Full text data of COPS7A
COPS7A
(CSN7A, DERP10)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
COP9 signalosome complex subunit 7a; SGN7a; Signalosome subunit 7a (Dermal papilla-derived protein 10; JAB1-containing signalosome subunit 7a)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
COP9 signalosome complex subunit 7a; SGN7a; Signalosome subunit 7a (Dermal papilla-derived protein 10; JAB1-containing signalosome subunit 7a)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9UBW8
ID CSN7A_HUMAN Reviewed; 275 AA.
AC Q9UBW8; A8K9A6; Q9NVX3; Q9UJW4;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-2000, sequence version 1.
DT 22-JAN-2014, entry version 100.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INTERACTION WITH
RP 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
RT COP9 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.,
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 [6]
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 (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
RT project: 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;
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 [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.,
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 [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.,
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 [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.,
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 [14]
RP IDENTIFICATION IN THE CSN COMPLEX, CLEAVAGE OF INITIATOR METHIONINE,
RP AND 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.,
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. Interacts with PMF1.
CC Interacts with the translation initiation factor EIF3S6. Interacts
CC with CK2 and PKD. Interacts directly with ID3.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed at high level in
CC brain, heart and skeletal muscle.
CC -!- PTM: Phosphorylated by CK2 and PKD kinases.
CC -!- SIMILARITY: Belongs to the CSN7/EIF3M family. CSN7 subfamily.
CC -!- SIMILARITY: Contains 1 PCI domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 RefSeq; NP_001157565.1; NM_001164093.1.
DR RefSeq; NP_001157566.1; NM_001164094.1.
DR RefSeq; NP_001157567.1; NM_001164095.1.
DR RefSeq; NP_057403.1; NM_016319.2.
DR RefSeq; XP_005253751.1; XM_005253694.1.
DR RefSeq; XP_005253752.1; XM_005253695.1.
DR UniGene; Hs.530823; -.
DR ProteinModelPortal; Q9UBW8; -.
DR SMR; Q9UBW8; 13-163.
DR DIP; DIP-53412N; -.
DR IntAct; Q9UBW8; 7.
DR MINT; MINT-1393951; -.
DR STRING; 9606.ENSP00000229251; -.
DR PhosphoSite; Q9UBW8; -.
DR DMDM; 55976618; -.
DR PaxDb; Q9UBW8; -.
DR PeptideAtlas; Q9UBW8; -.
DR PRIDE; Q9UBW8; -.
DR DNASU; 50813; -.
DR Ensembl; ENST00000229251; ENSP00000229251; ENSG00000111652.
DR Ensembl; ENST00000534877; ENSP00000438363; ENSG00000111652.
DR Ensembl; ENST00000534947; ENSP00000446039; ENSG00000111652.
DR Ensembl; ENST00000539735; ENSP00000441852; ENSG00000111652.
DR Ensembl; ENST00000543155; ENSP00000438115; ENSG00000111652.
DR GeneID; 50813; -.
DR KEGG; hsa:50813; -.
DR UCSC; uc001qqh.3; human.
DR CTD; 50813; -.
DR GeneCards; GC12P006833; -.
DR HGNC; HGNC:16758; COPS7A.
DR HPA; HPA026915; -.
DR neXtProt; NX_Q9UBW8; -.
DR PharmGKB; PA26758; -.
DR eggNOG; NOG289374; -.
DR HOGENOM; HOG000006003; -.
DR HOVERGEN; HBG051138; -.
DR InParanoid; Q9UBW8; -.
DR KO; K12180; -.
DR OMA; INALAPF; -.
DR OrthoDB; EOG7N63NJ; -.
DR PhylomeDB; Q9UBW8; -.
DR ChiTaRS; COPS7A; human.
DR GeneWiki; COPS7A; -.
DR GenomeRNAi; 50813; -.
DR NextBio; 53257; -.
DR PRO; PR:Q9UBW8; -.
DR ArrayExpress; Q9UBW8; -.
DR Bgee; Q9UBW8; -.
DR CleanEx; HS_COPS7A; -.
DR Genevestigator; Q9UBW8; -.
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; Coiled coil; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Nucleus; Phosphoprotein;
KW Reference proteome; Signalosome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 275 COP9 signalosome complex subunit 7a.
FT /FTId=PRO_0000120996.
FT DOMAIN 52 156 PCI.
FT COILED 185 233 Potential.
