Full text data of TAB1
TAB1
(MAP3K7IP1)
[Confidence: low (only semi-automatic identification from reviews)]
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)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
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)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q15750
ID TAB1_HUMAN Reviewed; 504 AA.
AC Q15750; Q2PP09; Q8IZW2;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 134.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Ueno N., Irie K., Nishida E., Matsumoto K.;
RT "TAB1: an activator of the TAK1 MAPKKK in TGF-beta signal
RT 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
RT interacts 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.,
RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
RA 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.,
RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
RA 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.,
RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
RA Khan A.S., Lane L., Tilahun Y., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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.,
RA Matsumoto K.;
RT "The kinase TAK1 can activate the NIK-I kappaB as well as the MAP
RT kinase cascade in the IL-1 signalling pathway.";
RL Nature 398:252-256(1999).
RN [8]
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 [9]
RP UBIQUITINATION, PHOSPHORYLATION AT SER-438, MUTAGENESIS OF SER-438,
RP AND DEUBIQUITINATION BY YOPP.
RX PubMed=16845370; DOI=10.1038/sj.embor.7400754;
RA Thiefes A., Wolf A., Doerrie A., Grassl G.A., Matsumoto K.,
RA Autenrieth I., Bohn E., Sakurai H., Niedenthal R., Resch K.,
RA Kracht M.;
RT "The Yersinia enterocolitica effector YopP inhibits host cell
RT signalling by inactivating the protein kinase TAK1 in the IL-1
RT signalling pathway.";
RL EMBO Rep. 7:838-844(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND MASS
RP SPECTROMETRY.
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.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND MASS
RP SPECTROMETRY.
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-378, AND MASS
RP SPECTROMETRY.
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 [13]
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
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.,
RA Buerckstuemmer T., 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 [15]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 1-401, AND ABSENCE OF
RP FUNCTION AS A 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 [16]
RP X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS) OF 1-370 IN COMPLEX WITH XIAP,
RP AND 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
RT BIR1 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. Interacts with TRAF6 and
CC MAP3K7; during IL-1 signaling. Identified in the TRIKA2 complex
CC composed of MAP3K7, TAB1 and TAB2.
CC -!- INTERACTION:
CC Q9NYJ8:TAB2; NbExp=3; IntAct=EBI-358643, EBI-358708;
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 Note=Does not bind nor activate MAP3K7/TAK1;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- PTM: Monoubiquitinated. Deubiquitinated by Y.enterocolitica YopP.
CC -!- SIMILARITY: Contains 1 PP2C-like domain.
CC -!- CAUTION: Lacks several key residues involved in metal-binding and
CC catalytic activity, therefore has lost phosphatase activity.
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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; CAB55304.1; -; Genomic_DNA.
DR EMBL; Z83845; CAQ07045.1; -; Genomic_DNA.
DR EMBL; CH471095; EAW60326.1; -; Genomic_DNA.
DR EMBL; BC050554; AAH50554.1; -; mRNA.
DR RefSeq; NP_006107.1; NM_006116.2.
DR RefSeq; NP_705717.1; NM_153497.2.
DR UniGene; Hs.507681; -.
DR UniGene; Hs.729080; -.
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; 4L53; X-ray; 2.55 A; A=468-496.
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; 4L53; -.
DR ProteinModelPortal; Q15750; -.
DR SMR; Q15750; 16-370, 468-496.
DR DIP; DIP-27524N; -.
DR IntAct; Q15750; 65.
DR MINT; MINT-88613; -.
DR BindingDB; Q15750; -.
DR ChEMBL; CHEMBL5605; -.
DR PhosphoSite; Q15750; -.
DR DMDM; 10720303; -.
DR PaxDb; Q15750; -.
DR PRIDE; Q15750; -.
DR DNASU; 10454; -.
DR Ensembl; ENST00000216160; ENSP00000216160; ENSG00000100324.
DR Ensembl; ENST00000331454; ENSP00000333049; ENSG00000100324.
DR GeneID; 10454; -.
DR KEGG; hsa:10454; -.
DR UCSC; uc003axt.3; human.
DR CTD; 10454; -.
DR GeneCards; GC22P039796; -.
DR HGNC; HGNC:18157; TAB1.
DR HPA; CAB032328; -.
DR MIM; 602615; gene.
DR neXtProt; NX_Q15750; -.
DR PharmGKB; PA30604; -.
