CSN3_HUMAN
ID CSN3_HUMAN Reviewed; 423 AA.
AC Q9UNS2; B2R683; B4DY81; O43191; Q7LDR6;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 188.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, FUNCTION,
RP AND SUBCELLULAR LOCATION.
RC TISSUE=Cervix carcinoma;
RX PubMed=9535219; DOI=10.1096/fasebj.12.6.469;
RA Seeger M., Kraft R., Ferrell K., Bech-Otschir D., Dumdey R., Schade R.,
RA Gordon C., Naumann M., Dubiel W.;
RT "A novel protein complex involved in signal transduction possessing
RT similarities to 26S proteasome subunits.";
RL FASEB J. 12:469-478(1998).
RN [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 plants
RT to humans and maps within the Smith-Magenis syndrome critical region in
RT 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [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., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., 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 the
RT 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (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 project:
RT 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., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT 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), CLEAVAGE
RP OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY 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., Pollmann C.,
RA Dubiel W.;
RT "COP9 signalosome-specific phosphorylation targets p53 to degradation by
RT the ubiquitin system.";
RL EMBO J. 20:1630-1639(2001).
RN [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 NF-
RT 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., Drapkin R.,
RA Kisselev A.F., Tanaka K., Nakatani Y.;
RT "The ubiquitin ligase activity in the DDB2 and CSA complexes is
RT differentially regulated by the COP9 signalosome in response to DNA
RT damage.";
RL Cell 113:357-367(2003).
RN [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., Bech-Otschir D.,
RA Huang X., Berse M., Sperling J., Schade R., Dubiel W.;
RT "Protein kinase CK2 and protein kinase D are associated with the COP9
RT signalosome.";
RL EMBO J. 22:1302-1312(2003).
RN [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 potentially
RT 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 p12 in
RT 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, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-423, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [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., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-423, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [24]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [25]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
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., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-410, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [27]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [28]
RP COMPOSITION OF THE CSN COMPLEX, AND INTERACTION WITH COPS9.
RX PubMed=26456823; DOI=10.1016/j.celrep.2015.09.021;
RA Rozen S., Fuezesi-Levi M.G., Ben-Nissan G., Mizrachi L., Gabashvili A.,
RA Levin Y., Ben-Dor S., Eisenstein M., Sharon M.;
RT "CSNAP is a stoichiometric subunit of the COP9 signalosome.";
RL Cell Rep. 13:585-598(2015).
RN [29]
RP INTERACTION WITH ERCC6.
RX PubMed=26030138; DOI=10.1371/journal.pone.0128558;
RA Nicolai S., Filippi S., Caputo M., Cipak L., Gregan J., Ammerer G.,
RA Frontini M., Willems D., Prantera G., Balajee A.S., Proietti-De-Santis L.;
RT "Identification of Novel Proteins Co-Purifying with Cockayne Syndrome Group
RT B (CSB) Reveals Potential Roles for CSB in RNA Metabolism and Chromatin
RT Dynamics.";
RL PLoS ONE 10:E0128558-E0128558(2015).
CC -!- FUNCTION: Component of the COP9 signalosome complex (CSN), a complex
CC involved in various cellular and developmental processes. The CSN
CC complex is an essential regulator of the ubiquitin (Ubl) conjugation
CC pathway by mediating the deneddylation of the cullin subunits of SCF-
CC type E3 ligase complexes, leading to decrease the Ubl ligase activity
CC of SCF-type complexes such as SCF, CSA or DDB2. The complex is also
CC involved in phosphorylation of p53/TP53, c-jun/JUN,
CC IkappaBalpha/NFKBIA, ITPK1 and IRF8/ICSBP, possibly via its association
CC with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN
CC promotes and protects degradation by the Ubl system, respectively.
CC {ECO:0000269|PubMed:11285227, ECO:0000269|PubMed:11337588,
CC ECO:0000269|PubMed:12628923, ECO:0000269|PubMed:12732143,
CC ECO:0000269|PubMed:9535219}.
CC -!- SUBUNIT: Component of the CSN complex, composed of COPS1/GPS1, COPS2,
CC COPS3, COPS4, COPS5, COPS6, COPS7 (COPS7A or COPS7B), COPS8 and COPS9
CC isoform 1 (PubMed:18850735, PubMed:26456823). In the complex, it
CC probably interacts directly with COPS1, COPS4, COPS8 and COPS9 isoform
CC 1 (PubMed:18850735, PubMed:26456823). Interacts with CK2 and PKD
CC (PubMed:12628923). Interacts with the translation initiation factor
CC EIF3S6 and IKBKG (PubMed:11418127, PubMed:12220626). Interacts with
CC ERCC6 (PubMed:26030138). {ECO:0000269|PubMed:11418127,
CC ECO:0000269|PubMed:12220626, ECO:0000269|PubMed:12628923,
CC ECO:0000269|PubMed:18850735, ECO:0000269|PubMed:26030138,
CC ECO:0000269|PubMed:26456823}.
CC -!- INTERACTION:
CC Q9UNS2; P01023: A2M; NbExp=3; IntAct=EBI-350590, EBI-640741;
CC Q9UNS2; P10398: ARAF; NbExp=3; IntAct=EBI-350590, EBI-365961;
CC Q9UNS2; P18085: ARF4; NbExp=3; IntAct=EBI-350590, EBI-1237085;
CC Q9UNS2; P45381: ASPA; NbExp=3; IntAct=EBI-350590, EBI-750475;
CC Q9UNS2; Q9UBB4: ATXN10; NbExp=3; IntAct=EBI-350590, EBI-702390;
CC Q9UNS2; Q96G97-4: BSCL2; NbExp=3; IntAct=EBI-350590, EBI-10178113;
CC Q9UNS2; Q9HAS0: C17orf75; NbExp=3; IntAct=EBI-350590, EBI-12954949;
CC Q9UNS2; P48643: CCT5; NbExp=3; IntAct=EBI-350590, EBI-355710;
CC Q9UNS2; P61201: COPS2; NbExp=11; IntAct=EBI-350590, EBI-1050386;
CC Q9UNS2; Q92905: COPS5; NbExp=17; IntAct=EBI-350590, EBI-594661;
CC Q9UNS2; Q7L5N1: COPS6; NbExp=23; IntAct=EBI-350590, EBI-486838;
CC Q9UNS2; Q9UBW8: COPS7A; NbExp=10; IntAct=EBI-350590, EBI-712982;
CC Q9UNS2; Q99627: COPS8; NbExp=15; IntAct=EBI-350590, EBI-2510102;
CC Q9UNS2; P09172: DBH; NbExp=3; IntAct=EBI-350590, EBI-8589586;
CC Q9UNS2; Q14203-5: DCTN1; NbExp=3; IntAct=EBI-350590, EBI-25840379;
CC Q9UNS2; P26378-2: ELAVL4; NbExp=3; IntAct=EBI-350590, EBI-21603100;
CC Q9UNS2; Q13216-2: ERCC8; NbExp=3; IntAct=EBI-350590, EBI-16466949;
CC Q9UNS2; Q8NFF5-2: FLAD1; NbExp=3; IntAct=EBI-350590, EBI-11526128;
CC Q9UNS2; O43559: FRS3; NbExp=3; IntAct=EBI-350590, EBI-725515;
CC Q9UNS2; P41250: GARS1; NbExp=3; IntAct=EBI-350590, EBI-724143;
CC Q9UNS2; Q53GS7: GLE1; NbExp=3; IntAct=EBI-350590, EBI-1955541;
CC Q9UNS2; P28799: GRN; NbExp=3; IntAct=EBI-350590, EBI-747754;
CC Q9UNS2; P07686: HEXB; NbExp=3; IntAct=EBI-350590, EBI-7133736;
CC Q9UNS2; P28358: HOXD10; NbExp=3; IntAct=EBI-350590, EBI-12690664;
CC Q9UNS2; P04792: HSPB1; NbExp=3; IntAct=EBI-350590, EBI-352682;
CC Q9UNS2; P42858: HTT; NbExp=22; IntAct=EBI-350590, EBI-466029;
CC Q9UNS2; Q9Y6K9: IKBKG; NbExp=2; IntAct=EBI-350590, EBI-81279;
CC Q9UNS2; Q6KB66-2: KRT80; NbExp=3; IntAct=EBI-350590, EBI-11999246;
CC Q9UNS2; P02545-2: LMNA; NbExp=3; IntAct=EBI-350590, EBI-351953;
CC Q9UNS2; P51608: MECP2; NbExp=3; IntAct=EBI-350590, EBI-1189067;
CC Q9UNS2; Q96AH0: NABP1; NbExp=3; IntAct=EBI-350590, EBI-2889252;
CC Q9UNS2; P19404: NDUFV2; NbExp=3; IntAct=EBI-350590, EBI-713665;
CC Q9UNS2; P35240: NF2; NbExp=3; IntAct=EBI-350590, EBI-1014472;
CC Q9UNS2; P29474: NOS3; NbExp=3; IntAct=EBI-350590, EBI-1391623;
CC Q9UNS2; Q9BZ23-2: PANK2; NbExp=3; IntAct=EBI-350590, EBI-25929070;
CC Q9UNS2; O43933: PEX1; NbExp=3; IntAct=EBI-350590, EBI-988601;
CC Q9UNS2; Q7Z412: PEX26; NbExp=3; IntAct=EBI-350590, EBI-752057;
CC Q9UNS2; O14832: PHYH; NbExp=3; IntAct=EBI-350590, EBI-721853;
CC Q9UNS2; O60260-5: PRKN; NbExp=3; IntAct=EBI-350590, EBI-21251460;
