RRB1_YEAST
ID RRB1_YEAST Reviewed; 511 AA.
AC Q04225; D6VZV4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Ribosome assembly protein RRB1;
GN Name=RRB1; OrderedLocusNames=YMR131C; ORFNames=YM9553.07C;
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 CHARACTERIZATION.
RX PubMed=11728313; DOI=10.1016/s0960-9822(01)00584-x;
RA Schaper S., Fromont-Racine M., Linder P., de la Cruz J., Namane A.,
RA Yaniv M.;
RT "A yeast homolog of chromatin assembly factor 1 is involved in early
RT ribosome assembly.";
RL Curr. Biol. 11:1885-1890(2001).
RN [4]
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5, AND IDENTIFICATION BY MASS
RP 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).
CC -!- FUNCTION: Involved in regulation of L3 expression and stability and
CC plays a role in early 60S ribosomal subunit assembly. May be required
CC for proper assembly of pre-ribosomal particles during early ribosome
CC biogenesis, presumably by targeting L3 onto the 35S precursor rRNA.
CC -!- SUBUNIT: Associates with ribosomal protein L3.
CC -!- SUBCELLULAR LOCATION: Nucleus.
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DR EMBL; Z48622; CAA88556.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10028.1; -; Genomic_DNA.
DR PIR; S53061; S53061.
DR RefSeq; NP_013850.1; NM_001182632.1.
DR AlphaFoldDB; Q04225; -.
DR SMR; Q04225; -.
DR BioGRID; 35308; 116.
DR DIP; DIP-6263N; -.
DR IntAct; Q04225; 8.
DR MINT; Q04225; -.
DR STRING; 4932.YMR131C; -.
DR iPTMnet; Q04225; -.
DR MaxQB; Q04225; -.
DR PaxDb; Q04225; -.
DR PRIDE; Q04225; -.
DR EnsemblFungi; YMR131C_mRNA; YMR131C; YMR131C.
DR GeneID; 855161; -.
DR KEGG; sce:YMR131C; -.
DR SGD; S000004738; RRB1.
DR VEuPathDB; FungiDB:YMR131C; -.
DR eggNOG; KOG0302; Eukaryota.
DR GeneTree; ENSGT00550000075124; -.
DR HOGENOM; CLU_025272_1_1_1; -.
DR InParanoid; Q04225; -.
DR OMA; DWSPLQP; -.
DR BioCyc; YEAST:G3O-32824-MON; -.
DR PRO; PR:Q04225; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q04225; protein.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0051082; F:unfolded protein binding; IDA:SGD.
DR GO; GO:0042254; P:ribosome biogenesis; IMP:SGD.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR022052; Histone-bd_RBBP4_N.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF12265; CAF1C_H4-bd; 1.
DR Pfam; PF00400; WD40; 2.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Ribosome biogenesis;
KW rRNA processing; WD repeat.
FT CHAIN 1..511
FT /note="Ribosome assembly protein RRB1"
FT /id="PRO_0000051202"
FT REPEAT 319..359
FT /note="WD 1"
FT REPEAT 364..404
FT /note="WD 2"
FT REPEAT 415..455
FT /note="WD 3"
FT REPEAT 477..510
FT /note="WD 4"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..65
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..201
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 511 AA; 57261 MW; 1D18CE3C60BAFF30 CRC64;
MSKRSIEVNE EQDRVVSAKT ESHSVPAIPA SEEQDAPKND LEEQLSDEFD SDGEIIEIDG
DDEINDEDDL RKKQEEAETL VQKDQSEGNK EKIQELYLPH MSRPLGPDEV LEADPTVYEM
LHNVNMPWPC LTLDVIPDTL GSERRNYPQS ILLTTATQSS RKKENELMVL ALSNLAKTLL
KDDNEGEDDE EDDEDDVDPV IENENIPLRD TTNRLKVSPF AISNQEVLTA TMSENGDVYI
YNLAPQSKAF STPGYQIPKS AKRPIHTVKN HGNVEGYGLD WSPLIKTGAL LSGDCSGQIY
FTQRHTSRWV TDKQPFTVSN NKSIEDIQWS RTESTVFATA GCDGYIRIWD TRSKKHKPAI
SVKASNTDVN VISWSDKIGY LLASGDDNGT WGVWDLRQFT PSNADAVQPV AQYDFHKGAI
TSIAFNPLDE SIVAVGSEDN TVTLWDLSVE ADDEEIKQQA AETKELQEIP PQLLFVHWQK
EVKDVKWHKQ IPGCLVSTGT DGLNVWKTIS V
