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Protein FULL name: COP9 signalosome complex subunit 1, JAB1-containing signalosome subunit 1, G protein pathway suppressor 1, Protein MFH.,
Protein SHORT name: Signalosome subunit 1 SGN1 GPS1
GPS1 (Homo sapiens) is product of expression of
GPS1
gene.
GPS1 is involved in:
DDS in Homo sapiens
Keywords:
FUNCTION: Essential component of the COP9 signalosome complex
(CSN), a complex involved in various cellular and developmental
processes. The CSN complex is an essential regulator of the
ubiquitin (Ubl) conjugation pathway by mediating the deneddylation
of the cullin subunits of SCF-type E3 ligase complexes, leading to
decrease the Ubl ligase activity of SCF-type complexes such as
SCF, CSA or DDB2. The complex is also involved in phosphorylation
of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8/ICSBP,
possibly via its association with CK2 and PKD kinases. CSN-
dependent phosphorylation of TP53 and JUN promotes and protects
degradation by the Ubl system, respectively. Suppresses G-protein-
and mitogen-activated protein kinase-mediated signal transduction.
SUBUNIT: Component of the CSN complex, composed of COPS1/GPS1,
COPS2, COPS3, COPS4, COPS5, COP6, COPS7 (COPS7A or COPS7B) and
COPS8. In the complex, it probably interacts directly with COPS2,
COPS3, COPS4 and CSN5. Interacts directly with inositol kinase
ITPK1. Interacts with CAPN8 (By similarity).
INTERACTION:
Q9P2S5:WDR8; NbExp=1; IntAct=EBI-725197, EBI-1054904;
SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
TISSUE SPECIFICITY: Widely expressed.
DOMAIN: The PCI domain is necessary and sufficient for the
interactions with other CSN subunits of the complex. Mediates the
interaction with CAPN8 (By similarity).
DOMAIN: The N-terminal part (1-216), which is not required for
deneddylating activity and CSN complex formation, is nevertheless
essential for other aspects of CSN complex function, such as
repression of c-fos/FOS expression.
PTM: Phosphorylated upon DNA damage, probably by ATM or ATR.
SIMILARITY: Belongs to the CSN1 family.
SIMILARITY: Contains 1 PCI domain.
SEQUENCE CAUTION:
Sequence=AAC50906.2; Type=Erroneous initiation;
Links to other databases:
Database
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ID
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Link
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Uniprot
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Q13098
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Q13098
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PFAM:
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PF01399
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PF01399
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InterPro:
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IPR000717
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IPR000717
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CATH:
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None
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SCOP:
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None
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PDB:
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-
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-
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Protein sequence:
MQIDVDPQEDPQNAPDVNYVVENPSLDLEQYAASYSGLMRIERLQFIADH
CPTLRVEALKMALSFVQRTFNVDMYEEIHRKLSEATRELQNAPDAIPESG
VEPPALDTAWVEATRKKALLKLEKLDTDLKNYKGNSIKESIRRGHDDLGD
HYLDCGDLSNALKCYSRARDYCTSAKHVINMCLNVIKVSVYLQNWSHVLS
YVSKAESTPEIAEQRGERDSQTQAILTKLKCAAGLAELAARKYKQAAKCL
LLASFDHCDFPELLSPSNVAIYGGLCALATFDRQELQRNVISSSSFKLFL
ELEPQVRDIIFKFYESKYASCLKMLDEMKDNLLLDMYLAPHVRTLYTQIR
NRALIQYFSPYVSADMHRMAAAFNTTVAALEDELTQLILEGLISARVDSH
SKILYARDVDQRSTTFEKSLLMGKEFQRRAKAMMLRAAVLRNQIHVKSPP
REGSQGELTPANSQSRMSTNM
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GPS1 (Homo sapiens) belongs to following protein families:
References:
Title
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Authors
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Journal
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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.
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Spain BH, Bowdish KS, Pacal AR, Staub SF, Koo D, Chang CY, Xie W, Colicelli J
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Mol Cell Biol
Dec. 1, 1996
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A novel protein complex involved in signal transduction possessing similarities to 26S proteasome subunits.
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Seeger M, Kraft R, Ferrell K, Bech-Otschir D, Dumdey R, Schade R, Gordon C, Naumann M, Dubiel W
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FASEB J
April 1, 1998
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The subunit 1 of the COP9 signalosome suppresses gene expression through its N-terminal domain and incorporates into the complex through the PCI domain.
