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CGR1_YEAST
ID   CGR1_YEAST              Reviewed;         120 AA.
AC   P53188; D6VUA9;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=rRNA-processing protein CGR1;
DE   AltName: Full=Coiled-coil growth-regulated protein 1;
GN   Name=CGR1; OrderedLocusNames=YGL029W;
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=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(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   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [4]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=11116400; DOI=10.1007/s002840010180;
RA   Sun J., McFarland M., Boettner D., Panepinto J., Rhodes J.C., Askew D.S.;
RT   "Cgr1p, a novel nucleolar protein encoded by Saccharomyces cerevisiae orf
RT   YGL0292w.";
RL   Curr. Microbiol. 42:65-69(2001).
RN   [5]
RP   FUNCTION.
RX   PubMed=11932453; DOI=10.1099/00221287-148-4-1081;
RA   Moy T.I., Boettner D., Rhodes J.C., Silver P.A., Askew D.S.;
RT   "Identification of a role for Saccharomyces cerevisiae Cgr1p in pre-rRNA
RT   processing and 60S ribosome subunit synthesis.";
RL   Microbiology 148:1081-1090(2002).
RN   [6]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [7]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [8]
RP   INDUCTION.
RX   PubMed=15878181; DOI=10.1016/j.mrfmmm.2005.02.005;
RA   Caba E., Dickinson D.A., Warnes G.R., Aubrecht J.;
RT   "Differentiating mechanisms of toxicity using global gene expression
RT   analysis in Saccharomyces cerevisiae.";
RL   Mutat. Res. 575:34-46(2005).
RN   [9]
RP   FUNCTION.
RX   PubMed=16544271; DOI=10.1002/yea.1353;
RA   Wade C.H., Umbarger M.A., McAlear M.A.;
RT   "The budding yeast rRNA and ribosome biosynthesis (RRB) regulon contains
RT   over 200 genes.";
RL   Yeast 23:293-306(2006).
CC   -!- FUNCTION: Involved in nucleolar integrity and required for processing
CC       of the pre-rRNA for the 60S ribosome subunit.
CC       {ECO:0000269|PubMed:11116400, ECO:0000269|PubMed:11932453,
CC       ECO:0000269|PubMed:16544271}.
CC   -!- INTERACTION:
CC       P53188; P36049: EBP2; NbExp=3; IntAct=EBI-23731, EBI-6289;
CC       P53188; P40078: NSA2; NbExp=4; IntAct=EBI-23731, EBI-22681;
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11116400,
CC       ECO:0000269|PubMed:14562095}.
CC   -!- INDUCTION: In response to cytotoxic stress but not genotoxic stress.
CC       {ECO:0000269|PubMed:15878181}.
CC   -!- MISCELLANEOUS: Present with 2340 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the CGR1 family. {ECO:0000305}.
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DR   EMBL; Z72551; CAA96730.1; -; Genomic_DNA.
DR   EMBL; AY558480; AAS56806.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA08070.1; -; Genomic_DNA.
DR   PIR; S64031; S64031.
DR   RefSeq; NP_011486.1; NM_001180894.1.
DR   PDB; 3JCT; EM; 3.08 A; 5=1-120.
DR   PDB; 6FT6; EM; 3.90 A; 5=1-120.
DR   PDB; 6M62; EM; 3.20 A; 5=1-120.
DR   PDB; 6YLG; EM; 3.00 A; 5=1-120.
DR   PDB; 6YLH; EM; 3.10 A; 5=1-120.
DR   PDB; 7OH3; EM; 3.40 A; 5=1-120.
DR   PDB; 7OHQ; EM; 3.10 A; 5=1-120.
DR   PDBsum; 3JCT; -.
DR   PDBsum; 6FT6; -.
DR   PDBsum; 6M62; -.
DR   PDBsum; 6YLG; -.
DR   PDBsum; 6YLH; -.
DR   PDBsum; 7OH3; -.
DR   PDBsum; 7OHQ; -.
DR   AlphaFoldDB; P53188; -.
DR   SMR; P53188; -.
DR   BioGRID; 33217; 312.
DR   DIP; DIP-5450N; -.
DR   IntAct; P53188; 43.
DR   MINT; P53188; -.
DR   STRING; 4932.YGL029W; -.
DR   MaxQB; P53188; -.
DR   PaxDb; P53188; -.
DR   PRIDE; P53188; -.
DR   EnsemblFungi; YGL029W_mRNA; YGL029W; YGL029W.
DR   GeneID; 852854; -.
DR   KEGG; sce:YGL029W; -.
DR   SGD; S000002997; CGR1.
DR   VEuPathDB; FungiDB:YGL029W; -.
DR   eggNOG; ENOG502S7VB; Eukaryota.
DR   HOGENOM; CLU_125051_0_1_1; -.
DR   InParanoid; P53188; -.
DR   OMA; NGKQWHD; -.
DR   BioCyc; YEAST:G3O-30545-MON; -.
DR   PRO; PR:P53188; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P53188; protein.
DR   GO; GO:0005730; C:nucleolus; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0030687; C:preribosome, large subunit precursor; HDA:SGD.
DR   GO; GO:0042254; P:ribosome biogenesis; IMP:SGD.
DR   GO; GO:0006364; P:rRNA processing; IDA:SGD.
DR   InterPro; IPR005579; Cgr1-like.
DR   Pfam; PF03879; Cgr1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Coiled coil; Nucleus; Reference proteome;
KW   Ribosome biogenesis; rRNA processing.
FT   CHAIN           1..120
FT                   /note="rRNA-processing protein CGR1"
FT                   /id="PRO_0000202773"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          81..120
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          47..106
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        81..100
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   120 AA;  14417 MW;  E2750E786489E9CA CRC64;
     MVNETGESQK AAKGTPVSGK VWKAEKTPLR AKSRVVKNKK LTSWELKKQK RLEDKQFKER
     LKALKDEKEE ARQAKITMLK ERREKKEENE RYERLAAKMH AKKVERMRRR EKRNKALKER
 
 
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