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Q04500

- UTP14_YEAST

UniProt

Q04500 - UTP14_YEAST

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Protein
U3 small nucleolar RNA-associated protein 14
Gene
UTP14, YML093W
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi260 – 2678ATP Reviewed prediction

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW

GO - Biological processi

  1. endonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Source: SGD
  2. 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) Source: SGD
  3. endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Biological processi

Ribosome biogenesis, rRNA processing

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-32678-MONOMER.

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
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XIII

Organism-specific databases

CYGDiYML093w.
SGDiS000004558. UTP14.

Subcellular locationi

Nucleusnucleolus 1 Publication

GO - Cellular componenti

  1. nucleolus Source: SGD
  2. small-subunit processome Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 899899U3 small nucleolar RNA-associated protein 14
PRO_0000065742Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei34 – 341Phosphoserine3 Publications
Modified residuei35 – 351Phosphoserine2 Publications
Modified residuei151 – 1511Phosphoserine3 Publications
Modified residuei423 – 4231Phosphoserine3 Publications
Modified residuei424 – 4241Phosphoserine2 Publications
Modified residuei488 – 4881Phosphoserine2 Publications
Modified residuei500 – 5001Phosphoserine2 Publications
Modified residuei562 – 5621Phosphoserine3 Publications
Modified residuei668 – 6681Phosphoserine2 Publications
Modified residuei738 – 7381Phosphoserine4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ04500.
PaxDbiQ04500.

Expressioni

Gene expression databases

GenevestigatoriQ04500.

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

BioGridi35050. 34 interactions.
DIPiDIP-6410N.
IntActiQ04500. 3 interactions.
MINTiMINT-8285383.
STRINGi4932.YML093W.

Structurei

3D structure databases

ProteinModelPortaliQ04500.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi162 – 1687Poly-Ser
Compositional biasi179 – 1824Poly-Glu
Compositional biasi704 – 7129Poly-Lys

Sequence similaritiesi

Belongs to the UTP14 family.

Phylogenomic databases

eggNOGiCOG5644.
GeneTreeiENSGT00390000008142.
HOGENOMiHOG000074497.
KOiK14567.
OMAiKANDAMV.
OrthoDBiEOG7HQNJB.

Family and domain databases

InterProiIPR006709. SSU_processome_Utp14.
[Graphical view]
PANTHERiPTHR14150. PTHR14150. 1 hit.
PfamiPF04615. Utp14. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q04500-1 [UniParc]FASTAAdd to Basket

« Hide

MAKKKSKSRS KSSRRVLDAL QLAEREINGE FDNSSDNDKR HDARRNGTVV    50
NLLKRSKGDT NSDEDDIDSE SFEDEELNSD EALGSDDDYD ILNSKFSQTI 100
RDKKENANYQ EEEDEGGYTS IDEEDLMPLS QVWDMDEKTA QSNGNDDEDA 150
SPQLKLQDTD ISSESSSSEE SESESEDDEE EEDPFDEISE DEEDIELNTI 200
TSKLIDETKS KAPKRLDTYG SGEANEYVLP SANAASGASG KLSLTDMMNV 250
IDDRQVIENA NLLKGKSSTY EVPLPQRIQQ RHDRKAAYEI SRQEVSKWND 300
IVQQNRRADH LIFPLNKPTE HNHASAFTRT QDVPQTELQE KVDQVLQESN 350
LANPEKDSKF EELSTAKMTP EEMRKRTTEM RLMRELMFRE ERKARRLKKI 400
KSKTYRKIKK KELMKNRELA AVSSDEDNED HDIARAKERM TLKHKTNSKW 450
AKDMIKHGMT NDAETREEME EMLRQGERLK AKMLDRNSDD EEDGRVQTLS 500
DVENEEKENI DSEALKSKLG KTGVMNMAFM KNGEAREREA NKETLRQLRA 550
VENGDDIKLF ESDEEETNGE NIQINKGRRI YTPGSLESNK DMNELNDHTR 600
KENKVDESRS LENRLRAKNS GQSKNARTNA EGAIIVEEES DGEPLQDGQN 650
NQQDEEAKDV NPWLANESDE EHTVKKQSSK VNVIDKDSSK NVKAMNKMEK 700
AELKQKKKKK GKSNDDEDLL LTADDSTRLK IVDPYGGSDD EQGDNVFMFK 750
QQDVIAEAFA GDDVVAEFQE EKKRVIDDED DKEVDTTLPG WGEWAGAGSK 800
PKNKKRKFIK KVKGVVNKDK RRDKNLQNVI INEKVNKKNL KYQSSAVPFP 850
FENREQYERS LRMPIGQEWT SRASHQELIK PRIMTKPGQV IDPLKAPFK 899
Length:899
Mass (Da):103,023
Last modified:November 1, 1997 - v1
Checksum:i0D4FC90D1CB3CFF1
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z46660 Genomic DNA. Translation: CAA86645.1.
BK006946 Genomic DNA. Translation: DAA09806.1.
PIRiS49634.
RefSeqiNP_013617.1. NM_001182452.1.

Genome annotation databases

EnsemblFungiiYML093W; YML093W; YML093W.
GeneIDi854881.
KEGGisce:YML093W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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. 34 interactions.
DIPi DIP-6410N.
IntActi Q04500. 3 interactions.
MINTi MINT-8285383.
STRINGi 4932.YML093W.

Proteomic databases

MaxQBi Q04500.
PaxDbi Q04500.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

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

Organism-specific databases

CYGDi YML093w.
SGDi S000004558. UTP14.

Phylogenomic databases

eggNOGi COG5644.
GeneTreei ENSGT00390000008142.
HOGENOMi HOG000074497.
KOi K14567.
OMAi KANDAMV.
OrthoDBi EOG7HQNJB.

Enzyme and pathway databases

BioCyci YEAST:G3O-32678-MONOMER.

Miscellaneous databases

NextBioi 977828.
PROi Q04500.

Gene expression databases

Genevestigatori 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...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: FUNCTION, INTERACTION WITH MPP10 AND SNORNA U3, IDENTIFICATION IN SSU PROCESSOME BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
  4. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  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-35; SER-151; SER-423; SER-424; SER-562 AND SER-738, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  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].
  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].
  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].
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiUTP14_YEAST
AccessioniPrimary (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: May 14, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

Similar proteinsi