Full text data of COPS7B
COPS7B
(CSN7B)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
COP9 signalosome complex subunit 7b; SGN7b; Signalosome subunit 7b (JAB1-containing signalosome subunit 7b)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
COP9 signalosome complex subunit 7b; SGN7b; Signalosome subunit 7b (JAB1-containing signalosome subunit 7b)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9H9Q2
ID CSN7B_HUMAN Reviewed; 264 AA.
AC Q9H9Q2; Q53S22; Q5BJG3; Q9H7V6;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAR-2001, sequence version 1.
DT 22-JAN-2014, entry version 87.
DE RecName: Full=COP9 signalosome complex subunit 7b;
DE Short=SGN7b;
DE Short=Signalosome subunit 7b;
DE AltName: Full=JAB1-containing signalosome subunit 7b;
GN Name=COPS7B; Synonyms=CSN7B;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Teratocarcinoma, and Trachea;
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 [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.,
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 99-264 (ISOFORM 1).
RC TISSUE=Lung, and Testis;
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 [5]
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 [6]
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 [7]
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 [8]
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 [9]
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 [10]
RP IDENTIFICATION IN THE CSN COMPLEX, CLEAVAGE OF INITIATOR METHIONINE,
RP AND ACETYLATION AT ALA-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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-261 AND SER-263 (ISOFORM
RP 3), AND MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
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 JUN, I-kappa-B-alpha/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 COPS1,
CC COPS2, COPS4, COPS5, COPS6 and COPS8.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9H9Q2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H9Q2-2; Sequence=VSP_011913;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q9H9Q2-3; Sequence=VSP_040266;
CC Note=Contains a phosphothreonine at position 261. Contains a
CC phosphoserine at position 263;
CC -!- SIMILARITY: Belongs to the CSN7/EIF3M family. CSN7 subfamily.
CC -!- SIMILARITY: Contains 1 PCI domain.
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DR EMBL; AK022674; BAB14170.1; -; mRNA.
DR EMBL; AK024273; BAB14868.1; -; mRNA.
DR EMBL; AC073476; AAY24152.1; -; Genomic_DNA.
DR EMBL; CH471063; EAW70980.1; -; Genomic_DNA.
DR EMBL; BC010739; AAH10739.2; -; mRNA.
DR EMBL; BC091493; AAH91493.1; -; mRNA.
DR RefSeq; NP_001269879.1; NM_001282950.1.
DR RefSeq; NP_001269881.1; NM_001282952.1.
DR RefSeq; NP_073567.1; NM_022730.2.
DR UniGene; Hs.335061; -.
DR ProteinModelPortal; Q9H9Q2; -.
DR SMR; Q9H9Q2; 4-163.
DR DIP; DIP-53525N; -.
DR IntAct; Q9H9Q2; 3.
DR STRING; 9606.ENSP00000272995; -.
DR ChEMBL; CHEMBL5706; -.
DR PhosphoSite; Q9H9Q2; -.
DR DMDM; 55976598; -.
DR PaxDb; Q9H9Q2; -.
DR PRIDE; Q9H9Q2; -.
DR DNASU; 64708; -.
DR Ensembl; ENST00000350033; ENSP00000272995; ENSG00000144524.
DR Ensembl; ENST00000373608; ENSP00000362710; ENSG00000144524.
DR Ensembl; ENST00000409091; ENSP00000386527; ENSG00000144524.
DR Ensembl; ENST00000410024; ENSP00000386567; ENSG00000144524.
DR GeneID; 64708; -.
DR KEGG; hsa:64708; -.
DR UCSC; uc002vsg.1; human.
DR CTD; 64708; -.
DR GeneCards; GC02P232646; -.
DR HGNC; HGNC:16760; COPS7B.
DR HPA; HPA034675; -.
DR neXtProt; NX_Q9H9Q2; -.
DR PharmGKB; PA26759; -.
DR eggNOG; NOG289374; -.
DR HOGENOM; HOG000006003; -.
DR HOVERGEN; HBG051138; -.
DR KO; K12180; -.
DR OrthoDB; EOG7N63NJ; -.
DR PhylomeDB; Q9H9Q2; -.
DR ChiTaRS; COPS7B; human.
