CSN7A_HUMAN
ID CSN7A_HUMAN Reviewed; 275 AA.
AC Q9UBW8; A8K9A6; Q9NVX3; Q9UJW4;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=COP9 signalosome complex subunit 7a;
DE Short=SGN7a;
DE Short=Signalosome subunit 7a;
DE AltName: Full=Dermal papilla-derived protein 10;
DE AltName: Full=JAB1-containing signalosome subunit 7a;
GN Name=COPS7A; Synonyms=CSN7A, DERP10;
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], TISSUE SPECIFICITY, AND INTERACTION WITH PMF1.
RC TISSUE=Placenta;
RX PubMed=12020345; DOI=10.1042/bj20020211;
RA Wang Y., Devereux W., Stewart T.M., Casero R.A. Jr.;
RT "Polyamine-modulated factor 1 binds to the human homologue of the 7a
RT subunit of the Arabidopsis COP9 signalosome: implications in gene
RT expression.";
RL Biochem. J. 366:79-86(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Hair follicle dermal papilla;
RA Ikeda A., Ukai Y., Yamashita M., Yoshimoto M.;
RT "Molecular cloning of a dermal papilla derived gene.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Okaze H., Hayashi A., Kozuma S., Saito T.;
RT "Cop9 complex subunit 7a.";
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Lau S.K., Au T.C.C., Kok L.D.S., Lee C.Y., Tsui S.K.W., Waye M.M.Y.,
RA Fung K.P.;
RT "Molecular cloning and characterization of a novel cDNA encoding human COP9
RT complex subunit 7a (COPS7a).";
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo, Mammary gland, and Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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 [8]
RP PARTIAL PROTEIN SEQUENCE, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9535219; DOI=10.1096/fasebj.12.6.469;
RA Seeger M., Kraft R., Ferrell K., Bech-Otschir D., Dumdey R., Schade R.,
RA Gordon C., Naumann M., Dubiel W.;
RT "A novel protein complex involved in signal transduction possessing
RT similarities to 26S proteasome subunits.";
RL FASEB J. 12:469-478(1998).
RN [9]
RP FUNCTION.
RX PubMed=11285227; DOI=10.1093/emboj/20.7.1630;
RA Bech-Otschir D., Kraft R., Huang X., Henklein P., Kapelari B., Pollmann C.,
RA Dubiel W.;
RT "COP9 signalosome-specific phosphorylation targets p53 to degradation by
RT the ubiquitin system.";
RL EMBO J. 20:1630-1639(2001).
RN [10]
RP FUNCTION, AND COMPOSITION OF THE CSN COMPLEX.
RX PubMed=11337588; DOI=10.1126/science.1059780;
RA Lyapina S., Cope G., Shevchenko A., Serino G., Tsuge T., Zhou C.,
RA Wolf D.A., Wei N., Shevchenko A., Deshaies R.J.;
RT "Promotion of NEDD-CUL1 conjugate cleavage by COP9 signalosome.";
RL Science 292:1382-1385(2001).
RN [11]
RP INTERACTION WITH EIF3S6.
RX PubMed=12220626; DOI=10.1016/s0014-5793(02)03147-2;
RA Hoareau Alves K., Bochard V., Rety S., Jalinot P.;
RT "Association of the mammalian proto-oncoprotein Int-6 with the three
RT protein complexes eIF3, COP9 signalosome and 26S proteasome.";
RL FEBS Lett. 527:15-21(2002).
RN [12]
RP FUNCTION.
RX PubMed=12732143; DOI=10.1016/s0092-8674(03)00316-7;
RA Groisman R., Polanowska J., Kuraoka I., Sawada J., Saijo M., Drapkin R.,
RA Kisselev A.F., Tanaka K., Nakatani Y.;
RT "The ubiquitin ligase activity in the DDB2 and CSA complexes is
RT differentially regulated by the COP9 signalosome in response to DNA
RT damage.";
RL Cell 113:357-367(2003).
