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Protein

Tyrosine-protein phosphatase non-receptor type 7

Gene

Ptpn7

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

May play a role in the regulation of T and B-lymphocyte development and signal transduction.By similarity

Catalytic activityi

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

Enzyme regulationi

Inhibited in cells after FCER1A triggering.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei257 – 2571SubstrateBy similarity
Active sitei290 – 2901Phosphocysteine intermediatePROSITE-ProRule annotation
Binding sitei334 – 3341SubstrateBy similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein phosphatase non-receptor type 7 (EC:3.1.3.48)
Alternative name(s):
Hematopoietic protein-tyrosine phosphatase
Short name:
HEPTP
Protein-tyrosine phosphatase LC-PTP
Gene namesi
Name:Ptpn7
Synonyms:Lcptp
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 13

Organism-specific databases

RGDi708516. Ptpn7.

Subcellular locationi

GO - Cellular componenti

  • cytoplasmic side of plasma membrane Source: Ensembl
  • cytoskeleton Source: UniProtKB-SubCell
  • cytosol Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 359359Tyrosine-protein phosphatase non-receptor type 7PRO_0000094763Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei44 – 441PhosphoserineBy similarity
Modified residuei66 – 661PhosphothreonineBy similarity
Modified residuei93 – 931PhosphoserineBy similarity
Modified residuei143 – 1431PhosphoserineBy similarity
Modified residuei290 – 2901Cysteine sulfenic acid (-SOH)1 Publication

Post-translational modificationi

Oxidized at active site cysteine. Treatment with pervanadate (vanadate and H2O2) or with antigen enhanced oxidation of active site cysteine.1 Publication

Keywords - PTMi

Oxidation, Phosphoprotein

Proteomic databases

PaxDbiP49445.
PRIDEiP49445.

PTM databases

PhosphoSiteiP49445.

Expressioni

Gene expression databases

GenevisibleiP49445. RN.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000007833.

Structurei

3D structure databases

ProteinModelPortaliP49445.
SMRiP49445. Positions 65-354.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini97 – 349253Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni38 – 5114Interaction with MAP kinasesBy similarityAdd
BLAST
Regioni290 – 2967Substrate bindingBy similarity

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG5599.
GeneTreeiENSGT00780000121945.
HOGENOMiHOG000294188.
HOVERGENiHBG001594.
InParanoidiP49445.
KOiK18019.
OMAiSEQYQFL.
OrthoDBiEOG7288QX.
PhylomeDBiP49445.
TreeFamiTF331016.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR008356. Tyr_Pase_KIM-con.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamiPF00102. Y_phosphatase. 1 hit.
[Graphical view]
PRINTSiPR01778. KIMPTPASE.
PR00700. 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.

P49445-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVQACEGRSR AQLPTLSLGA DMTQPPPAKA PAKKHVRLQE RRGSSVALML
60 70 80 90 100
DVRSLGTVEP ICSVNTPREV TLHFLRTAGH PLTRWTLQHQ PPSPKQLEEE
110 120 130 140 150
FLKIPSNFVN PEDLDIPGHA SKDRYKTILP NPQSRVCLGR AHSQEDSDYI
160 170 180 190 200
NANYIRGYDG KEKVYIATQG PMPNTVADFW EMVWQEDVSL IVMLTQLREG
210 220 230 240 250
KEKCVHYWPT EEEAYGPFQI RIQGMKEHPE YTVRHLTIQH QQECRSVKHI
260 270 280 290 300
LFSAWPDHQT PESAGPLLRL VAEVETPETA ANSGPIVVHC SAGIGRTGCF
310 320 330 340 350
IATRIGCQQL KARGEVDILG IVCQLRLDRG GMIQTAEQYQ FLHHTLALYA

AQLPPETDP
Length:359
Mass (Da):40,314
Last modified:February 1, 1996 - v1
Checksum:i5B98E196DB633677
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U28356 mRNA. Translation: AAA84443.1.
RefSeqiNP_663716.1. NM_145683.1.
XP_006249883.1. XM_006249821.2.
UniGeneiRn.10160.

Genome annotation databases

EnsembliENSRNOT00000007833; ENSRNOP00000007833; ENSRNOG00000005807.
GeneIDi246781.
KEGGirno:246781.
UCSCiRGD:708516. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U28356 mRNA. Translation: AAA84443.1.
RefSeqiNP_663716.1. NM_145683.1.
XP_006249883.1. XM_006249821.2.
UniGeneiRn.10160.

3D structure databases

ProteinModelPortaliP49445.
SMRiP49445. Positions 65-354.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000007833.

PTM databases

PhosphoSiteiP49445.

Proteomic databases

PaxDbiP49445.
PRIDEiP49445.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000007833; ENSRNOP00000007833; ENSRNOG00000005807.
GeneIDi246781.
KEGGirno:246781.
UCSCiRGD:708516. rat.

Organism-specific databases

CTDi5778.
RGDi708516. Ptpn7.

Phylogenomic databases

eggNOGiCOG5599.
GeneTreeiENSGT00780000121945.
HOGENOMiHOG000294188.
HOVERGENiHBG001594.
InParanoidiP49445.
KOiK18019.
OMAiSEQYQFL.
OrthoDBiEOG7288QX.
PhylomeDBiP49445.
TreeFamiTF331016.

Miscellaneous databases

NextBioi623877.
PROiP49445.

Gene expression databases

GenevisibleiP49445. RN.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR008356. Tyr_Pase_KIM-con.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamiPF00102. Y_phosphatase. 1 hit.
[Graphical view]
PRINTSiPR01778. KIMPTPASE.
PR00700. 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

  1. "Aggregation of IgE receptors in rat basophilic leukemia 2H3 cells induces tyrosine phosphorylation of the cytosolic protein-tyrosine phosphatase HePTP."
    Swieter M., Berenstein E.H., Swaim W.D., Siraganian R.P.
    J. Biol. Chem. 270:21902-21906(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Down-regulation of protein-tyrosine phosphatases activates an immune receptor in the absence of its translocation into lipid rafts."
    Heneberg P., Draberova L., Bambouskova M., Pompach P., Draber P.
    J. Biol. Chem. 285:12787-12802(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, OXIDATION AT CYS-290, ENZYME REGULATION.

Entry informationi

Entry nameiPTN7_RAT
AccessioniPrimary (citable) accession number: P49445
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: June 24, 2015
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.