CSN8_HUMAN
ID CSN8_HUMAN Reviewed; 209 AA.
AC Q99627; A8K1H6; Q53QS9;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=COP9 signalosome complex subunit 8;
DE Short=SGN8;
DE Short=Signalosome subunit 8;
DE AltName: Full=COP9 homolog;
DE Short=hCOP9;
DE AltName: Full=JAB1-containing signalosome subunit 8;
GN Name=COPS8; Synonyms=CSN8;
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] (ISOFORM 1).
RX PubMed=7634324; DOI=10.1016/0092-8674(95)90423-9;
RA Chamovitz D.A., Deng X.-W.;
RT "The novel components of the Arabidopsis light signaling pathway may define
RT a group of general developmental regulators shared by both animal and plant
RT kingdoms.";
RL Cell 82:353-354(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Corpus callosum;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and 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 [7]
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 [8]
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 [9]
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 [10]
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 [11]
RP FUNCTION.
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 [12]
RP IDENTIFICATION IN THE CSN COMPLEX, CLEAVAGE OF INITIATOR METHIONINE, AND
RP PHOSPHORYLATION AT SER-175.
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 [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175, 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 [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).
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, 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 {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 COPS3, COPS4 and COPS7
CC (COPS7A or COPS7B) (PubMed:18850735). {ECO:0000269|PubMed:11337588,
CC ECO:0000269|PubMed:18850735, ECO:0000269|PubMed:26456823}.
CC -!- INTERACTION:
CC Q99627; Q9UNS2: COPS3; NbExp=15; IntAct=EBI-2510102, EBI-350590;
CC Q99627; Q13098-7: GPS1; NbExp=4; IntAct=EBI-2510102, EBI-10983983;
CC Q99627; P51687: SUOX; NbExp=3; IntAct=EBI-2510102, EBI-3921347;
CC Q99627; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-2510102, EBI-739895;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9535219}. Nucleus
CC {ECO:0000269|PubMed:9535219}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q99627-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99627-2; Sequence=VSP_042715;
CC -!- SIMILARITY: Belongs to the CSN8 family. {ECO:0000305}.
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DR EMBL; U51205; AAB38529.1; -; mRNA.
DR EMBL; AK289891; BAF82580.1; -; mRNA.
DR EMBL; CR456994; CAG33275.1; -; mRNA.
DR EMBL; AC105760; AAY14978.1; -; Genomic_DNA.
DR EMBL; CH471063; EAW71097.1; -; Genomic_DNA.
DR EMBL; CH471063; EAW71098.1; -; Genomic_DNA.
DR EMBL; BC003090; AAH03090.1; -; mRNA.
DR EMBL; BC036499; AAH36499.1; -; mRNA.
DR EMBL; BC080617; AAH80617.1; -; mRNA.
DR CCDS; CCDS2517.1; -. [Q99627-1]
DR CCDS; CCDS42835.1; -. [Q99627-2]
DR RefSeq; NP_006701.1; NM_006710.4. [Q99627-1]
DR RefSeq; NP_937832.1; NM_198189.2. [Q99627-2]
DR PDB; 4D10; X-ray; 3.80 A; H/P=2-209.
DR PDB; 4D18; X-ray; 4.08 A; H/P=1-209.
DR PDB; 4WSN; X-ray; 5.50 A; H/P/X/f/n/v=1-209.
DR PDB; 6R6H; EM; 8.40 A; H=1-209.
DR PDB; 6R7F; EM; 8.20 A; H=1-209.
DR PDB; 6R7H; EM; 8.80 A; H=11-209.
DR PDB; 6R7I; EM; 5.90 A; H=1-209.
DR PDB; 6R7N; EM; 6.50 A; H=11-209.
DR PDBsum; 4D10; -.
DR PDBsum; 4D18; -.
DR PDBsum; 4WSN; -.
DR PDBsum; 6R6H; -.
DR PDBsum; 6R7F; -.
DR PDBsum; 6R7H; -.
DR PDBsum; 6R7I; -.
DR PDBsum; 6R7N; -.
DR AlphaFoldDB; Q99627; -.
DR SMR; Q99627; -.
DR BioGRID; 116124; 112.
DR ComplexPortal; CPX-1870; COP9 signalosome variant 1.
DR ComplexPortal; CPX-1871; COP9 signalosome variant 2.
DR CORUM; Q99627; -.
DR DIP; DIP-42075N; -.
DR IntAct; Q99627; 45.
DR MINT; Q99627; -.
