ID   UTP14_YEAST             Reviewed;         899 AA.
AC   Q04500; D6W0J2;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   27-MAR-2024, entry version 165.
DE   RecName: Full=U3 small nucleolar RNA-associated protein 14;
DE            Short=U3 snoRNA-associated protein 14;
DE   AltName: Full=U three protein 14;
GN   Name=UTP14; OrderedLocusNames=YML093W;
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=9169872;
RA   Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA   Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA   Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA   Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL   Nature 387:90-93(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   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   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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-151; SER-423; SER-562
RP   AND SER-738, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-668 AND SER-738, 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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-35; SER-151; SER-423;
RP   SER-424; SER-488; SER-500; SER-562; SER-668 AND SER-738, AND IDENTIFICATION
RP   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).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-151; SER-423;
RP   SER-488; SER-500; SER-562 AND SER-738, AND IDENTIFICATION BY MASS
RP   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).
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).
CC   -!- FUNCTION: Involved in nucleolar processing of pre-18S ribosomal RNA.
CC       {ECO:0000269|PubMed:12068309}.
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. {ECO:0000269|PubMed:12068309}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12068309}.
CC   -!- MISCELLANEOUS: Present with 1470 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the UTP14 family. {ECO:0000305}.
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DR   EMBL; Z46660; CAA86645.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA09806.1; -; Genomic_DNA.
DR   PIR; S49634; S49634.
DR   RefSeq; NP_013617.1; NM_001182452.1.
DR   PDB; 5WLC; EM; 3.80 A; SS=1-899.
DR   PDB; 6KE6; EM; 3.40 A; RQ=1-899.
DR   PDB; 6LQP; EM; 3.20 A; RQ=1-899.
DR   PDB; 6LQQ; EM; 4.10 A; RQ=1-899.
DR   PDB; 6LQR; EM; 8.60 A; RQ=1-899.
DR   PDB; 6LQS; EM; 3.80 A; RQ=1-899.
DR   PDB; 6LQT; EM; 4.90 A; RQ=1-899.
DR   PDB; 6LQU; EM; 3.70 A; RQ=1-899.
DR   PDB; 6LQV; EM; 4.80 A; RQ=1-899.
DR   PDB; 6ZQA; EM; 4.40 A; UN=1-899.
DR   PDB; 6ZQB; EM; 3.90 A; UN=276-897.
DR   PDB; 6ZQC; EM; 3.80 A; UN=1-899.
DR   PDB; 6ZQD; EM; 3.80 A; UN=1-899.
DR   PDB; 6ZQE; EM; 7.10 A; UN=786-800.
DR   PDB; 6ZQG; EM; 3.50 A; UN=1-899.
DR   PDB; 7AJT; EM; 4.60 A; UN=1-899.
DR   PDB; 7AJU; EM; 3.80 A; UN=1-899.
DR   PDB; 7D4I; EM; 4.00 A; RQ=1-899.
DR   PDB; 7D5S; EM; 4.60 A; RQ=1-899.
DR   PDB; 7D5T; EM; 6.00 A; RQ=1-899.
DR   PDB; 7D63; EM; 12.30 A; RQ=1-899.
DR   PDB; 7SUK; EM; 3.99 A; SS=276-350.
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; 6ZQA; -.
DR   PDBsum; 6ZQB; -.
DR   PDBsum; 6ZQC; -.
DR   PDBsum; 6ZQD; -.
DR   PDBsum; 6ZQE; -.
DR   PDBsum; 6ZQG; -.
DR   PDBsum; 7AJT; -.
DR   PDBsum; 7AJU; -.
DR   PDBsum; 7D4I; -.
DR   PDBsum; 7D5S; -.
DR   PDBsum; 7D5T; -.
DR   PDBsum; 7D63; -.
DR   PDBsum; 7SUK; -.
DR   AlphaFoldDB; Q04500; -.
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-11363; -.
DR   EMDB; EMD-11807; -.
DR   EMDB; EMD-11808; -.
DR   EMDB; EMD-30574; -.
DR   EMDB; EMD-30584; -.
DR   EMDB; EMD-30585; -.
DR   EMDB; EMD-30588; -.
DR   EMDB; EMD-9964; -.
DR   SMR; Q04500; -.
DR   BioGRID; 35050; 261.
DR   ComplexPortal; CPX-1604; Small ribosomal subunit processome.
DR   DIP; DIP-6410N; -.
DR   IntAct; Q04500; 19.
DR   MINT; Q04500; -.
DR   STRING; 4932.YML093W; -.
DR   GlyGen; Q04500; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q04500; -.
DR   MaxQB; Q04500; -.
DR   PaxDb; 4932-YML093W; -.
DR   PeptideAtlas; Q04500; -.
DR   EnsemblFungi; YML093W_mRNA; YML093W; YML093W.
DR   GeneID; 854881; -.
DR   KEGG; sce:YML093W; -.
DR   AGR; SGD:S000004558; -.
DR   SGD; S000004558; UTP14.
DR   VEuPathDB; FungiDB:YML093W; -.
DR   eggNOG; KOG2172; Eukaryota.
DR   GeneTree; ENSGT00390000008142; -.
DR   HOGENOM; CLU_003783_0_2_1; -.
DR   InParanoid; Q04500; -.
DR   OMA; QVIEPMD; -.
DR   OrthoDB; 5480898at2759; -.
DR   BioCyc; YEAST:G3O-32678-MONOMER; -.
DR   Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR   BioGRID-ORCS; 854881; 4 hits in 10 CRISPR screens.
DR   PRO; PR:Q04500; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; Q04500; Protein.
DR   GO; GO:0005730; C:nucleolus; IDA:SGD.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0032040; C:small-subunit processome; IDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000480; P:endonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR   GO; GO:0000447; P:endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR   GO; GO:0000472; P:endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR   GO; GO:0030490; P:maturation of SSU-rRNA; NAS:ComplexPortal.
DR   InterPro; IPR006709; SSU_processome_Utp14.
DR   PANTHER; PTHR14150; U3 SMALL NUCLEOLAR RNA-ASSOCIATED PROTEIN 14; 1.
DR   PANTHER; PTHR14150:SF12; U3 SMALL NUCLEOLAR RNA-ASSOCIATED PROTEIN 14 HOMOLOG A; 1.
DR   Pfam; PF04615; Utp14; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Ribonucleoprotein; Ribosome biogenesis;
KW   rRNA processing.
FT   CHAIN           1..899
FT                   /note="U3 small nucleolar RNA-associated protein 14"
FT                   /id="PRO_0000065742"
FT   REGION          1..197
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          485..509
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          559..721
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          776..805
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..48
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        63..87
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        97..111
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        135..164
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        165..195
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        591..614
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        615..629
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        660..721
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         260..267
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         34
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT   MOD_RES         35
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         151
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT   MOD_RES         423
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT   MOD_RES         424
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         488
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         500
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         562
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT   MOD_RES         668
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358,
FT                   ECO:0007744|PubMed:18407956"
FT   MOD_RES         738
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358,
FT                   ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   899 AA;  103023 MW;  0D4FC90D1CB3CFF1 CRC64;
     MAKKKSKSRS KSSRRVLDAL QLAEREINGE FDNSSDNDKR HDARRNGTVV NLLKRSKGDT
     NSDEDDIDSE SFEDEELNSD EALGSDDDYD ILNSKFSQTI RDKKENANYQ EEEDEGGYTS
     IDEEDLMPLS QVWDMDEKTA QSNGNDDEDA SPQLKLQDTD ISSESSSSEE SESESEDDEE
     EEDPFDEISE DEEDIELNTI TSKLIDETKS KAPKRLDTYG SGEANEYVLP SANAASGASG
     KLSLTDMMNV IDDRQVIENA NLLKGKSSTY EVPLPQRIQQ RHDRKAAYEI SRQEVSKWND
     IVQQNRRADH LIFPLNKPTE HNHASAFTRT QDVPQTELQE KVDQVLQESN LANPEKDSKF
     EELSTAKMTP EEMRKRTTEM RLMRELMFRE ERKARRLKKI KSKTYRKIKK KELMKNRELA
     AVSSDEDNED HDIARAKERM TLKHKTNSKW AKDMIKHGMT NDAETREEME EMLRQGERLK
     AKMLDRNSDD EEDGRVQTLS DVENEEKENI DSEALKSKLG KTGVMNMAFM KNGEAREREA
     NKETLRQLRA VENGDDIKLF ESDEEETNGE NIQINKGRRI YTPGSLESNK DMNELNDHTR
     KENKVDESRS LENRLRAKNS GQSKNARTNA EGAIIVEEES DGEPLQDGQN NQQDEEAKDV
     NPWLANESDE EHTVKKQSSK VNVIDKDSSK NVKAMNKMEK AELKQKKKKK GKSNDDEDLL
     LTADDSTRLK IVDPYGGSDD EQGDNVFMFK QQDVIAEAFA GDDVVAEFQE EKKRVIDDED
     DKEVDTTLPG WGEWAGAGSK PKNKKRKFIK KVKGVVNKDK RRDKNLQNVI INEKVNKKNL
     KYQSSAVPFP FENREQYERS LRMPIGQEWT SRASHQELIK PRIMTKPGQV IDPLKAPFK
//