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TGF-beta-activated kinase 1 and MAP3K7-binding protein 1 (Mitogen-activated protein kinase kinase kinase 7-interacting protein 1) (TGF-beta-activated kinase 1-binding protein 1) (TAK1-binding protein 1)

 TAB1_HUMAN              Reviewed;         504 AA.
Q15750; Q2PP09; Q8IZW2;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
17-JUN-2020, entry version 198.
RecName: Full=TGF-beta-activated kinase 1 and MAP3K7-binding protein 1;
AltName: Full=Mitogen-activated protein kinase kinase kinase 7-interacting protein 1;
AltName: Full=TGF-beta-activated kinase 1-binding protein 1;
Short=TAK1-binding protein 1;
Name=TAB1; Synonyms=MAP3K7IP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH MAP3K7.
TISSUE=Brain;
PubMed=8638164; DOI=10.1126/science.272.5265.1179;
Shibuya H., Yamaguchi K., Shirakabe K., Tonegawa A., Gotoh Y., Ueno N.,
Irie K., Nishida E., Matsumoto K.;
"TAB1: an activator of the TAK1 MAPKKK in TGF-beta signal transduction.";
Science 272:1179-1182(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING.
PubMed=12429732; DOI=10.1074/jbc.m210918200;
Ge B., Xiong X., Jing Q., Mosley J.L., Filose A., Bian D., Huang S.,
Han J.;
"TAB1beta (transforming growth factor-beta-activated protein kinase 1-
binding protein 1beta), a novel splicing variant of TAB1 that interacts
with p38alpha but not TAK1.";
J. Biol. Chem. 278:2286-2293(2003).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10591208; DOI=10.1038/990031;
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
Wright H.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=PNS;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
INTERACTION WITH TRAF6 AND MAP3K7.
PubMed=10094049; DOI=10.1038/18465;
Ninomiya-Tsuji J., Kishimoto K., Hiyama A., Inoue J., Cao Z., Matsumoto K.;
"The kinase TAK1 can activate the NIK-I kappaB as well as the MAP kinase
cascade in the IL-1 signalling pathway.";
Nature 398:252-256(1999).
[8]
INTERACTION WITH MAP3K7, AND MUTAGENESIS OF PHE-484.
PubMed=11323434; DOI=10.1074/jbc.m102631200;
Ono K., Ohtomo T., Sato S., Sugamata Y., Suzuki M., Hisamoto N.,
Ninomiya-Tsuji J., Tsuchiya M., Matsumoto K.;
"An evolutionarily conserved motif in the TAB1 C-terminal region is
necessary for interaction with and activation of TAK1 MAPKKK.";
J. Biol. Chem. 276:24396-24400(2001).
[9]
SUBUNIT, AND IDENTIFICATION IN THE TRIKA2 COMPLEX.
PubMed=11460167; DOI=10.1038/35085597;
Wang C., Deng L., Hong M., Akkaraju G.R., Inoue J., Chen Z.J.;
"TAK1 is a ubiquitin-dependent kinase of MKK and IKK.";
Nature 412:346-351(2001).
[10]
INTERACTION WITH XIAP AND BIRC7.
PubMed=11865055; DOI=10.1128/mcb.22.6.1754-1766.2002;
Sanna M.G., da Silva Correia J., Ducrey O., Lee J., Nomoto K., Schrantz N.,
Deveraux Q.L., Ulevitch R.J.;
"IAP suppression of apoptosis involves distinct mechanisms: the TAK1/JNK1
signaling cascade and caspase inhibition.";
Mol. Cell. Biol. 22:1754-1766(2002).
[11]
UBIQUITINATION, PHOSPHORYLATION AT SER-438, MUTAGENESIS OF SER-438, AND
DEUBIQUITINATION BY YOPP.
