TAB1_HUMAN
ID TAB1_HUMAN Reviewed; 504 AA.
AC Q15750; Q2PP09; Q8IZW2;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=TGF-beta-activated kinase 1 and MAP3K7-binding protein 1;
DE AltName: Full=Mitogen-activated protein kinase kinase kinase 7-interacting protein 1;
DE AltName: Full=TGF-beta-activated kinase 1-binding protein 1;
DE Short=TAK1-binding protein 1;
GN Name=TAB1; Synonyms=MAP3K7IP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH MAP3K7.
RC TISSUE=Brain;
RX PubMed=8638164; DOI=10.1126/science.272.5265.1179;
RA Shibuya H., Yamaguchi K., Shirakabe K., Tonegawa A., Gotoh Y., Ueno N.,
RA Irie K., Nishida E., Matsumoto K.;
RT "TAB1: an activator of the TAK1 MAPKKK in TGF-beta signal transduction.";
RL Science 272:1179-1182(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING.
RX PubMed=12429732; DOI=10.1074/jbc.m210918200;
RA Ge B., Xiong X., Jing Q., Mosley J.L., Filose A., Bian D., Huang S.,
RA Han J.;
RT "TAB1beta (transforming growth factor-beta-activated protein kinase 1-
RT binding protein 1beta), a novel splicing variant of TAB1 that interacts
RT with p38alpha but not TAK1.";
RL J. Biol. Chem. 278:2286-2293(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G);
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=PNS;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP INTERACTION WITH TRAF6 AND MAP3K7.
RX PubMed=10094049; DOI=10.1038/18465;
RA Ninomiya-Tsuji J., Kishimoto K., Hiyama A., Inoue J., Cao Z., Matsumoto K.;
RT "The kinase TAK1 can activate the NIK-I kappaB as well as the MAP kinase
RT cascade in the IL-1 signalling pathway.";
RL Nature 398:252-256(1999).
RN [8]
RP INTERACTION WITH MAP3K7, AND MUTAGENESIS OF PHE-484.
RX PubMed=11323434; DOI=10.1074/jbc.m102631200;
RA Ono K., Ohtomo T., Sato S., Sugamata Y., Suzuki M., Hisamoto N.,
RA Ninomiya-Tsuji J., Tsuchiya M., Matsumoto K.;
RT "An evolutionarily conserved motif in the TAB1 C-terminal region is
RT necessary for interaction with and activation of TAK1 MAPKKK.";
RL J. Biol. Chem. 276:24396-24400(2001).
RN [9]
RP SUBUNIT, AND IDENTIFICATION IN THE TRIKA2 COMPLEX.
RX PubMed=11460167; DOI=10.1038/35085597;
RA Wang C., Deng L., Hong M., Akkaraju G.R., Inoue J., Chen Z.J.;
RT "TAK1 is a ubiquitin-dependent kinase of MKK and IKK.";
RL Nature 412:346-351(2001).
RN [10]
RP INTERACTION WITH XIAP AND BIRC7.
RX PubMed=11865055; DOI=10.1128/mcb.22.6.1754-1766.2002;
RA Sanna M.G., da Silva Correia J., Ducrey O., Lee J., Nomoto K., Schrantz N.,
RA Deveraux Q.L., Ulevitch R.J.;
RT "IAP suppression of apoptosis involves distinct mechanisms: the TAK1/JNK1
RT signaling cascade and caspase inhibition.";
RL Mol. Cell. Biol. 22:1754-1766(2002).
RN [11]
RP UBIQUITINATION, PHOSPHORYLATION AT SER-438, MUTAGENESIS OF SER-438, AND
RP DEUBIQUITINATION BY YOPP.
RX PubMed=16845370; DOI=10.1038/sj.embor.7400754;
RA Thiefes A., Wolf A., Doerrie A., Grassl G.A., Matsumoto K., Autenrieth I.,
RA Bohn E., Sakurai H., Niedenthal R., Resch K., Kracht M.;
RT "The Yersinia enterocolitica effector YopP inhibits host cell signalling by
RT inactivating the protein kinase TAK1 in the IL-1 signalling pathway.";
RL EMBO Rep. 7:838-844(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-378, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-378, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438 AND THR-442, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 1-401, AND LACK OF FUNCTION AS A
RP PHOSPHATASE.
RX PubMed=16879102; DOI=10.1042/bj20061077;
RA Conner S.H., Kular G., Peggie M., Shepherd S., Schuettelkopf A.W.,
RA Cohen P., Van Aalten D.M.F.;
RT "TAK1-binding protein 1 is a pseudophosphatase.";
RL Biochem. J. 399:427-434(2006).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS) OF 1-370 IN COMPLEX WITH XIAP, AND
RP MUTAGENESIS OF ASP-213 AND PHE-216.
