Full text data of GPS1
GPS1
(COPS1, CSN1)
[Confidence: high (present in two of the MS resources)]
COP9 signalosome complex subunit 1; SGN1; Signalosome subunit 1 (G protein pathway suppressor 1; GPS-1; JAB1-containing signalosome subunit 1; Protein MFH)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
COP9 signalosome complex subunit 1; SGN1; Signalosome subunit 1 (G protein pathway suppressor 1; GPS-1; JAB1-containing signalosome subunit 1; Protein MFH)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00156282
IPI00156282 G protein pathway suppressor 1 isoform 2 COP9 signalosome complex subunit 1, The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
IPI00156282 G protein pathway suppressor 1 isoform 2 COP9 signalosome complex subunit 1, The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
UniProt
Q13098
ID CSN1_HUMAN Reviewed; 491 AA.
AC Q13098; Q8NA10; Q9BWL1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 10-FEB-2009, sequence version 4.
DT 22-JAN-2014, entry version 132.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND TISSUE SPECIFICITY.
RX PubMed=8943324;
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),
RT suppress G-protein- and mitogen-activated protein kinase-mediated
RT signal 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.,
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 [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.,
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 [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
RT project: 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
RT vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PARTIAL PROTEIN SEQUENCE, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9535219;
RA Seeger M., Kraft R., Ferrell K., Bech-Otschir D., Dumdey R.,
RA Schade R., Gordon C., Naumann M., Dubiel W.;
RT "A novel protein complex involved in signal transduction possessing
RT similarities to 26S proteasome subunits.";
RL FASEB J. 12:469-478(1998).
RN [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.,
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 [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
RT through its N-terminal domain and incorporates into the complex
RT through the PCI 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.,
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 [12]
RP FUNCTION.
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-479, AND MASS
RP SPECTROMETRY.
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
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-479, AND MASS
RP SPECTROMETRY.
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 [15]
RP IDENTIFICATION IN THE CSN COMPLEX, CLEAVAGE OF INITIATOR METHIONINE,
RP AND 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
RP SER-483, AND 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 [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.,
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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-479, AND MASS
RP SPECTROMETRY.
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 MASS 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 [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.,
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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-468; SER-474 AND
RP THR-479, AND MASS 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).
CC -!- FUNCTION: Essential component of the COP9 signalosome complex
CC (CSN), a complex involved in various cellular and developmental
CC processes. The CSN complex is an essential regulator of the
CC ubiquitin (Ubl) conjugation pathway by mediating the deneddylation
CC of the cullin subunits of SCF-type E3 ligase complexes, leading to
CC decrease the Ubl ligase activity of SCF-type complexes such as
CC SCF, CSA or DDB2. The complex is also involved in phosphorylation
CC of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8/ICSBP,
CC possibly via its association with CK2 and PKD kinases. CSN-
CC dependent phosphorylation of TP53 and JUN promotes and protects
CC degradation by the Ubl system, respectively. Suppresses G-protein-
CC and mitogen-activated protein kinase-mediated signal transduction.
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 COPS2,
CC COPS3, COPS4 and CSN5. Interacts directly with inositol kinase
CC ITPK1. Interacts with CAPN8 (By similarity).
CC -!- INTERACTION:
CC Q92905:COPS5; NbExp=3; IntAct=EBI-725197, EBI-594661;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
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 Note=No experimental confirmation available;
CC Name=2;
CC IsoId=Q13098-7; Sequence=VSP_036240, VSP_036242;
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- DOMAIN: The PCI domain is necessary and sufficient for the
CC interactions with other CSN subunits of the complex. Mediates the
CC interaction with CAPN8 (By similarity).
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
CC repression of c-fos/FOS expression.
CC -!- SIMILARITY: Belongs to the CSN1 family.
CC -!- SIMILARITY: Contains 1 PCI domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC50906.2; Type=Erroneous initiation;
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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 PIR; G01646; G01646.
DR RefSeq; NP_004118.3; NM_004127.4.
DR RefSeq; NP_997657.1; NM_212492.1.
DR RefSeq; XP_005256420.1; XM_005256363.1.
DR UniGene; Hs.268530; -.
DR ProteinModelPortal; Q13098; -.
DR SMR; Q13098; 167-418.
DR DIP; DIP-42077N; -.
DR IntAct; Q13098; 12.
DR MINT; MINT-1203964; -.
DR STRING; 9606.ENSP00000347251; -.
DR PhosphoSite; Q13098; -.
DR DMDM; 223590263; -.
DR PaxDb; Q13098; -.
DR PRIDE; Q13098; -.
DR DNASU; 2873; -.
DR Ensembl; ENST00000306823; ENSP00000302873; ENSG00000169727.
DR Ensembl; ENST00000355130; ENSP00000347251; ENSG00000169727.
DR Ensembl; ENST00000392358; ENSP00000376167; ENSG00000169727.
DR Ensembl; ENST00000578552; ENSP00000462265; ENSG00000169727.
DR GeneID; 2873; -.
DR KEGG; hsa:2873; -.
DR UCSC; uc002kdl.1; human.
DR CTD; 2873; -.
DR GeneCards; GC17P080009; -.
DR HGNC; HGNC:4549; GPS1.
DR MIM; 601934; gene.
DR neXtProt; NX_Q13098; -.
DR PharmGKB; PA28944; -.
DR eggNOG; COG5187; -.
DR HOGENOM; HOG000091977; -.
DR HOVERGEN; HBG030722; -.
DR KO; K12175; -.
DR OMA; CPPLRVE; -.
DR ChiTaRS; GPS1; human.
DR GeneWiki; GPS1; -.
DR GenomeRNAi; 2873; -.
DR NextBio; 11339; -.
DR PRO; PR:Q13098; -.
DR ArrayExpress; Q13098; -.
DR Bgee; Q13098; -.
DR CleanEx; HS_GPS1; -.
DR Genevestigator; Q13098; -.
DR GO; GO:0008180; C:COP9 signalosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005095; F:GTPase inhibitor activity; TAS:ProtInc.
DR GO; GO:0007049; P:cell cycle; TAS:ProtInc.
DR GO; GO:0010388; P:cullin deneddylation; IDA:UniProtKB.
DR GO; GO:0000188; P:inactivation of MAPK activity; TAS:ProtInc.
DR GO; GO:0007254; P:JNK cascade; TAS:ProtInc.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.25.40.10; -; 2.
DR InterPro; IPR019585; 26S_proteasome_reg_su-Rpn7.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR011990; TPR-like_helical.
DR InterPro; IPR011991; WHTH_DNA-bd_dom.
DR Pfam; PF01399; PCI; 1.
DR Pfam; PF10602; RPN7; 1.
DR SMART; SM00088; PINT; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Nucleus; Phosphoprotein;
KW Reference proteome; Signalosome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 491 COP9 signalosome complex subunit 1.
FT /FTId=PRO_0000120959.
FT DOMAIN 324 428 PCI.
FT MOD_RES 468 468 Phosphoserine.
FT MOD_RES 474 474 Phosphoserine.
FT MOD_RES 479 479 Phosphothreonine.
FT MOD_RES 483 483 Phosphoserine.
FT VAR_SEQ 1 11 MPLPVQVFNLQ -> MRDSSAPSSASSSVTDLYCTPHSSRS
FT DLVLPGTAGDFSLSASLSACTLLYE (in isoform 2).
FT /FTId=VSP_036240.
FT VAR_SEQ 12 109 GAVEPMQIDVDPQEDPQNAPDVNYVVENPSLDLEQYAASYS
FT GLMRIERLQFIADHCPTLRVEALKMALSFVQRTFNVDMYEE
FT IHRKLSEATRSSLREL -> PASSVSGSGGAESQDRMRDSS
FT APSSASSSVTDLYCTPHSSRSDLVLPGMAGDFSLSASLSAC
FT TLLYEGAVEPMQIDVDPQEDP (in isoform 3).
FT /FTId=VSP_036241.
FT VAR_SEQ 103 106 Missing (in isoform 2 and isoform 4).
FT /FTId=VSP_036242.
