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COP9 signalosome complex subunit 5 (SGN5) (Signalosome subunit 5) (EC 3.4.-.-) (Jun activation domain-binding protein 1) (Kip1 C-terminus-interacting protein 2)

 CSN5_MOUSE              Reviewed;         334 AA.
O35864; Q3UA70; Q8C1S1;
23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
28-MAR-2018, entry version 149.
RecName: Full=COP9 signalosome complex subunit 5;
Short=SGN5;
Short=Signalosome subunit 5;
EC=3.4.-.-;
AltName: Full=Jun activation domain-binding protein 1;
AltName: Full=Kip1 C-terminus-interacting protein 2;
Name=Cops5; Synonyms=Csn5, Jab1, Kic2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9341143; DOI=10.1074/jbc.272.43.27042;
Asano K., Vornlocher H.-P., Richter-Cook N.J., Merrick W.C.,
Hinnebusch A.G., Hershey J.W.B.;
"Structure of cDNAs encoding human eukaryotic initiation factor 3
subunits. Possible roles in RNA binding and macromolecular assembly.";
J. Biol. Chem. 272:27042-27052(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH CDKN1B.
STRAIN=NIH Swiss;
PubMed=10086358; DOI=10.1038/18230;
Tomoda K., Kubota Y., Kato J.-Y.;
"Degradation of the cyclin-dependent-kinase inhibitor p27Kip1 is
instigated by Jab1.";
Nature 398:160-165(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
STRAIN=BALB/cJ;
PubMed=10721695; DOI=10.1016/S0378-1119(99)00525-9;
Bounpheng M.A., Melnikova I.N., Dodds S.G., Chen H., Copeland N.G.,
Gilbert D.J., Jenkins N.A., Christy B.A.;
"Characterization of the mouse JAB1 cDNA and protein.";
Gene 242:41-50(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=BALB/cJ, and C57BL/6J; TISSUE=Bone marrow, and Embryo;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 192-210 AND 220-230, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Brain, and Hippocampus;
Lubec G., Klug S., Yang J.W., Zigmond M.;
Submitted (JUL-2007) to UniProtKB.
[7]
IDENTIFICATION IN THE CSN COMPLEX.
STRAIN=C57BL/6J;
PubMed=9707402; DOI=10.1016/S0960-9822(07)00372-7;
Wei N., Tsuge T., Serino G., Dohmae N., Takio K., Matsui M.,
Deng X.-W.;
"The COP9 complex is conserved between plants and mammals and is
related to the 26S proteasome regulatory complex.";
Curr. Biol. 8:919-922(1998).
[8]
INTERACTION WITH HIF1A.
PubMed=11707426; DOI=10.1074/jbc.C100442200;
Bae M.-K., Ahn M.-Y., Jeong J.-W., Bae M.-H., Lee Y.M., Bae S.-K.,
Park J.-W., Kim K.-R., Kim K.-W.;
"Jab1 interacts directly with HIF-1alpha and regulates its
stability.";
J. Biol. Chem. 277:9-12(2002).
[9]
MUTAGENESIS OF ASP-151.
PubMed=15082527; DOI=10.1101/gad.1180104;
Bemis L., Chan D.A., Finkielstein C.V., Qi L., Sutphin P.D., Chen X.,
Stenmark K., Giaccia A.J., Zundel W.;
"Distinct aerobic and hypoxic mechanisms of HIF-alpha regulation by
CSN5.";
Genes Dev. 18:739-744(2004).
[10]
INTERACTION WITH ID1 AND ID3.
PubMed=15451666; DOI=10.1016/j.jmb.2004.08.043;
Berse M., Bounpheng M., Huang X., Christy B., Pollmann C., Dubiel W.;
"Ubiquitin-dependent degradation of Id1 and Id3 is mediated by the
COP9 signalosome.";
J. Mol. Biol. 343:361-370(2004).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Probable protease subunit 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 the SCF-type E3 ligase
complexes, leading to decrease the Ubl ligase activity of SCF-type
complexes such as SCF, CSA or DDB2. Promotes the proteasomal
degradation of BRSK2. The complex is also involved in
phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1
and IRF8, 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. In the
complex, it probably acts as the catalytic center that mediates
the cleavage of Nedd8 from cullins. It however has no
metalloprotease activity by itself and requires the other subunits
of the CSN complex. Interacts directly with a large number of
proteins that are regulated by the CSN complex, confirming a key
role in the complex. {ECO:0000250|UniProtKB:Q92905}.