RX PubMed=17560374; DOI=10.1016/j.molcel.2007.05.006;
RA Lu M., Lin S.-C., Huang Y., Kang Y.J., Rich R., Lo Y.-C., Myszka D.,
RA Han J., Wu H.;
RT "XIAP induces NF-kappaB activation via the BIR1/TAB1 interaction and BIR1
RT dimerization.";
RL Mol. Cell 26:689-702(2007).
CC -!- FUNCTION: May be an important signaling intermediate between TGFB
CC receptors and MAP3K7/TAK1. May play an important role in mammalian
CC embryogenesis.
CC -!- SUBUNIT: Interacts with XIAP and BIRC7 (PubMed:17560374,
CC PubMed:11865055). Interacts with TRAF6 and MAP3K7; during IL-1
CC signaling (PubMed:8638164, PubMed:10094049, PubMed:11323434).
CC Identified in the TRIKA2 complex composed of MAP3K7, TAB1 and TAB2
CC (PubMed:11460167). {ECO:0000269|PubMed:10094049,
CC ECO:0000269|PubMed:11323434, ECO:0000269|PubMed:11460167,
CC ECO:0000269|PubMed:11865055, ECO:0000269|PubMed:17560374,
CC ECO:0000269|PubMed:8638164}.
CC -!- INTERACTION:
CC Q15750; P47929: LGALS7B; NbExp=3; IntAct=EBI-358643, EBI-357504;
CC Q15750; O43318: MAP3K7; NbExp=6; IntAct=EBI-358643, EBI-358684;
CC Q15750; O43318-2: MAP3K7; NbExp=3; IntAct=EBI-358643, EBI-358700;
CC Q15750; O15294: OGT; NbExp=3; IntAct=EBI-358643, EBI-539828;
CC Q15750; Q9NYJ8: TAB2; NbExp=6; IntAct=EBI-358643, EBI-358708;
CC Q15750; P98170: XIAP; NbExp=4; IntAct=EBI-358643, EBI-517127;
CC Q15750; PRO_0000449623 [P0DTD1]: rep; Xeno; NbExp=2; IntAct=EBI-358643, EBI-25475864;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=TAB1alpha;
CC IsoId=Q15750-1; Sequence=Displayed;
CC Name=2; Synonyms=TAB1beta;
CC IsoId=Q15750-2; Sequence=VSP_042024;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- PTM: Monoubiquitinated. Deubiquitinated by Y.enterocolitica YopP.
CC -!- MISCELLANEOUS: [Isoform 2]: Does not bind nor activate MAP3K7/TAK1.
CC {ECO:0000305}.
CC -!- CAUTION: Lacks several key residues involved in metal-binding and
CC catalytic activity, therefore has lost phosphatase activity.
CC {ECO:0000303|PubMed:16879102}.
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DR EMBL; U49928; AAC12660.1; -; mRNA.
DR EMBL; AF425640; AAN32760.1; -; mRNA.
DR EMBL; DQ314876; ABC40735.1; -; Genomic_DNA.
DR EMBL; AL022312; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z83845; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471095; EAW60326.1; -; Genomic_DNA.
DR EMBL; BC050554; AAH50554.1; -; mRNA.
DR CCDS; CCDS13992.1; -. [Q15750-2]
DR CCDS; CCDS13993.1; -. [Q15750-1]
DR RefSeq; NP_006107.1; NM_006116.2. [Q15750-1]
DR RefSeq; NP_705717.1; NM_153497.2. [Q15750-2]
DR PDB; 2J4O; X-ray; 2.25 A; A=1-401.
DR PDB; 2POM; X-ray; 2.27 A; A=1-370.
DR PDB; 2POP; X-ray; 3.10 A; A/C=1-370.
DR PDB; 2YDS; X-ray; 2.55 A; T=392-398.
DR PDB; 2YIY; X-ray; 2.49 A; A=468-497.
DR PDB; 4AY5; X-ray; 3.15 A; I/J/K/L=389-399.
DR PDB; 4AY6; X-ray; 3.30 A; E/F/G/H=389-401.
DR PDB; 4GS6; X-ray; 2.20 A; A=468-504.
DR PDB; 4KA3; X-ray; 2.71 A; B=395-415.
DR PDB; 4L3P; X-ray; 2.68 A; A=468-504.
DR PDB; 4L52; X-ray; 2.54 A; A=468-496.