DR eggNOG; NOG320352; -.
DR HOGENOM; HOG000044226; -.
DR HOVERGEN; HBG007302; -.
DR InParanoid; Q15750; -.
DR KO; K04403; -.
DR OMA; HPPEDNW; -.
DR OrthoDB; EOG7W41C0; -.
DR PhylomeDB; Q15750; -.
DR Reactome; REACT_6782; TRAF6 Mediated Induction of proinflammatory cytokines.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; Q15750; -.
DR ChiTaRS; TAB1; human.
DR EvolutionaryTrace; Q15750; -.
DR GeneWiki; MAP3K7IP1; -.
DR GenomeRNAi; 10454; -.
DR NextBio; 39627; -.
DR PRO; PR:Q15750; -.
DR ArrayExpress; Q15750; -.
DR Bgee; Q15750; -.
DR CleanEx; HS_MAP3K7IP1; -.
DR Genevestigator; Q15750; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0010008; C:endosome membrane; TAS:Reactome.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0008047; F:enzyme activator activity; TAS:ProtInc.
DR GO; GO:0019209; F:kinase activator activity; IEA:Ensembl.
DR GO; GO:0000187; P:activation of MAPK activity; TAS:Reactome.
DR GO; GO:0000185; P:activation of MAPKKK activity; TAS:ProtInc.
DR GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
DR GO; GO:0003007; P:heart morphogenesis; IEA:Ensembl.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB cascade; TAS:Reactome.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0045087; P:innate immune response; TAS:Reactome.
DR GO; GO:0007254; P:JNK cascade; TAS:Reactome.
DR GO; GO:0030324; P:lung development; IEA:Ensembl.
DR GO; GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; TAS:Reactome.
DR GO; GO:0070423; P:nucleotide-binding oligomerization domain containing signaling pathway; TAS:Reactome.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; TAS:Reactome.
DR GO; GO:0034166; P:toll-like receptor 10 signaling pathway; TAS:Reactome.
DR GO; GO:0034134; P:toll-like receptor 2 signaling pathway; TAS:Reactome.
DR GO; GO:0034138; P:toll-like receptor 3 signaling pathway; TAS:Reactome.
DR GO; GO:0034142; P:toll-like receptor 4 signaling pathway; TAS:Reactome.
DR GO; GO:0034146; P:toll-like receptor 5 signaling pathway; TAS:Reactome.
DR GO; GO:0034162; P:toll-like receptor 9 signaling pathway; TAS:Reactome.
DR GO; GO:0038123; P:toll-like receptor TLR1:TLR2 signaling pathway; TAS:Reactome.
DR GO; GO:0038124; P:toll-like receptor TLR6:TLR2 signaling pathway; TAS:Reactome.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0035666; P:TRIF-dependent toll-like receptor signaling pathway; TAS:Reactome.
DR Gene3D; 3.60.40.10; -; 1.
DR InterPro; IPR001932; PP2C-like_dom.
DR InterPro; IPR015655; Protein_Pase_2C.
DR PANTHER; PTHR13832; PTHR13832; 1.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; SSF81606; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome; Phosphoprotein;
KW Polymorphism; Reference proteome; Ubl conjugation.
FT CHAIN 1 504 TGF-beta-activated kinase 1 and MAP3K7-
FT binding protein 1.
FT /FTId=PRO_0000057797.
FT DOMAIN 64 368 PP2C-like.
FT COMPBIAS 452 457 Poly-Ser.
FT MOD_RES 7 7 Phosphoserine.
FT MOD_RES 378 378 Phosphoserine.
FT MOD_RES 438 438 Phosphoserine.
FT VAR_SEQ 436 504 NQSPTLTLQSTNTHTQSSSSSSDGGLFRSRPAHSLPPGEDG
FT RVEPYVDFAEFYRLWSVDHGEQSVVTAP -> KDPSRPASD
FT LTAIPQCQLNLLGSLTPG (in isoform 2).
FT /FTId=VSP_042024.
FT VARIANT 224 224 D -> E (in dbSNP:rs17001096).
FT /FTId=VAR_039271.
FT MUTAGEN 213 213 D->A: Loss of interaction with XIAP.
FT MUTAGEN 216 216 F->A: Loss of interaction with XIAP.
FT MUTAGEN 438 438 S->A: Loss of phosphorylation site.
