NOP6_YEAST
ID NOP6_YEAST Reviewed; 225 AA.
AC Q07623; D6VRE1;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Nucleolar protein 6;
GN Name=NOP6; OrderedLocusNames=YDL213C; ORFNames=D1018;
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].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9046097;
RX DOI=10.1002/(sici)1097-0061(199702)13:2<163::aid-yea54>3.0.co;2-4;
RA Bahr A., Moeller-Rieker S., Hankeln T., Kraemer C., Protin U.,
RA Schmidt E.R.;
RT "The nucleotide sequence of a 39 kb segment of yeast chromosome IV: 12 new
RT open reading frames, nine known genes and one gene for Gly-tRNA.";
RL Yeast 13:163-169(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [3]
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 [4]
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 [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 PREDICTION OF FUNCTION.
RX PubMed=14566057; DOI=10.1073/pnas.2132527100;
RA Samanta M.P., Liang S.;
RT "Predicting protein functions from redundancies in large-scale protein
RT interaction networks.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12579-12583(2003).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45, 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).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160, 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: Predicted to be involved in rRNA processing.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 8970 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the RRM NOP6 family. {ECO:0000305}.
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DR EMBL; X99000; CAA67478.1; -; Genomic_DNA.
DR EMBL; Z74261; CAA98791.1; -; Genomic_DNA.
DR EMBL; AY557652; AAS55978.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11651.1; -; Genomic_DNA.
DR PIR; S67772; S67772.
DR RefSeq; NP_010068.1; NM_001180273.1.
DR PDB; 2MZJ; NMR; -; A=75-156.
DR PDBsum; 2MZJ; -.
DR AlphaFoldDB; Q07623; -.
DR SMR; Q07623; -.
DR BioGRID; 31832; 264.
DR ComplexPortal; CPX-1604; Small ribosomal subunit processome, variant 1.
DR ComplexPortal; CPX-1607; Small ribosomal subunit processome, variant 2.
DR ComplexPortal; CPX-1608; Small ribosomal subunit processome, variant 3.
DR DIP; DIP-1807N; -.
DR IntAct; Q07623; 85.
DR MINT; Q07623; -.
DR STRING; 4932.YDL213C; -.
DR iPTMnet; Q07623; -.
DR MaxQB; Q07623; -.
DR PaxDb; Q07623; -.
DR PRIDE; Q07623; -.
DR EnsemblFungi; YDL213C_mRNA; YDL213C; YDL213C.
DR GeneID; 851313; -.
DR KEGG; sce:YDL213C; -.
DR SGD; S000002372; NOP6.
DR VEuPathDB; FungiDB:YDL213C; -.
DR eggNOG; ENOG502QVC2; Eukaryota.
DR HOGENOM; CLU_037639_2_0_1; -.
DR InParanoid; Q07623; -.
DR OMA; NIQRRMD; -.
DR BioCyc; YEAST:G3O-29595-MON; -.
DR PRO; PR:Q07623; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q07623; protein.
DR GO; GO:0030686; C:90S preribosome; IDA:SGD.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0032040; C:small-subunit processome; IPI:ComplexPortal.
DR GO; GO:0019843; F:rRNA binding; IDA:SGD.
DR GO; GO:0030515; F:snoRNA binding; IDA:SGD.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IC:ComplexPortal.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IGI:SGD.
DR CDD; cd12400; RRM_Nop6; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR034228; Nop6_RRM.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Phosphoprotein; Reference proteome;
KW Ribosome biogenesis; RNA-binding; rRNA processing.
FT CHAIN 1..225
FT /note="Nucleolar protein 6"
FT /id="PRO_0000268691"
FT DOMAIN 78..155
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..72
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT STRAND 77..83
FT /evidence="ECO:0007829|PDB:2MZJ"
FT HELIX 91..98
FT /evidence="ECO:0007829|PDB:2MZJ"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:2MZJ"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:2MZJ"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:2MZJ"
FT STRAND 114..120
FT /evidence="ECO:0007829|PDB:2MZJ"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:2MZJ"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:2MZJ"
FT HELIX 128..136
FT /evidence="ECO:0007829|PDB:2MZJ"
FT TURN 137..140
FT /evidence="ECO:0007829|PDB:2MZJ"
FT STRAND 149..154
FT /evidence="ECO:0007829|PDB:2MZJ"
SQ SEQUENCE 225 AA; 25216 MW; 2FB6E4C4BB1542B3 CRC64;
MGSEEDKKLT KKQLKAQQFR KSKEEKDQEK DVKKEQAPEG KRPNSAAGND GEEPVKKKRK
TRRGRGGKGK NGKKGNRFIV FVGSLPRDIT AVELQNHFKN SSPDQIRLRA DKGIAFLEFD
ADKDRTGIQR RMDIALLQHG TLLKEKKINV ELTVGGGGNS QERLEKLKNK NIKLDEERKE
RLTKMINDGN QKKIAKTTAT AAQTSGTDNK PVPAGIHPDR AKLLK