FT MOD_RES 2 2 N-acetylserine.
FT CONFLICT 218 218 K -> E (in Ref. 5; BAA91620).
FT CONFLICT 253 253 Q -> H (in Ref. 4; AAF04307).
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
//
ID CSN7A_HUMAN Reviewed; 275 AA.
AC Q9UBW8; A8K9A6; Q9NVX3; Q9UJW4;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-2000, sequence version 1.
DT 22-JAN-2014, entry version 100.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INTERACTION WITH
RP 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
RT COP9 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.,
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 [6]
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 (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
RT project: 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;
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 [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.,
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 [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.,
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 [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.,
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 [14]
RP IDENTIFICATION IN THE CSN COMPLEX, CLEAVAGE OF INITIATOR METHIONINE,
RP AND 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.,
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. Interacts with PMF1.
CC Interacts with the translation initiation factor EIF3S6. Interacts
CC with CK2 and PKD. Interacts directly with ID3.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed at high level in
CC brain, heart and skeletal muscle.
CC -!- PTM: Phosphorylated by CK2 and PKD kinases.
CC -!- SIMILARITY: Belongs to the CSN7/EIF3M family. CSN7 subfamily.
CC -!- SIMILARITY: Contains 1 PCI domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 RefSeq; NP_001157565.1; NM_001164093.1.
DR RefSeq; NP_001157566.1; NM_001164094.1.
DR RefSeq; NP_001157567.1; NM_001164095.1.
DR RefSeq; NP_057403.1; NM_016319.2.
DR RefSeq; XP_005253751.1; XM_005253694.1.
DR RefSeq; XP_005253752.1; XM_005253695.1.
DR UniGene; Hs.530823; -.
DR ProteinModelPortal; Q9UBW8; -.
DR SMR; Q9UBW8; 13-163.
DR DIP; DIP-53412N; -.
DR IntAct; Q9UBW8; 7.
DR MINT; MINT-1393951; -.
DR STRING; 9606.ENSP00000229251; -.
DR PhosphoSite; Q9UBW8; -.
DR DMDM; 55976618; -.
DR PaxDb; Q9UBW8; -.
DR PeptideAtlas; Q9UBW8; -.
DR PRIDE; Q9UBW8; -.
DR DNASU; 50813; -.
DR Ensembl; ENST00000229251; ENSP00000229251; ENSG00000111652.
DR Ensembl; ENST00000534877; ENSP00000438363; ENSG00000111652.
DR Ensembl; ENST00000534947; ENSP00000446039; ENSG00000111652.
DR Ensembl; ENST00000539735; ENSP00000441852; ENSG00000111652.
DR Ensembl; ENST00000543155; ENSP00000438115; ENSG00000111652.
DR GeneID; 50813; -.
DR KEGG; hsa:50813; -.
DR UCSC; uc001qqh.3; human.
DR CTD; 50813; -.
DR GeneCards; GC12P006833; -.
DR HGNC; HGNC:16758; COPS7A.
DR HPA; HPA026915; -.
DR neXtProt; NX_Q9UBW8; -.
DR PharmGKB; PA26758; -.
DR eggNOG; NOG289374; -.
DR HOGENOM; HOG000006003; -.
DR HOVERGEN; HBG051138; -.
DR InParanoid; Q9UBW8; -.
DR KO; K12180; -.
DR OMA; INALAPF; -.
DR OrthoDB; EOG7N63NJ; -.
DR PhylomeDB; Q9UBW8; -.
DR ChiTaRS; COPS7A; human.
DR GeneWiki; COPS7A; -.
DR GenomeRNAi; 50813; -.
DR NextBio; 53257; -.
DR PRO; PR:Q9UBW8; -.
DR ArrayExpress; Q9UBW8; -.
DR Bgee; Q9UBW8; -.
DR CleanEx; HS_COPS7A; -.
DR Genevestigator; Q9UBW8; -.
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; Coiled coil; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Nucleus; Phosphoprotein;
KW Reference proteome; Signalosome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 275 COP9 signalosome complex subunit 7a.
FT /FTId=PRO_0000120996.
FT DOMAIN 52 156 PCI.
FT COILED 185 233 Potential.
FT MOD_RES 2 2 N-acetylserine.
FT CONFLICT 218 218 K -> E (in Ref. 5; BAA91620).
FT CONFLICT 253 253 Q -> H (in Ref. 4; AAF04307).
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
//