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P25635 (PWP2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Periodic tryptophan protein 2
Alternative name(s):
U three protein 1
U3 small nucleolar RNA-associated protein 1
Short name=U3 snoRNA-associated protein 1
Gene names
Name:PWP2
Synonyms:UTP1
Ordered Locus Names:YCR057C
ORF Names:YCR55C/YCR57C/YCR58C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length923 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for bud-site selection and cell separation. Also involved in nucleolar processing of pre-18S ribosomal RNA. Ref.1 Ref.5

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.5

Subcellular location

Nucleusnucleolus Ref.5.

Miscellaneous

Present with 16700 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the WD repeat PWP2 family.

Contains 14 WD repeats.

Ontologies

Keywords
   Biological processRibosome biogenesis
rRNA processing
   Cellular componentNucleus
   DomainRepeat
WD repeat
   Molecular functionRibonucleoprotein
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcytokinesis, completion of separation

Inferred from mutant phenotype Ref.1. Source: SGD

endonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)

Inferred from mutant phenotype PubMed 15231838PubMed 15489292PubMed 15590835. 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 15231838PubMed 15489292PubMed 15590835. 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 15231838PubMed 15489292PubMed 15590835. Source: SGD

establishment of cell polarity

Inferred from mutant phenotype Ref.1. Source: SGD

maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)

Inferred from mutant phenotype Ref.5. Source: SGD

   Cellular_component90S preribosome

Inferred from direct assay PubMed 15231838. Source: SGD

Pwp2p-containing subcomplex of 90S preribosome

Inferred from direct assay PubMed 15231838PubMed 17515605. Source: SGD

cytoplasm

Inferred from direct assay Ref.1. Source: SGD

nucleolus

Inferred from direct assay Ref.5PubMed 12150911. Source: SGD

small-subunit processome

Inferred from direct assay Ref.5. Source: SGD

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 11805826PubMed 12150911PubMed 16429126PubMed 18467557. Source: IntAct

snoRNA binding

Inferred from physical interaction Ref.5. Source: SGD

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

DIP2Q122206EBI-14332,EBI-5896
UTP21Q060787EBI-14332,EBI-359

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 923923Periodic tryptophan protein 2
PRO_0000051179

Regions

Repeat12 – 5241WD 1
Repeat53 – 9341WD 2
Repeat94 – 13239WD 3
Repeat144 – 18340WD 4
Repeat189 – 22840WD 5
Repeat258 – 29740WD 6
Repeat300 – 34041WD 7
Repeat343 – 38240WD 8
Repeat385 – 42440WD 9
Repeat428 – 47043WD 10
Repeat471 – 51040WD 11
Repeat513 – 55240WD 12
Repeat575 – 61440WD 13
Repeat676 – 71439WD 14
Compositional bias226 – 24015Asp/Glu-rich (acidic)
Compositional bias862 – 92362Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue2251Phosphoserine Ref.9
Modified residue2321Phosphoserine Ref.7 Ref.8 Ref.9
Modified residue6511Phosphoserine Ref.7 Ref.8 Ref.9
Modified residue6641Phosphoserine Ref.8
Modified residue9121Phosphoserine Ref.7 Ref.8 Ref.9
Modified residue9131Phosphoserine Ref.7 Ref.8 Ref.9

Sequences

Sequence LengthMass (Da)Tools
P25635 [UniParc].

Last modified February 1, 1995. Version 2.
Checksum: CBEE4720F81378B6

FASTA923103,983
        10         20         30         40         50         60 
MKSDFKFSNL LGTVYRQGNI TFSDDGKQLL SPVGNRVSVF DLINNKSFTF EYEHRKNIAA 

        70         80         90        100        110        120 
IDLNKQGTLL ISIDEDGRAI LVNFKARNVL HHFNFKEKCS AVKFSPDGRL FALASGRFLQ 

       130        140        150        160        170        180 
IWKTPDVNKD RQFAPFVRHR VHAGHFQDIT SLTWSQDSRF ILTTSKDLSA KIWSVDSEEK 

       190        200        210        220        230        240 
NLAATTFNGH RDYVMGAFFS HDQEKIYTVS KDGAVFVWEF TKRPSDDDDN ESEDDDKQEE 

       250        260        270        280        290        300 
VDISKYSWRI TKKHFFYANQ AKVKCVTFHP ATRLLAVGFT SGEFRLYDLP DFTLIQQLSM 

       310        320        330        340        350        360 
GQNPVNTVSV NQTGEWLAFG SSKLGQLLVY EWQSESYILK QQGHFDSTNS LAYSPDGSRV 

