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Protein

COP9 signalosome complex subunit 7a

Gene

Cops7a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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, 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 (By similarity).By similarity

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-MMU-5696394. DNA Damage Recognition in GG-NER.
R-MMU-6781823. Formation of TC-NER Pre-Incision Complex.

Names & Taxonomyi

Protein namesi
Recommended name:
COP9 signalosome complex subunit 7a
Short name:
SGN7a
Short name:
Signalosome subunit 7a
Alternative name(s):
JAB1-containing signalosome subunit 7a
Gene namesi
Name:Cops7a
Synonyms:Csn7a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:1349400. Cops7a.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Signalosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 275274COP9 signalosome complex subunit 7aPRO_0000120997Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity

Post-translational modificationi

Phosphorylated by CK2 and PKD kinases.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9CZ04.
MaxQBiQ9CZ04.
PaxDbiQ9CZ04.
PeptideAtlasiQ9CZ04.
PRIDEiQ9CZ04.

PTM databases

iPTMnetiQ9CZ04.
PhosphoSiteiQ9CZ04.
SwissPalmiQ9CZ04.

Expressioni

Gene expression databases

BgeeiQ9CZ04.
ExpressionAtlasiQ9CZ04. baseline and differential.
GenevisibleiQ9CZ04. MM.

Interactioni

Subunit structurei

Component of the CSN complex, composed of COPS1/GPS1, COPS2, COPS3, COPS4, COPS5, COPS6, COPS7 (COPS7A or COPS7B) and COPS8. In the complex, it probably interacts directly with COPS1, COPS2, COPS4, COPS5, COPS6 and COPS8. Interacts with CK2 and PKD. Interacts with PMF1. Interacts with the translation initiation factor EIF3S6 (By similarity). Interacts directly with ID3.By similarity2 Publications

Protein-protein interaction databases

BioGridi205045. 3 interactions.
STRINGi10090.ENSMUSP00000108058.

Structurei

3D structure databases

ProteinModelPortaliQ9CZ04.
SMRiQ9CZ04. Positions 8-215.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini52 – 156105PCIAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili185 – 23349Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the CSN7/EIF3M family. CSN7 subfamily.Curated
Contains 1 PCI domain.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG3250. Eukaryota.
ENOG410XP7W. LUCA.
GeneTreeiENSGT00390000013069.
HOGENOMiHOG000006003.
HOVERGENiHBG051138.
InParanoidiQ9CZ04.
KOiK12180.
OMAiSEFSPVF.
OrthoDBiEOG7N63NJ.
PhylomeDBiQ9CZ04.
TreeFamiTF101149.

Family and domain databases

InterProiIPR000717. PCI_dom.
[Graphical view]
PfamiPF01399. PCI. 1 hit.
[Graphical view]
SMARTiSM00088. PINT. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9CZ04-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MSAEVKVTGQ NQEQFLLLAK SAKGAALATL IHQVLEAPGV YVFGELLDMP
60 70 80 90 100
NVRELAESDF ASTFRLLTVF AYGTYADYLA EARNLPPLTD AQKNKLRHLS
110 120 130 140 150
VVTLAAKVKC IPYAVLLEAL ALRNVRQLED LVIEAVYADV LRGSLDQRNQ
160 170 180 190 200
RLEVDYSIGR DIQRQDLSAI AQTLQEWCVG CEVVLSGIEE QVSRANQHKE
210 220 230 240 250
QQLGLKQQIE SEVANLKKTI KVTTAAAAAA TSQDPEQHLT ELREPASGTN
260 270
QRQPSKKASK GKGLRGSAKI WSKSN
Length:275
Mass (Da):30,224
Last modified:November 23, 2004 - v2
Checksum:iB104C9FA318FDE24
GO
Isoform 2 (identifier: Q9CZ04-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     264-275: LRGSAKIWSKSN → EKINPQSTVKPSAK

Note: No experimental confirmation available.
Show »
Length:277
Mass (Da):30,405
Checksum:i5ACADFD2B0CB2E4A
GO

Sequence cautioni

The sequence AAK43736.1 differs from that shown. Reason: Frameshift at position 35. Curated
The sequence BAB27144.1 differs from that shown. Reason: Frameshift at position 1. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti153 – 1531E → K in BAB28682 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei264 – 27512LRGSA…WSKSN → EKINPQSTVKPSAK in isoform 2. 1 PublicationVSP_011912Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF071316 mRNA. Translation: AAC33903.1.
AK010726 mRNA. Translation: BAB27144.1. Frameshift.
AK013155 mRNA. Translation: BAB28682.1.
AK019122 mRNA. Translation: BAB31554.1.
BC003724 mRNA. Translation: AAH03724.1.
AF240179 mRNA. Translation: AAK43736.1. Frameshift.
CCDSiCCDS20539.1. [Q9CZ04-1]
CCDS51909.1. [Q9CZ04-2]
RefSeqiNP_001157561.1. NM_001164089.1. [Q9CZ04-2]
NP_036133.1. NM_012003.2. [Q9CZ04-1]
XP_006506222.1. XM_006506159.2. [Q9CZ04-2]
XP_006506223.1. XM_006506160.2. [Q9CZ04-2]
XP_006506224.1. XM_006506161.2. [Q9CZ04-2]
XP_006506225.1. XM_006506162.2. [Q9CZ04-1]
XP_011239667.1. XM_011241365.1. [Q9CZ04-1]
UniGeneiMm.244536.

