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TOB1_MOUSE
ID   TOB1_MOUSE              Reviewed;         362 AA.
AC   Q61471; Q640M3;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   18-SEP-2013, sequence version 2.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Protein Tob1;
DE   AltName: Full=Transducer of erbB-2 1;
GN   Name=Tob1; Synonyms=Tob, Trob;
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 [GENOMIC DNA].
RC   STRAIN=129/SvJ; TISSUE=Liver;
RX   PubMed=9210596; DOI=10.1016/s0378-1119(97)00049-8;
RA   Yoshida Y., Matuda S., Yamamoto T.;
RT   "Cloning and characterization of the mouse tob gene.";
RL   Gene 191:109-113(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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   [4]
RP   SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL, NUCLEAR EXPORT SIGNAL,
RP   AND MUTAGENESIS OF 22-ARG--ARG-24; 37-LYS--LYS-39; LEU-234 AND LEU-236.
RX   PubMed=15235587; DOI=10.1038/sj.onc.1207890;
RA   Kawamura-Tsuzuku J., Suzuki T., Yoshida Y., Yamamoto T.;
RT   "Nuclear localization of Tob is important for regulation of its
RT   antiproliferative activity.";
RL   Oncogene 23:6630-6638(2004).
CC   -!- FUNCTION: Anti-proliferative protein; the function is mediated by
CC       association with deadenylase subunits of the CCR4-NOT complex. Mediates
CC       CPEB3-accelerated mRNA deadenylation by binding to CPEB3 and recruiting
CC       CNOT7 which leads to target mRNA deadenylation and decay.
CC       {ECO:0000250|UniProtKB:P50616}.
CC   -!- SUBUNIT: Interacts with ERBB2. Interacts with CNOT7. Interacts with
CC       CPEB3 (via C-terminal RNA-binding region); recruits CNOT7 to CPEB3 to
CC       form a ternary complex required for mRNA deadenylation and decay.
CC       Interacts with CNOT8. Interacts with CPEB4.
CC       {ECO:0000250|UniProtKB:P50616, ECO:0000250|UniProtKB:Q8R5K6}.
CC   -!- INTERACTION:
CC       Q61471; P57737: CORO7; Xeno; NbExp=3; IntAct=EBI-8527498, EBI-6916167;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15235587}. Nucleus
CC       {ECO:0000269|PubMed:15235587}. Note=Only a small fraction localizes to
CC       the cytoplasm except in late S-phase where more than half of proteins
CC       become cytoplasmic.
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- PTM: Phosphorylated on Ser and Thr residues. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the BTG family. {ECO:0000305}.
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DR   EMBL; D78382; BAA11384.1; -; Genomic_DNA.
DR   EMBL; AL645846; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC082588; AAH82588.1; -; mRNA.
DR   CCDS; CCDS25250.1; -.
DR   RefSeq; NP_033453.2; NM_009427.2.
DR   AlphaFoldDB; Q61471; -.
DR   SMR; Q61471; -.
DR   BioGRID; 204322; 2.
DR   IntAct; Q61471; 1.
DR   MINT; Q61471; -.
DR   STRING; 10090.ENSMUSP00000036039; -.
DR   iPTMnet; Q61471; -.
DR   PhosphoSitePlus; Q61471; -.
DR   PaxDb; Q61471; -.
DR   PRIDE; Q61471; -.
DR   ProteomicsDB; 259485; -.
DR   Antibodypedia; 4398; 295 antibodies from 32 providers.
DR   DNASU; 22057; -.
DR   Ensembl; ENSMUST00000041589; ENSMUSP00000036039; ENSMUSG00000037573.
DR   GeneID; 22057; -.
DR   KEGG; mmu:22057; -.
DR   UCSC; uc007kyf.1; mouse.
DR   CTD; 10140; -.
DR   MGI; MGI:1349721; Tob1.
DR   VEuPathDB; HostDB:ENSMUSG00000037573; -.
DR   eggNOG; KOG4006; Eukaryota.
DR   GeneTree; ENSGT00940000154208; -.
DR   HOGENOM; CLU_034687_0_0_1; -.
DR   InParanoid; Q61471; -.
DR   OMA; MKNSGRG; -.
DR   OrthoDB; 1439942at2759; -.
DR   PhylomeDB; Q61471; -.
DR   TreeFam; TF105274; -.
DR   BioGRID-ORCS; 22057; 2 hits in 74 CRISPR screens.
DR   ChiTaRS; Tob1; mouse.
DR   PRO; PR:Q61471; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q61471; protein.
DR   Bgee; ENSMUSG00000037573; Expressed in extensor digitorum longus and 259 other tissues.
