TAB1_MOUSE
ID TAB1_MOUSE Reviewed; 502 AA.
AC Q8CF89; Q7TQJ5; Q80V65; Q8R0D1;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 2.
DT 03-AUG-2022, entry version 135.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12464436; DOI=10.1016/s0925-4773(02)00391-x;
RA Komatsu Y., Shibuya H., Takeda N., Ninomiya-Tsuji J., Yasui T., Miyado K.,
RA Sekimoto T., Ueno N., Matsumoto K., Yamada G.;
RT "Targeted disruption of the Tab1 gene causes embryonic lethality and
RT defects in cardiovascular and lung morphogenesis.";
RL Mech. Dev. 119:239-249(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Eye, Kidney, and Mammary tumor;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Lung, Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q8CF89; P53349: Map3k1; NbExp=4; IntAct=EBI-1778503, EBI-447913;
CC Q8CF89; Q62073: Map3k7; NbExp=2; IntAct=EBI-1778503, EBI-1775345;
CC Q8CF89; Q86Y07-1: VRK2; Xeno; NbExp=2; IntAct=EBI-1778503, EBI-1207633;
CC -!- PTM: Monoubiquitinated. {ECO:0000250}.
CC -!- CAUTION: Lacks several key residues involved in metal-binding and
CC catalytic activity, therefore has lost phosphatase activity.
CC {ECO:0000250|UniProtKB:Q15750}.
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DR EMBL; AB088136; BAC43729.1; -; mRNA.
DR EMBL; BC027054; AAH27054.1; -; mRNA.
DR EMBL; BC041110; AAH41110.1; -; mRNA.
DR EMBL; BC054369; AAH54369.1; -; mRNA.
DR CCDS; CCDS27659.1; -.
DR RefSeq; NP_079885.2; NM_025609.2.
DR PDB; 4LOO; X-ray; 1.95 A; B=384-412.
DR PDB; 4LOP; X-ray; 2.05 A; K/L/M/N=384-412.
DR PDB; 4LOQ; X-ray; 2.32 A; K/L/M/N=384-412.
DR PDBsum; 4LOO; -.
DR PDBsum; 4LOP; -.
DR PDBsum; 4LOQ; -.
DR AlphaFoldDB; Q8CF89; -.
DR SMR; Q8CF89; -.
DR BioGRID; 211528; 12.
DR ELM; Q8CF89; -.
DR IntAct; Q8CF89; 12.
DR MINT; Q8CF89; -.
DR STRING; 10090.ENSMUSP00000023050; -.
DR iPTMnet; Q8CF89; -.
DR PhosphoSitePlus; Q8CF89; -.
DR EPD; Q8CF89; -.
DR MaxQB; Q8CF89; -.
DR PaxDb; Q8CF89; -.
DR PeptideAtlas; Q8CF89; -.
DR PRIDE; Q8CF89; -.
DR ProteomicsDB; 253463; -.
DR Antibodypedia; 12659; 646 antibodies from 44 providers.
DR DNASU; 66513; -.
DR Ensembl; ENSMUST00000023050; ENSMUSP00000023050; ENSMUSG00000022414.
DR GeneID; 66513; -.
DR KEGG; mmu:66513; -.
DR UCSC; uc007wve.1; mouse.
DR CTD; 10454; -.
DR MGI; MGI:1913763; Tab1.
DR VEuPathDB; HostDB:ENSMUSG00000022414; -.
DR eggNOG; KOG0698; Eukaryota.
DR GeneTree; ENSGT00510000048276; -.
DR HOGENOM; CLU_027717_1_0_1; -.
DR InParanoid; Q8CF89; -.
DR OMA; NTRCLGN; -.
DR OrthoDB; 755673at2759; -.
DR PhylomeDB; Q8CF89; -.
DR TreeFam; TF317785; -.
DR Reactome; R-MMU-168638; NOD1/2 Signaling Pathway.
