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 27-MAR-2024, entry version 188. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 8H38; EM; 4.25 A; H=1-209. DR PDB; 8H3A; EM; 7.51 A; H=1-209. DR PDB; 8H3F; EM; 6.73 A; H=1-209. 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 PDBsum; 8H38; -. DR PDBsum; 8H3A; -. DR PDBsum; 8H3F; -. DR AlphaFoldDB; Q99627; -. DR EMDB; EMD-3313; -. DR EMDB; EMD-3314; -. DR EMDB; EMD-3315; -. DR EMDB; EMD-3316; -. DR EMDB; EMD-3317; -. DR EMDB; EMD-3401; -. DR EMDB; EMD-34455; -. DR EMDB; EMD-34462; -. DR EMDB; EMD-34467; -. DR EMDB; EMD-4736; -. DR EMDB; EMD-4739; -. DR EMDB; EMD-4741; -. DR EMDB; EMD-4742; -. DR EMDB; EMD-4744; -. DR SMR; Q99627; -. DR BioGRID; 116124; 134. 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; 46. 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; 9606-ENSP00000346340; -. DR PeptideAtlas; Q99627; -. DR ProteomicsDB; 78367; -. [Q99627-1] DR ProteomicsDB; 78368; -. [Q99627-2] DR Pumba; Q99627; -. DR TopDownProteomics; Q99627-1; -. [Q99627-1] DR Antibodypedia; 34471; 273 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 AGR; HGNC:24335; -. 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; NNAKFLW; -. DR OrthoDB; 3675131at2759; -. 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 SIGNOR; Q99627; -. DR BioGRID-ORCS; 10920; 750 hits in 1176 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 211 other cell types or tissues. DR ExpressionAtlas; Q99627; baseline and differential. 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; NAS:ComplexPortal. DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB. DR GO; GO:2000434; P:regulation of protein neddylation; NAS:ComplexPortal. DR Gene3D; 1.25.40.990; -; 1. DR InterPro; IPR033205; COP9_CSN8. DR InterPro; IPR033464; CSN8_PSD8_EIF3K. DR InterPro; IPR000717; PCI_dom. DR PANTHER; PTHR13339; COP9 SIGNALOSOME COMPLEX SUBUNIT 8; 1. DR PANTHER; PTHR13339:SF0; COP9 SIGNALOSOME COMPLEX SUBUNIT 8; 1. DR Pfam; PF10075; CSN8_PSD8_EIF3K; 1. DR PROSITE; PS50250; PCI; 1. DR Genevisible; Q99627; HS. 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 //