FT TURN 18 20
FT STRAND 27 32
FT STRAND 35 37
FT STRAND 39 42
FT STRAND 51 58
FT TURN 59 61
FT STRAND 62 74
FT HELIX 75 86
FT STRAND 89 92
FT STRAND 94 96
FT HELIX 99 133
FT HELIX 141 143
FT HELIX 146 148
FT HELIX 149 162
FT STRAND 165 174
FT STRAND 177 185
FT STRAND 187 193
FT STRAND 195 202
FT HELIX 212 219
FT TURN 220 222
FT HELIX 225 231
FT STRAND 234 236
FT STRAND 239 241
FT HELIX 246 250
FT HELIX 252 254
FT TURN 256 260
FT STRAND 265 267
FT STRAND 271 277
FT STRAND 283 288
FT HELIX 290 300
FT STRAND 302 304
FT HELIX 305 319
FT HELIX 323 343
FT HELIX 348 351
FT STRAND 353 355
FT STRAND 358 366
FT STRAND 475 478
FT HELIX 485 495
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
//
ID TAB1_HUMAN Reviewed; 504 AA.
AC Q15750; Q2PP09; Q8IZW2;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 134.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Ueno N., Irie K., Nishida E., Matsumoto K.;
RT "TAB1: an activator of the TAK1 MAPKKK in TGF-beta signal
RT 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
RT interacts 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.,
RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
RA 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.,
RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
RA 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.,
RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
RA Khan A.S., Lane L., Tilahun Y., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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.,
RA Matsumoto K.;
RT "The kinase TAK1 can activate the NIK-I kappaB as well as the MAP
RT kinase cascade in the IL-1 signalling pathway.";
RL Nature 398:252-256(1999).
RN [8]
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 [9]
RP UBIQUITINATION, PHOSPHORYLATION AT SER-438, MUTAGENESIS OF SER-438,
RP AND DEUBIQUITINATION BY YOPP.
RX PubMed=16845370; DOI=10.1038/sj.embor.7400754;
RA Thiefes A., Wolf A., Doerrie A., Grassl G.A., Matsumoto K.,
RA Autenrieth I., Bohn E., Sakurai H., Niedenthal R., Resch K.,
RA Kracht M.;
RT "The Yersinia enterocolitica effector YopP inhibits host cell
RT signalling by inactivating the protein kinase TAK1 in the IL-1
RT signalling pathway.";
RL EMBO Rep. 7:838-844(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND MASS
RP SPECTROMETRY.
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.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND MASS
RP SPECTROMETRY.
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-378, AND MASS
RP SPECTROMETRY.
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 [13]
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
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.,
RA Buerckstuemmer T., 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 [15]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 1-401, AND ABSENCE OF
RP FUNCTION AS A 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 [16]
RP X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS) OF 1-370 IN COMPLEX WITH XIAP,
RP AND 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
RT BIR1 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. Interacts with TRAF6 and
CC MAP3K7; during IL-1 signaling. Identified in the TRIKA2 complex
CC composed of MAP3K7, TAB1 and TAB2.
CC -!- INTERACTION:
CC Q9NYJ8:TAB2; NbExp=3; IntAct=EBI-358643, EBI-358708;
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 Note=Does not bind nor activate MAP3K7/TAK1;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- PTM: Monoubiquitinated. Deubiquitinated by Y.enterocolitica YopP.
CC -!- SIMILARITY: Contains 1 PP2C-like domain.
CC -!- CAUTION: Lacks several key residues involved in metal-binding and
CC catalytic activity, therefore has lost phosphatase activity.
CC -----------------------------------------------------------------------
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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; CAB55304.1; -; Genomic_DNA.
DR EMBL; Z83845; CAQ07045.1; -; Genomic_DNA.
DR EMBL; CH471095; EAW60326.1; -; Genomic_DNA.
DR EMBL; BC050554; AAH50554.1; -; mRNA.
DR RefSeq; NP_006107.1; NM_006116.2.
DR RefSeq; NP_705717.1; NM_153497.2.
DR UniGene; Hs.507681; -.
DR UniGene; Hs.729080; -.
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; 4L53; X-ray; 2.55 A; A=468-496.
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; 4L53; -.
DR ProteinModelPortal; Q15750; -.
DR SMR; Q15750; 16-370, 468-496.
DR DIP; DIP-27524N; -.
DR IntAct; Q15750; 65.
DR MINT; MINT-88613; -.
DR BindingDB; Q15750; -.