DR GeneWiki; COPS7B; -.
DR GenomeRNAi; 64708; -.
DR NextBio; 66639; -.
DR PRO; PR:Q9H9Q2; -.
DR ArrayExpress; Q9H9Q2; -.
DR Bgee; Q9H9Q2; -.
DR CleanEx; HS_COPS7B; -.
DR Genevestigator; Q9H9Q2; -.
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.
DR InterPro; IPR027530; Csn7.
DR InterPro; IPR000717; PCI_dom.
DR PANTHER; PTHR15350:SF5; PTHR15350:SF5; 1.
DR Pfam; PF01399; PCI; 1.
DR SMART; SM00088; PINT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Complete proteome;
KW Cytoplasm; Nucleus; Phosphoprotein; Reference proteome; Signalosome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 264 COP9 signalosome complex subunit 7b.
FT /FTId=PRO_0000120999.
FT DOMAIN 52 156 PCI.
FT COILED 188 237 Potential.
FT MOD_RES 2 2 N-acetylalanine.
FT VAR_SEQ 1 107 Missing (in isoform 2).
FT /FTId=VSP_011913.
FT VAR_SEQ 213 264 VTNIKKTLKATASSSAQEMEQQLAERECPPHAEQRQPTKKM
FT SKVKGLVSSRH -> REKRDVPLLNLITTAFFWLPTSRRHS
FT KPPHPPRLRRWSSSWLNGSVPLTLSRGSPPRRCPK (in
FT isoform 3).
FT /FTId=VSP_040266.
SQ SEQUENCE 264 AA; 29622 MW; FF9279CEA6CB7707 CRC64;
MAGEQKPSSN LLEQFILLAK GTSGSALTAL ISQVLEAPGV YVFGELLELA NVQELAEGAN
AAYLQLLNLF AYGTYPDYIA NKESLPELST AQQNKLKHLT IVSLASRMKC IPYSVLLKDL
EMRNLRELED LIIEAVYTDI IQGKLDQRNQ LLEVDFCIGR DIRKKDINNI VKTLHEWCDG
CEAVLLGIEQ QVLRANQYKE NHNRTQQQVE AEVTNIKKTL KATASSSAQE MEQQLAEREC
PPHAEQRQPT KKMSKVKGLV SSRH
//
ID CSN7B_HUMAN Reviewed; 264 AA.
AC Q9H9Q2; Q53S22; Q5BJG3; Q9H7V6;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAR-2001, sequence version 1.
DT 22-JAN-2014, entry version 87.
DE RecName: Full=COP9 signalosome complex subunit 7b;
DE Short=SGN7b;
DE Short=Signalosome subunit 7b;
DE AltName: Full=JAB1-containing signalosome subunit 7b;
GN Name=COPS7B; Synonyms=CSN7B;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Teratocarcinoma, and Trachea;
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 [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.,
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 99-264 (ISOFORM 1).
RC TISSUE=Lung, and Testis;
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 [5]
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 [6]
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 [7]
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 [8]
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 [9]
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 [10]
RP IDENTIFICATION IN THE CSN COMPLEX, CLEAVAGE OF INITIATOR METHIONINE,
RP AND ACETYLATION AT ALA-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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-261 AND SER-263 (ISOFORM
RP 3), AND MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
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 JUN, I-kappa-B-alpha/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 COPS1,
CC COPS2, COPS4, COPS5, COPS6 and COPS8.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9H9Q2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H9Q2-2; Sequence=VSP_011913;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q9H9Q2-3; Sequence=VSP_040266;
CC Note=Contains a phosphothreonine at position 261. Contains a
CC phosphoserine at position 263;
CC -!- SIMILARITY: Belongs to the CSN7/EIF3M family. CSN7 subfamily.
CC -!- SIMILARITY: Contains 1 PCI domain.
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DR EMBL; AK022674; BAB14170.1; -; mRNA.
DR EMBL; AK024273; BAB14868.1; -; mRNA.
DR EMBL; AC073476; AAY24152.1; -; Genomic_DNA.
DR EMBL; CH471063; EAW70980.1; -; Genomic_DNA.
DR EMBL; BC010739; AAH10739.2; -; mRNA.