DR PDB; 4L53; X-ray; 2.55 A; A=468-496.
DR PDB; 4O91; X-ray; 2.39 A; A=468-504.
DR PDB; 5DIY; X-ray; 2.06 A; P/Q=392-398.
DR PDB; 5E7R; X-ray; 2.11 A; A=468-504.
DR PDB; 5GJD; X-ray; 2.79 A; A=468-504.
DR PDB; 5GJF; X-ray; 2.89 A; A=468-504.
DR PDB; 5GJG; X-ray; 2.61 A; A=468-504.
DR PDB; 5J7S; X-ray; 2.37 A; A=468-504.
DR PDB; 5J8I; X-ray; 2.40 A; A=468-504.
DR PDB; 5J9L; X-ray; 2.75 A; A=468-497.
DR PDB; 5JGA; X-ray; 2.00 A; A=468-504.
DR PDB; 5JGB; X-ray; 2.80 A; A=468-504.
DR PDB; 5JGD; X-ray; 3.10 A; A=468-504.
DR PDB; 5JH6; X-ray; 2.37 A; A=468-504.
DR PDB; 5JK3; X-ray; 2.37 A; A=468-504.
DR PDB; 5NZZ; X-ray; 2.60 A; A/B/C/D=1-504.
DR PDB; 5O90; X-ray; 2.49 A; B=386-414.
DR PDB; 5V5N; X-ray; 2.01 A; A=468-497.
DR PDB; 5VVU; X-ray; 2.70 A; B/D=392-398.
DR PDB; 7NTH; X-ray; 1.97 A; A=468-504.
DR PDB; 7NTI; X-ray; 1.98 A; A=468-504.
DR PDBsum; 2J4O; -.
DR PDBsum; 2POM; -.
DR PDBsum; 2POP; -.
DR PDBsum; 2YDS; -.
DR PDBsum; 2YIY; -.
DR PDBsum; 4AY5; -.
DR PDBsum; 4AY6; -.
DR PDBsum; 4GS6; -.
DR PDBsum; 4KA3; -.
DR PDBsum; 4L3P; -.
DR PDBsum; 4L52; -.
DR PDBsum; 4L53; -.
DR PDBsum; 4O91; -.
DR PDBsum; 5DIY; -.
DR PDBsum; 5E7R; -.
DR PDBsum; 5GJD; -.
DR PDBsum; 5GJF; -.
DR PDBsum; 5GJG; -.
DR PDBsum; 5J7S; -.
DR PDBsum; 5J8I; -.
DR PDBsum; 5J9L; -.
DR PDBsum; 5JGA; -.
DR PDBsum; 5JGB; -.
DR PDBsum; 5JGD; -.
DR PDBsum; 5JH6; -.
DR PDBsum; 5JK3; -.
DR PDBsum; 5NZZ; -.
DR PDBsum; 5O90; -.
DR PDBsum; 5V5N; -.
DR PDBsum; 5VVU; -.
DR PDBsum; 7NTH; -.
DR PDBsum; 7NTI; -.
DR AlphaFoldDB; Q15750; -.
DR SMR; Q15750; -.
DR BioGRID; 115717; 228.
DR CORUM; Q15750; -.
DR DIP; DIP-27524N; -.
DR ELM; Q15750; -.
DR IntAct; Q15750; 131.
DR MINT; Q15750; -.
DR STRING; 9606.ENSP00000216160; -.
DR BindingDB; Q15750; -.
DR ChEMBL; CHEMBL5605; -.
DR DrugBank; DB06757; Manganese.
DR MoonDB; Q15750; Predicted.
DR DEPOD; TAB1; -.
DR GlyGen; Q15750; 10 sites, 2 O-linked glycans (10 sites).
DR iPTMnet; Q15750; -.
DR PhosphoSitePlus; Q15750; -.
DR BioMuta; TAB1; -.
DR DMDM; 10720303; -.
DR CPTAC; CPTAC-906; -.
DR CPTAC; CPTAC-907; -.
DR EPD; Q15750; -.
DR jPOST; Q15750; -.
DR MassIVE; Q15750; -.
DR MaxQB; Q15750; -.
DR PaxDb; Q15750; -.
DR PeptideAtlas; Q15750; -.
DR PRIDE; Q15750; -.
DR ProteomicsDB; 60741; -. [Q15750-1]
DR ProteomicsDB; 60742; -. [Q15750-2]
DR Antibodypedia; 12659; 646 antibodies from 44 providers.
DR DNASU; 10454; -.