CC Q9UNS2; P41219: PRPH; NbExp=3; IntAct=EBI-350590, EBI-752074;
CC Q9UNS2; Q8TBF2: PRXL2B; NbExp=5; IntAct=EBI-350590, EBI-7280826;
CC Q9UNS2; P51149: RAB7A; NbExp=3; IntAct=EBI-350590, EBI-1056089;
CC Q9UNS2; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-350590, EBI-396669;
CC Q9UNS2; P37840: SNCA; NbExp=3; IntAct=EBI-350590, EBI-985879;
CC Q9UNS2; Q16143: SNCB; NbExp=3; IntAct=EBI-350590, EBI-727106;
CC Q9UNS2; Q07889: SOS1; NbExp=3; IntAct=EBI-350590, EBI-297487;
CC Q9UNS2; O14656: TOR1A; NbExp=3; IntAct=EBI-350590, EBI-524257;
CC Q9UNS2; Q6IQ55-3: TTBK2; NbExp=3; IntAct=EBI-350590, EBI-25930156;
CC Q9UNS2; P02766: TTR; NbExp=3; IntAct=EBI-350590, EBI-711909;
CC Q9UNS2; P09936: UCHL1; NbExp=3; IntAct=EBI-350590, EBI-714860;
CC Q9UNS2; P54577: YARS1; NbExp=3; IntAct=EBI-350590, EBI-1048893;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9535219}. Nucleus
CC {ECO:0000269|PubMed:9535219}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UNS2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UNS2-2; Sequence=VSP_044271;
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed at high level in heart
CC and skeletal muscle. {ECO:0000269|PubMed:10191102}.
CC -!- MISCELLANEOUS: Amplified and overexpressed in some osteosarcomas (OS),
CC suggesting that it may participate in TP53 degradation in OS.
CC -!- SIMILARITY: Belongs to the CSN3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC14197.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; 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 CCDS; CCDS11183.1; -. [Q9UNS2-1]
DR CCDS; CCDS56022.1; -. [Q9UNS2-2]
DR RefSeq; NP_001186054.1; NM_001199125.1. [Q9UNS2-2]
DR RefSeq; NP_001303283.1; NM_001316354.1.
DR RefSeq; NP_001303284.1; NM_001316355.1.
DR RefSeq; NP_001303285.1; NM_001316356.1.
DR RefSeq; NP_001303286.1; NM_001316357.1.
DR RefSeq; NP_001303287.1; NM_001316358.1.
DR RefSeq; NP_003644.2; NM_003653.3. [Q9UNS2-1]
DR RefSeq; XP_005256894.1; XM_005256837.4. [Q9UNS2-2]
DR PDB; 4D10; X-ray; 3.80 A; C/K=1-423.
DR PDB; 4D18; X-ray; 4.08 A; C/K=1-423.
DR PDB; 4WSN; X-ray; 5.50 A; C/K/S/a/i/q=1-423.
DR PDB; 6R6H; EM; 8.40 A; C=1-383.
DR PDB; 6R7F; EM; 8.20 A; C=1-403.
DR PDB; 6R7H; EM; 8.80 A; C=1-403.
DR PDB; 6R7I; EM; 5.90 A; C=3-403.
DR PDB; 6R7N; EM; 6.50 A; C=3-403.
DR PDBsum; 4D10; -.
DR PDBsum; 4D18; -.
DR PDBsum; 4WSN; -.
DR PDBsum; 6R6H; -.
DR PDBsum; 6R7F; -.
DR PDBsum; 6R7H; -.
DR PDBsum; 6R7I; -.
DR PDBsum; 6R7N; -.
DR AlphaFoldDB; Q9UNS2; -.
DR SMR; Q9UNS2; -.
DR BioGRID; 114103; 169.
DR ComplexPortal; CPX-1870; COP9 signalosome variant 1.
DR ComplexPortal; CPX-1871; COP9 signalosome variant 2.
DR CORUM; Q9UNS2; -.
DR DIP; DIP-32478N; -.
DR IntAct; Q9UNS2; 107.
DR MINT; Q9UNS2; -.
DR STRING; 9606.ENSP00000268717; -.
DR GlyGen; Q9UNS2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UNS2; -.
DR MetOSite; Q9UNS2; -.
DR PhosphoSitePlus; Q9UNS2; -.
DR SwissPalm; Q9UNS2; -.
DR BioMuta; COPS3; -.
DR DMDM; 55976621; -.
DR EPD; Q9UNS2; -.
DR jPOST; Q9UNS2; -.
DR MassIVE; Q9UNS2; -.
DR MaxQB; Q9UNS2; -.
DR PaxDb; Q9UNS2; -.
DR PeptideAtlas; Q9UNS2; -.
DR PRIDE; Q9UNS2; -.
DR ProteomicsDB; 5506; -.
DR ProteomicsDB; 85328; -. [Q9UNS2-1]
DR Antibodypedia; 13330; 376 antibodies from 39 providers.
DR DNASU; 8533; -.
DR Ensembl; ENST00000268717.10; ENSP00000268717.5; ENSG00000141030.13. [Q9UNS2-1]
DR Ensembl; ENST00000539941.6; ENSP00000437606.2; ENSG00000141030.13. [Q9UNS2-2]
DR GeneID; 8533; -.
DR KEGG; hsa:8533; -.
DR MANE-Select; ENST00000268717.10; ENSP00000268717.5; NM_003653.4; NP_003644.2.
DR UCSC; uc002grd.4; human. [Q9UNS2-1]
DR CTD; 8533; -.
DR DisGeNET; 8533; -.
DR GeneCards; COPS3; -.
DR HGNC; HGNC:2239; COPS3.
DR HPA; ENSG00000141030; Low tissue specificity.
DR MIM; 604665; gene.
DR neXtProt; NX_Q9UNS2; -.
DR OpenTargets; ENSG00000141030; -.
DR PharmGKB; PA26755; -.
DR VEuPathDB; HostDB:ENSG00000141030; -.
DR eggNOG; KOG2582; Eukaryota.
DR GeneTree; ENSGT00940000153653; -.
DR HOGENOM; CLU_028825_0_1_1; -.
DR InParanoid; Q9UNS2; -.
DR OMA; NHYHDLV; -.
DR OrthoDB; 929822at2759; -.
DR PhylomeDB; Q9UNS2; -.
DR TreeFam; TF101146; -.
DR PathwayCommons; Q9UNS2; -.
DR Reactome; R-HSA-5696394; DNA Damage Recognition in GG-NER.
DR Reactome; R-HSA-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-HSA-8951664; Neddylation.
DR SignaLink; Q9UNS2; -.
DR SIGNOR; Q9UNS2; -.
DR BioGRID-ORCS; 8533; 502 hits in 1091 CRISPR screens.
DR ChiTaRS; COPS3; human.
DR GeneWiki; COP9_signalosome_complex_subunit_3; -.
DR GenomeRNAi; 8533; -.
DR Pharos; Q9UNS2; Tbio.
DR PRO; PR:Q9UNS2; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9UNS2; protein.
DR Bgee; ENSG00000141030; Expressed in gastrocnemius and 207 other tissues.
DR ExpressionAtlas; Q9UNS2; baseline and differential.
DR Genevisible; Q9UNS2; HS.
DR GO; GO:0008180; C:COP9 signalosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0000338; P:protein deneddylation; IDA:UniProtKB.
DR GO; GO:0045116; P:protein neddylation; IC:ComplexPortal.
DR GO; GO:1902162; P:regulation of DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; IMP:UniProtKB.
DR GO; GO:2000434; P:regulation of protein neddylation; IC:ComplexPortal.
DR GO; GO:0009416; P:response to light stimulus; TAS:ProtInc.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR InterPro; IPR037753; CSN3.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR10758:SF1; PTHR10758:SF1; 1.
DR Pfam; PF01399; PCI; 1.
DR SMART; SM00088; PINT; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS50250; PCI; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; Nucleus; Phosphoprotein; Reference proteome;
KW Signalosome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:18850735, ECO:0000269|Ref.8,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..423
FT /note="COP9 signalosome complex subunit 3"
FT /id="PRO_0000120978"
FT DOMAIN 197..365
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 402..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:18850735, ECO:0000269|Ref.8,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88543"
FT MOD_RES 410
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 423
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18850735,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT VAR_SEQ 1..20
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="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
