UTP14_YEAST
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 03-AUG-2022, entry version 158.
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 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 AlphaFoldDB; Q04500; -.
DR SMR; Q04500; -.
DR BioGRID; 35050; 254.
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-6410N; -.
DR IntAct; Q04500; 19.
DR MINT; Q04500; -.
DR STRING; 4932.YML093W; -.
DR iPTMnet; Q04500; -.
DR MaxQB; Q04500; -.
DR PaxDb; Q04500; -.
DR PRIDE; Q04500; -.
DR EnsemblFungi; YML093W_mRNA; YML093W; YML093W.
DR GeneID; 854881; -.
DR KEGG; sce:YML093W; -.
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; RESKWAK; -.
DR BioCyc; YEAST:G3O-32678-MON; -.
DR Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
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; IC:ComplexPortal.
DR InterPro; IPR006709; SSU_processome_Utp14.
DR PANTHER; PTHR14150; PTHR14150; 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