PubMed=16845370; DOI=10.1038/sj.embor.7400754;
Thiefes A., Wolf A., Doerrie A., Grassl G.A., Matsumoto K., Autenrieth I.,
Bohn E., Sakurai H., Niedenthal R., Resch K., Kracht M.;
"The Yersinia enterocolitica effector YopP inhibits host cell signalling by
inactivating the protein kinase TAK1 in the IL-1 signalling pathway.";
EMBO Rep. 7:838-844(2006).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-378, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
"Quantitative phosphoproteomics reveals widespread full phosphorylation
site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-378, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438 AND THR-442, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
phosphoproteome.";
J. Proteomics 96:253-262(2014).
[19]
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 1-401, AND LACK OF FUNCTION AS A
PHOSPHATASE.
PubMed=16879102; DOI=10.1042/bj20061077;
Conner S.H., Kular G., Peggie M., Shepherd S., Schuettelkopf A.W.,
Cohen P., Van Aalten D.M.F.;
"TAK1-binding protein 1 is a pseudophosphatase.";
Biochem. J. 399:427-434(2006).
[20]
X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS) OF 1-370 IN COMPLEX WITH XIAP, AND
MUTAGENESIS OF ASP-213 AND PHE-216.
PubMed=17560374; DOI=10.1016/j.molcel.2007.05.006;
Lu M., Lin S.-C., Huang Y., Kang Y.J., Rich R., Lo Y.-C., Myszka D.,
Han J., Wu H.;
"XIAP induces NF-kappaB activation via the BIR1/TAB1 interaction and BIR1
dimerization.";
Mol. Cell 26:689-702(2007).
-!- FUNCTION: May be an important signaling intermediate between TGFB
receptors and MAP3K7/TAK1. May play an important role in mammalian
embryogenesis.
-!- SUBUNIT: Interacts with XIAP and BIRC7 (PubMed:17560374,
PubMed:11865055). Interacts with TRAF6 and MAP3K7; during IL-1
signaling (PubMed:8638164, PubMed:10094049, PubMed:11323434).
Identified in the TRIKA2 complex composed of MAP3K7, TAB1 and TAB2
(PubMed:11460167). {ECO:0000269|PubMed:10094049,
ECO:0000269|PubMed:11323434, ECO:0000269|PubMed:11460167,
ECO:0000269|PubMed:11865055, ECO:0000269|PubMed:17560374,
ECO:0000269|PubMed:8638164}.
-!- INTERACTION:
Q15750; P32121: ARRB2; NbExp=3; IntAct=EBI-358643, EBI-714559;
Q15750; P47929: LGALS7; NbExp=3; IntAct=EBI-358643, EBI-357504;
Q15750; O43318: MAP3K7; NbExp=4; IntAct=EBI-358643, EBI-358684;
Q15750; O43318-2: MAP3K7; NbExp=3; IntAct=EBI-358643, EBI-358700;
Q15750; Q16539: MAPK14; NbExp=2; IntAct=EBI-358643, EBI-73946;
Q15750; O15294: OGT; NbExp=3; IntAct=EBI-358643, EBI-539828;
Q15750; Q9NYJ8: TAB2; NbExp=5; IntAct=EBI-358643, EBI-358708;
Q15750; P98170: XIAP; NbExp=4; IntAct=EBI-358643, EBI-517127;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=TAB1alpha;
IsoId=Q15750-1; Sequence=Displayed;
Name=2; Synonyms=TAB1beta;
IsoId=Q15750-2; Sequence=VSP_042024;
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- PTM: Monoubiquitinated. Deubiquitinated by Y.enterocolitica YopP.
-!- MISCELLANEOUS: [Isoform 2]: Does not bind nor activate MAP3K7/TAK1.
{ECO:0000305}.
-!- CAUTION: Lacks several key residues involved in metal-binding and
catalytic activity, therefore has lost phosphatase activity.
{ECO:0000303|PubMed:16879102}.
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EMBL; U49928; AAC12660.1; -; mRNA.
EMBL; AF425640; AAN32760.1; -; mRNA.
EMBL; DQ314876; ABC40735.1; -; Genomic_DNA.
EMBL; AL022312; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z83845; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471095; EAW60326.1; -; Genomic_DNA.