-!- COFACTOR:
Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
Evidence={ECO:0000250};
-!- SUBUNIT: Component of the CSN complex, composed of COPS1/GPS1,
COPS2, COPS3, COPS4, COPS5, COPS6, COPS7 (COPS7A or COPS7B), COPS8
and COPS9. In the complex, it probably interacts directly with
COPS1, COPS2, COPS4, COPS6 and COPS7 (COPS7A or COPS7B) and COPS9.
The CSN complex interacts with the BRISC complex. Also exists as
monomeric form. Interacts with TP53, MIF, JUN, UCHL1, NCOA1, BCL3,
GFER, PGR, LHCGR, SMAD4, SMAD7, ITGB2 and TOP2A. Part of a complex
consisting of RANBP9, RAN, DYRK1B and COPS5. Interacts with
CDKN1B, HIF1A, ID1 and ID3. Interacts with IFIT3. Interacts with
BRSK2 (By similarity). Interacts with ZDHHC16 (By similarity).
Interacts with MINDY3 (By similarity). Interacts with FANK1;
regulates the phosphorylation of JUN and the transcriptional
activity of AP-1 (By similarity). {ECO:0000250|UniProtKB:Q92905}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:10721695}. Nucleus
{ECO:0000269|PubMed:10721695}. Cytoplasm, perinuclear region
{ECO:0000250|UniProtKB:Q92905}. Cytoplasmic vesicle, secretory
vesicle, synaptic vesicle {ECO:0000250|UniProtKB:Q92905}.
Note=Nuclear localization is diminished in the presence of IFIT3.
{ECO:0000250|UniProtKB:Q92905}.
-!- TISSUE SPECIFICITY: Widely expressed.
{ECO:0000269|PubMed:10721695}.
-!- DOMAIN: The JAMM motif is essential for the protease activity of
the CSN complex resulting in deneddylation of cullins. It
constitutes the catalytic center of the complex.
-!- MISCELLANEOUS: The CSN complex is associated with some 'Lys-63'-
specific deubiquitination. Such activity is however not mediated
by the core CSN complex but by the BRCC3/BRCC36 component of the
BRISC complex (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the peptidase M67A family. CSN5 subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U70736; AAD03470.1; -; mRNA.
EMBL; AF068223; AAF61318.1; -; mRNA.
EMBL; AF065386; AAC17179.1; -; mRNA.
EMBL; AK012499; BAB28282.1; -; mRNA.
EMBL; AK146271; BAE27030.1; -; mRNA.
EMBL; AK151492; BAE30445.1; -; mRNA.
EMBL; BC046753; AAH46753.1; -; mRNA.
CCDS; CCDS14818.1; -.
RefSeq; NP_001264030.1; NM_001277101.1.
RefSeq; NP_038743.1; NM_013715.2.
UniGene; Mm.402384; -.
ProteinModelPortal; O35864; -.
SMR; O35864; -.
BioGrid; 205030; 20.
CORUM; O35864; -.
IntAct; O35864; 2.
MINT; O35864; -.
STRING; 10090.ENSMUSP00000027050; -.
MEROPS; M67.002; -.
iPTMnet; O35864; -.
PhosphoSitePlus; O35864; -.
REPRODUCTION-2DPAGE; O35864; -.
EPD; O35864; -.
MaxQB; O35864; -.
PaxDb; O35864; -.
PeptideAtlas; O35864; -.
PRIDE; O35864; -.
Ensembl; ENSMUST00000027050; ENSMUSP00000027050; ENSMUSG00000025917.
GeneID; 26754; -.
KEGG; mmu:26754; -.
UCSC; uc007ahe.2; mouse.
CTD; 10987; -.
MGI; MGI:1349415; Cops5.
eggNOG; KOG1554; Eukaryota.
eggNOG; COG1310; LUCA.
GeneTree; ENSGT00550000074850; -.
HOGENOM; HOG000116528; -.
HOVERGEN; HBG051137; -.
InParanoid; O35864; -.
KO; K09613; -.
OMA; KYWVQTL; -.
OrthoDB; EOG091G0AAO; -.
PhylomeDB; O35864; -.
TreeFam; TF105601; -.
Reactome; R-MMU-5696394; DNA Damage Recognition in GG-NER.
Reactome; R-MMU-6781823; Formation of TC-NER Pre-Incision Complex.
Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
Reactome; R-MMU-8951664; Neddylation.
PRO; PR:O35864; -.
Proteomes; UP000000589; Chromosome 1.
Bgee; ENSMUSG00000025917; -.
ExpressionAtlas; O35864; baseline and differential.
Genevisible; O35864; MM.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0000785; C:chromatin; IEA:Ensembl.
GO; GO:0008180; C:COP9 signalosome; IDA:MGI.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
GO; GO:0005667; C:transcription factor complex; TAS:MGI.
GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
GO; GO:0035718; F:macrophage migration inhibitory factor binding; IPI:BHF-UCL.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
GO; GO:0008237; F:metallopeptidase activity; ISO:MGI.
GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; ISO:MGI.
GO; GO:0003713; F:transcription coactivator activity; TAS:MGI.
GO; GO:1990182; P:exosomal secretion; ISO:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
GO; GO:0051091; P:positive regulation of DNA binding transcription factor activity; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
GO; GO:0000338; P:protein deneddylation; ISO:MGI.
GO; GO:0016579; P:protein deubiquitination; ISO:MGI.
GO; GO:0051726; P:regulation of cell cycle; IMP:MGI.
GO; GO:1903894; P:regulation of IRE1-mediated unfolded protein response; ISO:MGI.
GO; GO:0046328; P:regulation of JNK cascade; ISO:MGI.
GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:MGI.
InterPro; IPR037740; CSN5.
InterPro; IPR000555; JAMM/MPN+_dom.
InterPro; IPR037518; MPN.
PANTHER; PTHR10410:SF6; PTHR10410:SF6; 1.
Pfam; PF01398; JAB; 1.
SMART; SM00232; JAB_MPN; 1.
PROSITE; PS50249; MPN; 1.
1: Evidence at protein level;
Acetylation; Cell junction; Complete proteome; Cytoplasm;
Cytoplasmic vesicle; Direct protein sequencing; Hydrolase;
Metal-binding; Metalloprotease; Nucleus; Protease; Reference proteome;
Signalosome; Synapse; Zinc.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q92905}.
CHAIN 2 334 COP9 signalosome complex subunit 5.
/FTId=PRO_0000194836.
DOMAIN 55 192 MPN. {ECO:0000255|PROSITE-
ProRule:PRU01182}.
MOTIF 138 151 JAMM motif. {ECO:0000255|PROSITE-
ProRule:PRU01182}.
METAL 138 138 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU01182}.
METAL 140 140 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU01182}.
METAL 151 151 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU01182}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:Q92905}.
MUTAGEN 151 151 D->N: Abolishes ability to deneddylate
cullins, but keeps ability to stabilize
HIF1A protein.
{ECO:0000269|PubMed:15082527}.
SEQUENCE 334 AA; 37549 MW; AD06BF4AAD03A1CF CRC64;
MAASGSGMAQ KTWELANNMQ EAQSIDEIYK YDKKQQQEIL AAKPWTKDHH YFKYCKISAL
ALLKMVMHAR SGGNLEVMGL MLGKVDGETM IIMDSFALPV EGTETRVNAQ AAAYEYMAAY
IENAKQVGRL ENAIGWYHSH PGYGCWLSGI DVSTQMLNQQ FQEPFVAVVI DPTRTISAGK
VNLGAFRTYP KGYKPPDEGP SEYQTIPLNK IEDFGVHCKQ YYALEVSYFK SSLDRKLLEL
LWNKYWVNTL SSSSLLTNAD YTTGQVFDLS EKLEQSEAQL GRGSFMLGLE THDRKSEDKL
AKATRDSCKT TIEAIHGLMS QVIKDKLFNQ INVA


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