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RRP36_YEAST
ID   RRP36_YEAST             Reviewed;         300 AA.
AC   Q12481; D6W2Y5;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 148.
DE   RecName: Full=rRNA biogenesis protein RRP36;
DE   AltName: Full=Ribosomal RNA-processing protein 36;
GN   Name=RRP36; OrderedLocusNames=YOR287C;
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 [GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=8896271;
RX   DOI=10.1002/(sici)1097-0061(199609)12:10b%3c1059::aid-yea994%3e3.0.co;2-7;
RA   Cheret G., Bernardi A., Sor F.J.;
RT   "DNA sequence analysis of the VPH1-SNF2 region on chromosome XV of
RT   Saccharomyces cerevisiae.";
RL   Yeast 12:1059-1064(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169874;
RA   Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA   Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA   Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA   Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA   Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA   Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA   Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA   Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA   Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA   Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA   Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA   Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA   Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA   Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA   Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA   Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL   Nature 387:98-102(1997).
RN   [3]
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   [4]
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).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-41 AND SER-42, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-41 AND SER-42, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-41 AND SER-42, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
RN   [8]
RP   SUBCELLULAR LOCATION, ASSOCIATION WITH NASCENT PRE-RIBOSOMES, INTERACTION
RP   WITH CKA1; CKA2; CKB1; CKB2; PWP2; UTP15; UTP17 AND UTP22, AND FUNCTION.
RX   PubMed=20038530; DOI=10.1128/mcb.00999-09;
RA   Gerus M., Bonnart C., Caizergues-Ferrer M., Henry Y., Henras A.K.;
RT   "Evolutionarily conserved function of RRP36 in early cleavages of the pre-
RT   rRNA and production of the 40S ribosomal subunit.";
RL   Mol. Cell. Biol. 30:1130-1144(2010).
CC   -!- FUNCTION: Component of the 90S pre-ribosome involved in the maturation
CC       of rRNAs. Required for early cleavages of the pre-RNAs in the 40S
CC       ribosomal subunit maturation pathway. {ECO:0000269|PubMed:16544271,
CC       ECO:0000269|PubMed:20038530}.
CC   -!- SUBUNIT: Associates with 90S and pre-40S pre-ribosomal particles.
CC       Interacts with CKA1, CKA2, CKB1, CKB2, PWP2, UTP15, UTP17 and UTP22.
CC       {ECO:0000269|PubMed:20038530}.
CC   -!- INTERACTION:
CC       Q12481; P15790: CKA1; NbExp=3; IntAct=EBI-31770, EBI-9533;
CC       Q12481; P38333: ENP1; NbExp=2; IntAct=EBI-31770, EBI-6482;
CC       Q12481; Q03532: HAS1; NbExp=2; IntAct=EBI-31770, EBI-8170;
CC       Q12481; P25586: KRR1; NbExp=3; IntAct=EBI-31770, EBI-21773;
CC       Q12481; Q12136: SAS10; NbExp=2; IntAct=EBI-31770, EBI-36084;
CC       Q12481; P53254: UTP22; NbExp=2; IntAct=EBI-31770, EBI-1878;
CC       Q12481; P40498: UTP25; NbExp=2; IntAct=EBI-31770, EBI-25113;
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:20038530}.
CC   -!- SIMILARITY: Belongs to the RRP36 family. {ECO:0000305}.
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DR   EMBL; X89633; CAA61790.1; -; Genomic_DNA.
DR   EMBL; Z75195; CAA99514.1; -; Genomic_DNA.
DR   EMBL; BK006948; DAA11051.1; -; Genomic_DNA.
DR   PIR; S67189; S67189.
DR   RefSeq; NP_014930.1; NM_001183706.1.
DR   AlphaFoldDB; Q12481; -.
DR   SMR; Q12481; -.
DR   BioGRID; 34674; 35.
DR   ComplexPortal; CPX-1604; Small ribosomal subunit processome, variant 1.
DR   ComplexPortal; CPX-1607; Small ribosomal subunit processome, variant 2.
DR   ComplexPortal; CPX-1608; Small ribosomal subunit processome, variant 3.
DR   IntAct; Q12481; 35.
DR   MINT; Q12481; -.
DR   STRING; 4932.YOR287C; -.
DR   iPTMnet; Q12481; -.
DR   MaxQB; Q12481; -.
DR   PaxDb; Q12481; -.
DR   PRIDE; Q12481; -.
DR   EnsemblFungi; YOR287C_mRNA; YOR287C; YOR287C.
DR   GeneID; 854461; -.
DR   KEGG; sce:YOR287C; -.
DR   SGD; S000005813; RRP36.
DR   VEuPathDB; FungiDB:YOR287C; -.
DR   eggNOG; KOG3190; Eukaryota.
DR   GeneTree; ENSGT00530000064271; -.
DR   HOGENOM; CLU_048802_3_0_1; -.
DR   InParanoid; Q12481; -.
DR   OMA; HRTSKHA; -.
DR   BioCyc; YEAST:G3O-33773-MON; -.
DR   Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR   PRO; PR:Q12481; -.
DR   Proteomes; UP000002311; Chromosome XV.
DR   RNAct; Q12481; protein.
DR   GO; GO:0030686; C:90S preribosome; IDA:SGD.
DR   GO; GO:0005730; C:nucleolus; IDA:SGD.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0032040; C:small-subunit processome; IPI:ComplexPortal.
DR   GO; GO:0000469; P:cleavage involved in rRNA processing; IMP:SGD.
DR   GO; GO:0030490; P:maturation of SSU-rRNA; IC:ComplexPortal.
DR   GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR   GO; GO:0042274; P:ribosomal small subunit biogenesis; IMP:SGD.
DR   InterPro; IPR009292; RRP36.
DR   PANTHER; PTHR21738; PTHR21738; 1.
DR   Pfam; PF06102; RRP36; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Nucleus; Phosphoprotein; Reference proteome;
KW   Ribonucleoprotein; Ribosome biogenesis; rRNA processing.
FT   CHAIN           1..300
FT                   /note="rRNA biogenesis protein RRP36"
FT                   /id="PRO_0000268165"
FT   REGION          33..151
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          184..248
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        33..83
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        84..105
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        106..139
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         14
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT   MOD_RES         41
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT   MOD_RES         42
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   300 AA;  36125 MW;  DA075857261E1490 CRC64;
     MSYYFKNLKP DLNSDVEEDD GNLLESIMAN KSKREIDEQE SSDDELKTLS FGSLKKAETV
     IDEEDFKDTK PVHKKPITTT YREESFDEDE DSEDQSDEDA GFFEEDSEDE THHGQKVPKK
     KSKHAPVEQS SKKRVPRVRN IPGLEIPRNK RSNLYQDIRF DKSTGKALDS SIIRKRYQFL
     DEYREKEIDE LQKLLQERKF LSKIDQGERE EMEQRLKSMK SRLQSMKNKD LEREILKEYE
     NDMNKNNNTR YHLKKSEKRK VVQKWKFDHM KAKQREKVME RKRKKRLGKE FKQFEFHNRR
 
 
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