EMBL; BC050554; AAH50554.1; -; mRNA.
CCDS; CCDS13992.1; -. [Q15750-2]
CCDS; CCDS13993.1; -. [Q15750-1]
RefSeq; NP_006107.1; NM_006116.2. [Q15750-1]
RefSeq; NP_705717.1; NM_153497.2. [Q15750-2]
PDB; 2J4O; X-ray; 2.25 A; A=1-401.
PDB; 2POM; X-ray; 2.27 A; A=1-370.
PDB; 2POP; X-ray; 3.10 A; A/C=1-370.
PDB; 2YDS; X-ray; 2.55 A; T=392-398.
PDB; 2YIY; X-ray; 2.49 A; A=468-497.
PDB; 4AY5; X-ray; 3.15 A; I/J/K/L=389-399.
PDB; 4AY6; X-ray; 3.30 A; E/F/G/H=389-401.
PDB; 4GS6; X-ray; 2.20 A; A=468-504.
PDB; 4KA3; X-ray; 2.71 A; B=395-415.
PDB; 4L3P; X-ray; 2.68 A; A=468-504.
PDB; 4L52; X-ray; 2.54 A; A=468-496.
PDB; 4L53; X-ray; 2.55 A; A=468-496.
PDB; 4O91; X-ray; 2.39 A; A=468-504.
PDB; 5DIY; X-ray; 2.06 A; P/Q=392-398.
PDB; 5E7R; X-ray; 2.11 A; A=468-504.
PDB; 5GJD; X-ray; 2.79 A; A=468-504.
PDB; 5GJF; X-ray; 2.89 A; A=468-504.
PDB; 5GJG; X-ray; 2.61 A; A=468-504.
PDB; 5J7S; X-ray; 2.37 A; A=468-504.
PDB; 5J8I; X-ray; 2.40 A; A=468-504.
PDB; 5J9L; X-ray; 2.75 A; A=468-497.
PDB; 5JGA; X-ray; 2.00 A; A=468-504.
PDB; 5JGB; X-ray; 2.80 A; A=468-504.
PDB; 5JGD; X-ray; 3.10 A; A=468-504.
PDB; 5JH6; X-ray; 2.37 A; A=468-504.
PDB; 5JK3; X-ray; 2.37 A; A=468-504.
PDB; 5NZZ; X-ray; 2.60 A; A/B/C/D=1-504.
PDB; 5O90; X-ray; 2.49 A; B=386-414.
PDB; 5V5N; X-ray; 2.01 A; A=468-497.
PDB; 5VVU; X-ray; 2.70 A; B/D=392-398.
PDBsum; 2J4O; -.
PDBsum; 2POM; -.
PDBsum; 2POP; -.
PDBsum; 2YDS; -.
PDBsum; 2YIY; -.
PDBsum; 4AY5; -.
PDBsum; 4AY6; -.
PDBsum; 4GS6; -.
PDBsum; 4KA3; -.
PDBsum; 4L3P; -.
PDBsum; 4L52; -.
PDBsum; 4L53; -.
PDBsum; 4O91; -.
PDBsum; 5DIY; -.
PDBsum; 5E7R; -.
PDBsum; 5GJD; -.
PDBsum; 5GJF; -.
PDBsum; 5GJG; -.
PDBsum; 5J7S; -.
PDBsum; 5J8I; -.
PDBsum; 5J9L; -.
PDBsum; 5JGA; -.
PDBsum; 5JGB; -.
PDBsum; 5JGD; -.
PDBsum; 5JH6; -.
PDBsum; 5JK3; -.
PDBsum; 5NZZ; -.
PDBsum; 5O90; -.
PDBsum; 5V5N; -.
PDBsum; 5VVU; -.
SMR; Q15750; -.
BioGRID; 115717; 164.
CORUM; Q15750; -.
DIP; DIP-27524N; -.
ELM; Q15750; -.
IntAct; Q15750; 122.
MINT; Q15750; -.
STRING; 9606.ENSP00000216160; -.
BindingDB; Q15750; -.