RN [13]
RP FUNCTION, PHOSPHORYLATION, AND INTERACTION WITH CK2 AND PKD.
RX PubMed=12628923; DOI=10.1093/emboj/cdg127;
RA Uhle S., Medalia O., Waldron R., Dumdey R., Henklein P., Bech-Otschir D.,
RA Huang X., Berse M., Sperling J., Schade R., Dubiel W.;
RT "Protein kinase CK2 and protein kinase D are associated with the COP9
RT signalosome.";
RL EMBO J. 22:1302-1312(2003).
RN [14]
RP IDENTIFICATION IN THE CSN COMPLEX, CLEAVAGE OF INITIATOR METHIONINE, AND
RP ACETYLATION AT SER-2.
RX PubMed=18850735; DOI=10.1021/pr800574c;
RA Fang L., Wang X., Yamoah K., Chen P.L., Pan Z.Q., Huang L.;
RT "Characterization of the human COP9 signalosome complex using affinity
RT purification and mass spectrometry.";
RL J. Proteome Res. 7:4914-4925(2008).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
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).
RN [17]
RP IDENTIFICATION BY 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 [18]
RP COMPOSITION OF THE CSN COMPLEX.
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).
RN [19]
RP INTERACTION WITH VACCINIA VIRUS PROTEIN C9L (MICROBIAL INFECTION).
RX PubMed=29444943; DOI=10.1128/jvi.00053-18;
RA Liu R., Moss B.;
RT "Vaccinia Virus C9 Ankyrin Repeat/F-Box Protein Is a Newly Identified
RT Antagonist of the Type I Interferon-Induced Antiviral State.";
RL J. Virol. 92:0-0(2018).
CC -!- FUNCTION: Component of the COP9 signalosome complex (CSN), a complex
CC involved in various cellular and developmental processes. The CSN
CC complex is an essential regulator of the ubiquitin (Ubl) conjugation
CC pathway by mediating the deneddylation of the cullin subunits of SCF-
CC type E3 ligase complexes, leading to decrease the Ubl ligase activity
CC of SCF-type complexes such as SCF, CSA or DDB2. The complex is also
CC involved in phosphorylation of p53/TP53, JUN, I-kappa-B-alpha/NFKBIA,
CC ITPK1 and IRF8/ICSBP, possibly via its association with CK2 and PKD
CC kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and
CC protects degradation by the Ubl system, respectively.
CC {ECO:0000269|PubMed:11285227, ECO:0000269|PubMed:11337588,
CC ECO:0000269|PubMed:12628923, ECO:0000269|PubMed:12732143,
CC ECO:0000269|PubMed:9535219}.
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 (PubMed:11337588, PubMed:18850735, PubMed:26456823). In the
CC complex, it probably interacts directly with COPS1, COPS2, COPS4,
CC COPS5, COPS6 and COPS8. Interacts with PMF1 (PubMed:12020345).
CC Interacts with the translation initiation factor EIF3S6
CC (PubMed:12220626). Interacts with CK2 and PKD (PubMed:12628923).
CC Interacts directly with ID3 (By similarity).
CC {ECO:0000250|UniProtKB:Q9CZ04, ECO:0000269|PubMed:11337588,
CC ECO:0000269|PubMed:12020345, ECO:0000269|PubMed:12220626,
CC ECO:0000269|PubMed:12628923, ECO:0000269|PubMed:18850735,
CC ECO:0000269|PubMed:26456823}.
CC -!- SUBUNIT: (Microbial infection) Interacts with vaccinia virus protein
CC C9L. {ECO:0000269|PubMed:29444943}.
CC -!- INTERACTION:
CC Q9UBW8; Q9UNS2: COPS3; NbExp=10; IntAct=EBI-712982, EBI-350590;
CC Q9UBW8; Q16236: NFE2L2; NbExp=2; IntAct=EBI-712982, EBI-2007911;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9535219}. Nucleus
CC {ECO:0000269|PubMed:9535219}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed at high level in brain,
CC heart and skeletal muscle. {ECO:0000269|PubMed:12020345}.
