferase binding [GO:1990226]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; methylated histone binding [GO:0035064]; transcription corepressor binding [GO:0001222]
PF14061;PF00628;PF18104;
2.30.30.140;3.90.980.20;3.30.40.10;
Polycomblike family
null
SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=Localizes specifically to the promoters of numerous target genes. Localizes to double-strand breaks (DSBs) sites following DNA damage. Co-localizes with NEK6 in the centrosome.
null
null
null
null
null
FUNCTION: Polycomb group (PcG) that specifically binds histone H3 trimethylated at 'Lys-36' (H3K36me3) and recruits the PRC2 complex. Involved in DNA damage response and is recruited at double-strand breaks (DSBs). Acts by binding to H3K36me3, a mark for transcriptional activation, and recruiting the PRC2 complex: it i...
Homo sapiens (Human)
O43193
MTLR_HUMAN
MGSPWNGSDGPEGAREPPWPALPPCDERRCSPFPLGALVPVTAVCLCLFVVGVSGNVVTVMLIGRYRDMRTTTNLYLGSMAVSDLLILLGLPFDLYRLWRSRPWVFGPLLCRLSLYVGEGCTYATLLHMTALSVERYLAICRPLRARVLVTRRRVRALIAVLWAVALLSAGPFLFLVGVEQDPGISVVPGLNGTARIASSPLASSPPLWLSRAPPPSPPSGPETAEAAALFSRECRPSPAQLGALRVMLWVTTAYFFLPFLCLSILYGLIGRELWSSRRPLRGPAASGRERGHRQTVRVLLVVVLAFIICWLPFHVGRII...
null
null
G protein-coupled receptor signaling pathway [GO:0007186]
cytosol [GO:0005829]; plasma membrane [GO:0005886]
G protein-coupled peptide receptor activity [GO:0008528]; hormone binding [GO:0042562]
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 motilin. {ECO:0000269|PubMed:11322507}.
Homo sapiens (Human)
O43194
GPR39_HUMAN
MASPSLPGSDCSQIIDHSHVPEFEVATWIKITLILVYLIIFVMGLLGNSATIRVTQVLQKKGYLQKEVTDHMVSLACSDILVFLIGMPMEFYSIIWNPLTTSSYTLSCKLHTFLFEACSYATLLHVLTLSFERYIAICHPFRYKAVSGPCQVKLLIGFVWVTSALVALPLLFAMGTEYPLVNVPSHRGLTCNRSSTRHHEQPETSNMSICTNLSSRWTVFQSSIFGAFVVYLVVLLSVAFMCWNMMQVLMKSQKGSLAGGTRPPQLRKSESEESRTARRQTIIFLRLIVVTLAVCWMPNQIRRIMAAAKPKHDWTRSYFR...
null
null
G protein-coupled receptor signaling pathway [GO:0007186]
plasma membrane [GO:0005886]
G protein-coupled receptor activity [GO:0004930]; metal ion binding [GO:0046872]
PF00001;
1.20.1070.10;
G-protein coupled receptor 1 family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26365466}; Multi-pass membrane protein.
null
null
null
null
null
FUNCTION: Zinc-sensing receptor that can sense changes in extracellular Zn(2+), mediate Zn(2+) signal transmission, and participates in the regulation of numerous physiological processes including glucose homeostasis regulation, gastrointestinal mobility, hormone secretion and cell death (PubMed:18180304). Activation b...
Homo sapiens (Human)
O43196
MSH5_HUMAN
MASLGANPRRTPQGPRPGAASSGFPSPAPVPGPREAEEEEVEEEEELAEIHLCVLWNSGYLGIAYYDTSDSTIHFMPDAPDHESLKLLQRVLDEINPQSVVTSAKQDENMTRFLGKLASQEHREPKRPEIIFLPSVDFGLEISKQRLLSGNYSFIPDAMTATEKILFLSSIIPFDCLLTVRALGGLLKFLGRRRIGVELEDYNVSVPILGFKKFMLTHLVNIDQDTYSVLQIFKSESHPSVYKVASGLKEGLSLFGILNRCHCKWGEKLLRLWFTRPTHDLGELSSRLDVIQFFLLPQNLDMAQMLHRLLGHIKNVPLIL...
null
null
chiasma assembly [GO:0051026]; mismatch repair [GO:0006298]
nucleus [GO:0005634]
ATP binding [GO:0005524]; ATP-dependent DNA damage sensor activity [GO:0140664]; double-stranded DNA binding [GO:0003690]; mismatched DNA binding [GO:0030983]
PF05192;PF05190;PF00488;
1.10.1420.10;3.40.50.300;
DNA mismatch repair MutS family
null
null
null
null
null
null
null
FUNCTION: Involved in DNA mismatch repair and meiotic recombination processes. Facilitates crossovers between homologs during meiosis (By similarity). {ECO:0000250}.
Homo sapiens (Human)
O43236
SEPT4_HUMAN
MDRSLGWQGNSVPEDRTEAGIKRFLEDTTDDGELSKFVKDFSGNASCHPPEAKTWASRPQVPEPRPQAPDLYDDDLEFRPPSRPQSSDNQQYFCAPAPLSPSARPRSPWGKLDPYDSSEDDKEYVGFATLPNQVHRKSVKKGFDFTLMVAGESGLGKSTLVNSLFLTDLYRDRKLLGAEERIMQTVEITKHAVDIEEKGVRLRLTIVDTPGFGDAVNNTECWKPVAEYIDQQFEQYFRDESGLNRKNIQDNRVHCCLYFISPFGHGLRPLDVEFMKALHQRVNIVPILAKADTLTPPEVDHKKRKIREEIEHFGIKIYQF...
null
null
apoptotic process [GO:0006915]; cytoskeleton-dependent cytokinesis [GO:0061640]; flagellated sperm motility [GO:0030317]; hematopoietic stem cell homeostasis [GO:0061484]; neuron migration [GO:0001764]; positive regulation of apoptotic process [GO:0043065]; positive regulation of intrinsic apoptotic signaling pathway [...
axon [GO:0030424]; cell division site [GO:0032153]; cytosol [GO:0005829]; dendrite [GO:0030425]; microtubule cytoskeleton [GO:0015630]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perikaryon [GO:0043204]; septin complex [GO:0031105]; septin ring...
GTP binding [GO:0005525]; GTPase activity [GO:0003924]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; molecular adaptor activity [GO:0060090]; structural molecule activity [GO:0005198]
PF00735;
3.40.50.300;
TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily, Septin GTPase family
PTM: Phosphorylated by DYRK1A. {ECO:0000250|UniProtKB:P28661}.; PTM: Ubiquitinated by AREL1. {ECO:0000269|PubMed:23479728}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P28661}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:25588830}. Cytoplasmic vesicle, secretory vesicle {ECO:0000269|PubMed:15116257}. Cell projection, axon {ECO:0000250|UniProtKB:P28661}. Cell projection, dendrite {ECO:0000250|UniProtKB:P28661}. Perikary...
null
null
null
null
null
FUNCTION: Filament-forming cytoskeletal GTPase (Probable). Pro-apoptotic protein involved in LGR5-positive intestinal stem cell and Paneth cell expansion in the intestines, via its interaction with XIAP (By similarity). May also play a role in the regulation of cell fate in the intestine (By similarity). Positive regul...
Homo sapiens (Human)
O43237
DC1L2_HUMAN
MAPVGVEKKLLLGPNGPAVAAAGDLTSEEEEGQSLWSSILSEVSTRARSKLPSGKNILVFGEDGSGKTTLMTKLQGAEHGKKGRGLEYLYLSVHDEDRDDHTRCNVWILDGDLYHKGLLKFAVSAESLPETLVIFVADMSRPWTVMESLQKWASVLREHIDKMKIPPEKMRELERKFVKDFQDYMEPEEGCQGSPQRRGPLTSGSDEENVALPLGDNVLTHNLGIPVLVVCTKCDAVSVLEKEHDYRDEHLDFIQSHLRRFCLQYGAALIYTSVKEEKNLDLLYKYIVHKTYGFHFTTPALVVEKDAVFIPAGWDNEKKI...
null
null
cellular response to nerve growth factor stimulus [GO:1990090]; centrosome localization [GO:0051642]; microtubule cytoskeleton organization [GO:0000226]; microtubule-based movement [GO:0007018]
centrosome [GO:0005813]; cytoplasmic dynein complex [GO:0005868]; cytosol [GO:0005829]; dynein complex [GO:0030286]; kinetochore [GO:0000776]; late endosome [GO:0005770]; membrane [GO:0016020]; microtubule [GO:0005874]
ATP binding [GO:0005524]; dynein heavy chain binding [GO:0045504]; identical protein binding [GO:0042802]
PF05783;
3.40.50.300;
Dynein light intermediate chain family
null
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305|PubMed:36071160}.
null
null
null
null
null
FUNCTION: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organe...
Homo sapiens (Human)
O43240
KLK10_HUMAN
MRAPHLHLSAASGARALAKLLPLLMAQLWAAEAALLPQNDTRLDPEAYGSPCARGSQPWQVSLFNGLSFHCAGVLVDQSWVLTAAHCGNKPLWARVGDDHLLLLQGEQLRRTTRSVVHPKYHQGSGPILPRRTDEHDLMLLKLARPVVLGPRVRALQLPYRCAQPGDQCQVAGWGTTAARRVKYNKGLTCSSITILSPKECEVFYPGVVTNNMICAGLDRGQDPCQSDSGGPLVCDETLQGILSWGVYPCGSAQHPAVYTQICKYMSWINKVIRSN
3.4.21.-
null
cell cycle [GO:0007049]; proteolysis [GO:0006508]
extracellular region [GO:0005576]; secretory granule [GO:0030141]
serine-type endopeptidase activity [GO:0004252]; serine-type peptidase activity [GO:0008236]
PF00089;
2.40.10.10;
Peptidase S1 family, Kallikrein subfamily
null
SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
null
null
null
null
null
FUNCTION: Has a tumor-suppressor role for NES1 in breast and prostate cancer.
Homo sapiens (Human)
O43242
PSMD3_HUMAN
MKQEGSARRRGADKAKPPPGGGEQEPPPPPAPQDVEMKEEAATGGGSTGEADGKTAAAAAEHSQRELDTVTLEDIKEHVKQLEKAVSGKEPRFVLRALRMLPSTSRRLNHYVLYKAVQGFFTSNNATRDFLLPFLEEPMDTEADLQFRPRTGKAASTPLLPEVEAYLQLLVVIFMMNSKRYKEAQKISDDLMQKISTQNRRALDLVAAKCYYYHARVYEFLDKLDVVRSFLHARLRTATLRHDADGQATLLNLLLRNYLHYSLYDQAEKLVSKSVFPEQANNNEWARYLYYTGRIKAIQLEYSEARRTMTNALRKAPQHT...
null
null
proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; regulation of protein catabolic process [GO:0042176]; ubiquitin-dependent protein catabolic process [GO:0006511]
cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; ficolin-1-rich granule lumen [GO:1904813]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; proteasome accessory complex [GO:0022624]; proteasome complex [GO:0000502]; proteasome regulatory particle, lid s...
enzyme regulator activity [GO:0030234]
PF01399;PF08375;
1.25.40.570;1.25.40.10;
Proteasome subunit S3 family
null
null
null
null
null
null
null
FUNCTION: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose ...
Homo sapiens (Human)
O43248
HXC11_HUMAN
MFNSVNLGNFCSPSRKERGADFGERGSCASNLYLPSCTYYMPEFSTVSSFLPQAPSRQISYPYSAQVPPVREVSYGLEPSGKWHHRNSYSSCYAAADELMHRECLPPSTVTEILMKNEGSYGGHHHPSAPHATPAGFYSSVNKNSVLPQAFDRFFDNAYCGGGDPPAEPPCSGKGEAKGEPEAPPASGLASRAEAGAEAEAEEENTNPSSSGSAHSVAKEPAKGAAPNAPRTRKKRCPYSKFQIRELEREFFFNVYINKEKRLQLSRMLNLTDRQVKIWFQNRRMKEKKLSRDRLQYFSGNPLL
null
null
anterior/posterior pattern specification [GO:0009952]; embryonic digit morphogenesis [GO:0042733]; embryonic skeletal joint morphogenesis [GO:0060272]; endoderm development [GO:0007492]; metanephros development [GO:0001656]; organ induction [GO:0001759]; positive regulation of transcription by RNA polymerase II [GO:004...
chromatin [GO:0000785]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific double-stranded DNA binding [GO:1990837]
PF12045;PF00046;
1.10.10.60;
Abd-B homeobox family
null
SUBCELLULAR LOCATION: Nucleus.
null
null
null
null
null
FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Binds to a promoter element of the lactase-phlorizin hydrolase gene.
Homo sapiens (Human)
O43251
RFOX2_HUMAN
MQNEPLTPGYHGFPARDSQGNQEPTTTPDAMVQPFTTIPFPPPPQNGIPTEYGVPHTQDYAGQTGEHNLTLYGSTQAHGEQSSNSPSTQNGSLTTEGGAQTDGQQSQTQSSENSESKSTPKRLHVSNIPFRFRDPDLRQMFGQFGKILDVEIIFNERGSKGFGFVTFENSADADRAREKLHGTVVEGRKIEVNNATARVMTNKKMVTPYANGWKLSPVVGAVYGPELYAASSFQADVSLGNDAAVPLSGRGGINTYIPLISLPLVPGFPYPTAATTAAAFRGAHLRGRGRTVYGAVRAVPPTAIPAYPGVVYQDGFYGAD...
null
null
intracellular estrogen receptor signaling pathway [GO:0030520]; mRNA processing [GO:0006397]; negative regulation of DNA-templated transcription [GO:0045892]; nervous system development [GO:0007399]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; regulation of cell population proliferation [GO:0...
cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
DNA-binding transcription factor binding [GO:0140297]; mRNA binding [GO:0003729]; RNA binding [GO:0003723]; transcription corepressor activity [GO:0003714]
PF12414;PF00076;
3.30.70.330;
null
null
SUBCELLULAR LOCATION: Nucleus. Cytoplasm {ECO:0000250}.
null
null
null
null
null
FUNCTION: RNA-binding protein that regulates alternative splicing events by binding to 5'-UGCAUGU-3' elements. Prevents binding of U2AF2 to the 3'-splice site. Regulates alternative splicing of tissue-specific exons and of differentially spliced exons during erythropoiesis (By similarity). RNA-binding protein that seem...
Homo sapiens (Human)
O43252
PAPS1_HUMAN
MEIPGSLCKKVKLSNNAQNWGMQRATNVTYQAHHVSRNKRGQVVGTRGGFRGCTVWLTGLSGAGKTTVSMALEEYLVCHGIPCYTLDGDNIRQGLNKNLGFSPEDREENVRRIAEVAKLFADAGLVCITSFISPYTQDRNNARQIHEGASLPFFEVFVDAPLHVCEQRDVKGLYKKARAGEIKGFTGIDSEYEKPEAPELVLKTDSCDVNDCVQQVVELLQERDIVPVDASYEVKELYVPENKLHLAKTDAETLPALKINKVDMQWVQVLAEGWATPLNGFMREREYLQCLHFDCLLDGGVINLSVPIVLTATHEDKERL...
2.7.1.25; 2.7.7.4
null
3'-phosphoadenosine 5'-phosphosulfate biosynthetic process [GO:0050428]; phosphorylation [GO:0016310]; skeletal system development [GO:0001501]; sulfate assimilation [GO:0000103]
cytosol [GO:0005829]
adenylylsulfate kinase activity [GO:0004020]; ATP binding [GO:0005524]; nucleotidyltransferase activity [GO:0016779]; protein homodimerization activity [GO:0042803]; sulfate adenylyltransferase (ATP) activity [GO:0004781]
PF01583;PF01747;PF14306;
3.40.50.620;3.40.50.300;3.10.400.10;
APS kinase family; Sulfate adenylyltransferase family
null
null
CATALYTIC ACTIVITY: Reaction=ATP + H(+) + sulfate = adenosine 5'-phosphosulfate + diphosphate; Xref=Rhea:RHEA:18133, ChEBI:CHEBI:15378, ChEBI:CHEBI:16189, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58243; EC=2.7.7.4; Evidence={ECO:0000269|PubMed:14747722, ECO:0000269|PubMed:9576487, ECO:0000269|PubMed:9648242, E...
null
PATHWAY: Sulfur metabolism; sulfate assimilation. {ECO:0000269|PubMed:14747722, ECO:0000269|PubMed:9576487, ECO:0000269|PubMed:9648242, ECO:0000269|PubMed:9668121}.
null
null
FUNCTION: Bifunctional enzyme with both ATP sulfurylase and APS kinase activity, which mediates two steps in the sulfate activation pathway. The first step is the transfer of a sulfate group to ATP to yield adenosine 5'-phosphosulfate (APS), and the second step is the transfer of a phosphate group from ATP to APS yield...
Homo sapiens (Human)
O43255
SIAH2_HUMAN
MSRPSSTGPSANKPCSKQPPPQPQHTPSPAAPPAAATISAAGPGSSAVPAAAAVISGPGGGGGAGPVSPQHHELTSLFECPVCFDYVLPPILQCQAGHLVCNQCRQKLSCCPTCRGALTPSIRNLAMEKVASAVLFPCKYATTGCSLTLHHTEKPEHEDICEYRPYSCPCPGASCKWQGSLEAVMSHLMHAHKSITTLQGEDIVFLATDINLPGAVDWVMMQSCFGHHFMLVLEKQEKYEGHQQFFAIVLLIGTRKQAENFAYRLELNGNRRRLTWEATPRSIHDGVAAAIMNSDCLVFDTAIAHLFADNGNLGINVTIS...
2.3.2.27
null
amyloid fibril formation [GO:1990000]; apoptotic process [GO:0006915]; canonical Wnt signaling pathway [GO:0060070]; cell cycle [GO:0007049]; negative regulation of apoptotic process [GO:0043066]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of cysteine-type endopeptidase act...
cytoplasm [GO:0005737]; cytosol [GO:0005829]; early endosome [GO:0005769]; intracellular membrane-bounded organelle [GO:0043231]; neuronal cell body [GO:0043025]; nucleoplasm [GO:0005654]
transcription corepressor activity [GO:0003714]; ubiquitin conjugating enzyme binding [GO:0031624]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270]
PF21362;PF03145;PF21361;
3.30.40.10;
SINA (Seven in absentia) family
PTM: Phosphorylated at Ser-28 by MAPK14, which mediates the degradation by the proteasome of EGLN3 (By similarity). Phosphorylated at Ser-28 by DYRK2; this increases the ubiquitin ligase activity and promotes degradation of EGLN3. {ECO:0000250|UniProtKB:Q06986, ECO:0000269|PubMed:22878263}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19224863, ECO:0000269|PubMed:22878263}. Nucleus {ECO:0000269|PubMed:22878263}. Note=Predominantly cytoplasmic. Partially nuclear. {ECO:0000269|PubMed:22878263}.
CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27;
null
PATHWAY: Protein modification; protein ubiquitination.
null
null
FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:11483518, PubMed:19224863, PubMed:9334332). E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiqui...
Homo sapiens (Human)
O43257
ZNHI1_HUMAN
MVEKKTSVRSQDPGQRRVLDRAARQRRINRQLEALENDNFQDDPHAGLPQLGKRLPQFDDDADTGKKKKKTRGDHFKLRFRKNFQALLEEQNLSVAEGPNYLTACAGPPSRPQRPFCAVCGFPSPYTCVSCGARYCTVRCLGTHQETRCLKWTV
null
null
calcium ion homeostasis [GO:0055074]; chromatin remodeling [GO:0006338]; heart process [GO:0003015]; intestinal stem cell homeostasis [GO:0036335]; muscle cell differentiation [GO:0042692]; positive regulation of DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class medi...
nucleoplasm [GO:0005654]; nucleosome [GO:0000786]; nucleus [GO:0005634]; Swr1 complex [GO:0000812]
histone binding [GO:0042393]; metal ion binding [GO:0046872]; nucleosome binding [GO:0031491]
PF04438;
3.30.60.190;
ZNHIT1 family
PTM: Phosphorylated on Thr by MAPK11 or MAPK14 (PubMed:17380123). Phosphorylation is required for MYOG induction, for deposition of histone H2AZ1 at the MYOG promoter and for SRCAP complex integrity (PubMed:20473270). {ECO:0000269|PubMed:17380123, ECO:0000269|PubMed:20473270}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17892483}.
null
null
null
null
null
FUNCTION: Plays a role in chromatin remodeling by promoting the incorporation of histone variant H2AZ1/H2A.Z into the genome to regulate gene expression (PubMed:20473270, PubMed:35175558). Promotes SRCAP complex-mediated deposition of histone variant H2AZ1 to lymphoid fate regulator genes, enhancing lymphoid lineage co...
Homo sapiens (Human)
O43264
ZW10_HUMAN
MASFVTEVLAHSGRLEKEDLGTRISRLTRRVEEIKGEVCNMISKKYSEFLPSMQSAQGLITQVDKLSEDIDLLKSRIESEVRRDLHVSTGEFTDLKQQLERDSVVLSLLKQLQEFSTAIEEYNCALTEKKYVTGAQRLEEAQKCLKLLKSRKCFDLKILKSLSMELTIQKQNILYHLGEEWQKLIVWKFPPSKDTSSLESYLQTELHLYTEQSHKEEKTPMPPISSVLLAFSVLGELHSKLKSFGQMLLKYILRPLASCPSLHAVIESQPNIVIIRFESIMTNLEYPSPSEVFTKIRLVLEVLQKQLLDLPLDTDLENEK...
null
null
cell division [GO:0051301]; endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; establishment of mitotic spindle orientation [GO:0000132]; Golgi organization [GO:0007030]; meiotic cell cycle [GO:0051321]; mitotic metaphase chromosome alignment [GO:0007080]; mitotic sister chromatid segregation [GO:0...
cytosol [GO:0005829]; Dsl1/NZR complex [GO:0070939]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; kinetochore [GO:0000776]; kinetochore microtubule [GO:0005828]; lipid droplet [GO:0005811]; membrane [GO:0016020]; nucleus [GO:0005634]; RZZ complex [GO:1990423]; spindle pole [GO:000092...
centromeric DNA binding [GO:0019237]
PF20666;PF20665;PF06248;
1.10.357.150;
ZW10 family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15029241}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:15029241}; Peripheral membrane protein {ECO:0000269|PubMed:15029241}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:11590237, ECO:0000269|PubMed:15485811, ECO:0000269|PubMed:15824131}. Cytoplasm, ...
null
null
null
null
null
FUNCTION: Essential component of the mitotic checkpoint, which prevents cells from prematurely exiting mitosis. Required for the assembly of the dynein-dynactin and MAD1-MAD2 complexes onto kinetochores. Its function related to the spindle assembly machinery is proposed to depend on its association in the mitotic RZZ c...
Homo sapiens (Human)
O43272
PROD_HUMAN
MALRRALPALRPCIPRFVPLSTAPASREQPAAGPAAVPGGGSATAVRPPVPAVDFGNAQEAYRSRRTWELARSLLVLRLCAWPALLARHEQLLYVSRKLLGQRLFNKLMKMTFYGHFVAGEDQESIQPLLRHYRAFGVSAILDYGVEEDLSPEEAEHKEMESCTSAAERDGSGTNKRDKQYQAHWAFGDRRNGVISARTYFYANEAKCDSHMETFLRCIEASGRVSDDGFIAIKLTALGRPQFLLQFSEVLAKWRCFFHQMAVEQGQAGLAAMDTKLEVAVLQESVAKLGIASRAEIEDWFTAETLGVSGTMDLLDWSSL...
1.5.5.2
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:15662599};
4-hydroxyproline catabolic process [GO:0019470]; intrinsic apoptotic signaling pathway in response to oxidative stress [GO:0008631]; proline catabolic process [GO:0006562]; proline catabolic process to glutamate [GO:0010133]; proline metabolic process [GO:0006560]; regulation of oxidative stress-induced neuron intrinsi...
intracellular membrane-bounded organelle [GO:0043231]; mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]
FAD binding [GO:0071949]; proline dehydrogenase activity [GO:0004657]
PF01619;
3.20.20.220;
Proline oxidase family
null
SUBCELLULAR LOCATION: Mitochondrion matrix.
CATALYTIC ACTIVITY: Reaction=a quinone + L-proline = (S)-1-pyrroline-5-carboxylate + a quinol + H(+); Xref=Rhea:RHEA:23784, ChEBI:CHEBI:15378, ChEBI:CHEBI:17388, ChEBI:CHEBI:24646, ChEBI:CHEBI:60039, ChEBI:CHEBI:132124; EC=1.5.5.2; Evidence={ECO:0000269|PubMed:15662599};
null
PATHWAY: Amino-acid degradation; L-proline degradation into L-glutamate; L-glutamate from L-proline: step 1/2.
null
null
FUNCTION: Converts proline to delta-1-pyrroline-5-carboxylate. {ECO:0000269|PubMed:15662599}.
Homo sapiens (Human)
O43278
SPIT1_HUMAN
MAPARTMARARLAPAGIPAVALWLLCTLGLQGTQAGPPPAPPGLPAGADCLNSFTAGVPGFVLDTNASVSNGATFLESPTVRRGWDCVRACCTTQNCNLALVELQPDRGEDAIAACFLINCLYEQNFVCKFAPREGFINYLTREVYRSYRQLRTQGFGGSGIPKAWAGIDLKVQPQEPLVLKDVENTDWRLLRGDTDVRVERKDPNQVELWGLKEGTYLFQLTVTSSDHPEDTANVTVTVLSTKQTEDYCLASNKVGRCRGSFPRWYYDPTEQICKSFVYGGCLGNKNNYLREEECILACRGVQGGPLRGSSGAQATFPQ...
null
null
branching involved in labyrinthine layer morphogenesis [GO:0060670]; cellular response to BMP stimulus [GO:0071773]; epidermis development [GO:0008544]; epithelium development [GO:0060429]; extracellular matrix organization [GO:0030198]; negative regulation of neural precursor cell proliferation [GO:2000178]; neural tu...
cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; membrane [GO:0016020]; plasma membrane [GO:0005886]
serine-type endopeptidase inhibitor activity [GO:0004867]
PF00014;PF00057;PF07502;
2.60.40.10;4.10.400.10;4.10.410.10;
null
null
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9045658}. Cytoplasm {ECO:0000269|PubMed:28710277}. Cell membrane {ECO:0000269|PubMed:28710277}.
null
null
null
null
null
FUNCTION: Inhibitor of HGFAC (PubMed:9045658). Inhibits serine protease activity of ST14/matriptase in vitro (PubMed:28710277). Inhibits serine protease activity of TMPRSS13, via the BPTI/Kunitz inhibitor 1 domain (PubMed:20977675). {ECO:0000269|PubMed:20977675, ECO:0000269|PubMed:28710277, ECO:0000269|PubMed:9045658}.
Homo sapiens (Human)
O43280
TREA_HUMAN
MPGRTWELCLLLLLGLGLGSQEALPPPCESEIYCHGELLNQVQMAKLYQDDKQFVDMPLSIAPEQVLQTFTELSRDHNHSIPREQLQAFVHEHFQAKGQELQPWTPADWKDSPQFLQKISDAKLRAWAGQLHQLWKKLGKKMKPEVLSHPERFSLIYSEHPFIVPGGRFVEFYYWDSYWVMEGLLLSEMAETVKGMLQNFLDLVKTYGHVPNGGRVYYLQRSQPPLLTLMMDCYLTHTNDTAFLQENIETLALELDFWTKNRTVSVSLEGKNYLLNRYYVPYGGPRPESYSKDVELADTLPEGDREALWAELKAGAESGW...
3.2.1.28
null
animal organ morphogenesis [GO:0009887]; trehalose catabolic process [GO:0005993]; trehalose metabolic process [GO:0005991]
extracellular exosome [GO:0070062]; membrane [GO:0016020]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]
alpha,alpha-trehalase activity [GO:0004555]
PF01204;
1.50.10.10;
Glycosyl hydrolase 37 family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P19813}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P19813}.
CATALYTIC ACTIVITY: Reaction=alpha,alpha-trehalose + H2O = alpha-D-glucose + beta-D-glucose; Xref=Rhea:RHEA:32675, ChEBI:CHEBI:15377, ChEBI:CHEBI:15903, ChEBI:CHEBI:16551, ChEBI:CHEBI:17925; EC=3.2.1.28; Evidence={ECO:0000269|PubMed:8773341, ECO:0000269|PubMed:9427547};
null
null
null
null
FUNCTION: Intestinal trehalase is probably involved in the hydrolysis of ingested trehalose. {ECO:0000269|PubMed:8773341, ECO:0000269|PubMed:9427547}.
Homo sapiens (Human)
O43281
EFS_HUMAN
MAIATSTQLARALYDNTAESPQELSFRRGDVLRVLQREGAGGLDGWCLCSLHGQQGIVPANRVKLLPAGPAPKPSLSPASPAQPGSPYPAPDHSNEDQEVYVVPPPARPCPTSGPPAGPCPPSPDLIYKIPRASGTQLAAPRDALEVYDVPPTALRVPSSGPYDCPASFSHPLTRVAPQPPGEDDAPYDVPLTPKPPAELEPDLEWEGGREPGPPIYAAPSNLKRASALLNLYEAPEELLADGEGGGTDEGIYDVPLLGPEAPPSPEPPGALASHDQDTLAQLLARSPPPPHRPRLPSAESLSRRPLPALPVPEAPSPSP...
null
null
cell adhesion [GO:0007155]; cell migration [GO:0016477]; intracellular signal transduction [GO:0035556]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]
cytoplasm [GO:0005737]; focal adhesion [GO:0005925]; plasma membrane [GO:0005886]
protein domain specific binding [GO:0019904]; SH3 domain binding [GO:0017124]
PF12026;PF14604;
1.20.120.230;2.30.30.40;
CAS family
PTM: Phosphorylated on multiple tyrosine residues. Phosphorylated on tyrosines by FYN and SRC (By similarity). {ECO:0000250}.
null
null
null
null
null
null
FUNCTION: Docking protein which plays a central coordinating role for tyrosine-kinase-based signaling related to cell adhesion. May serve as an activator of SRC and a downstream effector. Interacts with the SH3 domain of FYN and with CRK, SRC, and YES (By similarity). {ECO:0000250}.
Homo sapiens (Human)
O43283
M3K13_HUMAN
MANFQEHLSCSSSPHLPFSESKTFNGLQDELTAMGNHPSPKLLEDQQEKGMVRTELIESVHSPVTTTVLTSVSEDSRDQFENSVLQLREHDESETAVSQGNSNTVDGESTSGTEDIKIQFSRSGSGSGGFLEGLFGCLRPVWNIIGKAYSTDYKLQQQDTWEVPFEEISELQWLGSGAQGAVFLGKFRAEEVAIKKVREQNETDIKHLRKLKHPNIIAFKGVCTQAPCYCIIMEYCAHGQLYEVLRAGRKITPRLLVDWSTGIASGMNYLHLHKIIHRDLKSPNVLVTHTDAVKISDFGTSKELSDKSTKMSFAGTVAWM...
2.7.11.25
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q60700};
JNK cascade [GO:0007254]; peptidyl-serine phosphorylation [GO:0018105]; positive regulation of axon extension [GO:0045773]; positive regulation of branching morphogenesis of a nerve [GO:1905492]; positive regulation of JUN kinase activity [GO:0043507]; positive regulation of neuron maturation [GO:0014042]; positive reg...
cytoplasm [GO:0005737]; membrane [GO:0016020]
ATP binding [GO:0005524]; enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; IkappaB kinase complex binding [GO:0106137]; JUN kinase kinase kinase activity [GO:0004706]; MAP kinase kinase kinase activity [GO:0004709]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; prot...
PF07714;
1.10.510.10;
Protein kinase superfamily, STE Ser/Thr protein kinase family, MAP kinase kinase kinase subfamily
PTM: Autophosphorylated on serine and threonine residues. {ECO:0000269|PubMed:9353328}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9353328}. Membrane {ECO:0000269|PubMed:9353328}; Peripheral membrane protein {ECO:0000269|PubMed:9353328}.
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=2.7.11.25; Evidence={ECO:0000269|PubMed:9353328}; CATALYTIC...
null
null
null
null
FUNCTION: Activates the JUN N-terminal pathway through activation of the MAP kinase kinase MAP2K7. Acts synergistically with PRDX3 to regulate the activation of NF-kappa-B in the cytosol. This activation is kinase-dependent and involves activating the IKK complex, the IKBKB-containing complex that phosphorylates inhibi...
Homo sapiens (Human)
O43286
B4GT5_HUMAN
MRARRGLLRLPRRSLLAALFFFSLSSSLLYFVYVAPGIVNTYLFMMQAQGILIRDNVRTIGAQVYEQVLRSAYAKRNSSVNDSDYPLDLNHSETFLQTTTFLPEDFTYFANHTCPERLPSMKGPIDINMSEIGMDYIHELFSKDPTIKLGGHWKPSDCMPRWKVAILIPFRNRHEHLPVLFRHLLPMLQRQRLQFAFYVVEQVGTQPFNRAMLFNVGFQEAMKDLDWDCLIFHDVDHIPESDRNYYGCGQMPRHFATKLDKYMYLLPYTEFFGGVSGLTVEQFRKINGFPNAFWGWGGEDDDLWNRVQNAGYSVSRPEGD...
2.4.1.-; 2.4.1.274
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q9UBX8};
carbohydrate metabolic process [GO:0005975]; central nervous system myelination [GO:0022010]; central nervous system neuron axonogenesis [GO:0021955]; ganglioside biosynthetic process via lactosylceramide [GO:0010706]; glycoprotein biosynthetic process [GO:0009101]; glycosylation [GO:0070085]; neuron maturation [GO:004...
Golgi apparatus [GO:0005794]; Golgi cisterna membrane [GO:0032580]; Golgi membrane [GO:0000139]
galactosyltransferase activity [GO:0008378]; metal ion binding [GO:0046872]; N-acetyllactosamine synthase activity [GO:0003945]; UDP-galactose:glucosylceramide beta-1,4-galactosyltransferase activity [GO:0008489]
PF02709;PF13733;
null
Glycosyltransferase 7 family
null
SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:P15291}; Single-pass type II membrane protein. Golgi apparatus {ECO:0000250|UniProtKB:A0A1S6M251}. Note=Trans cisternae of Golgi stack. {ECO:0000250|UniProtKB:P15291}.
CATALYTIC ACTIVITY: Reaction=a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine + UDP-alpha-D-galactose = a beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer(d18:1(4E)) + H(+) + UDP; Xref=Rhea:RHEA:31495, ChEBI:CHEBI:15378, ChEBI:CHEBI:17950, ChEBI:CHEBI:22801, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914; EC=2.4.1.274; Evidence={ECO:0000...
null
PATHWAY: Protein modification; protein glycosylation.; PATHWAY: Sphingolipid metabolism.
null
null
FUNCTION: Catalyzes the synthesis of lactosylceramide (LacCer) via the transfer of galactose from UDP-galactose to glucosylceramide (GlcCer) (PubMed:24498430). LacCer is the starting point in the biosynthesis of all gangliosides (membrane-bound glycosphingolipids) which play pivotal roles in the CNS including neuronal ...
Homo sapiens (Human)
O43290
SNUT1_HUMAN
MGSSKKHRGEKEAAGTTAAAGTGGATEQPPRHREHKKHKHRSGGSGGSGGERRKRSRERGGERGSGRRGAEAEARSSTHGRERSQAEPSERRVKREKRDDGYEAAASSKTSSGDASSLSIEETNKLRAKLGLKPLEVNAIKKEAGTKEEPVTADVINPMALRQREELREKLAAAKEKRLLNQKLGKIKTLGEDDPWLDDTAAWIERSRQLQKEKDLAEKRAKLLEEMDQEFGVSTLVEEEFGQRRQDLYSARDLQGLTVEHAIDSFREGETMILTLKDKGVLQEEEDVLVNVNLVDKERAEKNVELRKKKPDYLPYAEDE...
null
null
maturation of 5S rRNA [GO:0000481]; mRNA cis splicing, via spliceosome [GO:0045292]; mRNA splicing, via spliceosome [GO:0000398]; positive regulation of cytotoxic T cell differentiation [GO:0045585]; spliceosomal snRNP assembly [GO:0000387]
Cajal body [GO:0015030]; catalytic step 2 spliceosome [GO:0071013]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; U2-type precatalytic spliceosome [GO:0071005]; U4/U6 x U5 tri-snRNP complex [GO:0046540]
RNA binding [GO:0003723]
PF19252;PF03343;
null
SNU66/SART1 family
PTM: Sumoylated with SUMO2.
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11350945, ECO:0000269|PubMed:9449708}. Note=Found in the nucleus of mitogen-activated peripheral blood mononuclear cells (PBMCs), tumor cells, or normal cell lines, but not in normal tissues except testis and fetal liver or in unstimulated PBMCs, suggesting preferential...
null
null
null
null
null
FUNCTION: Plays a role in mRNA splicing as a component of the U4/U6-U5 tri-snRNP, one of the building blocks of the spliceosome. May also bind to DNA. {ECO:0000269|PubMed:11350945, ECO:0000269|PubMed:25092792}.
Homo sapiens (Human)
O43291
SPIT2_HUMAN
MAQLCGLRRSRAFLALLGSLLLSGVLAADRERSIHDFCLVSKVVGRCRASMPRWWYNVTDGSCQLFVYGGCDGNSNNYLTKEECLKKCATVTENATGDLATSRNAADSSVPSAPRRQDSEDHSSDMFNYEEYCTANAVTGPCRASFPRWYFDVERNSCNNFIYGGCRGNKNSYRSEEACMLRCFRQQENPPLPLGSKVVVLAGLFVMVLILFLGASMVYLIRVARRNQERALRTVWSSGDDKEQLVKNTYVL
null
null
basement membrane organization [GO:0071711]; cellular response to BMP stimulus [GO:0071773]; epithelial cell morphogenesis involved in placental branching [GO:0060672]; establishment or maintenance of cell polarity [GO:0007163]; negative regulation of cell motility [GO:2000146]; negative regulation of cell-cell adhesio...
cytoplasm [GO:0005737]; extracellular region [GO:0005576]; membrane [GO:0016020]; plasma membrane [GO:0005886]
endopeptidase inhibitor activity [GO:0004866]; serine-type endopeptidase inhibitor activity [GO:0004867]
PF00014;
4.10.410.10;
null
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28710277, ECO:0000269|PubMed:34562451}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:28710277}.
null
null
null
null
null
FUNCTION: Inhibitor of HGFAC (PubMed:9346890). Also inhibits plasmin, and plasma and tissue kallikrein (PubMed:9115294). Inhibits serine protease activity of TMPRSS13 (PubMed:20977675, PubMed:28710277). Inhibits serine protease activity of ST14/matriptase in vitro (PubMed:28710277). {ECO:0000269|PubMed:20977675, ECO:00...
Homo sapiens (Human)
O43292
GPAA1_HUMAN
MGLLSDPVRRRALARLVLRLNAPLCVLSYVAGIAWFLALVFPPLTQRTYMSENAMGSTMVEEQFAGGDRARAFARDFAAHRKKSGALPVAWLERTMRSVGLEVYTQSFSRKLPFPDETHERYMVSGTNVYGILRAPRAASTESLVLTVPCGSDSTNSQAVGLLLALAAHFRGQIYWAKDIVFLVTEHDLLGTEAWLEAYHDVNVTGMQSSPLQGRAGAIQAAVALELSSDVVTSLDVAVEGLNGQLPNLDLLNLFQTFCQKGGLLCTLQGKLQPEDWTSLDGPLQGLQTLLLMVLRQASGRPHGSHGLFLRYRVEALTLR...
null
null
attachment of GPI anchor to protein [GO:0016255]; protein retention in ER lumen [GO:0006621]; protein-containing complex assembly [GO:0065003]
centrosome [GO:0005813]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; GPI-anchor transamidase complex [GO:0042765]; membrane [GO:0016020]; mitochondrion [GO:0005739]
tubulin binding [GO:0015631]
PF04114;
3.40.630.10;
null
null
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11483512}; Multi-pass membrane protein {ECO:0000269|PubMed:11483512}.
null
null
PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
null
null
FUNCTION: Component of the GPI transamidase complex, necessary for transfer of GPI to proteins (PubMed:34576938). Essential for GPI-anchoring of precursor proteins but not for GPI synthesis. Acts before or during formation of the carbonyl intermediate. {ECO:0000269|PubMed:29100095, ECO:0000269|PubMed:34576938, ECO:0000...
Homo sapiens (Human)
O43293
DAPK3_HUMAN
MSTFRQEDVEDHYEMGEELGSGQFAIVRKCRQKGTGKEYAAKFIKKRRLSSSRRGVSREEIEREVNILREIRHPNIITLHDIFENKTDVVLILELVSGGELFDFLAEKESLTEDEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNVPNPRIKLIDFGIAHKIEAGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGETKQETLTNISAVNYDFDEEYFSNTSELAKDFIRRLLVKDPKRRMTIAQSLEHSWIKAIRRRNVRGEDSGRKPERRRLKTTRLKEYTIKSHSSLPPNNSYA...
2.7.11.1
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:10356987};
apoptotic process [GO:0006915]; apoptotic signaling pathway [GO:0097190]; cellular response to type II interferon [GO:0071346]; chromatin organization [GO:0006325]; intracellular signal transduction [GO:0035556]; negative regulation of translation [GO:0017148]; positive regulation of apoptotic process [GO:0043065]; pos...
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PML body [GO:0016605]
ATP binding [GO:0005524]; cAMP response element binding protein binding [GO:0008140]; identical protein binding [GO:0042802]; leucine zipper domain binding [GO:0043522]; protein homodimerization activity [GO:0042803]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; sm...
PF00069;
1.10.510.10;
Protein kinase superfamily, CAMK Ser/Thr protein kinase family, DAP kinase subfamily
PTM: The phosphorylation status is critical for kinase activity, oligomerization and intracellular localization. Phosphorylation at Thr-180, Thr-225 and Thr-265 is essential for activity. The phosphorylated form is localized in the cytoplasm promoted by phosphorylation at Thr-299; nuclear translocation or retention is ...
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15367680, ECO:0000269|PubMed:15910542, ECO:0000269|PubMed:20854903}. Cytoplasm {ECO:0000269|PubMed:15367680, ECO:0000269|PubMed:15611134, ECO:0000269|PubMed:17953487, ECO:0000269|PubMed:20854903}. Note=Predominantly localizes to the cytoplasm but can shuttle between the...
