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P61202

- CSN2_MOUSE

UniProt

P61202 - CSN2_MOUSE

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Protein

COP9 signalosome complex subunit 2

Gene
Cops2, Csn2, Trip15
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 NIF3L1.3 Publications

GO - Molecular functioni

  1. protein binding Source: MGI
  2. transcription corepressor activity Source: MGI

GO - Biological processi

  1. cell proliferation Source: MGI
  2. cullin deneddylation Source: Ensembl
  3. negative regulation of transcription, DNA-templated Source: MGI
  4. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  5. neuron differentiation Source: Ensembl
  6. skeletal muscle cell differentiation Source: MGI
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Cops2
Synonyms:Csn2, Trip15
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:1330276. Cops2.

Subcellular locationi

Cytoplasm. Nucleus 1 Publication

GO - Cellular componenti

  1. COP9 signalosome Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Signalosome

Pathology & Biotechi

Disruption phenotypei

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.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 443443COP9 signalosome complex subunit 2PRO_0000120969Add
BLAST

Post-translational modificationi

Phosphorylated by CK2 and PKD kinases By similarity.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP61202.
PaxDbiP61202.
PRIDEiP61202.

PTM databases

PhosphoSiteiP61202.

Expressioni

Tissue specificityi

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

Gene expression databases

ArrayExpressiP61202.
BgeeiP61202.
CleanExiMM_CSN2.
GenevestigatoriP61202.

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 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 CUL2.3 Publications

Protein-protein interaction databases

BioGridi198836. 20 interactions.
MINTiMINT-1869849.

Structurei

3D structure databases

ProteinModelPortaliP61202.
SMRiP61202. Positions 71-98, 133-441.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini248 – 413166PCIAdd
BLAST

Sequence similaritiesi

Belongs to the CSN2 family.
Contains 1 PCI domain.

Phylogenomic databases

eggNOGiCOG5159.
GeneTreeiENSGT00530000063301.
HOVERGENiHBG003924.
KOiK12176.
OMAiYGLEYSE.
OrthoDBiEOG7H7926.
TreeFamiTF105738.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
1.25.40.10. 1 hit.
InterProiIPR013143. PAM.
IPR000717. PCI_dom.
IPR011990. TPR-like_helical.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF01399. PCI. 1 hit.
[Graphical view]
SMARTiSM00753. PAM. 1 hit.
SM00088. PINT. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P61202-1) [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

MSDMEDDFMC DDEEDYDLEY SEDSNSEPNV DLENQYYNSK ALKEDDPKAA    50
LSSFQKVLEL EGEKGEWGFK ALKQMIKINF KLTNFPEMMN RYKQLLTYIR 100
SAVTRNYSEK SINSILDYIS TSKQMDLLQE FYETTLEALK DAKNDRLWFK 150
TNTKLGKLYL EREEYGKLQK ILRQLHQSCQ TDDGEDDLKK GTQLLEIYAL 200
EIQMYTAQKN NKKLKALYEQ SLHIKSAIPH PLIMGVIREC GGKMHLREGE 250
FEKAHTDFFE AFKNYDESGS PRRTTCLKYL VLANMLMKSG INPFDSQEAK 300
PYKNDPEILA MTNLVSAYQN NDITEFEKIL KTNHSNIMDD PFIREHIEEL 350
LRNIRTQVLI KLIKPYTRIH IPFISKELNI DVADVESLLV QCILDNTIHG 400
RIDQVNQLLE LDHQKRGGAR YTALDKWTNQ LNSLNQAVVS KLA 443
Length:443
Mass (Da):51,597
Last modified:May 10, 2004 - v1
Checksum:i1DB6FA774C13BC59
GO
Isoform 2 (identifier: P61202-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:450
Mass (Da):52,405
Checksum:i581DE764677E90C0
GO

Sequence cautioni

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei124 – 1241Q → QNSDFLCQ in isoform 2. VSP_011885

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti40 – 401K → Y in BAB26900. 1 Publication
Sequence conflicti52 – 521S → T in BAB26900. 1 Publication
Sequence conflicti344 – 3441R → K in AAH23096. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF087688 mRNA. Translation: AAC36309.1.
AF114247
, 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.
CCDSiCCDS16679.1. [P61202-1]
CCDS71133.1. [P61202-2]
RefSeqiNP_001272441.1. NM_001285512.1.
NP_034069.2. NM_009939.3. [P61202-1]
UniGeneiMm.3596.

Genome annotation databases

EnsembliENSMUST00000028635; ENSMUSP00000028635; ENSMUSG00000027206. [P61202-1]
ENSMUST00000110463; ENSMUSP00000106090; ENSMUSG00000027206. [P61202-2]
GeneIDi12848.
KEGGimmu:12848.
UCSCiuc008mdb.1. mouse. [P61202-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF087688 mRNA. Translation: AAC36309.1 .
AF114247
, 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 .
CCDSi CCDS16679.1. [P61202-1 ]
CCDS71133.1. [P61202-2 ]
RefSeqi NP_001272441.1. NM_001285512.1.
NP_034069.2. NM_009939.3. [P61202-1 ]
UniGenei Mm.3596.

3D structure databases

ProteinModelPortali P61202.
SMRi P61202. Positions 71-98, 133-441.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 198836. 20 interactions.
MINTi MINT-1869849.

PTM databases

PhosphoSitei P61202.

Proteomic databases

MaxQBi P61202.
PaxDbi P61202.
PRIDEi P61202.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000028635 ; ENSMUSP00000028635 ; ENSMUSG00000027206 . [P61202-1 ]
ENSMUST00000110463 ; ENSMUSP00000106090 ; ENSMUSG00000027206 . [P61202-2 ]
GeneIDi 12848.
KEGGi mmu:12848.
UCSCi uc008mdb.1. mouse. [P61202-1 ]

Organism-specific databases

CTDi 9318.
MGIi MGI:1330276. Cops2.

Phylogenomic databases

eggNOGi COG5159.
GeneTreei ENSGT00530000063301.
HOVERGENi HBG003924.
KOi K12176.
OMAi YGLEYSE.
OrthoDBi EOG7H7926.
TreeFami TF105738.

Miscellaneous databases

ChiTaRSi COPS2. mouse.
NextBioi 282396.
PROi P61202.
SOURCEi Search...

Gene expression databases

ArrayExpressi P61202.
Bgeei P61202.
CleanExi MM_CSN2.
Genevestigatori P61202.

Family and domain databases

Gene3Di 1.10.10.10. 1 hit.
1.25.40.10. 1 hit.
InterProi IPR013143. PAM.
IPR000717. PCI_dom.
IPR011990. TPR-like_helical.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view ]
Pfami PF01399. PCI. 1 hit.
[Graphical view ]
SMARTi SM00753. PAM. 1 hit.
SM00088. PINT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiCSN2_MOUSE
AccessioniPrimary (citable) accession number: P61202
Secondary accession number(s): O88950
, Q15647, Q3V1W6, Q8R5B0, Q9CWU1, Q9R249, Q9UNQ5
Entry historyi
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 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

External Data

Dasty 3

Similar proteinsi