RRP12_YEAST
ID RRP12_YEAST Reviewed; 1228 AA.
AC Q12754; D6W400; Q7LH12;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Ribosomal RNA-processing protein 12;
GN Name=RRP12; OrderedLocusNames=YPL012W;
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=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 SUBCELLULAR LOCATION.
RX PubMed=12628929; DOI=10.1093/emboj/cdg121;
RA Schaefer T., Strauss D., Petfalski E., Tollervey D., Hurt E.;
RT "The path from nucleolar 90S to cytoplasmic 40S pre-ribosomes.";
RL EMBO J. 22:1370-1380(2003).
RN [4]
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 [5]
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 [6]
RP FUNCTION, INTERACTION WITH GSP1, AND SUBCELLULAR LOCATION.
RX PubMed=14729571; DOI=10.1101/gad.285604;
RA Oeffinger M., Dlakic M., Tollervey D.;
RT "A pre-ribosome-associated HEAT-repeat protein is required for export of
RT both ribosomal subunits.";
RL Genes Dev. 18:196-209(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1067, AND IDENTIFICATION BY
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1067, AND IDENTIFICATION BY
RP 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1059 AND SER-1067, 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).
CC -!- FUNCTION: In association with GSP1, required for nuclear export of both
CC pre-40S and pre-60S ribosomal subunits. Required for the late
CC maturation of the 18S and 5.8S rRNA of the pre-40S ribosomes and for
CC maturation of the 25S and 5.8S rRNA of the pre-60S ribosomes.
CC {ECO:0000269|PubMed:14729571}.
CC -!- SUBUNIT: Interacts with GSP1. {ECO:0000269|PubMed:14729571}.
CC -!- INTERACTION:
CC Q12754; P36049: EBP2; NbExp=3; IntAct=EBI-30678, EBI-6289;
CC Q12754; P43586: LOC1; NbExp=3; IntAct=EBI-30678, EBI-22906;
CC Q12754; Q12176: MAK21; NbExp=3; IntAct=EBI-30678, EBI-10944;
CC Q12754; P37838: NOP4; NbExp=4; IntAct=EBI-30678, EBI-12122;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12628929,
CC ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14729571}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:12628929, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:14729571}.
CC -!- MISCELLANEOUS: Present with 8170 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the RRP12 family. {ECO:0000305}.
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DR EMBL; U33335; AAB68093.1; -; Genomic_DNA.
DR EMBL; Z71255; CAA95029.1; -; Genomic_DNA.
DR EMBL; Z48483; CAA88374.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11416.1; -; Genomic_DNA.
DR PIR; S59681; S59681.
DR RefSeq; NP_015313.1; NM_001183826.1.
DR AlphaFoldDB; Q12754; -.
DR BioGRID; 36165; 183.
DR DIP; DIP-6497N; -.
DR IntAct; Q12754; 62.
DR MINT; Q12754; -.
DR STRING; 4932.YPL012W; -.
DR iPTMnet; Q12754; -.
DR MaxQB; Q12754; -.
DR PaxDb; Q12754; -.
DR PRIDE; Q12754; -.
DR EnsemblFungi; YPL012W_mRNA; YPL012W; YPL012W.
DR GeneID; 856095; -.
DR KEGG; sce:YPL012W; -.
DR SGD; S000005933; RRP12.
DR VEuPathDB; FungiDB:YPL012W; -.
DR eggNOG; KOG1248; Eukaryota.
DR GeneTree; ENSGT00390000013106; -.
DR HOGENOM; CLU_003753_1_0_1; -.
DR InParanoid; Q12754; -.
DR OMA; VLVRTNC; -.
DR BioCyc; YEAST:G3O-33931-MON; -.
DR PRO; PR:Q12754; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q12754; protein.
DR GO; GO:0030686; C:90S preribosome; HDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005730; C:nucleolus; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0030688; C:preribosome, small subunit precursor; IDA:GO_Central.
DR GO; GO:0005840; C:ribosome; TAS:SGD.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:GO_Central.
DR GO; GO:0042254; P:ribosome biogenesis; TAS:SGD.
DR GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR012978; Uncharacterised_NUC173.
DR Pfam; PF08161; NUC173; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Phosphoprotein; Reference proteome;
KW Ribosome biogenesis; RNA-binding.
FT CHAIN 1..1228
FT /note="Ribosomal RNA-processing protein 12"
FT /id="PRO_0000270563"
FT REGION 1168..1228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1210..1228
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1059
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1067
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
SQ SEQUENCE 1228 AA; 137509 MW; 92333BCD53CB095F CRC64;
MDQDKVAFLL ELEDKLAKIR SQVNSKLENQ KHIAIILTAV EENIAGQATN DVSKNIVNYI
ISFMSLLDQA VDPSTHEIKD IQLASSSTYL LDLIFHYSPK VLLRSKFSEI LTKIAPCITA
EKANAPLIRA AIGCLESLLI AQDAQAWNNT YDLNVTPKRG LQGILELSLD VRPKVRKRAL
DAVHAVLLNP PVAPTAEHVA AVFVADFCDK QLAGILNDLS NLSNKQLKAQ KTKEDINASV
MRSLRLITSV VSTGQWPSSQ IEPLCDVLLG VTKSSEQYLV SASFECFESM FKTMAETTIS
SGLAENKYLR VLDTIFALKP SNVDTLLTKS WIAVVIKGMS TYATHQPLKA LRKIPGVFHI
MCTYLASETP EVYQAASQCL ISILSESVKD DLLLYTPSVD EKVFKNVDEI ISQIAKTFID
FLSIRYSHCS REILKILVAA FNKFRYRSNP HFLKSLKIVD TWRVNEEQFM DLRNEIELVI
GASISAMGPE MILAEAPLNL DNPSSERPGR AWLLPLIRDY TKNANLATFQ NELAPYIKSF
QSKFDKVPEE SIQLRVFQTI VDQIWSTLPR FCELPMDLRE SFTDEFASEL SSLLYSEVEL
RTTICHALKV LAESNVSYAE ESSSHNVLLL QRFPISEAQK NIEYLSTKST NLLAVLFNVY
TQTTPNARSY ILETIDQYLK ITSKEDLEKT FNNVCGLLKN SMNEESSGNV NKEKKKPQLT
ATLLDLIICM ITYLPVSSYS ALFSMFSLTV NSADALIQKR AYRIITKLSE LKSGSTAVAQ
FISDIENVMV DSASSVQTSA KAARLTAIKT IVELLPLDHL DFIVRTVAEV ILSTKDVNEK
SRETAFDTLI CMGRKMNEPN GIIKLFQIPG YDPTTPDQSS SISEFFKIIS AGLIGESQHM
VSSSITGYAC LVFEFKNELD SGILMDIYDT IELYLTSNSR EIVKSAIGFT KVCVLGLPEE
LMRPKVPELL LKLLRWSHEH TGHFKAKVKH IIERLIRRFG YDYIEANFPE EDRRLLTNIR
KMRNRNKRKD EEVTTGVSDV AATKGSRFMS AFDEAVYGSD EENDNGSDQE ENVAGGKMKN
GAKQFIVESG DNPLDLLDSQ TLAHISSTRP KKFNKNQNRA RFNDDAFNFD SEGKLVVKGQ
PKPSTNVDDP LSAVTSGINA YLEAVKSGPV RGQRNKLKFR KNGKDSDEFG DDDDGEKDSR
LMRGRVNQGN KIGKHNKKGP KFKSRKKL