       370        380        390        400        410        420 
VTASEDGKIK VWDITSGFCL ATFEEHTSSV TAVQFAKRGQ VMFSSSLDGT VRAWDLIRYR 

       430        440        450        460        470        480 
NFRTFTGTER IQFNCLAVDP SGEVVCAGSL DNFDIHVWSV QTGQLLDALS GHEGPVSCLS 

       490        500        510        520        530        540 
FSQENSVLAS ASWDKTIRIW SIFGRSQQVE PIEVYSDVLA LSMRPDGKEV AVSTLKGQIS 

       550        560        570        580        590        600 
IFNIEDAKQV GNIDCRKDII SGRFNQDRFT AKNSERSKFF TTIHYSFDGM AIVAGGNNNS 

       610        620        630        640        650        660 
ICLYDVPNEV LLKRFIVSRN MALNGTLEFL NSKKMTEAGS LDLIDDAGEN SDLEDRIDNS 

       670        680        690        700        710        720 
LPGSQRGGDL STRKMRPEVR VTSVQFSPTA NAFAAASTEG LLIYSTNDTI LFDPFDLDVD 

       730        740        750        760        770        780 
VTPHSTVEAL REKQFLNALV MAFRLNEEYL INKVYEAIPI KEIPLVASNI PAIYLPRILK 

       790        800        810        820        830        840 
FIGDFAIESQ HIEFNLIWIK ALLSASGGYI NEHKYLFSTA MRSIQRFIVR VAKEVVNTTT 

       850        860        870        880        890        900 
DNKYTYRFLV STDGSMEDGA ADDDEVLLKD DADEDNEENE ENDVVMESDD EEGWIGFNGK 

       910        920 
DNKLPLSNEN DSSDEEENEK ELP 

« Hide

References

« Hide 'large scale' references
[1]"PWP2, a member of the WD-repeat family of proteins, is an essential Saccharomyces cerevisiae gene involved in cell separation."
Shafaatian R., Payton M.A., Reid J.D.
Mol. Gen. Genet. 252:101-114(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
Strain: ATCC 204511 / S288c / AB972.
[2]"The complete DNA sequence of yeast chromosome III."
Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M. expand/collapse author list , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.
Nature 357:38-46(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Gromadka R.
Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[4]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"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.
[6]"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].
[7]"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-232; SER-651; SER-912 AND SER-913, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[8]"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-232; SER-651; SER-664; SER-912 AND SER-913, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"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-225; SER-232; SER-651; SER-912 AND SER-913, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X78964 Genomic DNA. Translation: CAA55558.1.
X59720 Genomic DNA. Translation: CAA42286.1.
BK006937 Genomic DNA. Translation: DAA07532.1.
PIRS44226.
RefSeqNP_009984.1. NM_001178769.1.

3D structure databases

ProteinModelPortalP25635.
SMRP25635. Positions 19-723.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31035. 118 interactions.
DIPDIP-1868N.
IntActP25635. 115 interactions.
MINTMINT-392472.

Proteomic databases

MaxQBP25635.
PaxDbP25635.
PeptideAtlasP25635.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYCR057C; YCR057C; YCR057C.
GeneID850422.
KEGGsce:YCR057C.

Organism-specific databases

CYGDYCR057c.
SGDS000000653. PWP2.

Phylogenomic databases

eggNOGCOG2319.
GeneTreeENSGT00550000074981.
HOGENOMHOG000160363.
KOK14558.
OMAIRAWDLI.
OrthoDBEOG7BCNM6.

Enzyme and pathway databases

BioCycYEAST:G3O-29363-MONOMER.

Gene expression databases

GenevestigatorP25635.

Family and domain databases

Gene3D2.130.10.10. 4 hits.
InterProIPR020472. G-protein_beta_WD-40_rep.
IPR027145. PWP2.
IPR011047. Quinonprotein_ADH-like_supfam.
IPR007148. SSU_processome_Utp12.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PANTHERPTHR19858. PTHR19858. 1 hit.
PfamPF04003. Utp12. 1 hit.
PF00400. WD40. 6 hits.
[Graphical view]
PRINTSPR00320. GPROTEINBRPT.
SMARTSM00320. WD40. 13 hits.
[Graphical view]
SUPFAMSSF50978. SSF50978. 3 hits.
SSF50998. SSF50998. 2 hits.
PROSITEPS00678. WD_REPEATS_1. 3 hits.
PS50082. WD_REPEATS_2. 5 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio965992.
PROP25635.

Entry information

Entry namePWP2_YEAST
AccessionPrimary (citable) accession number: P25635
Secondary accession number(s): D6VR63, P25633, P25636
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: February 1, 1995
Last modified: June 11, 2014
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome III

Yeast (Saccharomyces cerevisiae) chromosome III: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families