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P40048

- PTP3_YEAST

UniProt

P40048 - PTP3_YEAST

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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: 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 .
PIRi S50578.
RefSeqi NP_010998.2. NM_001178966.2.

3D structure databases

ProteinModelPortali P40048.
SMRi P40048. Positions 529-886.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 36819. 80 interactions.
DIPi DIP-2370N.
IntActi P40048. 2 interactions.
MINTi MINT-376861.
STRINGi 4932.YER075C.

Proteomic databases

MaxQBi P40048.
PaxDbi P40048.
PeptideAtlasi P40048.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YER075C ; YER075C ; YER075C .
GeneIDi 856807.
KEGGi sce:YER075C.

Organism-specific databases

CYGDi YER075c.
SGDi S000000877. PTP3.

Phylogenomic databases

eggNOGi COG5599.
GeneTreei ENSGT00690000103379.
HOGENOMi HOG000115788.
InParanoidi P40048.
KOi K01104.
OMAi LFKFQLP.
OrthoDBi EOG7CVQ79.

Enzyme and pathway databases

BioCyci YEAST:G3O-30246-MONOMER.

Miscellaneous databases

NextBioi 983065.

Gene expression databases

Genevestigatori P40048.

Family and domain databases

Gene3Di 3.40.250.10. 1 hit.
3.90.190.10. 2 hits.
InterProi IPR029021. 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 ]
Pfami PF00581. Rhodanese. 1 hit.
PF00102. Y_phosphatase. 2 hits.
[Graphical view ]
PRINTSi PR00700. PRTYPHPHTASE.
SMARTi SM00194. PTPc. 1 hit.
SM00450. RHOD. 1 hit.
[Graphical view ]
SUPFAMi SSF52799. SSF52799. 2 hits.
SSF52821. SSF52821. 1 hit.
PROSITEi PS50206. RHODANESE_3. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 133 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