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Protein

Tyrosine-protein phosphatase 3

Gene

PTP3

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

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.2 Publications

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei804 – 8041Phosphocysteine intermediatePROSITE-ProRule annotation

GO - Molecular functioni

  1. protein tyrosine phosphatase activity Source: SGD

GO - Biological processi

  1. inactivation of MAPK activity involved in conjugation with cellular fusion Source: SGD
  2. inactivation of MAPK activity involved in osmosensory signaling pathway Source: SGD
  3. peptidyl-tyrosine dephosphorylation Source: GOC
  4. protein dephosphorylation Source: SGD
  5. regulation of protein localization Source: SGD
  6. regulation of sporulation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Enzyme and pathway databases

BioCyciYEAST:G3O-30246-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein phosphatase 3 (EC:3.1.3.48)
Alternative name(s):
Protein-tyrosine phosphatase 3
Short name:
PTPase 3
Gene namesi
Name:PTP3
Ordered Locus Names:YER075C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome V

Organism-specific databases

CYGDiYER075c.
SGDiS000000877. PTP3.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: SGD
  2. nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 928928Tyrosine-protein phosphatase 3PRO_0000094857Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei75 – 751Phosphothreonine2 Publications
Modified residuei248 – 2481Phosphoserine1 Publication
Modified residuei297 – 2971Phosphoserine1 Publication
Modified residuei368 – 3681Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP40048.
PaxDbiP40048.
PeptideAtlasiP40048.

Expressioni

Gene expression databases

GenevestigatoriP40048.

Interactioni

Subunit structurei

Interacts with HOG1.1 Publication

Protein-protein interaction databases

BioGridi36819. 80 interactions.
DIPiDIP-2370N.
IntActiP40048. 2 interactions.
MINTiMINT-376861.
STRINGi4932.YER075C.

Structurei

3D structure databases

ProteinModelPortaliP40048.
SMRiP40048. Positions 529-886.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini111 – 232122RhodanesePROSITE-ProRule annotationAdd
BLAST
Domaini502 – 878377Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi308 – 3114Poly-Ser
Compositional biasi592 – 5976Poly-Thr
Compositional biasi702 – 71514Poly-AsnAdd
BLAST
Compositional biasi724 – 7329Poly-Asp

Sequence similaritiesi

Contains 1 rhodanese domain.PROSITE-ProRule annotation
Contains 1 tyrosine-protein phosphatase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5599.
GeneTreeiENSGT00690000103379.
HOGENOMiHOG000115788.
InParanoidiP40048.
KOiK01104.
OMAiLFKFQLP.
OrthoDBiEOG7CVQ79.

