CSN9_MOUSE
ID CSN9_MOUSE Reviewed; 57 AA.
AC Q3U898;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=COP9 signalosome complex subunit 9 {ECO:0000305};
GN Name=Cops9 {ECO:0000250|UniProtKB:Q8WXC6}; Synonyms=Myeov2;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow;
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 [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas;
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.
CC Plays a role in cell proliferation. {ECO:0000250|UniProtKB:Q8WXC6}.
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 interacts directly with COPS3, COPS5 and COPS6.
CC {ECO:0000250|UniProtKB:Q8WXC6}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8WXC6}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q8WXC6}. Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q8WXC6}. Note=Excluded from the nucleolus.
CC Recruited to the nucleoplasm and chromatin following DNA damage
CC induction. {ECO:0000250|UniProtKB:Q8WXC6}.
CC -!- DOMAIN: The Phe/Asp-rich domain at the C-terminus is necessary for its
CC incorporation into the CSN complex. {ECO:0000250|UniProtKB:Q8WXC6}.
CC -!- SIMILARITY: Belongs to the CSN9 family. {ECO:0000305}.
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DR EMBL; AK152318; BAE31120.1; -; mRNA.
DR CCDS; CCDS48325.1; -.
DR RefSeq; NP_001156897.1; NM_001163425.1.
DR AlphaFoldDB; Q3U898; -.
DR BioGRID; 211807; 1.
DR STRING; 10090.ENSMUSP00000095247; -.
DR iPTMnet; Q3U898; -.
DR PhosphoSitePlus; Q3U898; -.
DR MaxQB; Q3U898; -.
DR PaxDb; Q3U898; -.
DR PRIDE; Q3U898; -.
DR ProteomicsDB; 279287; -.
DR Ensembl; ENSMUST00000097642; ENSMUSP00000095247; ENSMUSG00000073616.
DR GeneID; 66915; -.
DR KEGG; mmu:66915; -.
DR UCSC; uc007cbq.2; mouse.
DR CTD; 150678; -.
DR MGI; MGI:1914165; Cops9.
DR VEuPathDB; HostDB:ENSMUSG00000073616; -.
DR eggNOG; ENOG502S7KZ; Eukaryota.
DR GeneTree; ENSGT01050000245149; -.
DR HOGENOM; CLU_191079_0_0_1; -.
DR InParanoid; Q3U898; -.
DR OMA; SNDKHVH; -.
DR OrthoDB; 1635275at2759; -.
DR TreeFam; TF323869; -.
DR BioGRID-ORCS; 66915; 4 hits in 69 CRISPR screens.
DR ChiTaRS; Cops9; mouse.
DR PRO; PR:Q3U898; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q3U898; protein.
DR Bgee; ENSMUSG00000073616; Expressed in facial nucleus and 257 other tissues.
DR ExpressionAtlas; Q3U898; baseline and differential.
DR Genevisible; Q3U898; MM.
DR GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR GO; GO:0008180; C:COP9 signalosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0034644; P:cellular response to UV; ISS:UniProtKB.
DR GO; GO:0051220; P:cytoplasmic sequestering of protein; ISO:MGI.
DR GO; GO:2000435; P:negative regulation of protein neddylation; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR InterPro; IPR029391; CSN9_metazoa.
DR PANTHER; PTHR28562; PTHR28562; 1.
DR Pfam; PF15004; MYEOV2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Phosphoprotein; Reference proteome; Signalosome.
FT CHAIN 1..57
FT /note="COP9 signalosome complex subunit 9"
FT /id="PRO_0000332925"
FT MOD_RES 26
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8WXC6"
SQ SEQUENCE 57 AA; 6197 MW; 83144AFBF3DC610C CRC64;
MKPAVDEMFP EGAGPYVDLD EAGGSTGLLM DLAANEKAVH ADFFNDFEDL FDDDDVQ
