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TAB1_CAEEL
ID   TAB1_CAEEL              Reviewed;         386 AA.
AC   G5EEM6;
DT   06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=TGF-beta-activated kinase 1 and MAP3K7-binding protein 1 {ECO:0000250|UniProtKB:Q15750};
DE   AltName: Full=TAB1-like protein 1 {ECO:0000303|PubMed:10391246};
DE   AltName: Full=TAK1 kinase/MOM-4 binding Protein {ECO:0000312|WormBase:C44H4.5};
GN   Name=tap-1 {ECO:0000312|WormBase:C44H4.5};
GN   ORFNames=C44H4.5 {ECO:0000312|WormBase:C44H4.5};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN   [1] {ECO:0000312|EMBL:AAD39814.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH MOM-4, AND
RP   DISRUPTION PHENOTYPE.
RX   PubMed=10391246; DOI=10.1038/21666;
RA   Meneghini M.D., Ishitani T., Carter J.C., Hisamoto N., Ninomiya-Tsuji J.,
RA   Thorpe C.J., Hamill D.R., Matsumoto K., Bowerman B.;
RT   "MAP kinase and Wnt pathways converge to downregulate an HMG-domain
RT   repressor in Caenorhabditis elegans.";
RL   Nature 399:793-797(1999).
RN   [2] {ECO:0000312|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [3] {ECO:0000305}
RP   FUNCTION, INTERACTION WITH MOM-4, AND MUTAGENESIS OF ALA-364.
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).
CC   -!- FUNCTION: Involved in the Wnt signaling pathway by regulating mom-4
CC       kinase activity. {ECO:0000269|PubMed:10391246,
CC       ECO:0000269|PubMed:11323434}.
CC   -!- SUBUNIT: Interacts with mom-4; the interaction enhances mom-4 kinase
CC       activity. {ECO:0000269|PubMed:10391246, ECO:0000269|PubMed:11323434}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes no obvious
CC       phenotype. Results in a 3-fold increase in the number of animals
CC       lacking a gut in a mom-4 (or11) mutant background.
CC       {ECO:0000269|PubMed:10391246}.
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; AF145375; AAD39814.1; -; mRNA.
DR   EMBL; BX284606; CAB01866.1; -; Genomic_DNA.
DR   PIR; T19940; T19940.
DR   RefSeq; NP_510428.1; NM_078027.4.
DR   AlphaFoldDB; G5EEM6; -.
DR   SMR; G5EEM6; -.
DR   IntAct; G5EEM6; 2.
DR   STRING; 6239.C44H4.5; -.
DR   EPD; G5EEM6; -.
DR   PaxDb; G5EEM6; -.
DR   PeptideAtlas; G5EEM6; -.
DR   EnsemblMetazoa; C44H4.5.1; C44H4.5.1; WBGene00006524.
DR   GeneID; 181556; -.
DR   KEGG; cel:CELE_C44H4.5; -.
DR   CTD; 181556; -.
DR   WormBase; C44H4.5; CE08726; WBGene00006524; tap-1.
DR   eggNOG; KOG0698; Eukaryota.
DR   HOGENOM; CLU_767943_0_0_1; -.
DR   InParanoid; G5EEM6; -.
DR   OMA; NTRCLGN; -.
DR   OrthoDB; 892993at2759; -.
DR   PhylomeDB; G5EEM6; -.
DR   Reactome; R-CEL-1169408; ISG15 antiviral mechanism.
DR   Reactome; R-CEL-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
DR   Reactome; R-CEL-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
DR   SignaLink; G5EEM6; -.
DR   PRO; PR:G5EEM6; -.
DR   Proteomes; UP000001940; Chromosome X.
DR   Bgee; WBGene00006524; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; IPI:WormBase.
DR   GO; GO:0030295; F:protein kinase activator activity; IDA:WormBase.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central.
DR   GO; GO:0001714; P:endodermal cell fate specification; IGI:WormBase.
DR   GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IMP:WormBase.
DR   GO; GO:0032873; P:negative regulation of stress-activated MAPK cascade; IBA:GO_Central.
DR   GO; GO:0035970; P:peptidyl-threonine dephosphorylation; IBA:GO_Central.
DR   GO; GO:0045860; P:positive regulation of protein kinase activity; IDA:WormBase.
DR   CDD; cd00143; PP2Cc; 1.
DR   Gene3D; 3.60.40.10; -; 1.
DR   InterPro; IPR036457; PPM-type_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase_dom.
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   Reference proteome.
FT   CHAIN           1..386
FT                   /note="TGF-beta-activated kinase 1 and MAP3K7-binding
FT                   protein 1"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000436906"
FT   DOMAIN          22..327
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT   SITE            364
FT                   /note="Required for interaction with mom-4"
FT                   /evidence="ECO:0000269|PubMed:11323434"
FT   MUTAGEN         364
FT                   /note="A->P: Abolishes interaction with mom-4."
FT                   /evidence="ECO:0000269|PubMed:11323434"
SQ   SEQUENCE   386 AA;  43469 MW;  957D1DC9F2914554 CRC64;
     MGDDGFLDQY PANTDAGIGT VHSCRYSKQK NPVQNNDFLS CSMCIHNGPI KLYGIFSGFN
     GGDSTAKFVM NRLVYEIFGE NPITPTLLPY QVVEEFKRKF ENVAERYLLM NTDDLNNRLL
     KLEEQSETGN NAVSEINQKI RQGTTAIVVM IINQDLYVLN CGNSLAIAMN SENVVQLNSN
     LHNNDNPLEI VRIKGLGINP ETVLNPTRAI GDLQRTHLFE ETEAFKNAKG PPVISTPDVQ
     YTKIDPSWRH LVLISDGVVQ NLKEVEVENI PTEVSVRLIE DHTVTSTAQA LVDSFARKHR
     DAYTMSDDKN FCISNHREEM TVIYVKLEED YQAALYEQFD SAISTMESTN ATLYEPCSTP
     YVDATNFNSG KNYEKMKKLL LTRPSK
 
 
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