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Protein

Protein-tyrosine-phosphatase PTP1

Gene

PTP1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Protein-tyrosine-phosphatase that dephosphorylates and probably inhibits MPK6 in non-oxidative stress conditions. In association with MKP1, represses salicylic acid (SA) and camalexin biosynthesis, thus modulating defense response. May also repress MPK3. Dephosphorylates and inactivates MPK4 in vitro.4 Publications

Catalytic activityi

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

Enzyme regulationi

Inhibited by hydrogen peroxide.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei234 – 2341SubstrateCurated
Active sitei265 – 2651Phosphocysteine intermediate
Binding sitei311 – 3111SubstrateBy similarity

GO - Molecular functioni

  • MAP kinase tyrosine phosphatase activity Source: UniProtKB
  • protein tyrosine phosphatase activity Source: TAIR

GO - Biological processi

  • defense response Source: UniProtKB-KW
  • intracellular signal transduction Source: TAIR
  • negative regulation of defense response Source: UniProtKB
  • peptidyl-tyrosine dephosphorylation Source: GOC
  • peptidyl-tyrosine dephosphorylation involved in inactivation of protein kinase activity Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Plant defense

Enzyme and pathway databases

BioCyciARA:AT1G71860-MONOMER.
ARA:GQT-335-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein-tyrosine-phosphatase PTP1 (EC:3.1.3.48)
Alternative name(s):
Protein tyrosine phosphatase 1
Short name:
AtPTP1
Gene namesi
Name:PTP1
Ordered Locus Names:At1g71860
ORF Names:F14O23.24
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G71860.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • nucleus Source: UniProtKB
  • plasma membrane Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

No visible phenotype under normal growth conditions.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi234 – 2341D → A: Loss of activity. 1 Publication
Mutagenesisi265 – 2651C → S: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 340340Protein-tyrosine-phosphatase PTP1PRO_0000417329Add
BLAST

Proteomic databases

PRIDEiO82656.

Expressioni

Tissue specificityi

Expressed in roots, stems and flowers, and at low levels in leaves.1 Publication

Inductioni

By salt treatment. Down-regulated by cold.1 Publication

Gene expression databases

ExpressionAtlasiO82656. baseline and differential.

Interactioni

Subunit structurei

Interacts with MPK6.1 Publication

Protein-protein interaction databases

BioGridi28736. 4 interactions.
IntActiO82656. 1 interaction.
MINTiMINT-8390809.
STRINGi3702.AT1G71860.1.

Structurei

3D structure databases

ProteinModelPortaliO82656.
SMRiO82656. Positions 42-328.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini58 – 326269Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni265 – 2717Substrate bindingBy similarity

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000243992.
InParanoidiO82656.
OMAiPDSIAHE.
PhylomeDBiO82656.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamiPF00102. Y_phosphatase. 1 hit.
[Graphical view]
PRINTSiPR00700. PRTYPHPHTASE.
SMARTiSM00194. PTPc. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
PROSITEiPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: O82656-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MATGKTSSAA NLFTGSTRFD LSSADSPPSK LSLSSDQLNH CHQALGVFRG
60 70 80 90 100
KIQNPDSIAH EFTGLQANRM WPSELLLNST VAMNSVNVEK NRYSDVVPFD
110 120 130 140 150
KNRIVLNPCK DSSAKGYVNA SLIKTSESES ISQFIATQGP LPHTMEDFWE
160 170 180 190 200
MVIQQHCPII VMLTRLVDNN RTVKCGDYFQ DEDGPREFGN ISLTTKWIKT
210 220 230 240 250
TDTSLMLRNL EVNYKETEDQ PMSVLHIQYP EWPDHGVPKD TVAVREILKR
260 270 280 290 300
LYQVPPSLGP IIVHCSAGIG RTGTYCAIHN TIQRILAGDM SALDLAKTVA
310 320 330 340
LFRKQRIGMV QTMDQYFFCY NAIVDELEDL TAGTNAGTSS
Length:340
Mass (Da):37,799
Last modified:November 1, 1998 - v1
Checksum:i7885C03A664CA02D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti147 – 1471D → A in AAC68859 (PubMed:9596642).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF055635 mRNA. Translation: AAC68859.1.
AJ006309 Genomic DNA. Translation: CAA06978.1.
AC012654 Genomic DNA. Translation: AAF43239.1.
CP002684 Genomic DNA. Translation: AEE35242.1.
CP002684 Genomic DNA. Translation: AEE35243.1.
AY070403 mRNA. Translation: AAL49899.1.
AY117240 mRNA. Translation: AAM51315.1.
PIRiC96741.
T51846.
RefSeqiNP_001031266.1. NM_001036189.1. [O82656-1]
NP_177331.1. NM_105844.3. [O82656-1]
UniGeneiAt.407.

