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Q7L5N1

- CSN6_HUMAN

UniProt

Q7L5N1 - CSN6_HUMAN

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Protein

COP9 signalosome complex subunit 6

Gene
COPS6, CSN6, HVIP
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.6 Publications

GO - Molecular functioni

  1. protein binding Source: UniProtKB

GO - Biological processi

  1. cullin deneddylation Source: UniProtKB
  2. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction

Protein family/group databases

MEROPSiM67.972.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:COPS6
Synonyms:CSN6, HVIP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:21749. COPS6.

Subcellular locationi

Nucleus. Cytoplasm
Note: The interaction with HIV-1 Vpr protein possibly leads its translocation to a perinuclear region.2 Publications

GO - Cellular componenti

  1. COP9 signalosome Source: UniProtKB
  2. cytoplasm Source: UniProtKB-SubCell
  3. extracellular vesicular exosome Source: UniProt
  4. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Signalosome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134919933.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 327327COP9 signalosome complex subunit 6PRO_0000194860Add
BLAST

Proteomic databases

MaxQBiQ7L5N1.
PaxDbiQ7L5N1.
PeptideAtlasiQ7L5N1.
PRIDEiQ7L5N1.

PTM databases

PhosphoSiteiQ7L5N1.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

ArrayExpressiQ7L5N1.
BgeeiQ7L5N1.
CleanExiHS_COPS6.
GenevestigatoriQ7L5N1.

Organism-specific databases

HPAiHPA044315.

Interactioni

Subunit structurei

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.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BTBD2Q9BX702EBI-486838,EBI-710091
RFWD2Q8NHY23EBI-486838,EBI-1176214
SFNP319477EBI-486838,EBI-476295

Protein-protein interaction databases

BioGridi116176. 300 interactions.
DIPiDIP-32655N.
IntActiQ7L5N1. 131 interactions.
MINTiMINT-5005311.
STRINGi9606.ENSP00000304102.

Structurei

3D structure databases

ProteinModelPortaliQ7L5N1.
SMRiQ7L5N1. Positions 38-323.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini39 – 148110MPNAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni211 – 327117Interaction with VprAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1310.
HOGENOMiHOG000253002.
HOVERGENiHBG107770.
InParanoidiQ7L5N1.
KOiK12179.
OMAiIGKQKGR.
OrthoDBiEOG7WT41Q.
PhylomeDBiQ7L5N1.
TreeFamiTF101148.

Family and domain databases

InterProiIPR000555. JAMM/MPN+_dom.
IPR024969. Rpn11/EIF3F_C.
[Graphical view]
PfamiPF01398. JAB. 1 hit.
PF13012. MitMem_reg. 1 hit.
[Graphical view]
SMARTiSM00232. JAB_MPN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q7L5N1-1 [UniParc]FASTAAdd to Basket

« Hide

MAAAAAAAAA TNGTGGSSGM EVDAAVVPSV MACGVTGSVS VALHPLVILN    50
ISDHWIRMRS QEGRPVQVIG ALIGKQEGRN IEVMNSFELL SHTVEEKIII 100
DKEYYYTKEE QFKQVFKELE FLGWYTTGGP PDPSDIHVHK QVCEIIESPL 150
FLKLNPMTKH TDLPVSVFES VIDIINGEAT MLFAELTYTL ATEEAERIGV 200
DHVARMTATG SGENSTVAEH LIAQHSAIKM LHSRVKLILE YVKASEAGEV 250
PFNHEILREA YALCHCLPVL STDKFKTDFY DQCNDVGLMA YLGTITKTCN 300
TMNQFVNKFN VLYDRQGIGR RMRGLFF 327
Length:327
Mass (Da):36,163
Last modified:July 5, 2004 - v1
Checksum:iE33CAC6ADF799A8D
GO

Sequence cautioni

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CH236956 Genomic DNA. Translation: EAL23857.1.
CH471091 Genomic DNA. Translation: EAW76601.1.
BC002520 mRNA. Translation: AAH02520.2.
U70735 mRNA. Translation: AAD03469.1. Different initiation.
CCDSiCCDS5682.1.
RefSeqiNP_006824.2. NM_006833.4.
UniGeneiHs.15591.

Genome annotation databases

EnsembliENST00000303904; ENSP00000304102; ENSG00000168090.
GeneIDi10980.
KEGGihsa:10980.
UCSCiuc003usu.3. human.

Polymorphism databases

DMDMi55976470.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CH236956 Genomic DNA. Translation: EAL23857.1 .
CH471091 Genomic DNA. Translation: EAW76601.1 .
BC002520 mRNA. Translation: AAH02520.2 .
U70735 mRNA. Translation: AAD03469.1 . Different initiation.
CCDSi CCDS5682.1.
RefSeqi NP_006824.2. NM_006833.4.
UniGenei Hs.15591.

3D structure databases

ProteinModelPortali Q7L5N1.
SMRi Q7L5N1. Positions 38-323.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116176. 300 interactions.
DIPi DIP-32655N.
IntActi Q7L5N1. 131 interactions.
MINTi MINT-5005311.
STRINGi 9606.ENSP00000304102.

Protein family/group databases

MEROPSi M67.972.

PTM databases

PhosphoSitei Q7L5N1.

Polymorphism databases

DMDMi 55976470.

Proteomic databases

MaxQBi Q7L5N1.
PaxDbi Q7L5N1.
PeptideAtlasi Q7L5N1.
PRIDEi Q7L5N1.

Protocols and materials databases

DNASUi 10980.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000303904 ; ENSP00000304102 ; ENSG00000168090 .
GeneIDi 10980.
KEGGi hsa:10980.
UCSCi uc003usu.3. human.

Organism-specific databases

CTDi 10980.
GeneCardsi GC07P099686.
HGNCi HGNC:21749. COPS6.
HPAi HPA044315.
MIMi 614729. gene.
neXtProti NX_Q7L5N1.
PharmGKBi PA134919933.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1310.
HOGENOMi HOG000253002.
HOVERGENi HBG107770.
InParanoidi Q7L5N1.
KOi K12179.
OMAi IGKQKGR.
OrthoDBi EOG7WT41Q.
PhylomeDBi Q7L5N1.
TreeFami TF101148.

Miscellaneous databases

ChiTaRSi COPS6. human.
GeneWikii COPS6.
GenomeRNAii 10980.
NextBioi 41718.
PROi Q7L5N1.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q7L5N1.
Bgeei Q7L5N1.
CleanExi HS_COPS6.
Genevestigatori Q7L5N1.

Family and domain databases

InterProi IPR000555. JAMM/MPN+_dom.
IPR024969. Rpn11/EIF3F_C.
[Graphical view ]
Pfami PF01398. JAB. 1 hit.
PF13012. MitMem_reg. 1 hit.
[Graphical view ]
SMARTi SM00232. JAB_MPN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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. 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.

Entry informationi

Entry nameiCSN6_HUMAN
AccessioniPrimary (citable) accession number: Q7L5N1
Secondary accession number(s): A4D2A3, O15387
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: July 5, 2004
Last modified: September 3, 2014
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

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.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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