NOP12_YEAST
ID NOP12_YEAST Reviewed; 459 AA.
AC Q08208; D6W225;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Nucleolar protein 12;
GN Name=NOP12; OrderedLocusNames=YOL041C;
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=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 [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, AND SUBCELLULAR LOCATION.
RX PubMed=11452019; DOI=10.1093/nar/29.14.2938;
RA Wu K., Wu P., Aris J.P.;
RT "Nucleolar protein Nop12p participates in synthesis of 25S rRNA in
RT Saccharomyces cerevisiae.";
RL Nucleic Acids Res. 29:2938-2949(2001).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70 AND SER-184, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70 AND SER-184, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70; THR-181 AND SER-184, 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: Involved in pre-25S rRNA processing.
CC {ECO:0000269|PubMed:11452019}.
CC -!- INTERACTION:
CC Q08208; P43586: LOC1; NbExp=3; IntAct=EBI-35895, EBI-22906;
CC Q08208; P38112: MAK5; NbExp=3; IntAct=EBI-35895, EBI-10394;
CC Q08208; P39744: NOC2; NbExp=3; IntAct=EBI-35895, EBI-29259;
CC Q08208; P37838: NOP4; NbExp=4; IntAct=EBI-35895, EBI-12122;
CC Q08208; P53131: PRP43; NbExp=2; IntAct=EBI-35895, EBI-505;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11452019,
CC ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 5910 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the RRM RBM34 family. {ECO:0000305}.
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DR EMBL; Z74783; CAA99043.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10741.1; -; Genomic_DNA.
DR PIR; S66726; S66726.
DR RefSeq; NP_014601.1; NM_001183295.1.
DR AlphaFoldDB; Q08208; -.
DR BioGRID; 34361; 459.
DR DIP; DIP-6505N; -.
DR IntAct; Q08208; 55.
DR MINT; Q08208; -.
DR STRING; 4932.YOL041C; -.
DR iPTMnet; Q08208; -.
DR MaxQB; Q08208; -.
DR PaxDb; Q08208; -.
DR PRIDE; Q08208; -.
DR EnsemblFungi; YOL041C_mRNA; YOL041C; YOL041C.
DR GeneID; 854116; -.
DR KEGG; sce:YOL041C; -.
DR SGD; S000005401; NOP12.
DR VEuPathDB; FungiDB:YOL041C; -.
DR eggNOG; KOG0118; Eukaryota.
DR HOGENOM; CLU_006468_0_0_1; -.
DR InParanoid; Q08208; -.
DR OMA; NAYAVYT; -.
DR BioCyc; YEAST:G3O-33455-MON; -.
DR PRO; PR:Q08208; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08208; protein.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0030684; C:preribosome; IDA:SGD.
DR GO; GO:0003723; F:RNA binding; ISS:SGD.
DR GO; GO:0019843; F:rRNA binding; IDA:GO_Central.
DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR CDD; cd12669; RRM1_Nop12p_like; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR034777; Nop12_RRM1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Nucleus; Phosphoprotein; Reference proteome; Ribosome biogenesis;
KW RNA-binding; rRNA processing.
FT CHAIN 1..459
FT /note="Nucleolar protein 12"
FT /id="PRO_0000081675"
FT DOMAIN 279..371
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 38..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 423..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..358
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..440
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 181
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
SQ SEQUENCE 459 AA; 51942 MW; 338F73B13DAE3282 CRC64;
MSSAIDNLFG NIDEKKIESS VDKLFSSSCG PINKLEVKSK TRTVLPDSKK RERAAEADQE
EKEASKPDVS DEQTEEVALP KVKKAKKSKR NDEDEDLEAR YYAKLLNEEA EAEDDKPTVT
KTDETSVPLT SAAKKVDFKE DELEKAERTV FIGNILSTVI TSKKVYKEFK KLFGTNPIAE
TEESGNEKEE ESSKKSDNNE FAIESIRFRS ISFDEALPRK VAFVQQKFHK SRDTINAYIV
YKNKSAVRKI CSNLNAVVFQ DHHLRVDSVA HPAPHDKKRS IFVGNLDFEE IEESLWKHFE
PCGDIEYVRI IRDSKTNMGK GFAYVQFKDL QSVNKALLLN EKPMKSQKQE DENTKKPTKK
ARKLRVSRCK NMKKGTTIGT GLDRNGLTDS QRTRAGRAKK ILGKADRATL GQEITIEGLR
AKKGEGSTHL KKKKQRSATG RVTKRSIAFK KAQAEKSKK