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:10356987, ECO:000026...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=12 uM for myosin (isoform 2) {ECO:0000269|PubMed:17126281}; KM=6.2 uM for myosin (isoform 1) {ECO:0000269|PubMed:17126281}; KM=73 uM for MYL12B (isoform 2) {ECO:0000269|PubMed:17126281}; KM=10.4 uM for MYL12B (isoform 1) {ECO:0000269|PubMed:17126281}; Vmax=248 nmol...
null
null
null
FUNCTION: Serine/threonine kinase which is involved in the regulation of apoptosis, autophagy, transcription, translation and actin cytoskeleton reorganization. Involved in the regulation of smooth muscle contraction. Regulates both type I (caspase-dependent) apoptotic and type II (caspase-independent) autophagic cell ...
Homo sapiens (Human)
O43294
TGFI1_HUMAN
MEDLDALLSDLETTTSHMPRSGAPKERPAEPLTPPPSYGHQPQTGSGESSGASGDKDHLYSTVCKPRSPKPAAPAAPPFSSSSGVLGTGLCELDRLLQELNATQFNITDEIMSQFPSSKVASGEQKEDQSEDKKRPSLPSSPSPGLPKASATSATLELDRLMASLSDFRVQNHLPASGPTQPPVVSSTNEGSPSPPEPTGKGSLDTMLGLLQSDLSRRGVPTQAKGLCGSCNKPIAGQVVTALGRAWHPEHFVCGGCSTALGGSSFFEKDGAPFCPECYFERFSPRCGFCNQPIRHKMVTALGTHWHPEHFCCVSCGEPF...
null
null
actin cytoskeleton organization [GO:0030036]; cell adhesion [GO:0007155]; cell fate commitment [GO:0045165]; epithelial cell differentiation [GO:0030855]; fat cell differentiation [GO:0045444]; heart development [GO:0007507]; morphogenesis of embryonic epithelium [GO:0016331]; muscle structure development [GO:0061061];...
adherens junction [GO:0005912]; cytosol [GO:0005829]; filamentous actin [GO:0031941]; focal adhesion [GO:0005925]; intracellular membrane-bounded organelle [GO:0043231]; nuclear matrix [GO:0016363]; stress fiber [GO:0001725]; Z disc [GO:0030018]
actin binding [GO:0003779]; I-SMAD binding [GO:0070411]; metal ion binding [GO:0046872]; muscle alpha-actinin binding [GO:0051371]; nuclear androgen receptor binding [GO:0050681]; Roundabout binding [GO:0048495]; transcription coactivator activity [GO:0003713]
PF00412;PF03535;
2.10.110.10;
Paxillin family
PTM: Phosphorylated by gonadotropin-releasing hormone-activated SRC. {ECO:0000269|PubMed:10838081, ECO:0000269|PubMed:11311131, ECO:0000269|PubMed:11856738, ECO:0000269|PubMed:17202804, ECO:0000269|PubMed:17233630}.
SUBCELLULAR LOCATION: Cell junction, focal adhesion. Nucleus matrix. Cytoplasm, cytoskeleton. Note=Associated with the actin cytoskeleton; colocalizes with stress fibers.
null
null
null
null
null
FUNCTION: Functions as a molecular adapter coordinating multiple protein-protein interactions at the focal adhesion complex and in the nucleus. Links various intracellular signaling modules to plasma membrane receptors and regulates the Wnt and TGFB signaling pathways. May also regulate SLC6A3 and SLC6A4 targeting to t...
Homo sapiens (Human)
O43295
SRGP3_HUMAN
MSSQTKFKKDKEIIAEYEAQIKEIRTQLVEQFKCLEQQSESRLQLLQDLQEFFRRKAEIELEYSRSLEKLAERFSSKIRSSREHQFKKDQYLLSPVNCWYLVLHQTRRESRDHATLNDIFMNNVIVRLSQISEDVIRLFKKSKEIGLQMHEELLKVTNELYTVMKTYHMYHAESISAESKLKEAEKQEEKQFNKSGDLSMNLLRHEDRPQRRSSVKKIEKMKEKRQAKYSENKLKCTKARNDYLLNLAATNAAISKYYIHDVSDLIDCCDLGFHASLARTFRTYLSAEYNLETSRHEGLDVIENAVDNLDSRSDKHTVMD...
null
null
negative regulation of cell migration [GO:0030336]; regulation of small GTPase mediated signal transduction [GO:0051056]; signal transduction [GO:0007165]
cytoplasm [GO:0005737]; cytosol [GO:0005829]
GTPase activator activity [GO:0005096]
PF00611;PF00620;PF00018;
1.20.1270.60;1.10.555.10;2.30.30.40;
null
null
null
null
null
null
null
null
FUNCTION: GTPase-activating protein for RAC1 and perhaps Cdc42, but not for RhoA small GTPase. May attenuate RAC1 signaling in neurons. {ECO:0000269|PubMed:12195014, ECO:0000269|PubMed:12447388}.
Homo sapiens (Human)
O43296
ZN264_HUMAN
MAAAVLTDRAQVSVTFDDVAVTFTKEEWGQLDLAQRTLYQEVMLENCGLLVSLGCPVPKAELICHLEHGQEPWTRKEDLSQDTCPGDKGKPKTTEPTTCEPALSEGISLQGQVTQGNSVDSQLGQAEDQDGLSEMQEGHFRPGIDPQEKSPGKMSPECDGLGTADGVCSRIGQEQVSPGDRVRSHNSCESGKDPMIQEEENNFKCSECGKVFNKKHLLAGHEKIHSGVKPYECTECGKTFIKSTHLLQHHMIHTGERPYECMECGKAFNRKSYLTQHQRIHSGEKPYKCNECGKAFTHRSNFVLHNRRHTGEKSFVCTEC...
null
null
regulation of transcription by RNA polymerase II [GO:0006357]
nucleus [GO:0005634]
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
PF01352;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: May be involved in transcriptional regulation.
Homo sapiens (Human)
O43298
ZBT43_HUMAN
MEPGTNSFRVEFPDFSSTILQKLNQQRQQGQLCDVSIVVQGHIFRAHKAVLAASSPYFCDQVLLKNSRRIVLPDVMNPRVFENILLSSYTGRLVMPAPEIVSYLTAASFLQMWHVVDKCTEVLEGNPTVLCQKLNHGSDHQSPSSSSYNGLVESFELGSGGHTDFPKAQELRDGENEEESTKDELSSQLTEHEYLPSNSSTEHDRLSTEMASQDGEEGASDSAEFHYTRPMYSKPSIMAHKRWIHVKPERLEQACEGMDVHATYDEHQVTESINTVQTEHTVQPSGVEEDFHIGEKKVEAEFDEQADESNYDEQVDFYGS...
null
null
regulation of transcription by RNA polymerase II [GO:0006357]
chromatin [GO:0000785]; nucleus [GO:0005634]
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase III general transcription initiation factor binding [GO:0001025]; sequence-specific double-stranded DNA b...
PF00651;
3.30.160.60;
Krueppel C2H2-type zinc-finger protein family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
null
null
null
null
null
FUNCTION: May be involved in transcriptional regulation.
Homo sapiens (Human)
O43299
AP5Z1_HUMAN
MFSAGAESLLHQAREIQDEELKKFCSRICKLLQAEDLGPDTLDSLQRLFLIISATKYSRRLEKTCVDLLQATLGLPACPEQLQVLCAAILREMSPSDSLSLAWDHTQNSRQLSLVASVLLAQGDRNEEVRAVGQGVLRALESRQPEGPSLRHLLPVMAKVVVLSPGTLQEDQATLLSKRLVDWLRYASLQQGLPHSGGFFSTPRARQPGPVTEVDGAVATDFFTVLSSGHRFTDDQWLNVQAFSMLRAWLLHSGPEGPGTLDTDDRSEQEGSTLSVISATSSAGRLLPPRERLREVAFEYCQRLIEQSNRRALRKGDSDL...
null
null
double-strand break repair via homologous recombination [GO:0000724]; endosomal transport [GO:0016197]; protein transport [GO:0015031]; vesicle-mediated transport [GO:0016192]
AP-5 adaptor complex [GO:0044599]; AP-type membrane coat adaptor complex [GO:0030119]; cytoplasm [GO:0005737]; late endosome [GO:0005770]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
null
PF14764;
1.25.10.10;
null
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20613862}. Nucleus {ECO:0000269|PubMed:20613862}. Note=By SDS-PAGE, 2 isoforms have been observed, the shorter seems to be predominantly nuclear and the longer is mostly cytoplasmic. {ECO:0000269|PubMed:20613862}.
null
null
null
null
null
FUNCTION: As part of AP-5, a probable fifth adaptor protein complex it may be involved in endosomal transport. According to PubMed:20613862 it is a putative helicase required for efficient homologous recombination DNA double-strand break repair. {ECO:0000269|PubMed:20613862, ECO:0000269|PubMed:22022230}.
Homo sapiens (Human)
O43300
LRRT2_HUMAN
MGLHFKWPLGAPMLAAIYAMSMVLKMLPALGMACPPKCRCEKLLFYCDSQGFHSVPNATDKGSLGLSLRHNHITELERDQFASFSQLTWLHLDHNQISTVKEDAFQGLYKLKELILSSNKIFYLPNTTFTQLINLQNLDLSFNQLSSLHPELFYGLRKLQTLHLRSNSLRTIPVRLFWDCRSLEFLDLSTNRLRSLARNGFAGLIKLRELHLEHNQLTKINFAHFLRLSSLHTLFLQWNKISNLTCGMEWTWGTLEKLDLTGNEIKAIDLTVFETMPNLKILLMDNNKLNSLDSKILNSLRSLTTVGLSGNLWECSARIC...
null
null
long-term synaptic potentiation [GO:0060291]; negative regulation of receptor internalization [GO:0002091]; positive regulation of synapse assembly [GO:0051965]; regulation of postsynaptic density assembly [GO:0099151]; synapse organization [GO:0050808]
excitatory synapse [GO:0060076]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; GABA-ergic synapse [GO:0098982]; glutamatergic synapse [GO:0098978]; hippocampal mossy fiber to CA3 synapse [GO:0098686]; postsynaptic density membrane [GO:0098839]; postsynaptic specialization membrane [GO:0099634]; S...
neurexin family protein binding [GO:0042043]
PF13855;
3.80.10.10;
LRRTM family
null
SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Postsynaptic cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Localized to excitatory synapses. {ECO:0000250}.
null
null
null
null
null
FUNCTION: Involved in the development and maintenance of excitatory synapses in the vertebrate nervous system. Regulates surface expression of AMPA receptors and instructs the development of functional glutamate release sites. Acts as a ligand for the presynaptic receptors NRXN1-A and NRXN1-B (By similarity). {ECO:0000...
Homo sapiens (Human)
O43303
CP110_HUMAN
MEEYEKFCEKSLARIQEASLSTESFLPAQSESISLIRFHGVAILSPLLNIEKRKEMQQEKQKALDVEARKQVNRKKALLTRVQEILDNVQVRKAPNASDFDQWEMETVYSNSEVRNLNVPATFPNSFPSHTEHSTAAKLDKIAGILPLDNEDQCKTDGIDLARDSEGFNSPKQCDSSNISHVENEAFPKTSSATPQETLISDGPFSVNEQQDLPLLAEVIPDPYVMSLQNLMKKSKEYIEREQSRRSLRGSINRIVNESHLDKEHDAVEVADCVKEKGQLTGKHCVSVIPDKPSLNKSNVLLQGASTQASSMSMPVLASF...
null
null
centriole replication [GO:0007099]; centrosome duplication [GO:0051298]; ciliary basal body organization [GO:0032053]; negative regulation of centriole elongation [GO:1903723]; negative regulation of cilium assembly [GO:1902018]; positive regulation of cilium assembly [GO:0045724]; regulation of cytokinesis [GO:0032465...
centriole [GO:0005814]; centrosome [GO:0005813]; cilium [GO:0005929]; cytosol [GO:0005829]; protein-containing complex [GO:0032991]
null
PF16025;
null
null
PTM: Phosphorylated by CDKs. {ECO:0000269|PubMed:12361598}.; PTM: Ubiquitinated by the SCF(CCNF) during G2 phase, leading to its degradation by the proteasome and preventing centrosome reduplication. Deubiquitinated by USP33 in S and G2/M phase, leading to stabilize CCP110 during the period which centrioles duplicate a...
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:12361598, ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:16760425, ECO:0000269|PubMed:17681131, ECO:0000269|PubMed:17719545, ECO:0000269|PubMed:20596027, ECO:0000269|PubMed:21620453, ECO:0000269|PubM...
null
null
null
null
null
FUNCTION: Necessary for centrosome duplication at different stages of procentriole formation. Acts as a key negative regulator of ciliogenesis in collaboration with CEP97 by capping the mother centriole thereby preventing cilia formation (PubMed:17681131, PubMed:17719545, PubMed:23486064, PubMed:30375385, PubMed:353017...
Homo sapiens (Human)
O43306
ADCY6_HUMAN
MSWFSGLLVPKVDERKTAWGERNGQKRSRRRGTRAGGFCTPRYMSCLRDAEPPSPTPAGPPRCPWQDDAFIRRGGPGKGKELGLRAVALGFEDTEVTTTAGGTAEVAPDAVPRSGRSCWRRLVQVFQSKQFRSAKLERLYQRYFFQMNQSSLTLLMAVLVLLTAVLLAFHAAPARPQPAYVALLACAAALFVGLMVVCNRHSFRQDSMWVVSYVVLGILAAVQVGGALAADPRSPSAGLWCPVFFVYIAYTLLPIRMRAAVLSGLGLSTLHLILAWQLNRGDAFLWKQLGANVLLFLCTNVIGICTHYPAEVSQRQAFQE...
4.6.1.1
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:15385642}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:15385642}; Note=Binds 2 magnesium ions per subunit. Is also active with manganese (in vitro). {ECO:0000250|UniProtKB:P30803};
adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway [GO:0007193]; blood vessel diameter maintenance [GO:0097746]; cAMP biosynthetic process [GO:0006171]; cellular response to catecholamine stimulus [GO:0071870]...
cilium [GO:0005929]; membrane [GO:0016020]; plasma membrane [GO:0005886]; stereocilium [GO:0032420]
adenylate cyclase activity [GO:0004016]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein kinase binding [GO:0019901]; protein kinase C binding [GO:0005080]
PF16214;PF06327;PF00211;
3.30.70.1230;
Adenylyl cyclase class-4/guanylyl cyclase family
PTM: Phosphorylation by RAF1 increases enzyme activity. Phosphorylation by PKA at Ser-662 inhibits the GNAS-mediated increase in catalytic activity. Phosphorylation by PKC at Ser-556, Ser-662 and Thr-919 inhibits catalytic activity. {ECO:0000250|UniProtKB:Q03343}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17110384}; Multi-pass membrane protein {ECO:0000305}. Cell projection, cilium {ECO:0000250|UniProtKB:Q01341}. Cell projection, stereocilium {ECO:0000250|UniProtKB:Q01341}.
CATALYTIC ACTIVITY: Reaction=ATP = 3',5'-cyclic AMP + diphosphate; Xref=Rhea:RHEA:15389, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58165; EC=4.6.1.1; Evidence={ECO:0000269|PubMed:17110384, ECO:0000269|PubMed:17916776};
null
null
null
null
FUNCTION: Catalyzes the formation of the signaling molecule cAMP downstream of G protein-coupled receptors (PubMed:17110384, PubMed:17916776). Functions in signaling cascades downstream of beta-adrenergic receptors in the heart and in vascular smooth muscle cells (PubMed:17916776). Functions in signaling cascades downs...
Homo sapiens (Human)
O43307
ARHG9_HUMAN
MTLLITGDSIVSAEAVWDHVTMANRELAFKAGDVIKVLDASNKDWWWGQIDDEEGWFPASFVRLWVNQEDEVEEGPSDVQNGHLDPNSDCLCLGRPLQNRDQMRANVINEIMSTERHYIKHLKDICEGYLKQCRKRRDMFSDEQLKVIFGNIEDIYRFQMGFVRDLEKQYNNDDPHLSEIGPCFLEHQDGFWIYSEYCNNHLDACMELSKLMKDSRYQHFFEACRLLQQMIDIAIDGFLLTPVQKICKYPLQLAELLKYTAQDHSDYRYVAAALAVMRNVTQQINERKRRLENIDKIAQWQASVLDWEGEDILDRSSELI...
null
null
regulation of postsynaptic specialization assembly [GO:0099150]; regulation of small GTPase mediated signal transduction [GO:0051056]
cytosol [GO:0005829]; GABA-ergic synapse [GO:0098982]; postsynaptic density [GO:0014069]; postsynaptic specialization [GO:0099572]
guanyl-nucleotide exchange factor activity [GO:0005085]
PF00169;PF00621;PF07653;
1.20.900.10;2.30.29.30;2.30.30.40;
null
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10559246}. Postsynaptic density {ECO:0000250|UniProtKB:Q3UTH8}.
null
null
null
null
null
FUNCTION: Acts as a guanine nucleotide exchange factor (GEF) for CDC42. Promotes formation of GPHN clusters (By similarity). {ECO:0000250|UniProtKB:Q9QX73, ECO:0000269|PubMed:10559246}.
Homo sapiens (Human)
O43309
ZSC12_HUMAN
MASTWAIQAHMDQDEPLEVKIEEEKYTTRQDWDLRKNNTHSREVFRQYFRQFCYQETSGPREALSRLRELCHQWLRPETHTKEQILELLVLEQFLTILPEELQAWVQEQHPESGEEVVTVLEDLERELDEPGEQVSVHTGEQEMFLQETVRLRKEGEPSMSLQSMKAQPKYESPELESQQEQVLDVETGNEYGNLKQEVSEEMEPHGKTSSKFENDMSKSARCGETREPEEITEEPSACSREDKQPTCDENGVSLTENSDHTEHQRICPGEESYGCDDCGKAFSQHSHLIEHQRIHTGDRPYKCEECGKAFRGRTVLIRH...
null
null
regulation of transcription by RNA polymerase II [GO:0006357]
nucleus [GO:0005634]
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
PF02023;PF00096;
3.30.160.60;1.10.4020.10;
Krueppel C2H2-type zinc-finger protein family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187}.
null
null
null
null
null
FUNCTION: May be involved in transcriptional regulation.
Homo sapiens (Human)
O43310
CTIF_HUMAN
MENSSAASASSEAGSSRSQEIEELERFIDSYVLEYQVQGLLADKTEGDGESERTQSHISQWTADCSEPLDSSCSFSRGRAPPQQNGSKDNSLDMLGTDIWAANTFDSFSGATWDLQPEKLDFTQFHRKVRHTPKQPLPHIDREGCGKGKLEDGDGINLNDIEKVLPAWQGYHPMPHEVEIAHTKKLFRRRRNDRRRQQRPPGGNKPQQHGDHQPGSAKHNRDHQKSYQGGSAPHPSGRPTHHGYSQNRRWHHGNMKHPPGDKGEAGAHRNAKETMTIENPKLEDTAGDTGHSSLEAPRSPDTLAPVASERLPPQQSGGPE...
null
null
nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; regulation of translational initiation [GO:0006446]
cytosol [GO:0005829]; perinuclear region of cytoplasm [GO:0048471]
RNA binding [GO:0003723]; translation activator activity [GO:0008494]
PF02854;
1.25.40.180;
CTIF family
null
SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:19648179}.
null
null
null
null
null
FUNCTION: Specifically required for the pioneer round of mRNA translation mediated by the cap-binding complex (CBC), that takes place during or right after mRNA export via the nuclear pore complex (NPC). Acts via its interaction with the NCBP1/CBP80 component of the CBC complex and recruits the 40S small subunit of the...
Homo sapiens (Human)
O43312
MTSS1_HUMAN
MEAVIEKECSALGGLFQTIISDMKGSYPVWEDFINKAGKLQSQLRTTVVAAAAFLDAFQKVADMATNTRGGTREIGSALTRMCMRHRSIEAKLRQFSSALIDCLINPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTLKLQKKAKKGRGDIQPQLDSALQDVNDKYLLLEETEKQAVRKALIEERGRFCTFISMLRPVIEEEISMLGEITHLQTISEDLKSLTMDPHKLPSSSEQVILDLKGSDYSWSYQTPPSSPSTTMSRKSSVCSSLNSVNSSDSRSSGSHSHSPSSHYRYRSSNLAQQAPVRLSSVSSH...
null
null
actin cytoskeleton organization [GO:0030036]; adherens junction maintenance [GO:0034334]; cell adhesion [GO:0007155]; cellular response to fluid shear stress [GO:0071498]; epithelial cell proliferation involved in renal tubule morphogenesis [GO:2001013]; glomerulus morphogenesis [GO:0072102]; microspike assembly [GO:00...
actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; endocytic vesicle [GO:0030139]; ruffle [GO:0001726]
actin binding [GO:0003779]; actin monomer binding [GO:0003785]; identical protein binding [GO:0042802]; phospholipid binding [GO:0005543]; signaling receptor binding [GO:0005102]
PF08397;PF02205;
1.20.1270.60;
MTSS family
null
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
null
null
null
null
null
FUNCTION: May be related to cancer progression or tumor metastasis in a variety of organ sites, most likely through an interaction with the actin cytoskeleton.