DR ChEMBL; CHEMBL5605; -.
DR PhosphoSite; Q15750; -.
DR DMDM; 10720303; -.
DR PaxDb; Q15750; -.
DR PRIDE; Q15750; -.
DR DNASU; 10454; -.
DR Ensembl; ENST00000216160; ENSP00000216160; ENSG00000100324.
DR Ensembl; ENST00000331454; ENSP00000333049; ENSG00000100324.
DR GeneID; 10454; -.
DR KEGG; hsa:10454; -.
DR UCSC; uc003axt.3; human.
DR CTD; 10454; -.
DR GeneCards; GC22P039796; -.
DR HGNC; HGNC:18157; TAB1.
DR HPA; CAB032328; -.
DR MIM; 602615; gene.
DR neXtProt; NX_Q15750; -.
DR PharmGKB; PA30604; -.
DR eggNOG; NOG320352; -.
DR HOGENOM; HOG000044226; -.
DR HOVERGEN; HBG007302; -.
DR InParanoid; Q15750; -.
DR KO; K04403; -.
DR OMA; HPPEDNW; -.
DR OrthoDB; EOG7W41C0; -.
DR PhylomeDB; Q15750; -.
DR Reactome; REACT_6782; TRAF6 Mediated Induction of proinflammatory cytokines.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; Q15750; -.
DR ChiTaRS; TAB1; human.
DR EvolutionaryTrace; Q15750; -.
DR GeneWiki; MAP3K7IP1; -.
DR GenomeRNAi; 10454; -.
DR NextBio; 39627; -.
DR PRO; PR:Q15750; -.
DR ArrayExpress; Q15750; -.
DR Bgee; Q15750; -.
DR CleanEx; HS_MAP3K7IP1; -.
DR Genevestigator; Q15750; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0010008; C:endosome membrane; TAS:Reactome.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0008047; F:enzyme activator activity; TAS:ProtInc.
DR GO; GO:0019209; F:kinase activator activity; IEA:Ensembl.
DR GO; GO:0000187; P:activation of MAPK activity; TAS:Reactome.
DR GO; GO:0000185; P:activation of MAPKKK activity; TAS:ProtInc.
DR GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
DR GO; GO:0003007; P:heart morphogenesis; IEA:Ensembl.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB cascade; TAS:Reactome.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0045087; P:innate immune response; TAS:Reactome.
DR GO; GO:0007254; P:JNK cascade; TAS:Reactome.
DR GO; GO:0030324; P:lung development; IEA:Ensembl.
DR GO; GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; TAS:Reactome.
DR GO; GO:0070423; P:nucleotide-binding oligomerization domain containing signaling pathway; TAS:Reactome.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; TAS:Reactome.
DR GO; GO:0034166; P:toll-like receptor 10 signaling pathway; TAS:Reactome.
DR GO; GO:0034134; P:toll-like receptor 2 signaling pathway; TAS:Reactome.
DR GO; GO:0034138; P:toll-like receptor 3 signaling pathway; TAS:Reactome.
DR GO; GO:0034142; P:toll-like receptor 4 signaling pathway; TAS:Reactome.
DR GO; GO:0034146; P:toll-like receptor 5 signaling pathway; TAS:Reactome.
DR GO; GO:0034162; P:toll-like receptor 9 signaling pathway; TAS:Reactome.
DR GO; GO:0038123; P:toll-like receptor TLR1:TLR2 signaling pathway; TAS:Reactome.
DR GO; GO:0038124; P:toll-like receptor TLR6:TLR2 signaling pathway; TAS:Reactome.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0035666; P:TRIF-dependent toll-like receptor signaling pathway; TAS:Reactome.
DR Gene3D; 3.60.40.10; -; 1.
DR InterPro; IPR001932; PP2C-like_dom.
DR InterPro; IPR015655; Protein_Pase_2C.
DR PANTHER; PTHR13832; PTHR13832; 1.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; SSF81606; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome; Phosphoprotein;
KW Polymorphism; Reference proteome; Ubl conjugation.
FT CHAIN 1 504 TGF-beta-activated kinase 1 and MAP3K7-
FT binding protein 1.
FT /FTId=PRO_0000057797.
FT DOMAIN 64 368 PP2C-like.
FT COMPBIAS 452 457 Poly-Ser.
FT MOD_RES 7 7 Phosphoserine.
