Q9UBW8 (CSN7A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	275 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 component	Cytoplasm Nucleus Signalosome
Domain	Coiled coil
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cullin deneddylation Inferred from direct assay PubMed 19141280. Source: UniProtKB
Cellular_component	cytoplasm Inferred from direct assay. Source: HPA signalosome Inferred from direct assay Ref.14. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.14
	Chain	2 – 275	274	COP9 signalosome complex subunit 7a		PRO_0000120996
Regions
	Domain	52 – 156	105	PCI
	Coiled coil	185 – 233	49	Potential
Amino acid modifications
	Modified residue	2	1	N-acetylserine Ref.14
Experimental info
	Sequence conflict	218	1	K → E in BAA91620. Ref.5
	Sequence conflict	253	1	Q → H in AAF04307. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q9UBW8 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 20888B35BFFF6326	FASTA	275	30,277
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
IPI	IPI00301419.
RefSeq	NP_001157565.1. NM_001164093.1. NP_001157566.1. NM_001164094.1. NP_001157567.1. NM_001164095.1. NP_057403.1. NM_016319.2.
UniGene	Hs.530823.
3D structure databases
ProteinModelPortal	Q9UBW8.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-53412N.
IntAct	Q9UBW8. 6 interactions.
MINT	MINT-1393951.
STRING	9606.ENSP00000229251.
PTM databases
PhosphoSite	Q9UBW8.
Polymorphism databases
DMDM	55976618.
Proteomic databases
PaxDb	Q9UBW8.
PeptideAtlas	Q9UBW8.
PRIDE	Q9UBW8.
Protocols and materials databases
DNASU	50813.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000229251; ENSP00000229251; ENSG00000111652. ENST00000442593; ENSP00000414459; ENSG00000111652. ENST00000534877; ENSP00000438363; ENSG00000111652. ENST00000534947; ENSP00000446039; ENSG00000111652. ENST00000539735; ENSP00000441852; ENSG00000111652. ENST00000543155; ENSP00000438115; ENSG00000111652.
GeneID	50813.
KEGG	hsa:50813.
UCSC	uc001qqh.3. human.
Organism-specific databases
CTD	50813.
GeneCards	GC12P006833.
HGNC	HGNC:16758. COPS7A.
HPA	HPA026915.
neXtProt	NX_Q9UBW8.
PharmGKB	PA26758.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG289374.
HOGENOM	HOG000006003.
HOVERGEN	HBG051138.
InParanoid	Q9UBW8.
KO	K12180.
OMA	HNVRQLE.
OrthoDB	EOG42Z4R2.
PhylomeDB	Q9UBW8.
Gene expression databases
ArrayExpress	Q9UBW8.
Bgee	Q9UBW8.
CleanEx	HS_COPS7A.
Genevestigator	Q9UBW8.
GermOnline	ENSG00000111652. Homo sapiens.
Family and domain databases
InterPro	IPR000717. PCI_dom. [Graphical view]
Pfam	PF01399. PCI. 1 hit. [Graphical view]
SMART	SM00088. PINT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	COPS7A. human.
GenomeRNAi	50813.
NextBio	53257.

Entry information

Entry name

CSN7A_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.