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Protein Domain : IPR008356

Name  Protein-tyrosine phosphatase, KIM-containing Short Name  Tyr_Pase_KIM-con
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. The structures of receptor PTPases comprise a variable length extracellulardomain, followed by a TM region and a cytoplasmic C-terminal catalyticdomain. The extracellular regions of some receptor PTPases house fibronectintype III repeats, immunoglobulin-like domains, MAM domains or carbonicanhydrase-like domains. The cytoplasmic region generally contains 2 copiesof the PTPase domain: the first of these is enzymatically active; the secondis inactive, but appears to affect substrate specificity in the first.PTPase domains contain ~300 residues, including 2 conserved cysteines, thesecond of which is required for activity. Other conserved residues in itsimmediate vicinity are also catalytically important [].This entry represents protein-tyrosine phosphatases that contain a Kinase Interaction Motif (KIM), including receptor PTPases and non-receptor (types 2 and 7) PTPases. Enzymes PTP-STEP, PTP-SL and LC-PTP each contain a KIM in the N-terminal portion of the molecule. The KIM sequence mediates interaction withMAP kinases, predominantly ERK1 and ERK2. It has been experimentally shownthat over-expression of PTP-SL down-regulates the activation of ERK2 and itsnuclear translocation [].

Publication Counts Displayer

1 Child Features

DB identifier Name Short Name Type
IPR016334 Protein-tyrosine phosphatase, receptor type R/non-receptor type 5 Tyr_Pase_rcpt_R/non-rcpt_5 Family

2 Contains

DB identifier Name Short Name Type
IPR000387 Protein-tyrosine/Dual specificity phosphatase Tyr/Dual-sp_Pase Domain
IPR016130 Protein-tyrosine phosphatase, active site Tyr_Pase_AS Active_site

1 Cross References

Identifier
Source . Name

Subject . Primary Identifier
PR01778 PRINTS IPR008356

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, KIM-containing   GO:0004725 protein tyrosine phosphatase activity
Protein-tyrosine phosphatase, KIM-containing   GO:0006470 protein dephosphorylation

2 Ontology Annotations


Subject . Secondary Identifier

Subject . Name

Subject . Symbol

Ontology Term . Identifier

Ontology Term . Name
Protein-tyrosine phosphatase, KIM-containing   GO:0004725 protein tyrosine phosphatase activity
Protein-tyrosine phosphatase, KIM-containing   GO:0006470 protein dephosphorylation

0 Parent Features

0 Proteins