CSN7B_MOUSE
ID CSN7B_MOUSE Reviewed; 264 AA.
AC Q8BV13; O88547; Q3TGG7; Q921G4;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=COP9 signalosome complex subunit 7b;
DE Short=SGN7b;
DE Short=Signalosome subunit 7b;
DE AltName: Full=JAB1-containing signalosome subunit 7b;
GN Name=Cops7b; Synonyms=Csn7b;
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], AND IDENTIFICATION IN THE CSN 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].
RC STRAIN=C57BL/6J; TISSUE=Amnion, and Head;
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=Czech II; 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Liver, Lung, 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, 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) and COPS8 and
CC COPS9 (PubMed:9707402). In the complex, it probably interacts directly
CC with COPS1, COPS2, COPS4, COPS5, COPS6 and COPS8. Interacts with EIF3S6
CC (By similarity). {ECO:0000250|UniProtKB:Q9H9Q2,
CC ECO:0000269|PubMed:9707402}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CSN7/EIF3M family. CSN7 subfamily.
CC {ECO:0000305}.
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DR EMBL; AF071317; AAC33904.1; -; mRNA.
DR EMBL; AK081309; BAC38192.1; -; mRNA.
DR EMBL; AK168740; BAE40581.1; -; mRNA.
DR EMBL; BC012659; AAH12659.1; -; mRNA.
DR CCDS; CCDS15122.1; -.
DR RefSeq; NP_766562.1; NM_172974.2.
DR RefSeq; XP_006529686.1; XM_006529623.3.
DR RefSeq; XP_006529687.1; XM_006529624.3.
DR AlphaFoldDB; Q8BV13; -.
DR SMR; Q8BV13; -.
DR BioGRID; 205046; 23.
DR IntAct; Q8BV13; 1.
DR MINT; Q8BV13; -.
DR STRING; 10090.ENSMUSP00000113587; -.
DR iPTMnet; Q8BV13; -.
DR PhosphoSitePlus; Q8BV13; -.
DR EPD; Q8BV13; -.
DR MaxQB; Q8BV13; -.
DR PaxDb; Q8BV13; -.
DR PeptideAtlas; Q8BV13; -.
DR PRIDE; Q8BV13; -.
DR ProteomicsDB; 284035; -.
DR Antibodypedia; 20213; 108 antibodies from 20 providers.
DR DNASU; 26895; -.
DR Ensembl; ENSMUST00000027446; ENSMUSP00000027446; ENSMUSG00000026240.
DR Ensembl; ENSMUST00000121534; ENSMUSP00000113587; ENSMUSG00000026240.
DR GeneID; 26895; -.
DR KEGG; mmu:26895; -.
DR UCSC; uc007bvr.1; mouse.
DR CTD; 64708; -.
DR MGI; MGI:1349388; Cops7b.
DR VEuPathDB; HostDB:ENSMUSG00000026240; -.
DR eggNOG; KOG3250; Eukaryota.
DR GeneTree; ENSGT00940000157155; -.
DR HOGENOM; CLU_054426_1_0_1; -.
DR InParanoid; Q8BV13; -.
DR OMA; GTYKQFR; -.
DR OrthoDB; 1396757at2759; -.
DR PhylomeDB; Q8BV13; -.
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; 26895; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Cops7b; mouse.
DR PRO; PR:Q8BV13; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8BV13; protein.
DR Bgee; ENSMUSG00000026240; Expressed in undifferentiated genital tubercle and 276 other tissues.
DR ExpressionAtlas; Q8BV13; baseline and differential.
DR Genevisible; Q8BV13; MM.
DR GO; GO:0008180; C:COP9 signalosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; 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; IPR041481; CSN7_helixI.
DR InterPro; IPR027530; Csn7B.
DR InterPro; IPR000717; PCI_dom.
DR PANTHER; PTHR15350; PTHR15350; 1.
DR PANTHER; PTHR15350:SF8; PTHR15350:SF8; 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; Coiled coil; Cytoplasm; Nucleus; Reference proteome;
KW Signalosome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9H9Q2"
FT CHAIN 2..264
FT /note="COP9 signalosome complex subunit 7b"
FT /id="PRO_0000121000"
FT DOMAIN 2..159
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 223..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 194..237
FT /evidence="ECO:0000255"
FT COMPBIAS 236..252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9H9Q2"
FT CONFLICT 90
FT /note="V -> A (in Ref. 3; AAH12659)"
FT /evidence="ECO:0000305"
FT CONFLICT 97
FT /note="K -> N (in Ref. 1; AAC33904)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="V -> L (in Ref. 1; AAC33904)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 264 AA; 29689 MW; BD6088424F5537EA CRC64;
MAGEQKPSSN LLEQFILLAK GTSGSALTTL ISQVLEAPGV YVFGELLELA NVQELAEGAN
AAYLQLLNLF AYGTYPDYIA NKESLPELSV AQQNKLKHLT IVSLASRMKC IPYSVLLKDL
EMRNLRELED LIIEAVYTDI IQGKLDQRNQ LLEVDFCIGR DIRKKDINNI VKTLHEWCDG
CEAVLLGIEQ QVLRANQYKE NHHRTQQQVE AEVSNIKKTL KATASSSAQE MEQQLAEREC
PPHTEQRQPT KKMSKVKGLV SSRH
