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