CSN1_HUMAN
ID CSN1_HUMAN Reviewed; 491 AA.
AC Q13098; Q8NA10; Q9BWL1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 4.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=COP9 signalosome complex subunit 1;
DE Short=SGN1;
DE Short=Signalosome subunit 1;
DE AltName: Full=G protein pathway suppressor 1;
DE Short=GPS-1;
DE AltName: Full=JAB1-containing signalosome subunit 1;
DE AltName: Full=Protein MFH;
GN Name=GPS1; Synonyms=COPS1, CSN1;
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 4), AND TISSUE SPECIFICITY.
RX PubMed=8943324; DOI=10.1128/mcb.16.12.6698;
RA Spain B.H., Bowdish K.S., Pacal A., Flueckiger Staub S., Koo D.,
RA Chang K.-Y.R., Xie W., Colicelli J.;
RT "Two human cDNAs, including a homolog of Arabidopsis FUS6 (COP11), suppress
RT G-protein- and mitogen-activated protein kinase-mediated signal
RT transduction in yeast and mammalian cells.";
RL Mol. Cell. Biol. 16:6698-6706(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Testis;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Placenta, and Prostate;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 17-491 (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PARTIAL PROTEIN SEQUENCE, FUNCTION, AND SUBCELLULAR LOCATION.
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 [7]
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 [8]
RP DOMAIN, AND INTERACTION WITH COPS2; COPS3 AND COPS4.
RX PubMed=11114242; DOI=10.1006/jmbi.2000.4288;
RA Tsuge T., Matsui M., Wei N.;
RT "The subunit 1 of the COP9 signalosome suppresses gene expression through
RT its N-terminal domain and incorporates into the complex through the PCI
RT domain.";
RL J. Mol. Biol. 305:1-9(2001).
RN [9]
RP FUNCTION, AND COMPOSITION OF THE CSN COMPLEX.
RX PubMed=11337588; DOI=10.1126/science.1059780;
RA Lyapina S., Cope G., Shevchenko A., Serino G., Tsuge T., Zhou C.,
RA Wolf D.A., Wei N., Shevchenko A., Deshaies R.J.;
RT "Promotion of NEDD-CUL1 conjugate cleavage by COP9 signalosome.";
RL Science 292:1382-1385(2001).
RN [10]
RP INTERACTION WITH ITPK1.
RX PubMed=12324474; DOI=10.1074/jbc.m208709200;
RA Sun Y., Wilson M.P., Majerus P.W.;
RT "Inositol 1,3,4-trisphosphate 5/6-kinase associates with the COP9
RT signalosome by binding to CSN1.";
RL J. Biol. Chem. 277:45759-45764(2002).
RN [11]
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 [12]
RP FUNCTION.
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-479, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-479, AND IDENTIFICATION BY
RP 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 [15]
RP IDENTIFICATION IN THE CSN COMPLEX, CLEAVAGE OF INITIATOR METHIONINE, AND
RP PHOSPHORYLATION AT SER-468; SER-474; THR-479 AND SER-483.
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-474; THR-479 AND SER-483, 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 [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-479, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-474 AND THR-479, AND
RP IDENTIFICATION BY 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 [20]
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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-468; SER-474 AND THR-479, AND
RP IDENTIFICATION BY 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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-468; SER-474; THR-479 AND
RP SER-483, AND IDENTIFICATION BY 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 [23]
RP COMPOSITION OF THE CSN COMPLEX.
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).
CC -!- FUNCTION: Essential component of the COP9 signalosome complex (CSN), a
CC complex involved in various cellular and developmental processes. The
CC 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 Ubl
CC ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The
CC complex is also 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 Suppresses G-protein- and mitogen-activated protein kinase-mediated
CC signal transduction. {ECO:0000269|PubMed:11285227,
CC ECO:0000269|PubMed:11337588, ECO:0000269|PubMed:12628923,
CC ECO:0000269|PubMed:12732143, 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:11337588, PubMed:18850735, PubMed:26456823). In the
CC complex, it probably interacts directly with COPS2, COPS3, COPS4 and
CC COPS5 (PubMed:11114242). Interacts directly with inositol kinase ITPK1
CC (PubMed:12324474). Interacts with CAPN8 (By similarity).
CC {ECO:0000250|UniProtKB:Q99LD4, ECO:0000269|PubMed:11114242,
CC ECO:0000269|PubMed:11337588, ECO:0000269|PubMed:12324474,
CC ECO:0000269|PubMed:18850735, ECO:0000269|PubMed:26456823}.
CC -!- INTERACTION:
CC Q13098; Q92905: COPS5; NbExp=16; IntAct=EBI-725197, EBI-594661;
CC Q13098-7; Q9NZN8: CNOT2; NbExp=3; IntAct=EBI-10983983, EBI-743033;
CC Q13098-7; P61201: COPS2; NbExp=5; IntAct=EBI-10983983, EBI-1050386;
CC Q13098-7; Q99627: COPS8; NbExp=4; IntAct=EBI-10983983, EBI-2510102;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9535219}. Nucleus
CC {ECO:0000269|PubMed:9535219}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q13098-4; Sequence=Displayed;
CC Name=4;
CC IsoId=Q13098-5; Sequence=VSP_036242;
CC Name=3;
CC IsoId=Q13098-6; Sequence=VSP_036241, VSP_011882;
CC Name=2;
CC IsoId=Q13098-7; Sequence=VSP_036240, VSP_036242;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:8943324}.
CC -!- DOMAIN: The PCI domain is necessary and sufficient for the interactions
CC with other CSN subunits of the complex. Mediates the interaction with
CC CAPN8 (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The N-terminal part (1-216), which is not required for
CC deneddylating activity and CSN complex formation, is nevertheless
CC essential for other aspects of CSN complex function, such as repression
CC of c-fos/FOS expression. {ECO:0000269|PubMed:11114242}.
CC -!- SIMILARITY: Belongs to the CSN1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC50906.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U20285; AAC50906.2; ALT_INIT; mRNA.
DR EMBL; AK093283; BAC04120.1; -; mRNA.
DR EMBL; AC135056; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000155; AAH00155.3; -; mRNA.
DR EMBL; BC064503; AAH64503.1; -; mRNA.
DR EMBL; BT009834; AAP88836.1; -; mRNA.
DR CCDS; CCDS11800.1; -. [Q13098-7]
DR CCDS; CCDS32774.1; -. [Q13098-4]
DR CCDS; CCDS82226.1; -. [Q13098-5]
DR PIR; G01646; G01646.
DR RefSeq; NP_001308021.1; NM_001321092.1. [Q13098-5]
DR RefSeq; NP_004118.3; NM_004127.5. [Q13098-4]
DR RefSeq; NP_997657.1; NM_212492.2. [Q13098-7]
DR RefSeq; XP_016880023.1; XM_017024534.1.
DR PDB; 4D10; X-ray; 3.80 A; A/I=12-491.
DR PDB; 4D18; X-ray; 4.08 A; A/I=12-491.
DR PDB; 4WSN; X-ray; 5.50 A; A/I/Q/Y/g/o=12-491.
DR PDB; 6R6H; EM; 8.40 A; A=1-491.
DR PDB; 6R7F; EM; 8.20 A; A=37-469.
DR PDB; 6R7H; EM; 8.80 A; A=37-469.
DR PDB; 6R7I; EM; 5.90 A; A=37-491.
DR PDB; 6R7N; EM; 6.50 A; A=1-491.
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; Q13098; -.
DR SMR; Q13098; -.
DR BioGRID; 109131; 145.
DR ComplexPortal; CPX-1870; COP9 signalosome variant 1.
DR ComplexPortal; CPX-1871; COP9 signalosome variant 2.
DR CORUM; Q13098; -.
DR DIP; DIP-42077N; -.
DR IntAct; Q13098; 59.
DR MINT; Q13098; -.
DR STRING; 9606.ENSP00000376167; -.
DR GlyGen; Q13098; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q13098; -.
DR MetOSite; Q13098; -.
DR PhosphoSitePlus; Q13098; -.
DR SwissPalm; Q13098; -.
DR BioMuta; GPS1; -.
DR DMDM; 223590263; -.
DR EPD; Q13098; -.
DR jPOST; Q13098; -.
DR MassIVE; Q13098; -.
DR MaxQB; Q13098; -.
DR PaxDb; Q13098; -.
DR PeptideAtlas; Q13098; -.
DR PRIDE; Q13098; -.
DR ProteomicsDB; 59147; -. [Q13098-4]
DR ProteomicsDB; 59148; -. [Q13098-5]
DR ProteomicsDB; 59149; -. [Q13098-6]
DR ProteomicsDB; 59150; -. [Q13098-7]
DR TopDownProteomics; Q13098-5; -. [Q13098-5]
DR Antibodypedia; 19873; 367 antibodies from 36 providers.
DR DNASU; 2873; -.
DR Ensembl; ENST00000306823.10; ENSP00000302873.6; ENSG00000169727.13. [Q13098-4]
DR Ensembl; ENST00000392358.6; ENSP00000376167.2; ENSG00000169727.13. [Q13098-7]
DR Ensembl; ENST00000578552.6; ENSP00000462265.1; ENSG00000169727.13. [Q13098-5]
DR GeneID; 2873; -.
DR KEGG; hsa:2873; -.
DR MANE-Select; ENST00000578552.6; ENSP00000462265.1; NM_001321092.3; NP_001308021.1. [Q13098-5]
DR UCSC; uc002kdk.2; human. [Q13098-4]
DR CTD; 2873; -.
DR DisGeNET; 2873; -.
DR GeneCards; GPS1; -.
DR HGNC; HGNC:4549; GPS1.
DR HPA; ENSG00000169727; Low tissue specificity.
DR MIM; 601934; gene.