ChEMBL; CHEMBL5605; -.
DrugBank; DB06757; Manganese.
MoonDB; Q15750; Predicted.
iPTMnet; Q15750; -.
PhosphoSitePlus; Q15750; -.
BioMuta; TAB1; -.
DMDM; 10720303; -.
CPTAC; CPTAC-906; -.
CPTAC; CPTAC-907; -.
EPD; Q15750; -.
jPOST; Q15750; -.
MassIVE; Q15750; -.
MaxQB; Q15750; -.
PaxDb; Q15750; -.
PeptideAtlas; Q15750; -.
PRIDE; Q15750; -.
ProteomicsDB; 60741; -. [Q15750-1]
ProteomicsDB; 60742; -. [Q15750-2]
Antibodypedia; 12659; 604 antibodies.
DNASU; 10454; -.
Ensembl; ENST00000216160; ENSP00000216160; ENSG00000100324. [Q15750-1]
Ensembl; ENST00000331454; ENSP00000333049; ENSG00000100324. [Q15750-2]
GeneID; 10454; -.
KEGG; hsa:10454; -.
UCSC; uc003axt.4; human. [Q15750-1]
CTD; 10454; -.
DisGeNET; 10454; -.
EuPathDB; HostDB:ENSG00000100324.13; -.
GeneCards; TAB1; -.
HGNC; HGNC:18157; TAB1.
HPA; ENSG00000100324; Low tissue specificity.
MIM; 602615; gene.
neXtProt; NX_Q15750; -.
OpenTargets; ENSG00000100324; -.
PharmGKB; PA30604; -.
eggNOG; KOG0698; Eukaryota.
eggNOG; COG0631; LUCA.
GeneTree; ENSGT00510000048276; -.
HOGENOM; CLU_027717_1_0_1; -.
InParanoid; Q15750; -.
KO; K04403; -.
OMA; NTRCLGN; -.
PhylomeDB; Q15750; -.
TreeFam; TF317785; -.
Reactome; R-HSA-168638; NOD1/2 Signaling Pathway.
Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
Reactome; R-HSA-445989; TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
Reactome; R-HSA-450302; activated TAK1 mediates p38 MAPK activation.
Reactome; R-HSA-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
Reactome; R-HSA-5357956; TNFR1-induced NFkappaB signaling pathway.
Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
Reactome; R-HSA-9014325; TICAM1,TRAF6-dependent induction of TAK1 complex.
Reactome; R-HSA-9020702; Interleukin-1 signaling.
Reactome; R-HSA-937042; IRAK2 mediated activation of TAK1 complex.
Reactome; R-HSA-937072; TRAF6-mediated induction of TAK1 complex within TLR4 complex.
Reactome; R-HSA-9645460; Alpha-protein kinase 1 signaling pathway.
Reactome; R-HSA-975163; IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation.
SignaLink; Q15750; -.
SIGNOR; Q15750; -.
BioGRID-ORCS; 10454; 3 hits in 785 CRISPR screens.
ChiTaRS; TAB1; human.
EvolutionaryTrace; Q15750; -.
GeneWiki; MAP3K7IP1; -.
GenomeRNAi; 10454; -.
Pharos; Q15750; Tbio.
PRO; PR:Q15750; -.
Proteomes; UP000005640; Chromosome 22.
RNAct; Q15750; protein.
Bgee; ENSG00000100324; Expressed in corpus callosum and 187 other tissues.
ExpressionAtlas; Q15750; baseline and differential.
Genevisible; Q15750; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0010008; C:endosome membrane; TAS:Reactome.
GO; GO:0016607; C:nuclear speck; IDA:HPA.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
GO; GO:0008047; F:enzyme activator activity; TAS:ProtInc.
GO; GO:0019209; F:kinase activator activity; IEA:Ensembl.
GO; GO:0004724; F:magnesium-dependent protein serine/threonine phosphatase activity; IBA:GO_Central.
GO; GO:0048273; F:mitogen-activated protein kinase p38 binding; IBA:GO_Central.