Genome annotation databases

EnsemblPlantsiAT1G71860.1; AT1G71860.1; AT1G71860. [O82656-1]
AT1G71860.3; AT1G71860.3; AT1G71860. [O82656-1]
GeneIDi843516.
KEGGiath:AT1G71860.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF055635 mRNA. Translation: AAC68859.1.
AJ006309 Genomic DNA. Translation: CAA06978.1.
AC012654 Genomic DNA. Translation: AAF43239.1.
CP002684 Genomic DNA. Translation: AEE35242.1.
CP002684 Genomic DNA. Translation: AEE35243.1.
AY070403 mRNA. Translation: AAL49899.1.
AY117240 mRNA. Translation: AAM51315.1.
PIRiC96741.
T51846.
RefSeqiNP_001031266.1. NM_001036189.1. [O82656-1]
NP_177331.1. NM_105844.3. [O82656-1]
UniGeneiAt.407.

3D structure databases

ProteinModelPortaliO82656.
SMRiO82656. Positions 42-328.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi28736. 4 interactions.
IntActiO82656. 1 interaction.
MINTiMINT-8390809.
STRINGi3702.AT1G71860.1.

Proteomic databases

PRIDEiO82656.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G71860.1; AT1G71860.1; AT1G71860. [O82656-1]
AT1G71860.3; AT1G71860.3; AT1G71860. [O82656-1]
GeneIDi843516.
KEGGiath:AT1G71860.

Organism-specific databases

TAIRiAT1G71860.

Phylogenomic databases

HOGENOMiHOG000243992.
InParanoidiO82656.
OMAiPDSIAHE.
PhylomeDBiO82656.

Enzyme and pathway databases

BioCyciARA:AT1G71860-MONOMER.
ARA:GQT-335-MONOMER.

Miscellaneous databases

PROiO82656.

Gene expression databases

ExpressionAtlasiO82656. baseline and differential.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamiPF00102. Y_phosphatase. 1 hit.
[Graphical view]
PRINTSiPR00700. PRTYPHPHTASE.
SMARTiSM00194. PTPc. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
PROSITEiPS00383. 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. "Molecular characterization of a tyrosine-specific protein phosphatase encoded by a stress-responsive gene in Arabidopsis."
    Xu Q., Fu H.H., Gupta R., Luan S.
    Plant Cell 10:849-857(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INDUCTION, MUTAGENESIS OF ASP-234 AND CYS-265.
  2. "Higher plant tyrosine-specific protein phosphatases (PTPs) contain novel amino-terminal domains: expression during embryogenesis."
    Fordham-Skelton A.P., Skipsey M., Eveans I.M., Edwards R., Gatehouse J.A.
    Plant Mol. Biol. 39:593-605(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: cv. Columbia.
  3. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  4. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  5. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  6. "ATMPK4, an Arabidopsis homolog of mitogen-activated protein kinase, is activated in vitro by AtMEK1 through threonine phosphorylation."
    Huang Y., Li H., Gupta R., Morris P.C., Luan S., Kieber J.J.
    Plant Physiol. 122:1301-1310(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Redox control of protein tyrosine phosphatases and mitogen-activated protein kinases in plants."
    Gupta R., Luan S.
    Plant Physiol. 132:1149-1152(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION.
  8. "MAP kinase phosphatase1 and protein tyrosine phosphatase1 are repressors of salicylic acid synthesis and SNC1-mediated responses in Arabidopsis."
    Bartels S., Anderson J.C., Gonzalez Besteiro M.A., Carreri A., Hirt H., Buchala A., Metraux J.P., Peck S.C., Ulm R.
    Plant Cell 21:2884-2897(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MPK6, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiPTP1_ARATH
AccessioniPrimary (citable) accession number: O82656
Secondary accession number(s): O65190
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2012
Last sequence update: November 1, 1998
Last modified: June 24, 2015
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

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.