DR STRING; 9606.ENSP00000346340; -.
DR ChEMBL; CHEMBL4296015; -.
DR GlyGen; Q99627; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q99627; -.
DR PhosphoSitePlus; Q99627; -.
DR BioMuta; COPS8; -.
DR EPD; Q99627; -.
DR jPOST; Q99627; -.
DR MassIVE; Q99627; -.
DR MaxQB; Q99627; -.
DR PaxDb; Q99627; -.
DR PeptideAtlas; Q99627; -.
DR PRIDE; Q99627; -.
DR ProteomicsDB; 78367; -. [Q99627-1]
DR ProteomicsDB; 78368; -. [Q99627-2]
DR TopDownProteomics; Q99627-1; -. [Q99627-1]
DR Antibodypedia; 34471; 251 antibodies from 35 providers.
DR DNASU; 10920; -.
DR Ensembl; ENST00000354371.7; ENSP00000346340.2; ENSG00000198612.11. [Q99627-1]
DR Ensembl; ENST00000392008.6; ENSP00000375865.2; ENSG00000198612.11. [Q99627-2]
DR GeneID; 10920; -.
DR KEGG; hsa:10920; -.
DR MANE-Select; ENST00000354371.7; ENSP00000346340.2; NM_006710.5; NP_006701.1.
DR UCSC; uc002vwg.4; human. [Q99627-1]
DR CTD; 10920; -.
DR DisGeNET; 10920; -.
DR GeneCards; COPS8; -.
DR HGNC; HGNC:24335; COPS8.
DR HPA; ENSG00000198612; Low tissue specificity.
DR MIM; 616011; gene.
DR neXtProt; NX_Q99627; -.
DR OpenTargets; ENSG00000198612; -.
DR PharmGKB; PA134968686; -.
DR VEuPathDB; HostDB:ENSG00000198612; -.
DR eggNOG; KOG4414; Eukaryota.
DR GeneTree; ENSGT00390000000977; -.
DR HOGENOM; CLU_098091_2_0_1; -.
DR InParanoid; Q99627; -.
DR OMA; DFSTRMV; -.
DR PhylomeDB; Q99627; -.
DR TreeFam; TF101150; -.
DR PathwayCommons; Q99627; -.
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; Q99627; -.
DR BioGRID-ORCS; 10920; 722 hits in 1088 CRISPR screens.
DR ChiTaRS; COPS8; human.
DR GeneWiki; COPS8; -.
DR GenomeRNAi; 10920; -.
DR Pharos; Q99627; Tbio.
DR PRO; PR:Q99627; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q99627; protein.
DR Bgee; ENSG00000198612; Expressed in secondary oocyte and 209 other tissues.
DR ExpressionAtlas; Q99627; baseline and differential.
DR Genevisible; Q99627; 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:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0007250; P:activation of NF-kappaB-inducing kinase activity; IMP:UniProtKB.
DR GO; GO:0010387; P:COP9 signalosome assembly; IEA:InterPro.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0000338; P:protein deneddylation; IDA:UniProtKB.
DR GO; GO:0045116; P:protein neddylation; IC:ComplexPortal.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:2000434; P:regulation of protein neddylation; IC:ComplexPortal.
DR InterPro; IPR033205; COP9_CSN8.
DR InterPro; IPR033464; CSN8_PSD8_EIF3K.
DR InterPro; IPR000717; PCI_dom.
DR PANTHER; PTHR13339; PTHR13339; 1.
DR Pfam; PF10075; CSN8_PSD8_EIF3K; 1.
DR PROSITE; PS50250; PCI; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Direct protein sequencing;
KW Nucleus; Phosphoprotein; Reference proteome; Signalosome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:18850735"
FT CHAIN 2..209
FT /note="COP9 signalosome complex subunit 8"
FT /id="PRO_0000121007"
FT DOMAIN 8..179
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18850735,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..49
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042715"
SQ SEQUENCE 209 AA; 23226 MW; 203E236D8E304A8A CRC64;
MPVAVMAESA FSFKKLLDQC ENQELEAPGG IATPPVYGQL LALYLLHNDM NNARYLWKRI
PPAIKSANSE LGGIWSVGQR IWQRDFPGIY TTINAHQWSE TVQPIMEALR DATRRRAFAL
VSQAYTSIIA DDFAAFVGLP VEEAVKGILE QGWQADSTTR MVLPRKPVAG ALDVSFNKFI
PLSEPAPVPP IPNEQQLARL TDYVAFLEN
