CSN5_MOUSE
ID CSN5_MOUSE Reviewed; 334 AA.
AC O35864; Q3UA70; Q8C1S1;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=COP9 signalosome complex subunit 5;
DE Short=SGN5;
DE Short=Signalosome subunit 5;
DE EC=3.4.-.-;
DE AltName: Full=Jun activation domain-binding protein 1;
DE AltName: Full=Kip1 C-terminus-interacting protein 2;
GN Name=Cops5; Synonyms=Csn5, Jab1, Kic2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9341143; DOI=10.1074/jbc.272.43.27042;
RA Asano K., Vornlocher H.-P., Richter-Cook N.J., Merrick W.C.,
RA Hinnebusch A.G., Hershey J.W.B.;
RT "Structure of cDNAs encoding human eukaryotic initiation factor 3 subunits.
RT Possible roles in RNA binding and macromolecular assembly.";
RL J. Biol. Chem. 272:27042-27052(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH CDKN1B.
RC STRAIN=NIH Swiss;
RX PubMed=10086358; DOI=10.1038/18230;
RA Tomoda K., Kubota Y., Kato J.-Y.;
RT "Degradation of the cyclin-dependent-kinase inhibitor p27Kip1 is instigated
RT by Jab1.";
RL Nature 398:160-165(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ;
RX PubMed=10721695; DOI=10.1016/s0378-1119(99)00525-9;
RA Bounpheng M.A., Melnikova I.N., Dodds S.G., Chen H., Copeland N.G.,
RA Gilbert D.J., Jenkins N.A., Christy B.A.;
RT "Characterization of the mouse JAB1 cDNA and protein.";
RL Gene 242:41-50(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=BALB/cJ, and C57BL/6J; TISSUE=Bone marrow, and Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 192-210 AND 220-230, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Yang J.W., Zigmond M.;
RL Submitted (JUL-2007) to UniProtKB.
RN [7]
RP IDENTIFICATION IN THE CSN COMPLEX.
RC STRAIN=C57BL/6J;
RX PubMed=9707402; DOI=10.1016/s0960-9822(07)00372-7;
RA Wei N., Tsuge T., Serino G., Dohmae N., Takio K., Matsui M., Deng X.-W.;
RT "The COP9 complex is conserved between plants and mammals and is related to
RT the 26S proteasome regulatory complex.";
RL Curr. Biol. 8:919-922(1998).
RN [8]
RP INTERACTION WITH HIF1A.
RX PubMed=11707426; DOI=10.1074/jbc.c100442200;
RA Bae M.-K., Ahn M.-Y., Jeong J.-W., Bae M.-H., Lee Y.M., Bae S.-K.,
RA Park J.-W., Kim K.-R., Kim K.-W.;
RT "Jab1 interacts directly with HIF-1alpha and regulates its stability.";
RL J. Biol. Chem. 277:9-12(2002).
RN [9]
RP MUTAGENESIS OF ASP-151.
RX PubMed=15082527; DOI=10.1101/gad.1180104;
RA Bemis L., Chan D.A., Finkielstein C.V., Qi L., Sutphin P.D., Chen X.,
RA Stenmark K., Giaccia A.J., Zundel W.;
RT "Distinct aerobic and hypoxic mechanisms of HIF-alpha regulation by CSN5.";
RL Genes Dev. 18:739-744(2004).
RN [10]
RP INTERACTION WITH ID1 AND ID3.
RX PubMed=15451666; DOI=10.1016/j.jmb.2004.08.043;
RA Berse M., Bounpheng M., Huang X., Christy B., Pollmann C., Dubiel W.;
RT "Ubiquitin-dependent degradation of Id1 and Id3 is mediated by the COP9
RT signalosome.";
RL J. Mol. Biol. 343:361-370(2004).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Probable protease subunit of the COP9 signalosome complex
CC (CSN), a complex involved in various cellular and developmental
CC processes. The CSN complex is an essential regulator of the ubiquitin
CC (Ubl) conjugation pathway by mediating the deneddylation of the cullin
CC subunits of the SCF-type E3 ligase complexes, leading to decrease the
CC Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2.