FT MOD_RES 378 378 Phosphoserine.
FT MOD_RES 438 438 Phosphoserine.
FT VAR_SEQ 436 504 NQSPTLTLQSTNTHTQSSSSSSDGGLFRSRPAHSLPPGEDG
FT RVEPYVDFAEFYRLWSVDHGEQSVVTAP -> KDPSRPASD
FT LTAIPQCQLNLLGSLTPG (in isoform 2).
FT /FTId=VSP_042024.
FT VARIANT 224 224 D -> E (in dbSNP:rs17001096).
FT /FTId=VAR_039271.
FT MUTAGEN 213 213 D->A: Loss of interaction with XIAP.
FT MUTAGEN 216 216 F->A: Loss of interaction with XIAP.
FT MUTAGEN 438 438 S->A: Loss of phosphorylation site.
FT TURN 18 20
FT STRAND 27 32
FT STRAND 35 37
FT STRAND 39 42
FT STRAND 51 58
FT TURN 59 61
FT STRAND 62 74
FT HELIX 75 86
FT STRAND 89 92
FT STRAND 94 96
FT HELIX 99 133
FT HELIX 141 143
FT HELIX 146 148
FT HELIX 149 162
FT STRAND 165 174
FT STRAND 177 185
FT STRAND 187 193
FT STRAND 195 202
FT HELIX 212 219
FT TURN 220 222
FT HELIX 225 231
FT STRAND 234 236
FT STRAND 239 241
FT HELIX 246 250
FT HELIX 252 254
FT TURN 256 260
FT STRAND 265 267
FT STRAND 271 277
FT STRAND 283 288
FT HELIX 290 300
FT STRAND 302 304
FT HELIX 305 319
FT HELIX 323 343
FT HELIX 348 351
FT STRAND 353 355
FT STRAND 358 366
FT STRAND 475 478
FT HELIX 485 495
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
//
MIM
602615
*RECORD*
*FIELD* NO
602615
*FIELD* TI
*602615 MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 7-INTERACTING PROTEIN
1; MAP3K7IP1
read more;;TAK1-BINDING PROTEIN 1; TAB1
*FIELD* TX
CLONING
Shibuya et al. (1996) used the yeast 2-hybrid system to identify brain
cDNAs encoding proteins that interacted with TAK1 (602614). They
recovered a gene encoding a predicted 504-amino acid protein that they
named TAB1 (TAK1-binding protein-1). On Northern blots, TAB1 was
expressed as a 3.5-kb mRNA in all tissues tested.
GENE FUNCTION
Shibuya et al. (1996) found that in both yeast and mammalian cells, TAB1
activated the kinase activity of TAK1 by direct interaction. They showed
that the C-terminal 68 amino acids of TAB1 are sufficient for binding
and activation of TAK1 in mammalian cells, while the N-terminal 418
amino acids act as a dominant-negative inhibitor of transforming growth
factor-beta (TGFB; 190180)-induced gene expression. Since TAK1 functions
as an MAPKKK in the TGFB signaling pathway, Shibuya et al. (1996)
suggested that TAB1 may be an important signaling intermediate between
TGFB receptors and TAK1.
Using a yeast 2-hybrid screen of gastrointestinal tract tissue with
p38-alpha (MAPK14; 600289) as the bait, Ge et al. (2002) isolated
multiple clones encoding TAB1. Immunoprecipitation and GST pull-down
analyses indicated that TAB1 interacts with p38-alpha, but not with
other MAPKs, with or without treatment with TNF (191160). Immunoblot
analysis showed that coexpression of TAB1 and p38-alpha enhanced
autophosphorylation of p38-alpha even in the presence of
dominant-negative forms of MAP2Ks (e.g., MAP2K3; 602315) and TAK1. The
amino acids between positions 373 and 418 of TAB1 were found to be
required for phosphorylation of p38-alpha. Expression of TLR2 (603028)
caused p38-alpha phosphorylation in the presence or absence of
inhibitors, whereas p38-alpha phosphorylation after stimulation of TLR4
(603030) could be inhibited by mutant TAB1, suggesting that activation
of p38-alpha can be TAB1 dependent or independent. Immunoblot analysis
detected the formation of TRAF6 (602355)-TAB1-p38-alpha complexes.