Homo sapiens (Human)
O43313
ATMIN_HUMAN
MAASEAAAAAGSAALAAGARAVPAATTGAAAAASGPWVPPGPRLRGSRPRPAGATQQPAVPAPPAGELIQPSVSELSRAVRTNILCTVRGCGKILPNSPALNMHLVKSHRLQDGIVNPTIRKDLKTGPKFYCCPIEGCPRGPERPFSQFSLVKQHFMKMHAEKKHKCSKCSNSYGTEWDLKRHAEDCGKTFRCTCGCPYASRTALQSHIYRTGHEIPAEHRDPPSKKRKMENCAQNQKLSNKTIESLNNQPIPRPDTQELEASEIKLEPSFEDSCGSNTDKQTLTTPPRYPQKLLLPKPKVALVKLPVMQFSVMPVFVPT...
null
null
DNA damage response [GO:0006974]; motile cilium assembly [GO:0044458]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of gene expression [GO:0010628]; positive regulation of non-motile cilium assembly [GO:1902857]; positive regulation of transcription by RNA polymerase II [GO:00459...
nuclear body [GO:0016604]; nucleus [GO:0005634]
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; dynein complex binding [GO:0070840]; metal ion binding [GO:0046872]; transcription cis-regulatory region binding [GO:0000976]
null
3.30.160.60;
null
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15933716, ECO:0000269|PubMed:17525732}. Note=Nuclear, in discrete foci during G1 phase.
null
null
null
null
null
FUNCTION: Transcription factor. Plays a crucial role in cell survival and RAD51 foci formation in response to methylating DNA damage. Involved in regulating the activity of ATM in the absence of DNA damage. May play a role in stabilizing ATM. Binds to the DYNLL1 promoter and activates its transcription. {ECO:0000269|Pu...
Homo sapiens (Human)
O43314
VIP2_HUMAN
MSEAPRFFVGPEDTEINPGNYRHFFHHADEDDEEEDDSPPERQIVVGICSMAKKSKSKPMKEILERISLFKYITVVVFEEEVILNEPVENWPLCDCLISFHSKGFPLDKAVAYAKLRNPFVINDLNMQYLIQDRREVYSILQAEGILLPRYAILNRDPNNPKECNLIEGEDHVEVNGEVFQKPFVEKPVSAEDHNVYIYYPTSAGGGSQRLFRKIGSRSSVYSPESNVRKTGSYIYEEFMPTDGTDVKVYTVGPDYAHAEARKSPALDGKVERDSEGKEVRYPVILNAREKLIAWKVCLAFKQTVCGFDLLRANGQSYVC...
2.7.4.24
null
inositol metabolic process [GO:0006020]; inositol phosphate biosynthetic process [GO:0032958]; inositol phosphate metabolic process [GO:0043647]; phosphorylation [GO:0016310]; sensory perception of sound [GO:0007605]
cytosol [GO:0005829]
ATP binding [GO:0005524]; diphosphoinositol-pentakisphosphate kinase activity [GO:0033857]; inositol heptakisphosphate kinase activity [GO:0000829]; inositol hexakisphosphate 1-kinase activity [GO:0052723]; inositol hexakisphosphate 3-kinase activity [GO:0052724]; inositol hexakisphosphate 5-kinase activity [GO:0000832...
PF00328;PF18086;
3.40.50.11950;3.30.470.20;3.40.50.1240;
Histidine acid phosphatase family, VIP1 subfamily
null
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:17690096}.
CATALYTIC ACTIVITY: Reaction=1D-myo-inositol hexakisphosphate + ATP = 1-diphospho-1D-myo-inositol 2,3,4,5,6-pentakisphosphate + ADP; Xref=Rhea:RHEA:37459, ChEBI:CHEBI:30616, ChEBI:CHEBI:58130, ChEBI:CHEBI:74946, ChEBI:CHEBI:456216; EC=2.7.4.24; Evidence={ECO:0000269|PubMed:21222653, ECO:0000269|PubMed:29590114}; Physio...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.13 uM for InsP6 {ECO:0000269|PubMed:17690096}; KM=0.19 uM for InsP7 {ECO:0000269|PubMed:17690096}; Vmax=0.39 nmol/min/mg enzyme with InsP6 as substrate {ECO:0000269|PubMed:17690096}; Vmax=1.38 nmol/min/mg enzyme with InsP7 as substrate {ECO:0000269|PubMed:1769009...
null
null
null
FUNCTION: Bifunctional inositol kinase that acts in concert with the IP6K kinases IP6K1, IP6K2 and IP6K3 to synthesize the diphosphate group-containing inositol pyrophosphates diphosphoinositol pentakisphosphate, PP-InsP5, and bis-diphosphoinositol tetrakisphosphate, (PP)2-InsP4 (PubMed:17690096, PubMed:17702752, PubMe...
Homo sapiens (Human)
O43315
AQP9_HUMAN
MQPEGAEKGKSFKQRLVLKSSLAKETLSEFLGTFILIVLGCGCVAQAILSRGRFGGVITINVGFSMAVAMAIYVAGGVSGGHINPAVSLAMCLFGRMKWFKLPFYVGAQFLGAFVGAATVFGIYYDGLMSFAGGKLLIVGENATAHIFATYPAPYLSLANAFADQVVATMILLIIVFAIFDSRNLGAPRGLEPIAIGLLIIVIASSLGLNSGCAMNPARDLSPRLFTALAGWGFEVFRAGNNFWWIPVVGPLVGAVIGGLIYVLVIEIHHPEPDSVFKTEQSEDKPEKYELSVIM
null
null
amine transport [GO:0015837]; canalicular bile acid transport [GO:0015722]; cellular response to cAMP [GO:0071320]; glycerol transmembrane transport [GO:0015793]; purine nucleobase transport [GO:0006863]; pyrimidine nucleobase transport [GO:0015855]; response to pain [GO:0048265]; urea transmembrane transport [GO:00719...
basolateral plasma membrane [GO:0016323]; intracellular membrane-bounded organelle [GO:0043231]; plasma membrane [GO:0005886]
glycerol channel activity [GO:0015254]; purine nucleobase transmembrane transporter activity [GO:0005345]; pyrimidine nucleobase transmembrane transporter activity [GO:0005350]; urea channel activity [GO:0015265]; urea transmembrane transporter activity [GO:0015204]; water channel activity [GO:0015250]
PF00230;
1.20.1080.10;
MIP/aquaporin (TC 1.A.8) family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10564231, ECO:0000269|PubMed:9514918}; Multi-pass membrane protein {ECO:0000305}.
null
null
null
null
null
FUNCTION: Forms a water channel with a broad specificity. Also permeable glycerol and urea. Mediates passage of a wide variety of small, non-charged solutes including carbamides, polyols, purines, and pyrimidines. {ECO:0000269|PubMed:10564231, ECO:0000269|PubMed:30420639, ECO:0000269|PubMed:9514918}.
Homo sapiens (Human)
O43316
PAX4_HUMAN
MHQDGISSMNQLGGLFVNGRPLPLDTRQQIVRLAVSGMRPCDISRILKVSNGCVSKILGRYYRTGVLEPKGIGGSKPRLATPPVVARIAQLKGECPALFAWEIQRQLCAEGLCTQDKTPSVSSINRVLRALQEDQGLPCTRLRSPAVLAPAVLTPHSGSETPRGTHPGTGHRNRTIFSPSQAEALEKEFQRGQYPDSVARGKLATATSLPEDTVRVWFSNRRAKWRRQEKLKWEMQLPGASQGLTVPRVAPGIISAQQSPGSVPTAALPALEPLGPSCYQLCWATAPERCLSDTPPKACLKPCWDCGSFLLPVIAPSCVD...
null
null
animal organ morphogenesis [GO:0009887]; cell differentiation [GO:0030154]; regulation of transcription by RNA polymerase II [GO:0006357]
chromatin [GO:0000785]; nucleoplasm [GO:0005654]
DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific double-stranded DNA binding [GO:1990837]
PF00046;PF00292;
1.10.10.60;1.10.10.10;
Paired homeobox family
null
SUBCELLULAR LOCATION: Nucleus.
null
null
null
null
null
FUNCTION: Plays an important role in the differentiation and development of pancreatic islet beta cells. Transcriptional repressor that binds to a common element in the glucagon, insulin and somatostatin promoters. Competes with PAX6 for this same promoter binding site. Isoform 2 appears to be a dominant negative form ...
Homo sapiens (Human)
O43318
M3K7_HUMAN
MSTASAASSSSSSSAGEMIEAPSQVLNFEEIDYKEIEVEEVVGRGAFGVVCKAKWRAKDVAIKQIESESERKAFIVELRQLSRVNHPNIVKLYGACLNPVCLVMEYAEGGSLYNVLHGAEPLPYYTAAHAMSWCLQCSQGVAYLHSMQPKALIHRDLKPPNLLLVAGGTVLKICDFGTACDIQTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAFRIMWAVHNGTRPPLIKNLPKPIESLMTRCWSKDPSQRPSMEEIVKIMTHLMRYFPGADEPLQYPCQYSDEGQSNSATSTGSFM...
2.7.11.25
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305|PubMed:16289117};
activation of NF-kappaB-inducing kinase activity [GO:0007250]; anoikis [GO:0043276]; canonical NF-kappaB signal transduction [GO:0007249]; cellular response to angiotensin [GO:1904385]; cellular response to hypoxia [GO:0071456]; cellular response to tumor necrosis factor [GO:0071356]; cytoplasmic pattern recognition re...
ATAC complex [GO:0140672]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; endosome membrane [GO:0010008]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
ATP binding [GO:0005524]; DNA-binding transcription factor binding [GO:0140297]; histone kinase activity [GO:0035173]; identical protein binding [GO:0042802]; linear polyubiquitin binding [GO:1990450]; magnesium ion binding [GO:0000287]; MAP kinase activity [GO:0004707]; MAP kinase kinase kinase activity [GO:0004709]; ...
PF07714;
1.10.510.10;
Protein kinase superfamily, STE Ser/Thr protein kinase family, MAP kinase kinase kinase subfamily
PTM: Association with TAB1/MAP3K7IP1 promotes autophosphorylation at Ser-192 and subsequent activation. Association with TAB2/MAP3K7IP2, itself associated with free unanchored Lys-63 polyubiquitin chain, promotes autophosphorylation and subsequent activation of MAP3K7. Dephosphorylation at Ser-192 by PPM1B/PP2CB and at...
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12242293}. Cell membrane {ECO:0000269|PubMed:12242293}; Peripheral membrane protein {ECO:0000269|PubMed:12242293}; Cytoplasmic side {ECO:0000269|PubMed:12242293}. Note=Although the majority of MAP3K7/TAK1 is found in the cytosol, when complexed with TAB1/MAP3K7IP1 and...
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=2.7.11.25; Evidence={ECO:0000269|PubMed:10094049, ECO:00002...
null
null
null
null
FUNCTION: Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway (PubMed:10094049, PubMed:11460167, PubMed:12589052, PubMed:16845370, PubMed:16893890, PubMed:21512573, PubMed:8663074, PubMed:9079627). Plays an important role in the cascades of cellular responses evoke...
Homo sapiens (Human)
O43320
FGF16_HUMAN
MAEVGGVFASLDWDLHGFSSSLGNVPLADSPGFLNERLGQIEGKLQRGSPTDFAHLKGILRRRQLYCRTGFHLEIFPNGTVHGTRHDHSRFGILEFISLAVGLISIRGVDSGLYLGMNERGELYGSKKLTRECVFREQFEENWYNTYASTLYKHSDSERQYYVALNKDGSPREGYRTKRHQKFTHFLPRPVDPSKLPSMSRDLFHYR
null
null
animal organ morphogenesis [GO:0009887]; cell differentiation [GO:0030154]; cell-cell signaling [GO:0007267]; fibroblast growth factor receptor signaling pathway [GO:0008543]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of endothelial cell chemotaxis to fibroblast growth facto...
cytoplasm [GO:0005737]; extracellular region [GO:0005576]; extracellular space [GO:0005615]
fibroblast growth factor receptor binding [GO:0005104]; growth factor activity [GO:0008083]
PF00167;
2.80.10.50;
Heparin-binding growth factors family
null
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O54769}.
null
null
null
null
null
FUNCTION: Plays an important role in the regulation of embryonic development, cell proliferation and cell differentiation, and is required for normal cardiomyocyte proliferation and heart development. {ECO:0000269|PubMed:16597617}.
Homo sapiens (Human)
O43323
DHH_HUMAN
MALLTNLLPLCCLALLALPAQSCGPGRGPVGRRRYARKQLVPLLYKQFVPGVPERTLGASGPAEGRVARGSERFRDLVPNYNPDIIFKDEENSGADRLMTERCKERVNALAIAVMNMWPGVRLRVTEGWDEDGHHAQDSLHYEGRALDITTSDRDRNKYGLLARLAVEAGFDWVYYESRNHVHVSVKADNSLAVRAGGCFPGNATVRLWSGERKGLRELHRGDWVLAADASGRVVPTPVLLFLDRDLQRRASFVAVETEWPPRKLLLTPWHLVFAARGPAPAPGDFAPVFARRLRAGDSVLAPGGDALRPARVARVAREE...
3.1.-.-
null
cell fate specification [GO:0001708]; cell-cell signaling [GO:0007267]; Leydig cell differentiation [GO:0033327]; male sex determination [GO:0030238]; myelination [GO:0042552]; osteoblast differentiation [GO:0001649]; positive regulation of smoothened signaling pathway [GO:0045880]; protein autoprocessing [GO:0016540];...
endoplasmic reticulum membrane [GO:0005789]; extracellular space [GO:0005615]; Golgi membrane [GO:0000139]; plasma membrane [GO:0005886]
calcium ion binding [GO:0005509]; cholesterol-protein transferase activity [GO:0140853]; patched binding [GO:0005113]; peptidase activity [GO:0008233]; zinc ion binding [GO:0008270]
PF01085;PF01079;
3.30.1380.10;2.170.16.10;
Hedgehog family
PTM: [Desert hedgehog protein]: Partially autoproteolyzed (PubMed:24342078, PubMed:30298535). The C-terminal domain displays an autoproteolysis activity and a cholesterol transferase activity (By similarity). Both activities result in the cleavage of the full-length protein and covalent attachment of a cholesterol moie...
SUBCELLULAR LOCATION: [Desert hedgehog protein N-product]: Cell membrane {ECO:0000250|UniProtKB:Q62226}; Lipid-anchor {ECO:0000250|UniProtKB:Q62226}.; SUBCELLULAR LOCATION: [Desert hedgehog protein]: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q15465}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q15465}. ...
CATALYTIC ACTIVITY: [Desert hedgehog protein]: Reaction=cholesterol + glycyl-L-cysteinyl-[protein] + H(+) = [protein]-C-terminal glycyl cholesterol ester + N-terminal L-cysteinyl-[protein]; Xref=Rhea:RHEA:59504, Rhea:RHEA-COMP:12707, Rhea:RHEA-COMP:15369, Rhea:RHEA-COMP:15374, ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, ChEB...
null
null
null
null
FUNCTION: [Desert hedgehog protein]: The C-terminal part of the desert hedgehog protein precursor displays an autoproteolysis and a cholesterol transferase activity (By similarity). Both activities result in the cleavage of the full-length protein into two parts (N-product and C-product) followed by the covalent attach...
Homo sapiens (Human)
O43324
MCA3_HUMAN
MAAAAELSLLEKSLGLSKGNKYSAQGERQIPVLQTNNGPSLTGLTTIAAHLVKQANKEYLLGSTAEEKAIVQQWLEYRVTQVDGHSSKNDIHTLLKDLNSYLEDKVYLTGYNFTLADILLYYGLHRFIVDLTVQEKEKYLNVSRWFCHIQHYPGIRQHLSSVVFIKNRLYTNSH
null
null
cellular response to leukemia inhibitory factor [GO:1990830]; negative regulation of cell population proliferation [GO:0008285]; positive regulation of apoptotic process [GO:0043065]; positive regulation of apoptotic signaling pathway [GO:2001235]; positive regulation of cellular senescence [GO:2000774]; positive regul...
aminoacyl-tRNA synthetase multienzyme complex [GO:0017101]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
null
PF00043;
1.20.1050.10;3.40.30.90;
null
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15680327}. Cytoplasm, cytosol {ECO:0000269|PubMed:19289464}. Nucleus {ECO:0000269|PubMed:15680327}. Note=Cytoplasmic under growth arrest conditions. Translocated into the nucleus when growth resumes (S phase) and following DNA damage.
null
null
null
null
null
FUNCTION: Positive modulator of ATM response to DNA damage. {ECO:0000250|UniProtKB:Q9D1M4}.
Homo sapiens (Human)
O43353
RIPK2_HUMAN
MNGEAICSALPTIPYHKLADLRYLSRGASGTVSSARHADWRVQVAVKHLHIHTPLLDSERKDVLREAEILHKARFSYILPILGICNEPEFLGIVTEYMPNGSLNELLHRKTEYPDVAWPLRFRILHEIALGVNYLHNMTPPLLHHDLKTQNILLDNEFHVKIADFGLSKWRMMSLSQSRSSKSAPEGGTIIYMPPENYEPGQKSRASIKHDIYSYAVITWEVLSRKQPFEDVTNPLQIMYSVSQGHRPVINEESLPYDIPHRARMISLIESGWAQNPDERPSFLKCLIELEPVLRTFEEITFLEAVIQLKKTKLQSVSSA...
2.7.10.2; 2.7.11.1
null
activation of cysteine-type endopeptidase activity [GO:0097202]; adaptive immune response [GO:0002250]; apoptotic process [GO:0006915]; canonical NF-kappaB signal transduction [GO:0007249]; CD4-positive, alpha-beta T cell proliferation [GO:0035739]; cellular response to lipoteichoic acid [GO:0071223]; cellular response...
cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]; vesicle [GO:0031982]
ATP binding [GO:0005524]; CARD domain binding [GO:0050700]; caspase binding [GO:0089720]; identical protein binding [GO:0042802]; JUN kinase kinase kinase activity [GO:0004706]; LIM domain binding [GO:0030274]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein homodimerization activity [GO:00...
PF00619;PF07714;
1.10.533.10;1.10.510.10;
Protein kinase superfamily, TKL Ser/Thr protein kinase family
PTM: Polyubiquitinated via both 'Lys-63'- and 'Met-1'-linked polyubiquitin following recruitment by NOD1 or NOD2, creating docking sites for downstream effectors, triggering activation of the NF-kappa-B and MAP kinases signaling (PubMed:22607974, PubMed:29452636, PubMed:30026309). 'Lys-63'-linked polyubiquitination by ...
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21887730}. Cell membrane {ECO:0000269|PubMed:17355968}; Peripheral membrane protein {ECO:0000305|PubMed:17355968}. Endoplasmic reticulum {ECO:0000269|PubMed:28656966}. Note=Recruited to the cell membrane by NOD2 following stimulation by bacterial peptidoglycans. {ECO:...
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:16824733}; CATALYTIC...
null
null
null
null
FUNCTION: Serine/threonine/tyrosine-protein kinase that plays an essential role in modulation of innate and adaptive immune responses (PubMed:14638696, PubMed:17054981, PubMed:21123652, PubMed:28656966, PubMed:9575181, PubMed:9642260). Acts as a key effector of NOD1 and NOD2 signaling pathways: upon activation by bacte...
Homo sapiens (Human)
O43364
HXA2_HUMAN
MNYEFEREIGFINSQPSLAECLTSFPPVADTFQSSSIKTSTLSHSTLIPPPFEQTIPSLNPGSHPRHGAGGRPKPSPAGSRGSPVPAGALQPPEYPWMKEKKAAKKTALLPAAAAAATAAATGPACLSHKESLEIADGSGGGSRRLRTAYTNTQLLELEKEFHFNKYLCRPRRVEIAALLDLTERQVKVWFQNRRMKHKRQTQCKENQNSEGKCKSLEDSEKVEEDEEEKTLFEQALSVSGALLEREGYTFQQNALSQQQAPNGHNGDSQSFPVSPLTSNEKNLKHFQHQSPTVPNCLSTMGQNCGAGLNNDSPEALEVP...
null
null
anterior/posterior pattern specification [GO:0009952]; brain segmentation [GO:0035284]; cell fate determination [GO:0001709]; cellular response to retinoic acid [GO:0071300]; dorsal/ventral pattern formation [GO:0009953]; embryonic viscerocranium morphogenesis [GO:0048703]; middle ear morphogenesis [GO:0042474]; motor ...
chromatin [GO:0000785]; intracellular membrane-bounded organelle [GO:0043231]; nucleoplasm [GO:0005654]
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]; sequence-specific double-stranded DNA binding [GO:1990837]
PF00046;
1.10.10.60;
Antp homeobox family, Proboscipedia subfamily
null
SUBCELLULAR LOCATION: Nucleus.
null
null
null
null
null
FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.
Homo sapiens (Human)
O43365
HXA3_HUMAN
MQKATYYDSSAIYGGYPYQAANGFAYNANQQPYPASAALGADGEYHRPACSLQSPSSAGGHPKAHELSEACLRTLSAPPSQPPSLGEPPLHPPPPQAAPPAPQPPQPAPQPPAPTPAAPPPPSSASPPQNASNNPTPANAAKSPLLNSPTVAKQIFPWMKESRQNTKQKTSSSSSGESCAGDKSPPGQASSKRARTAYTSAQLVELEKEFHFNRYLCRPRRVEMANLLNLTERQIKIWFQNRRMKYKKDQKGKGMLTSSGGQSPSRSPVPPGAGGYLNSMHSLVNSVPYEPQSPPPFSKPPQGTYGLPPASYPASLPSCA...
null
null
angiogenesis [GO:0001525]; animal organ formation [GO:0048645]; anterior/posterior pattern specification [GO:0009952]; blood vessel remodeling [GO:0001974]; cartilage development [GO:0051216]; embryonic skeletal system morphogenesis [GO:0048704]; gene expression [GO:0010467]; glossopharyngeal nerve morphogenesis [GO:00...
chromatin [GO:0000785]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; HMG box domain binding [GO:0071837]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
PF13293;PF00046;
1.10.10.60;
Antp homeobox family
null
SUBCELLULAR LOCATION: Nucleus.
null
null
null
null
null
FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.