DR Reactome; R-MMU-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-MMU-450302; activated TAK1 mediates p38 MAPK activation.
DR Reactome; R-MMU-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
DR Reactome; R-MMU-5357956; TNFR1-induced NFkappaB signaling pathway.
DR Reactome; R-MMU-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR Reactome; R-MMU-9020702; Interleukin-1 signaling.
DR Reactome; R-MMU-937042; IRAK2 mediated activation of TAK1 complex.
DR Reactome; R-MMU-937072; TRAF6-mediated induction of TAK1 complex within TLR4 complex.
DR Reactome; R-MMU-9645460; Alpha-protein kinase 1 signaling pathway.
DR Reactome; R-MMU-975163; IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation.
DR BioGRID-ORCS; 66513; 15 hits in 74 CRISPR screens.
DR ChiTaRS; Tab1; mouse.
DR PRO; PR:Q8CF89; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q8CF89; protein.
DR Bgee; ENSMUSG00000022414; Expressed in dorsal pancreas and 210 other tissues.
DR ExpressionAtlas; Q8CF89; baseline and differential.
DR Genevisible; Q8CF89; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0019209; F:kinase activator activity; IMP:MGI.
DR GO; GO:0048273; F:mitogen-activated protein kinase p38 binding; ISO:MGI.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0035904; P:aorta development; IMP:MGI.
DR GO; GO:0003279; P:cardiac septum development; IMP:MGI.
DR GO; GO:0060976; P:coronary vasculature development; IMP:MGI.
DR GO; GO:0003007; P:heart morphogenesis; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0030324; P:lung development; IMP:MGI.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; ISO:MGI.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:MGI.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; ISO:MGI.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IMP:MGI.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 3.60.40.10; -; 1.
DR IDEAL; IID50233; -.
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; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..502
FT /note="TGF-beta-activated kinase 1 and MAP3K7-binding
FT protein 1"
FT /id="PRO_0000057798"
FT DOMAIN 28..365
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..476
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 414..460
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 482
FT /note="Required for interaction with MAP3K7"
FT /evidence="ECO:0000250|UniProtKB:Q15750"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 436
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15750"
FT MOD_RES 440
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15750"
FT CONFLICT 199
FT /note="Q -> H (in Ref. 1; BAC43729)"
FT /evidence="ECO:0000305"
FT CONFLICT 210..212
FT /note="ENE -> DND (in Ref. 1; BAC43729)"
FT /evidence="ECO:0000305"
FT CONFLICT 323
FT /note="L -> P (in Ref. 1; BAC43729)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 502 AA; 54616 MW; F7529D2E3CF30696 CRC64;
MAAQRRSLLQ SEQQPSWTDD LPLCHLSGVG SASNRSYSAD GKGTESHPPE DNWLKFRSEN
NCFLYGVFNG YDGNRVTNFV AQRLSAELLL GQLNTEHTEA DVRRVLLQAF DVVERSFLES
IDDALAEKAS LQSQLPEGVP QHQLPPQYQK ILERLKALER EISGGAMAVV AVLLNSKLYV
ANVGTNRALL CKSTVDGLQV TQLNMDHTTE NEDELFRLSQ LGLDAGKIKQ MGVICGQEST
RRIGDYKVKY GYTDIDLLSA AKSKPIIAEP EIHGAQPLDG VTGFLVLMSE GLYKALEAAH
GPGQANQEIA AMIDTEFAKQ TSLDAVAQAV VDRVKRIHSD TFASGGERAK FCPRHEDMTL
LVRNFGYPLG EMSQPTPTPA PGGRVYPVSV PYSSAQSTSK TSVTLSLVMP SQGQMVNGSH
SASTLDEATP TLTNQSPTLT LQSTNTHTQS SSSSSDGGLF RSRPAHSLPP GEDGRVEPYV
DFAEFYRLWS VDHGEQSVMT AP
