Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9UBW8 (CSN7A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
COP9 signalosome complex subunit 7a

Short name=SGN7a
Short name=Signalosome subunit 7a
Alternative name(s):
Dermal papilla-derived protein 10
JAB1-containing signalosome subunit 7a
Gene names
Name:COPS7A
Synonyms:CSN7A, DERP10
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length275 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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, JUN, I-kappa-B-alpha/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. Ref.8 Ref.9 Ref.10 Ref.12 Ref.13

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 COPS1, COPS2, COPS4, COPS5, COPS6 and COPS8. Interacts with PMF1. Interacts with the translation initiation factor EIF3S6. Interacts with CK2 and PKD. Interacts directly with ID3. Ref.1 Ref.11 Ref.13 Ref.14

Subcellular location

Cytoplasm. Nucleus Ref.8.

Tissue specificity

Widely expressed. Expressed at high level in brain, heart and skeletal muscle. Ref.1

Post-translational modification

Phosphorylated by CK2 and PKD kinases. Ref.13

Sequence similarities

Belongs to the CSN7/EIF3M family. CSN7 subfamily.

Contains 1 PCI domain.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
Signalosome
   DomainCoiled coil
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcullin deneddylation

Inferred from direct assay PubMed 19141280. Source: UniProtKB

   Cellular_componentCOP9 signalosome

Inferred from direct assay Ref.14. Source: UniProtKB

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.14
Chain2 – 275274COP9 signalosome complex subunit 7a
PRO_0000120996

Regions

Domain52 – 156105PCI
Coiled coil185 – 23349 Potential

Amino acid modifications

Modified residue21N-acetylserine Ref.14

Experimental info

Sequence conflict2181K → E in BAA91620. Ref.5
Sequence conflict2531Q → H in AAF04307. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q9UBW8 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 20888B35BFFF6326

FASTA27530,277
        10         20         30         40         50         60 
MSAEVKVTGQ NQEQFLLLAK SAKGAALATL IHQVLEAPGV YVFGELLDMP NVRELAESDF 

        70         80         90        100        110        120 
ASTFRLLTVF AYGTYADYLA EARNLPPLTE AQKNKLRHLS VVTLAAKVKC IPYAVLLEAL 

       130        140        150        160        170        180 
ALRNVRQLED LVIEAVYADV LRGSLDQRNQ RLEVDYSIGR DIQRQDLSAI ARTLQEWCVG 

       190        200        210        220        230        240 
CEVVLSGIEE QVSRANQHKE QQLGLKQQIE SEVANLKKTI KVTTAAAAAA TSQDPEQHLT 

       250        260        270 
ELREPAPGTN QRQPSKKASK GKGLRGSAKI WSKSN 

« Hide

References

« Hide 'large scale' references
[1]"Polyamine-modulated factor 1 binds to the human homologue of the 7a subunit of the Arabidopsis COP9 signalosome: implications in gene expression."
Wang Y., Devereux W., Stewart T.M., Casero R.A. Jr.
Biochem. J. 366:79-86(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INTERACTION WITH PMF1.
Tissue: Placenta.
[2]"Molecular cloning of a dermal papilla derived gene."
Ikeda A., Ukai Y., Yamashita M., Yoshimoto M.
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Hair follicle dermal papilla.
[3]"Cop9 complex subunit 7a."
Okaze H., Hayashi A., Kozuma S., Saito T.
Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"Molecular cloning and characterization of a novel cDNA encoding human COP9 complex subunit 7a (COPS7a)."
Lau S.K., Au T.C.C., Kok L.D.S., Lee C.Y., Tsui S.K.W., Waye M.M.Y., Fung K.P.
Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[5]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Embryo, Mammary gland and Thymus.
[6]Mural R.J., Istrail S., Sutton 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].
[7]"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: Skin.
[8]"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.
[9]"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.
[10]"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.
[11]"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.
[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, PHOSPHORYLATION, INTERACTION WITH CK2 AND PKD.
[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, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2.
[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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF210052 mRNA. Translation: AAF19205.1.
AB014764 mRNA. Translation: BAB87805.1.
AB033603 mRNA. Translation: BAA85390.1.
AF193844 mRNA. Translation: AAF04307.1.
AK001318 mRNA. Translation: BAA91620.1.
AK021721 mRNA. Translation: BAG51042.1.
AK022488 mRNA. Translation: BAB14052.1.
AK292621 mRNA. Translation: BAF85310.1.
CH471116 Genomic DNA. Translation: EAW88745.1.
CH471116 Genomic DNA. Translation: EAW88747.1.
CH471116 Genomic DNA. Translation: EAW88748.1.
BC011789 mRNA. Translation: AAH11789.1.
RefSeqNP_001157565.1. NM_001164093.1.
NP_001157566.1. NM_001164094.1.
NP_001157567.1. NM_001164095.1.
NP_057403.1. NM_016319.2.
XP_005253751.1. XM_005253694.1.
XP_005253752.1. XM_005253695.1.
UniGeneHs.530823.

3D structure databases

ProteinModelPortalQ9UBW8.
SMRQ9UBW8. Positions 13-163.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119130. 54 interactions.
DIPDIP-53412N.
IntActQ9UBW8. 7 interactions.
MINTMINT-1393951.
STRING9606.ENSP00000229251.

PTM databases

PhosphoSiteQ9UBW8.

Polymorphism databases

DMDM55976618.

Proteomic databases

PaxDbQ9UBW8.
PeptideAtlasQ9UBW8.
PRIDEQ9UBW8.

Protocols and materials databases

DNASU50813.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000229251; ENSP00000229251; ENSG00000111652.
ENST00000534877; ENSP00000438363; ENSG00000111652.
ENST00000534947; ENSP00000446039; ENSG00000111652.
ENST00000539735; ENSP00000441852; ENSG00000111652.
ENST00000543155; ENSP00000438115; ENSG00000111652.
GeneID50813.
KEGGhsa:50813.
UCSCuc001qqh.3. human.

Organism-specific databases

CTD50813.
GeneCardsGC12P006833.
HGNCHGNC:16758. COPS7A.
HPAHPA026915.
neXtProtNX_Q9UBW8.
PharmGKBPA26758.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG289374.
HOGENOMHOG000006003.
HOVERGENHBG051138.
InParanoidQ9UBW8.
KOK12180.
OMAINALAPF.
OrthoDBEOG7N63NJ.
PhylomeDBQ9UBW8.
TreeFamTF101149.

Gene expression databases

ArrayExpressQ9UBW8.
BgeeQ9UBW8.
CleanExHS_COPS7A.
GenevestigatorQ9UBW8.

Family and domain databases

InterProIPR027530. Csn7.
IPR000717. PCI_dom.
[Graphical view]
PANTHERPTHR15350:SF5. PTHR15350:SF5. 1 hit.
PfamPF01399. PCI. 1 hit.
[Graphical view]
SMARTSM00088. PINT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCOPS7A. human.
GeneWikiCOPS7A.
GenomeRNAi50813.
NextBio53257.
PROQ9UBW8.

Entry information

Entry nameCSN7A_HUMAN
AccessionPrimary (citable) accession number: Q9UBW8
Secondary accession number(s): A8K9A6, Q9NVX3, Q9UJW4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 103 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

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM