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Protein Domain : IPR012265

Name  Protein-tyrosine phosphatase, non-receptor type-1/2 Short Name  Ptpn1/Ptpn2
Type  Family Description  Protein tyrosine (pTyr) phosphorylation is a common post-translational modification which can create novel recognition motifs for protein interactions and cellular localisation, affect protein stability, and regulate enzyme activity. Consequently, maintaining an appropriate level of protein tyrosine phosphorylation is essential for many cellular functions. Tyrosine-specific protein phosphatases (PTPase; ) catalyse the removal of a phosphate group attached to a tyrosine residue, using a cysteinyl-phosphate enzyme intermediate. These enzymes are key regulatory components in signal transduction pathways (such as the MAP kinase pathway) and cell cycle control, and are important in the control of cell growth, proliferation, differentiation and transformation [, ]. The PTP superfamily can be divided into four subfamilies []:(1) pTyr-specific phosphatases(2) dual specificity phosphatases (dTyr and dSer/dThr)(3) Cdc25 phosphatases (dTyr and/or dThr)(4) LMW (low molecular weight) phosphatasesBased on their cellular localisation, PTPases are also classified as:Receptor-like, which are transmembrane receptors that contain PTPase domains []Non-receptor (intracellular) PTPases []All PTPases carry the highly conserved active site motif C(X)5R (PTP signature motif), employ a common catalytic mechanism, and share a similar core structure made of a central parallel beta-sheet with flanking alpha-helices containing a beta-loop-alpha-loop that encompasses the PTP signature motif []. Functional diversity between PTPases is endowed by regulatory domains and subunits. This entry represents non-receptor PTPase types 1 and 2 (also known as T-cell PTPase). These types appear to have different biological functions: in knock-out mice, type1 knock-outs showed increased insulin sensitivity but a normal lifespan, while type 2 knock-outs died when only a few weeks old [, ]. Substrate-trapping experiments suggest that these types recognise different cellular targets, though it is not known if this is due to sequence differences or to other regulatory mechanisms. Regulation of function and activity can occur at the transcriptional, alternative splicing, proteolytic processing and covalent modification levels. For example, T-cell PTPase has two different isoforms generated by alternative splicing, one of which recognises nuclear substrates, while the other recognises cytoplasmic substrates. These proteins adopt an alpha-beta-alpha fold where the active site is located in a deep cleft located on the surface of the protein [, ].

Publication Counts Displayer

0 Child Features

3 Contains

DB identifier Name Short Name Type
IPR000387 Protein-tyrosine/Dual specificity phosphatase Tyr/Dual-sp_Pase Domain
IPR000242 Protein-tyrosine phosphatase, receptor/non-receptor type Tyr_Pase_rcpt/non-rcpt Domain
IPR016130 Protein-tyrosine phosphatase, active site Tyr_Pase_AS Active_site

1 Cross References

Identifier
Source . Name

Subject . Primary Identifier
PIRSF000926 PIRSF IPR012265

2 Data Sets

Name URL
InterPro data set  
InterPro GO Annotation data set  

0 Found In

2 GO Annotation


Subject . Secondary Identifier

Subject . Name

Subject . Symbol

Ontology Term . Identifier

Ontology Term . Name
Protein-tyrosine phosphatase, non-receptor type-1/2   GO:0004725 protein tyrosine phosphatase activity
Protein-tyrosine phosphatase, non-receptor type-1/2   GO:0006470 protein dephosphorylation

2 Ontology Annotations


Subject . Secondary Identifier

Subject . Name

Subject . Symbol

Ontology Term . Identifier

Ontology Term . Name
Protein-tyrosine phosphatase, non-receptor type-1/2   GO:0004725 protein tyrosine phosphatase activity
Protein-tyrosine phosphatase, non-receptor type-1/2   GO:0006470 protein dephosphorylation

0 Parent Features

0 Proteins