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P61202 (CSN2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 98. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
COP9 signalosome complex subunit 2

Short name=SGN2
Short name=Signalosome subunit 2
Alternative name(s):
Alien homolog
JAB1-containing signalosome subunit 2
Thyroid receptor-interacting protein 15
Short name=TR-interacting protein 15
Short name=TRIP-15
Gene names
Name:Cops2
Synonyms:Csn2, Trip15
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length443 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Essential 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/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. Involved in early stage of neuronal differentiation via its interaction with NIF3L1. Ref.5 Ref.6 Ref.7

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, COPS4, COPS5 COPS6 and COPS7 (COPS7A or COPS7B). Specifically interacts with the ligand binding domain of the thyroid receptor (TR). Does not require the presence of thyroid hormone for its interaction. Interacts with IRF8/ICSBP1 and with nuclear receptors NR2F1 and NR0B1 By similarity. Interacts with NIF3L1. Interacts with CUL1 and CUL2. Ref.4 Ref.5 Ref.6

Subcellular location

Cytoplasm. Nucleus Ref.1.

Tissue specificity

Widely expressed in embryonic, fetal and adult tissues, except cartilage and smooth muscle. Ref.1

Post-translational modification

Phosphorylated by CK2 and PKD kinases By similarity.

Disruption phenotype

Its absence causes arrest of embryo development at the peri-implantation stage. Blastocysts without Cops2 fail to outgrow in culture and exhibit a cell proliferation defect in inner cell mass, accompanied by a slight decrease in Oct4. In addition, lack of Cops2 disrupts the CSN complex and results in a drastic increase in cyclin E. It also induces elevated levels of p53 and p21, which may contribute to premature cell cycle arrest of the mutant. Ref.7

Sequence similarities

Belongs to the CSN2 family.

Contains 1 PCI domain.

Sequence caution

The sequence AAH23096.1 differs from that shown. Reason: Erroneous initiation.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P61202-1)

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.
Isoform 2 (identifier: P61202-2)

The sequence of this isoform differs from the canonical sequence as follows:
     124-124: Q → QNSDFLCQ

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 443443COP9 signalosome complex subunit 2
PRO_0000120969

Regions

Domain248 – 413166PCI

Natural variations

Alternative sequence1241Q → QNSDFLCQ in isoform 2.
VSP_011885

Experimental info

Sequence conflict401K → Y in BAB26900. Ref.2
Sequence conflict521S → T in BAB26900. Ref.2
Sequence conflict3441R → K in AAH23096. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 10, 2004. Version 1.
Checksum: 1DB6FA774C13BC59

FASTA44351,597
        10         20         30         40         50         60 
MSDMEDDFMC DDEEDYDLEY SEDSNSEPNV DLENQYYNSK ALKEDDPKAA LSSFQKVLEL 

        70         80         90        100        110        120 
EGEKGEWGFK ALKQMIKINF KLTNFPEMMN RYKQLLTYIR SAVTRNYSEK SINSILDYIS 

       130        140        150        160        170        180 
TSKQMDLLQE FYETTLEALK DAKNDRLWFK TNTKLGKLYL EREEYGKLQK ILRQLHQSCQ 

       190        200        210        220        230        240 
TDDGEDDLKK GTQLLEIYAL EIQMYTAQKN NKKLKALYEQ SLHIKSAIPH PLIMGVIREC 

       250        260        270        280        290        300 
GGKMHLREGE FEKAHTDFFE AFKNYDESGS PRRTTCLKYL VLANMLMKSG INPFDSQEAK 

       310        320        330        340        350        360 
PYKNDPEILA MTNLVSAYQN NDITEFEKIL KTNHSNIMDD PFIREHIEEL LRNIRTQVLI 

       370        380        390        400        410        420 
KLIKPYTRIH IPFISKELNI DVADVESLLV QCILDNTIHG RIDQVNQLLE LDHQKRGGAR 

       430        440 
YTALDKWTNQ LNSLNQAVVS KLA 

« Hide

Isoform 2 [UniParc].