GO; GO:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central.
GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
GO; GO:0000187; P:activation of MAPK activity; TAS:Reactome.
GO; GO:0000185; P:activation of MAPKKK activity; TAS:ProtInc.
GO; GO:0035904; P:aorta development; IEA:Ensembl.
GO; GO:0003279; P:cardiac septum development; IEA:Ensembl.
GO; GO:0060976; P:coronary vasculature development; IEA:Ensembl.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0003007; P:heart morphogenesis; IEA:Ensembl.
GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; TAS:Reactome.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:0070498; P:interleukin-1-mediated signaling pathway; TAS:Reactome.
GO; GO:0007254; P:JNK cascade; TAS:Reactome.
GO; GO:0030324; P:lung development; IEA:Ensembl.
GO; GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; TAS:Reactome.
GO; GO:0070423; P:nucleotide-binding oligomerization domain containing signaling pathway; TAS:Reactome.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; TAS:Reactome.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
CDD; cd00143; PP2Cc; 1.
Gene3D; 3.60.40.10; -; 1.
InterPro; IPR015655; PP2C.
InterPro; IPR036457; PPM-type_dom_sf.
InterPro; IPR001932; PPM-type_phosphatase_dom.
PANTHER; PTHR13832; PTHR13832; 1.
Pfam; PF00481; PP2C; 1.
SMART; SM00332; PP2Cc; 1.
SUPFAM; SSF81606; SSF81606; 1.
PROSITE; PS51746; PPM_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Phosphoprotein; Polymorphism;
Reference proteome; Ubl conjugation.
CHAIN 1..504
/note="TGF-beta-activated kinase 1 and MAP3K7-binding
protein 1"
/id="PRO_0000057797"
DOMAIN 28..365
/note="PPM-type phosphatase"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
COMPBIAS 452..457
/note="Poly-Ser"
SITE 484
/note="Required for interaction with MAP3K7"
/evidence="ECO:0000269|PubMed:11323434"
MOD_RES 7
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648"
MOD_RES 378
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163"
MOD_RES 438
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:16845370"
MOD_RES 442
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:24275569"
VAR_SEQ 436..504
/note="NQSPTLTLQSTNTHTQSSSSSSDGGLFRSRPAHSLPPGEDGRVEPYVDFAEF
YRLWSVDHGEQSVVTAP -> KDPSRPASDLTAIPQCQLNLLGSLTPG (in
isoform 2)"
/evidence="ECO:0000303|PubMed:12429732"
/id="VSP_042024"
VARIANT 224
/note="D -> E (in dbSNP:rs17001096)"
/id="VAR_039271"
MUTAGEN 213
/note="D->A: Loss of interaction with XIAP."
/evidence="ECO:0000269|PubMed:17560374"
MUTAGEN 216
/note="F->A: Loss of interaction with XIAP."
/evidence="ECO:0000269|PubMed:17560374"
MUTAGEN 438
/note="S->A: Loss of phosphorylation site."
/evidence="ECO:0000269|PubMed:16845370"
MUTAGEN 484
/note="F->A: Abolishes interaction with MAP3K7."
