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 27-MAR-2024, entry version 211. 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}; 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; 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 PDB; 8H38; EM; 4.25 A; A=12-491. DR PDB; 8H3A; EM; 7.51 A; A=12-491. DR PDB; 8H3F; EM; 6.73 A; A=12-491. 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 PDBsum; 8H38; -. DR PDBsum; 8H3A; -. DR PDBsum; 8H3F; -. DR AlphaFoldDB; Q13098; -. DR EMDB; EMD-3313; -. DR EMDB; EMD-3314; -. DR EMDB; EMD-3315; -. DR EMDB; EMD-3316; -. DR EMDB; EMD-3317; -. DR EMDB; EMD-3401; -. DR EMDB; EMD-34455; -. DR EMDB; EMD-34462; -. DR EMDB; EMD-34467; -. DR EMDB; EMD-4736; -. DR EMDB; EMD-4739; -. DR EMDB; EMD-4741; -. DR EMDB; EMD-4742; -. DR EMDB; EMD-4744; -. DR SMR; Q13098; -. DR BioGRID; 109131; 221. 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; 63. 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; 9606-ENSP00000376167; -. DR PeptideAtlas; Q13098; -. DR ProteomicsDB; 59147; -. [Q13098-4] DR ProteomicsDB; 59148; -. [Q13098-5] DR ProteomicsDB; 59149; -. [Q13098-6] DR ProteomicsDB; 59150; -. [Q13098-7] DR Pumba; Q13098; -. DR TopDownProteomics; Q13098-5; -. [Q13098-5] DR Antibodypedia; 19873; 389 antibodies from 36 providers. DR DNASU; 2873; -. DR Ensembl; ENST00000306823.10; ENSP00000302873.6; ENSG00000169727.14. [Q13098-4] DR Ensembl; ENST00000392358.6; ENSP00000376167.2; ENSG00000169727.14. [Q13098-7] DR Ensembl; ENST00000578552.6; ENSP00000462265.1; ENSG00000169727.14. [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 AGR; HGNC:4549; -. 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; IYLQNWA; -. DR OrthoDB; 1601at2759; -. 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 SIGNOR; Q13098; -. DR BioGRID-ORCS; 2873; 741 hits in 1170 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 190 other cell types or tissues. DR ExpressionAtlas; Q13098; baseline and differential. 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; NAS:ComplexPortal. DR GO; GO:2000434; P:regulation of protein neddylation; NAS:ComplexPortal. DR Gene3D; 1.25.40.570; -; 1. DR InterPro; IPR048624; CSN1_C. 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; 26S PROTESOME SUBUNIT 6; 1. DR PANTHER; PTHR14145:SF2; COP9 SIGNALOSOME COMPLEX SUBUNIT 1; 1. DR Pfam; PF21151; CSN1_C; 1. DR Pfam; PF01399; PCI; 1. DR Pfam; PF10602; RPN7; 1. DR SMART; SM00088; PINT; 1. DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1. DR PROSITE; PS50250; PCI; 1. DR Genevisible; Q13098; HS. 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 //