ID   NOP4_YEAST              Reviewed;         685 AA.
AC   P37838; D6W3X0;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 191.
DE   RecName: Full=Nucleolar protein 4;
DE   AltName: Full=Nucleolar protein NOP77;
GN   Name=NOP4; Synonyms=NOP77; OrderedLocusNames=YPL043W;
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].
RX   PubMed=8039505; DOI=10.1002/j.1460-2075.1994.tb06611.x;
RA   Sun C., Woolford J.L. Jr.;
RT   "The yeast NOP4 gene product is an essential nucleolar protein required for
RT   pre-rRNA processing and accumulation of 60S ribosomal subunits.";
RL   EMBO J. 13:3127-3135(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8039506; DOI=10.1002/j.1460-2075.1994.tb06612.x;
RA   Berges T., Petfalski E., Tollervey D., Hurt E.C.;
RT   "Synthetic lethality with fibrillarin identifies NOP77p, a nucleolar
RT   protein required for pre-rRNA processing and modification.";
RL   EMBO J. 13:3136-3148(1994).
RN   [3]
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   [4]
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   [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 THR-379, AND IDENTIFICATION BY
RP   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 SER-247, 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   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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, AND IDENTIFICATION BY
RP   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: Required for 60S ribosomal subunit synthesis. Probably
CC       involved in the processing of 27S rRNA to produce mature 25S rRNA.
CC   -!- SUBUNIT: Interacts with NOP1.
CC   -!- INTERACTION:
CC       P37838; P38779: CIC1; NbExp=5; IntAct=EBI-12122, EBI-24538;
CC       P37838; Q12389: DBP10; NbExp=3; IntAct=EBI-12122, EBI-5644;
CC       P37838; P32892: DRS1; NbExp=4; IntAct=EBI-12122, EBI-6170;
CC       P37838; P36049: EBP2; NbExp=5; IntAct=EBI-12122, EBI-6289;
CC       P37838; Q03532: HAS1; NbExp=4; IntAct=EBI-12122, EBI-8170;
CC       P37838; P43586: LOC1; NbExp=4; IntAct=EBI-12122, EBI-22906;
CC       P37838; Q12176: MAK21; NbExp=6; IntAct=EBI-12122, EBI-10944;
CC       P37838; P38112: MAK5; NbExp=4; IntAct=EBI-12122, EBI-10394;
CC       P37838; P39744: NOC2; NbExp=4; IntAct=EBI-12122, EBI-29259;
CC       P37838; Q02892: NOG1; NbExp=3; IntAct=EBI-12122, EBI-12105;
CC       P37838; Q08208: NOP12; NbExp=4; IntAct=EBI-12122, EBI-35895;
CC       P37838; P53883: NOP13; NbExp=3; IntAct=EBI-12122, EBI-29032;
CC       P37838; P37838: NOP4; NbExp=3; IntAct=EBI-12122, EBI-12122;
CC       P37838; P40010: NUG1; NbExp=3; IntAct=EBI-12122, EBI-22449;
CC       P37838; P53131: PRP43; NbExp=3; IntAct=EBI-12122, EBI-505;
CC       P37838; Q12754: RRP12; NbExp=4; IntAct=EBI-12122, EBI-30678;
CC       P37838; P36080: RRP14; NbExp=3; IntAct=EBI-12122, EBI-26762;
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus.
CC   -!- MISCELLANEOUS: Present with 4990 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; U02598; AAA20590.1; -; Genomic_DNA.
DR   EMBL; X76245; CAA53824.1; -; Genomic_DNA.
DR   EMBL; U44030; AAB68177.1; -; Genomic_DNA.
DR   EMBL; BK006949; DAA11386.1; -; Genomic_DNA.
DR   PIR; S46365; S46365.
DR   RefSeq; NP_015282.1; NM_001183857.1.
DR   AlphaFoldDB; P37838; -.
DR   SMR; P37838; -.
DR   BioGRID; 36136; 203.
DR   DIP; DIP-3891N; -.
DR   IntAct; P37838; 76.
DR   MINT; P37838; -.
DR   STRING; 4932.YPL043W; -.
DR   iPTMnet; P37838; -.
DR   MaxQB; P37838; -.
DR   PaxDb; P37838; -.
