UTP9_YEAST
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 03-AUG-2022, entry version 156.
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 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 AlphaFoldDB; P38882; -.
DR SMR; P38882; -.
DR BioGRID; 36630; 355.
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; P38882; -.
DR PRIDE; P38882; -.
DR EnsemblFungi; YHR196W_mRNA; YHR196W; YHR196W.
DR GeneID; 856603; -.
DR KEGG; sce:YHR196W; -.
DR SGD; S000001239; UTP9.
DR VEuPathDB; FungiDB:YHR196W; -.
DR eggNOG; ENOG502QSYR; Eukaryota.
DR HOGENOM; CLU_037435_0_0_1; -.
DR InParanoid; P38882; -.
DR OMA; FHLTDGK; -.
DR BioCyc; YEAST:G3O-31224-MON; -.
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; IC: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; -; 1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
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
