COPRS_MOUSE
ID COPRS_MOUSE Reviewed; 173 AA.
AC Q9CQ13;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Coordinator of PRMT5 and differentiation stimulator;
DE AltName: Full=Cooperator of PRMT5;
GN Name=Coprs; Synonyms=Copr5;
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; TISSUE=Embryonic stem cell, and Stomach;
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 MRNA].
RC STRAIN=FVB/N; 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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64 AND SER-65, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, 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 [4]
RP FUNCTION, INTERACTION WITH PRMT5 AND CBFB, AND IDENTIFICATION IN A COMPLEX
RP WITH PRMT5; RUNX1 AND CBFB.
RX PubMed=22193545; DOI=10.1038/cdd.2011.193;
RA Paul C., Sardet C., Fabbrizio E.;
RT "The histone- and PRMT5-associated protein COPR5 is required for myogenic
RT differentiation.";
RL Cell Death Differ. 19:900-908(2012).
CC -!- FUNCTION: Histone-binding protein required for histone H4
CC methyltransferase activity of PRMT5. Specifically required for histone
CC H4 'Arg-3' methylation mediated by PRMT5, but not histone H3 'Arg-8'
CC methylation, suggesting that it modulates the substrate specificity of
CC PRMT5. Specifically interacts with the N-terminus of histone H4 but not
CC with histone H3, suggesting that it acts by promoting the association
CC between histone H4 and PRMT5. Involved in CCNE1 promoter repression (By
CC similarity). Plays a role in muscle cell differentiation by modulating
CC the recruitment of PRMT5 to the promoter of genes involved in the
CC coordination between cell cycle exit and muscle differentiation.
CC {ECO:0000250, ECO:0000269|PubMed:22193545}.
CC -!- SUBUNIT: Interacts with PRMT5. Interacts with histone H4; specifically
CC interacts with the N-terminus of histone H4 but not with histone H3 (By
CC similarity). Interacts with CBFB. Found in a complex with PRMT5, RUNX1
CC and CBFB. {ECO:0000250, ECO:0000269|PubMed:22193545}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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DR EMBL; AK008882; BAB25950.1; -; mRNA.
DR EMBL; AK010573; BAB27036.1; -; mRNA.
DR EMBL; BC029192; AAH29192.1; -; mRNA.
DR CCDS; CCDS40237.1; -.
DR RefSeq; NP_079832.1; NM_025556.3.
DR AlphaFoldDB; Q9CQ13; -.
DR BioGRID; 211464; 3.
DR STRING; 10090.ENSMUSP00000033839; -.
DR iPTMnet; Q9CQ13; -.
DR PhosphoSitePlus; Q9CQ13; -.
DR EPD; Q9CQ13; -.
DR MaxQB; Q9CQ13; -.
DR PaxDb; Q9CQ13; -.
DR PeptideAtlas; Q9CQ13; -.
DR PRIDE; Q9CQ13; -.
DR ProteomicsDB; 285264; -.
DR Antibodypedia; 65565; 5 antibodies from 5 providers.
DR Ensembl; ENSMUST00000033839; ENSMUSP00000033839; ENSMUSG00000031458.
DR GeneID; 66423; -.
DR KEGG; mmu:66423; -.
DR UCSC; uc009kyr.2; mouse.
DR CTD; 55352; -.
DR MGI; MGI:1913673; Coprs.
DR VEuPathDB; HostDB:ENSMUSG00000031458; -.
DR eggNOG; ENOG502ST7I; Eukaryota.
DR GeneTree; ENSGT00390000007384; -.
DR HOGENOM; CLU_126074_0_0_1; -.
DR InParanoid; Q9CQ13; -.
DR OMA; NDIPTHG; -.
DR OrthoDB; 1312667at2759; -.
DR PhylomeDB; Q9CQ13; -.
DR TreeFam; TF338109; -.
DR Reactome; R-MMU-3214858; RMTs methylate histone arginines.
DR BioGRID-ORCS; 66423; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Coprs; mouse.
DR PRO; PR:Q9CQ13; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9CQ13; protein.
DR Bgee; ENSMUSG00000031458; Expressed in facial nucleus and 253 other tissues.
DR ExpressionAtlas; Q9CQ13; baseline and differential.
DR Genevisible; Q9CQ13; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR GO; GO:0001835; P:blastocyst hatching; IMP:MGI.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0043985; P:histone H4-R3 methylation; ISS:UniProtKB.
DR GO; GO:0007517; P:muscle organ development; IMP:UniProtKB.
DR InterPro; IPR029289; COPR5.
DR PANTHER; PTHR36461; PTHR36461; 1.
DR Pfam; PF15340; COPR5; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chromatin regulator; Myogenesis; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..173
FT /note="Coordinator of PRMT5 and differentiation stimulator"
FT /id="PRO_0000336078"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9NQ92"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 173 AA; 18666 MW; DAE67C0AB03683F8 CRC64;
MDPQAATGRG PGERSSQEAP SAEAGFATAD LSGRETETEL AVDRLASGAQ SIPADIPAHA
EGPSSEEEGF AVEKEADGEL YAWELSEGPS CPPMEQAADL FNEDWDLELK ADQGNPYDAD
DIQGSISQEI KPWVCCAPQG DMIYDPSWHH PPPLIPHYSK MVFETGQFDD AED
