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CSI1_YEAST
ID   CSI1_YEAST              Reviewed;         295 AA.
AC   Q04368; D6VZJ9;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Cop9 signalosome-interactor 1;
GN   Name=CSI1; OrderedLocusNames=YMR025W; ORFNames=YM9711.15;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169872;
RA   Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA   Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA   Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA   Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL   Nature 387:90-93(1997).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   FUNCTION OF THE COP9 SIGNALOSOME COMPLEX.
RX   PubMed=12186635; DOI=10.1186/1471-2156-3-15;
RA   Wee S., Hetfeld B., Dubiel W., Wolf D.A.;
RT   "Conservation of the COP9/signalosome in budding yeast.";
RL   BMC Genet. 3:15-15(2002).
RN   [4]
RP   INTERACTION WITH CSN9 AND CSN12, IDENTIFICATION IN THE COP9 SIGNALOSOME
RP   COMPLEX, AND FUNCTION OF THE COP9 SIGNALOSOME COMPLEX.
RX   PubMed=12446563; DOI=10.1093/embo-reports/kvf235;
RA   Maytal-Kivity V., Piran R., Pick E., Hofmann K., Glickman M.H.;
RT   "COP9 signalosome components play a role in the mating pheromone response
RT   of S. cerevisiae.";
RL   EMBO Rep. 3:1215-1221(2002).
RN   [5]
RP   INTERACTION WITH RRI1/CSN5, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=11805826; DOI=10.1038/415141a;
RA   Gavin A.-C., Boesche M., Krause R., Grandi P., Marzioch M., Bauer A.,
RA   Schultz J., Rick J.M., Michon A.-M., Cruciat C.-M., Remor M., Hoefert C.,
RA   Schelder M., Brajenovic M., Ruffner H., Merino A., Klein K., Hudak M.,
RA   Dickson D., Rudi T., Gnau V., Bauch A., Bastuck S., Huhse B., Leutwein C.,
RA   Heurtier M.-A., Copley R.R., Edelmann A., Querfurth E., Rybin V.,
RA   Drewes G., Raida M., Bouwmeester T., Bork P., Seraphin B., Kuster B.,
RA   Neubauer G., Superti-Furga G.;
RT   "Functional organization of the yeast proteome by systematic analysis of
RT   protein complexes.";
RL   Nature 415:141-147(2002).
RN   [6]
RP   INTERACTION WITH CSN9; CSN12 AND RPN5, AND IDENTIFICATION IN THE COP9
RP   SIGNALOSOME COMPLEX.
RX   PubMed=12672462; DOI=10.1016/s1357-2725(02)00378-3;
RA   Maytal-Kivity V., Pick E., Piran R., Hofmann K., Glickman M.H.;
RT   "The COP9 signalosome-like complex in S. cerevisiae and links to other PCI
RT   complexes.";
RL   Int. J. Biochem. Cell Biol. 35:706-715(2003).
CC   -!- FUNCTION: Component of the COP9 signalosome (CSN) complex that acts as
CC       an regulator of the ubiquitin (Ubl) conjugation pathway by mediating
CC       the deneddylation of the cullin subunit of SCF-type E3 ubiquitin-
CC       protein ligase complexes The CSN complex is involved in the regulation
CC       of the mating pheromone response. {ECO:0000269|PubMed:12186635,
CC       ECO:0000269|PubMed:12446563}.
CC   -!- SUBUNIT: Component of a COP9 signalosome-like (CSN) complex, composed
CC       of RRI1/CSN5, CSN9, RRI2/CSN10, PCI8/CSN11, CSN12 and CSI1. In the
CC       complex, it probably interacts directly with CSN9 and CSN12. Interacts
CC       also with RPN5. {ECO:0000269|PubMed:11805826,
CC       ECO:0000269|PubMed:12446563, ECO:0000269|PubMed:12672462}.
CC   -!- INTERACTION:
CC       Q04368; Q03981: CSN9; NbExp=5; IntAct=EBI-28044, EBI-33535;
CC       Q04368; Q12468: RRI1; NbExp=3; IntAct=EBI-28044, EBI-37511;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}.
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DR   EMBL; Z49211; CAA89128.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA09923.1; -; Genomic_DNA.
DR   PIR; S54027; S54027.
DR   RefSeq; NP_013738.1; NM_001182521.1.
DR   AlphaFoldDB; Q04368; -.
DR   BioGRID; 35197; 150.
DR   ComplexPortal; CPX-1894; COP9 signalosome complex.
DR   DIP; DIP-1810N; -.
DR   IntAct; Q04368; 7.
DR   MINT; Q04368; -.
DR   STRING; 4932.YMR025W; -.
DR   MaxQB; Q04368; -.
DR   PaxDb; Q04368; -.
DR   PRIDE; Q04368; -.
DR   EnsemblFungi; YMR025W_mRNA; YMR025W; YMR025W.
DR   GeneID; 855040; -.
DR   KEGG; sce:YMR025W; -.
DR   SGD; S000004627; CSI1.
DR   VEuPathDB; FungiDB:YMR025W; -.
DR   HOGENOM; CLU_082192_0_0_1; -.
DR   InParanoid; Q04368; -.
DR   OMA; GYKIENS; -.
DR   BioCyc; YEAST:G3O-32730-MON; -.
DR   PRO; PR:Q04368; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; Q04368; protein.
DR   GO; GO:0008180; C:COP9 signalosome; IDA:SGD.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR   GO; GO:0000754; P:adaptation of signaling pathway by response to pheromone involved in conjugation with cellular fusion; IMP:SGD.
DR   GO; GO:0000338; P:protein deneddylation; IMP:SGD.
PE   1: Evidence at protein level;
KW   Cytoplasm; Nucleus; Reference proteome; Signalosome.
FT   CHAIN           1..295
FT                   /note="Cop9 signalosome-interactor 1"
FT                   /id="PRO_0000079398"
SQ   SEQUENCE   295 AA;  34520 MW;  709BA7D999EBE4D6 CRC64;
     MDLLKFSSLA ISEINFLHES SFDSIDHSWF LLIGCKLDQD DEIYIPINGN EAESQWYIEK
     VIRIPMQEND KINQERLERR INLTKVTQKD ICILGILDLC QLEEDENITN KVTEKVLTQL
     TALALKYLIK YNVFRQHTSF QEAVNSLKGY KIENSVQIGA EIILDFLQDK VQIKDVNDRY
     QIPTPNNTVD PGFDEFQLID MKDKEINIQK YNNNTIRKLL EKINRMIIFL KNYDATDKPF
     SSTQDVILRK ISMLVTQLQR GGTSDMNYLL DNKINEIKLL EISCKQWEIS NMLKK
 
 
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