Full text data of COPS3
COPS3
(CSN3)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
COP9 signalosome complex subunit 3; SGN3; Signalosome subunit 3 (JAB1-containing signalosome subunit 3)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
COP9 signalosome complex subunit 3; SGN3; Signalosome subunit 3 (JAB1-containing signalosome subunit 3)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9UNS2
ID CSN3_HUMAN Reviewed; 423 AA.
AC Q9UNS2; B2R683; B4DY81; O43191; Q7LDR6;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 116.
DE RecName: Full=COP9 signalosome complex subunit 3;
DE Short=SGN3;
DE Short=Signalosome subunit 3;
DE AltName: Full=JAB1-containing signalosome subunit 3;
GN Name=COPS3; Synonyms=CSN3;
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), PARTIAL PROTEIN SEQUENCE,
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Cervix carcinoma;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10191102; DOI=10.1006/geno.1998.5748;
RA Potocki L., Chen K.-S., Lupski J.R.;
RT "Subunit 3 of the COP9 signal transduction complex is conserved from
RT plants to humans and maps within the Smith-Magenis syndrome critical
RT region in 17p11.2.";
RL Genomics 57:180-182(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Hippocampus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in
RT the human lineage.";
RL Nature 440:1045-1049(2006).
RN [5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 PROTEIN SEQUENCE OF 2-13 (ISOFORM 1).
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [8]
RP PROTEIN SEQUENCE OF 2-13; 31-37; 244-251 AND 313-336 (ISOFORM 1),
RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma, and Platelet;
RA Bienvenut W.V., Quadroni M.;
RL Submitted (OCT-2005) to UniProtKB.
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 INTERACTION WITH IKBKG.
RX PubMed=11418127; DOI=10.1016/S0014-5793(01)02535-2;
RA Hong X., Xu L.-G., Li X., Zhai Z., Shu H.-B.;
RT "CSN3 interacts with IKKgamma and inhibits TNF- but not IL-1-induced
RT NF-kappaB activation.";
RL FEBS Lett. 499:133-136(2001).
RN [11]
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 [12]
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 [13]
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 [14]
RP FUNCTION, 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 [15]
RP OVEREXPRESSION IN OSTEOSARCOMA.
RX PubMed=12917637; DOI=10.1038/sj.onc.1206671;
RA Henriksen J., Aagesen T.H., Maelandsmo G.M., Lothe R.A., Myklebost O.,
RA Forus A.;
RT "Amplification and overexpression of COPS3 in osteosarcomas
RT potentially target TP53 for proteasome-mediated degradation.";
RL Oncogene 22:5358-5361(2003).
RN [16]
RP OVEREXPRESSION IN OSTEOSARCOMA.
RX PubMed=15325100; DOI=10.1016/j.cancergencyto.2004.03.007;
RA Van Dartel M., Hulsebos T.J.M.;
RT "Amplification and overexpression of genes in 17p11.2 approximately
RT p12 in osteosarcoma.";
RL Cancer Genet. Cytogenet. 153:77-80(2004).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [18]
RP IDENTIFICATION IN THE CSN COMPLEX, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, AND PHOSPHORYLATION AT SER-423.
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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-410 AND SER-423, AND
RP MASS SPECTROMETRY.
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 [20]
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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-423, 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 [22]
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).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-423, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [24]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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 COPS1,
CC COPS4 and COPS8. Interacts with CK2 and PKD. Interacts with the
CC translation initiation factor EIF3S6 and IKBKG.
CC -!- INTERACTION:
CC P10398:ARAF; NbExp=3; IntAct=EBI-350590, EBI-365961;
CC Q9Y6K9:IKBKG; NbExp=2; IntAct=EBI-350590, EBI-81279;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UNS2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UNS2-2; Sequence=VSP_044271;
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed at high level in
CC heart and skeletal muscle.
CC -!- MISCELLANEOUS: Amplified and overexpressed in some osteosarcomas
CC (OS), suggesting that it may participate in TP53 degradation in
CC OS.
CC -!- SIMILARITY: Belongs to the CSN3 family.
CC -!- SIMILARITY: Contains 1 PCI domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC14197.1; Type=Frameshift; Positions=5;
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DR EMBL; AF031647; AAC14197.1; ALT_FRAME; mRNA.
DR EMBL; AF098109; AAD41247.1; -; mRNA.
DR EMBL; AK312476; BAG35380.1; -; mRNA.
DR EMBL; AK302304; BAG63643.1; -; mRNA.
DR EMBL; AK316400; BAH14771.1; -; mRNA.
DR EMBL; AC055811; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471196; EAW55712.1; -; Genomic_DNA.