DR neXtProt; NX_Q13098; -.
DR OpenTargets; ENSG00000169727; -.
DR PharmGKB; PA28944; -.
DR VEuPathDB; HostDB:ENSG00000169727; -.
DR eggNOG; KOG0686; Eukaryota.
DR GeneTree; ENSGT00510000046608; -.
DR InParanoid; Q13098; -.
DR OMA; QNWAHVM; -.
DR OrthoDB; 859626at2759; -.
DR PhylomeDB; Q13098; -.
DR TreeFam; TF101167; -.
DR PathwayCommons; Q13098; -.
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 Reactome; R-HSA-9013422; RHOBTB1 GTPase cycle.
DR SignaLink; Q13098; -.
DR BioGRID-ORCS; 2873; 715 hits in 1092 CRISPR screens.
DR ChiTaRS; GPS1; human.
DR GeneWiki; GPS1; -.
DR GenomeRNAi; 2873; -.
DR Pharos; Q13098; Tbio.
DR PRO; PR:Q13098; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q13098; protein.
DR Bgee; ENSG00000169727; Expressed in apex of heart and 188 other tissues.
DR ExpressionAtlas; Q13098; baseline and differential.
DR Genevisible; Q13098; 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:0005095; F:GTPase inhibitor activity; TAS:ProtInc.
DR GO; GO:0007254; P:JNK cascade; TAS:ProtInc.
DR GO; GO:0000338; P:protein deneddylation; IDA:UniProtKB.
DR GO; GO:0045116; P:protein neddylation; IC:ComplexPortal.
DR GO; GO:2000434; P:regulation of protein neddylation; IC:ComplexPortal.
DR InterPro; IPR033008; CSN1.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR019585; Rpn7/CSN1.
DR InterPro; IPR045135; Rpn7_N.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR14145; PTHR14145; 1.
DR PANTHER; PTHR14145:SF2; PTHR14145:SF2; 1.
DR Pfam; PF01399; PCI; 1.
DR Pfam; PF10602; RPN7; 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; Alternative splicing; Cytoplasm; Direct protein sequencing;
KW Nucleus; Phosphoprotein; Reference proteome; Signalosome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:18850735"
FT CHAIN 2..491
FT /note="COP9 signalosome complex subunit 1"
FT /id="PRO_0000120959"
FT DOMAIN 269..431
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 465..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 468
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18850735,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 474
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18850735,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 479
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18850735,
FT ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 483
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18850735,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..11
FT /note="MPLPVQVFNLQ -> MRDSSAPSSASSSVTDLYCTPHSSRSDLVLPGTAGDF
FT SLSASLSACTLLYE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_036240"
FT VAR_SEQ 12..109
FT /note="GAVEPMQIDVDPQEDPQNAPDVNYVVENPSLDLEQYAASYSGLMRIERLQFI
FT ADHCPTLRVEALKMALSFVQRTFNVDMYEEIHRKLSEATRSSLREL -> PASSVSGSG
FT GAESQDRMRDSSAPSSASSSVTDLYCTPHSSRSDLVLPGMAGDFSLSASLSACTLLYEG
FT AVEPMQIDVDPQEDP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036241"
FT VAR_SEQ 103..106
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8943324"
FT /id="VSP_036242"
FT VAR_SEQ 471..491
FT /note="REGSQGELTPANSQSRMSTNM -> TSTDLGPPGGSVLPAAQLRGLATGCHP
FT ACVPSLGLRRQAAASCGPSWKERPAGLDPVGFCPQGADCAAPRPSGTISQTPPVPASVR
FT CRQVGGVH (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_011882"
FT CONFLICT 259
FT /note="A -> T (in Ref. 2; BAC04120)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 491 AA; 55537 MW; BF925164ED985638 CRC64;
MPLPVQVFNL QGAVEPMQID VDPQEDPQNA PDVNYVVENP SLDLEQYAAS YSGLMRIERL
QFIADHCPTL RVEALKMALS FVQRTFNVDM YEEIHRKLSE ATRSSLRELQ NAPDAIPESG
VEPPALDTAW VEATRKKALL KLEKLDTDLK NYKGNSIKES IRRGHDDLGD HYLDCGDLSN
ALKCYSRARD YCTSAKHVIN MCLNVIKVSV YLQNWSHVLS YVSKAESTPE IAEQRGERDS
QTQAILTKLK CAAGLAELAA RKYKQAAKCL LLASFDHCDF PELLSPSNVA IYGGLCALAT
FDRQELQRNV ISSSSFKLFL ELEPQVRDII FKFYESKYAS CLKMLDEMKD NLLLDMYLAP
HVRTLYTQIR NRALIQYFSP YVSADMHRMA AAFNTTVAAL EDELTQLILE GLISARVDSH
SKILYARDVD QRSTTFEKSL LMGKEFQRRA KAMMLRAAVL RNQIHVKSPP REGSQGELTP
ANSQSRMSTN M