FT VAR_SEQ 471 491 REGSQGELTPANSQSRMSTNM -> TSTDLGPPGGSVLPAA
FT QLRGLATGCHPACVPSLGLRRQAAASCGPSWKERPAGLDPV
FT GFCPQGADCAAPRPSGTISQTPPVPASVRCRQVGGVH (in
FT isoform 3).
FT /FTId=VSP_011882.
FT CONFLICT 259 259 A -> T (in Ref. 2; BAC04120).
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
//
ID CSN1_HUMAN Reviewed; 491 AA.
AC Q13098; Q8NA10; Q9BWL1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 10-FEB-2009, sequence version 4.
DT 22-JAN-2014, entry version 132.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND TISSUE SPECIFICITY.
RX PubMed=8943324;
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),
RT suppress G-protein- and mitogen-activated protein kinase-mediated
RT signal 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.,
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 [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.,
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 [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
RT project: 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
RT vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PARTIAL PROTEIN SEQUENCE, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9535219;
RA Seeger M., Kraft R., Ferrell K., Bech-Otschir D., Dumdey R.,
RA Schade R., Gordon C., Naumann M., Dubiel W.;
RT "A novel protein complex involved in signal transduction possessing
RT similarities to 26S proteasome subunits.";
RL FASEB J. 12:469-478(1998).
RN [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.,
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 [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
RT through its N-terminal domain and incorporates into the complex
RT through the PCI 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.,
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 [12]
RP FUNCTION.
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-479, AND MASS
RP SPECTROMETRY.
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
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-479, AND MASS
RP SPECTROMETRY.
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 [15]
RP IDENTIFICATION IN THE CSN COMPLEX, CLEAVAGE OF INITIATOR METHIONINE,
RP AND 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
RP SER-483, AND 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 [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.,
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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-479, AND MASS
RP SPECTROMETRY.
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 MASS 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 [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.,
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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-468; SER-474 AND
RP THR-479, AND MASS 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).
CC -!- FUNCTION: Essential component of the COP9 signalosome complex
CC (CSN), a complex involved in various cellular and developmental
CC processes. The CSN complex is an essential regulator of the
CC ubiquitin (Ubl) conjugation pathway by mediating the deneddylation
CC of the cullin subunits of SCF-type E3 ligase complexes, leading to
CC decrease the Ubl ligase activity of SCF-type complexes such as
CC SCF, CSA or DDB2. The complex is also involved in phosphorylation
CC of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8/ICSBP,
CC possibly via its association with CK2 and PKD kinases. CSN-
CC dependent phosphorylation of TP53 and JUN promotes and protects
CC degradation by the Ubl system, respectively. Suppresses G-protein-
CC and mitogen-activated protein kinase-mediated signal transduction.
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 COPS2,
CC COPS3, COPS4 and CSN5. Interacts directly with inositol kinase
CC ITPK1. Interacts with CAPN8 (By similarity).
CC -!- INTERACTION:
CC Q92905:COPS5; NbExp=3; IntAct=EBI-725197, EBI-594661;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
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 Note=No experimental confirmation available;
CC Name=2;
CC IsoId=Q13098-7; Sequence=VSP_036240, VSP_036242;
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- DOMAIN: The PCI domain is necessary and sufficient for the
CC interactions with other CSN subunits of the complex. Mediates the
CC interaction with CAPN8 (By similarity).
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
CC repression of c-fos/FOS expression.
CC -!- SIMILARITY: Belongs to the CSN1 family.
CC -!- SIMILARITY: Contains 1 PCI domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC50906.2; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
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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 PIR; G01646; G01646.
DR RefSeq; NP_004118.3; NM_004127.4.
DR RefSeq; NP_997657.1; NM_212492.1.
DR RefSeq; XP_005256420.1; XM_005256363.1.
DR UniGene; Hs.268530; -.
DR ProteinModelPortal; Q13098; -.
DR SMR; Q13098; 167-418.
DR DIP; DIP-42077N; -.
DR IntAct; Q13098; 12.
DR MINT; MINT-1203964; -.
DR STRING; 9606.ENSP00000347251; -.
DR PhosphoSite; Q13098; -.
DR DMDM; 223590263; -.
DR PaxDb; Q13098; -.
DR PRIDE; Q13098; -.
