ID   UTP9_YEAST              Reviewed;         575 AA.
AC   P38882; D3DLE4;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   27-MAR-2024, entry version 163.
DE   RecName: Full=U3 small nucleolar RNA-associated protein 9;
DE            Short=U3 snoRNA-associated protein 9;
DE   AltName: Full=U three protein 9;
DE   AltName: Full=U3 protein 9 required for transcription;
DE   AltName: Full=t-UTP9;
GN   Name=UTP9; OrderedLocusNames=YHR196W;
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   FUNCTION, INTERACTION WITH MPP10 AND SNORNA U3, IDENTIFICATION IN SSU
RP   PROCESSOME BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX   PubMed=12068309; DOI=10.1038/nature00769;
RA   Dragon F., Gallagher J.E.G., Compagnone-Post P.A., Mitchell B.M.,
RA   Porwancher K.A., Wehner K.A., Wormsley S., Settlage R.E., Shabanowitz J.,
RA   Osheim Y., Beyer A.L., Hunt D.F., Baserga S.J.;
RT   "A large nucleolar U3 ribonucleoprotein required for 18S ribosomal RNA
RT   biogenesis.";
RL   Nature 417:967-970(2002).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA   Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA   Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA   Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT   "Assigning function to yeast proteins by integration of technologies.";
RL   Mol. Cell 12:1353-1365(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   FUNCTION, IDENTIFICATION IN COMPLEX WITH OTHER T-UTPS, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=15489292; DOI=10.1101/gad.1226604;
RA   Gallagher J.E.G., Dunbar D.A., Granneman S., Mitchell B.M., Osheim Y.,
RA   Beyer A.L., Baserga S.J.;
RT   "RNA polymerase I transcription and pre-rRNA processing are linked by
RT   specific SSU processome components.";
RL   Genes Dev. 18:2506-2517(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-547 AND SER-564, AND
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).
CC   -!- FUNCTION: Involved in nucleolar processing of pre-18S ribosomal RNA.
CC       Required for optimal pre-ribosomal RNA transcription by RNA polymerase
CC       I together with a subset of U3 proteins required for transcription (t-
CC       UTPs). {ECO:0000269|PubMed:12068309, ECO:0000269|PubMed:15489292}.
CC   -!- SUBUNIT: Interacts with snoRNA U3. Interacts with MPP10. Component of
CC       the ribosomal small subunit (SSU) processome composed of at least 40
CC       protein subunits and snoRNA U3. In the absence of snoRNA3, forms a
CC       complex with other t-UTPs. This complex can associate with pre-18S
CC       ribosomal RNAs. {ECO:0000269|PubMed:12068309,
CC       ECO:0000269|PubMed:15489292}.
CC   -!- INTERACTION:
CC       P38882; Q04305: UTP15; NbExp=10; IntAct=EBI-24892, EBI-28183;
CC       P38882; Q06679: UTP4; NbExp=6; IntAct=EBI-24892, EBI-35712;
CC       P38882; P53276: UTP8; NbExp=6; IntAct=EBI-24892, EBI-23301;
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12068309,
CC       ECO:0000269|PubMed:15489292}. Note=Associated with ribosomal chromatin,
CC       even in the absence of transcription.
CC   -!- MISCELLANEOUS: Present with 20000 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
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DR   EMBL; U00030; AAB68369.1; -; Genomic_DNA.
DR   EMBL; BK006934; DAA06888.1; -; Genomic_DNA.
DR   PIR; S46692; S46692.
DR   RefSeq; NP_012066.1; NM_001179327.1.
DR   PDB; 5WLC; EM; 3.80 A; LK=1-575.
DR   PDB; 6KE6; EM; 3.40 A; A9=1-575.
DR   PDB; 6LQP; EM; 3.20 A; A9=1-575.
DR   PDB; 6LQQ; EM; 4.10 A; A9=1-575.
DR   PDB; 6LQR; EM; 8.60 A; A9=1-575.
DR   PDB; 6LQS; EM; 3.80 A; A9=1-575.
DR   PDB; 6LQT; EM; 4.90 A; A9=1-575.
DR   PDB; 6LQU; EM; 3.70 A; A9=1-575.
DR   PDB; 6LQV; EM; 4.80 A; A9=1-575.
DR   PDB; 6ND4; EM; 4.30 A; K=428-575.
DR   PDB; 6ZQA; EM; 4.40 A; UI=1-575.
DR   PDB; 6ZQB; EM; 3.90 A; UI=1-575.
DR   PDB; 6ZQC; EM; 3.80 A; UI=1-575.
DR   PDB; 6ZQD; EM; 3.80 A; UI=1-575.
DR   PDB; 6ZQE; EM; 7.10 A; UE=1-575.
DR   PDB; 7AJT; EM; 4.60 A; UI=1-575.
DR   PDB; 7AJU; EM; 3.80 A; UI=1-575.
DR   PDB; 7D4I; EM; 4.00 A; A9=1-575.
DR   PDB; 7D5S; EM; 4.60 A; A9=1-575.
DR   PDB; 7D63; EM; 12.30 A; A9=1-575.
DR   PDB; 7SUK; EM; 3.99 A; LK=428-515.
DR   PDBsum; 5WLC; -.
DR   PDBsum; 6KE6; -.
DR   PDBsum; 6LQP; -.
DR   PDBsum; 6LQQ; -.
DR   PDBsum; 6LQR; -.
DR   PDBsum; 6LQS; -.
DR   PDBsum; 6LQT; -.