Homo sapiens (Human)
O43374
RASL2_HUMAN
MAKRSSLYIRIVEGKNLPAKDITGSSDPYCIVKVDNEPIIRTATVWKTLCPFWGEEYQVHLPPTFHAVAFYVMDEDALSRDDVIGKVCLTRDTIASHPKGFSGWAHLTEVDPDEEVQGEIHLRLEVWPGARACRLRCSVLEARDLAPKDRNGTSDPFVRVRYKGRTRETSIVKKSCYPRWNETFEFELQEGAMEALCVEAWDWDLVSRNDFLGKVVIDVQRLRVVQQEEGWFRLQPDQSKSRRHDEGNLGSLQLEVRLRDETVLPSSYYQPLVHLLCHEVKLGMQGPGQLIPLIEETTSTECRQDVATNLLKLFLGQGLA...
null
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00041}; Note=Binds 3 Ca(2+) ions per C2 domain. {ECO:0000255|PROSITE-ProRule:PRU00041};
cellular response to calcium ion [GO:0071277]; intracellular signal transduction [GO:0035556]; negative regulation of GTPase activity [GO:0034260]; negative regulation of Ras protein signal transduction [GO:0046580]
cytosol [GO:0005829]; plasma membrane [GO:0005886]
GTPase activator activity [GO:0005096]; metal ion binding [GO:0046872]; phospholipid binding [GO:0005543]
PF00779;PF00168;PF00169;PF00616;
2.60.40.150;2.30.29.30;
null
null
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:11448776}. Cell membrane {ECO:0000269|PubMed:11448776}; Peripheral membrane protein {ECO:0000269|PubMed:11448776}. Note=Localized to the cytosol as a result of its lack of phosphoinositide binding activity. Upon agonist-stimulated calcium mobilization, utiliz...
null
null
null
null
null
FUNCTION: Ca(2+)-dependent Ras GTPase-activating protein, that switches off the Ras-MAPK pathway following a stimulus that elevates intracellular calcium. Functions as an adaptor for Cdc42 and Rac1 during FcR-mediated phagocytosis. {ECO:0000269|PubMed:11448776}.
Homo sapiens (Human)
O43379
WDR62_HUMAN
MAAVGSGGYARNDAGEKLPSVMAGVPARRGQSSPPPAPPICLRRRTRLSTASEETVQNRVSLEKVLGITAQNSSGLTCDPGTGHVAYLAGCVVVILDPKENKQQHIFNTARKSLSALAFSPDGKYIVTGENGHRPAVRIWDVEEKNQVAEMLGHKYGVACVAFSPNMKHIVSMGYQHDMVLNVWDWKKDIVVASNKVSCRVIALSFSEDSSYFVTVGNRHVRFWFLEVSTETKVTSTVPLVGRSGILGELHNNIFCGVACGRGRMAGSTFCVSYSGLLCQFNEKRVLEKWINLKVSLSSCLCVSQELIFCGCTDGIVRIF...
null
null
centriole replication [GO:0007099]; cerebral cortex development [GO:0021987]; mitotic spindle organization [GO:0007052]; neurogenesis [GO:0022008]; positive regulation of neuroblast proliferation [GO:0002052]; positive regulation of neuron migration [GO:2001224]; regulation of centrosome cycle [GO:0046605]; regulation ...
centriolar satellite [GO:0034451]; centriole [GO:0005814]; centrosome [GO:0005813]; cytosol [GO:0005829]; mitotic spindle [GO:0072686]; nucleus [GO:0005634]; spindle pole [GO:0000922]
null
PF12894;PF00400;
2.130.10.10;
null
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20729831, ECO:0000269|PubMed:21496009}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:20890278, ECO:0000269|PubMed:20890279, ECO:0000269|PubMed:28089251}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:20890278, ECO:00...
null
null
null
null
null
FUNCTION: Required for cerebral cortical development. Plays a role in neuronal proliferation and migration (PubMed:20729831, PubMed:20890278). Plays a role in mother-centriole-dependent centriole duplication; the function seems also to involve CEP152, CDK5RAP2 and CEP63 through a stepwise assembled complex at the centr...
Homo sapiens (Human)
O43390
HNRPR_HUMAN
MANQVNGNAVQLKEEEEPMDTSSVTHTEHYKTLIEAGLPQKVAERLDEIFQTGLVAYVDLDERAIDALREFNEEGALSVLQQFKESDLSHVQNKSAFLCGVMKTYRQREKQGSKVQESTKGPDEAKIKALLERTGYTLDVTTGQRKYGGPPPDSVYSGVQPGIGTEVFVGKIPRDLYEDELVPLFEKAGPIWDLRLMMDPLSGQNRGYAFITFCGKEAAQEAVKLCDSYEIRPGKHLGVCISVANNRLFVGSIPKNKTKENILEEFSKVTEGLVDVILYHQPDDKKKNRGFCFLEYEDHKSAAQARRRLMSGKVKVWGNV...
null
null
mRNA processing [GO:0006397]; mRNA splicing, via spliceosome [GO:0000398]
catalytic step 2 spliceosome [GO:0071013]; endoplasmic reticulum [GO:0005783]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:1990904]; spliceosomal complex [GO:0005681]
mRNA binding [GO:0003729]; RNA binding [GO:0003723]
PF18360;PF00076;
3.30.70.330;
null
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:31079900}. Microsome {ECO:0000250|UniProtKB:Q7TMK9}. Nucleus, nucleoplasm {ECO:0000269|PubMed:17289661}. Cytoplasm {ECO:0000269|PubMed:17289661}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. The tyrosine phosphorylated form bound to RNA is ...
null
null
null
null
null
FUNCTION: Component of ribonucleosomes, which are complexes of at least 20 other different heterogeneous nuclear ribonucleoproteins (hnRNP). hnRNP play an important role in processing of precursor mRNA in the nucleus.
Homo sapiens (Human)
O43395
PRPF3_HUMAN
MALSKRELDELKPWIEKTVKRVLGFSEPTVVTAALNCVGKGMDKKKAADHLKPFLDDSTLRFVDKLFEAVEEGRSSRHSKSSSDRSRKRELKEVFGDDSEISKESSGVKKRRIPRFEEVEEEPEVIPGPPSESPGMLTKLQIKQMMEAATRQIEERKKQLSFISPPTPQPKTPSSSQPERLPIGNTIQPSQAATFMNDAIEKARKAAELQARIQAQLALKPGLIGNANMVGLANLHAMGIAPPKVELKDQTKPTPLILDEQGRTVDATGKEIELTHRMPTLKANIRAVKREQFKQQLKEKPSEDMESNTFFDPRVSIAPS...
null
null
mRNA processing [GO:0006397]; mRNA splicing, via spliceosome [GO:0000398]; RNA splicing [GO:0008380]; RNA splicing, via transesterification reactions [GO:0000375]; spliceosomal tri-snRNP complex assembly [GO:0000244]
Cajal body [GO:0015030]; cytosol [GO:0005829]; 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]
identical protein binding [GO:0042802]; RNA binding [GO:0003723]
PF08572;PF06544;PF01480;
1.20.1390.10;
null
PTM: Ubiquitinated. Undergoes 'Lys-63'-linked polyubiquitination by PRPF19 and deubiquitination by USP4. 'Lys-63'-linked ubiquitination increases the affinity for PRPF8 and may regulate the assembly of the U4/U6-U5 tri-snRNP complex. {ECO:0000269|PubMed:20595234}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17932117, ECO:0000269|PubMed:26912367, ECO:0000269|PubMed:28781166, ECO:0000269|PubMed:9328476, ECO:0000269|PubMed:9404889}. Nucleus speckle.
null
null
null
null
null
FUNCTION: Plays a role in pre-mRNA splicing as component of the U4/U6-U5 tri-snRNP complex that is involved in spliceosome assembly, and as component of the precatalytic spliceosome (spliceosome B complex). {ECO:0000269|PubMed:26912367, ECO:0000269|PubMed:28781166, ECO:0000305|PubMed:20595234}.
Homo sapiens (Human)
O43396
TXNL1_HUMAN
MVGVKPVGSDPDFQPELSGAGSRLAVVKFTMRGCGPCLRIAPAFSSMSNKYPQAVFLEVDVHQCQGTAATNNISATPTFLFFRNKVRIDQYQGADAVGLEEKIKQHLENDPGSNEDTDIPKGYMDLMPFINKAGCECLNESDEHGFDNCLRKDTTFLESDCDEQLLITVAFNQPVKLYSMKFQGPDNGQGPKYVKIFINLPRSMDFEEAERSEPTQALELTEDDIKEDGIVPLRYVKFQNVNSVTIFVQSNQGEEETTRISYFTFIGTPVQATNMNDFKRVVGKKGESH
null
null
null
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]; proteasome complex [GO:0000502]
disulfide oxidoreductase activity [GO:0015036]; protein-disulfide reductase activity [GO:0015035]
PF06201;PF00085;
3.40.30.10;2.60.120.470;
null
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19349277}. Nucleus {ECO:0000269|PubMed:19349277}. Note=At least 85% of the cellular TXNL1 is proteasome-associated.
null
null
null
null
null
FUNCTION: Active thioredoxin with a redox potential of about -250 mV. {ECO:0000269|PubMed:19349277}.
Homo sapiens (Human)
O43399
TPD54_HUMAN
MDSAGQDINLNSPNKGLLSDSMTDVPVDTGVAARTPAVEGLTEAEEEELRAELTKVEEEIVTLRQVLAAKERHCGELKRRLGLSTLGELKQNLSRSWHDVQVSSAYVKTSEKLGEWNEKVTQSDLYKKTQETLSQAGQKTSAALSTVGSAISRKLGDMRNSATFKSFEDRVGTIKSKVVGDRENGSDNLPSSAGSGDKPLSDPAPF
null
null
carbohydrate metabolic process [GO:0005975]; regulation of cell population proliferation [GO:0042127]
cytoplasm [GO:0005737]; perinuclear region of cytoplasm [GO:0048471]
protein homodimerization activity [GO:0042803]; RNA binding [GO:0003723]
PF04201;
1.50.10.10;
TPD52 family
null
null
null
null
null
null
null
null
Homo sapiens (Human)
O43402
EMC8_HUMAN
MPGVKLTTQAYCKMVLHGAKYPHCAVNGLLVAEKQKPRKEHLPLGGPGAHHTLFVDCIPLFHGTLALAPMLEVALTLIDSWCKDHSYVIAGYYQANERVKDASPNQVAEKVASRIAEGFSDTALIMVDNTKFTMDCVAPTIHVYEHHENRWRCRDPHHDYCEDWPEAQRISASLLDSRSYETLVDFDNHLDDIRNDWTNPEINKAVLHLC
null
null
protein insertion into ER membrane by stop-transfer membrane-anchor sequence [GO:0045050]; tail-anchored membrane protein insertion into ER membrane [GO:0071816]
cytoplasm [GO:0005737]; EMC complex [GO:0072546]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]
null
PF03665;
null
EMC8/EMC9 family
null
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22119785}; Peripheral membrane protein {ECO:0000305|PubMed:32439656}; Cytoplasmic side {ECO:0000269|PubMed:32439656}.
null
null
null
null
null
FUNCTION: Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins (PubMed:29242231, PubMed:29809151, PubMed:30415835, PubMed:32439656, PubMed:32459176). Preferentially accommodates proteins...
Homo sapiens (Human)
O43405
COCH_HUMAN
MSAAWIPALGLGVCLLLLPGPAGSEGAAPIAITCFTRGLDIRKEKADVLCPGGCPLEEFSVYGNIVYASVSSICGAAVHRGVISNSGGPVRVYSLPGRENYSSVDANGIQSQMLSRWSASFTVTKGKSSTQEATGQAVSTAHPPTGKRLKKTPEKKTGNKDCKADIAFLIDGSFNIGQRRFNLQKNFVGKVALMLGIGTEGPHVGLVQASEHPKIEFYLKNFTSAKDVLFAIKEVGFRGGNSNTGKALKHTAQKFFTVDAGVRKGIPKVVVVFIDGWPSDDIEEAGIVAREFGVNVFIVSVAKPIPEELGMVQDVTFVDK...
null
null
regulation of cell shape [GO:0008360]; sensory perception of sound [GO:0007605]
collagen-containing extracellular matrix [GO:0062023]; extracellular region [GO:0005576]
collagen binding [GO:0005518]
PF03815;PF00092;
2.170.130.20;3.40.50.410;
null
PTM: N-glycosylated. {ECO:0000269|PubMed:12843317}.; PTM: A 50 kDa form is created by proteolytic cleavage. {ECO:0000269|PubMed:12843317}.
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:12843317, ECO:0000269|PubMed:22610276}.
null
null
null
null
null
FUNCTION: Plays a role in the control of cell shape and motility in the trabecular meshwork. {ECO:0000269|PubMed:21886777}.
Homo sapiens (Human)
O43422
P52K_HUMAN
MPNFCAAPNCTRKSTQSDLAFFRFPRDPARCQKWVENCRRADLEDKTPDQLNKHYRLCAKHFETSMICRTSPYRTVLRDNAIPTIFDLTSHLNNPHSRHRKRIKELSEDEIRTLKQKKIDETSEQEQKHKETNNSNAQNPSEEEGEGQDEDILPLTLEEKENKEYLKSLFEILILMGKQNIPLDGHEADEIPEGLFTPDNFQALLECRINSGEEVLRKRFETTAVNTLFCSKTQQRQMLEICESCIREETLREVRDSHFFSIITDDVVDIAGEEHLPVLVRFVDESHNLREEFIGFLPYEADAEILAVKFHTMITEKWGL...
null
null
negative regulation of cell population proliferation [GO:0008285]; signal transduction [GO:0007165]
nucleus [GO:0005634]
DNA binding [GO:0003677]; metal ion binding [GO:0046872]; protein dimerization activity [GO:0046983]
PF05699;PF14291;PF05485;
null
null
null
null
null
null
null
null
null
FUNCTION: Upstream regulator of interferon-induced serine/threonine protein kinase R (PKR). May block the PKR-inhibitory function of DNAJC3, resulting in restoration of kinase activity and suppression of cell growth.
Homo sapiens (Human)
O43424
GRID2_HUMAN
MEVFPFLLVLSVWWSRTWDSANADSIIHIGAIFDESAKKDDEVFRTAVGDLNQNEEILQTEKITFSVTFVDGNNPFQAVQEACELMNQGILALVSSIGCTSAGSLQSLADAMHIPHLFIQRSTAGTPRSGCGLTRSNRNDDYTLSVRPPVYLHDVILRVVTEYAWQKFIIFYDSEYDIRGIQEFLDKVSQQGMDVALQKVENNINKMITTLFDTMRIEELNRYRDTLRRAILVMNPATAKSFITEVVETNLVAFDCHWIIINEEINDVDVQELVRRSIGRLTIIRQTFPVPQNISQRCFRGNHRISSTLCDPKDPFAQNM...
null
null
cerebellar granule cell differentiation [GO:0021707]; excitatory postsynaptic potential [GO:0060079]; excitatory synapse assembly [GO:1904861]; glutamate receptor signaling pathway [GO:0007215]; heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0007157]; modulation of chemical synaptic tra...
dendritic spine [GO:0043197]; glutamatergic synapse [GO:0098978]; ionotropic glutamate receptor complex [GO:0008328]; parallel fiber to Purkinje cell synapse [GO:0098688]; plasma membrane [GO:0005886]; postsynaptic density membrane [GO:0098839]; synapse [GO:0045202]
glutamate receptor activity [GO:0008066]; identical protein binding [GO:0042802]; PDZ domain binding [GO:0030165]; scaffold protein binding [GO:0097110]; transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential [GO:1904315]
PF01094;PF00060;PF10613;
1.10.287.70;3.40.50.2300;3.40.190.10;
Glutamate-gated ion channel (TC 1.A.10.1) family, GRID2 subfamily
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Postsynaptic cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
null
null
null
null
null
FUNCTION: Receptor for glutamate. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists. Promotes synaptogenesis and mediates the D-Serine-dependent lo...
Homo sapiens (Human)
O43426
SYNJ1_HUMAN
MAFSKGFRIYHKLDPPPFSLIVETRHKEECLMFESGAVAVLSSAEKEAIKGTYSKVLDAYGLLGVLRLNLGDTMLHYLVLVTGCMSVGKIQESEVFRVTSTEFISLRIDSSDEDRISEVRKVLNSGNFYFAWSASGISLDLSLNAHRSMQEQTTDNRFFWNQSLHLHLKHYGVNCDDWLLRLMCGGVEIRTIYAAHKQAKACLISRLSCERAGTRFNVRGTNDDGHVANFVETEQVVYLDDSVSSFIQIRGSVPLFWEQPGLQVGSHRVRMSRGFEANAPAFDRHFRTLKNLYGKQIIVNLLGSKEGEHMLSKAFQSHLK...
3.1.3.36
null
inositol phosphate metabolic process [GO:0043647]; learning [GO:0007612]; membrane organization [GO:0061024]; neurotransmitter transport [GO:0006836]; phosphatidylinositol biosynthetic process [GO:0006661]; phosphatidylinositol dephosphorylation [GO:0046856]; phosphatidylinositol metabolic process [GO:0046488]; positiv...
clathrin coat of coated pit [GO:0030132]; cytosol [GO:0005829]; membrane coat [GO:0030117]; perinuclear region of cytoplasm [GO:0048471]; presynapse [GO:0098793]; synaptic membrane [GO:0097060]; terminal bouton [GO:0043195]; vesicle membrane [GO:0012506]
inositol-1,4,5-trisphosphate 5-phosphatase activity [GO:0052658]; phosphatidylinositol phosphate 4-phosphatase activity [GO:0034596]; phosphatidylinositol phosphate 5-phosphatase activity [GO:0034595]; phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity [GO:0052629]; phosphatidylinositol-3,5-bisphosphate 5-pho...
PF08952;PF02383;
3.30.70.330;3.60.10.10;
Synaptojanin family; Inositol 1,4,5-trisphosphate 5-phosphatase family
null
SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O18964}.
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + phosphate; Xref=Rhea:RHEA:22764, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58178, ChEBI:CHEBI:58456; EC=3.1.3.36; Evidence={ECO:0000269|PubM...
null
null
null
null
FUNCTION: Phosphatase that acts on various phosphoinositides, including phosphatidylinositol 4-phosphate, phosphatidylinositol (4,5)-bisphosphate and phosphatidylinositol (3,4,5)-trisphosphate (PubMed:23804563, PubMed:27435091). Has a role in clathrin-mediated endocytosis (By similarity). Hydrolyzes PIP2 bound to actin...
Homo sapiens (Human)
O43427
FIBP_HUMAN
MTSELDIFVGNTTLIDEDVYRLWLDGYSVTDAVALRVRSGILEQTGATAAVLQSDTMDHYRTFHMLERLLHAPPKLLHQLIFQIPPSRQALLIERYYAFDEAFVREVLGKKLSKGTKKDLDDISTKTGITLKSCRRQFDNFKRVFKVVEEMRGSLVDNIQQHFLLSDRLARDYAAIVFFANNRFETGKKKLQYLSFGDFAFCAELMIQNWTLGAVGEAPTDPDSQMDDMDMDLDKEFLQDLKELKVLVADKDLLDLHKSLVCTALRGKLGVFSEMEANFKNLSRGLVNVAAKLTHNKDVRDLFVDLVEKFVEPCRSDHWP...
null
null
fibroblast growth factor receptor signaling pathway [GO:0008543]; platelet aggregation [GO:0070527]
endomembrane system [GO:0012505]; membrane [GO:0016020]; mitochondrion [GO:0005739]; nuclear speck [GO:0016607]; nucleus [GO:0005634]
fibroblast growth factor binding [GO:0017134]
PF05427;
null
null
null
SUBCELLULAR LOCATION: Nucleus. Endomembrane system; Peripheral membrane protein. Note=Also associated with cytoplasmic membranes, particularly of mitochondria.
null
null
null
null
null
FUNCTION: May be involved in mitogenic function of FGF1. May mediate with IER2 FGF-signaling in the establishment of laterality in the embryo (By similarity). {ECO:0000250|UniProtKB:Q6T938, ECO:0000269|PubMed:9806903}.
Homo sapiens (Human)
O43432
IF4G3_HUMAN
MNSQPQTRSPFFQRPQIQPPRATIPNSSPSIRPGAQTPTAVYQANQHIMMVNHLPMPYPVPQGPQYCIPQYRHSGPPYVGPPQQYPVQPPGPGPFYPGPGPGDFPNAYGTPFYPSQPVYQSAPIIVPTQQQPPPAKREKKTIRIRDPNQGGKDITEEIMSGGGSRNPTPPIGRPTSTPTPPQQLPSQVPEHSPVVYGTVESAHLAASTPVTAASDQKQEEKPKPDPVLKSPSPVLRLVLSGEKKEQEGQTSETTAIVSIAELPLPPSPTTVSSVARSTIAAPTSSALSSQPIFTTAIDDRCELSSPREDTIPIPSLTSCT...
null
null
positive regulation of translation [GO:0045727]; regulation of translational initiation [GO:0006446]; spermatid development [GO:0007286]; translational initiation [GO:0006413]
cytosol [GO:0005829]; eukaryotic translation initiation factor 4F complex [GO:0016281]; intracellular non-membrane-bounded organelle [GO:0043232]
mRNA binding [GO:0003729]; RNA binding [GO:0003723]; RNA cap binding [GO:0000339]; translation factor activity, RNA binding [GO:0008135]; translation initiation factor activity [GO:0003743]
PF02847;PF02854;PF02020;
1.25.40.180;
Eukaryotic initiation factor 4G family
PTM: Following infection by certain enteroviruses, rhinoviruses and aphthoviruses, EIF4G1 is cleaved by the viral protease 2A, or the leader protease in the case of aphthoviruses. This shuts down the capped cellular mRNA transcription. {ECO:0000269|PubMed:12663812, ECO:0000269|PubMed:15016848}.
null
null
null
null
null
null
FUNCTION: Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome (PubMed:9418880). Functional homolog of EIF4G1 (PubMed:9418880). {ECO:0000269|PubMed:9418880}.