DR EMBL; BC001891; AAH01891.1; -; mRNA.
DR RefSeq; NP_001186054.1; NM_001199125.1.
DR RefSeq; NP_003644.2; NM_003653.3.
DR RefSeq; XP_005256894.1; XM_005256837.1.
DR UniGene; Hs.6076; -.
DR ProteinModelPortal; Q9UNS2; -.
DR SMR; Q9UNS2; 233-358.
DR DIP; DIP-32478N; -.
DR IntAct; Q9UNS2; 13.
DR MINT; MINT-129190; -.
DR STRING; 9606.ENSP00000268717; -.
DR PhosphoSite; Q9UNS2; -.
DR DMDM; 55976621; -.
DR PaxDb; Q9UNS2; -.
DR PeptideAtlas; Q9UNS2; -.
DR PRIDE; Q9UNS2; -.
DR DNASU; 8533; -.
DR Ensembl; ENST00000268717; ENSP00000268717; ENSG00000141030.
DR Ensembl; ENST00000539941; ENSP00000437606; ENSG00000141030.
DR GeneID; 8533; -.
DR KEGG; hsa:8533; -.
DR UCSC; uc002grd.3; human.
DR CTD; 8533; -.
DR GeneCards; GC17M017151; -.
DR HGNC; HGNC:2239; COPS3.
DR HPA; HPA021997; -.
DR MIM; 604665; gene.
DR neXtProt; NX_Q9UNS2; -.
DR PharmGKB; PA26755; -.
DR eggNOG; NOG249849; -.
DR HOGENOM; HOG000030451; -.
DR HOVERGEN; HBG051135; -.
DR InParanoid; Q9UNS2; -.
DR KO; K12177; -.
DR OMA; HKIDQEM; -.
DR OrthoDB; EOG7ZPNJV; -.
DR PhylomeDB; Q9UNS2; -.
DR SignaLink; Q9UNS2; -.
DR ChiTaRS; COPS3; human.
DR GeneWiki; COP9_signalosome_complex_subunit_3; -.
DR GenomeRNAi; 8533; -.
DR NextBio; 31960; -.
DR PRO; PR:Q9UNS2; -.
DR ArrayExpress; Q9UNS2; -.
DR Bgee; Q9UNS2; -.
DR CleanEx; HS_COPS3; -.
DR CleanEx; HS_CSN3; -.
DR Genevestigator; Q9UNS2; -.
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 GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0009416; P:response to light stimulus; TAS:ProtInc.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR011991; WHTH_DNA-bd_dom.
DR Pfam; PF01399; PCI; 1.
DR SMART; SM00088; PINT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Nucleus; Phosphoprotein;
KW Reference proteome; Signalosome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 423 COP9 signalosome complex subunit 3.
FT /FTId=PRO_0000120978.
FT DOMAIN 195 362 PCI.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 410 410 Phosphoserine.
FT MOD_RES 423 423 Phosphoserine.
FT VAR_SEQ 1 20 Missing (in isoform 2).
FT /FTId=VSP_044271.
SQ SEQUENCE 423 AA; 47873 MW; 1D371050C7D7BF8D CRC64;
MASALEQFVN SVRQLSAQGQ MTQLCELINK SGELLAKNLS HLDTVLGALD VQEHSLGVLA
VLFVKFSMPS VPDFETLFSQ VQLFISTCNG EHIRYATDTF AGLCHQLTNA LVERKQPLRG
IGILKQAIDK MQMNTNQLTS IHADLCQLCL LAKCFKPALP YLDVDMMDIC KENGAYDAKH
FLCYYYYGGM IYTGLKNFER ALYFYEQAIT TPAMAVSHIM LESYKKYILV SLILLGKVQQ
LPKYTSQIVG RFIKPLSNAY HELAQVYSTN NPSELRNLVN KHSETFTRDN NMGLVKQCLS
SLYKKNIQRL TKTFLTLSLQ DMASRVQLSG PQEAEKYVLH MIEDGEIFAS INQKDGMVSF
HDNPEKYNNP AMLHNIDQEM LKCIELDERL KAMDQEITVN PQFVQKSMGS QEDDSGNKPS
SYS
//
ID CSN3_HUMAN Reviewed; 423 AA.
AC Q9UNS2; B2R683; B4DY81; O43191; Q7LDR6;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 116.