DR Ensembl; ENST00000216160.11; ENSP00000216160.6; ENSG00000100324.14. [Q15750-1]
DR Ensembl; ENST00000331454.3; ENSP00000333049.3; ENSG00000100324.14. [Q15750-2]
DR GeneID; 10454; -.
DR KEGG; hsa:10454; -.
DR MANE-Select; ENST00000216160.11; ENSP00000216160.6; NM_006116.3; NP_006107.1.
DR UCSC; uc003axt.4; human. [Q15750-1]
DR CTD; 10454; -.
DR DisGeNET; 10454; -.
DR GeneCards; TAB1; -.
DR HGNC; HGNC:18157; TAB1.
DR HPA; ENSG00000100324; Low tissue specificity.
DR MIM; 602615; gene.
DR neXtProt; NX_Q15750; -.
DR OpenTargets; ENSG00000100324; -.
DR PharmGKB; PA30604; -.
DR VEuPathDB; HostDB:ENSG00000100324; -.
DR eggNOG; KOG0698; Eukaryota.
DR GeneTree; ENSGT00510000048276; -.
DR HOGENOM; CLU_027717_1_0_1; -.
DR InParanoid; Q15750; -.
DR OMA; NTRCLGN; -.
DR PhylomeDB; Q15750; -.
DR TreeFam; TF317785; -.
DR PathwayCommons; Q15750; -.
DR Reactome; R-HSA-168638; NOD1/2 Signaling Pathway.
DR Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-HSA-445989; TAK1-dependent IKK and NF-kappa-B activation.
DR Reactome; R-HSA-450302; activated TAK1 mediates p38 MAPK activation.
DR Reactome; R-HSA-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
DR Reactome; R-HSA-5357956; TNFR1-induced NFkappaB signaling pathway.
DR Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR Reactome; R-HSA-9014325; TICAM1,TRAF6-dependent induction of TAK1 complex.
DR Reactome; R-HSA-9020702; Interleukin-1 signaling.
DR Reactome; R-HSA-937042; IRAK2 mediated activation of TAK1 complex.
DR Reactome; R-HSA-937072; TRAF6-mediated induction of TAK1 complex within TLR4 complex.
DR Reactome; R-HSA-9645460; Alpha-protein kinase 1 signaling pathway.
DR Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses.
DR Reactome; R-HSA-975163; IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation.
DR SignaLink; Q15750; -.
DR SIGNOR; Q15750; -.
DR BioGRID-ORCS; 10454; 17 hits in 1084 CRISPR screens.
DR ChiTaRS; TAB1; human.
DR EvolutionaryTrace; Q15750; -.
DR GeneWiki; MAP3K7IP1; -.
DR GenomeRNAi; 10454; -.
DR Pharos; Q15750; Tchem.
DR PRO; PR:Q15750; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q15750; protein.
DR Bgee; ENSG00000100324; Expressed in parotid gland and 150 other tissues.
DR ExpressionAtlas; Q15750; baseline and differential.
DR Genevisible; Q15750; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0010008; C:endosome membrane; TAS:Reactome.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0008047; F:enzyme activator activity; TAS:ProtInc.
DR GO; GO:0019209; F:kinase activator activity; IEA:Ensembl.
DR GO; GO:0048273; F:mitogen-activated protein kinase p38 binding; IEA:Ensembl.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0035904; P:aorta development; IEA:Ensembl.
DR GO; GO:0003279; P:cardiac septum development; IEA:Ensembl.
DR GO; GO:0060976; P:coronary vasculature development; IEA:Ensembl.
DR GO; GO:0003007; P:heart morphogenesis; IEA:Ensembl.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0030324; P:lung development; IEA:Ensembl.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; IEA:Ensembl.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 3.60.40.10; -; 1.
DR InterPro; IPR015655; PP2C.
DR InterPro; IPR036457; PPM-type_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase_dom.
DR PANTHER; PTHR13832; PTHR13832; 1.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; SSF81606; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..504
FT /note="TGF-beta-activated kinase 1 and MAP3K7-binding
FT protein 1"
FT /id="PRO_0000057797"
FT DOMAIN 28..365
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 430..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 484
FT /note="Required for interaction with MAP3K7"
FT /evidence="ECO:0000269|PubMed:11323434"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 378
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 438
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16845370,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 442
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 436..504
FT /note="NQSPTLTLQSTNTHTQSSSSSSDGGLFRSRPAHSLPPGEDGRVEPYVDFAEF
FT YRLWSVDHGEQSVVTAP -> KDPSRPASDLTAIPQCQLNLLGSLTPG (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:12429732"
FT /id="VSP_042024"
FT VARIANT 224
FT /note="D -> E (in dbSNP:rs17001096)"
FT /id="VAR_039271"
FT MUTAGEN 213
FT /note="D->A: Loss of interaction with XIAP."