Homo sapiens (Human)
O43435
TBX1_HUMAN
MHFSTVTRDMEAFTASSLSSLGAAGGFPGAASPGADPYGPREPPPPPPRYDPCAAAAPGAPGPPPPPHAYPFAPAAGAATSAAAEPEGPGASCAAAAKAPVKKNAKVAGVSVQLEMKALWDEFNQLGTEMIVTKAGRRMFPTFQVKLFGMDPMADYMLLMDFVPVDDKRYRYAFHSSSWLVAGKADPATPGRVHYHPDSPAKGAQWMKQIVSFDKLKLTNNLLDDNGHIILNSMHRYQPRFHVVYVDPRKDSEKYAEENFKTFVFEETRFTAVTAYQNHRITQLKIASNPFAKGFRDCDPEDWPRNHRPGALPLMSAFAR...
null
null
angiogenesis [GO:0001525]; anterior/posterior pattern specification [GO:0009952]; aorta morphogenesis [GO:0035909]; artery morphogenesis [GO:0048844]; blood vessel development [GO:0001568]; blood vessel morphogenesis [GO:0048514]; cell fate specification [GO:0001708]; cell population proliferation [GO:0008283]; cellula...
chromatin [GO:0000785]; nucleus [GO:0005634]
DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; protein dimerization activity [GO:0046983]; protein homodimerization activity [GO:0042803]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:...
PF00907;
2.60.40.820;
null
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00201}.
null
null
null
null
null
FUNCTION: Transcription factor that plays a key role in cardiovascular development by promoting pharyngeal arch segmentation during embryonic development (By similarity). Also involved in craniofacial muscle development (By similarity). Together with NKX2-5, acts as a regulator of asymmetric cardiac morphogenesis by pr...
Homo sapiens (Human)
O43439
MTG8R_HUMAN
MAKESGISLKEIQVLARQWKVGPEKRVPAMPGSPVEVKIQSRSSPPTMPPLPPINPGGPRPVSFTPTALSNGINHSPPTLNGAPSPPQRFSNGPASSTSSALTNQQLPATCGARQLSKLKRFLTTLQQFGNDISPEIGEKVRTLVLALVNSTVTIEEFHCKLQEATNFPLRPFVIPFLKANLPLLQRELLHCARAAKQTPSQYLAQHEHLLLNTSIASPADSSELLMEVHGNGKRPSPERREENSFDRDTIAPEPPAKRVCTISPAPRHSPALTVPLMNPGGQFHPTPPPLQHYTLEDIATSHLYREPNKMLEHREVRDR...
null
null
DNA-templated transcription [GO:0006351]; intestinal epithelial cell differentiation [GO:0060575]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of neuron projection development [GO:0010977]; negative regulation of Notch signaling pathway [GO:0045746]; negative regulation of trans...
nucleoplasm [GO:0005654]; nucleus [GO:0005634]
metal ion binding [GO:0046872]; transcription corepressor activity [GO:0003714]
PF08788;PF07531;PF01753;
6.10.140.2220;6.10.250.230;1.20.120.1110;
CBFA2T family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
null
null
null
null
null
FUNCTION: Transcriptional corepressor which facilitates transcriptional repression via its association with DNA-binding transcription factors and recruitment of other corepressors and histone-modifying enzymes (PubMed:12559562, PubMed:15203199). Via association with PRDM14 is involved in regulation of embryonic stem ce...
Homo sapiens (Human)
O43447
PPIH_HUMAN
MAVANSSPVNPVVFFDVSIGGQEVGRMKIELFADVVPKTAENFRQFCTGEFRKDGVPIGYKGSTFHRVIKDFMIQGGDFVNGDGTGVASIYRGPFADENFKLRHSAPGLLSMANSGPSTNGCQFFITCSKCDWLDGKHVVFGKIIDGLLVMRKIENVPTGPNNKPKLPVVISQCGEM
5.2.1.8
null
mRNA splicing, via spliceosome [GO:0000398]; positive regulation of viral genome replication [GO:0045070]; protein folding [GO:0006457]; protein peptidyl-prolyl isomerization [GO:0000413]; protein-containing complex assembly [GO:0065003]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; spliceosomal complex [GO:0005681]; U4/U6 snRNP [GO:0071001]; U4/U6 x U5 tri-snRNP complex [GO:0046540]
cyclosporin A binding [GO:0016018]; peptidyl-prolyl cis-trans isomerase activity [GO:0003755]; ribonucleoprotein complex binding [GO:0043021]
PF00160;
2.40.100.10;
Cyclophilin-type PPIase family, PPIase H subfamily
null
SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:9570313}. Cytoplasm {ECO:0000269|PubMed:9570313}. Note=Colocalizes with spliceosomal snRNPs. A small proportion may also be cytoplasmic.
CATALYTIC ACTIVITY: Reaction=[protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833, ChEBI:CHEBI:83834; EC=5.2.1.8; Evidence={ECO:0000269|PubMed:20676357};
null
null
null
null
FUNCTION: PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding (PubMed:20676357). Participates in pre-mRNA splicing. May play a role in the assembly of the U4/U5/U6 tri-snRNP complex, one of the building blocks of the spliceosome. Ma...
Homo sapiens (Human)
O43448
KCAB3_HUMAN
MQVSIACTEQNLRSRSSEDRLCGPRPGPGGGNGGPAGGGHGNPPGGGGSGPKARAALVPRPPAPAGALRESTGRGTGMKYRNLGKSGLRVSCLGLGTWVTFGSQISDETAEDVLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSKGWRRSSYVITTKIFWGGQAETERGLSRKHIIEGLRGSLERLQLGYVDIVFANRSDPNCPMEEIVRAMTYVINQGLALYWGTSRWGAAEIMEAYSMARQFNLIPPVCEQAEHHLFQREKVEMQLPELYHKIGVGSVTWYPLACGLITSKYDGRVPDTCRASIKGYQWLKDKVQS...
1.1.1.-
null
potassium ion transport [GO:0006813]; regulation of potassium ion transmembrane transport [GO:1901379]
cytoplasm [GO:0005737]; plasma membrane [GO:0005886]; voltage-gated potassium channel complex [GO:0008076]
aldo-keto reductase (NADP) activity [GO:0004033]; potassium channel regulator activity [GO:0015459]; transmembrane transporter binding [GO:0044325]; voltage-gated potassium channel activity [GO:0005249]
PF00248;
3.20.20.100;
Shaker potassium channel beta subunit family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
null
null
null
null
null
FUNCTION: Accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. Alters the functional properties of Kv1.5. {ECO:0000269|PubMed:9857044}.
Homo sapiens (Human)
O43451
MGA_HUMAN
MARKKLKKFTTLEIVLSVLLLVLFIISIVLIVLLAKESLKSTAPDPGTTGTPDPGTTGTPDPGTTGTTHARTTGPPDPGTTGTTPVSAECPVVNELERINCIPDQPPTKATCDQRGCCWNPQGAVSVPWCYYSKNHSYHVEGNLVNTNAGFTARLKNLPSSPVFGSNVDNVLLTAEYQTSNRFHFKLTDQTNNRFEVPHEHVQSFSGNAAASLTYQVEISRQPFSIKVTRRSNNRVLFDSSIGPLLFADQFLQLSTRLPSTNVYGLGEHVHQQYRHDMNWKTWPIFNRDTTPNGNGTNLYGAQTFFLCLEDASGLSFGVF...
3.2.1.20
null
dextrin catabolic process [GO:1901027]; maltose catabolic process [GO:0000025]; starch catabolic process [GO:0005983]
apical plasma membrane [GO:0016324]; extracellular exosome [GO:0070062]; ficolin-1-rich granule membrane [GO:0101003]; plasma membrane [GO:0005886]; tertiary granule membrane [GO:0070821]
alpha-1,4-glucosidase activity [GO:0004558]; amylase activity [GO:0016160]; carbohydrate binding [GO:0030246]; catalytic activity [GO:0003824]; glucan 1,4-alpha-glucosidase activity [GO:0004339]; maltose alpha-glucosidase activity [GO:0032450]
PF13802;PF01055;PF21365;PF00088;
3.20.20.80;2.60.40.1760;2.60.40.1180;4.10.110.10;
Glycosyl hydrolase 31 family
PTM: N- and O-glycosylated. {ECO:0000269|PubMed:18036614, ECO:0000269|PubMed:3143729}.; PTM: Does not undergo intracellular or extracellular proteolytic cleavage. {ECO:0000269|PubMed:3143729}.; PTM: Sulfated. {ECO:0000250}.
SUBCELLULAR LOCATION: Apical cell membrane; Single-pass type II membrane protein. Note=Brush border. {ECO:0000269|PubMed:3143729}.
CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-glucose residues with release of alpha-D-glucose.; EC=3.2.1.20; Evidence={ECO:0000269|PubMed:12547908, ECO:0000269|PubMed:18036614, ECO:0000269|PubMed:18356321, ECO:0000269|PubMed:22058037, ECO:0000269|PubMed:27480812}; CATALYTIC AC...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.27 mM for maltoheptaose (with ctMGAM) {ECO:0000269|PubMed:22058037}; KM=1.05 mM for maltohexaose (with ctMGAM) {ECO:0000269|PubMed:22058037}; KM=0.61 mM for maltopentaose (with ctMGAM) {ECO:0000269|PubMed:22058037}; KM=0.96 mM for maltotetraose (with ctMGAM) {ECO...
PATHWAY: Carbohydrate degradation. {ECO:0000305|PubMed:18036614, ECO:0000305|PubMed:22058037, ECO:0000305|PubMed:27480812}.
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7. Has substantial activity at acidic pH. {ECO:0000269|PubMed:18356321};
null
FUNCTION: Alpha-(1,4) exo-glucosidase involved in breakdown of dietary starch oligosaccharides in small intestine. Cleaves the non-reducing alpha-(1,4)-linked glucose residue in linear dextrins with retention of anomeric center stereochemistry (PubMed:12547908, PubMed:18036614, PubMed:18356321, PubMed:22058037, PubMed:...
Homo sapiens (Human)
O43462
MBTP2_HUMAN
MIPVSLVVVVVGGWTVVYLTDLVLKSSVYFKHSYEDWLENNGLSISPFHIRWQTAVFNRAFYSWGRRKARMLYQWFNFGMVFGVIAMFSSFFLLGKTLMQTLAQMMADSPSSYSSSSSSSSSSSSSSSSSSSSSSSLHNEQVLQVVVPGINLPVNQLTYFFTAVLISGVVHEIGHGIAAIREQVRFNGFGIFLFIIYPGAFVDLFTTHLQLISPVQQLRIFCAGIWHNFVLALLGILALVLLPVILLPFYYTGVGVLITEVAEDSPAIGPRGLFVGDLVTHLQDCPVTNVQDWNECLDTIAYEPQIGYCISASTLQQLSF...
3.4.24.85
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:10805775}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:10805775};
ATF6-mediated unfolded protein response [GO:0036500]; bone maturation [GO:0070977]; cholesterol metabolic process [GO:0008203]; endoplasmic reticulum unfolded protein response [GO:0030968]; membrane protein intracellular domain proteolysis [GO:0031293]; mitotic G2 DNA damage checkpoint signaling [GO:0007095]; positive ...
cytoplasm [GO:0005737]; Golgi membrane [GO:0000139]; membrane [GO:0016020]
metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; transcription regulator activator activity [GO:0140537]
PF02163;
2.30.42.10;
Peptidase M50A family
null
SUBCELLULAR LOCATION: Membrane {ECO:0000305|PubMed:19361614}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:19361614}. Golgi apparatus membrane {ECO:0000305|PubMed:16417584}; Multi-pass membrane protein {ECO:0000255}.
CATALYTIC ACTIVITY: Reaction=Cleaves several transcription factors that are type-2 transmembrane proteins within membrane-spanning domains. Known substrates include sterol regulatory element-binding protein (SREBP) -1, SREBP-2 and forms of the transcriptional activator ATF6. SREBP-2 is cleaved at the site 477-DRSRILL-|...
null
null
null
null
FUNCTION: Zinc metalloprotease that mediates intramembrane proteolysis of proteins such as ATF6, ATF6B, SREBF1/SREBP1 and SREBF2/SREBP2 (PubMed:10805775, PubMed:11163209). Catalyzes the second step in the proteolytic activation of the sterol regulatory element-binding proteins (SREBPs) SREBF1/SREBP1 and SREBF2/SREBP2: ...
Homo sapiens (Human)
O43463
SUV91_HUMAN
MAENLKGCSVCCKSSWNQLQDLCRLAKLSCPALGISKRNLYDFEVEYLCDYKKIREQEYYLVKWRGYPDSESTWEPRQNLKCVRILKQFHKDLERELLRRHHRSKTPRHLDPSLANYLVQKAKQRRALRRWEQELNAKRSHLGRITVENEVDLDGPPRAFVYINEYRVGEGITLNQVAVGCECQDCLWAPTGGCCPGASLHKFAYNDQGQVRLRAGLPIYECNSRCRCGYDCPNRVVQKGIRYDLCIFRTDDGRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGATYLFDLDYVEDVYTVDAAYYGNISH...
2.1.1.355
null
cell cycle [GO:0007049]; cell differentiation [GO:0030154]; cellular response to glucose starvation [GO:0042149]; cellular response to hypoxia [GO:0071456]; chromatin organization [GO:0006325]; circadian rhythm [GO:0007623]; DNA damage response [GO:0006974]; energy homeostasis [GO:0097009]; epigenetic programming in th...
chromatin silencing complex [GO:0005677]; chromosome, centromeric region [GO:0000775]; condensed nuclear chromosome [GO:0000794]; cytoplasmic vesicle [GO:0031410]; eNoSc complex [GO:0061773]; heterochromatin [GO:0000792]; nuclear lamina [GO:0005652]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634...
chromatin binding [GO:0003682]; histone H3 methyltransferase activity [GO:0140938]; histone H3K9 methyltransferase activity [GO:0046974]; histone H3K9 trimethyltransferase activity [GO:0140949]; histone methyltransferase activity [GO:0042054]; S-adenosylmethionine-dependent methyltransferase activity [GO:0008757]; tran...
PF00385;PF05033;PF00856;
2.40.50.40;2.170.270.10;
Class V-like SAM-binding methyltransferase superfamily, Histone-lysine methyltransferase family, Suvar3-9 subfamily
PTM: Phosphorylated on serine residues, and to a lesser degree, on threonine residues. The phosphorylated form is stabilized by SBF1 and is less active in its transcriptional repressor function. {ECO:0000269|PubMed:10671371}.; PTM: Ubiquitinated by the DCX(DCAF13) E3 ubiquitin ligase complex, leading to its degradation...
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:29170282, ECO:0000269|PubMed:30111536}. Nucleus lamina. Nucleus, nucleoplasm. Chromosome, centromere. Note=Associates with centromeric constitutive heterochromatin.; SUBCELLULAR LOCATION: Cytoplasmic vesicle, phagosome lumen {ECO:0000269|PubMed:29170282}. Cell membrane ...
CATALYTIC ACTIVITY: Reaction=L-lysyl(9)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(9)-[histone H3] + 3 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60276, Rhea:RHEA-COMP:15538, Rhea:RHEA-COMP:15546, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:...
null
null
null
null
FUNCTION: Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3 using monomethylated H3 'Lys-9' as substrate. Also weakly methylates histone H1 (in vitro). H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) p...
Homo sapiens (Human)
O43464
HTRA2_HUMAN
MAAPRAGRGAGWSLRAWRALGGIRWGRRPRLTPDLRALLTSGTSDPRARVTYGTPSLWARLSVGVTEPRACLTSGTPGPRAQLTAVTPDTRTREASENSGTRSRAWLAVALGAGGAVLLLLWGGGRGPPAVLAAVPSPPPASPRSQYNFIADVVEKTAPAVVYIEILDRHPFLGREVPISNGSGFVVAADGLIVTNAHVVADRRRVRVRLLSGDTYEAVVTAVDPVADIATLRIQTKEPLPTLPLGRSADVRQGEFVVAMGSPFALQNTITSGIVSSAQRPARDLGLPQTNVEYIQTDAAIDFGNSGGPLVNLDGEVIGV...
3.4.21.108
null
adult walking behavior [GO:0007628]; cellular response to growth factor stimulus [GO:0071363]; cellular response to heat [GO:0034605]; cellular response to interferon-beta [GO:0035458]; cellular response to oxidative stress [GO:0034599]; cellular response to retinoic acid [GO:0071300]; ceramide metabolic process [GO:00...
CD40 receptor complex [GO:0035631]; chromatin [GO:0000785]; cytoplasmic side of plasma membrane [GO:0009898]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; mitochondrial intermembrane space [GO:0005758]; mitochond...
identical protein binding [GO:0042802]; peptidase activity [GO:0008233]; serine-type endopeptidase activity [GO:0004252]; serine-type peptidase activity [GO:0008236]; unfolded protein binding [GO:0051082]
PF17820;PF13365;
2.30.42.10;2.40.10.120;
Peptidase S1C family
PTM: Autoproteolytically activated. {ECO:0000269|PubMed:10873535}.
SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Mitochondrion membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Note=Predominantly present in the intermembrane space. Released into the cytosol following apoptotic stimuli, such as UV treatment, and stimulation of mitochondria with caspase-8 tr...
CATALYTIC ACTIVITY: Reaction=Cleavage of non-polar aliphatic amino-acids at the P1 position, with a preference for Val, Ile and Met. At the P2 and P3 positions, Arg is selected most strongly with a secondary preference for other hydrophilic residues.; EC=3.4.21.108;
null
null
null
null
FUNCTION: Serine protease that shows proteolytic activity against a non-specific substrate beta-casein. Promotes or induces cell death either by direct binding to and inhibition of BIRC proteins (also called inhibitor of apoptosis proteins, IAPs), leading to an increase in caspase activity, or by a BIRC inhibition-inde...
Homo sapiens (Human)
O43474
KLF4_HUMAN
MRQPPGESDMAVSDALLPSFSTFASGPAGREKTLRQAGAPNNRWREELSHMKRLPPVLPGRPYDLAAATVATDLESGGAGAACGGSNLAPLPRRETEEFNDLLDLDFILSNSLTHPPESVAATVSSSASASSSSSPSSSGPASAPSTCSFTYPIRAGNDPGVAPGGTGGGLLYGRESAPPPTAPFNLADINDVSPSGGFVAELLRPELDPVYIPPQQPQPPGGGLMGKFVLKASLSAPGSEYGSPSVISVSKGSPDGSHPVVVAPYNGGPPRTCPKIKQEAVSSCTHLGAGPPLSNGHRPAAHDFPLGRQLPSRTTPTLG...
null
null
canonical Wnt signaling pathway [GO:0060070]; cellular response to cycloheximide [GO:0071409]; cellular response to growth factor stimulus [GO:0071363]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to laminar fluid shear stress [GO:0071499]; cellular response to leukemia inhibitory factor [GO:...
chromatin [GO:0000785]; cytosol [GO:0005829]; euchromatin [GO:0000791]; microtubule cytoskeleton [GO:0015630]; nucleoplasm [GO:0005654]; transcription regulator complex [GO:0005667]
beta-catenin binding [GO:0008013]; chromatin DNA binding [GO:0031490]; 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]; histone deacetylase bi...
PF00096;
3.30.160.60;
Krueppel C2H2-type zinc-finger protein family
PTM: Ubiquitinated. 'Lys-48'-linked ubiquitinated and targeted for proteasomal degradation by the SCF(BTRC) E3 ubiquitin-protein ligase complex, thereby negatively regulating cell pluripotency maintenance and embryogenesis. {ECO:0000250|UniProtKB:Q60793}.; PTM: Polyglutamylated by TTLL1 and TTLL4 at Glu-411, which inhi...
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q60793}. Cytoplasm {ECO:0000250|UniProtKB:Q60793}.
null
null
null
null
null
FUNCTION: Transcription factor; can act both as activator and as repressor. Binds the 5'-CACCC-3' core sequence. Binds to the promoter region of its own gene and can activate its own transcription. Regulates the expression of key transcription factors during embryonic development. Plays an important role in maintaining...
Homo sapiens (Human)
O43482
MS18B_HUMAN
MAAQPLRHRSRCATPPRGDFCGGTERAIDQASFTTSMEWDTQVVKGSSPLGPAGLGAEEPAAGPQLPSWLQPERCAVFQCAQCHAVLADSVHLAWDLSRSLGAVVFSRVTNNVVLEAPFLVGIEGSLKGSTYNLLFCGSCGIPVGFHLYSTHAALAALRGHFCLSSDKMVCYLLKTKAIVNASEMDIQNVPLSEKIAELKEKIVLTHNRLKSLMKILSEVTPDQSKPEN
null
null
cell communication [GO:0007154]; cell division [GO:0051301]; CENP-A containing chromatin assembly [GO:0034080]; chromosome segregation [GO:0007059]
Cajal body [GO:0015030]; chromatin [GO:0000785]; chromocenter [GO:0010369]; chromosome, centromeric region [GO:0000775]; intracellular membrane-bounded organelle [GO:0043231]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
identical protein binding [GO:0042802]; metal ion binding [GO:0046872]
PF03226;
null
Mis18 family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17199038}. Chromosome {ECO:0000269|PubMed:17199038}. Chromosome, centromere {ECO:0000269|PubMed:17199038}. Note=Associated with centromeres in interphase cells, from late anaphase to the G1 phase. Not detected on centromeres during earlier phases of mitosis. Associated ...
null
null
null
null
null
FUNCTION: Required for recruitment of CENPA to centromeres and normal chromosome segregation during mitosis. {ECO:0000269|PubMed:17199038}.