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Tsuge T, Matsui M, Wei N
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J Mol Biol
Feb. 5, 2001
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COP9 signalosome-specific phosphorylation targets p53 to degradation by the ubiquitin system.
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Bech-Otschir D, Kraft R, Huang X, Henklein P, Kapelari B, Pollmann C, Dubiel W
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EMBO J
April 2, 2001
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Promotion of NEDD-CUL1 conjugate cleavage by COP9 signalosome.
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Lyapina S, Cope G, Shevchenko A, Serino G, Tsuge T, Zhou C, Wolf DA, Wei N, Shevchenko A, Deshaies RJ
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Science
May 18, 2001
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Inositol 1,3,4-trisphosphate 5/6-kinase associates with the COP9 signalosome by binding to CSN1.
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Sun Y, Wilson MP, Majerus PW
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J Biol Chem
Nov. 1, 2002
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Protein kinase CK2 and protein kinase D are associated with the COP9 signalosome.
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Uhle S, Medalia O, Waldron R, Dumdey R, Henklein P, Bech-Otschir D, Huang X, Berse M, Sperling J, Schade R, Dubiel W
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EMBO J
March 17, 2003
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The ubiquitin ligase activity in the DDB2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage.
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Groisman R, Polanowska J, Kuraoka I, Sawada J, Saijo M, Drapkin R, Kisselev AF, Tanaka K, Nakatani Y
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Cell
May 2, 2003
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Complete sequencing and characterization of 21,243 full-length human cDNAs.
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Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S
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Nat Genet
Feb. 1, 2004
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The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
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Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J
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Genome Res
Oct. 1, 2004
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DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage.
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Zody MC, Garber M, Adams DJ, Sharpe T, Harrow J, Lupski JR, Nicholson C, Searle SM, Wilming L, Young SK, Abouelleil A, Allen NR, Bi W, Bloom T, Borowsky ML, Bugalter BE, Butler J, Chang JL, Chen CK, Cook A, Corum B, Cuomo CA, de Jong PJ, DeCaprio D, Dewar K, FitzGerald M, Gilbert J, Gibson R, Gnerre S, Goldstein S, Grafham DV, Grocock R, Hafez N, Hagopian DS, Hart E, Norman CH, Humphray S, Jaffe DB, Jones M, Kamal M, Khodiyar VK, LaButti K, Laird G, Lehoczky J, Liu X, Lokyitsang T, Loveland J, Lui A, Macdonald P, Major JE, Matthews L, Mauceli E, McCarroll SA, Mihalev AH, Mudge J, Nguyen C, Nicol R, O'Leary SB, Osoegawa K, Schwartz DC, Shaw-Smith C, Stankiewicz P, Steward C, Swarbreck D, Venkataraman V, Whittaker CA, Yang X, Zimmer AR, Bradley A, Hubbard T, Birren BW, Rogers J, Lander ES, Nusbaum C
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Nature
April 20, 2006
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A probability-based approach for high-throughput protein phosphorylation analysis and site localization.
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Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP
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Nat Biotechnol
Oct. 1, 2006
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Tyrosine phosphorylated Par3 regulates epithelial tight junction assembly promoted by EGFR signaling.
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Wang Y, Du D, Fang L, Yang G, Zhang C, Zeng R, Ullrich A, Lottspeich F, Chen Z
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EMBO J
Nov. 1, 2006
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Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry.
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Molina H, Horn DM, Tang N, Mathivanan S, Pandey A
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Proc Natl Acad Sci U S A
Jan. 13, 2007
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ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.
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Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ
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Science
May 25, 2007
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A quantitative atlas of mitotic phosphorylation.
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Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP
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Proc Natl Acad Sci U S A
Aug. 5, 2008
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Characterization of the human COP9 signalosome complex using affinity purification and mass spectrometry.
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Fang L, Wang X, Yamoah K, Chen PL, Pan ZQ, Huang L
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J Proteome Res
Nov. 1, 2008
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Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.
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Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK
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Sci Signal
Jan. 1, 2009
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Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.
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Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S
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Anal Chem
June 1, 2009
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Lysine acetylation targets protein complexes and co-regulates major cellular functions.
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Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M
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Science
Aug. 14, 2009
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Last modification of this entry: Oct. 12, 2010.
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