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Protein Domain : IPR012152

Name  Protein-tyrosine phosphatase, non-receptor type-6, -11 Short Name  Tyr_Pase_non-rcpt_typ-6/11
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 6 and 11, also known as SHP-1 and SHP-2 respectively. SHP-1 is expressed predominantly in haematopoietic and epithelial cells, playing an important role in haematopoiesis and functioning as a terminator of signalling transduction, predominantly by dephosphorylation of appropriate substrate proteins []. SHP-2 is expressed in most cell types and is involved in signal transduction stimulated by epidermal growth factor, platelet-derived growth factor, and insulin, acting as a positive regulator of cell proliferation []. The structure of human SHP-2 () shows that its catalytic activity is regulated by its two SH2 domains []. In the absence of protein, the N-terminal SH2 domain binds the phosphatase domain, inhibiting its activity, while the binding of a tyrosine-phosphorylated substrate to this domain causes a conformational change which activates the enzyme. The C-terminal SH2 domain does not play a direct role in activation, but contributes to substrate specificity and binding energy.

Publication Counts Displayer

0 Child Features

4 Contains

DB identifier Name Short Name Type
IPR000980 SH2 domain SH2 Domain
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
PIRSF000929 PIRSF IPR012152

3 Data Sets

Name URL
TrEMBL data set http://www.ebi.ac.uk/trembl/
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-6, -11   GO:0004725 protein tyrosine phosphatase activity
Protein-tyrosine phosphatase, non-receptor type-6, -11   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-6, -11   GO:0004725 protein tyrosine phosphatase activity
Protein-tyrosine phosphatase, non-receptor type-6, -11   GO:0006470 protein dephosphorylation

0 Parent Features

5 Proteins

DB identifier Primary Accession
Organism . Name
K7GV80_CAEJA K7GV80 Caenorhabditis japonica
K7GV81_CAEJA K7GV81 Caenorhabditis japonica
G0PM67_CAEBE G0PM67 Caenorhabditis brenneri
G5EC24_CAEEL G5EC24 Caenorhabditis elegans
E3LRF0_CAERE E3LRF0 Caenorhabditis remanei