NOP16_YEAST
ID NOP16_YEAST Reviewed; 231 AA.
AC P40007; D3DLP8;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Nucleolar protein 16;
GN Name=NOP16; OrderedLocusNames=YER002W;
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=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP IDENTIFICATION IN THE PRE-66S RIBOSOMAL PARTICLE, FUNCTION, INTERACTION
RP WITH NOP7, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11583614; DOI=10.1016/s1097-2765(01)00344-6;
RA Harnpicharnchai P., Jakovljevic J., Horsey E., Miles T., Roman J., Rout M.,
RA Meagher D., Imai B., Guo Y., Brame C.J., Shabanowitz J., Hunt D.F.,
RA Woolford J.L. Jr.;
RT "Composition and functional characterization of yeast 66S ribosome assembly
RT intermediates.";
RL Mol. Cell 8:505-515(2001).
RN [5]
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 [6]
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 [7]
RP IDENTIFICATION IN THE PRE-66S RIBOSOMAL PARTICLE, INTERACTION WITH RRP1,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15100437; DOI=10.1261/rna.5255804;
RA Horsey E.W., Jakovljevic J., Miles T.D., Harnpicharnchai P.,
RA Woolford J.L. Jr.;
RT "Role of the yeast Rrp1 protein in the dynamics of pre-ribosome
RT maturation.";
RL RNA 10:813-827(2004).
RN [8]
RP IDENTIFICATION IN THE PRE-66S RIBOSOMAL PARTICLE, INTERACTION WITH RRP15,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15769876; DOI=10.1261/rna.7200205;
RA De Marchis M.L., Giorgi A., Schinina M.E., Bozzoni I., Fatica A.;
RT "Rrp15p, a novel component of pre-ribosomal particles required for 60S
RT ribosome subunit maturation.";
RL RNA 11:495-502(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176 AND SER-178, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, 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).
CC -!- FUNCTION: Involved in the biogenesis of the 60S ribosomal subunit.
CC {ECO:0000269|PubMed:11583614}.
CC -!- SUBUNIT: Component of the pre-66S ribosomal particle. Interacts with
CC NOP7, RRP1 and RRP15 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 2860 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the NOP16 family. {ECO:0000305}.
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DR EMBL; U18778; AAB64535.1; -; Genomic_DNA.
DR EMBL; AY557812; AAS56138.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07652.1; -; Genomic_DNA.
DR PIR; S50460; S50460.
DR RefSeq; NP_010917.3; NM_001178893.3.
DR PDB; 6C0F; EM; 3.70 A; 7=1-231.
DR PDB; 6CB1; EM; 4.60 A; 7=1-231.
DR PDB; 6ELZ; EM; 3.30 A; v=1-231.
DR PDB; 6EM1; EM; 3.60 A; v=1-231.
DR PDB; 6EM3; EM; 3.20 A; v=1-231.
DR PDB; 6EM4; EM; 4.10 A; v=1-231.
DR PDB; 6EM5; EM; 4.30 A; v=1-231.
DR PDB; 7OHP; EM; 3.90 A; v=1-231.
DR PDB; 7OHR; EM; 4.72 A; v=1-231.
DR PDB; 7OHS; EM; 4.38 A; v=1-231.
DR PDB; 7OHV; EM; 3.90 A; v=1-231.
DR PDB; 7OHW; EM; 3.50 A; v=1-231.
DR PDB; 7OHX; EM; 3.30 A; v=1-231.
DR PDBsum; 6C0F; -.
DR PDBsum; 6CB1; -.
DR PDBsum; 6ELZ; -.
DR PDBsum; 6EM1; -.
DR PDBsum; 6EM3; -.
DR PDBsum; 6EM4; -.
DR PDBsum; 6EM5; -.
DR PDBsum; 7OHP; -.
DR PDBsum; 7OHR; -.
DR PDBsum; 7OHS; -.
DR PDBsum; 7OHV; -.
DR PDBsum; 7OHW; -.
DR PDBsum; 7OHX; -.
DR AlphaFoldDB; P40007; -.
DR SMR; P40007; -.
DR BioGRID; 36732; 155.
DR DIP; DIP-6555N; -.
DR IntAct; P40007; 13.
DR MINT; P40007; -.
DR STRING; 4932.YER002W; -.
DR iPTMnet; P40007; -.
DR MaxQB; P40007; -.
DR PaxDb; P40007; -.
DR PRIDE; P40007; -.
DR EnsemblFungi; YER002W_mRNA; YER002W; YER002W.
DR GeneID; 856719; -.
DR KEGG; sce:YER002W; -.
DR SGD; S000000804; NOP16.
DR VEuPathDB; FungiDB:YER002W; -.
DR eggNOG; KOG4771; Eukaryota.
DR GeneTree; ENSGT00390000003426; -.
DR HOGENOM; CLU_078857_0_0_1; -.
DR InParanoid; P40007; -.
DR OMA; MQQTEAD; -.
DR BioCyc; YEAST:G3O-30190-MON; -.
DR PRO; PR:P40007; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P40007; protein.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IDA:SGD.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IMP:SGD.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR InterPro; IPR019002; Ribosome_biogenesis_Nop16.
DR PANTHER; PTHR13243; PTHR13243; 1.
DR Pfam; PF09420; Nop16; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; Ribosome biogenesis; rRNA processing.
FT CHAIN 1..231
FT /note="Nucleolar protein 16"
FT /id="PRO_0000202619"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 77..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..102
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:18407956"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT HELIX 4..11
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:6EM3"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 34..38
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 46..53
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 158..166
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 179..191
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 196..201
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 212..225
FT /evidence="ECO:0007829|PDB:6EM3"
SQ SEQUENCE 231 AA; 26901 MW; B1D27F0B817AADED CRC64;
MTSVRKRKMN RSSVGKATRR NKDKQRKINI QSNPIIAANW DYSLTMAQNY KKLGLRAKLQ
TPAGGKEADL SKVVKRIPLT KPVLDEDEDE DEGEDEQNDY NAATVELDEN EIPEGGARIQ
RDKNGDVVRV VYGKKKNFDA DEDVNEIKAR DTTEETEVVK KLEELASRPV IRKERSQSER
EEEWLEKLYK KHGDDYKKMF FDKKLNIYQQ SEGDLKRRLL RWKKRNGIAS K