FT /evidence="ECO:0000269|PubMed:17560374"
FT MUTAGEN 216
FT /note="F->A: Loss of interaction with XIAP."
FT /evidence="ECO:0000269|PubMed:17560374"
FT MUTAGEN 438
FT /note="S->A: Loss of phosphorylation site."
FT /evidence="ECO:0000269|PubMed:16845370"
FT MUTAGEN 484
FT /note="F->A: Abolishes interaction with MAP3K7."
FT /evidence="ECO:0000269|PubMed:11323434"
FT TURN 18..20
FT /evidence="ECO:0007829|PDB:2J4O"
FT STRAND 27..32
FT /evidence="ECO:0007829|PDB:2J4O"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:2J4O"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:2J4O"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:5NZZ"
FT STRAND 51..58
FT /evidence="ECO:0007829|PDB:2J4O"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:2J4O"
FT STRAND 62..74
FT /evidence="ECO:0007829|PDB:2J4O"
FT HELIX 75..86
FT /evidence="ECO:0007829|PDB:2J4O"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:2J4O"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:2POP"
FT HELIX 99..133
FT /evidence="ECO:0007829|PDB:2J4O"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:2POM"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:2J4O"
FT HELIX 149..162
FT /evidence="ECO:0007829|PDB:2J4O"
FT STRAND 165..174
FT /evidence="ECO:0007829|PDB:2J4O"
FT STRAND 177..185
FT /evidence="ECO:0007829|PDB:2J4O"
FT STRAND 187..193
FT /evidence="ECO:0007829|PDB:2J4O"
FT STRAND 195..202
FT /evidence="ECO:0007829|PDB:2J4O"
FT HELIX 212..219
FT /evidence="ECO:0007829|PDB:2J4O"
FT TURN 220..222
FT /evidence="ECO:0007829|PDB:2J4O"
FT HELIX 225..231
FT /evidence="ECO:0007829|PDB:2J4O"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:2POM"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:2POM"
FT HELIX 246..250
FT /evidence="ECO:0007829|PDB:2J4O"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:2J4O"
FT TURN 256..260
FT /evidence="ECO:0007829|PDB:2J4O"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:2J4O"
FT STRAND 271..277
FT /evidence="ECO:0007829|PDB:2J4O"
FT STRAND 283..288
FT /evidence="ECO:0007829|PDB:2J4O"
FT HELIX 290..300
FT /evidence="ECO:0007829|PDB:2J4O"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:2POP"
FT HELIX 305..319
FT /evidence="ECO:0007829|PDB:2J4O"
FT HELIX 323..343
FT /evidence="ECO:0007829|PDB:2J4O"
FT HELIX 348..351
FT /evidence="ECO:0007829|PDB:2J4O"
FT STRAND 353..355
FT /evidence="ECO:0007829|PDB:2J4O"
FT STRAND 358..366
FT /evidence="ECO:0007829|PDB:2J4O"
FT STRAND 475..478
FT /evidence="ECO:0007829|PDB:7NTH"
FT HELIX 485..494
FT /evidence="ECO:0007829|PDB:7NTH"
SQ SEQUENCE 504 AA; 54644 MW; A45743288718983A CRC64;
MAAQRRSLLQ SEQQPSWTDD LPLCHLSGVG SASNRSYSAD GKGTESHPPE DSWLKFRSEN
NCFLYGVFNG YDGNRVTNFV AQRLSAELLL GQLNAEHAEA DVRRVLLQAF DVVERSFLES
IDDALAEKAS LQSQLPEGVP QHQLPPQYQK ILERLKTLER EISGGAMAVV AVLLNNKLYV
ANVGTNRALL CKSTVDGLQV TQLNVDHTTE NEDELFRLSQ LGLDAGKIKQ VGIICGQEST
RRIGDYKVKY GYTDIDLLSA AKSKPIIAEP EIHGAQPLDG VTGFLVLMSE GLYKALEAAH
GPGQANQEIA AMIDTEFAKQ TSLDAVAQAV VDRVKRIHSD TFASGGERAR FCPRHEDMTL
LVRNFGYPLG EMSQPTPSPA PAAGGRVYPV SVPYSSAQST SKTSVTLSLV MPSQGQMVNG
AHSASTLDEA TPTLTNQSPT LTLQSTNTHT QSSSSSSDGG LFRSRPAHSL PPGEDGRVEP
YVDFAEFYRL WSVDHGEQSV VTAP
