CSN7A_MOUSE
ID CSN7A_MOUSE Reviewed; 275 AA.
AC Q9CZ04; O88546; Q925R8; Q9CPQ4; Q9CWD2;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=COP9 signalosome complex subunit 7a;
DE Short=SGN7a;
DE Short=Signalosome subunit 7a;
DE AltName: Full=JAB1-containing signalosome subunit 7a;
GN Name=Cops7a; Synonyms=Csn7a;
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] (ISOFORM 1), AND IDENTIFICATION IN THE CSN
RP COMPLEX.
RC STRAIN=C57BLKS/J;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=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 NUCLEOTIDE SEQUENCE [MRNA] OF 9-67.
RX PubMed=11819679; DOI=10.3748/wjg.v6.i5.709;
RA Cui D.X., Zeng G.Y., Wang F., Xu J.R., Ren D.Q., Guo Y.H., Tian F.R.,
RA Yan X.J., Hou Y., Su C.Z.;
RT "Mechanism of exogenous nucleic acids and their precursors improving the
RT repair of intestinal epithelium after gamma-irradiation in mice.";
RL World J. Gastroenterol. 6:709-717(2000).
RN [5]
RP INTERACTION WITH 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 [6]
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: 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, JUN, I-kappa-B-alpha/NFKBIA,
CC ITPK1 and IRF8/ICSBP, possibly via its association with CK2 and PKD
CC kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and
CC protects degradation by the Ubl system, respectively (By similarity).
CC {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 COPS1, COPS2, COPS4, COPS5, COPS6 and COPS8. Interacts with PMF1.
CC Interacts with the translation initiation factor EIF3S6. Interacts with
CC CK2 and PKD (By similarity). Interacts directly with ID3
CC (PubMed:15451666). {ECO:0000250|UniProtKB:Q9UBW8,
CC ECO:0000269|PubMed:15451666, ECO:0000269|PubMed:9707402}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9CZ04-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9CZ04-2; Sequence=VSP_011912;
CC -!- PTM: Phosphorylated by CK2 and PKD kinases.
CC -!- SIMILARITY: Belongs to the CSN7/EIF3M family. CSN7 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK43736.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB27144.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF071316; AAC33903.1; -; mRNA.
DR EMBL; AK010726; BAB27144.1; ALT_FRAME; mRNA.
DR EMBL; AK013155; BAB28682.1; -; mRNA.
DR EMBL; AK019122; BAB31554.1; -; mRNA.
DR EMBL; BC003724; AAH03724.1; -; mRNA.
DR EMBL; AF240179; AAK43736.1; ALT_FRAME; mRNA.
DR CCDS; CCDS20539.1; -. [Q9CZ04-1]
DR CCDS; CCDS51909.1; -. [Q9CZ04-2]
DR RefSeq; NP_001157561.1; NM_001164089.1. [Q9CZ04-2]
DR RefSeq; NP_036133.1; NM_012003.2. [Q9CZ04-1]
DR RefSeq; XP_006506222.1; XM_006506159.3.
DR RefSeq; XP_006506223.1; XM_006506160.2.
DR RefSeq; XP_006506224.1; XM_006506161.2. [Q9CZ04-2]
DR RefSeq; XP_006506225.1; XM_006506162.3.
DR RefSeq; XP_011239667.1; XM_011241365.2.
DR RefSeq; XP_017177082.1; XM_017321593.1.
DR AlphaFoldDB; Q9CZ04; -.
DR SMR; Q9CZ04; -.
DR BioGRID; 205045; 33.
DR CORUM; Q9CZ04; -.
DR STRING; 10090.ENSMUSP00000108058; -.
DR iPTMnet; Q9CZ04; -.
DR PhosphoSitePlus; Q9CZ04; -.
DR SwissPalm; Q9CZ04; -.
DR EPD; Q9CZ04; -.
DR jPOST; Q9CZ04; -.
DR MaxQB; Q9CZ04; -.
DR PaxDb; Q9CZ04; -.