Homo sapiens (Human)
O43488
ARK72_HUMAN
MLSAASRVVSRAAVHCALRSPPPEARALAMSRPPPPRVASVLGTMEMGRRMDAPASAAAVRAFLERGHTELDTAFMYSDGQSETILGGLGLGLGGGDCRVKIATKANPWDGKSLKPDSVRSQLETSLKRLQCPQVDLFYLHAPDHGTPVEETLHACQRLHQEGKFVELGLSNYASWEVAEICTLCKSNGWILPTVYQGMYNATTRQVETELFPCLRHFGLRFYAYNPLAGGLLTGKYKYEDKDGKQPVGRFFGNSWAETYRNRFWKEHHFEAIALVEKALQAAYGASAPSVTSAALRWMYHHSQLQGAHGDAVILGMSSL...
1.1.1.n11
null
carbohydrate metabolic process [GO:0005975]; cellular aldehyde metabolic process [GO:0006081]; daunorubicin metabolic process [GO:0044597]; doxorubicin metabolic process [GO:0044598]; lipid metabolic process [GO:0006629]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; mitochondrion [GO:0005739]
alditol:NADP+ 1-oxidoreductase activity [GO:0004032]; aldo-keto reductase (NADP) activity [GO:0004033]; electron transfer activity [GO:0009055]; phenanthrene-9,10-epoxide hydrolase activity [GO:0019119]
PF00248;
3.20.20.100;
Aldo/keto reductase family, Aldo/keto reductase 2 subfamily
null
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255}. Golgi apparatus {ECO:0000250|UniProtKB:Q8CG45}. Cytoplasm {ECO:0000269|PubMed:9576847}.
CATALYTIC ACTIVITY: Reaction=4-hydroxybutanoate + NADP(+) = H(+) + NADPH + succinate semialdehyde; Xref=Rhea:RHEA:26381, ChEBI:CHEBI:15378, ChEBI:CHEBI:16724, ChEBI:CHEBI:57706, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.n11; Evidence={ECO:0000269|PubMed:10510318};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=20 uM for succinic semialdehyde {ECO:0000269|PubMed:10510318}; KM=17 uM for 2-carboxybenzaldehyde {ECO:0000269|PubMed:10510318}; KM=8 uM for 9,10-phenanthrenequinone {ECO:0000269|PubMed:10510318}; KM=102 uM for 1,2-naphthoquinone {ECO:0000269|PubMed:10510318};
null
null
null
FUNCTION: Catalyzes the NADPH-dependent reduction of succinic semialdehyde to gamma-hydroxybutyrate. May have an important role in producing the neuromodulator gamma-hydroxybutyrate (GHB). Has broad substrate specificity. Has NADPH-dependent aldehyde reductase activity towards 2-carboxybenzaldehyde, 2-nitrobenzaldehyde...
Homo sapiens (Human)
O43490
PROM1_HUMAN
MALVLGSLLLLGLCGNSFSGGQPSSTDAPKAWNYELPATNYETQDSHKAGPIGILFELVHIFLYVVQPRDFPEDTLRKFLQKAYESKIDYDKPETVILGLKIVYYEAGIILCCVLGLLFIILMPLVGYFFCMCRCCNKCGGEMHQRQKENGPFLRKCFAISLLVICIIISIGIFYGFVANHQVRTRIKRSRKLADSNFKDLRTLLNETPEQIKYILAQYNTTKDKAFTDLNSINSVLGGGILDRLRPNIIPVLDEIKSMATAIKETKEALENMNSTLKSLHQQSTQLSSSLTSVKTSLRSSLNDPLCLVHPSSETCNSIR...
null
null
camera-type eye photoreceptor cell differentiation [GO:0060219]; glomerular parietal epithelial cell differentiation [GO:0072139]; photoreceptor cell maintenance [GO:0045494]; podocyte differentiation [GO:0072112]; positive regulation of nephron tubule epithelial cell differentiation [GO:2000768]; retina layer formatio...
apical plasma membrane [GO:0016324]; cell surface [GO:0009986]; cilium [GO:0005929]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; microvillus [GO:0005902]; microvillus membrane [GO:0031528]; p...
actinin binding [GO:0042805]; cadherin binding [GO:0045296]; cholesterol binding [GO:0015485]
PF05478;
null
Prominin family
PTM: Isoform 1 and isoform 2 are glycosylated. {ECO:0000269|PubMed:12042327}.; PTM: Acetylation at Lys-225, Lys-257 and Lys-264 by NAT8 and NAT8B may control PROM1 protein expression and its function in cell apoptosis. {ECO:0000269|PubMed:24556617}.
SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell projection, microvillus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell projection, cilium, photoreceptor outer segment {ECO:0000250}. Endoplasmic reticulum. Endoplasmic reticulum-Golgi inte...
null
null
null
null
null
FUNCTION: May play a role in cell differentiation, proliferation and apoptosis (PubMed:24556617). Binds cholesterol in cholesterol-containing plasma membrane microdomains and may play a role in the organization of the apical plasma membrane in epithelial cells. During early retinal development acts as a key regulator o...
Homo sapiens (Human)
O43491
E41L2_HUMAN
MTTEVGSVSEVKKDSSQLGTDATKEKPKEVAENQQNQSSDPEEEKGSQPPPAAESQSSLRRQKREKETSESRGISRFIPPWLKKQKSYTLVVAKDGGDKKEPTQAVVEEQVLDKEEPLPEEQRQAKGDAEEMAQKKQEIKVEVKEEKPSVSKEEKPSVSKVEMQPTELVSKEREEKVKETQEDKLEGGAAKRETKEVQTNELKAEKASQKVTKKTKTVQCKVTLLDGTEYSCDLEKHAKGQVLFDKVCEHLNLLEKDYFGLLFQESPEQKNWLDPAKEIKRQLRNLPWLFTFNVKFYPPDPSQLTEDITRYFLCLQLRQD...
null
null
actomyosin structure organization [GO:0031032]; cell cycle [GO:0007049]; cell division [GO:0051301]; cortical actin cytoskeleton organization [GO:0030866]; positive regulation of protein localization to cell cortex [GO:1904778]
cell cortex [GO:0005938]; cell junction [GO:0030054]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; spectrin [GO:0008091]
actin binding [GO:0003779]; PH domain binding [GO:0042731]; spectrin binding [GO:0030507]; structural molecule activity [GO:0005198]
PF05902;PF08736;PF09380;PF00373;PF09379;PF04382;
1.20.80.10;2.30.29.30;
null
null
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000269|PubMed:23870127}. Cell membrane {ECO:0000269|PubMed:22361696}.
null
null
null
null
null
FUNCTION: Required for dynein-dynactin complex and NUMA1 recruitment at the mitotic cell cortex during anaphase (PubMed:23870127). {ECO:0000269|PubMed:23870127}.
Homo sapiens (Human)
O43493
TGON2_HUMAN
MRFVVALVLLNVAAAGAVPLLATESVKQEEAGVRPSAGNVSTHPSLSQRPGGSTKSHPEPQTPKDSPSKSSAEAQTPEDTPNKSGAEAKTQKDSSNKSGAEAKTQKGSTSKSGSEAQTTKDSTSKSHPELQTPKDSTGKSGAEAQTPEDSPNRSGAEAKTQKDSPSKSGSEAQTTKDVPNKSGADGQTPKDGSSKSGAEDQTPKDVPNKSGAEKQTPKDGSNKSGAEEQGPIDGPSKSGAEEQTSKDSPNKVVPEQPSRKDHSKPISNPSDNKELPKADTNQLADKGKLSPHAFKTESGEETDLISPPQEEVKSSEPTED...
null
null
null
clathrin-coated endocytic vesicle membrane [GO:0030669]; endoplasmic reticulum lumen [GO:0005788]; endosome [GO:0005768]; Golgi apparatus [GO:0005794]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; trans-Golgi network [GO:0005802]; trans-Golgi network transport vesicle [GO:0030140]; transport vesicle [GO:0030...
null
PF17818;
null
null
null
SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Golgi apparatus, trans-Golgi network membrane; Single-pass type I membrane protein. Note=Primarily in trans-Golgi network. Cycles between the trans-Golgi network and the cell surface returning via endosomes.
null
null
null
null
null
FUNCTION: May be involved in regulating membrane traffic to and from trans-Golgi network.
Homo sapiens (Human)
O43497
CAC1G_HUMAN
MDEEEDGAGAEESGQPRSFMRLNDLSGAGGRPGPGSAEKDPGSADSEAEGLPYPALAPVVFFYLSQDSRPRSWCLRTVCNPWFERISMLVILLNCVTLGMFRPCEDIACDSQRCRILQAFDDFIFAFFAVEMVVKMVALGIFGKKCYLGDTWNRLDFFIVIAGMLEYSLDLQNVSFSAVRTVRVLRPLRAINRVPSMRILVTLLLDTLPMLGNVLLLCFFVFFIFGIVGVQLWAGLLRNRCFLPENFSLPLSVDLERYYQTENEDESPFICSQPRENGMRSCRSVPTLRGDGGGGPPCGLDYEAYNSSSNTTCVNWNQYY...
null
null
AV node cell action potential [GO:0086016]; AV node cell to bundle of His cell signaling [GO:0086027]; calcium ion import [GO:0070509]; calcium ion import across plasma membrane [GO:0098703]; calcium ion transmembrane transport [GO:0070588]; cardiac muscle cell action potential involved in contraction [GO:0086002]; che...
cytoplasm [GO:0005737]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; synapse [GO:0045202]; 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]; scaffold protein binding [GO:0097110]; voltage-gated calcium channel activity involved in AV node cell action potential [GO:0086056]; voltage-gated calcium channel activity involved SA node cell action pot...
PF00520;
1.10.287.70;1.20.120.350;
Calcium channel alpha-1 subunit (TC 1.A.1.11) family, CACNA1G 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:26715324}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:26715324}.
null
null
null
null
null
FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha...
Homo sapiens (Human)
O43502
RA51C_HUMAN
MRGKTFRFEMQRDLVSFPLSPAVRVKLVSAGFQTAEELLEVKPSELSKEVGISKAEALETLQIIRRECLTNKPRYAGTSESHKKCTALELLEQEHTQGFIITFCSALDDILGGGVPLMKTTEICGAPGVGKTQLCMQLAVDVQIPECFGGVAGEAVFIDTEGSFMVDRVVDLATACIQHLQLIAEKHKGEEHRKALEDFTLDNILSHIYYFRCRDYTELLAQVYLLPDFLSEHSKVRLVIVDGIAFPFRHDLDDLSLRTRLLNGLAQQMISLANNHRLAVILTNQMTTKIDRNQALLVPALGESWGHAATIRLIFHWDRK...
null
null
DNA recombination [GO:0006310]; DNA repair [GO:0006281]; double-strand break repair via homologous recombination [GO:0000724]; female meiosis sister chromatid cohesion [GO:0007066]; male meiosis I [GO:0007141]; meiotic DNA recombinase assembly [GO:0000707]; positive regulation of G2/M transition of mitotic cell cycle [...
cell junction [GO:0030054]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; Rad51B-Rad51C-Rad51D-XRCC2 complex [GO:0033063]; Rad51C-XRCC3 complex...
ATP binding [GO:0005524]; ATP-dependent DNA damage sensor activity [GO:0140664]; crossover junction DNA endonuclease activity [GO:0008821]; DNA binding [GO:0003677]; four-way junction DNA binding [GO:0000400]
PF08423;
1.10.150.20;3.40.50.300;
RecA family, RAD51 subfamily
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12966089, ECO:0000269|PubMed:16215984}. Cytoplasm {ECO:0000269|PubMed:16215984}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:16215984}. Mitochondrion {ECO:0000269|PubMed:20413593}. Note=DNA damage induces an increase in nuclear levels. Accumulates in DNA damage in...
null
null
null
null
null
FUNCTION: Essential for the homologous recombination (HR) pathway of DNA repair. Involved in the homologous recombination repair (HRR) pathway of double-stranded DNA breaks arising during DNA replication or induced by DNA-damaging agents. Part of the RAD51 paralog protein complexes BCDX2 and CX3 which act at different ...
Homo sapiens (Human)
O43504
LTOR5_HUMAN
MEATLEQHLEDTMKNPSIVGVLCTDSQGLNLGCRGTLSDEHAGVISVLAQQAAKLTSDPTDIPVVCLESDNGNIMIQKHDGITVAVHKMAS
null
null
cellular response to amino acid stimulus [GO:0071230]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043154]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of gene expression [GO:0010628]; positive regulation of interleu...
cytosol [GO:0005829]; FNIP-folliculin RagC/D GAP [GO:1990877]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; protein-containing complex [GO:0032991]; Ragulator complex [GO:0071986]
guanyl-nucleotide exchange factor activity [GO:0005085]
PF16672;
3.30.450.30;
LAMTOR5 family
null
SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:22980980}. Cytoplasm, cytosol {ECO:0000269|PubMed:12773388}.
null
null
null
null
null
FUNCTION: As part of the Ragulator complex it is involved in amino acid sensing and activation of mTORC1, a signaling complex promoting cell growth in response to growth factors, energy levels, and amino acids (PubMed:22980980, PubMed:29158492, PubMed:30181260). Activated by amino acids through a mechanism involving th...
Homo sapiens (Human)
O43505
B4GA1_HUMAN
MQMSYAIRCAFYQLLLAALMLVAMLQLLYLSLLSGLHGQEEQDQYFEFFPPSPRSVDQVKAQLRTALASGGVLDASGDYRVYRGLLKTTMDPNDVILATHASVDNLLHLSGLLERWEGPLSVSVFAATKEEAQLATVLAYALSSHCPDMRARVAMHLVCPSRYEAAVPDPREPGEFALLRSCQEVFDKLARVAQPGINYALGTNVSYPNNLLRNLAREGANYALVIDVDMVPSEGLWRGLREMLDQSNQWGGTALVVPAFEIRRARRMPMNKNELVQLYQVGEVRPFYYGLCTPCQAPTNYSRWVNLPEESLLRPAYVVP...
2.4.1.-
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:25279699};
axon guidance [GO:0007411]; keratan sulfate biosynthetic process [GO:0018146]; protein O-linked mannosylation [GO:0035269]
extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]
glucuronosyltransferase activity [GO:0015020]; metal ion binding [GO:0046872]; N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase activity [GO:0008532]
PF13896;
null
Glycosyltransferase 49 family
null
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:19587235, ECO:0000269|PubMed:23359570, ECO:0000269|PubMed:25279699}; Single-pass type II membrane protein {ECO:0000269|PubMed:23359570}. Note=Localizes near the trans-Golgi apparatus. {ECO:0000269|PubMed:25279699}.
CATALYTIC ACTIVITY: Reaction=3-O-[beta-D-Xyl-(1->4)-Rib-ol-P-Rib-ol-P-3-beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-(O-6-P-alpha-D-Man)]-Thr-[protein] + UDP-alpha-D-glucuronate = 3-O-[beta-D-GlcA-(1->3)-beta-D-Xyl-(1->4)-Rib-ol-P-Rib-ol-P-3-beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-(O-6-P-alpha-D-Man)]-Thr-[protein] + H(...
null
PATHWAY: Protein modification; protein glycosylation. {ECO:0000269|PubMed:25279697, ECO:0000269|PubMed:25279699, ECO:0000269|PubMed:9405606}.
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. {ECO:0000269|PubMed:25279699};
null
FUNCTION: Beta-1,4-glucuronyltransferase involved in O-mannosylation of alpha-dystroglycan (DAG1) (PubMed:19587235, PubMed:23359570, PubMed:25279697, PubMed:25279699). Transfers a glucuronic acid (GlcA) residue onto a xylose (Xyl) acceptor to produce the glucuronyl-beta-1,4-xylose-beta disaccharide primer, which is fur...
Homo sapiens (Human)
O43506
ADA20_HUMAN
MAVGEPLVHIRVTLLLLWFGMFLSISGHSQARPSQYFTSPEVVIPLKVISRGRGAKAPGWLSYSLRFGGQRYIVHMRVNKLLFAAHLPVFTYTEQHALLQDQPFIQDDCYYHGYVEGVPESLVALSTCSGGFLGMLQINDLVYEIKPISVSATFEHLVYKIDSDDTQFPPMRCGLTEEKIAHQMELQLSYNFTLKQSSFVGWWTHQRFVELVVVVDNIRYLFSQSNATTVQHEVFNVVNIVDSFYHPLEVDVILTGIDIWTASNPLPTSGDLDNVLEDFSIWKNYNLNNRLQHDVAHLFIKDTQGMKLGVAYVKGICQNP...
3.4.24.-
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305}; Note=Binds 1 zinc ion per subunit. {ECO:0000305};
male gonad development [GO:0008584]; proteolysis [GO:0006508]; single fertilization [GO:0007338]
external side of plasma membrane [GO:0009897]; plasma membrane [GO:0005886]; sperm head plasma membrane [GO:1990913]
metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; metallopeptidase activity [GO:0008237]
PF08516;PF00200;PF01562;PF01421;
3.40.390.10;4.10.70.10;
null
PTM: Has no obvious cleavage site for furin endopeptidase, suggesting that the proteolytic processing is regulated.
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
null
null
null
null
null
FUNCTION: May be involved in sperm maturation and/or fertilization.
Homo sapiens (Human)
O43508
TNF12_HUMAN
MAARRSQRRRGRRGEPGTALLVPLALGLGLALACLGLLLAVVSLGSRASLSAQEPAQEELVAEEDQDPSELNPQTEESQDPAPFLNRLVRPRRSAPKGRKTRARRAIAAHYEVHPRPGQDGAQAGVDGTVSGWEEARINSSSPLRYNRQIGEFIVTRAGLYYLYCQVHFDEGKAVYLKLDLLVDGVLALRCLEEFSATAASSLGPQLRLCQVSGLLALRPGSSLRIRTLPWAHLKAAPFLTYFGLFQVH
null
null
angiogenesis [GO:0001525]; apoptotic process [GO:0006915]; cell differentiation [GO:0030154]; endothelial cell migration [GO:0043542]; extrinsic apoptotic signaling pathway [GO:0097191]; immune response [GO:0006955]; positive regulation of angiogenesis [GO:0045766]; positive regulation of endothelial cell proliferation...
extracellular region [GO:0005576]; extracellular space [GO:0005615]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]
cytokine activity [GO:0005125]; receptor ligand activity [GO:0048018]; signaling receptor binding [GO:0005102]; tumor necrosis factor receptor binding [GO:0005164]
PF00229;
2.60.120.40;
Tumor necrosis factor family
PTM: The soluble form derives from the membrane form by proteolytic processing.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12411489}; Single-pass type II membrane protein {ECO:0000269|PubMed:12411489}.; SUBCELLULAR LOCATION: [Tumor necrosis factor ligand superfamily member 12, secreted form]: Secreted.; SUBCELLULAR LOCATION: [Isoform TWE-PRIL]: Cell membrane; Single-pass membrane prot...
null
null
null
null
null
FUNCTION: Binds to FN14 and possibly also to TNRFSF12/APO3. Weak inducer of apoptosis in some cell types. Mediates NF-kappa-B activation. Promotes angiogenesis and the proliferation of endothelial cells. Also involved in induction of inflammatory cytokines. Promotes IL8 secretion. {ECO:0000269|PubMed:10085077, ECO:0000...
Homo sapiens (Human)
O43511
S26A4_HUMAN
MAAPGGRSEPPQLPEYSCSYMVSRPVYSELAFQQQHERRLQERKTLRESLAKCCSCSRKRAFGVLKTLVPILEWLPKYRVKEWLLSDVISGVSTGLVATLQGMAYALLAAVPVGYGLYSAFFPILTYFIFGTSRHISVGPFPVVSLMVGSVVLSMAPDEHFLVSSSNGTVLNTTMIDTAARDTARVLIASALTLLVGIIQLIFGGLQIGFIVRYLADPLVGGFTTAAAFQVLVSQLKIVLNVSTKNYNGVLSIIYTLVEIFQNIGDTNLADFTAGLLTIVVCMAVKELNDRFRHKIPVPIPIEVIVTIIATAISYGANLE...
null
null
inorganic anion transport [GO:0015698]; iodide transport [GO:0015705]; monoatomic ion transport [GO:0006811]; regulation of pH [GO:0006885]; regulation of protein localization [GO:0032880]; sensory perception of sound [GO:0007605]; sulfate transport [GO:0008272]
apical plasma membrane [GO:0016324]; brush border membrane [GO:0031526]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; plasma membrane [GO:0005886]
bicarbonate transmembrane transporter activity [GO:0015106]; chloride transmembrane transporter activity [GO:0015108]; chloride:bicarbonate antiporter activity [GO:0140900]; iodide transmembrane transporter activity [GO:0015111]; oxalate transmembrane transporter activity [GO:0019531]; secondary active sulfate transmem...