DE RecName: Full=COP9 signalosome complex subunit 3;
DE Short=SGN3;
DE Short=Signalosome subunit 3;
DE AltName: Full=JAB1-containing signalosome subunit 3;
GN Name=COPS3; Synonyms=CSN3;
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), PARTIAL PROTEIN SEQUENCE,
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Cervix carcinoma;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10191102; DOI=10.1006/geno.1998.5748;
RA Potocki L., Chen K.-S., Lupski J.R.;
RT "Subunit 3 of the COP9 signal transduction complex is conserved from
RT plants to humans and maps within the Smith-Magenis syndrome critical
RT region in 17p11.2.";
RL Genomics 57:180-182(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Hippocampus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in
RT the human lineage.";
RL Nature 440:1045-1049(2006).
RN [5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 PROTEIN SEQUENCE OF 2-13 (ISOFORM 1).
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [8]
RP PROTEIN SEQUENCE OF 2-13; 31-37; 244-251 AND 313-336 (ISOFORM 1),
RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma, and Platelet;
RA Bienvenut W.V., Quadroni M.;
RL Submitted (OCT-2005) to UniProtKB.
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 INTERACTION WITH IKBKG.
RX PubMed=11418127; DOI=10.1016/S0014-5793(01)02535-2;
RA Hong X., Xu L.-G., Li X., Zhai Z., Shu H.-B.;
RT "CSN3 interacts with IKKgamma and inhibits TNF- but not IL-1-induced
RT NF-kappaB activation.";
RL FEBS Lett. 499:133-136(2001).
RN [11]
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 [12]
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 [13]
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 [14]
RP FUNCTION, 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 [15]
RP OVEREXPRESSION IN OSTEOSARCOMA.
RX PubMed=12917637; DOI=10.1038/sj.onc.1206671;
RA Henriksen J., Aagesen T.H., Maelandsmo G.M., Lothe R.A., Myklebost O.,
RA Forus A.;
RT "Amplification and overexpression of COPS3 in osteosarcomas
RT potentially target TP53 for proteasome-mediated degradation.";
RL Oncogene 22:5358-5361(2003).
RN [16]
RP OVEREXPRESSION IN OSTEOSARCOMA.
RX PubMed=15325100; DOI=10.1016/j.cancergencyto.2004.03.007;
RA Van Dartel M., Hulsebos T.J.M.;
RT "Amplification and overexpression of genes in 17p11.2 approximately
RT p12 in osteosarcoma.";
RL Cancer Genet. Cytogenet. 153:77-80(2004).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [18]
RP IDENTIFICATION IN THE CSN COMPLEX, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, AND PHOSPHORYLATION AT SER-423.
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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-410 AND SER-423, AND
RP MASS SPECTROMETRY.
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 [20]
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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-423, 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 [22]
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).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-423, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [24]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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 COPS1,
CC COPS4 and COPS8. Interacts with CK2 and PKD. Interacts with the
CC translation initiation factor EIF3S6 and IKBKG.
CC -!- INTERACTION:
CC P10398:ARAF; NbExp=3; IntAct=EBI-350590, EBI-365961;
CC Q9Y6K9:IKBKG; NbExp=2; IntAct=EBI-350590, EBI-81279;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UNS2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UNS2-2; Sequence=VSP_044271;
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed at high level in
CC heart and skeletal muscle.
CC -!- MISCELLANEOUS: Amplified and overexpressed in some osteosarcomas
CC (OS), suggesting that it may participate in TP53 degradation in
CC OS.
CC -!- SIMILARITY: Belongs to the CSN3 family.
CC -!- SIMILARITY: Contains 1 PCI domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC14197.1; Type=Frameshift; Positions=5;
CC -----------------------------------------------------------------------
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DR EMBL; AF031647; AAC14197.1; ALT_FRAME; mRNA.
DR EMBL; AF098109; AAD41247.1; -; mRNA.
DR EMBL; AK312476; BAG35380.1; -; mRNA.
DR EMBL; AK302304; BAG63643.1; -; mRNA.
DR EMBL; AK316400; BAH14771.1; -; mRNA.
DR EMBL; AC055811; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471196; EAW55712.1; -; Genomic_DNA.
DR EMBL; BC001891; AAH01891.1; -; mRNA.
DR RefSeq; NP_001186054.1; NM_001199125.1.
DR RefSeq; NP_003644.2; NM_003653.3.
DR RefSeq; XP_005256894.1; XM_005256837.1.
DR UniGene; Hs.6076; -.
DR ProteinModelPortal; Q9UNS2; -.
DR SMR; Q9UNS2; 233-358.
DR DIP; DIP-32478N; -.
DR IntAct; Q9UNS2; 13.
DR MINT; MINT-129190; -.
DR STRING; 9606.ENSP00000268717; -.
DR PhosphoSite; Q9UNS2; -.
DR DMDM; 55976621; -.
DR PaxDb; Q9UNS2; -.
