MCRI1_MOUSE
ID MCRI1_MOUSE Reviewed; 97 AA.
AC Q3UGS4; Q8QZS4;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Mapk-regulated corepressor-interacting protein 1;
DE AltName: Full=Protein FAM195B;
GN Name=Mcrip1; Synonyms=Fam195b;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
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 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-41, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Lung, Spleen, and Testis;
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).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=25728771; DOI=10.1016/j.molcel.2015.01.023;
RA Ichikawa K., Kubota Y., Nakamura T., Weng J.S., Tomida T., Saito H.,
RA Takekawa M.;
RT "MCRIP1, an ERK substrate, mediates ERK-induced gene silencing during
RT epithelial-mesenchymal transition by regulating the co-repressor CtBP.";
RL Mol. Cell 58:35-46(2015).
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 -!- TISSUE SPECIFICITY: Widely expressed (at protein level).
CC {ECO:0000269|PubMed:25728771}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH25536.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK147780; BAE28133.1; -; mRNA.
DR EMBL; AL669855; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466558; EDL34763.1; -; Genomic_DNA.
DR EMBL; BC025536; AAH25536.1; ALT_INIT; mRNA.
DR CCDS; CCDS36391.1; -.
DR RefSeq; NP_001028403.1; NM_001033231.2.
DR AlphaFoldDB; Q3UGS4; -.
DR SMR; Q3UGS4; -.
DR BioGRID; 228660; 9.
DR STRING; 10090.ENSMUSP00000034913; -.
DR iPTMnet; Q3UGS4; -.
DR PhosphoSitePlus; Q3UGS4; -.
DR EPD; Q3UGS4; -.
DR jPOST; Q3UGS4; -.
DR MaxQB; Q3UGS4; -.
DR PaxDb; Q3UGS4; -.
DR PeptideAtlas; Q3UGS4; -.
DR PRIDE; Q3UGS4; -.
DR ProteomicsDB; 292200; -.
DR Antibodypedia; 63491; 34 antibodies from 10 providers.
DR Ensembl; ENSMUST00000034913; ENSMUSP00000034913; ENSMUSG00000061111.
DR GeneID; 192173; -.
DR KEGG; mmu:192173; -.
DR UCSC; uc007mtf.1; mouse.
DR CTD; 348262; -.
DR MGI; MGI:2384752; Mcrip1.
DR VEuPathDB; HostDB:ENSMUSG00000061111; -.
DR eggNOG; ENOG502S25D; Eukaryota.
DR GeneTree; ENSGT00940000161850; -.
DR HOGENOM; CLU_161057_0_0_1; -.
DR InParanoid; Q3UGS4; -.
DR OMA; QNHERND; -.
DR OrthoDB; 1461250at2759; -.
DR PhylomeDB; Q3UGS4; -.
DR TreeFam; TF326620; -.
DR BioGRID-ORCS; 192173; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Fam195b; mouse.
DR PRO; PR:Q3UGS4; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q3UGS4; protein.
DR Bgee; ENSMUSG00000061111; Expressed in embryonic brain and 251 other tissues.
DR Genevisible; Q3UGS4; MM.
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_0000393955"
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:21183079"
FT MOD_RES 30
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:C9JLW8"
FT MOD_RES 41
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
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
