Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P32945 (PPQ1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 128. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein phosphatase PPQ

EC=3.1.3.16
Gene names
Name:PPQ1
Synonyms:SAL6
Ordered Locus Names:YPL179W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length549 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Phosphatase involved in the regulation of protein synthesis. Affects translational accuracy.

Catalytic activity

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Cofactor

Binds 1 iron ion per subunit By similarity.

Binds 1 manganese ion per subunit By similarity.

Miscellaneous

Present with 319 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the PPP phosphatase family. PP-Z subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 549549Serine/threonine-protein phosphatase PPQ
PRO_0000058893

Regions

Compositional bias113 – 219107Ser-rich

Sites

Active site3621Proton donor By similarity
Metal binding3011Iron By similarity
Metal binding3031Iron By similarity
Metal binding3291Iron By similarity
Metal binding3291Manganese By similarity
Metal binding3611Manganese By similarity
Metal binding4101Manganese By similarity
Metal binding4851Manganese By similarity

Sequences

Sequence LengthMass (Da)Tools
P32945 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: 1E26D05E2865A8C1

FASTA54961,420
        10         20         30         40         50         60 
MRRSPSRSNN NFAVPNCSTN SNSSQQQLTT PSDDLNSNEP NDPDDSRSLP TIKKFNNKHS 

        70         80         90        100        110        120 
INNYNTLASA GKNNNNKRAS NDNLLIPGEN AHKQKIYTKD ENLKSLYLDI DVSVAKALSS 

       130        140        150        160        170        180 
SATAPKLINT ARTSSTTTAT TSNNILTSPS YRESNYSSPS SYSFSSYYSS ATSASSSTSS 

       190        200        210        220        230        240 
FLKSSGLSSR VKSPSSSVKA GSFGAPSSPT SGIPNPKSSK KPIFLRRYSH DTSSNEGLDI 

       250        260        270        280        290        300 
DVAIEKLLQV GESREITKTS KKKNFPFHSW EIQLICYHAR EIFLNQPTLL RLQAPIKVVG 

       310        320        330        340        350        360 
DVHGQFNDLL RILKLSGVPS DTNYLFLGDY VDRGKNSLET ILLLLCYKIK YKDNFFMLRG 

       370        380        390        400        410        420 
NHESANVTKM YGFYDECKRR LSSKVWKMFV DVFNTLPLAA IIQDKIFCVH GGISPDLHDM 

       430        440        450        460        470        480 
KQIEKVARPT DIPESGLVTD LLWSDPDPQV TDWSENDRGV SYTFSKRNVL DFCAKFKFDL 

       490        500        510        520        530        540 
ILRGHMVVED GYEFFARKKF VTIFSAPNYC GEFHNWGAVM SVTTGMMCSF ELLKPRALKN 


KKKLYKTKV 

« Hide

References

« Hide 'large scale' references
[1]"PPQ, a novel protein phosphatase containing a Ser + Asn-rich amino-terminal domain, is involved in the regulation of protein synthesis."
Chen M.X., Chen Y.H., Cohen P.T.W.
Eur. J. Biochem. 218:689-699(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]Erratum
Chen M.X., Chen Y.H., Cohen P.T.W.
Eur. J. Biochem. 221:1133-1133(1994)
[3]"The yeast translational allosuppressor, SAL6: a new member of the PP1-like phosphatase family with a long serine-rich N-terminal extension."
Vincent A., Newnam G.P., Liebman S.W.
Genetics 138:597-607(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: S288c / GRF88.
[4]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. expand/collapse author list , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[6]"Polymerase chain reactions using Saccharomyces, Drosophila and human DNA predict a large family of protein serine/threonine phosphatases."
Chen M.X., Chen Y.H., Cohen P.T.W.
FEBS Lett. 306:54-58(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 305-328.
[7]"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].
[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: 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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X75485 Genomic DNA. Translation: CAA53214.1.
U00795 Genomic DNA. Translation: AAC48924.1.
Z73535 Genomic DNA. Translation: CAA97886.1.
S39958 Genomic DNA. Translation: AAB22461.1.
BK006949 Genomic DNA. Translation: DAA11255.1.
PIRS39533.
RefSeqNP_015146.1. NM_001183993.1.

3D structure databases

ProteinModelPortalP32945.
SMRP32945. Positions 238-535.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36003. 47 interactions.
DIPDIP-5504N.
IntActP32945. 3 interactions.
MINTMINT-564004.
STRING4932.YPL179W.

Proteomic databases

PaxDbP32945.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYPL179W; YPL179W; YPL179W.
GeneID855923.
KEGGsce:YPL179W.

Organism-specific databases

CYGDYPL179w.
SGDS000006100. PPQ1.

Phylogenomic databases

eggNOGCOG0639.
GeneTreeENSGT00710000107291.
HOGENOMHOG000172697.
KOK06269.
OrthoDBEOG7M3J8G.

Enzyme and pathway databases

BioCycYEAST:G3O-34074-MONOMER.

Gene expression databases

GenevestigatorP32945.

Family and domain databases

InterProIPR004843. Calcineurin-like_PHP_apaH.
IPR011159. PPPtase_PPZ.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamPF00149. Metallophos. 1 hit.
[Graphical view]
PIRSFPIRSF000909. PPPtase_PPZ. 1 hit.
PRINTSPR00114. STPHPHTASE.
SMARTSM00156. PP2Ac. 1 hit.
[Graphical view]
PROSITEPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio980649.

Entry information

Entry namePPQ1_YEAST
AccessionPrimary (citable) accession number: P32945
Secondary accession number(s): D6W3I9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: April 16, 2014
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XVI

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

Yeast

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

SIMILARITY comments

Index of protein domains and families