UTP14

Functionⁱ

Involved in nucleolar processing of pre-18S ribosomal RNA.1 Publication

Regions

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Nucleotide bindingⁱ	260 – 267	8	ATPSequence analysis

GO - Molecular functionⁱ

ATP binding Source: UniProtKB-KW

Enzyme and pathway databases

BioCycⁱ	YEAST:G3O-32678-MONOMER.
Reactomeⁱ	R-SCE-6790901. rRNA modification in the nucleus. R-SCE-6791226. Major pathway of rRNA processing in the nucleolus.

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: U3 small nucleolar RNA-associated protein 14 Short name: U3 snoRNA-associated protein 14 Alternative name(s): U three protein 14
Gene namesⁱ	Name:UTP14 Ordered Locus Names:YML093W
Organismⁱ	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifierⁱ	559292 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae
Proteomesⁱ	UP000002311 Componentⁱ: Chromosome XIII

Organism-specific databases

EuPathDBⁱ	FungiDB:YML093W.
SGDⁱ	S000004558. UTP14.

Subcellular locationⁱ

Nucleus › nucleolus
1 Publication
Manual assertion based on experiment inⁱ
- Ref.3
  "A large nucleolar U3 ribonucleoprotein required for 18S ribosomal RNA biogenesis."
  Dragon F., Gallagher J.E.G., Compagnone-Post P.A., Mitchell B.M., Porwancher K.A., Wehner K.A., Wormsley S., Settlage R.E., Shabanowitz J., Osheim Y., Beyer A.L., Hunt D.F., Baserga S.J.
  Nature 417:967-970(2002) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, INTERACTION WITH MPP10 AND SNORNA U3, IDENTIFICATION IN SSU PROCESSOME BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.

GO - Cellular componentⁱ

nucleolus
Source: SGD
Inferred from direct assayⁱ
- 12068309
nucleoplasm Source: Reactome
small-subunit processome
Source: SGD
Inferred from direct assayⁱ
- 12068309

Complete GO annotation...

Keywords - Cellular componentⁱ

Nucleus

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Chainⁱ	1 – 899	899	U3 small nucleolar RNA-associated protein 14		PRO_0000065742	Add BLAST

Amino acid modifications

Feature key	Position(s)	Length	Description
Modified residueⁱ	34 – 34	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.5 "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-151; SER-423; SER-562 AND SER-738, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.7 "A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-35; SER-151; SER-423; SER-424; SER-488; SER-500; SER-562; SER-668 AND SER-738, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.8 "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution." Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O. Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-151; SER-423; SER-488; SER-500; SER-562 AND SER-738, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	35 – 35	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.7 "A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-35; SER-151; SER-423; SER-424; SER-488; SER-500; SER-562; SER-668 AND SER-738, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	151 – 151	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.5 "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-151; SER-423; SER-562 AND SER-738, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.7 "A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-35; SER-151; SER-423; SER-424; SER-488; SER-500; SER-562; SER-668 AND SER-738, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.8 "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution." Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O. Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-151; SER-423; SER-488; SER-500; SER-562 AND SER-738, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	423 – 423	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.5 "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-151; SER-423; SER-562 AND SER-738, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.7 "A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-35; SER-151; SER-423; SER-424; SER-488; SER-500; SER-562; SER-668 AND SER-738, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.8 "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution." Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O. Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-151; SER-423; SER-488; SER-500; SER-562 AND SER-738, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	424 – 424	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.7 "A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-35; SER-151; SER-423; SER-424; SER-488; SER-500; SER-562; SER-668 AND SER-738, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	488 – 488	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.7 "A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-35; SER-151; SER-423; SER-424; SER-488; SER-500; SER-562; SER-668 AND SER-738, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.8 "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution." Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O. Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-151; SER-423; SER-488; SER-500; SER-562 AND SER-738, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	500 – 500	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.7 "A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-35; SER-151; SER-423; SER-424; SER-488; SER-500; SER-562; SER-668 AND SER-738, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.8 "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution." Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O. Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-151; SER-423; SER-488; SER-500; SER-562 AND SER-738, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	562 – 562	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.5 "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-151; SER-423; SER-562 AND SER-738, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.7 "A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-35; SER-151; SER-423; SER-424; SER-488; SER-500; SER-562; SER-668 AND SER-738, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.8 "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution." Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O. Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-151; SER-423; SER-488; SER-500; SER-562 AND SER-738, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	668 – 668	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.6 "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-668 AND SER-738, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.7 "A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-35; SER-151; SER-423; SER-424; SER-488; SER-500; SER-562; SER-668 AND SER-738, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	738 – 738	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.5 "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-151; SER-423; SER-562 AND SER-738, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.6 "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-668 AND SER-738, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.7 "A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-35; SER-151; SER-423; SER-424; SER-488; SER-500; SER-562; SER-668 AND SER-738, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.8 "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution." Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O. Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-151; SER-423; SER-488; SER-500; SER-562 AND SER-738, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Keywords - PTMⁱ

Phosphoprotein

Proteomic databases

MaxQBⁱ	Q04500.