CC -!- PTM: Phosphorylated by CK2 and PKD kinases.
CC {ECO:0000269|PubMed:12628923}.
CC -!- SIMILARITY: Belongs to the CSN7/EIF3M family. CSN7 subfamily.
CC {ECO:0000305}.
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DR EMBL; AF210052; AAF19205.1; -; mRNA.
DR EMBL; AB014764; BAB87805.1; -; mRNA.
DR EMBL; AB033603; BAA85390.1; -; mRNA.
DR EMBL; AF193844; AAF04307.1; -; mRNA.
DR EMBL; AK001318; BAA91620.1; -; mRNA.
DR EMBL; AK021721; BAG51042.1; -; mRNA.
DR EMBL; AK022488; BAB14052.1; -; mRNA.
DR EMBL; AK292621; BAF85310.1; -; mRNA.
DR EMBL; CH471116; EAW88745.1; -; Genomic_DNA.
DR EMBL; CH471116; EAW88747.1; -; Genomic_DNA.
DR EMBL; CH471116; EAW88748.1; -; Genomic_DNA.
DR EMBL; BC011789; AAH11789.1; -; mRNA.
DR CCDS; CCDS8558.1; -.
DR RefSeq; NP_001157565.1; NM_001164093.1.
DR RefSeq; NP_001157566.1; NM_001164094.1.
DR RefSeq; NP_001157567.1; NM_001164095.2.
DR RefSeq; NP_057403.1; NM_016319.3.
DR RefSeq; XP_005253751.1; XM_005253694.2.
DR PDB; 4D10; X-ray; 3.80 A; G/O=1-218.
DR PDB; 4D18; X-ray; 4.08 A; G/O=1-218.
DR PDB; 4WSN; X-ray; 5.50 A; G/O/W/e/m/u=1-218.
DR PDBsum; 4D10; -.
DR PDBsum; 4D18; -.
DR PDBsum; 4WSN; -.
DR AlphaFoldDB; Q9UBW8; -.
DR SMR; Q9UBW8; -.
DR BioGRID; 119130; 141.
DR ComplexPortal; CPX-1870; COP9 signalosome variant 1.
DR CORUM; Q9UBW8; -.
DR DIP; DIP-53412N; -.
DR IntAct; Q9UBW8; 73.
DR MINT; Q9UBW8; -.
DR STRING; 9606.ENSP00000438115; -.
DR GlyGen; Q9UBW8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UBW8; -.
DR PhosphoSitePlus; Q9UBW8; -.
DR BioMuta; COPS7A; -.
DR DMDM; 55976618; -.
DR EPD; Q9UBW8; -.
DR jPOST; Q9UBW8; -.
DR MassIVE; Q9UBW8; -.
DR MaxQB; Q9UBW8; -.
DR PaxDb; Q9UBW8; -.
DR PeptideAtlas; Q9UBW8; -.
DR PRIDE; Q9UBW8; -.
DR ProteomicsDB; 84087; -.
DR Antibodypedia; 11091; 227 antibodies from 31 providers.
DR DNASU; 50813; -.
DR Ensembl; ENST00000229251.7; ENSP00000229251.3; ENSG00000111652.10.
DR Ensembl; ENST00000534877.5; ENSP00000438363.1; ENSG00000111652.10.
DR Ensembl; ENST00000534947.5; ENSP00000446039.1; ENSG00000111652.10.
DR Ensembl; ENST00000539735.5; ENSP00000441852.1; ENSG00000111652.10.
DR Ensembl; ENST00000543155.6; ENSP00000438115.1; ENSG00000111652.10.
DR GeneID; 50813; -.
DR KEGG; hsa:50813; -.
DR MANE-Select; ENST00000543155.6; ENSP00000438115.1; NM_001164094.2; NP_001157566.1.
DR UCSC; uc001qqh.4; human.
DR CTD; 50813; -.
DR DisGeNET; 50813; -.
