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P40048 (PTP3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 131. 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:
Tyrosine-protein phosphatase 3

EC=3.1.3.48
Alternative name(s):
Protein-tyrosine phosphatase 3
Short name=PTPase 3
Gene names
Name:PTP3
Ordered Locus Names:YER075C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length928 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Major phosphatase responsible for tyrosine dephosphorylation of MAP kinases FUS3 and HOG1 to inactivate their activity; it also has important roles, along with MSG5, in the inactivation of FUS3 following pheromone stimulation. Ref.4 Ref.5

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Subunit structure

Interacts with HOG1. Ref.5

Subcellular location

Cytoplasm Ref.6.

Miscellaneous

Present with 768 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the protein-tyrosine phosphatase family. Non-receptor class subfamily.

Contains 1 rhodanese domain.

Contains 1 tyrosine-protein phosphatase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 928928Tyrosine-protein phosphatase 3
PRO_0000094857

Regions

Domain111 – 232122Rhodanese
Domain502 – 878377Tyrosine-protein phosphatase
Compositional bias308 – 3114Poly-Ser
Compositional bias592 – 5976Poly-Thr
Compositional bias702 – 71514Poly-Asn
Compositional bias724 – 7329Poly-Asp

Sites

Active site8041Phosphocysteine intermediate By similarity

Amino acid modifications

Modified residue751Phosphothreonine Ref.8 Ref.9
Modified residue2481Phosphoserine Ref.11
Modified residue2971Phosphoserine Ref.11
Modified residue3681Phosphoserine Ref.10 Ref.11

Experimental info

Sequence conflict7171A → P in AAB70811. Ref.1
Sequence conflict7171A → P in AAB64614. Ref.2
Sequence conflict7381K → Q in AAB70811. Ref.1
Sequence conflict7381K → Q in AAB64614. Ref.2
Sequence conflict8571Q → E in AAB70811. Ref.1
Sequence conflict8571Q → E in AAB64614. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P40048 [UniParc].

Last modified September 21, 2011. Version 2.
Checksum: 9BB710EDAF7E3940

FASTA928105,224
        10         20         30         40         50         60 
MKDSVDCPSI LPTDRTSVLS ETSTLVGSSS HVYSRHAPMN SYHNSMNSNI YHSPKASSPL 

        70         80         90        100        110        120 
VSYKTSSPVL LKRATAPVLP SFKPKEQRYN KPQGCSLITA VELGKIIETL PDEKVLLLDV 

       130        140        150        160        170        180 
RPFTEHAKSI ITNSIHVCLP STLLRRKNFT FSKLLDNLTP SEQSVLKSKL AIDNLRIIIY 

       190        200        210        220        230        240 
DSTANQTESS VSLPCYGIAS KLIEFDTNVK KTVSILMCGF PQFKILFPDH INTNTFNSDC 

       250        260        270        280        290        300 
ISSAEPKSPK TNLMNSLHNT APHMTATTPL SSPQMNLKLK VPDDSRSDHS NFSSSPSPRN 

       310        320        330        340        350        360 
VLSDSPMSSS SPISALFKFQ LPAPQTNINQ MFKFSQNEEI MGLETYLSAV NIKEEHERWY 

       370        380        390        400        410        420 
NNDSAKKSLQ NFQFPKNQNS LEKDTNKDKL GFQIRYENLS KNYEKEVIDS VIPEWFQHLM 

       430        440        450        460        470        480 
SIPKIELVSQ FQKLDFLEKR RLNHSVSFRK KENSFILEKP SSYPEQLTST SSSTIMPPKF 

       490        500        510        520        530        540 
PDVNKVQKRS HSQPIFTQYS KYKSMLSLES DSDSESDDVI ISSGVELGAK NRYKDIFPYE 

       550        560        570        580        590        600 
HSRVILKKGL QSSKGIKHSH STSDGGILDN YINANYLSLP RFSVEQNSSF QTTTTTTRRV 

       610        620        630        640        650        660 
RYIATQAPMP STVHDFYTCI LNNGVPLVLS LTNDFENGIE KCYRYWQEGN YNGIHVKLLE 