MaxQBⁱ

Q04500.

PTM databases

iPTMnetⁱ	Q04500.

iPTMnetⁱ

Q04500.

Interactionⁱ

Subunit structureⁱ

Interacts with snoRNA U3. Interacts with MPP10. Component of the ribosomal small subunit (SSU) processome composed of at least 40 protein subunits and snoRNA U3.1 Publication

Protein-protein interaction databases

BioGridⁱ	35050. 40 interactions.
DIPⁱ	DIP-6410N.
IntActⁱ	Q04500. 5 interactions.
MINTⁱ	MINT-8285383.

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	Q04500.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Compositional bias

Feature key	Position(s)	Length	Description
Compositional biasⁱ	162 – 168	7	Poly-Ser
Compositional biasⁱ	179 – 182	4	Poly-Glu
Compositional biasⁱ	704 – 712	9	Poly-Lys

Sequence similaritiesⁱ

Belongs to the UTP14 family.Curated

Phylogenomic databases

GeneTreeⁱ	ENSGT00390000008142.
HOGENOMⁱ	HOG000074497.
InParanoidⁱ	Q04500.
KOⁱ	K14567.
OMAⁱ	KPMVVQA.
OrthoDBⁱ	EOG092C1VSC.

Family and domain databases

InterProⁱ	IPR006709. SSU_processome_Utp14. [Graphical view]
PANTHERⁱ	PTHR14150. PTHR14150. 1 hit.
Pfamⁱ	PF04615. Utp14. 1 hit. [Graphical view]

Sequenceⁱ

Sequence statusⁱ: Complete.

Q04500-1 [UniParc]FASTA Add to basket

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        10         20         30         40         50
MAKKKSKSRS KSSRRVLDAL QLAEREINGE FDNSSDNDKR HDARRNGTVV 
        60         70         80         90        100
NLLKRSKGDT NSDEDDIDSE SFEDEELNSD EALGSDDDYD ILNSKFSQTI 
       110        120        130        140        150
RDKKENANYQ EEEDEGGYTS IDEEDLMPLS QVWDMDEKTA QSNGNDDEDA 
       160        170        180        190        200
SPQLKLQDTD ISSESSSSEE SESESEDDEE EEDPFDEISE DEEDIELNTI 
       210        220        230        240        250
TSKLIDETKS KAPKRLDTYG SGEANEYVLP SANAASGASG KLSLTDMMNV 
       260        270        280        290        300
IDDRQVIENA NLLKGKSSTY EVPLPQRIQQ RHDRKAAYEI SRQEVSKWND 
       310        320        330        340        350
IVQQNRRADH LIFPLNKPTE HNHASAFTRT QDVPQTELQE KVDQVLQESN 
       360        370        380        390        400
LANPEKDSKF EELSTAKMTP EEMRKRTTEM RLMRELMFRE ERKARRLKKI 
       410        420        430        440        450
KSKTYRKIKK KELMKNRELA AVSSDEDNED HDIARAKERM TLKHKTNSKW 
       460        470        480        490        500
AKDMIKHGMT NDAETREEME EMLRQGERLK AKMLDRNSDD EEDGRVQTLS 
       510        520        530        540        550
DVENEEKENI DSEALKSKLG KTGVMNMAFM KNGEAREREA NKETLRQLRA 
       560        570        580        590        600
VENGDDIKLF ESDEEETNGE NIQINKGRRI YTPGSLESNK DMNELNDHTR 
       610        620        630        640        650
KENKVDESRS LENRLRAKNS GQSKNARTNA EGAIIVEEES DGEPLQDGQN 
       660        670        680        690        700
NQQDEEAKDV NPWLANESDE EHTVKKQSSK VNVIDKDSSK NVKAMNKMEK 
       710        720        730        740        750
AELKQKKKKK GKSNDDEDLL LTADDSTRLK IVDPYGGSDD EQGDNVFMFK 
       760        770        780        790        800
QQDVIAEAFA GDDVVAEFQE EKKRVIDDED DKEVDTTLPG WGEWAGAGSK 
       810        820        830        840        850
PKNKKRKFIK KVKGVVNKDK RRDKNLQNVI INEKVNKKNL KYQSSAVPFP 
       860        870        880        890 
FENREQYERS LRMPIGQEWT SRASHQELIK PRIMTKPGQV IDPLKAPFK

Length:899

Mass (Da):103,023

Last modified:November 1, 1997 - v1

Checksum:ⁱ0D4FC90D1CB3CFF1

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	Z46660 Genomic DNA. Translation: CAA86645.1. BK006946 Genomic DNA. Translation: DAA09806.1.
PIRⁱ	S49634.
RefSeqⁱ	NP_013617.1. NM_001182452.1.