DR DNASU; 2873; -.
DR Ensembl; ENST00000306823; ENSP00000302873; ENSG00000169727.
DR Ensembl; ENST00000355130; ENSP00000347251; ENSG00000169727.
DR Ensembl; ENST00000392358; ENSP00000376167; ENSG00000169727.
DR Ensembl; ENST00000578552; ENSP00000462265; ENSG00000169727.
DR GeneID; 2873; -.
DR KEGG; hsa:2873; -.
DR UCSC; uc002kdl.1; human.
DR CTD; 2873; -.
DR GeneCards; GC17P080009; -.
DR HGNC; HGNC:4549; GPS1.
DR MIM; 601934; gene.
DR neXtProt; NX_Q13098; -.
DR PharmGKB; PA28944; -.
DR eggNOG; COG5187; -.
DR HOGENOM; HOG000091977; -.
DR HOVERGEN; HBG030722; -.
DR KO; K12175; -.
DR OMA; CPPLRVE; -.
DR ChiTaRS; GPS1; human.
DR GeneWiki; GPS1; -.
DR GenomeRNAi; 2873; -.
DR NextBio; 11339; -.
DR PRO; PR:Q13098; -.
DR ArrayExpress; Q13098; -.
DR Bgee; Q13098; -.
DR CleanEx; HS_GPS1; -.
DR Genevestigator; Q13098; -.
DR GO; GO:0008180; C:COP9 signalosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005095; F:GTPase inhibitor activity; TAS:ProtInc.
DR GO; GO:0007049; P:cell cycle; TAS:ProtInc.
DR GO; GO:0010388; P:cullin deneddylation; IDA:UniProtKB.
DR GO; GO:0000188; P:inactivation of MAPK activity; TAS:ProtInc.
DR GO; GO:0007254; P:JNK cascade; TAS:ProtInc.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.25.40.10; -; 2.
DR InterPro; IPR019585; 26S_proteasome_reg_su-Rpn7.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR011990; TPR-like_helical.
DR InterPro; IPR011991; WHTH_DNA-bd_dom.
DR Pfam; PF01399; PCI; 1.
DR Pfam; PF10602; RPN7; 1.
DR SMART; SM00088; PINT; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Nucleus; Phosphoprotein;
KW Reference proteome; Signalosome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 491 COP9 signalosome complex subunit 1.
FT /FTId=PRO_0000120959.
FT DOMAIN 324 428 PCI.
FT MOD_RES 468 468 Phosphoserine.
FT MOD_RES 474 474 Phosphoserine.
FT MOD_RES 479 479 Phosphothreonine.
FT MOD_RES 483 483 Phosphoserine.
FT VAR_SEQ 1 11 MPLPVQVFNLQ -> MRDSSAPSSASSSVTDLYCTPHSSRS
FT DLVLPGTAGDFSLSASLSACTLLYE (in isoform 2).
FT /FTId=VSP_036240.
FT VAR_SEQ 12 109 GAVEPMQIDVDPQEDPQNAPDVNYVVENPSLDLEQYAASYS
FT GLMRIERLQFIADHCPTLRVEALKMALSFVQRTFNVDMYEE
FT IHRKLSEATRSSLREL -> PASSVSGSGGAESQDRMRDSS
FT APSSASSSVTDLYCTPHSSRSDLVLPGMAGDFSLSASLSAC
FT TLLYEGAVEPMQIDVDPQEDP (in isoform 3).
FT /FTId=VSP_036241.
FT VAR_SEQ 103 106 Missing (in isoform 2 and isoform 4).
FT /FTId=VSP_036242.
FT VAR_SEQ 471 491 REGSQGELTPANSQSRMSTNM -> TSTDLGPPGGSVLPAA
FT QLRGLATGCHPACVPSLGLRRQAAASCGPSWKERPAGLDPV
FT GFCPQGADCAAPRPSGTISQTPPVPASVRCRQVGGVH (in
FT isoform 3).
FT /FTId=VSP_011882.
FT CONFLICT 259 259 A -> T (in Ref. 2; BAC04120).
