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MCRI1_RAT
ID   MCRI1_RAT               Reviewed;          97 AA.
AC   B0BN72;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Mapk-regulated corepressor-interacting protein 1;
DE   AltName: Full=Protein FAM195B;
GN   Name=Mcrip1; Synonyms=Fam195b;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
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-21, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: The phosphorylation status of MCRIP1 functions as a molecular
CC       switch to regulate epithelial-mesenchymal transition. Unphosphorylated
CC       MCRIP1 binds to and inhibits the transcriptional corepressor CTBP(s).
CC       When phosphorylated by MAPK/ERK, MCRIP1 releases CTBP(s) resulting in
CC       transcriptional silencing of the E-cadherin gene and induction of
CC       epithelial-mesenchymal transition. {ECO:0000250|UniProtKB:C9JLW8}.
CC   -!- SUBUNIT: Interacts (unphosphorylated form, via the PXDLS motif) with
CC       CTBP1, competitively inhibiting CTBP-ZEB1 interaction. Interacts with
CC       CTBP2. Interacts with MCRIP2. Interacts with DDX6.
CC       {ECO:0000250|UniProtKB:C9JLW8}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:C9JLW8}.
CC       Cytoplasm, Stress granule {ECO:0000250|UniProtKB:C9JLW8}.
CC   -!- PTM: Phosphorylation by MAPK3/1 (ERK1/2) regulates MCRIP1 binding to
CC       CTBP(s). {ECO:0000250|UniProtKB:C9JLW8}.
CC   -!- SIMILARITY: Belongs to the MCRIP family. {ECO:0000305}.
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DR   EMBL; CH473948; EDM06851.1; -; Genomic_DNA.
DR   EMBL; BC158709; AAI58710.1; -; mRNA.
DR   RefSeq; NP_001101781.1; NM_001108311.1.
DR   RefSeq; XP_006247958.1; XM_006247896.3.
DR   RefSeq; XP_017452903.1; XM_017597414.1.
DR   AlphaFoldDB; B0BN72; -.
DR   SMR; B0BN72; -.
DR   STRING; 10116.ENSRNOP00000051843; -.
DR   iPTMnet; B0BN72; -.
DR   PhosphoSitePlus; B0BN72; -.
DR   jPOST; B0BN72; -.
DR   PaxDb; B0BN72; -.
DR   PeptideAtlas; B0BN72; -.
DR   PRIDE; B0BN72; -.
DR   GeneID; 360677; -.
DR   KEGG; rno:360677; -.
DR   CTD; 348262; -.
DR   RGD; 1311925; Mcrip1.
DR   VEuPathDB; HostDB:ENSRNOG00000036691; -.
DR   eggNOG; ENOG502S25D; Eukaryota.
DR   HOGENOM; CLU_161057_0_0_1; -.
DR   InParanoid; B0BN72; -.
DR   OMA; QNHERND; -.
DR   OrthoDB; 1461250at2759; -.
DR   PhylomeDB; B0BN72; -.
DR   TreeFam; TF326620; -.
DR   PRO; PR:B0BN72; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   Proteomes; UP000234681; Chromosome 10.
DR   Bgee; ENSRNOG00000036691; Expressed in heart and 18 other tissues.
DR   Genevisible; B0BN72; RN.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0010717; P:regulation of epithelial to mesenchymal transition; ISS:UniProtKB.
DR   InterPro; IPR029428; MCRIP.
DR   Pfam; PF14799; FAM195; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..97
FT                   /note="Mapk-regulated corepressor-interacting protein 1"
FT                   /id="PRO_0000393956"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           80..84
FT                   /note="PXDLS motif"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         21
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         30
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:C9JLW8"
FT   MOD_RES         41
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UGS4"
FT   MOD_RES         79
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:C9JLW8"
SQ   SEQUENCE   97 AA;  11101 MW;  50792192F1C63720 CRC64;
     MTSSPVSRVV YNGKRNSSPR SPTNSSEIFT PAHEENVRFI YEAWQGVERD LRSQLSSGER
     CLVEEYVEKV PNPSLKTFKP IDLSDLKRRN TQDAKKS
 
 
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