       670        680        690        700        710        720 
KKILKMPSTT SMRKNTMGTQ NSSLYSAGVQ GNSSNYSTDN DNDNDNNNNN NNNSNIAVTA 

       730        740        750        760        770        780 
AACDDDDDDD DDAILIRKIL LTYHDQEKPY ELLQIQVKNW PDLGTLLNPI SILQAINVKN 

       790        800        810        820        830        840 
HIIDTLFARN YYQNDQLPTI LVHCSAGCGR TGTLCTIDSI LSNFEMFEML QKEFVKLKYP 

       850        860        870        880        890        900 
AKLFDPISWT INIFRKQRIS MVQNINQFIF IYDCLLFYFR LRLDDITERT DGDGSNKDNI 

       910        920 
SLSALIEQIE KLEILQTFVD DKLKELPQ 

« Hide

References

« Hide 'large scale' references
[1]"Differential regulation of FUS3 MAP kinase by tyrosine-specific phosphatases PTP2/PTP3 and dual-specificity phosphatase MSG5 in Saccharomyces cerevisiae."
Zhan X.-L., Deschenes R.J., Guan K.-L.
Genes Dev. 11:1690-1702(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome V."
Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W. expand/collapse author list , Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.
Nature 387:78-81(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"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, SEQUENCE REVISION TO 717; 738 AND 857.
Strain: ATCC 204508 / S288c.
[4]"Regulation of the Saccharomyces cerevisiae HOG1 mitogen-activated protein kinase by the PTP2 and PTP3 protein tyrosine phosphatases."
Wurgler-Murphy S.M., Maeda T., Witten E.A., Saito H.
Mol. Cell. Biol. 17:1289-1297(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[5]"Two protein-tyrosine phosphatases inactivate the osmotic stress response pathway in yeast by targeting the mitogen-activated protein kinase, Hog1."
Jacoby T., Flanagan H., Faykin A., Seto A.G., Mattison C.P., Ota I.M.
J. Biol. Chem. 272:17749-17755(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH HOG1.
[6]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[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]"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 THR-75, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[9]"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 THR-75, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"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-368, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"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-248; SER-297 AND SER-368, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF006304 Genomic DNA. Translation: AAB70811.1.
U18814 Genomic DNA. Translation: AAB64614.1.
BK006939 Genomic DNA. Translation: DAA07735.2.
PIRS50578.
RefSeqNP_010998.2. NM_001178966.2.

3D structure databases

ProteinModelPortalP40048.
SMRP40048. Positions 529-877.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36819. 79 interactions.
DIPDIP-2370N.
IntActP40048. 2 interactions.
MINTMINT-376861.
STRING4932.YER075C.

Proteomic databases

MaxQBP40048.
PaxDbP40048.
PeptideAtlasP40048.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYER075C; YER075C; YER075C.
GeneID856807.
KEGGsce:YER075C.

Organism-specific databases

CYGDYER075c.
SGDS000000877. PTP3.

Phylogenomic databases

eggNOGCOG5599.
GeneTreeENSGT00690000103379.
HOGENOMHOG000115788.
KOK01104.
OMALFKFQLP.
OrthoDBEOG7CVQ79.

Enzyme and pathway databases

BioCycYEAST:G3O-30246-MONOMER.

Gene expression databases

GenevestigatorP40048.

Family and domain databases

Gene3D3.40.250.10. 1 hit.
3.90.190.10. 2 hits.
InterProIPR029021. Prot-tyrosine_phosphatase-like.
IPR001763. Rhodanese-like_dom.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamPF00581. Rhodanese. 1 hit.
PF00102. Y_phosphatase. 2 hits.
[Graphical view]
PRINTSPR00700. PRTYPHPHTASE.
SMARTSM00194. PTPc. 1 hit.
SM00450. RHOD. 1 hit.
[Graphical view]
SUPFAMSSF52799. SSF52799. 2 hits.
SSF52821. SSF52821. 1 hit.
PROSITEPS50206. RHODANESE_3. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio983065.

Entry information

Entry namePTP3_YEAST
AccessionPrimary (citable) accession number: P40048
Secondary accession number(s): D3DLY1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: September 21, 2011
Last modified: July 9, 2014
This is version 131 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 V

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

Yeast

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

SIMILARITY comments

Index of protein domains and families