ID NOP13_YEAST Reviewed; 403 AA.
AC P53883; D6W110;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 2.
DT 27-MAR-2024, entry version 182.
DE RecName: Full=Nucleolar protein 13;
GN Name=NOP13; OrderedLocusNames=YNL175C; ORFNames=N1665;
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=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 296.
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=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 ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-105, 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-2, AND IDENTIFICATION BY MASS
RP 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 THR-105 AND SER-335, 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 -!- INTERACTION:
CC P53883; P37838: NOP4; NbExp=3; IntAct=EBI-29032, EBI-12122;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11452019,
CC ECO:0000269|PubMed:14562095}. Note=Also found in nucleoplasm.
CC -!- MISCELLANEOUS: Present with 3830 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z71451; CAA96066.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10376.2; -; Genomic_DNA.
DR PIR; S63130; S63130.
DR RefSeq; NP_014224.2; NM_001183013.2.
DR AlphaFoldDB; P53883; -.
DR SMR; P53883; -.
DR BioGRID; 35656; 219.
DR DIP; DIP-4331N; -.
DR IntAct; P53883; 84.
DR MINT; P53883; -.
DR STRING; 4932.YNL175C; -.
DR iPTMnet; P53883; -.
DR MaxQB; P53883; -.
DR PaxDb; 4932-YNL175C; -.
DR PeptideAtlas; P53883; -.
DR EnsemblFungi; YNL175C_mRNA; YNL175C; YNL175C.
DR GeneID; 855547; -.
DR KEGG; sce:YNL175C; -.
DR AGR; SGD:S000005119; -.
DR SGD; S000005119; NOP13.
DR VEuPathDB; FungiDB:YNL175C; -.
DR eggNOG; KOG4210; Eukaryota.
DR HOGENOM; CLU_027451_0_0_1; -.
DR InParanoid; P53883; -.
DR OMA; FQHCGEI; -.
DR OrthoDB; 53583at2759; -.
DR BioCyc; YEAST:G3O-33187-MONOMER; -.
DR Reactome; R-SCE-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-SCE-72649; Translation initiation complex formation.
DR Reactome; R-SCE-72702; Ribosomal scanning and start codon recognition.
DR BioGRID-ORCS; 855547; 1 hit in 10 CRISPR screens.
DR PRO; PR:P53883; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53883; Protein.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0030684; C:preribosome; IDA:SGD.
DR GO; GO:0003723; F:RNA binding; ISS:SGD.
DR CDD; cd12396; RRM1_Nop13p_fungi; 1.
DR CDD; cd12397; RRM2_Nop13p_fungi; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR034225; Nop13/Rnp24_RRM1.
DR InterPro; IPR034226; Nop13/Rnp24_RRM2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR23236; EUKARYOTIC TRANSLATION INITIATION FACTOR 4B/4H; 1.
DR PANTHER; PTHR23236:SF95; NUCLEOLAR PROTEIN 13; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 2.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW Acetylation; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:15665377"
FT CHAIN 2..403
FT /note="Nucleolar protein 13"
FT /id="PRO_0000082036"
FT DOMAIN 125..219
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 239..317
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 72..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..328
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:15665377"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:18407956"
FT MOD_RES 105
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 296
FT /note="A -> E (in Ref. 1; CAA96066)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 403 AA; 45609 MW; FB1A0FB46B13C201 CRC64;
MSETELSKED AVTKKDNEEQ VKKALLDPTK KRKAEDEIEI DLKSSIPLSK KQKRLLRRGK
VTLEELNAKY NIDPKSIEEY KEDAEKKKSG ASEKDAQGEE STINTPTGDE SGEVVKKKKK
DENKYGVWIG NLSFDTTKDD LVRFFIAKTK DNEDEKSRVT EQDITRLSMP RVAAKNSNAM
KNKGFCYMFF KNVEQMKAVL ELSESHLNGR NMLIKDSENY SGRPDKDDLV AMSKNPPSRI
LFVGNLSFDV TDDLLRKHFQ HCGDIVKIRM ATFEDSGKCK GFAFIDFKNE EGSTNALKDK
SCRKIAGRPL RMEYGEDRSK RQVRKKVENV SRNNSSSFDI SNNKGYDRAG QDNGSKPEYK
RSNANRRPPV DSNNRTKSSV ALATAQRGSA AIVPSQGKKV KFD
//
