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Reviewed, UniProtKB/Swiss-Prot Q13098 (CSN1_HUMAN)

Last modified July 7, 2009. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    COP9 signalosome complex subunit 1
      Short name=Signalosome subunit 1
      Short name=SGN1
Alternative name(s):
    JAB1-containing signalosome subunit 1
    G protein pathway suppressor 1
      Short name=Protein GPS1
    Protein MFH
Gene names
Name: GPS1
Synonyms: COPS1, CSN1
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length491 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

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. Ref.6 Ref.7 Ref.9 Ref.11 Ref.12

Subunit structure

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.

Subcellular location

Cytoplasm. Nucleus. Ref.6

Tissue specificity

Widely expressed. Ref.1

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.

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. Ref.8

Post-translational modification

Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18

Sequence similarities

Belongs to the CSN1 family.

Contains 1 PCI domain.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
Signalosome
   Coding sequence diversityAlternative splicing
   PTMPhosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processJNK cascade Ref.1

Traceable author statement. Source: ProtInc

cell cycle Ref.1

Traceable author statement. Source: ProtInc

inactivation of MAPK activity Ref.1

Traceable author statement. Source: ProtInc

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

signalosome

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionGTPase inhibitor activity Ref.1

Traceable author statement. Source: ProtInc

protein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

WDR8Q9P2S51EBI-725197,EBI-1054904

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q13098-4)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 4 (identifier: Q13098-5)

The sequence of this isoform differs from the canonical sequence as follows:
     103-106: Missing.
Isoform 3 (identifier: Q13098-6)

The sequence of this isoform differs from the canonical sequence as follows:
     12-109: GAVEPMQIDV...EATRSSLREL → PASSVSGSGG...QIDVDPQEDP
     471-491: REGSQGELTPANSQSRMSTNM → TSTDLGPPGG...VRCRQVGGVH
Note: No experimental confirmation available.
Isoform 2 (identifier: Q13098-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1-11: MPLPVQVFNLQ → MRDSSAPSSASSSVTDLYCTPHSSRSDLVLPGTAGDFSLSASLSACTLLYE
     103-106: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 491490COP9 signalosome complex subunit 1
PRO_0000120959

Regions

Domain324 – 428105PCI

Amino acid modifications

Modified residue3771Phosphotyrosine Ref.13
Modified residue4681Phosphoserine Ref.15 Ref.17
Modified residue4741Phosphoserine Ref.16 Ref.17 Ref.18
Modified residue4791Phosphothreonine Ref.14 Ref.16 Ref.17 Ref.18
Modified residue4831Phosphoserine Ref.16 Ref.17 Ref.18
Modified residue4881Phosphoserine Ref.15

Natural variations

Alternative sequence1 – 1111MPLPVQVFNLQ → MRDSSAPSSASSSVTDLYCT PHSSRSDLVLPGTAGDFSLS ASLSACTLLYE in isoform 2.
VSP_036240
Alternative sequence12 – 10998GAVEP…SLREL → PASSVSGSGGAESQDRMRDS SAPSSASSSVTDLYCTPHSS RSDLVLPGMAGDFSLSASLS ACTLLYEGAVEPMQIDVDPQ EDP in isoform 3.
VSP_036241
Alternative sequence103 – 1064Missing in isoform 2 and isoform 4.
VSP_036242
Alternative sequence471 – 49121REGSQ…MSTNM → TSTDLGPPGGSVLPAAQLRG LATGCHPACVPSLGLRRQAA ASCGPSWKERPAGLDPVGFC PQGADCAAPRPSGTISQTPP VPASVRCRQVGGVH in isoform 3.
VSP_011882

Experimental info

Sequence conflict2591A → T in BAC04120. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 10, 2009. Version 4.
Checksum: BF925164ED985638

FASTA49155,537
        10         20         30         40         50         60 
MPLPVQVFNL QGAVEPMQID VDPQEDPQNA PDVNYVVENP SLDLEQYAAS YSGLMRIERL 

