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Q7L5N1 (CSN6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
COP9 signalosome complex subunit 6

Short name=SGN6
Short name=Signalosome subunit 6
Alternative name(s):
JAB1-containing signalosome subunit 6
MOV34 homolog
Vpr-interacting protein
Short name=hVIP
Gene names
Name:COPS6
Synonyms:CSN6, HVIP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length327 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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, 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. Has some glucocorticoid receptor-responsive activity. Stabilizes RFWD2/COP1 through reducing RFWD2 auto-ubiquitination and decelerating RFWD2 turnover rate, hence regulates the ubiquitination of RFWD2 targets. Ref.5 Ref.8 Ref.9 Ref.12 Ref.13 Ref.16

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, COPS4, COPS5 and COPS7 (COPS7A or COPS7B). Interacts with the translation initiation factor EIF3S6. Interacts weakly with RBX1. Interacts with the HIV-1 protein Vpr. Directly interacts with RFWD2 and 14-3-3 protein sigma/SFN. Ref.6 Ref.7 Ref.9 Ref.10 Ref.11 Ref.14 Ref.16

Subcellular location

Nucleus. Cytoplasm. Note: The interaction with HIV-1 Vpr protein possibly leads its translocation to a perinuclear region. Ref.5 Ref.7

Tissue specificity

Widely expressed. Ref.7

Sequence similarities

Belongs to the peptidase M67A family. CSN6 subfamily.

Contains 1 MPN (JAB/Mov34) domain.

Caution

Although related to the peptidase M67A family, it lacks the JAMM motif that probably constitutes the catalytic center and therefore it probably does not have a protease activity.

Sequence caution

The sequence AAD03469.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processHost-virus interaction
   Cellular componentCytoplasm
Nucleus
Signalosome
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcullin deneddylation

Inferred from direct assay PubMed 19141280. Source: UniProtKB

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentCOP9 signalosome

Inferred from direct assay Ref.14. Source: UniProtKB

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 17337451. Source: UniProtKB

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 327327COP9 signalosome complex subunit 6
PRO_0000194860

Regions

Domain39 – 148110MPN
Region211 – 327117Interaction with Vpr

Sequences

Sequence LengthMass (Da)Tools
Q7L5N1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: E33CAC6ADF799A8D

FASTA32736,163
        10         20         30         40         50         60 
MAAAAAAAAA TNGTGGSSGM EVDAAVVPSV MACGVTGSVS VALHPLVILN ISDHWIRMRS 

        70         80         90        100        110        120 
QEGRPVQVIG ALIGKQEGRN IEVMNSFELL SHTVEEKIII DKEYYYTKEE QFKQVFKELE 

       130        140        150        160        170        180 
FLGWYTTGGP PDPSDIHVHK QVCEIIESPL FLKLNPMTKH TDLPVSVFES VIDIINGEAT 

       190        200        210        220        230        240 
MLFAELTYTL ATEEAERIGV DHVARMTATG SGENSTVAEH LIAQHSAIKM LHSRVKLILE 

       250        260        270        280        290        300 
YVKASEAGEV PFNHEILREA YALCHCLPVL STDKFKTDFY DQCNDVGLMA YLGTITKTCN 