CC Promotes the proteasomal degradation of BRSK2. The complex is also
CC involved in phosphorylation of p53/TP53, c-jun/JUN,
CC IkappaBalpha/NFKBIA, ITPK1 and IRF8, possibly via its association with
CC CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN
CC promotes and protects degradation by the Ubl system, respectively. In
CC the complex, it probably acts as the catalytic center that mediates the
CC cleavage of Nedd8 from cullins. It however has no metalloprotease
CC activity by itself and requires the other subunits of the CSN complex.
CC Interacts directly with a large number of proteins that are regulated
CC by the CSN complex, confirming a key role in the complex.
CC {ECO:0000250|UniProtKB:Q92905}.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250};
CC -!- SUBUNIT: Component of the CSN complex, composed of COPS1/GPS1, COPS2,
CC COPS3, COPS4, COPS5, COPS6, COPS7 (COPS7A or COPS7B), COPS8 and COPS9.
CC In the complex, it probably interacts directly with COPS1, COPS2,
CC COPS4, COPS6 and COPS7 (COPS7A or COPS7B) and COPS9. The CSN complex
CC interacts with the BRISC complex. Also exists as monomeric form.
CC Interacts with TP53, MIF, JUN, UCHL1, NCOA1, BCL3, GFER, PGR, LHCGR,
CC SMAD4, SMAD7, ITGB2 and TOP2A. Part of a complex consisting of RANBP9,
CC RAN, DYRK1B and COPS5. Interacts with CDKN1B, HIF1A, ID1 and ID3.
CC Interacts with IFIT3. Interacts with BRSK2 (By similarity). Interacts
CC with ZDHHC16 (By similarity). Interacts with MINDY3 (By similarity).
CC Interacts with FANK1; regulates the phosphorylation of JUN and the
CC transcriptional activity of AP-1 (By similarity). Interacts with NUPR1;
CC this interaction allows COPS5-dependent CDKN1B nuclear to cytoplasm
CC translocation (By similarity). {ECO:0000250|UniProtKB:Q92905}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:10721695}.
CC Nucleus {ECO:0000269|PubMed:10721695}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q92905}. Cytoplasmic vesicle, secretory vesicle,
CC synaptic vesicle {ECO:0000250|UniProtKB:Q92905}. Note=Nuclear
CC localization is diminished in the presence of IFIT3.
CC {ECO:0000250|UniProtKB:Q92905}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10721695}.
CC -!- DOMAIN: The JAMM motif is essential for the protease activity of the
CC CSN complex resulting in deneddylation of cullins. It constitutes the
CC catalytic center of the complex. {ECO:0000269|PubMed:15082527}.
CC -!- MISCELLANEOUS: The CSN complex is associated with some 'Lys-63'-
CC specific deubiquitination. Such activity is however not mediated by the
CC core CSN complex but by the BRCC3/BRCC36 component of the BRISC complex
CC (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M67A family. CSN5 subfamily.
CC {ECO:0000305}.
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DR EMBL; U70736; AAD03470.1; -; mRNA.
DR EMBL; AF068223; AAF61318.1; -; mRNA.
DR EMBL; AF065386; AAC17179.1; -; mRNA.
DR EMBL; AK012499; BAB28282.1; -; mRNA.
DR EMBL; AK146271; BAE27030.1; -; mRNA.
DR EMBL; AK151492; BAE30445.1; -; mRNA.
DR EMBL; BC046753; AAH46753.1; -; mRNA.
DR CCDS; CCDS14818.1; -.
DR RefSeq; NP_001264030.1; NM_001277101.1.
DR RefSeq; NP_038743.1; NM_013715.2.
DR AlphaFoldDB; O35864; -.
DR SMR; O35864; -.
DR BioGRID; 205030; 64.
DR CORUM; O35864; -.
DR IntAct; O35864; 1.
DR MINT; O35864; -.
DR STRING; 10090.ENSMUSP00000027050; -.
DR MEROPS; M67.002; -.
DR iPTMnet; O35864; -.
DR PhosphoSitePlus; O35864; -.
DR REPRODUCTION-2DPAGE; O35864; -.
DR EPD; O35864; -.
DR jPOST; O35864; -.
DR MaxQB; O35864; -.
DR PaxDb; O35864; -.
DR PeptideAtlas; O35864; -.
DR PRIDE; O35864; -.
DR ProteomicsDB; 284138; -.
DR Antibodypedia; 1439; 540 antibodies from 43 providers.
DR DNASU; 26754; -.
DR Ensembl; ENSMUST00000027050; ENSMUSP00000027050; ENSMUSG00000025917.
DR GeneID; 26754; -.
DR KEGG; mmu:26754; -.
DR UCSC; uc007ahe.2; mouse.
DR CTD; 10987; -.
DR MGI; MGI:1349415; Cops5.
DR VEuPathDB; HostDB:ENSMUSG00000025917; -.
DR eggNOG; KOG1554; Eukaryota.
DR GeneTree; ENSGT00550000074850; -.
DR HOGENOM; CLU_053034_0_1_1; -.
DR InParanoid; O35864; -.
DR OMA; ALWNKYW; -.
DR OrthoDB; 1031881at2759; -.
DR PhylomeDB; O35864; -.
DR TreeFam; TF105601; -.
DR Reactome; R-MMU-5696394; DNA Damage Recognition in GG-NER.
DR Reactome; R-MMU-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-MMU-8951664; Neddylation.
DR BioGRID-ORCS; 26754; 25 hits in 77 CRISPR screens.
DR ChiTaRS; Cops5; mouse.
DR PRO; PR:O35864; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; O35864; protein.
DR Bgee; ENSMUSG00000025917; Expressed in undifferentiated genital tubercle and 290 other tissues.
DR ExpressionAtlas; O35864; baseline and differential.
DR Genevisible; O35864; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0008180; C:COP9 signalosome; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
DR GO; GO:0005667; C:transcription regulator complex; TAS:MGI.
DR GO; GO:0019784; F:deNEDDylase activity; IBA:GO_Central.
DR GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
DR GO; GO:0070122; F:isopeptidase activity; IEA:InterPro.
DR GO; GO:0035718; F:macrophage migration inhibitory factor binding; IPI:BHF-UCL.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0140492; F:metal-dependent deubiquitinase activity; ISO:MGI.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; ISO:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; TAS:MGI.
DR GO; GO:1990182; P:exosomal secretion; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0000338; P:protein deneddylation; ISO:MGI.
DR GO; GO:0016579; P:protein deubiquitination; ISO:MGI.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:MGI.
DR GO; GO:1903894; P:regulation of IRE1-mediated unfolded protein response; ISO:MGI.
DR GO; GO:0046328; P:regulation of JNK cascade; ISO:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:MGI.
DR InterPro; IPR037740; CSN5.
DR InterPro; IPR040961; CSN5_C.
DR InterPro; IPR000555; JAMM/MPN+_dom.
DR InterPro; IPR037518; MPN.
DR PANTHER; PTHR10410:SF6; PTHR10410:SF6; 1.
DR Pfam; PF18323; CSN5_C; 1.
DR Pfam; PF01398; JAB; 1.
DR SMART; SM00232; JAB_MPN; 1.
DR PROSITE; PS50249; MPN; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Cytoplasmic vesicle; Direct protein sequencing;
KW Hydrolase; Metal-binding; Metalloprotease; Nucleus; Protease;
KW Reference proteome; Signalosome; Synapse; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q92905"
FT CHAIN 2..334
FT /note="COP9 signalosome complex subunit 5"
FT /id="PRO_0000194836"
FT DOMAIN 55..192
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT MOTIF 138..151
FT /note="JAMM motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 138
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q92905"
FT MUTAGEN 151
FT /note="D->N: Abolishes ability to deneddylate cullins, but
FT keeps ability to stabilize HIF1A protein."
FT /evidence="ECO:0000269|PubMed:15082527"
SQ 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