        70         80         90        100        110        120 
QFIADHCPTL RVEALKMALS FVQRTFNVDM YEEIHRKLSE ATRSSLRELQ NAPDAIPESG 

       130        140        150        160        170        180 
VEPPALDTAW VEATRKKALL KLEKLDTDLK NYKGNSIKES IRRGHDDLGD HYLDCGDLSN 

       190        200        210        220        230        240 
ALKCYSRARD YCTSAKHVIN MCLNVIKVSV YLQNWSHVLS YVSKAESTPE IAEQRGERDS 

       250        260        270        280        290        300 
QTQAILTKLK CAAGLAELAA RKYKQAAKCL LLASFDHCDF PELLSPSNVA IYGGLCALAT 

       310        320        330        340        350        360 
FDRQELQRNV ISSSSFKLFL ELEPQVRDII FKFYESKYAS CLKMLDEMKD NLLLDMYLAP 

       370        380        390        400        410        420 
HVRTLYTQIR NRALIQYFSP YVSADMHRMA AAFNTTVAAL EDELTQLILE GLISARVDSH 

       430        440        450        460        470        480 
SKILYARDVD QRSTTFEKSL LMGKEFQRRA KAMMLRAAVL RNQIHVKSPP REGSQGELTP 

       490 
ANSQSRMSTN M 

« Hide

Isoform 4.

Checksum: 8E706F5C8E4763A5
Show »

FASTA48755,093
Isoform 3.

Checksum: B0C46F7860CB480E
Show »

FASTA54959,818
Isoform 2.

Checksum: 6081BEBD48CAF32C
Show »

FASTA52759,050

References

« Hide 'large scale' references
[1]"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."
Spain B.H., Bowdish K.S., Pacal A., Flueckiger Staub S., Koo D., Chang K.-Y.R., Xie W., Colicelli J.
Mol. Cell. Biol. 16:6698-6706(1996) [PubMed: 8943324] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), TISSUE SPECIFICITY.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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 T.-O., 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.
Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Testis.
[3]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed: 16625196] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Placenta and Prostate.
[5]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 17-491 (ISOFORM 1).
[6]"A novel protein complex involved in signal transduction possessing similarities to 26S proteasome subunits."
Seeger M., Kraft R., Ferrell K., Bech-Otschir D., Dumdey R., Schade R., Gordon C., Naumann M., Dubiel W.
FASEB J. 12:469-478(1998) [PubMed: 9535219] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION.
[7]"COP9 signalosome-specific phosphorylation targets p53 to degradation by the ubiquitin system."
Bech-Otschir D., Kraft R., Huang X., Henklein P., Kapelari B., Pollmann C., Dubiel W.
EMBO J. 20:1630-1639(2001) [PubMed: 11285227] [Abstract]
Cited for: FUNCTION.
[8]"The subunit 1 of the COP9 signalosome suppresses gene expression through its N-terminal domain and incorporates into the complex through the PCI domain."
Tsuge T., Matsui M., Wei N.
J. Mol. Biol. 305:1-9(2001) [PubMed: 11114242] [Abstract]
Cited for: DOMAIN, INTERACTION WITH COPS2; COPS3 AND COPS4.
[9]"Promotion of NEDD-CUL1 conjugate cleavage by COP9 signalosome."
Lyapina S., Cope G., Shevchenko A., Serino G., Tsuge T., Zhou C., Wolf D.A., Wei N., Shevchenko A., Deshaies R.J.
Science 292:1382-1385(2001) [PubMed: 11337588] [Abstract]
Cited for: FUNCTION, COMPOSITION OF THE CSN COMPLEX.
[10]"Inositol 1,3,4-trisphosphate 5/6-kinase associates with the COP9 signalosome by binding to CSN1."
Sun Y., Wilson M.P., Majerus P.W.
J. Biol. Chem. 277:45759-45764(2002) [PubMed: 12324474] [Abstract]
Cited for: INTERACTION WITH ITPK1.
[11]"The ubiquitin ligase activity in the DDB2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage."
Groisman R., Polanowska J., Kuraoka I., Sawada J., Saijo M., Drapkin R., Kisselev A.F., Tanaka K., Nakatani Y.
Cell 113:357-367(2003) [PubMed: 12732143] [Abstract]
Cited for: FUNCTION.
[12]"Protein kinase CK2 and protein kinase D are associated with the COP9 signalosome."
Uhle S., Medalia O., Waldron R., Dumdey R., Henklein P., Bech-Otschir D., Huang X., Berse M., Sperling J., Schade R., Dubiel W.
EMBO J. 22:1302-1312(2003) [PubMed: 12628923] [Abstract]
Cited for: FUNCTION.
[13]"Tyrosine phosphorylated Par3 regulates epithelial tight junction assembly promoted by EGFR signaling."
Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A., Lottspeich F., Chen Z.
EMBO J. 25:5058-5070(2006) [PubMed: 17053785] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-377, MASS SPECTROMETRY.
[14]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-479, MASS SPECTROMETRY.
Tissue: Epithelium.
[15]"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry."
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-468 AND SER-488, MASS SPECTROMETRY.
[16]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-474; THR-479 AND SER-483, MASS SPECTROMETRY.
[17]"Characterization of the human COP9 signalosome complex using affinity purification and mass spectrometry."
Fang L., Wang X., Yamoah K., Chen P.L., Pan Z.Q., Huang L.
J. Proteome Res. 7:4914-4925(2008) [PubMed: 18850735] [Abstract]
Cited for: INITIATOR METHIONINE REMOVAL, PHOSPHORYLATION AT SER-468; SER-474; THR-479 AND SER-483.
[18]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-474; THR-479 AND SER-483, MASS SPECTROMETRY.
[19]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.

