ID   CSN8_MOUSE              Reviewed;         209 AA.
AC   Q8VBV7; Q3TRS9; Q80XF4; Q8R4D2;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 150.
DE   RecName: Full=COP9 signalosome complex subunit 8;
DE            Short=SGN8;
DE            Short=Signalosome subunit 8;
DE   AltName: Full=COP9 homolog;
DE   AltName: Full=JAB1-containing signalosome subunit 8;
GN   Name=Cops8; Synonyms=Csn8;
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 [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RC   STRAIN=129/SvJ;
RX   PubMed=14636993; DOI=10.1016/s0378-1119(03)00836-9;
RA   Lykke-Andersen K., Wei N.;
RT   "Gene structure and embryonic expression of mouse COP9 signalosome subunit
RT   8 (Csn8).";
RL   Gene 321:65-72(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=BALB/cJ, C57BL/6J, and NOD;
RC   TISSUE=Embryo, Hypothalamus, Placenta, Thymus, and Urinary bladder;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon, Kidney, and Mammary tumor;
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   [4]
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   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, 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: Component of the COP9 signalosome complex (CSN), a complex
CC       involved in various cellular and developmental processes. The CSN
CC       complex is an essential regulator of the ubiquitin (Ubl) conjugation
CC       pathway by mediating the deneddylation of the cullin subunits of SCF-
CC       type E3 ligase complexes, leading to decrease the Ubl ligase activity
CC       of SCF-type complexes such as SCF, CSA or DDB2. The complex is also
CC       involved in phosphorylation of p53/TP53, c-jun/JUN,
CC       IkappaBalpha/NFKBIA, ITPK1 and IRF8/ICSBP, possibly via its association
CC       with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN
CC       promotes and protects degradation by the Ubl system, respectively (By
CC       similarity). {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       (PubMed:9707402). In the complex, it probably interacts directly with
CC       COPS3, COPS4 and COPS7 (COPS7A or COPS7B) (By similarity).
CC       {ECO:0000250|UniProtKB:Q99627, ECO:0000269|PubMed:9707402}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:14636993}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in embryonic stem (ES) cells and
CC       throughout early embryo development from zygote, preimplantation
CC       embryos, to post-implantation embryos. Predominantly expressed in the
CC       inner cell mass (ICM) of 3.5 dpc blastocyst and widely expressed in 9.5
CC       dpc embryos. {ECO:0000269|PubMed:14636993}.
CC   -!- SIMILARITY: Belongs to the CSN8 family. {ECO:0000305}.
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DR   EMBL; AF482000; AAL89689.1; -; mRNA.
DR   EMBL; AF502144; AAP13731.1; -; Genomic_DNA.
DR   EMBL; AK079111; BAC37543.1; -; mRNA.
DR   EMBL; AK079522; BAC37670.1; -; mRNA.
DR   EMBL; AK088323; BAC40281.1; -; mRNA.
DR   EMBL; AK090013; BAC41045.1; -; mRNA.
DR   EMBL; AK145899; BAE26735.1; -; mRNA.
DR   EMBL; AK162502; BAE36948.1; -; mRNA.
DR   EMBL; BC017690; AAH17690.1; -; mRNA.
DR   EMBL; BC021488; AAH21488.1; -; mRNA.
DR   EMBL; BC024421; AAH24421.1; -; mRNA.
DR   CCDS; CCDS15153.1; -.
DR   RefSeq; NP_598566.3; NM_133805.3.
DR   AlphaFoldDB; Q8VBV7; -.
DR   SMR; Q8VBV7; -.
DR   BioGRID; 224368; 42.
DR   CORUM; Q8VBV7; -.
DR   IntAct; Q8VBV7; 2.
DR   MINT; Q8VBV7; -.
DR   STRING; 10090.ENSMUSP00000035884; -.
DR   GlyGen; Q8VBV7; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8VBV7; -.
DR   PhosphoSitePlus; Q8VBV7; -.
DR   SwissPalm; Q8VBV7; -.