       310        320 
TMNQFVNKFN VLYDRQGIGR RMRGLFF 

« Hide

References

« Hide 'large scale' references
[1]"Human chromosome 7: DNA sequence and biology."
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S. expand/collapse author list , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Placenta.
[4]"Structure of cDNAs encoding human eukaryotic initiation factor 3 subunits. Possible roles in RNA binding and macromolecular assembly."
Asano K., Vornlocher H.-P., Richter-Cook N.J., Merrick W.C., Hinnebusch A.G., Hershey J.W.B.
J. Biol. Chem. 272:27042-27052(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 22-327.
[5]"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] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION.
[6]"Biochemical mechanism of HIV-I Vpr function. Specific interaction with a cellular protein."
Zhao L.-J., Mukherjee S., Narayan O.
J. Biol. Chem. 269:15577-15582(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HIV-1 VPR.
[7]"HIV-1 Vpr interacts with a human 34-kDa mov34 homologue, a cellular factor linked to the G2/M phase transition of the mammalian cell cycle."
Mahalingam S., Ayyavoo V., Patel M., Kieber-Emmons T., Kao G.D., Muschel R.J., Weiner D.B.
Proc. Natl. Acad. Sci. U.S.A. 95:3419-3424(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH HUMAN VPR.
[8]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[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] [Europe PMC] [Abstract]
Cited for: FUNCTION, COMPOSITION OF THE CSN COMPLEX, INTERACTION WITH RBX1.
[10]"Association of the mammalian proto-oncoprotein Int-6 with the three protein complexes eIF3, COP9 signalosome and 26S proteasome."
Hoareau Alves K., Bochard V., Rety S., Jalinot P.
FEBS Lett. 527:15-21(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EIF3S6.
[11]"Carboxyl terminus of hVIP/mov34 is critical for HIV-1-Vpr interaction and glucocorticoid-mediated signaling."
Ramanathan M.P., Curley E. III, Su M., Chambers J.A., Weiner D.B.
J. Biol. Chem. 277:47854-47860(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH VPR.
[12]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[14]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE CSN COMPLEX.
[15]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"COP9 signalosome subunit 6 stabilizes COP1, which functions as an E3 ubiquitin ligase for 14-3-3sigma."
Choi H.H., Gully C., Su C.H., Velazquez-Torres G., Chou P.C., Tseng C., Zhao R., Phan L., Shaiken T., Chen J., Yeung S.C., Lee M.H.
Oncogene 30:4791-4801(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RFWD2 AND SFN.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CH236956 Genomic DNA. Translation: EAL23857.1.
CH471091 Genomic DNA. Translation: EAW76601.1.
BC002520 mRNA. Translation: AAH02520.2.
U70735 mRNA. Translation: AAD03469.1. Different initiation.
CCDSCCDS5682.1.
RefSeqNP_006824.2. NM_006833.4.
UniGeneHs.15591.

3D structure databases

ProteinModelPortalQ7L5N1.
SMRQ7L5N1. Positions 38-323.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116176. 299 interactions.
DIPDIP-32655N.
IntActQ7L5N1. 131 interactions.
MINTMINT-5005311.
STRING9606.ENSP00000304102.

Protein family/group databases

MEROPSM67.972.

PTM databases

PhosphoSiteQ7L5N1.

Polymorphism databases

DMDM55976470.

Proteomic databases

MaxQBQ7L5N1.
PaxDbQ7L5N1.
PeptideAtlasQ7L5N1.
PRIDEQ7L5N1.

Protocols and materials databases

DNASU10980.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000303904; ENSP00000304102; ENSG00000168090.
GeneID10980.
KEGGhsa:10980.
UCSCuc003usu.3. human.

Organism-specific databases

CTD10980.
GeneCardsGC07P099686.
HGNCHGNC:21749. COPS6.
HPAHPA044315.
MIM614729. gene.
neXtProtNX_Q7L5N1.
PharmGKBPA134919933.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1310.
HOGENOMHOG000253002.
HOVERGENHBG107770.
InParanoidQ7L5N1.
KOK12179.
OMAIGKQKGR.
OrthoDBEOG7WT41Q.
PhylomeDBQ7L5N1.
TreeFamTF101148.

Gene expression databases

ArrayExpressQ7L5N1.
BgeeQ7L5N1.
CleanExHS_COPS6.
GenevestigatorQ7L5N1.

Family and domain databases

InterProIPR000555. JAMM/MPN+_dom.
IPR024969. Rpn11/EIF3F_C.
[Graphical view]
PfamPF01398. JAB. 1 hit.
PF13012. MitMem_reg. 1 hit.
[Graphical view]
SMARTSM00232. JAB_MPN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCOPS6. human.
GeneWikiCOPS6.
GenomeRNAi10980.
NextBio41718.
PROQ7L5N1.
SOURCESearch...

Entry information

Entry nameCSN6_HUMAN
AccessionPrimary (citable) accession number: Q7L5N1
Secondary accession number(s): A4D2A3, O15387
Entry history
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: July 5, 2004
Last modified: July 9, 2014
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MIM cross-references

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

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM