COPRS_HUMAN
ID COPRS_HUMAN Reviewed; 184 AA.
AC Q9NQ92; A6NP14; E1P656; Q96EF5; Q96P75;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 3.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Coordinator of PRMT5 and differentiation stimulator;
DE AltName: Full=Cooperator of PRMT5;
DE AltName: Full=Protein TTP1;
GN Name=COPRS; Synonyms=C17orf79, COPR5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLY-43.
RX PubMed=10843809; DOI=10.1006/geno.2000.6179;
RA Jenne D.E., Tinschert S., Stegmann E., Reimann H., Nuernberg P., Horn D.,
RA Naumann I., Buske A., Thiel G.;
RT "A common set of at least 11 functional genes is lost in the majority of
RT NF1 patients with gross deletions.";
RL Genomics 66:93-97(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Liu Y., Cheng J., Zhang Y., Duan H., Mou J., Han P., Li K.;
RT "Suppression subtractive hybridization for cloning of gene 1 transactivated
RT by C-terminally truncated middle surface protein of hepatitis B virus.";
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLY-43.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLY-43.
RC TISSUE=Lung;
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 [6]
RP PROTEIN SEQUENCE OF 1-26 AND 58-69, ACETYLATION AT MET-1, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Mammary carcinoma;
RA Bienvenut W.V., Matallanas D., Cooper W.N., Kolch W.;
RL Submitted (JUL-2007) to UniProtKB.
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PRMT5 AND HISTONE H4.
RX PubMed=18404153; DOI=10.1038/embor.2008.45;
RA Lacroix M., Messaoudi S.E., Rodier G., Le Cam A., Sardet C., Fabbrizio E.;
RT "The histone-binding protein COPR5 is required for nuclear functions of the
RT protein arginine methyltransferase PRMT5.";
RL EMBO Rep. 9:452-458(2008).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
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.
CC Plays a role in muscle cell differentiation by modulating the
CC recruitment of PRMT5 to the promoter of genes involved in the
CC coordination between cell cycle exit and muscle differentiation (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:18404153}.
CC -!- SUBUNIT: Interacts with PRMT5. Interacts with histone H4; specifically
CC interacts with the N-terminus of histone H4 but not with histone H3.
CC Interacts with CBFB (By similarity). Found in a complex with PRMT5,
CC RUNX1 and CBFB (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q9NQ92; P62805: H4C9; NbExp=3; IntAct=EBI-1642558, EBI-302023;
CC Q9NQ92; O14744: PRMT5; NbExp=6; IntAct=EBI-1642558, EBI-351098;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18404153}.
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DR EMBL; AJ272196; CAB77267.2; -; mRNA.
DR EMBL; AF407672; AAK97661.1; -; mRNA.
DR EMBL; AC004253; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471147; EAW80262.1; -; Genomic_DNA.
DR EMBL; CH471147; EAW80263.1; -; Genomic_DNA.
DR EMBL; BC012386; AAH12386.1; -; mRNA.
DR CCDS; CCDS11268.1; -.
DR RefSeq; NP_060875.2; NM_018405.3.
DR AlphaFoldDB; Q9NQ92; -.
DR BioGRID; 120632; 73.
DR CORUM; Q9NQ92; -.
DR IntAct; Q9NQ92; 36.
DR MINT; Q9NQ92; -.
DR STRING; 9606.ENSP00000304327; -.
DR GlyGen; Q9NQ92; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NQ92; -.
DR PhosphoSitePlus; Q9NQ92; -.
DR BioMuta; COPRS; -.
DR DMDM; 189082907; -.
DR EPD; Q9NQ92; -.
DR jPOST; Q9NQ92; -.
DR MassIVE; Q9NQ92; -.
DR MaxQB; Q9NQ92; -.
DR PaxDb; Q9NQ92; -.
DR PeptideAtlas; Q9NQ92; -.
DR PRIDE; Q9NQ92; -.
DR ProteomicsDB; 82111; -.
DR Antibodypedia; 65565; 5 antibodies from 5 providers.
DR DNASU; 55352; -.
DR Ensembl; ENST00000302362.11; ENSP00000304327.6; ENSG00000172301.11.
DR GeneID; 55352; -.
DR KEGG; hsa:55352; -.
DR MANE-Select; ENST00000302362.11; ENSP00000304327.6; NM_018405.4; NP_060875.2.
DR UCSC; uc002hgp.4; human.
DR CTD; 55352; -.
DR DisGeNET; 55352; -.
DR GeneCards; COPRS; -.
DR HGNC; HGNC:28848; COPRS.
DR HPA; ENSG00000172301; Tissue enhanced (testis).
DR neXtProt; NX_Q9NQ92; -.
DR OpenTargets; ENSG00000172301; -.
DR PharmGKB; PA143485403; -.
DR VEuPathDB; HostDB:ENSG00000172301; -.
DR eggNOG; ENOG502ST7I; Eukaryota.
DR GeneTree; ENSGT00390000007384; -.
DR HOGENOM; CLU_126074_0_0_1; -.
DR InParanoid; Q9NQ92; -.
DR OMA; NDIPTHG; -.
DR OrthoDB; 1312667at2759; -.
DR PhylomeDB; Q9NQ92; -.
DR TreeFam; TF338109; -.
DR PathwayCommons; Q9NQ92; -.
DR Reactome; R-HSA-3214858; RMTs methylate histone arginines.
DR SignaLink; Q9NQ92; -.
DR BioGRID-ORCS; 55352; 18 hits in 1080 CRISPR screens.
DR ChiTaRS; COPRS; human.
DR GenomeRNAi; 55352; -.
DR Pharos; Q9NQ92; Tbio.
DR PRO; PR:Q9NQ92; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9NQ92; protein.
DR Bgee; ENSG00000172301; Expressed in left testis and 181 other tissues.
DR ExpressionAtlas; Q9NQ92; baseline and differential.
DR Genevisible; Q9NQ92; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0042393; F:histone binding; IDA:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0043985; P:histone H4-R3 methylation; IDA:UniProtKB.
DR GO; GO:0007517; P:muscle organ development; ISS: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; Direct protein sequencing; Myogenesis;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..184
FT /note="Coordinator of PRMT5 and differentiation stimulator"
FT /id="PRO_0000336077"
FT REGION 1..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..92
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:22814378"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CQ13"
FT VARIANT 43
FT /note="S -> G (in dbSNP:rs8068049)"
FT /evidence="ECO:0000269|PubMed:10843809,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.4"
FT /id="VAR_043538"
SQ SEQUENCE 184 AA; 20066 MW; 38D3E94C34C48745 CRC64;
MDLQAAGAQA QGAAEPSRGP PLPSARGAPP SPEAGFATAD HSSQERETEK AMDRLARGTQ
SIPNDSPARG EGTHSEEEGF AMDEEDSDGE LNTWELSEGT NCPPKEQPGD LFNEDWDSEL
KADQGNPYDA DDIQESISQE LKPWVCCAPQ GDMIYDPSWH HPPPLIPYYS KMVFETGQFD
DAED