/evidence="ECO:0000269|PubMed:11323434"
TURN 18..20
/evidence="ECO:0000244|PDB:2J4O"
STRAND 27..32
/evidence="ECO:0000244|PDB:2J4O"
STRAND 35..37
/evidence="ECO:0000244|PDB:2J4O"
STRAND 39..42
/evidence="ECO:0000244|PDB:2J4O"
STRAND 44..46
/evidence="ECO:0000244|PDB:5NZZ"
STRAND 51..58
/evidence="ECO:0000244|PDB:2J4O"
TURN 59..61
/evidence="ECO:0000244|PDB:2J4O"
STRAND 62..74
/evidence="ECO:0000244|PDB:2J4O"
HELIX 75..86
/evidence="ECO:0000244|PDB:2J4O"
STRAND 89..92
/evidence="ECO:0000244|PDB:2J4O"
STRAND 94..96
/evidence="ECO:0000244|PDB:2POP"
HELIX 99..133
/evidence="ECO:0000244|PDB:2J4O"
HELIX 141..143
/evidence="ECO:0000244|PDB:2POM"
HELIX 146..148
/evidence="ECO:0000244|PDB:2J4O"
HELIX 149..162
/evidence="ECO:0000244|PDB:2J4O"
STRAND 165..174
/evidence="ECO:0000244|PDB:2J4O"
STRAND 177..185
/evidence="ECO:0000244|PDB:2J4O"
STRAND 187..193
/evidence="ECO:0000244|PDB:2J4O"
STRAND 195..202
/evidence="ECO:0000244|PDB:2J4O"
HELIX 212..219
/evidence="ECO:0000244|PDB:2J4O"
TURN 220..222
/evidence="ECO:0000244|PDB:2J4O"
HELIX 225..231
/evidence="ECO:0000244|PDB:2J4O"
STRAND 234..236
/evidence="ECO:0000244|PDB:2POM"
STRAND 239..241
/evidence="ECO:0000244|PDB:2POM"
HELIX 246..250
/evidence="ECO:0000244|PDB:2J4O"
HELIX 252..254
/evidence="ECO:0000244|PDB:2J4O"
TURN 256..260
/evidence="ECO:0000244|PDB:2J4O"
STRAND 265..267
/evidence="ECO:0000244|PDB:2J4O"
STRAND 271..277
/evidence="ECO:0000244|PDB:2J4O"
STRAND 283..288
/evidence="ECO:0000244|PDB:2J4O"
HELIX 290..300
/evidence="ECO:0000244|PDB:2J4O"
STRAND 302..304
/evidence="ECO:0000244|PDB:2POP"
HELIX 305..319
/evidence="ECO:0000244|PDB:2J4O"
HELIX 323..343
/evidence="ECO:0000244|PDB:2J4O"
HELIX 348..351
/evidence="ECO:0000244|PDB:2J4O"
STRAND 353..355
/evidence="ECO:0000244|PDB:2J4O"
STRAND 358..366
/evidence="ECO:0000244|PDB:2J4O"
STRAND 474..476
/evidence="ECO:0000244|PDB:5JGA"
HELIX 485..495
/evidence="ECO:0000244|PDB:5JGA"
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


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WP32: Translation Factors
WP1566: Citrate cycle (TCA cycle)
WP2218: sGC
WP1653: Galactose metabolism
WP1502: Mitochondrial biogenesis
WP1693: Purine metabolism
WP346: Protein Modifications
WP1657: Glycerolipid metabolism
WP2371: Parkinsons Disease Pathway
WP1663: Homologous recombination
WP1909: Signal regulatory protein (SIRP) family interactions
WP1701: Starch and sucrose metabolism
WP2203: TSLP Signaling Pathway
WP1714: Tyrosine metabolism
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WP1625: Base excision repair
WP232: G Protein Signaling Pathways
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Related Genes :
[TAB2 KIAA0733 MAP3K7IP2] TGF-beta-activated kinase 1 and MAP3K7-binding protein 2 (Mitogen-activated protein kinase kinase kinase 7-interacting protein 2) (TAK1-binding protein 2) (TAB-2) (TGF-beta-activated kinase 1-binding protein 2)