DR GeneCards; COPS7A; -.
DR HGNC; HGNC:16758; COPS7A.
DR HPA; ENSG00000111652; Low tissue specificity.
DR MIM; 616009; gene.
DR neXtProt; NX_Q9UBW8; -.
DR OpenTargets; ENSG00000111652; -.
DR PharmGKB; PA26758; -.
DR VEuPathDB; HostDB:ENSG00000111652; -.
DR eggNOG; KOG3250; Eukaryota.
DR GeneTree; ENSGT00940000159873; -.
DR InParanoid; Q9UBW8; -.
DR OMA; DIHAFAQ; -.
DR OrthoDB; 1396757at2759; -.
DR PhylomeDB; Q9UBW8; -.
DR TreeFam; TF101149; -.
DR PathwayCommons; Q9UBW8; -.
DR Reactome; R-HSA-5696394; DNA Damage Recognition in GG-NER.
DR Reactome; R-HSA-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-HSA-8951664; Neddylation.
DR SignaLink; Q9UBW8; -.
DR BioGRID-ORCS; 50813; 12 hits in 1085 CRISPR screens.
DR ChiTaRS; COPS7A; human.
DR GeneWiki; COPS7A; -.
DR GenomeRNAi; 50813; -.
DR Pharos; Q9UBW8; Tbio.
DR PRO; PR:Q9UBW8; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9UBW8; protein.
DR Bgee; ENSG00000111652; Expressed in prefrontal cortex and 208 other tissues.
DR ExpressionAtlas; Q9UBW8; baseline and differential.
DR Genevisible; Q9UBW8; HS.
DR GO; GO:0008180; C:COP9 signalosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0010387; P:COP9 signalosome assembly; IEA:InterPro.
DR GO; GO:0000338; P:protein deneddylation; IDA:UniProtKB.
DR GO; GO:0045116; P:protein neddylation; IC:ComplexPortal.
DR GO; GO:2000434; P:regulation of protein neddylation; IC:ComplexPortal.
DR InterPro; IPR045237; COPS7/eIF3m.
DR InterPro; IPR037757; COPS7A.
DR InterPro; IPR041481; CSN7_helixI.
DR InterPro; IPR000717; PCI_dom.
DR PANTHER; PTHR15350; PTHR15350; 1.
DR PANTHER; PTHR15350:SF7; PTHR15350:SF7; 1.
DR Pfam; PF18392; CSN7a_helixI; 1.
DR Pfam; PF01399; PCI; 1.
DR SMART; SM00088; PINT; 1.
DR PROSITE; PS50250; PCI; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Coiled coil; Cytoplasm;
KW Direct protein sequencing; Host-virus interaction; Nucleus; Phosphoprotein;
KW Reference proteome; Signalosome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:18850735"
FT CHAIN 2..275
FT /note="COP9 signalosome complex subunit 7a"
FT /id="PRO_0000120996"
FT DOMAIN 2..159
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 227..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 185..233
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:18850735"
FT CONFLICT 218
FT /note="K -> E (in Ref. 5; BAA91620)"
FT /evidence="ECO:0000305"
FT CONFLICT 253
FT /note="Q -> H (in Ref. 4; AAF04307)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 275 AA; 30277 MW; 20888B35BFFF6326 CRC64;
MSAEVKVTGQ NQEQFLLLAK SAKGAALATL IHQVLEAPGV YVFGELLDMP NVRELAESDF
ASTFRLLTVF AYGTYADYLA EARNLPPLTE AQKNKLRHLS VVTLAAKVKC IPYAVLLEAL
ALRNVRQLED LVIEAVYADV LRGSLDQRNQ RLEVDYSIGR DIQRQDLSAI ARTLQEWCVG
CEVVLSGIEE QVSRANQHKE QQLGLKQQIE SEVANLKKTI KVTTAAAAAA TSQDPEQHLT
ELREPAPGTN QRQPSKKASK GKGLRGSAKI WSKSN