DR   PRIDE; P37838; -.
DR   EnsemblFungi; YPL043W_mRNA; YPL043W; YPL043W.
DR   GeneID; 856063; -.
DR   KEGG; sce:YPL043W; -.
DR   SGD; S000005964; NOP4.
DR   VEuPathDB; FungiDB:YPL043W; -.
DR   eggNOG; KOG0127; Eukaryota.
DR   GeneTree; ENSGT00940000175222; -.
DR   HOGENOM; CLU_011608_3_0_1; -.
DR   InParanoid; P37838; -.
DR   OMA; RNLPWSV; -.
DR   BioCyc; YEAST:G3O-33957-MON; -.
DR   PRO; PR:P37838; -.
DR   Proteomes; UP000002311; Chromosome XVI.
DR   RNAct; P37838; protein.
DR   GO; GO:0005730; C:nucleolus; HDA:SGD.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0070180; F:large ribosomal subunit rRNA binding; IDA:GO_Central.
DR   GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR   GO; GO:0003723; F:RNA binding; IBA: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   GO; GO:0042273; P:ribosomal large subunit biogenesis; IMP:SGD.
DR   CDD; cd12675; RRM2_Nop4p; 1.
DR   CDD; cd12676; RRM3_Nop4p; 1.
DR   CDD; cd12677; RRM4_Nop4p; 1.
DR   Gene3D; 3.30.70.330; -; 4.
DR   InterPro; IPR034806; Nop4_RRM2.
DR   InterPro; IPR034809; Nop4_RRM4.
DR   InterPro; IPR034808; Nop4p_RRM3.
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; 3.
DR   SMART; SM00360; RRM; 4.
DR   SUPFAM; SSF54928; SSF54928; 3.
DR   PROSITE; PS50102; RRM; 4.
PE   1: Evidence at protein level;
KW   Nucleus; Phosphoprotein; Reference proteome; Repeat; Ribosome biogenesis;
KW   RNA-binding; rRNA processing.
FT   CHAIN           1..685
FT                   /note="Nucleolar protein 4"
FT                   /id="PRO_0000081677"
FT   DOMAIN          26..103
FT                   /note="RRM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          147..225
FT                   /note="RRM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          290..383
FT                   /note="RRM 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          462..612
FT                   /note="RRM 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          106..142
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          231..285
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          622..685
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        244..267
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        268..285
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        622..674
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         247
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         379
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:15665377"
FT   VARIANT         308
FT                   /note="P -> A"
SQ   SEQUENCE   685 AA;  77825 MW;  61261815EA3DEE5C CRC64;
     MEETIENVEV PSSNVSKQND DGLDMKTLFV RSIPQDVTDE QLADFFSNFA PIKHAVVVKD
     TNKRSRGFGF VSFAVEDDTK EALAKARKTK FNGHILRVDI AKRRDRSKKT SEVVEKSTPE
     SSEKITGQNN EDEDDADGED SMLKGKPKLI IRNMPWSCRD PVKLKKIFGR YGTVVEATIP
     RKRDGKLCGF AFVTMKKISN CRIALENTKD LKIDGRKVAV DFAVQKNRWE DYKKAQPEMN
     DKDDNESGNE DAEENHDDEE DENEEEDRQV DQASKNKESK RKAQNKREDF SVFVRNVPYD
     ATEESLAPHF SKFGSVKYAL PVIDKSTGLA KGTAFVAFKD QYTYNECIKN APAAGSTSLL
     IGDDVMPEYV YEGRVLSITP TLVREDAGRM AEKNAAKRKE ALGKAPGEKD RRNLYLLNEG
     RVVEGSKMAD LLTNTDMEIR EKSYKLRVEQ LKKNPSLHLS MTRLAIRNLP RAMNDKALKA
     LARKAVVEFA TEVKNKERHP LSKEEIIRST KEKYKFMGPD EIEAQKKKDK KSGVVKQAKV
     IMEVKGSTAG RSRGYGFVEF RDHKNALMGL RWLNCHAVTS DEILEGLNDD EKKQVDNDLG
     KGRRLCVEFA IENSNVVKRR REQLKQARTK RTRPDNEDTG DVGESENKKP KKEEATTPTN
     PDDKKMGDDI KRIIGFKRKR KHAKK