Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Coordinator of PRMT5 and differentiation stimulator

Gene

Coprs

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Histone-binding protein required for histone H4 methyltransferase activity of PRMT5. Specifically required for histone H4 'Arg-3' methylation mediated by PRMT5, but not histone H3 'Arg-8' methylation, suggesting that it modulates the substrate specificity of PRMT5. Specifically interacts with the N-terminus of histone H4 but not with histone H3, suggesting that it acts by promoting the association between histone H4 and PRMT5. Involved in CCNE1 promoter repression (By similarity). Plays a role in muscle cell differentiation by modulating the recruitment of PRMT5 to the promoter of genes involved in the coordination between cell cycle exit and muscle differentiation.By similarity1 Publication

GO - Molecular functioni

GO - Biological processi

  • histone H4-R3 methylation Source: UniProtKB
  • muscle organ development Source: UniProtKB
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Biological processi

Myogenesis, Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiR-MMU-3214858. RMTs methylate histone arginines.

Names & Taxonomyi

Protein namesi
Recommended name:
Coordinator of PRMT5 and differentiation stimulator
Alternative name(s):
Cooperator of PRMT5
Gene namesi
Name:Coprs
Synonyms:Copr5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:1913673. Coprs.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 173173Coordinator of PRMT5 and differentiation stimulatorPRO_0000336078Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei64 – 641PhosphoserineCombined sources
Modified residuei65 – 651PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9CQ13.
MaxQBiQ9CQ13.
PaxDbiQ9CQ13.
PRIDEiQ9CQ13.

PTM databases

PhosphoSiteiQ9CQ13.

Expressioni

Gene expression databases

BgeeiQ9CQ13.
GenevisibleiQ9CQ13. MM.

Interactioni

Subunit structurei

Interacts with PRMT5. Interacts with histone H4; specifically interacts with the N-terminus of histone H4 but not with histone H3 (By similarity). Interacts with CBFB. Found in a complex with PRMT5, RUNX1 and CBFB.By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000033839.

Family & Domainsi

Phylogenomic databases

eggNOGiENOG410J4CS. Eukaryota.
ENOG4111D7J. LUCA.
GeneTreeiENSGT00390000007384.
HOGENOMiHOG000111893.
InParanoidiQ9CQ13.
OMAiDLNTWEL.
OrthoDBiEOG75XGN5.
PhylomeDBiQ9CQ13.
TreeFamiTF338109.

Family and domain databases

InterProiIPR029289. COPR5.
[Graphical view]
PfamiPF15340. COPR5. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9CQ13-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDPQAATGRG PGERSSQEAP SAEAGFATAD LSGRETETEL AVDRLASGAQ
60 70 80 90 100
SIPADIPAHA EGPSSEEEGF AVEKEADGEL YAWELSEGPS CPPMEQAADL
110 120 130 140 150
FNEDWDLELK ADQGNPYDAD DIQGSISQEI KPWVCCAPQG DMIYDPSWHH
160 170
PPPLIPHYSK MVFETGQFDD AED
Length:173
Mass (Da):18,666
Last modified:June 1, 2001 - v1
Checksum:iDAE67C0AB03683F8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK008882 mRNA. Translation: BAB25950.1.
AK010573 mRNA. Translation: BAB27036.1.
BC029192 mRNA. Translation: AAH29192.1.
CCDSiCCDS40237.1.
RefSeqiNP_079832.1. NM_025556.3.
UniGeneiMm.29063.

Genome annotation databases

EnsembliENSMUST00000033839; ENSMUSP00000033839; ENSMUSG00000031458.
GeneIDi66423.
KEGGimmu:66423.
UCSCiuc009kyr.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK008882 mRNA. Translation: BAB25950.1.
AK010573 mRNA. Translation: BAB27036.1.
BC029192 mRNA. Translation: AAH29192.1.
CCDSiCCDS40237.1.
RefSeqiNP_079832.1. NM_025556.3.
UniGeneiMm.29063.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000033839.

PTM databases

PhosphoSiteiQ9CQ13.

Proteomic databases

EPDiQ9CQ13.
MaxQBiQ9CQ13.
PaxDbiQ9CQ13.
PRIDEiQ9CQ13.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000033839; ENSMUSP00000033839; ENSMUSG00000031458.
GeneIDi66423.
KEGGimmu:66423.
UCSCiuc009kyr.2. mouse.

Organism-specific databases

CTDi55352.
MGIiMGI:1913673. Coprs.

Phylogenomic databases

eggNOGiENOG410J4CS. Eukaryota.
ENOG4111D7J. LUCA.
GeneTreeiENSGT00390000007384.
HOGENOMiHOG000111893.
InParanoidiQ9CQ13.
OMAiDLNTWEL.
OrthoDBiEOG75XGN5.
PhylomeDBiQ9CQ13.
TreeFamiTF338109.

Enzyme and pathway databases

ReactomeiR-MMU-3214858. RMTs methylate histone arginines.

Miscellaneous databases

NextBioi321651.
PROiQ9CQ13.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CQ13.
GenevisibleiQ9CQ13. MM.

Family and domain databases

InterProiIPR029289. COPR5.
[Graphical view]
PfamiPF15340. COPR5. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryonic stem cell and Stomach.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64 AND SER-65, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain and Testis.
  4. "The histone- and PRMT5-associated protein COPR5 is required for myogenic differentiation."
    Paul C., Sardet C., Fabbrizio E.
    Cell Death Differ. 19:900-908(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PRMT5 AND CBFB, IDENTIFICATION IN A COMPLEX WITH PRMT5; RUNX1 AND CBFB.

Entry informationi

Entry nameiCOPRS_MOUSE
AccessioniPrimary (citable) accession number: Q9CQ13
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: June 1, 2001
Last modified: March 16, 2016
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.