CSN9_HUMAN
ID CSN9_HUMAN Reviewed; 57 AA.
AC Q8WXC6; Q8N110;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 3.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=COP9 signalosome complex subunit 9 {ECO:0000305};
DE AltName: Full=CSN acidic protein {ECO:0000303|PubMed:26456823};
DE Short=CSNAP {ECO:0000303|PubMed:26456823};
DE AltName: Full=Myeloma-overexpressed gene 2 protein {ECO:0000303|Ref.1};
GN Name=COPS9 {ECO:0000312|HGNC:HGNC:21314};
GN Synonyms=MYEOV2 {ECO:0000303|Ref.1};
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] (ISOFORMS 1 AND 2).
RA Tang L.-J., Hu W.-X., He L.-F., Tian J.-Y., Liu X.-F., Tan D.-R.;
RT "Molecular cloning and expression of a novel gene in multiple myeloma
RT cells.";
RL Zhongguo Sheng Wu Hua Xue Yu Fen Zi Sheng Wu Xue Bao 19:60-63(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP INTERACTION WITH COPS5; CUL1; CUL3 AND RPL11 (ISOFORM 2), ASSOCIATION WITH
RP THE CSN COMPLEX (ISOFORM 2), SUBCELLULAR LOCATION (ISOFORM 2), AND DOMAIN
RP (ISOFORM 2).
RX PubMed=23776465; DOI=10.1371/journal.pone.0065285;
RA Ebina M., Tsuruta F., Katoh M.C., Kigoshi Y., Someya A., Chiba T.;
RT "Myeloma overexpressed 2 (Myeov2) regulates L11 subnuclear localization
RT through Nedd8 modification.";
RL PLoS ONE 8:E65285-E65285(2013).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-26, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [6]
RP FUNCTION (ISOFORM 1), COMPOSITION OF THE CSN COMPLEX (ISOFORM 1),
RP INTERACTION WITH COPS3; COPS5 AND COPS6 (ISOFORM 1), SUBCELLULAR LOCATION
RP (ISOFORM 1), DOMAIN (ISOFORM 1), IDENTIFICATION BY MASS SPECTROMETRY
RP (ISOFORM 1), AND MUTAGENESIS OF PHE-44 AND PHE-51.
RX PubMed=26456823; DOI=10.1016/j.celrep.2015.09.021;
RA Rozen S., Fuezesi-Levi M.G., Ben-Nissan G., Mizrachi L., Gabashvili A.,
RA Levin Y., Ben-Dor S., Eisenstein M., Sharon M.;
RT "CSNAP is a stoichiometric subunit of the COP9 signalosome.";
RL Cell Rep. 13:585-598(2015).
CC -!- FUNCTION: [Isoform 1]: Component of the COP9 signalosome complex (CSN),
CC a complex involved in various cellular and developmental processes. The
CC CSN complex is an essential regulator of the ubiquitin (Ubl)
CC conjugation pathway by mediating the deneddylation of the cullin
CC subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl
CC ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The
CC complex is also involved in phosphorylation of p53/TP53, c-jun/JUN,
CC IkappaBalpha/NFKBIA, ITPK1 and IRF8/ICSBP, possibly via its association
CC with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN
CC promotes and protects degradation by the Ubl system, respectively.
CC Plays a role in cell proliferation. {ECO:0000269|PubMed:26456823}.
CC -!- FUNCTION: [Isoform 2]: Negatively regulates neddylation of proteins,
CC including ribosoaml protein RPL11. {ECO:0000269|PubMed:23776465}.
CC -!- SUBUNIT: Component of the CSN complex, composed of COPS1/GPS1, COPS2,
CC COPS3, COPS4, COPS5, COPS6, COPS7 (COPS7A or COPS7B), COPS8 and COPS9
CC isoform 1. In the complex, it interacts directly with COPS3, COPS5 and
CC COPS6 (PubMed:26456823). Isoform 2 associates with CSN complex
CC (PubMed:23776465). Isoform 2 interacts with COPS5, CUL1, CUL3 and RPL11
CC (PubMed:23776465). According to PubMed:26456823, does not associate
CC with CSN complex. {ECO:0000269|PubMed:23776465,
CC ECO:0000269|PubMed:26456823}.
CC -!- INTERACTION:
CC Q8WXC6-1; P57075-2: UBASH3A; NbExp=3; IntAct=EBI-17466401, EBI-7353612;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus
CC {ECO:0000269|PubMed:26456823}. Cytoplasm {ECO:0000269|PubMed:26456823}.
CC Nucleus, nucleoplasm {ECO:0000269|PubMed:26456823}. Note=Excluded from
CC the nucleolus. Recruited to the nucleoplasm and chromatin following DNA
CC damage induction. {ECO:0000269|PubMed:26456823}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:23776465}. Note=Excluded from the nucleolus.
CC {ECO:0000269|PubMed:23776465}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=CSNAP {ECO:0000303|PubMed:26456823};
CC IsoId=Q8WXC6-2; Sequence=Displayed;
CC Name=2; Synonyms=MYEOV2-L {ECO:0000303|Ref.1};
CC IsoId=Q8WXC6-1; Sequence=VSP_037073, VSP_037074, VSP_037075;
CC -!- DOMAIN: [Isoform 1]: The Phe/Asp-rich domain at the C-terminus is
CC necessary for its incorporation into the CSN complex.
CC {ECO:0000269|PubMed:26456823}.
CC -!- DOMAIN: [Isoform 2]: Amino acids 60-89 in isoform 2 are necessary for
CC interaction with COPS5, CUL1, CUL3. {ECO:0000269|PubMed:23776465}.