DR   Genevisible; Q61471; MM.
DR   GO; GO:0030014; C:CCR4-NOT complex; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0030971; F:receptor tyrosine kinase binding; ISS:UniProtKB.
DR   GO; GO:0046332; F:SMAD binding; IDA:MGI.
DR   GO; GO:0003714; F:transcription corepressor activity; IDA:MGI.
DR   GO; GO:0030514; P:negative regulation of BMP signaling pathway; IDA:MGI.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR   GO; GO:0060212; P:negative regulation of nuclear-transcribed mRNA poly(A) tail shortening; ISS:UniProtKB.
DR   GO; GO:0045668; P:negative regulation of osteoblast differentiation; IMP:MGI.
DR   GO; GO:0017148; P:negative regulation of translation; ISS:UniProtKB.
DR   GO; GO:1900153; P:positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; ISS:UniProtKB.
DR   GO; GO:0060213; P:positive regulation of nuclear-transcribed mRNA poly(A) tail shortening; ISS:UniProtKB.
DR   GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR   GO; GO:0060390; P:regulation of SMAD protein signal transduction; IDA:MGI.
DR   Gene3D; 3.90.640.90; -; 1.
DR   InterPro; IPR002087; Anti_prolifrtn.
DR   InterPro; IPR036054; BTG-like_sf.
DR   InterPro; IPR015677; Tob1.
DR   InterPro; IPR015676; Tob1/2.
DR   PANTHER; PTHR17537; PTHR17537; 1.
DR   PANTHER; PTHR17537:SF6; PTHR17537:SF6; 1.
DR   Pfam; PF07742; BTG; 1.
DR   PRINTS; PR00310; ANTIPRLFBTG1.
DR   SMART; SM00099; btg1; 1.
DR   SUPFAM; SSF160696; SSF160696; 1.
DR   PROSITE; PS00960; BTG_1; 1.
DR   PROSITE; PS01203; BTG_2; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..362
FT                   /note="Protein Tob1"
FT                   /id="PRO_0000143813"
FT   REGION          82..92
FT                   /note="Important for nuclear localization"
FT   REGION          144..171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          161..220
FT                   /note="Required for interaction with CPEB3"
FT                   /evidence="ECO:0000250|UniProtKB:P50616"
FT   REGION          234..284
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           22..39
FT                   /note="Bipartite nuclear localization signal"
FT   MOTIF           228..236
FT                   /note="Nuclear export signal"
FT   COMPBIAS        234..254
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        268..284
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         204
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P50616"
FT   MUTAGEN         22..24
FT                   /note="RRR->QQQ: Localizes to cytoplasm; when associated
FT                   with 37-NNN-39."
FT                   /evidence="ECO:0000269|PubMed:15235587"
FT   MUTAGEN         37..39
FT                   /note="KKK->NNN: Localizes to cytoplasm; when associated
FT                   with 22-QQQ-24."
FT                   /evidence="ECO:0000269|PubMed:15235587"
FT   MUTAGEN         234
FT                   /note="L->A: Not exported to the cytoplasm; when associated
FT                   with A-236."
FT                   /evidence="ECO:0000269|PubMed:15235587"
FT   MUTAGEN         236
FT                   /note="L->A: Not exported to the cytoplasm; when associated
FT                   with A-234."
FT                   /evidence="ECO:0000269|PubMed:15235587"
FT   CONFLICT        136
FT                   /note="A -> P (in Ref. 1; BAA11384)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        217
FT                   /note="D -> H (in Ref. 1; BAA11384)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        271
FT                   /note="P -> PQ (in Ref. 1; BAA11384)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   362 AA;  40056 MW;  4D4F1F492A7CA6FC CRC64;
     MQLEIQVALN FIISYLYNKL PRRRVNIFGE ELERLLKKKY EGHWYPEKPY KGSGFRCIHV
     GEKVDPVIEQ ASKESGLDID DVRGNLPQDL SVWIDPFEVS YQIGEKGPVK VLYVDDSSET
     GCELDKEIKN SFNPEAQVFM PISDPASSVS SSPSPPFGHS AAVSPTFMPR STQPLTFTTA
     TFAATKFGST KMKNSGRSSK VARTSPINLG LTVNVNDLLK QKAISSSVHS LYGLGLGSQQ
     QPQPQPQQQQ QQQPSSSQPP PPLPQQQQQQ PQQQQQQQQQ TSALSPNAKE FIFPNMQGQG
     SSTNGMFPGD SPLNLSPLQY SNAFDVFAAY GGLNEKSFVD GLNFSLNNMQ YSNQQFQPVM
     AN
 
 
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