DR EMBL; BC091493; AAH91493.1; -; mRNA.
DR RefSeq; NP_001269879.1; NM_001282950.1.
DR RefSeq; NP_001269881.1; NM_001282952.1.
DR RefSeq; NP_073567.1; NM_022730.2.
DR UniGene; Hs.335061; -.
DR ProteinModelPortal; Q9H9Q2; -.
DR SMR; Q9H9Q2; 4-163.
DR DIP; DIP-53525N; -.
DR IntAct; Q9H9Q2; 3.
DR STRING; 9606.ENSP00000272995; -.
DR ChEMBL; CHEMBL5706; -.
DR PhosphoSite; Q9H9Q2; -.
DR DMDM; 55976598; -.
DR PaxDb; Q9H9Q2; -.
DR PRIDE; Q9H9Q2; -.
DR DNASU; 64708; -.
DR Ensembl; ENST00000350033; ENSP00000272995; ENSG00000144524.
DR Ensembl; ENST00000373608; ENSP00000362710; ENSG00000144524.
DR Ensembl; ENST00000409091; ENSP00000386527; ENSG00000144524.
DR Ensembl; ENST00000410024; ENSP00000386567; ENSG00000144524.
DR GeneID; 64708; -.
DR KEGG; hsa:64708; -.
DR UCSC; uc002vsg.1; human.
DR CTD; 64708; -.
DR GeneCards; GC02P232646; -.
DR HGNC; HGNC:16760; COPS7B.
DR HPA; HPA034675; -.
DR neXtProt; NX_Q9H9Q2; -.
DR PharmGKB; PA26759; -.
DR eggNOG; NOG289374; -.
DR HOGENOM; HOG000006003; -.
DR HOVERGEN; HBG051138; -.
DR KO; K12180; -.
DR OrthoDB; EOG7N63NJ; -.
DR PhylomeDB; Q9H9Q2; -.
DR ChiTaRS; COPS7B; human.
DR GeneWiki; COPS7B; -.
DR GenomeRNAi; 64708; -.
DR NextBio; 66639; -.
DR PRO; PR:Q9H9Q2; -.
DR ArrayExpress; Q9H9Q2; -.
DR Bgee; Q9H9Q2; -.
DR CleanEx; HS_COPS7B; -.
DR Genevestigator; Q9H9Q2; -.
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.
DR InterPro; IPR027530; Csn7.
DR InterPro; IPR000717; PCI_dom.
DR PANTHER; PTHR15350:SF5; PTHR15350:SF5; 1.
DR Pfam; PF01399; PCI; 1.
DR SMART; SM00088; PINT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Complete proteome;
KW Cytoplasm; Nucleus; Phosphoprotein; Reference proteome; Signalosome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 264 COP9 signalosome complex subunit 7b.
FT /FTId=PRO_0000120999.
FT DOMAIN 52 156 PCI.
FT COILED 188 237 Potential.
FT MOD_RES 2 2 N-acetylalanine.
FT VAR_SEQ 1 107 Missing (in isoform 2).
FT /FTId=VSP_011913.
FT VAR_SEQ 213 264 VTNIKKTLKATASSSAQEMEQQLAERECPPHAEQRQPTKKM
FT SKVKGLVSSRH -> REKRDVPLLNLITTAFFWLPTSRRHS
FT KPPHPPRLRRWSSSWLNGSVPLTLSRGSPPRRCPK (in
FT isoform 3).
FT /FTId=VSP_040266.
SQ SEQUENCE 264 AA; 29622 MW; FF9279CEA6CB7707 CRC64;
MAGEQKPSSN LLEQFILLAK GTSGSALTAL ISQVLEAPGV YVFGELLELA NVQELAEGAN
AAYLQLLNLF AYGTYPDYIA NKESLPELST AQQNKLKHLT IVSLASRMKC IPYSVLLKDL
EMRNLRELED LIIEAVYTDI IQGKLDQRNQ LLEVDFCIGR DIRKKDINNI VKTLHEWCDG
CEAVLLGIEQ QVLRANQYKE NHNRTQQQVE AEVTNIKKTL KATASSSAQE MEQQLAEREC
PPHAEQRQPT KKMSKVKGLV SSRH
//