CC -!- SIMILARITY: Belongs to the CSN9 family. {ECO:0000305}.
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DR EMBL; AF453951; AAL41026.1; -; mRNA.
DR EMBL; AF487338; AAL96264.2; -; mRNA.
DR EMBL; AC013469; AAY14738.1; -; Genomic_DNA.
DR EMBL; CH471063; EAW71178.1; -; Genomic_DNA.
DR CCDS; CCDS2532.1; -. [Q8WXC6-1]
DR CCDS; CCDS63183.1; -. [Q8WXC6-2]
DR RefSeq; NP_001156896.1; NM_001163424.1. [Q8WXC6-2]
DR RefSeq; NP_612209.1; NM_138336.1. [Q8WXC6-1]
DR AlphaFoldDB; Q8WXC6; -.
DR BioGRID; 127315; 55.
DR IntAct; Q8WXC6; 12.
DR iPTMnet; Q8WXC6; -.
DR PhosphoSitePlus; Q8WXC6; -.
DR BioMuta; COPS9; -.
DR EPD; Q8WXC6; -.
DR jPOST; Q8WXC6; -.
DR MassIVE; Q8WXC6; -.
DR PeptideAtlas; Q8WXC6; -.
DR PRIDE; Q8WXC6; -.
DR ProteomicsDB; 75006; -. [Q8WXC6-2]
DR ProteomicsDB; 75007; -. [Q8WXC6-1]
DR Antibodypedia; 50515; 25 antibodies from 12 providers.
DR DNASU; 150678; -.
DR Ensembl; ENST00000307266.7; ENSP00000304147.3; ENSG00000172428.11. [Q8WXC6-1]
DR Ensembl; ENST00000607357.2; ENSP00000475979.1; ENSG00000172428.11. [Q8WXC6-2]
DR GeneID; 150678; -.
DR KEGG; hsa:150678; -.
DR MANE-Select; ENST00000607357.2; ENSP00000475979.1; NM_001163424.2; NP_001156896.1.
DR UCSC; uc002vyu.1; human. [Q8WXC6-2]
DR CTD; 150678; -.
DR GeneCards; COPS9; -.
DR HGNC; HGNC:21314; COPS9.
DR HPA; ENSG00000172428; Low tissue specificity.
DR MIM; 619349; gene.
DR neXtProt; NX_Q8WXC6; -.
DR OpenTargets; ENSG00000172428; -.
DR PharmGKB; PA142671302; -.
DR VEuPathDB; HostDB:ENSG00000172428; -.
DR GeneTree; ENSGT00390000000076; -.
DR HOGENOM; CLU_1102500_0_0_1; -.
DR InParanoid; Q8WXC6; -.
DR OMA; SNDKHVH; -.
DR OrthoDB; 1134658at2759; -.
DR PhylomeDB; Q8WXC6; -.
DR TreeFam; TF323869; -.
DR PathwayCommons; Q8WXC6; -.
DR SignaLink; Q8WXC6; -.
DR BioGRID-ORCS; 150678; 40 hits in 1082 CRISPR screens.
DR GenomeRNAi; 150678; -.
DR Pharos; Q8WXC6; Tbio.
DR PRO; PR:Q8WXC6; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q8WXC6; protein.
DR Bgee; ENSG00000172428; Expressed in upper arm skin and 182 other tissues.
DR ExpressionAtlas; Q8WXC6; baseline and differential.
DR Genevisible; Q8WXC6; HS.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0008180; C:COP9 signalosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0034644; P:cellular response to UV; IDA:UniProtKB.
DR GO; GO:0051220; P:cytoplasmic sequestering of protein; IMP:UniProtKB.
DR GO; GO:2000435; P:negative regulation of protein neddylation; IMP:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB.
DR InterPro; IPR029391; CSN9_metazoa.
DR PANTHER; PTHR28562; PTHR28562; 1.
DR Pfam; PF15004; MYEOV2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome; Signalosome.
FT CHAIN 1..57
FT /note="COP9 signalosome complex subunit 9"
FT /id="PRO_0000332924"
FT MOD_RES 26
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1
FT /note="M -> MWRAPEAALRPEVSLERRGPEM (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_037073"
FT VAR_SEQ 21
FT /note="E -> EVARARRESPS (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_037074"
FT VAR_SEQ 57
FT /note="Q -> HSSGLPRTSQQSSMVPALQRGQSEHGVRGKAAERPVVSEERCELNGR
FT EVAALDRAFGSTGHGQGAEALMFTRCREHPLCGTNKATSEGKMGTGRLRNSLRKNQSKW
FT LGSYLEVLRTTRSRREVSEDSTISVSTHWRGKCFKSDETPSVAGGEEGKKTTQPCIDVR
FT (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_037075"
FT MUTAGEN 44
FT /note="F->A: Does not abolish interaction with CSN complex.
FT Abolishes interaction with CSN complex; when associated
FT with A-51."
FT /evidence="ECO:0000269|PubMed:26456823"
FT MUTAGEN 51
FT /note="F->A: Decreases interaction with CSN complex.
FT Abolishes interaction with CSN complex; when associated
FT with A-44."
FT /evidence="ECO:0000269|PubMed:26456823"
SQ SEQUENCE 57 AA; 6211 MW; 8306DAFBF3DC610C CRC64;
MKPAVDEMFP EGAGPYVDLD EAGGSTGLLM DLAANEKAVH ADFFNDFEDL FDDDDIQ