Checksum: 581DE764677E90C0
Show »

FASTA45052,405

References

« Hide 'large scale' references
[1]"Coding sequence, genomic organization, chromosomal localization, and expression pattern of the signalosome component Cops2: the mouse homologue of Drosophila alien."
Schaefer L., Beermann M.L., Miller J.B.
Genomics 56:310-316(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[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. expand/collapse author list , 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] (ISOFORMS 1 AND 2).
Strain: C57BL/6J.
Tissue: Eye.
[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] OF 2-443 (ISOFORM 1).
Strain: Czech II.
Tissue: Mammary tumor.
[4]"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] OF 4-443 (ISOFORM 1), IDENTIFICATION IN THE CSN COMPLEX.
Strain: C57BL/6.
[5]"The COP9 signalosome inhibits p27(kip1) degradation and impedes G1-S phase progression via deneddylation of SCF Cul1."
Yang X., Menon S., Lykke-Andersen K., Tsuge T., Xiao D., Wang X., Rodriguez-Suarez R.J., Zhang H., Wei N.
Curr. Biol. 12:667-672(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CUL1 AND CUL2.
[6]"The role of transcriptional corepressor Nif3l1 in early stage of neural differentiation via cooperation with Trip15/CSN2."
Akiyama H., Fujisawa N., Tashiro Y., Takanabe N., Sugiyama A., Tashiro F.
J. Biol. Chem. 278:10752-10762(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH NIF3L1.
[7]"Disruption of the COP9 signalosome Csn2 subunit in mice causes deficient cell proliferation, accumulation of p53 and cyclin E, and early embryonic death."
Lykke-Andersen K., Schaefer L., Menon S., Deng X.-W., Miller J.B., Wei N.
Mol. Cell. Biol. 23:6790-6797(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF087688 mRNA. Translation: AAC36309.1.
AF114247 expand/collapse EMBL AC list , AF114236, AF114237, AF114238, AF114239, AF114240, AF114241, AF114242, AF114244, AF114245, AF114246 Genomic DNA. Translation: AAD26162.1.
AK010383 mRNA. Translation: BAB26900.1.
AK084421 mRNA. Translation: BAC39179.1.
AK132207 mRNA. Translation: BAE21033.1.
BC023096 mRNA. Translation: AAH23096.1. Different initiation.
AF071312 mRNA. Translation: AAC33899.1.
CCDSCCDS16679.1. [P61202-1]
CCDS71133.1. [P61202-2]
RefSeqNP_001272441.1. NM_001285512.1.
NP_034069.2. NM_009939.3. [P61202-1]
UniGeneMm.3596.

3D structure databases

ProteinModelPortalP61202.
SMRP61202. Positions 71-98, 133-441.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198836. 20 interactions.
MINTMINT-1869849.

PTM databases

PhosphoSiteP61202.

Proteomic databases

MaxQBP61202.
PaxDbP61202.
PRIDEP61202.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000028635; ENSMUSP00000028635; ENSMUSG00000027206. [P61202-1]
ENSMUST00000110463; ENSMUSP00000106090; ENSMUSG00000027206. [P61202-2]
GeneID12848.
KEGGmmu:12848.
UCSCuc008mdb.1. mouse. [P61202-1]

Organism-specific databases

CTD9318.
MGIMGI:1330276. Cops2.

Phylogenomic databases

eggNOGCOG5159.
GeneTreeENSGT00530000063301.
HOVERGENHBG003924.
KOK12176.
OMAYGLEYSE.
OrthoDBEOG7H7926.
TreeFamTF105738.

Gene expression databases

ArrayExpressP61202.
BgeeP61202.
CleanExMM_CSN2.
GenevestigatorP61202.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
1.25.40.10. 1 hit.
InterProIPR013143. PAM.
IPR000717. PCI_dom.
IPR011990. TPR-like_helical.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF01399. PCI. 1 hit.
[Graphical view]
SMARTSM00753. PAM. 1 hit.
SM00088. PINT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCOPS2. mouse.
NextBio282396.
PROP61202.
SOURCESearch...

Entry information

Entry nameCSN2_MOUSE
AccessionPrimary (citable) accession number: P61202
Secondary accession number(s): O88950 expand/collapse secondary AC list , Q15647, Q3V1W6, Q8R5B0, Q9CWU1, Q9R249, Q9UNQ5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: May 10, 2004
Last modified: July 9, 2014
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot