Full text data of COPS8
COPS8
(CSN8)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
COP9 signalosome complex subunit 8; SGN8; Signalosome subunit 8 (COP9 homolog; hCOP9; JAB1-containing signalosome subunit 8)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
COP9 signalosome complex subunit 8; SGN8; Signalosome subunit 8 (COP9 homolog; hCOP9; JAB1-containing signalosome subunit 8)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q99627
ID CSN8_HUMAN Reviewed; 209 AA.
AC Q99627; A8K1H6; Q53QS9;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-1997, sequence version 1.
DT 22-JAN-2014, entry version 112.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT define a group of general developmental regulators shared by both
RT animal and plant 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA 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.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA 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.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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;
RA Seeger M., Kraft R., Ferrell K., Bech-Otschir D., Dumdey R.,
RA Schade R., 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.,
RA Pollmann C., Dubiel W.;
RT "COP9 signalosome-specific phosphorylation targets p53 to degradation
RT by 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.,
RA Drapkin R., 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.,
RA Bech-Otschir D., Huang X., Berse M., Sperling J., Schade R.,
RA 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,
RP AND 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 MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Component of the COP9 signalosome complex (CSN), a
CC complex involved in various cellular and developmental processes.
CC The 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
CC Ubl ligase activity of SCF-type complexes such as SCF, CSA or
CC DDB2. The complex is also involved in phosphorylation of p53/TP53,
CC c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8/ICSBP, possibly via
CC its association with CK2 and PKD kinases. CSN-dependent
CC phosphorylation of TP53 and JUN promotes and protects degradation
CC by the Ubl system, respectively.
CC -!- SUBUNIT: Component of the CSN complex, composed of COPS1/GPS1,
CC COPS2, COPS3, COPS4, COPS5, COP6, COPS7 (COPS7A or COPS7B) and
CC COPS8. In the complex, it probably interacts directly with COPS3,
CC COPS4 and COPS7 (COPS7A or COPS7B).
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
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 Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the CSN8 family.
CC -!- SIMILARITY: Contains 1 PCI domain.
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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 RefSeq; NP_006701.1; NM_006710.4.
DR RefSeq; NP_937832.1; NM_198189.2.
DR UniGene; Hs.531713; -.
DR ProteinModelPortal; Q99627; -.
DR DIP; DIP-42075N; -.
DR IntAct; Q99627; 5.
DR MINT; MINT-1204089; -.
DR STRING; 9606.ENSP00000346340; -.
DR PhosphoSite; Q99627; -.
DR DMDM; 55976572; -.
DR PaxDb; Q99627; -.
DR PRIDE; Q99627; -.
DR DNASU; 10920; -.
DR Ensembl; ENST00000354371; ENSP00000346340; ENSG00000198612.
DR Ensembl; ENST00000392008; ENSP00000375865; ENSG00000198612.
DR GeneID; 10920; -.
DR KEGG; hsa:10920; -.
DR UCSC; uc002vwg.3; human.
DR CTD; 10920; -.
DR GeneCards; GC02P237993; -.
DR HGNC; HGNC:24335; COPS8.
DR HPA; HPA036485; -.
DR neXtProt; NX_Q99627; -.
DR PharmGKB; PA134968686; -.
DR eggNOG; NOG321945; -.
DR HOGENOM; HOG000253954; -.
DR HOVERGEN; HBG051139; -.
DR InParanoid; Q99627; -.
DR KO; K12181; -.
DR OMA; GIATPQV; -.
DR OrthoDB; EOG76DTV5; -.
DR PhylomeDB; Q99627; -.
DR ChiTaRS; COPS8; human.
DR GeneWiki; COPS8; -.
DR GenomeRNAi; 10920; -.
DR NextBio; 41481; -.
DR PRO; PR:Q99627; -.
DR ArrayExpress; Q99627; -.
DR Bgee; Q99627; -.
DR CleanEx; HS_COPS8; -.
DR Genevestigator; Q99627; -.
DR GO; GO:0008180; C:COP9 signalosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0010388; P:cullin deneddylation; IDA:UniProtKB.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Nucleus; Phosphoprotein;
KW Reference proteome; Signalosome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 209 COP9 signalosome complex subunit 8.
FT /FTId=PRO_0000121007.
FT DOMAIN 68 151 PCI.
FT MOD_RES 175 175 Phosphoserine.
FT VAR_SEQ 1 49 Missing (in isoform 2).
FT /FTId=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
//
ID CSN8_HUMAN Reviewed; 209 AA.
AC Q99627; A8K1H6; Q53QS9;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-1997, sequence version 1.
DT 22-JAN-2014, entry version 112.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT define a group of general developmental regulators shared by both
RT animal and plant 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA 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.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA 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.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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;
RA Seeger M., Kraft R., Ferrell K., Bech-Otschir D., Dumdey R.,
RA Schade R., 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.,
RA Pollmann C., Dubiel W.;
RT "COP9 signalosome-specific phosphorylation targets p53 to degradation
RT by 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.,
RA Drapkin R., 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.,
RA Bech-Otschir D., Huang X., Berse M., Sperling J., Schade R.,
RA 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,
RP AND 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 MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Component of the COP9 signalosome complex (CSN), a
CC complex involved in various cellular and developmental processes.
CC The 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
CC Ubl ligase activity of SCF-type complexes such as SCF, CSA or
CC DDB2. The complex is also involved in phosphorylation of p53/TP53,
CC c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8/ICSBP, possibly via
CC its association with CK2 and PKD kinases. CSN-dependent
CC phosphorylation of TP53 and JUN promotes and protects degradation
CC by the Ubl system, respectively.
CC -!- SUBUNIT: Component of the CSN complex, composed of COPS1/GPS1,
CC COPS2, COPS3, COPS4, COPS5, COP6, COPS7 (COPS7A or COPS7B) and
CC COPS8. In the complex, it probably interacts directly with COPS3,
CC COPS4 and COPS7 (COPS7A or COPS7B).
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
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 Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the CSN8 family.
CC -!- SIMILARITY: Contains 1 PCI domain.
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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 RefSeq; NP_006701.1; NM_006710.4.
DR RefSeq; NP_937832.1; NM_198189.2.
DR UniGene; Hs.531713; -.
DR ProteinModelPortal; Q99627; -.
DR DIP; DIP-42075N; -.
DR IntAct; Q99627; 5.
DR MINT; MINT-1204089; -.
DR STRING; 9606.ENSP00000346340; -.
DR PhosphoSite; Q99627; -.
DR DMDM; 55976572; -.
DR PaxDb; Q99627; -.
DR PRIDE; Q99627; -.
DR DNASU; 10920; -.
DR Ensembl; ENST00000354371; ENSP00000346340; ENSG00000198612.
DR Ensembl; ENST00000392008; ENSP00000375865; ENSG00000198612.
DR GeneID; 10920; -.
DR KEGG; hsa:10920; -.
DR UCSC; uc002vwg.3; human.
DR CTD; 10920; -.
DR GeneCards; GC02P237993; -.
DR HGNC; HGNC:24335; COPS8.
DR HPA; HPA036485; -.
DR neXtProt; NX_Q99627; -.
DR PharmGKB; PA134968686; -.
DR eggNOG; NOG321945; -.
DR HOGENOM; HOG000253954; -.
DR HOVERGEN; HBG051139; -.
DR InParanoid; Q99627; -.
DR KO; K12181; -.
DR OMA; GIATPQV; -.
DR OrthoDB; EOG76DTV5; -.
DR PhylomeDB; Q99627; -.
DR ChiTaRS; COPS8; human.
DR GeneWiki; COPS8; -.
DR GenomeRNAi; 10920; -.
DR NextBio; 41481; -.
DR PRO; PR:Q99627; -.
DR ArrayExpress; Q99627; -.
DR Bgee; Q99627; -.
DR CleanEx; HS_COPS8; -.
DR Genevestigator; Q99627; -.
DR GO; GO:0008180; C:COP9 signalosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0010388; P:cullin deneddylation; IDA:UniProtKB.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Nucleus; Phosphoprotein;
KW Reference proteome; Signalosome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 209 COP9 signalosome complex subunit 8.
FT /FTId=PRO_0000121007.
FT DOMAIN 68 151 PCI.
FT MOD_RES 175 175 Phosphoserine.
FT VAR_SEQ 1 49 Missing (in isoform 2).
FT /FTId=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
//