DR PeptideAtlas; Q9UNS2; -.
DR PRIDE; Q9UNS2; -.
DR DNASU; 8533; -.
DR Ensembl; ENST00000268717; ENSP00000268717; ENSG00000141030.
DR Ensembl; ENST00000539941; ENSP00000437606; ENSG00000141030.
DR GeneID; 8533; -.
DR KEGG; hsa:8533; -.
DR UCSC; uc002grd.3; human.
DR CTD; 8533; -.
DR GeneCards; GC17M017151; -.
DR HGNC; HGNC:2239; COPS3.
DR HPA; HPA021997; -.
DR MIM; 604665; gene.
DR neXtProt; NX_Q9UNS2; -.
DR PharmGKB; PA26755; -.
DR eggNOG; NOG249849; -.
DR HOGENOM; HOG000030451; -.
DR HOVERGEN; HBG051135; -.
DR InParanoid; Q9UNS2; -.
DR KO; K12177; -.
DR OMA; HKIDQEM; -.
DR OrthoDB; EOG7ZPNJV; -.
DR PhylomeDB; Q9UNS2; -.
DR SignaLink; Q9UNS2; -.
DR ChiTaRS; COPS3; human.
DR GeneWiki; COP9_signalosome_complex_subunit_3; -.
DR GenomeRNAi; 8533; -.
DR NextBio; 31960; -.
DR PRO; PR:Q9UNS2; -.
DR ArrayExpress; Q9UNS2; -.
DR Bgee; Q9UNS2; -.
DR CleanEx; HS_COPS3; -.
DR CleanEx; HS_CSN3; -.
DR Genevestigator; Q9UNS2; -.
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 GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0009416; P:response to light stimulus; TAS:ProtInc.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR011991; WHTH_DNA-bd_dom.
DR Pfam; PF01399; PCI; 1.
DR SMART; SM00088; PINT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Nucleus; Phosphoprotein;
KW Reference proteome; Signalosome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 423 COP9 signalosome complex subunit 3.
FT /FTId=PRO_0000120978.
FT DOMAIN 195 362 PCI.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 410 410 Phosphoserine.
FT MOD_RES 423 423 Phosphoserine.
FT VAR_SEQ 1 20 Missing (in isoform 2).
FT /FTId=VSP_044271.
SQ SEQUENCE 423 AA; 47873 MW; 1D371050C7D7BF8D CRC64;
MASALEQFVN SVRQLSAQGQ MTQLCELINK SGELLAKNLS HLDTVLGALD VQEHSLGVLA
VLFVKFSMPS VPDFETLFSQ VQLFISTCNG EHIRYATDTF AGLCHQLTNA LVERKQPLRG
IGILKQAIDK MQMNTNQLTS IHADLCQLCL LAKCFKPALP YLDVDMMDIC KENGAYDAKH
FLCYYYYGGM IYTGLKNFER ALYFYEQAIT TPAMAVSHIM LESYKKYILV SLILLGKVQQ
LPKYTSQIVG RFIKPLSNAY HELAQVYSTN NPSELRNLVN KHSETFTRDN NMGLVKQCLS
SLYKKNIQRL TKTFLTLSLQ DMASRVQLSG PQEAEKYVLH MIEDGEIFAS INQKDGMVSF
HDNPEKYNNP AMLHNIDQEM LKCIELDERL KAMDQEITVN PQFVQKSMGS QEDDSGNKPS
SYS
//
MIM
604665
*RECORD*
*FIELD* NO
604665
*FIELD* TI
*604665 COP9, SUBUNIT 3; COPS3
;;SGN3
*FIELD* TX
To identify new components of the 26S proteasome, Seeger et al. (1998)
read moreobtained peptide sequences from a 45-kD protein. By micropeptide
sequence analysis and probing of cDNA libraries, Seeger et al. (1998)
isolated a cDNA encoding COPS3, which they termed SGN3, for subunit 3 of
a novel 450-kD signalosome complex that also includes TRIP15 (604508),
COPS5 (604850), GPS1 (601934), and 4 other subunits. Sequence analysis
predicted that COPS3 is a 403-amino acid protein which contains regions
with homology to the 26S proteasome S3 regulatory subunit.
Autoradiographic analysis showed that the complex phosphorylates JUN
(165160), IKBA (164008), and the C-terminal part of the p105 precursor
of NFKB (164011). The 26S proteasome is not a phosphorylation target,
although immunofluorescence microscopy demonstrated that the 450-kD
complex has a cytosolic localization, concentrated around the nucleus.