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
//
MIM
601934
*RECORD*
*FIELD* NO
601934
*FIELD* TI
*601934 G PROTEIN PATHWAY SUPPRESSOR 1; GPS1
;;FUS6/COP11, ARABIDOPSIS, HOMOLOG OF
read more*FIELD* TX
CLONING
Spain et al. (1996) used a yeast complementation system to identify
human proteins involved in G protein-MAP kinase signaling cascades. They
cloned the genes of 2 such proteins, termed GPS1 and GPS2 (601935).
Sequence analysis revealed that the GPS1 gene encodes a 500-amino acid
polypeptide that has striking similarity to the protein encoded by the
Arabidopsis FUS6/COP11 gene. The FUS6/COP11 gene product is a negative
regulator of light-mediated signal transduction that is known to be
essential for normal development in plants. Spain et al. (1996) also
isolated a second GPS1 clone, termed GPS1-1, which encodes a polypeptide
that is 13 amino acids shorter than GPS1, apparently transcribed from an
alternative initiation site. When overexpressed in mammalian cells,
full-length GPS1 potently suppressed a RAS- and mitogen-activated
protein kinase-mediated signal and interfered with JNK activity,
suggesting that its function may be signal repression. Spain et al.
(1996) stated that these results are consistent with the proposed
function of FUS6/COP11 as a signal transduction repressor.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the GPS1
gene to chromosome 17 (TMAP RH98836).
*FIELD* RF
1. Spain, B. H.; Bowdish, K. S.; Pacal, A. R.; Staub, S. F.; Koo,
D.; Chang, C.-Y. R.; Xie, W.; Colicelli, J.: Two human cDNAs, including
a homolog of Arabidopsis FUS6(COP11), suppress G-protein- and mitogen-activated
protein kinase-mediated signal transduction in yeast and mammalian
cells. Molec. Cell. Biol. 16: 6698-6706, 1996.
*FIELD* CD
Jennifer P. Macke: 7/23/1997
*FIELD* ED
carol: 02/09/2007
carol: 1/23/2001
jenny: 10/1/1997
jenny: 9/2/1997
jenny: 8/13/1997
*RECORD*
*FIELD* NO
601934
*FIELD* TI
*601934 G PROTEIN PATHWAY SUPPRESSOR 1; GPS1
;;FUS6/COP11, ARABIDOPSIS, HOMOLOG OF
read more*FIELD* TX
CLONING
Spain et al. (1996) used a yeast complementation system to identify
human proteins involved in G protein-MAP kinase signaling cascades. They
cloned the genes of 2 such proteins, termed GPS1 and GPS2 (601935).
Sequence analysis revealed that the GPS1 gene encodes a 500-amino acid
polypeptide that has striking similarity to the protein encoded by the
Arabidopsis FUS6/COP11 gene. The FUS6/COP11 gene product is a negative
regulator of light-mediated signal transduction that is known to be
essential for normal development in plants. Spain et al. (1996) also
isolated a second GPS1 clone, termed GPS1-1, which encodes a polypeptide
that is 13 amino acids shorter than GPS1, apparently transcribed from an
alternative initiation site. When overexpressed in mammalian cells,
full-length GPS1 potently suppressed a RAS- and mitogen-activated
protein kinase-mediated signal and interfered with JNK activity,
suggesting that its function may be signal repression. Spain et al.
(1996) stated that these results are consistent with the proposed
function of FUS6/COP11 as a signal transduction repressor.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the GPS1
gene to chromosome 17 (TMAP RH98836).
*FIELD* RF
1. Spain, B. H.; Bowdish, K. S.; Pacal, A. R.; Staub, S. F.; Koo,
D.; Chang, C.-Y. R.; Xie, W.; Colicelli, J.: Two human cDNAs, including
a homolog of Arabidopsis FUS6(COP11), suppress G-protein- and mitogen-activated
protein kinase-mediated signal transduction in yeast and mammalian
cells. Molec. Cell. Biol. 16: 6698-6706, 1996.
*FIELD* CD
Jennifer P. Macke: 7/23/1997
*FIELD* ED
carol: 02/09/2007
carol: 1/23/2001
jenny: 10/1/1997
jenny: 9/2/1997
jenny: 8/13/1997