Q04500 (UTP14_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
U3 small nucleolar RNA-associated protein 14
Short name=U3 snoRNA-associated protein 14

Alternative name(s):
U three protein 14

Gene names

Name:	UTP14
Ordered Locus Names:	YML093W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	899 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in nucleolar processing of pre-18S ribosomal RNA. Ref.3
Subunit structure	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. Ref.3
Subcellular location	Nucleus › nucleolus Ref.3.
Miscellaneous	Present with 1470 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the UTP14 family.

Ontologies

Keywords
Biological process	Ribosome biogenesis rRNA processing
Cellular component	Nucleus
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ribonucleoprotein
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	endonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Inferred from mutant phenotype PubMed 15489292. Source: SGD 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) Inferred from mutant phenotype PubMed 15489292. Source: SGD endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Inferred from mutant phenotype PubMed 15489292. Source: SGD
Cellular_component	nucleolus Inferred from direct assay Ref.3. Source: SGD small-subunit processome Inferred from direct assay Ref.3. Source: SGD
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 899	899	U3 small nucleolar RNA-associated protein 14		PRO_0000065742
Regions
	Nucleotide binding	260 – 267	8	ATP Potential
	Compositional bias	162 – 168	7	Poly-Ser
	Compositional bias	179 – 182	4	Poly-Glu
	Compositional bias	704 – 712	9	Poly-Lys
Amino acid modifications
	Modified residue	34	1	Phosphoserine Ref.5 Ref.7 Ref.8
	Modified residue	35	1	Phosphoserine Ref.5 Ref.7
	Modified residue	151	1	Phosphoserine Ref.5 Ref.7 Ref.8
	Modified residue	423	1	Phosphoserine Ref.5 Ref.7 Ref.8
	Modified residue	424	1	Phosphoserine Ref.5 Ref.7
	Modified residue	488	1	Phosphoserine Ref.7 Ref.8
	Modified residue	500	1	Phosphoserine Ref.7 Ref.8
	Modified residue	562	1	Phosphoserine Ref.5 Ref.7 Ref.8
	Modified residue	668	1	Phosphoserine Ref.6 Ref.7
	Modified residue	738	1	Phosphoserine Ref.5 Ref.6 Ref.7 Ref.8

Sequences

	Sequence		Length	Mass (Da)
	Q04500 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: 0D4FC90D1CB3CFF1	FASTA	899	103,023
	10 20 30 40 50 60 MAKKKSKSRS KSSRRVLDAL QLAEREINGE FDNSSDNDKR HDARRNGTVV NLLKRSKGDT 70 80 90 100 110 120 NSDEDDIDSE SFEDEELNSD EALGSDDDYD ILNSKFSQTI RDKKENANYQ EEEDEGGYTS 130 140 150 160 170 180 IDEEDLMPLS QVWDMDEKTA QSNGNDDEDA SPQLKLQDTD ISSESSSSEE SESESEDDEE 190 200 210 220 230 240 EEDPFDEISE DEEDIELNTI TSKLIDETKS KAPKRLDTYG SGEANEYVLP SANAASGASG 250 260 270 280 290 300 KLSLTDMMNV IDDRQVIENA NLLKGKSSTY EVPLPQRIQQ RHDRKAAYEI SRQEVSKWND 310 320 330 340 350 360 IVQQNRRADH LIFPLNKPTE HNHASAFTRT QDVPQTELQE KVDQVLQESN LANPEKDSKF 370 380 390 400 410 420 EELSTAKMTP EEMRKRTTEM RLMRELMFRE ERKARRLKKI KSKTYRKIKK KELMKNRELA 430 440 450 460 470 480 AVSSDEDNED HDIARAKERM TLKHKTNSKW AKDMIKHGMT NDAETREEME EMLRQGERLK 490 500 510 520 530 540 AKMLDRNSDD EEDGRVQTLS DVENEEKENI DSEALKSKLG KTGVMNMAFM KNGEAREREA 550 560 570 580 590 600 NKETLRQLRA VENGDDIKLF ESDEEETNGE NIQINKGRRI YTPGSLESNK DMNELNDHTR 610 620 630 640 650 660 KENKVDESRS LENRLRAKNS GQSKNARTNA EGAIIVEEES DGEPLQDGQN NQQDEEAKDV 670 680 690 700 710 720 NPWLANESDE EHTVKKQSSK VNVIDKDSSK NVKAMNKMEK AELKQKKKKK GKSNDDEDLL 730 740 750 760 770 780 LTADDSTRLK IVDPYGGSDD EQGDNVFMFK QQDVIAEAFA GDDVVAEFQE EKKRVIDDED 790 800 810 820 830 840 DKEVDTTLPG WGEWAGAGSK PKNKKRKFIK KVKGVVNKDK RRDKNLQNVI INEKVNKKNL 850 860 870 880 890 KYQSSAVPFP FENREQYERS LRMPIGQEWT SRASHQELIK PRIMTKPGQV IDPLKAPFK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII." Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. , Skelton J., Walsh S.V., Whitehead S., Barrell B.G. Nature 387:90-93(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[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.
[4]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] 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]	"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB." Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R. Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z46660 Genomic DNA. Translation: CAA86645.1. BK006946 Genomic DNA. Translation: DAA09806.1.
PIR	S49634.
RefSeq	NP_013617.1. NM_001182452.1.
3D structure databases
ProteinModelPortal	Q04500.
ModBase	Search...
MobiDB	Search...
Protein-protein interaction databases
BioGrid	35050. 34 interactions.
DIP	DIP-6410N.
IntAct	Q04500. 3 interactions.
MINT	MINT-8285383.
STRING	4932.YML093W.
Proteomic databases
PaxDb	Q04500.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YML093W; YML093W; YML093W.
GeneID	854881.
KEGG	sce:YML093W.
Organism-specific databases
CYGD	YML093w.
SGD	S000004558. UTP14.
Phylogenomic databases
eggNOG	COG5644.
GeneTree	ENSGT00390000008142.
HOGENOM	HOG000074497.
KO	K14567.
OMA	ICIEAND.
OrthoDB	EOG7HQNJB.
Enzyme and pathway databases
BioCyc	YEAST:G3O-32678-MONOMER.
Gene expression databases
Genevestigator	Q04500.
Family and domain databases
InterPro	IPR006709. SSU_processome_Utp14. [Graphical view]
PANTHER	PTHR14150. PTHR14150. 1 hit.
Pfam	PF04615. Utp14. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	977828.
PRO	Q04500.

Entry information

Entry name

UTP14_YEAST

Accession

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

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	March 19, 2014
This is version 103 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program