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P49445 (PTN7_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 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 names
Name:Ptpn7
Synonyms:Lcptp
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length359 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Enzyme regulation

Inhibited in cells after FCER1A triggering. Ref.2

Subcellular location

Cytoplasm By similarity. Cytoplasmcytoskeleton Ref.2.

Post-translational modification

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

Sequence similarities

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

Contains 1 tyrosine-protein phosphatase domain.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 359359Tyrosine-protein phosphatase non-receptor type 7
PRO_0000094763

Regions

Domain97 – 349253Tyrosine-protein phosphatase
Region38 – 5114Interaction with MAP kinases By similarity
Region290 – 2967Substrate binding By similarity

Sites

Active site2901Phosphocysteine intermediate By similarity
Binding site2571Substrate By similarity
Binding site3341Substrate By similarity

Amino acid modifications

Modified residue441Phosphoserine By similarity
Modified residue661Phosphothreonine By similarity
Modified residue931Phosphoserine By similarity
Modified residue1431Phosphoserine By similarity
Modified residue2901Cysteine sulfenic acid (-SOH)

Sequences

Sequence LengthMass (Da)Tools
P49445 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 5B98E196DB633677

FASTA35940,314
        10         20         30         40         50         60 
MVQACEGRSR AQLPTLSLGA DMTQPPPAKA PAKKHVRLQE RRGSSVALML DVRSLGTVEP 

        70         80         90        100        110        120 
ICSVNTPREV TLHFLRTAGH PLTRWTLQHQ PPSPKQLEEE FLKIPSNFVN PEDLDIPGHA 

       130        140        150        160        170        180 
SKDRYKTILP NPQSRVCLGR AHSQEDSDYI NANYIRGYDG KEKVYIATQG PMPNTVADFW 

       190        200        210        220        230        240 
EMVWQEDVSL IVMLTQLREG KEKCVHYWPT EEEAYGPFQI RIQGMKEHPE YTVRHLTIQH 

       250        260        270        280        290        300 
QQECRSVKHI LFSAWPDHQT PESAGPLLRL VAEVETPETA ANSGPIVVHC SAGIGRTGCF 

       310        320        330        340        350 
IATRIGCQQL KARGEVDILG IVCQLRLDRG GMIQTAEQYQ FLHHTLALYA AQLPPETDP 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U28356 mRNA. Translation: AAA84443.1.
RefSeqNP_663716.1. NM_145683.1.
XP_006249883.1. XM_006249821.1.
UniGeneRn.10160.

3D structure databases

ProteinModelPortalP49445.
SMRP49445. Positions 65-354.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000007833.

PTM databases

PhosphoSiteP49445.

Proteomic databases

PaxDbP49445.
PRIDEP49445.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000007833; ENSRNOP00000007833; ENSRNOG00000005807.
GeneID246781.
KEGGrno:246781.
UCSCRGD:708516. rat.

Organism-specific databases

CTD5778.
RGD708516. Ptpn7.

Phylogenomic databases

eggNOGCOG5599.
GeneTreeENSGT00750000117606.
HOGENOMHOG000294188.
HOVERGENHBG001594.
InParanoidP49445.
KOK18019.
OMAGTVEPIC.
OrthoDBEOG7288QX.
PhylomeDBP49445.
TreeFamTF331016.

Gene expression databases

GenevestigatorP49445.

Family and domain databases

InterProIPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR008356. Tyr_Pase_KIM-con.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamPF00102. Y_phosphatase. 1 hit.
[Graphical view]
PRINTSPR01778. KIMPTPASE.
PR00700. PRTYPHPHTASE.
SMARTSM00194. PTPc. 1 hit.
[Graphical view]
PROSITEPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio623877.
PROP49445.

Entry information

Entry namePTN7_RAT
AccessionPrimary (citable) accession number: P49445
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: April 16, 2014
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families