[TAB1 MAP3K7IP1] TGF-beta-activated kinase 1 and MAP3K7-binding protein 1 (Mitogen-activated protein kinase kinase kinase 7-interacting protein 1) (TGF-beta-activated kinase 1-binding protein 1) (TAK1-binding protein 1)
[Tab1 Map3k7ip1] TGF-beta-activated kinase 1 and MAP3K7-binding protein 1 (Mitogen-activated protein kinase kinase kinase 7-interacting protein 1) (TGF-beta-activated kinase 1-binding protein 1) (TAK1-binding protein 1)
[TAB3 MAP3K7IP3] TGF-beta-activated kinase 1 and MAP3K7-binding protein 3 (Mitogen-activated protein kinase kinase kinase 7-interacting protein 3) (NF-kappa-B-activating protein 1) (TAK1-binding protein 3) (TAB-3) (TGF-beta-activated kinase 1-binding protein 3)
[Tab2 Kiaa0733 Map3k7ip2] TGF-beta-activated kinase 1 and MAP3K7-binding protein 2 (Mitogen-activated protein kinase kinase kinase 7-interacting protein 2) (TAK1-binding protein 2) (TAB-2) (TGF-beta-activated kinase 1-binding protein 2)
[MAP3K7 TAK1] Mitogen-activated protein kinase kinase kinase 7 (EC 2.7.11.25) (Transforming growth factor-beta-activated kinase 1) (TGF-beta-activated kinase 1)
[Map3k7 Tak1] Mitogen-activated protein kinase kinase kinase 7 (EC 2.7.11.25) (Transforming growth factor-beta-activated kinase 1) (TGF-beta-activated kinase 1)
[tap-1 C44H4.5] TGF-beta-activated kinase 1 and MAP3K7-binding protein 1 (TAB1-like protein 1) (TAK1 kinase/MOM-4 binding Protein)
[Tab3 Kiaa4135 Map3k7ip3] TGF-beta-activated kinase 1 and MAP3K7-binding protein 3 (Mitogen-activated protein kinase kinase kinase 7-interacting protein 3) (TAK1-binding protein 3) (TAB-3) (TGF-beta-activated kinase 1-binding protein 3)
[Map3k7] Mitogen-activated protein kinase kinase kinase 7 (EC 2.7.11.25)
[MAPK14 CSBP CSBP1 CSBP2 CSPB1 MXI2 SAPK2A] Mitogen-activated protein kinase 14 (MAP kinase 14) (MAPK 14) (EC 2.7.11.24) (Cytokine suppressive anti-inflammatory drug-binding protein) (CSAID-binding protein) (CSBP) (MAP kinase MXI2) (MAX-interacting protein 2) (Mitogen-activated protein kinase p38 alpha) (MAP kinase p38 alpha) (Stress-activated protein kinase 2a) (SAPK2a)
[Tab2 Map3k7ip2] TGF-beta-activated kinase 1 and MAP3K7-binding protein 2 (Mitogen-activated protein kinase kinase kinase 7-interacting protein 2) (TGF-beta-activated kinase 1-binding protein 2)
[tab2 map3k7ip2 zgc:77446] TGF-beta-activated kinase 1 and MAP3K7-binding protein 2 (Mitogen-activated protein kinase kinase kinase 7-interacting protein 2) (TGF-beta-activated kinase 1-binding protein 2)
[MAPK8IP1 IB1 JIP1 PRKM8IP] C-Jun-amino-terminal kinase-interacting protein 1 (JIP-1) (JNK-interacting protein 1) (Islet-brain 1) (IB-1) (JNK MAP kinase scaffold protein 1) (Mitogen-activated protein kinase 8-interacting protein 1)
[Mapk8ip1 Ib1 Jip1 Mapk8ip Prkm8ip] C-Jun-amino-terminal kinase-interacting protein 1 (JIP-1) (JNK-interacting protein 1) (Islet-brain-1) (IB-1) (JNK MAP kinase scaffold protein 1) (Mitogen-activated protein kinase 8-interacting protein 1)
[Mapk8ip1 Ib1 Jip1 Mapk8ip] C-Jun-amino-terminal kinase-interacting protein 1 (JIP-1) (JNK-interacting protein 1) (Islet-brain-1) (IB-1) (JIP-1-related protein) (JRP) (JNK MAP kinase scaffold protein 1) (Mitogen-activated protein kinase 8-interacting protein 1)
[MAPK9 JNK2 PRKM9 SAPK1A] Mitogen-activated protein kinase 9 (MAP kinase 9) (MAPK 9) (EC 2.7.11.24) (JNK-55) (Stress-activated protein kinase 1a) (SAPK1a) (Stress-activated protein kinase JNK2) (c-Jun N-terminal kinase 2)
[MAPK8 JNK1 PRKM8 SAPK1 SAPK1C] Mitogen-activated protein kinase 8 (MAP kinase 8) (MAPK 8) (EC 2.7.11.24) (JNK-46) (Stress-activated protein kinase 1c) (SAPK1c) (Stress-activated protein kinase JNK1) (c-Jun N-terminal kinase 1)
[TGFBR1 ALK5 SKR4] TGF-beta receptor type-1 (TGFR-1) (EC 2.7.11.30) (Activin A receptor type II-like protein kinase of 53kD) (Activin receptor-like kinase 5) (ALK-5) (ALK5) (Serine/threonine-protein kinase receptor R4) (SKR4) (TGF-beta type I receptor) (Transforming growth factor-beta receptor type I) (TGF-beta receptor type I) (TbetaR-I)
[Mapk8 Jnk1 Prkm8] Mitogen-activated protein kinase 8 (MAP kinase 8) (MAPK 8) (EC 2.7.11.24) (SAPK gamma) (Stress-activated protein kinase JNK1) (c-Jun N-terminal kinase 1) (p54 gamma)
[Mapk14 Crk1 Csbp1 Csbp2] Mitogen-activated protein kinase 14 (MAP kinase 14) (MAPK 14) (EC 2.7.11.24) (CRK1) (Mitogen-activated protein kinase p38 alpha) (MAP kinase p38 alpha)
[MAP3K7] Mitogen-activated protein kinase kinase kinase 7 (EC 2.7.11.25)
[Mapk8 Jnk1 Prkm8] Mitogen-activated protein kinase 8 (MAP kinase 8) (MAPK 8) (EC 2.7.11.24) (Stress-activated protein kinase JNK1) (c-Jun N-terminal kinase 1)
[MAPK11 PRKM11 SAPK2 SAPK2B] Mitogen-activated protein kinase 11 (MAP kinase 11) (MAPK 11) (EC 2.7.11.24) (Mitogen-activated protein kinase p38 beta) (MAP kinase p38 beta) (p38b) (Stress-activated protein kinase 2b) (SAPK2b) (p38-2)
[MAPK10 JNK3 JNK3A PRKM10 SAPK1B] Mitogen-activated protein kinase 10 (MAP kinase 10) (MAPK 10) (EC 2.7.11.24) (MAP kinase p49 3F12) (Stress-activated protein kinase 1b) (SAPK1b) (Stress-activated protein kinase JNK3) (c-Jun N-terminal kinase 3)
[MAP2K6 MEK6 MKK6 PRKMK6 SKK3] Dual specificity mitogen-activated protein kinase kinase 6 (MAP kinase kinase 6) (MAPKK 6) (EC 2.7.12.2) (MAPK/ERK kinase 6) (MEK 6) (Stress-activated protein kinase kinase 3) (SAPK kinase 3) (SAPKK-3) (SAPKK3)
[Mapk14 Csbp1 Csbp2] Mitogen-activated protein kinase 14 (MAP kinase 14) (MAPK 14) (EC 2.7.11.24) (CRK1) (Mitogen-activated protein kinase p38 alpha) (MAP kinase p38 alpha)
[Mapk11 Prkm11] Mitogen-activated protein kinase 11 (MAP kinase 11) (MAPK 11) (EC 2.7.11.24) (Mitogen-activated protein kinase p38 beta) (MAP kinase p38 beta) (p38B)
[Tgfbr1] TGF-beta receptor type-1 (TGFR-1) (EC 2.7.11.30) (Serine/threonine-protein kinase receptor R4) (SKR4) (TGF-beta type I receptor) (Transforming growth factor-beta receptor type I) (TGF-beta receptor type I) (TbetaR-I)
[Mapk9 Jnk2 Prkm9] Mitogen-activated protein kinase 9 (MAP kinase 9) (MAPK 9) (EC 2.7.11.24) (Stress-activated protein kinase JNK2) (c-Jun N-terminal kinase 2)

Bibliography :