Genome annotation databases

EnsembliENSMUST00000032220; ENSMUSP00000032220; ENSMUSG00000030127. [Q9CZ04-1]
ENSMUST00000112439; ENSMUSP00000108058; ENSMUSG00000030127. [Q9CZ04-2]
GeneIDi26894.
KEGGimmu:26894.
UCSCiuc009dsr.2. mouse. [Q9CZ04-2]
uc009dss.2. mouse. [Q9CZ04-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF071316 mRNA. Translation: AAC33903.1.
AK010726 mRNA. Translation: BAB27144.1. Frameshift.
AK013155 mRNA. Translation: BAB28682.1.
AK019122 mRNA. Translation: BAB31554.1.
BC003724 mRNA. Translation: AAH03724.1.
AF240179 mRNA. Translation: AAK43736.1. Frameshift.
CCDSiCCDS20539.1. [Q9CZ04-1]
CCDS51909.1. [Q9CZ04-2]
RefSeqiNP_001157561.1. NM_001164089.1. [Q9CZ04-2]
NP_036133.1. NM_012003.2. [Q9CZ04-1]
XP_006506222.1. XM_006506159.2. [Q9CZ04-2]
XP_006506223.1. XM_006506160.2. [Q9CZ04-2]
XP_006506224.1. XM_006506161.2. [Q9CZ04-2]
XP_006506225.1. XM_006506162.2. [Q9CZ04-1]
XP_011239667.1. XM_011241365.1. [Q9CZ04-1]
UniGeneiMm.244536.

3D structure databases

ProteinModelPortaliQ9CZ04.
SMRiQ9CZ04. Positions 8-215.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi205045. 3 interactions.
STRINGi10090.ENSMUSP00000108058.

PTM databases

iPTMnetiQ9CZ04.
PhosphoSiteiQ9CZ04.
SwissPalmiQ9CZ04.

Proteomic databases

EPDiQ9CZ04.
MaxQBiQ9CZ04.
PaxDbiQ9CZ04.
PeptideAtlasiQ9CZ04.
PRIDEiQ9CZ04.

Protocols and materials databases

DNASUi26894.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000032220; ENSMUSP00000032220; ENSMUSG00000030127. [Q9CZ04-1]
ENSMUST00000112439; ENSMUSP00000108058; ENSMUSG00000030127. [Q9CZ04-2]
GeneIDi26894.
KEGGimmu:26894.
UCSCiuc009dsr.2. mouse. [Q9CZ04-2]
uc009dss.2. mouse. [Q9CZ04-1]

Organism-specific databases

CTDi50813.
MGIiMGI:1349400. Cops7a.

Phylogenomic databases

eggNOGiKOG3250. Eukaryota.
ENOG410XP7W. LUCA.
GeneTreeiENSGT00390000013069.
HOGENOMiHOG000006003.
HOVERGENiHBG051138.
InParanoidiQ9CZ04.
KOiK12180.
OMAiSEFSPVF.
OrthoDBiEOG7N63NJ.
PhylomeDBiQ9CZ04.
TreeFamiTF101149.

Enzyme and pathway databases

ReactomeiR-MMU-5696394. DNA Damage Recognition in GG-NER.
R-MMU-6781823. Formation of TC-NER Pre-Incision Complex.

Miscellaneous databases

PROiQ9CZ04.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CZ04.
ExpressionAtlasiQ9CZ04. baseline and differential.
GenevisibleiQ9CZ04. MM.

Family and domain databases

InterProiIPR000717. PCI_dom.
[Graphical view]
PfamiPF01399. PCI. 1 hit.
[Graphical view]
SMARTiSM00088. PINT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The COP9 complex is conserved between plants and mammals and is related to the 26S proteasome regulatory complex."
    Wei N., Tsuge T., Serino G., Dohmae N., Takio K., Matsui M., Deng X.-W.
    Curr. Biol. 8:919-922(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION IN THE CSN COMPLEX.
    Strain: C57BLKS/J.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Embryo.
  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] (ISOFORM 1).
    Strain: FVB/N.
    Tissue: Mammary tumor.
  4. "Mechanism of exogenous nucleic acids and their precursors improving the repair of intestinal epithelium after gamma-irradiation in mice."
    Cui D.X., Zeng G.Y., Wang F., Xu J.R., Ren D.Q., Guo Y.H., Tian F.R., Yan X.J., Hou Y., Su C.Z.
    World J. Gastroenterol. 6:709-717(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 9-67.
  5. "Ubiquitin-dependent degradation of Id1 and Id3 is mediated by the COP9 signalosome."
    Berse M., Bounpheng M., Huang X., Christy B., Pollmann C., Dubiel W.
    J. Mol. Biol. 343:361-370(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ID3.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiCSN7A_MOUSE
AccessioniPrimary (citable) accession number: Q9CZ04
Secondary accession number(s): O88546
, Q925R8, Q9CPQ4, Q9CWD2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: November 23, 2004
Last modified: July 6, 2016
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.