Elsea et al. (1999) reported the localization and partial
characterization of SGN3. They mapped the SGN3 gene to 17p11.2 by
somatic cell hybrid analysis. By analysis of genomic clones, they
further localized the SGN3 gene to the distal end of the Smith-Magenis
syndrome (SMS) critical region (182290), near marker D17S71. Although
SMS patients were haploinsufficient for SGN3, analyses showed that the
SGN3 protein was present at equivalent levels in patient and parental
control cells, and that the COP9 signalosome complex was assembled and
in normal quantities in transformed lymphoblastoid cell lines from
patients. Elsea et al. (1999) concluded that SGN3 probably does not play
a significant role with respect to SMS, although its involvement could
not be ruled out since the importance of the COP9 signalosome in
embryogenesis or differentiation was not well understood.
*FIELD* RF
1. Elsea, S. H.; Mykytyn, K.; Ferrell, K.; Coulter, K. L.; Das, P.;
Dubiel, W.; Patel, P. I.; Metherall, J. E.: Hemizygosity for the
COP9 signalosome subunit gene, SGN3, in the Smith-Magenis syndrome. Am.
J. Med. Genet. 87: 342-348, 1999.
2. Seeger, M.; Kraft, R.; Ferrell, K.; Bech-Otschir, D.; Dumdey, R.;
Schade, R.; Gordon, C.; Naumann, M.; Dubiel, W.: A novel protein
complex involved in signal transduction possessing similarities to
26S proteasome subunits. FASEB J. 12: 469-478, 1998.
*FIELD* CN
Paul J. Converse - updated: 10/12/2000
*FIELD* CD
Sonja A. Rasmussen: 3/8/2000
*FIELD* ED
carol: 10/26/2000
mcapotos: 10/19/2000
terry: 10/12/2000
mgross: 3/8/2000
*RECORD*
*FIELD* NO
604665
*FIELD* TI
*604665 COP9, SUBUNIT 3; COPS3
;;SGN3
*FIELD* TX
To identify new components of the 26S proteasome, Seeger et al. (1998)
read moreobtained peptide sequences from a 45-kD protein. By micropeptide
sequence analysis and probing of cDNA libraries, Seeger et al. (1998)
isolated a cDNA encoding COPS3, which they termed SGN3, for subunit 3 of
a novel 450-kD signalosome complex that also includes TRIP15 (604508),
COPS5 (604850), GPS1 (601934), and 4 other subunits. Sequence analysis
predicted that COPS3 is a 403-amino acid protein which contains regions
with homology to the 26S proteasome S3 regulatory subunit.
Autoradiographic analysis showed that the complex phosphorylates JUN
(165160), IKBA (164008), and the C-terminal part of the p105 precursor
of NFKB (164011). The 26S proteasome is not a phosphorylation target,
although immunofluorescence microscopy demonstrated that the 450-kD
complex has a cytosolic localization, concentrated around the nucleus.
Elsea et al. (1999) reported the localization and partial
characterization of SGN3. They mapped the SGN3 gene to 17p11.2 by
somatic cell hybrid analysis. By analysis of genomic clones, they
further localized the SGN3 gene to the distal end of the Smith-Magenis
syndrome (SMS) critical region (182290), near marker D17S71. Although
SMS patients were haploinsufficient for SGN3, analyses showed that the
SGN3 protein was present at equivalent levels in patient and parental
control cells, and that the COP9 signalosome complex was assembled and
in normal quantities in transformed lymphoblastoid cell lines from
patients. Elsea et al. (1999) concluded that SGN3 probably does not play
a significant role with respect to SMS, although its involvement could
not be ruled out since the importance of the COP9 signalosome in
embryogenesis or differentiation was not well understood.
*FIELD* RF
1. Elsea, S. H.; Mykytyn, K.; Ferrell, K.; Coulter, K. L.; Das, P.;
Dubiel, W.; Patel, P. I.; Metherall, J. E.: Hemizygosity for the
COP9 signalosome subunit gene, SGN3, in the Smith-Magenis syndrome. Am.
J. Med. Genet. 87: 342-348, 1999.
2. Seeger, M.; Kraft, R.; Ferrell, K.; Bech-Otschir, D.; Dumdey, R.;
Schade, R.; Gordon, C.; Naumann, M.; Dubiel, W.: A novel protein
complex involved in signal transduction possessing similarities to
26S proteasome subunits. FASEB J. 12: 469-478, 1998.
*FIELD* CN
Paul J. Converse - updated: 10/12/2000
*FIELD* CD
Sonja A. Rasmussen: 3/8/2000
*FIELD* ED
carol: 10/26/2000
mcapotos: 10/19/2000
terry: 10/12/2000
mgross: 3/8/2000