DR PeptideAtlas; Q9CZ04; -.
DR PRIDE; Q9CZ04; -.
DR ProteomicsDB; 285349; -. [Q9CZ04-1]
DR ProteomicsDB; 285350; -. [Q9CZ04-2]
DR Antibodypedia; 11091; 227 antibodies from 31 providers.
DR DNASU; 26894; -.
DR Ensembl; ENSMUST00000032220; ENSMUSP00000032220; ENSMUSG00000030127. [Q9CZ04-1]
DR Ensembl; ENSMUST00000112439; ENSMUSP00000108058; ENSMUSG00000030127. [Q9CZ04-2]
DR GeneID; 26894; -.
DR KEGG; mmu:26894; -.
DR UCSC; uc009dsr.2; mouse. [Q9CZ04-2]
DR UCSC; uc009dss.2; mouse. [Q9CZ04-1]
DR CTD; 50813; -.
DR MGI; MGI:1349400; Cops7a.
DR VEuPathDB; HostDB:ENSMUSG00000030127; -.
DR eggNOG; KOG3250; Eukaryota.
DR GeneTree; ENSGT00940000159873; -.
DR InParanoid; Q9CZ04; -.
DR OMA; DIDSRGH; -.
DR OrthoDB; 1396757at2759; -.
DR PhylomeDB; Q9CZ04; -.
DR TreeFam; TF101149; -.
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; 26894; 8 hits in 74 CRISPR screens.
DR ChiTaRS; Cops7a; mouse.
DR PRO; PR:Q9CZ04; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9CZ04; protein.
DR Bgee; ENSMUSG00000030127; Expressed in spermatocyte and 272 other tissues.
DR ExpressionAtlas; Q9CZ04; baseline and differential.
DR Genevisible; Q9CZ04; MM.
DR GO; GO:0008180; C:COP9 signalosome; ISO: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; ISO:MGI.
DR GO; GO:0010387; P:COP9 signalosome assembly; IEA:InterPro.
DR GO; GO:0000338; P:protein deneddylation; ISO:MGI.
DR InterPro; IPR045237; COPS7/eIF3m.
DR InterPro; IPR037757; COPS7A.
DR InterPro; IPR041481; CSN7_helixI.
DR InterPro; IPR000717; PCI_dom.
DR PANTHER; PTHR15350; PTHR15350; 1.
DR PANTHER; PTHR15350:SF7; PTHR15350:SF7; 1.
DR Pfam; PF18392; CSN7a_helixI; 1.
DR Pfam; PF01399; PCI; 1.
DR SMART; SM00088; PINT; 1.
DR PROSITE; PS50250; PCI; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Cytoplasm; Nucleus;
KW Phosphoprotein; Reference proteome; Signalosome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9UBW8"
FT CHAIN 2..275
FT /note="COP9 signalosome complex subunit 7a"
FT /id="PRO_0000120997"
FT DOMAIN 2..159
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 228..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 185..233
FT /evidence="ECO:0000255"
FT COMPBIAS 243..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBW8"
FT VAR_SEQ 264..275
FT /note="LRGSAKIWSKSN -> EKINPQSTVKPSAK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_011912"
FT CONFLICT 153
FT /note="E -> K (in Ref. 2; BAB28682)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 275 AA; 30224 MW; B104C9FA318FDE24 CRC64;
MSAEVKVTGQ NQEQFLLLAK SAKGAALATL IHQVLEAPGV YVFGELLDMP NVRELAESDF
ASTFRLLTVF AYGTYADYLA EARNLPPLTD AQKNKLRHLS VVTLAAKVKC IPYAVLLEAL
ALRNVRQLED LVIEAVYADV LRGSLDQRNQ RLEVDYSIGR DIQRQDLSAI AQTLQEWCVG
CEVVLSGIEE QVSRANQHKE QQLGLKQQIE SEVANLKKTI KVTTAAAAAA TSQDPEQHLT
ELREPASGTN QRQPSKKASK GKGLRGSAKI WSKSN