PF01740;PF00916;
3.30.750.24;
SLC26A/SulP transporter (TC 2.A.53) family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11932316, ECO:0000269|PubMed:24051746}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000269|PubMed:11274445, ECO:0000269|PubMed:35601831}; Multi-pass membrane protein {ECO:0000255}.
CATALYTIC ACTIVITY: Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823, ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:10192399, ECO:0000269|PubMed:24051746}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29825; Evidence={ECO:0000305|PubMed:10192399}; CATALYTIC ACTIVITY: Reaction=iodide(out) = iodide(i...
null
null
null
null
FUNCTION: Sodium-independent transporter of chloride and iodide (PubMed:10192399, PubMed:11932316, PubMed:12107249, PubMed:16684826, PubMed:24051746). Mediates electroneutral chloride-bicarbonate, chloride-iodide and chloride-formate exchange with 1:1 stoichiometry (PubMed:10644529, PubMed:15155570, PubMed:24051746, Pu...
Homo sapiens (Human)
O43513
MED7_HUMAN
MGEPQQVSALPPPPMQYIKEYTDENIQEGLAPKPPPPIKDSYMMFGNQFQCDDLIIRPLESQGIERLHPMQFDHKKELRKLNMSILINFLDLLDILIRSPGSIKREEKLEDLKLLFVHVHHLINEYRPHQARETLRVMMEVQKRQRLETAERFQKHLERVIEMIQNCLASLPDDLPHSEAGMRVKTEPMDADDSNNCTGQNEHQRENSGHRRDQIIEKDAALCVLIDEMNERP
null
null
positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; positive regulation of transcription initiation by RNA polymerase II [GO:0060261]; protein ubiquitination [GO:0016567]; regulation of transcription by RNA polymerase II [GO:0006357]; RNA polymerase II preinitiation complex assembly [GO:0...
core mediator complex [GO:0070847]; mediator complex [GO:0016592]; nuclear body [GO:0016604]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667]; ubiquitin ligase complex [GO:0000151]
transcription coactivator activity [GO:0003713]; ubiquitin protein ligase activity [GO:0061630]
PF05983;
6.10.140.200;
Mediator complex subunit 7 family
PTM: Constitutively sumoylated. {ECO:0000269|PubMed:17709345}.
SUBCELLULAR LOCATION: Nucleus.
null
null
null
null
null
FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to...
Homo sapiens (Human)
O43516
WIPF1_HUMAN
MPVPPPPAPPPPPTFALANTEKPTLNKTEQAGRNALLSDISKGKKLKKTVTNDRSAPILDKPKGAGAGGGGGGFGGGGGFGGGGGGGGGGSFGGGGPPGLGGLFQAGMPKLRSTANRDNDSGGSRPPLLPPGGRSTSAKPFSPPSGPGRFPVPSPGHRSGPPEPQRNRMPPPRPDVGSKPDSIPPPVPSTPRPIQSSPHNRGSPPVPGGPRQPSPGPTPPPFPGNRGTALGGGSIRQSPLSSSSPFSNRPPLPPTPSRALDDKPPPPPPPVGNRPSIHREAVPPPPPQNNKPPVPSTPRPSASSQAPPPPPPPSRPGPPP...
null
null
actin filament-based movement [GO:0030048]; actin polymerization or depolymerization [GO:0008154]; protein-containing complex assembly [GO:0065003]; response to other organism [GO:0051707]
actin cytoskeleton [GO:0015629]; actin filament [GO:0005884]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; ruffle [GO:0001726]
actin binding [GO:0003779]; profilin binding [GO:0005522]; protein folding chaperone [GO:0044183]; SH3 domain binding [GO:0017124]
PF02205;
2.30.29.30;
Verprolin family
null
SUBCELLULAR LOCATION: Cytoplasmic vesicle {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell projection, ruffle {ECO:0000269|PubMed:19910490}. Note=Vesicle surfaces and along actin tails. Colocalizes with actin stress fibers. When coexpressed with WASL, no longer associated with actin filaments but accumulated ...
null
null
null
null
null
FUNCTION: Plays a role in the reorganization of the actin cytoskeleton. Contributes with NCK1 and GRB2 in the recruitment and activation of WASL. May participate in regulating the subcellular localization of WASL, resulting in the disassembly of stress fibers in favor of filopodia formation. Plays a role in the formati...
Homo sapiens (Human)
O43520
AT8B1_HUMAN
MSTERDSETTFDEDSQPNDEVVPYSDDETEDELDDQGSAVEPEQNRVNREAEENREPFRKECTWQVKANDRKYHEQPHFMNTKFLCIKESKYANNAIKTYKYNAFTFIPMNLFEQFKRAANLYFLALLILQAVPQISTLAWYTTLVPLLVVLGVTAIKDLVDDVARHKMDKEINNRTCEVIKDGRFKVAKWKEIQVGDVIRLKKNDFVPADILLLSSSEPNSLCYVETAELDGETNLKFKMSLEITDQYLQREDTLATFDGFIECEEPNNRLDKFTGTLFWRNTSFPLDADKILLRGCVIRNTDFCHGLVIFAGADTKIM...
7.6.2.1
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9Y2Q0};
apical protein localization [GO:0045176]; bile acid and bile salt transport [GO:0015721]; bile acid metabolic process [GO:0008206]; Golgi organization [GO:0007030]; inner ear receptor cell development [GO:0060119]; monoatomic ion transmembrane transport [GO:0034220]; negative regulation of DNA-templated transcription [...
apical plasma membrane [GO:0016324]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; nuclear body [GO:0016604]; nucleoplasm [GO:0005654]; phospholipid-translocating ATPase complex [GO:1990531]; plasma membrane [GO:0005886]; stereocilium [GO:0032420]; trans-Golgi network [GO:00058...
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled intramembrane lipid transporter activity [GO:0140326]; cardiolipin binding [GO:1901612]; magnesium ion binding [GO:0000287]; phosphatidylcholine flippase activity [GO:0140345]; phosphatidylcholine floppase activity [GO:0090554]; phosphatidyl...
PF13246;PF00122;PF16212;PF16209;
3.40.1110.10;2.70.150.10;3.40.50.1000;
Cation transport ATPase (P-type) (TC 3.A.3) family, Type IV subfamily
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17948906, ECO:0000269|PubMed:20947505, ECO:0000269|PubMed:20961850, ECO:0000269|PubMed:21914794, ECO:0000269|PubMed:25315773}; Multi-pass membrane protein. Apical cell membrane {ECO:0000269|PubMed:20512993}. Cell projection, stereocilium {ECO:0000250|UniProtKB:Q14...
CATALYTIC ACTIVITY: Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2.; EC=7.6.2.1; Evidence={ECO:0000269|PubMed:17948906, ECO:0000269|PubMed:25315773}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phosphocholine(in) + AD...
null
null
null
null
FUNCTION: Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of phospholipids, in particular phosphatidylcholines (PC), from the outer to the inner leaflet of the plasma membrane (PubMed:17948906, PubMed:25315773). May participate in the establishment of t...
Homo sapiens (Human)
O43521
B2L11_HUMAN
MAKQPSDVSSECDREGRQLQPAERPPQLRPGAPTSLQTEPQGNPEGNHGGEGDSCPHGSPQGPLAPPASPGPFATRSPLFIFMRRSSLLSRSSSGYFSFDTDRSPAPMSCDKSTQTPSPPCQAFNHYLSAMASMRQAEPADMRPEIWIAQELRRIGDEFNAYYARRVFLNNYQAAEDHPRMVILRLLRYIVRLVWRMH
null
null
activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; apoptotic process [GO:0006915]; apoptotic process involved in embryonic digit morphogenesis [GO:1902263]; B cell homeostasis [GO:0001782]; cell-matrix adhesion [GO:0007160]; cellular response to glucocorticoid stimulus [GO:00...
Bcl-2 family protein complex [GO:0097136]; BIM-BCL-2 complex [GO:0097141]; BIM-BCL-xl complex [GO:0097140]; cytosol [GO:0005829]; endomembrane system [GO:0012505]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]
microtubule binding [GO:0008017]; protein kinase binding [GO:0019901]
PF08945;PF06773;
null
Bcl-2 family
PTM: Phosphorylation at Ser-69 by MAPK1/MAPK3 leads to interaction with TRIM2 and polyubiquitination, followed by proteasomal degradation (PubMed:15486195, PubMed:21478148). Deubiquitination catalyzed by USP27X stabilizes the protein (By similarity). {ECO:0000250|UniProtKB:O54918, ECO:0000269|PubMed:15486195, ECO:00002...
SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Associated with intracytoplasmic membranes. {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform BimEL]: Mitochondrion. Note=Translocates from microtubules to mitochondria on loss of cell adherence.; SUBCELLULAR LOCATION:...
null
null
null
null
null
FUNCTION: Induces apoptosis and anoikis. Isoform BimL is more potent than isoform BimEL. Isoform Bim-alpha1, isoform Bim-alpha2 and isoform Bim-alpha3 induce apoptosis, although less potent than isoform BimEL, isoform BimL and isoform BimS. Isoform Bim-gamma induces apoptosis. Isoform Bim-alpha3 induces apoptosis possi...
Homo sapiens (Human)
O43524
FOXO3_HUMAN
MAEAPASPAPLSPLEVELDPEFEPQSRPRSCTWPLQRPELQASPAKPSGETAADSMIPEEEDDEDDEDGGGRAGSAMAIGGGGGSGTLGSGLLLEDSARVLAPGGQDPGSGPATAAGGLSGGTQALLQPQQPLPPPQPGAAGGSGQPRKCSSRRNAWGNLSYADLITRAIESSPDKRLTLSQIYEWMVRCVPYFKDKGDSNSSAGWKNSIRHNLSLHSRFMRVQNEGTGKSSWWIINPDGGKSGKAPRRRAVSMDNSNKYTKSRGRAAKKKAALQTAPESADDSPSQLSKWPGSPTSRSSDELDAWTDFRSRTNSNASTV...
null
null
antral ovarian follicle growth [GO:0001547]; brain morphogenesis [GO:0048854]; canonical Wnt signaling pathway [GO:0060070]; cellular response to amyloid-beta [GO:1904646]; cellular response to corticosterone stimulus [GO:0071386]; cellular response to glucose starvation [GO:0042149]; cellular response to glucose stimu...
chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrial matrix [GO:0005759]; mitochondrial outer membrane [GO:0005741]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; RNA polymerase II transcription repressor complex [GO:0090571]
beta-catenin binding [GO:0008013]; chromatin DNA binding [GO:0031490]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:000098...
PF00250;PF16676;PF16675;
6.10.250.1690;1.10.10.10;
null
PTM: In the presence of survival factors such as IGF-1, phosphorylated on Thr-32 and Ser-253 by AKT1/PKB (PubMed:10102273). This phosphorylated form then interacts with 14-3-3 proteins and is retained in the cytoplasm (PubMed:10102273). Survival factor withdrawal induces dephosphorylation and promotes translocation to ...
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:10102273, ECO:0000269|PubMed:15084260, ECO:0000269|PubMed:16751106, ECO:0000269|PubMed:17711846, ECO:0000269|PubMed:21329882, ECO:0000269|PubMed:22313691, ECO:0000269|PubMed:22761832, ECO:0000269|PubMed:23283301}. Nucleus {ECO:0000269|PubMed:10102273, ECO:000...
null
null
null
null
null
FUNCTION: Transcriptional activator that recognizes and binds to the DNA sequence 5'-[AG]TAAA[TC]A-3' and regulates different processes, such as apoptosis and autophagy (PubMed:10102273, PubMed:16751106, PubMed:21329882, PubMed:30513302). Acts as a positive regulator of autophagy in skeletal muscle: in starved cells, e...
Homo sapiens (Human)
O43525
KCNQ3_HUMAN
MGLKARRAAGAAGGGGDGGGGGGGAANPAGGDAAAAGDEERKVGLAPGDVEQVTLALGAGADKDGTLLLEGGGRDEGQRRTPQGIGLLAKTPLSRPVKRNNAKYRRIQTLIYDALERPRGWALLYHALVFLIVLGCLILAVLTTFKEYETVSGDWLLLLETFAIFIFGAEFALRIWAAGCCCRYKGWRGRLKFARKPLCMLDIFVLIASVPVVAVGNQGNVLATSLRSLRFLQILRMLRMDRRGGTWKLLGSAICAHSKELITAWYIGFLTLILSSFLVYLVEKDVPEVDAQGEEMKEEFETYADALWWGLITLATIGYG...
null
null
action potential initiation [GO:0099610]; apoptosome assembly [GO:0097314]; cellular response to calcium ion [GO:0071277]; cellular response to xenobiotic stimulus [GO:0071466]; chemical synaptic transmission [GO:0007268]; endocytosis [GO:0006897]; excitatory chemical synaptic transmission [GO:0098976]; exocytosis [GO:...
axon initial segment [GO:0043194]; cell surface [GO:0009986]; mitochondrion [GO:0005739]; node of Ranvier [GO:0033268]; plasma membrane [GO:0005886]; synapse [GO:0045202]; voltage-gated potassium channel complex [GO:0008076]
calmodulin binding [GO:0005516]; voltage-gated potassium channel activity [GO:0005249]
PF00520;PF03520;PF11956;
1.10.287.70;6.10.140.1910;
Potassium channel family, KQT (TC 1.A.1.15) subfamily, Kv7.3/KCNQ3 sub-subfamily
PTM: KCNQ2/KCNQ3 are ubiquitinated by NEDD4L. Ubiquitination leads to protein degradation (Probable). Degradation induced by NEDD4L is inhibited by USP36 (PubMed:27445338). {ECO:0000269|PubMed:27445338, ECO:0000305|PubMed:27445338}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10788442}; Multi-pass membrane protein {ECO:0000255}.
null
null
null
null
null
FUNCTION: Associates with KCNQ2 or KCNQ5 to form a potassium channel with essentially identical properties to the channel underlying the native M-current, a slowly activating and deactivating potassium conductance which plays a critical role in determining the subthreshold electrical excitability of neurons as well as ...
Homo sapiens (Human)
O43526
KCNQ2_HUMAN
MVQKSRNGGVYPGPSGEKKLKVGFVGLDPGAPDSTRDGALLIAGSEAPKRGSILSKPRAGGAGAGKPPKRNAFYRKLQNFLYNVLERPRGWAFIYHAYVFLLVFSCLVLSVFSTIKEYEKSSEGALYILEIVTIVVFGVEYFVRIWAAGCCCRYRGWRGRLKFARKPFCVIDIMVLIASIAVLAAGSQGNVFATSALRSLRFLQILRMIRMDRRGGTWKLLGSVVYAHSKELVTAWYIGFLCLILASFLVYLAEKGENDHFDTYADALWWGLITLTTIGYGDKYPQTWNGRLLAATFTLIGVSFFALPAGILGSGFALKV...
null
null
chemical synaptic transmission [GO:0007268]; nervous system development [GO:0007399]; potassium ion transmembrane transport [GO:0071805]
axon initial segment [GO:0043194]; node of Ranvier [GO:0033268]; plasma membrane [GO:0005886]; synapse [GO:0045202]; voltage-gated potassium channel complex [GO:0008076]
ankyrin binding [GO:0030506]; calmodulin binding [GO:0005516]; voltage-gated potassium channel activity [GO:0005249]
PF00520;PF16642;PF03520;PF11956;
1.10.287.70;6.10.140.1910;
Potassium channel family, KQT (TC 1.A.1.15) subfamily, Kv7.2/KCNQ2 sub-subfamily
PTM: KCNQ2/KCNQ3 heteromeric current can be increased by intracellular cyclic AMP, an effect that depends on phosphorylation of Ser-52 in the N-terminal region. {ECO:0000269|PubMed:16319223, ECO:0000269|PubMed:9872318}.; PTM: KCNQ2/KCNQ3 are ubiquitinated by NEDD4L. Ubiquitination leads to protein degradation (Probable...
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10788442, ECO:0000269|PubMed:9836639}; Multi-pass membrane protein {ECO:0000255}.
null
null
null
null
null
FUNCTION: Associates with KCNQ3 to form a potassium channel with essentially identical properties to the channel underlying the native M-current, a slowly activating and deactivating potassium conductance which plays a critical role in determining the subthreshold electrical excitability of neurons as well as the respo...
Homo sapiens (Human)
O43529
CHSTA_HUMAN
MHHQWLLLAACFWVIFMFMVASKFITLTFKDPDVYSAKQEFLFLTTMPEVRKLPEEKHIPEELKPTGKELPDSQLVQPLVYMERLELIRNVCRDDALKNLSHTPVSKFVLDRIFVCDKHKILFCQTPKVGNTQWKKVLIVLNGAFSSIEEIPENVVHDHEKNGLPRLSSFSDAEIQKRLKTYFKFFIVRDPFERLISAFKDKFVHNPRFEPWYRHEIAPGIIRKYRRNRTETRGIQFEDFVRYLGDPNHRWLDLQFGDHIIHWVTYVELCAPCEIMYSVIGHHETLEDDAPYILKEAGIDHLVSYPTIPPGITVYNRTKV...
2.8.2.-
null
androgen metabolic process [GO:0008209]; carbohydrate biosynthetic process [GO:0016051]; cell adhesion [GO:0007155]; estrogen metabolic process [GO:0008210]; learning [GO:0007612]; long-term memory [GO:0007616]; proteoglycan biosynthetic process [GO:0030166]
Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; membrane [GO:0016020]
HNK-1 sulfotransferase activity [GO:0016232]; sulfotransferase activity [GO:0008146]
PF03567;
null
Sulfotransferase 2 family
null
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:O54702}; Single-pass type II membrane protein {ECO:0000255}.
CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + 3-O-{beta-D-GlcA-(1->[3)-alpha-D-Xyl-(1->3)-beta-D-GlcA-(1->](n)-4)-beta-D-Xyl-(1->4)-Rib-ol-P-Rib-ol-P-3-beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-O-6-P-alpha-D-Man}-L-Thr-[protein] = 3-O-{O-3-S-beta-D-GlcA-(1->[3)-alpha-D-Xyl-(1->3)-beta-D-GlcA-(1->](n)-4)-bet...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.21 mM for dehydroepiandrosterone 3-O-(beta-D-glucuronate) (GlcUA-3-DHEA) {ECO:0000269|PubMed:23269668}; KM=0.321 mM for 17beta-estradiol 3-O-(beta-D-glucuronate) (GlcUA-3-E2) {ECO:0000269|PubMed:23269668}; KM=1.518 mM for N-acetyllactosamine 3-O-(beta-D-glucurona...
PATHWAY: Steroid metabolism. {ECO:0000269|PubMed:23269668}.; PATHWAY: Protein modification; carbohydrate sulfation. {ECO:0000269|PubMed:32149355}.
null
null
FUNCTION: Catalyzes the transfer of sulfate from 3'-phosphoadenylyl sulfate (PAPS) to position 3 of terminal glucuronic acid of both protein- and lipid-linked oligosaccharides. Participates in biosynthesis of HNK-1 carbohydrate structure 3-O-sulfo-beta-D-GlcA-(1->3)-beta-D-Gal-(1->4)-D-GlcNAc-R, a sulfated glucuronyl-l...
Homo sapiens (Human)
O43541
SMAD6_HUMAN
MFRSKRSGLVRRLWRSRVVPDREEGGSGGGGGGDEDGSLGSRAEPAPRAREGGGCGRSEVRPVAPRRPRDAVGQRGAQGAGRRRRAGGPPRPMSEPGAGAGSSLLDVAEPGGPGWLPESDCETVTCCLFSERDAAGAPRDASDPLAGAALEPAGGGRSREARSRLLLLEQELKTVTYSLLKRLKERSLDTLLEAVESRGGVPGGCVLVPRADLRLGGQPAPPQLLLGRLFRWPDLQHAVELKPLCGCHSFAAAADGPTVCCNPYHFSRLCGPESPPPPYSRLSPRDEYKPLDLSDSTLSYTETEATNSLITAPGEFSDAS...
null
null
anatomical structure morphogenesis [GO:0009653]; aorta development [GO:0035904]; aortic valve morphogenesis [GO:0003180]; BMP signaling pathway [GO:0030509]; cell differentiation [GO:0030154]; cell-substrate adhesion [GO:0031589]; coronary vasculature development [GO:0060976]; fat cell differentiation [GO:0045444]; imm...
chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; heteromeric SMAD protein complex [GO:0071144]; nuclear body [GO:0016604]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]
chromatin binding [GO:0003682]; co-SMAD binding [GO:0070410]; I-SMAD binding [GO:0070411]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; protein sequestering activity [GO:0140311]; R-SMAD binding [GO:0070412]; transcription cis-regulatory region binding [GO:0000976]; transcription regulator in...
PF03165;PF03166;
2.60.200.10;3.90.520.10;
Dwarfin/SMAD family
PTM: Phosphorylated by BMP type 1 receptor kinase and by PRKX. {ECO:0000269|PubMed:16491121}.; PTM: Monoubiquitinated at Lys-173 by the E2/E3 hybrid ubiquitin-protein ligase UBE2O, leading to reduced binding affinity for the activated BMP type I receptor ACVR1/ALK2, thereby enhancing BMP7 and regulating adipocyte diffe...
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16491121}.
null
null
null
null
null
FUNCTION: Transforming growth factor-beta superfamily receptors signaling occurs through the Smad family of intracellular mediators. SMAD6 is an inhibitory Smad (i-Smad) that negatively regulates signaling downstream of type I transforming growth factor-beta (PubMed:10647776, PubMed:10708948, PubMed:10708949, PubMed:16...
Homo sapiens (Human)