Genome annotation databases

EnsemblFungiⁱ	YML093W; YML093W; YML093W.
GeneIDⁱ	854881.
KEGGⁱ	sce:YML093W.

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	Z46660 Genomic DNA. Translation: CAA86645.1. BK006946 Genomic DNA. Translation: DAA09806.1.
PIRⁱ	S49634.
RefSeqⁱ	NP_013617.1. NM_001182452.1.

3D structure databases

ProteinModelPortalⁱ	Q04500.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	35050. 40 interactions.
DIPⁱ	DIP-6410N.
IntActⁱ	Q04500. 5 interactions.
MINTⁱ	MINT-8285383.

PTM databases

iPTMnetⁱ	Q04500.

iPTMnetⁱ

Q04500.

Proteomic databases

MaxQBⁱ	Q04500.

MaxQBⁱ

Q04500.

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblFungiⁱ	YML093W; YML093W; YML093W.
GeneIDⁱ	854881.
KEGGⁱ	sce:YML093W.

Organism-specific databases

EuPathDBⁱ	FungiDB:YML093W.
SGDⁱ	S000004558. UTP14.

Phylogenomic databases

GeneTreeⁱ	ENSGT00390000008142.
HOGENOMⁱ	HOG000074497.
InParanoidⁱ	Q04500.
KOⁱ	K14567.
OMAⁱ	KPMVVQA.
OrthoDBⁱ	EOG092C1VSC.

Enzyme and pathway databases

BioCycⁱ	YEAST:G3O-32678-MONOMER.
Reactomeⁱ	R-SCE-6790901. rRNA modification in the nucleus. R-SCE-6791226. Major pathway of rRNA processing in the nucleolus.

Miscellaneous databases

PROⁱ	Q04500.

PROⁱ

Q04500.

Family and domain databases

InterProⁱ	IPR006709. SSU_processome_Utp14. [Graphical view]
PANTHERⁱ	PTHR14150. PTHR14150. 1 hit.
Pfamⁱ	PF04615. Utp14. 1 hit. [Graphical view]
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ

UTP14_YEAST

Accessionⁱ

Primary (citable) accession number: Q04500
Secondary accession number(s): D6W0J2

Entry historyⁱ

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	September 7, 2016
This is version 119 of the entry and version 1 of the sequence. [Complete history]

Entry statusⁱ

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Miscellaneousⁱ

Miscellaneous

Present with 1470 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termⁱ

Complete proteome, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
Yeast
Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
Yeast chromosome XIII
Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

Similar proteinsⁱ

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:

100%	UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%	UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%	UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q04500 (UTP14_YEAST)

UniProt

Q04500 - UTP14_YEAST

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U3 small nucleolar RNA-associated protein 14

Select a section on the left to see content.

<p>Provides any useful information about the protein, mostly biological knowledge.</p><p><a href='../manual/function_section' target='_top'>More...</a></p>Functioni

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

Enzyme and pathway databases

<p>Provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.</p><p><a href='../manual/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>Provides information on the location and the topology of the mature protein in the cell.</p><p><a href='../manual/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Cellular componenti

<p>Describes post-translational modifications (PTMs) and/or processing events.</p><p><a href='../manual/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Proteomic databases

PTM databases

<p>Provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.</p><p><a href='../manual/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>Provides information on the tertiary and secondary structure of a protein.</p><p><a href='../manual/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>Provides information on sequence similarities with other proteins and the domain(s) present in a protein.</p><p><a href='../manual/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Compositional bias

<p>Provides information about the sequence similarity with other proteins.</p><p><a href='../manual/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

<p>Displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including length and molecular weight.</p><p><a href='../manual/sequences_section' target='_top'>More...</a></p>Sequencei

Sequence databases

Genome annotation databases

<p>Is used to point to information related to entries and found in data collections other than UniProtKB.</p><p><a href='../manual/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>Provides general information on the entry.</p><p><a href='../manual/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>Contains any relevant information that doesn’t fit in any other defined sections</p><p><a href='../manual/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Miscellaneous

Documents

Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequenceⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