DR   PDBsum; 6LQU; -.
DR   PDBsum; 6LQV; -.
DR   PDBsum; 6ND4; -.
DR   PDBsum; 6ZQA; -.
DR   PDBsum; 6ZQB; -.
DR   PDBsum; 6ZQC; -.
DR   PDBsum; 6ZQD; -.
DR   PDBsum; 6ZQE; -.
DR   PDBsum; 7AJT; -.
DR   PDBsum; 7AJU; -.
DR   PDBsum; 7D4I; -.
DR   PDBsum; 7D5S; -.
DR   PDBsum; 7D63; -.
DR   PDBsum; 7SUK; -.
DR   AlphaFoldDB; P38882; -.
DR   EMDB; EMD-0441; -.
DR   EMDB; EMD-0949; -.
DR   EMDB; EMD-0950; -.
DR   EMDB; EMD-0951; -.
DR   EMDB; EMD-0952; -.
DR   EMDB; EMD-0953; -.
DR   EMDB; EMD-0954; -.
DR   EMDB; EMD-0955; -.
DR   EMDB; EMD-11357; -.
DR   EMDB; EMD-11358; -.
DR   EMDB; EMD-11359; -.
DR   EMDB; EMD-11360; -.
DR   EMDB; EMD-11361; -.
DR   EMDB; EMD-11807; -.
DR   EMDB; EMD-11808; -.
DR   EMDB; EMD-30574; -.
DR   EMDB; EMD-30584; -.
DR   EMDB; EMD-30588; -.
DR   EMDB; EMD-8859; -.
DR   EMDB; EMD-9964; -.
DR   SMR; P38882; -.
DR   BioGRID; 36630; 381.
DR   ComplexPortal; CPX-1409; UTP-A complex.
DR   DIP; DIP-6634N; -.
DR   IntAct; P38882; 71.
DR   MINT; P38882; -.
DR   STRING; 4932.YHR196W; -.
DR   iPTMnet; P38882; -.
DR   MaxQB; P38882; -.
DR   PaxDb; 4932-YHR196W; -.
DR   PeptideAtlas; P38882; -.
DR   EnsemblFungi; YHR196W_mRNA; YHR196W; YHR196W.
DR   GeneID; 856603; -.
DR   KEGG; sce:YHR196W; -.
DR   AGR; SGD:S000001239; -.
DR   SGD; S000001239; UTP9.
DR   VEuPathDB; FungiDB:YHR196W; -.
DR   eggNOG; ENOG502QSYR; Eukaryota.
DR   HOGENOM; CLU_037435_0_0_1; -.
DR   InParanoid; P38882; -.
DR   OMA; RFAFQAN; -.
DR   OrthoDB; 2012168at2759; -.
DR   BioCyc; YEAST:G3O-31224-MONOMER; -.
DR   BioGRID-ORCS; 856603; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P38882; -.
DR   Proteomes; UP000002311; Chromosome VIII.
DR   RNAct; P38882; Protein.
DR   GO; GO:0030686; C:90S preribosome; HDA:SGD.
DR   GO; GO:0005730; C:nucleolus; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0033553; C:rDNA heterochromatin; IDA:SGD.
DR   GO; GO:0032040; C:small-subunit processome; IDA:SGD.
DR   GO; GO:0034455; C:t-UTP complex; IDA:SGD.
DR   GO; GO:0034511; F:U3 snoRNA binding; IDA:SGD.
DR   GO; GO:0030490; P:maturation of SSU-rRNA; NAS:ComplexPortal.
DR   GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR   GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; IMP:SGD.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   SUPFAM; SSF69322; Tricorn protease domain 2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Nucleus; Phosphoprotein; Reference proteome;
KW   Ribonucleoprotein; Ribosome biogenesis; rRNA processing; Transcription.
FT   CHAIN           1..575
FT                   /note="U3 small nucleolar RNA-associated protein 9"
FT                   /id="PRO_0000065744"
FT   REGION          340..375
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        342..375
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         547
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         564
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
SQ   SEQUENCE   575 AA;  65271 MW;  0C482C6A32855FF1 CRC64;
     MGSSLDLVAS FSHDSTRFAF QASVAQKNNV DIYPLNETKD YVVNSSLVSH IDYETNDMKV
     SDVIFFGWCS DLIDTQSSNI KRKLDEDEGT GESSEQRCEN FFVNGFPDGR IVVYSSNGKD
     IVNIIKNKKE ILGADTDESD IWILDSDKVV KKLQYNNSKP LKTFTLVDGK DDEIVHFQIL
     HQNGTLLVCI ITKQMVYIVD PSKRRPSTKY SFEISDAVAC EFSSDGKYLL IANNEELIAY
     DLKEDSKLIQ SWPVQVKTLK TLDDLIMALT TDGKINNYKI GEADKVCSIV VNEDLEIIDF
     TPINSKQQVL ISWLNVNEPN FESISLKEIE TQGYITINKN EKNNADEADQ KKLEEKEEEA
     QPEVQHEKKE TETKINKKVS KSDQVEIANI LSSHLEANST EILDDLMSGS WTEPEIKKFI
     LTKINTVDHL SKIFLTISKS ITQNPWNEEN LLPLWLKWLL TLKSGELNSI KDKHTKKNCK
     HLKSALRSSE EILPVLLGIQ GRLEMLRRQA KLREDLAQLS MQEGEDDEIE VIEHSNVISN
     PLQDQASPVE KLEPDSIVYA NGESDEFVDA SEYKD
//