Family and domain databases

Gene3Di3.40.250.10. 1 hit.
3.90.190.10. 2 hits.
InterProiIPR029021. 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]
PfamiPF00581. Rhodanese. 1 hit.
PF00102. Y_phosphatase. 2 hits.
[Graphical view]
PRINTSiPR00700. PRTYPHPHTASE.
SMARTiSM00194. PTPc. 1 hit.
SM00450. RHOD. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 2 hits.
SSF52821. SSF52821. 1 hit.
PROSITEiPS50206. RHODANESE_3. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P40048-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKDSVDCPSI LPTDRTSVLS ETSTLVGSSS HVYSRHAPMN SYHNSMNSNI
60 70 80 90 100
YHSPKASSPL VSYKTSSPVL LKRATAPVLP SFKPKEQRYN KPQGCSLITA
110 120 130 140 150
VELGKIIETL PDEKVLLLDV RPFTEHAKSI ITNSIHVCLP STLLRRKNFT
160 170 180 190 200
FSKLLDNLTP SEQSVLKSKL AIDNLRIIIY DSTANQTESS VSLPCYGIAS
210 220 230 240 250
KLIEFDTNVK KTVSILMCGF PQFKILFPDH INTNTFNSDC ISSAEPKSPK
260 270 280 290 300
TNLMNSLHNT APHMTATTPL SSPQMNLKLK VPDDSRSDHS NFSSSPSPRN
310 320 330 340 350
VLSDSPMSSS SPISALFKFQ LPAPQTNINQ MFKFSQNEEI MGLETYLSAV
360 370 380 390 400
NIKEEHERWY NNDSAKKSLQ NFQFPKNQNS LEKDTNKDKL GFQIRYENLS
410 420 430 440 450
KNYEKEVIDS VIPEWFQHLM SIPKIELVSQ FQKLDFLEKR RLNHSVSFRK
460 470 480 490 500
KENSFILEKP SSYPEQLTST SSSTIMPPKF PDVNKVQKRS HSQPIFTQYS
510 520 530 540 550
KYKSMLSLES DSDSESDDVI ISSGVELGAK NRYKDIFPYE HSRVILKKGL
560 570 580 590 600
QSSKGIKHSH STSDGGILDN YINANYLSLP RFSVEQNSSF QTTTTTTRRV
610 620 630 640 650
RYIATQAPMP STVHDFYTCI LNNGVPLVLS LTNDFENGIE KCYRYWQEGN
660 670 680 690 700
YNGIHVKLLE KKILKMPSTT SMRKNTMGTQ NSSLYSAGVQ GNSSNYSTDN
710 720 730 740 750
DNDNDNNNNN NNNSNIAVTA AACDDDDDDD DDAILIRKIL LTYHDQEKPY
760 770 780 790 800
ELLQIQVKNW PDLGTLLNPI SILQAINVKN HIIDTLFARN YYQNDQLPTI
810 820 830 840 850
LVHCSAGCGR TGTLCTIDSI LSNFEMFEML QKEFVKLKYP AKLFDPISWT
860 870 880 890 900
INIFRKQRIS MVQNINQFIF IYDCLLFYFR LRLDDITERT DGDGSNKDNI
910 920
SLSALIEQIE KLEILQTFVD DKLKELPQ
Length:928
Mass (Da):105,224
Last modified:September 21, 2011 - v2
Checksum:i9BB710EDAF7E3940
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti717 – 7171A → P in AAB70811 (PubMed:9224718).Curated
Sequence conflicti717 – 7171A → P in AAB64614 (PubMed:9169868).Curated
Sequence conflicti738 – 7381K → Q in AAB70811 (PubMed:9224718).Curated
Sequence conflicti738 – 7381K → Q in AAB64614 (PubMed:9169868).Curated
Sequence conflicti857 – 8571Q → E in AAB70811 (PubMed:9224718).Curated
Sequence conflicti857 – 8571Q → E in AAB64614 (PubMed:9169868).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF006304 Genomic DNA. Translation: AAB70811.1.
U18814 Genomic DNA. Translation: AAB64614.1.
BK006939 Genomic DNA. Translation: DAA07735.2.
PIRiS50578.
RefSeqiNP_010998.2. NM_001178966.2.

Genome annotation databases

EnsemblFungiiYER075C; YER075C; YER075C.
GeneIDi856807.
KEGGisce:YER075C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF006304 Genomic DNA. Translation: AAB70811.1.
U18814 Genomic DNA. Translation: AAB64614.1.
BK006939 Genomic DNA. Translation: DAA07735.2.
PIRiS50578.
RefSeqiNP_010998.2. NM_001178966.2.

3D structure databases

ProteinModelPortaliP40048.
SMRiP40048. Positions 529-886.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36819. 80 interactions.
DIPiDIP-2370N.
IntActiP40048. 2 interactions.
MINTiMINT-376861.
STRINGi4932.YER075C.

Proteomic databases

MaxQBiP40048.
PaxDbiP40048.
PeptideAtlasiP40048.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYER075C; YER075C; YER075C.
GeneIDi856807.
KEGGisce:YER075C.

Organism-specific databases

CYGDiYER075c.
SGDiS000000877. PTP3.

Phylogenomic databases

eggNOGiCOG5599.
GeneTreeiENSGT00690000103379.
HOGENOMiHOG000115788.
InParanoidiP40048.
KOiK01104.
OMAiLFKFQLP.
OrthoDBiEOG7CVQ79.

Enzyme and pathway databases

BioCyciYEAST:G3O-30246-MONOMER.

Miscellaneous databases

NextBioi983065.

Gene expression databases

GenevestigatoriP40048.

Family and domain databases

Gene3Di3.40.250.10. 1 hit.
3.90.190.10. 2 hits.
InterProiIPR029021. 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]
PfamiPF00581. Rhodanese. 1 hit.
PF00102. Y_phosphatase. 2 hits.
[Graphical view]
PRINTSiPR00700. PRTYPHPHTASE.
SMARTiSM00194. PTPc. 1 hit.
SM00450. RHOD. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 2 hits.
SSF52821. SSF52821. 1 hit.
PROSITEiPS50206. RHODANESE_3. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. 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. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  7. 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].

Entry informationi

Entry nameiPTP3_YEAST
AccessioniPrimary (citable) accession number: P40048
Secondary accession number(s): D3DLY1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: September 21, 2011
Last modified: January 7, 2015
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 768 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 V
    Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

External Data

Dasty 3

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 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.