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Protein

Protein PXR1

Gene

PXR1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in rRNA-processing at A0, A1 and A2 sites through its action in U18 and U24 snoRNA 3'-end final trimming. Negative regulator of telomerase through competition for binding to EST2 with TLC1.3 Publications

GO - Molecular functioni

  • enzyme activator activity Source: SGD
  • nucleic acid binding Source: InterPro
  • telomerase inhibitor activity Source: SGD

GO - Biological processi

  • box C/D snoRNA 3'-end processing Source: SGD
  • negative regulation of telomerase activity Source: GOC
  • negative regulation of telomere maintenance via telomerase Source: SGD
  • positive regulation of catalytic activity Source: GOC
  • rRNA processing Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Ribosome biogenesis, rRNA processing

Enzyme and pathway databases

BioCyciYEAST:G3O-30943-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein PXR1
Alternative name(s):
G-patch nucleolar protein
PinX1-related protein 1
Gene namesi
Name:PXR1
Synonyms:GNO1
Ordered Locus Names:YGR280C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGR280C.
SGDiS000003512. PXR1.

Subcellular locationi

GO - Cellular componenti

  • nucleolus Source: SGD
  • nucleoplasm Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 271271Protein PXR1PRO_0000202871Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei230 – 2301PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP53335.
PeptideAtlasiP53335.

PTM databases

iPTMnetiP53335.

Interactioni

Subunit structurei

Interacts with EST2.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
PRP43P531313EBI-23652,EBI-505

Protein-protein interaction databases

BioGridi33530. 33 interactions.
DIPiDIP-4308N.
IntActiP53335. 10 interactions.
MINTiMINT-516266.

Structurei

3D structure databases

ProteinModelPortaliP53335.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 7248G-patchPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi139 – 22688Lys-richAdd
BLAST

Sequence similaritiesi

Belongs to the PINX1 family.Curated
Contains 1 G-patch domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00450000040279.
HOGENOMiHOG000048630.
InParanoidiP53335.
KOiK11135.
OMAiLNEIFMI.
OrthoDBiEOG7RV9TT.

Family and domain databases

InterProiIPR000467. G_patch_dom.
[Graphical view]
PfamiPF01585. G-patch. 1 hit.
[Graphical view]
SMARTiSM00443. G_patch. 1 hit.
[Graphical view]
PROSITEiPS50174. G_PATCH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P53335-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGLAATRTKQ RFGLDPRNTA WSNDTSRFGH QFLEKFGWKP GMGLGLSPMN
60 70 80 90 100
SNTSHIKVSI KDDNVGLGAK LKRKDKKDEF DNGECAGLDV FQRILGRLNG
110 120 130 140 150
KESKISEELD TQRKQKIIDG KWGIHFVKGE VLASTWDPKT HKLRNYSNAK
160 170 180 190 200
KRKREGDDSE DEDDDDKEDK DSDKKKHKKH KKHKKDKKKD KKDKKEHKKH
210 220 230 240 250
KKEEKRLKKE KRAEKTKETK KTSKLKSSES ASNIPDAVNT RLSVRSKWIK
260 270
QKRAALMDSK ALNEIFMITN D
Length:271
Mass (Da):31,312
Last modified:October 1, 1996 - v1
Checksum:iD5AB6EB2C129922D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti148 – 1481N → H in AAM18461 (PubMed:11701125).Curated
Sequence conflicti151 – 1511K → N in AAM18461 (PubMed:11701125).Curated
Sequence conflicti165 – 1673DDK → ADQ in AAM18461 (PubMed:11701125).Curated
Sequence conflicti193 – 1931D → A in AAM18461 (PubMed:11701125).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF432905 mRNA. Translation: AAM18461.1.
Z73065 Genomic DNA. Translation: CAA97311.1.
AY558384 Genomic DNA. Translation: AAS56710.1.
BK006941 Genomic DNA. Translation: DAA08368.1.
PIRiS64615.
RefSeqiNP_011796.1. NM_001181409.1.

Genome annotation databases

EnsemblFungiiYGR280C; YGR280C; YGR280C.
GeneIDi853197.
KEGGisce:YGR280C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF432905 mRNA. Translation: AAM18461.1.
Z73065 Genomic DNA. Translation: CAA97311.1.
AY558384 Genomic DNA. Translation: AAS56710.1.
BK006941 Genomic DNA. Translation: DAA08368.1.
PIRiS64615.
RefSeqiNP_011796.1. NM_001181409.1.

3D structure databases

ProteinModelPortaliP53335.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33530. 33 interactions.
DIPiDIP-4308N.
IntActiP53335. 10 interactions.
MINTiMINT-516266.

PTM databases

iPTMnetiP53335.

Proteomic databases

MaxQBiP53335.
PeptideAtlasiP53335.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGR280C; YGR280C; YGR280C.
GeneIDi853197.
KEGGisce:YGR280C.

Organism-specific databases

EuPathDBiFungiDB:YGR280C.
SGDiS000003512. PXR1.

Phylogenomic databases

GeneTreeiENSGT00450000040279.
HOGENOMiHOG000048630.
InParanoidiP53335.
KOiK11135.
OMAiLNEIFMI.
OrthoDBiEOG7RV9TT.

Enzyme and pathway databases

BioCyciYEAST:G3O-30943-MONOMER.

Miscellaneous databases

NextBioi973362.
PROiP53335.

Family and domain databases

InterProiIPR000467. G_patch_dom.
[Graphical view]
PfamiPF01585. G-patch. 1 hit.
[Graphical view]
SMARTiSM00443. G_patch. 1 hit.
[Graphical view]
PROSITEiPS50174. G_PATCH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The Pin2/TRF1-interacting protein PinX1 is a potent telomerase inhibitor."
    Zhou X.Z., Lu K.P.
    Cell 107:347-359(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Sequence analysis of a near-subtelomeric 35.4 kb DNA segment on the right arm of chromosome VII from Saccharomyces cerevisiae carrying the MAL1 locus reveals 15 complete open reading frames, including ZUO1, BGL2 and BIO2 genes and an ABC transporter gene."
    Volckaert G., Voet M., Robben J.
    Yeast 13:251-259(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  6. "The yeast homolog of human PinX1 is involved in rRNA and small nucleolar RNA maturation, not in telomere elongation inhibition."
    Guglielmi B., Werner M.
    J. Biol. Chem. 277:35712-35719(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. "Nucleolar protein PinX1p regulates telomerase by sequestering its protein catalytic subunit in an inactive complex lacking telomerase RNA."
    Lin J., Blackburn E.H.
    Genes Dev. 18:387-396(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH EST2.
  10. "The budding yeast rRNA and ribosome biosynthesis (RRB) regulon contains over 200 genes."
    Wade C.H., Umbarger M.A., McAlear M.A.
    Yeast 23:293-306(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "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-230, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPXR1_YEAST
AccessioniPrimary (citable) accession number: P53335
Secondary accession number(s): D6VV57, Q8TG89
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 11, 2016
This is version 119 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 3850 molecules/cell in log phase SD medium.1 Publication

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 VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: 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.