DR   REPRODUCTION-2DPAGE; Q8VBV7; -.
DR   EPD; Q8VBV7; -.
DR   MaxQB; Q8VBV7; -.
DR   PaxDb; 10090-ENSMUSP00000035884; -.
DR   PeptideAtlas; Q8VBV7; -.
DR   ProteomicsDB; 285330; -.
DR   Pumba; Q8VBV7; -.
DR   TopDownProteomics; Q8VBV7; -.
DR   Antibodypedia; 34471; 273 antibodies from 35 providers.
DR   DNASU; 108679; -.
DR   Ensembl; ENSMUST00000036153.12; ENSMUSP00000035884.6; ENSMUSG00000034432.12.
DR   GeneID; 108679; -.
DR   KEGG; mmu:108679; -.
DR   UCSC; uc007bzi.1; mouse.
DR   AGR; MGI:1915363; -.
DR   CTD; 10920; -.
DR   MGI; MGI:1915363; Cops8.
DR   VEuPathDB; HostDB:ENSMUSG00000034432; -.
DR   eggNOG; KOG4414; Eukaryota.
DR   GeneTree; ENSGT00390000000977; -.
DR   HOGENOM; CLU_098091_1_1_1; -.
DR   InParanoid; Q8VBV7; -.
DR   OMA; NNAKFLW; -.
DR   OrthoDB; 3675131at2759; -.
DR   PhylomeDB; Q8VBV7; -.
DR   TreeFam; TF101150; -.
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; 108679; 14 hits in 78 CRISPR screens.
DR   ChiTaRS; Cops8; mouse.
DR   PRO; PR:Q8VBV7; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q8VBV7; Protein.
DR   Bgee; ENSMUSG00000034432; Expressed in spermatocyte and 273 other cell types or tissues.
DR   ExpressionAtlas; Q8VBV7; baseline and differential.
DR   GO; GO:0008180; C:COP9 signalosome; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR   GO; GO:0010387; P:COP9 signalosome assembly; IEA:InterPro.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR   GO; GO:0000338; P:protein deneddylation; ISO:MGI.
DR   Gene3D; 1.25.40.990; -; 1.
DR   InterPro; IPR033205; COP9_CSN8.
DR   InterPro; IPR033464; CSN8_PSD8_EIF3K.
DR   InterPro; IPR000717; PCI_dom.
DR   PANTHER; PTHR13339; COP9 SIGNALOSOME COMPLEX SUBUNIT 8; 1.
DR   PANTHER; PTHR13339:SF0; COP9 SIGNALOSOME COMPLEX SUBUNIT 8; 1.
DR   Pfam; PF10075; CSN8_PSD8_EIF3K; 1.
DR   PROSITE; PS50250; PCI; 1.
DR   Genevisible; Q8VBV7; MM.
PE   1: Evidence at protein level;
KW   Cytoplasm; Nucleus; Phosphoprotein; Reference proteome; Signalosome.
FT   CHAIN           1..209
FT                   /note="COP9 signalosome complex subunit 8"
FT                   /id="PRO_0000121008"
FT   DOMAIN          8..179
FT                   /note="PCI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT   MOD_RES         175
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99627"
FT   CONFLICT        193
FT                   /note="N -> M (in Ref. 1; AAL89689)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        193
FT                   /note="N -> T (in Ref. 1; AAP13731)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        194..195
FT                   /note="EQ -> SR (in Ref. 1)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   209 AA;  23256 MW;  786226FB7BFAC80E CRC64;
     MPVAVMADNA FSFRKLLDQC ENQELEAPGG IATPPVYGQL LALYLLQNDM NNARYLWKRI
     PPAIKSANSE LGGIWSVGQR IWQRDFPGIY TTINAHQWSE TVQPIMEALR DATRRRAFAL
     VSQAYTSIIA DDFAAFVGLP VEEAVKGVLE QGWQADSTTR MVLPRKPASG TLDVSLNRFI
     PLSEPAPVPP IPNEQQLARL TDYVAFLEN
//