Formation of these complexes could be enhanced by stimulation with
lipopolysaccharide. Ge et al. (2002) concluded that activation of
p38-alpha by a nonenzymatic adaptor protein such as TAB1 may be an
important alternative activation pathway operating in parallel with
kinase cascades in regulating intracellular signaling.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the TAB1
gene to chromosome 22 (TMAP WI-18691).
*FIELD* RF
1. Ge, B.; Gram, H.; Di Padova, F.; Huang, B.; New, L.; Ulevitch,
R. J.; Luo, Y.; Han, J.: MAPKK-independent activation of p38-alpha
mediated by TAB1-dependent autophosphorylation of p38-alpha. Science 295:
1291-1294, 2002.
2. 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.
*FIELD* CN
Joanna S. Amberger - updated: 03/12/2002
Paul J. Converse - updated: 2/18/2002
*FIELD* CD
Rebekah S. Rasooly: 5/11/1998
*FIELD* ED
joanna: 03/12/2002
mgross: 2/18/2002
mgross: 6/30/2000
dkim: 9/11/1998
alopez: 5/11/1998
*RECORD*
*FIELD* NO
602615
*FIELD* TI
*602615 MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 7-INTERACTING PROTEIN
1; MAP3K7IP1
read more;;TAK1-BINDING PROTEIN 1; TAB1
*FIELD* TX
CLONING
Shibuya et al. (1996) used the yeast 2-hybrid system to identify brain
cDNAs encoding proteins that interacted with TAK1 (602614). They
recovered a gene encoding a predicted 504-amino acid protein that they
named TAB1 (TAK1-binding protein-1). On Northern blots, TAB1 was
expressed as a 3.5-kb mRNA in all tissues tested.
GENE FUNCTION
Shibuya et al. (1996) found that in both yeast and mammalian cells, TAB1
activated the kinase activity of TAK1 by direct interaction. They showed
that the C-terminal 68 amino acids of TAB1 are sufficient for binding
and activation of TAK1 in mammalian cells, while the N-terminal 418
amino acids act as a dominant-negative inhibitor of transforming growth
factor-beta (TGFB; 190180)-induced gene expression. Since TAK1 functions
as an MAPKKK in the TGFB signaling pathway, Shibuya et al. (1996)
suggested that TAB1 may be an important signaling intermediate between
TGFB receptors and TAK1.
Using a yeast 2-hybrid screen of gastrointestinal tract tissue with
p38-alpha (MAPK14; 600289) as the bait, Ge et al. (2002) isolated
multiple clones encoding TAB1. Immunoprecipitation and GST pull-down
analyses indicated that TAB1 interacts with p38-alpha, but not with
other MAPKs, with or without treatment with TNF (191160). Immunoblot
analysis showed that coexpression of TAB1 and p38-alpha enhanced
autophosphorylation of p38-alpha even in the presence of
dominant-negative forms of MAP2Ks (e.g., MAP2K3; 602315) and TAK1. The
amino acids between positions 373 and 418 of TAB1 were found to be
required for phosphorylation of p38-alpha. Expression of TLR2 (603028)
caused p38-alpha phosphorylation in the presence or absence of
inhibitors, whereas p38-alpha phosphorylation after stimulation of TLR4
(603030) could be inhibited by mutant TAB1, suggesting that activation
of p38-alpha can be TAB1 dependent or independent. Immunoblot analysis
detected the formation of TRAF6 (602355)-TAB1-p38-alpha complexes.
Formation of these complexes could be enhanced by stimulation with
lipopolysaccharide. Ge et al. (2002) concluded that activation of
p38-alpha by a nonenzymatic adaptor protein such as TAB1 may be an
important alternative activation pathway operating in parallel with
kinase cascades in regulating intracellular signaling.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the TAB1
gene to chromosome 22 (TMAP WI-18691).
*FIELD* RF
1. Ge, B.; Gram, H.; Di Padova, F.; Huang, B.; New, L.; Ulevitch,
R. J.; Luo, Y.; Han, J.: MAPKK-independent activation of p38-alpha
mediated by TAB1-dependent autophosphorylation of p38-alpha. Science 295:
1291-1294, 2002.
2. 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.
*FIELD* CN
Joanna S. Amberger - updated: 03/12/2002
Paul J. Converse - updated: 2/18/2002
*FIELD* CD
Rebekah S. Rasooly: 5/11/1998
*FIELD* ED
joanna: 03/12/2002
mgross: 2/18/2002
mgross: 6/30/2000
dkim: 9/11/1998
alopez: 5/11/1998