Cross-references

Sequence databases

U20285 mRNA. Translation: AAC50906.2. Different initiation.
AK093283 mRNA. Translation: BAC04120.1.
AC135056 Genomic DNA. No translation available.
BC000155 mRNA. Translation: AAH00155.3.
BC064503 mRNA. Translation: AAH64503.1.
BT009834 mRNA. Translation: AAP88836.1.
IPIIPI00156282.
IPI00300386.
IPI00414289.
IPI00921488.
PIRG01646.
RefSeqNP_004118.3.
NP_997657.1.
UniGeneHs.268530

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActQ13098. 2 interactions.

PTM databases

PhosphoSiteQ13098.

Proteomic databases

PRIDEQ13098.

Genome annotation databases

EnsemblENSG00000169727. Homo sapiens. [Contig view]
GeneID2873.
KEGGhsa:2873.
UCSCuc002kdk.1. human.
uc002kdl.1. human.

Organism-specific databases

GeneCardsGC17P077603.
H-InvDBHIX0014267.
HGNCHGNC:4549. GPS1.
MIM601934. gene.
PharmGKBPA28661.
GenAtlasSearch...

Phylogenomic databases

HOVERGENQ13098.
OMAQ13098. IHRKLTE.

Gene expression databases

BgeeQ13098.
CleanExHS_GPS1.
GermOnlineENSG00000169727. Homo sapiens.

Family and domain databases

InterProIPR019585. 26S_proteasome_reg_su-Rpn7.
IPR000717. PCI.
[Graphical view]
PfamPF01399. PCI. 1 hit.
PF10602. RPN7. 1 hit.
[Graphical view]
SMARTSM00088. PINT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio11339.
SOURCESearch...

Entry information

Entry nameCSN1_HUMAN
AccessionPrimary (citable) accession number: Q13098
Secondary accession number(s): Q8NA10, Q9BWL1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 10, 2009
Last modified: July 7, 2009
This is version 87 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents