NOP10_YEAST
ID NOP10_YEAST Reviewed; 58 AA.
AC Q6Q547; D3DL22;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=H/ACA ribonucleoprotein complex subunit NOP10;
DE AltName: Full=Nucleolar protein 10;
DE AltName: Full=Nucleolar protein family A member 3;
DE AltName: Full=snoRNP protein NOP10;
GN Name=NOP10; OrderedLocusNames=YHR072W-A;
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=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
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 PROTEIN SEQUENCE OF 1-10, FUNCTION, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION IN H/ACA SNORNP COMPLEXES.
RX PubMed=9843512; DOI=10.1093/emboj/17.23.7078;
RA Henras A., Henry Y., Bousquet-Antonelli C., Noaillac-Depeyre J.,
RA Gelugne J.-P., Caizergues-Ferrer M.;
RT "Nhp2p and Nop10p are essential for the function of H/ACA snoRNPs.";
RL EMBO J. 17:7078-7090(1998).
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 CHARACTERIZATION OF THE H/ACA SNORNP COMPLEX.
RX PubMed=15388873; DOI=10.1261/rna.7770604;
RA Henras A.K., Capeyrou R., Henry Y., Caizergues-Ferrer M.;
RT "Cbf5p, the putative pseudouridine synthase of H/ACA-type snoRNPs, can form
RT a complex with Gar1p and Nop10p in absence of Nhp2p and box H/ACA
RT snoRNAs.";
RL RNA 10:1704-1712(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND IDENTIFICATION BY
RP 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 [8]
RP FUNCTION, AND IDENTIFICATION IN THE H/ACA SNORNP COMPLEX.
RX PubMed=21131909; DOI=10.1038/emboj.2010.316;
RA Wu G., Xiao M., Yang C., Yu Y.T.;
RT "U2 snRNA is inducibly pseudouridylated at novel sites by Pus7p and snR81
RT RNP.";
RL EMBO J. 30:79-89(2011).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [10]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-28, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- FUNCTION: Non-catalytic component of the H/ACA small nucleolar
CC ribonucleoprotein (H/ACA snoRNP), which catalyzes pseudouridylation of
CC rRNA and is required for ribosome biogenesis (PubMed:9843512). This
CC involves the isomerization of uridine such that the ribose is
CC subsequently attached to C5, instead of the normal N1 (PubMed:9843512).
CC Pseudouridine ('psi') residues may serve to stabilize the conformation
CC of rRNAs (PubMed:9843512). The H/ACA snoRNP complex also mediates
CC pseudouridylation of other types of RNAs (PubMed:21131909). The H/ACA
CC snoRNP complex mediates pseudouridylation at position 93 in U2 snRNA
CC (PubMed:21131909). Essential for growth (PubMed:9843512).
CC {ECO:0000269|PubMed:21131909, ECO:0000269|PubMed:9843512}.
CC -!- SUBUNIT: Component of the small nucleolar ribonucleoprotein particles
CC containing H/ACA-type snoRNAs (H/ACA snoRNPs) (PubMed:9843512,
CC PubMed:21131909). The protein component of the H/ACA snoRNP contains
CC CBF5, GAR1, NHP2 and NOP10 (PubMed:9843512, PubMed:21131909). The
CC complex contains a stable core composed of CBF5 and NOP10, to which
CC GAR1 and NHP2 subsequently bind (PubMed:9843512).
CC {ECO:0000269|PubMed:21131909, ECO:0000269|PubMed:9843512}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:9843512}.
CC -!- SIMILARITY: Belongs to the NOP10 family. {ECO:0000305}.
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DR EMBL; U10556; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY558548; AAS56874.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06766.1; -; Genomic_DNA.
DR RefSeq; NP_058135.1; NM_001184438.1.
DR PDB; 1Y2Y; NMR; -; A=1-58.
DR PDB; 2AQA; NMR; -; A=2-58.
DR PDB; 3U28; X-ray; 1.90 A; B=1-58.
DR PDB; 3UAI; X-ray; 3.06 A; B=1-58.
DR PDBsum; 1Y2Y; -.
DR PDBsum; 2AQA; -.
DR PDBsum; 3U28; -.
DR PDBsum; 3UAI; -.
DR AlphaFoldDB; Q6Q547; -.
DR BMRB; Q6Q547; -.
DR SMR; Q6Q547; -.
DR BioGRID; 36506; 134.
DR ComplexPortal; CPX-737; Box H/ACA ribonucleoprotein complex.
DR DIP; DIP-5845N; -.
DR IntAct; Q6Q547; 12.
DR MINT; Q6Q547; -.
DR STRING; 4932.YHR072W-A; -.
DR iPTMnet; Q6Q547; -.
DR MaxQB; Q6Q547; -.
DR PaxDb; Q6Q547; -.
DR PRIDE; Q6Q547; -.
DR EnsemblFungi; YHR072W-A_mRNA; YHR072W-A; YHR072W-A.
DR GeneID; 856471; -.
DR KEGG; sce:YHR072W-A; -.
DR SGD; S000007455; NOP10.
DR VEuPathDB; FungiDB:YHR072W-A; -.
DR eggNOG; KOG3503; Eukaryota.
DR GeneTree; ENSGT00390000012563; -.
DR HOGENOM; CLU_184680_1_0_1; -.
DR InParanoid; Q6Q547; -.
DR OMA; MYTLGPD; -.
DR BioCyc; MetaCyc:G3O-31263-MON; -.
DR BioCyc; YEAST:G3O-31263-MON; -.
DR EvolutionaryTrace; Q6Q547; -.
DR PRO; PR:Q6Q547; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; Q6Q547; protein.
DR GO; GO:0031429; C:box H/ACA snoRNP complex; IDA:UniProtKB.
DR GO; GO:0090661; C:box H/ACA telomerase RNP complex; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IDA:GO_Central.
DR GO; GO:0005732; C:sno(s)RNA-containing ribonucleoprotein complex; IDA:UniProtKB.
DR GO; GO:0034513; F:box H/ACA snoRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IDA:SGD.
DR GO; GO:0070034; F:telomerase RNA binding; IBA:GO_Central.
DR GO; GO:0000469; P:cleavage involved in rRNA processing; IMP:SGD.
DR GO; GO:0031118; P:rRNA pseudouridine synthesis; IMP:SGD.
DR GO; GO:0000454; P:snoRNA guided rRNA pseudouridine synthesis; IDA:ComplexPortal.
DR GO; GO:0031120; P:snRNA pseudouridine synthesis; IDA:UniProtKB.
DR DisProt; DP00475; -.
DR InterPro; IPR007264; H/ACA_rnp_Nop10.
DR InterPro; IPR036756; H/ACA_rnp_Nop10_sf.
DR PANTHER; PTHR13305; PTHR13305; 1.
DR Pfam; PF04135; Nop10p; 1.
DR SUPFAM; SSF144210; SSF144210; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosome biogenesis;
KW rRNA processing; Ubl conjugation.
FT CHAIN 1..58
FT /note="H/ACA ribonucleoprotein complex subunit NOP10"
FT /id="PRO_0000149013"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT CROSSLNK 28
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:3U28"
FT STRAND 8..12
FT /evidence="ECO:0007829|PDB:1Y2Y"
FT STRAND 13..17
FT /evidence="ECO:0007829|PDB:3U28"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:3U28"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:1Y2Y"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:2AQA"
FT HELIX 42..47
FT /evidence="ECO:0007829|PDB:3U28"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:1Y2Y"
SQ SEQUENCE 58 AA; 6636 MW; 4718D35AF7911FBA CRC64;
MHLMYTLGPD GKRIYTLKKV TESGEITKSA HPARFSPDDK YSRQRVTLKK RFGLVPGQ
