Protein Domain : IPR000340

Type:  Domain Name:  Dual specificity phosphatase, catalytic domain
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 dual specificity protein-tyrosine phosphatases. Ser/Thr and Tyr dual specificity phosphatases are a group of enzymes with both Ser/Thr () and tyrosine specific protein phosphatase () activity able to remove both the serine/threonine or tyrosine-bound phosphate group from a wide range of phosphoproteins, including a number of enzymes which have been phosphorylated under the action of a kinase. Dual specificity protein phosphatases (DSPs) regulate mitogenic signal transduction and control the cell cycle. The crystal structure of a human DSP, vaccinia H1-related phosphatase (or VHR), has been determined at 2.1 angstrom resolution []. A shallow active site pocket in VHR allows for the hydrolysis of phosphorylated serine, threonine, or tyrosine protein residues, whereas the deeper active site of protein tyrosine phosphatases (PTPs) restricts substrate specificity to only phosphotyrosine. Positively charged crevices near the active site may explain the enzyme's preference for substrates with two phosphorylated residues. The VHR structure defines a conserved structural scaffold for both DSPs and PTPs. A "recognition region" connecting helix alpha1 to strand beta1, may determine differences in substrate specificity between VHR, the PTPs, and other DSPs.These proteins may also have inactive phosphatase domains, and dependent on the domain composition this loss of catalytic activity has different effects on protein function. Inactive single domain phosphatases can still specifically bind substrates, and protect again dephosphorylation, while the inactive domains of tandem phosphatases can be further subdivided into two classes. Those which bind phosphorylated tyrosine residues may recruit multi-phosphorylated substrates for the adjacent active domains and are more conserved, while the other class have accumulated several variable amino acid substitutions and have a complete loss of tyrosine binding capability. The second class shows a release of evolutionary constraint for the sites around the catalytic centre, which emphasises a difference in function from the first group. There is a region of higher conservation common to both classes, suggesting a new regulatory centre []. Short Name:  Dual-sp_phosphatase_cat-dom
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0 Child Features

2 Contains

DB identifier Type Name
IPR000387 Domain Tyrosine specific protein phosphatases domain
IPR016130 Active_site Protein-tyrosine phosphatase, active site

1 Cross References

Identifier
PF00782

7 Found Ins

DB identifier Type Name
IPR017074 Family mRNA capping enzyme, bifunctional
IPR020417 Family Atypical dual specificity phosphatase
IPR016278 Family Dual specificity protein phosphatase 12
IPR020420 Family Atypical dual specificity phosphatase, subfamily B
IPR020405 Family Atypical dual specificity phosphatase, subfamily A
IPR017361 Family Bifunctional phosphatidylinositol trisphosphate phosphatase/dual specificity phosphatase PTEN
IPR008343 Family Mitogen-activated protein (MAP) kinase phosphatase

2 GO Annotations

GO Term Gene Name
GO:0008138 IPR000340
GO:0006470 IPR000340

2 Ontology Annotations

GO Term Gene Name
GO:0008138 IPR000340
GO:0006470 IPR000340

1 Parent Features

DB identifier Type Name
IPR029021 Domain Protein-tyrosine phosphatase-like

3256 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
92881 D8RG08 PAC:15421425 Selaginella moellendorffii 725  
36819 D8RL57 PAC:15412257 Selaginella moellendorffii 174  
412678 D8RL46 PAC:15413200 Selaginella moellendorffii 233  
97017 D8RMK4 PAC:15407453 Selaginella moellendorffii 350  
27743 D8RQX2 PAC:15407144 Selaginella moellendorffii 172  
34445 D8RS38 PAC:15403319 Selaginella moellendorffii 255  
100916 D8RTN6 PAC:15403908 Selaginella moellendorffii 560  
6245 D8RTR0 PAC:15420138 Selaginella moellendorffii 114  
416191 D8RYD2 PAC:15420989 Selaginella moellendorffii 201  
138678 D8TFX3 PAC:15402223 Selaginella moellendorffii 347  
68807 D8QYM1 PAC:15417327 Selaginella moellendorffii 84  
418983 D8S7F7 PAC:15410710 Selaginella moellendorffii 174  
113946 D8SCL1 PAC:15420089 Selaginella moellendorffii 167  
406660 D8R123 PAC:15417631 Selaginella moellendorffii 206  
35954 D8SKE1 PAC:15410215 Selaginella moellendorffii 213  
83906 D8R2W0 PAC:15417857 Selaginella moellendorffii 155  
27712 D8QQ09 PAC:15407087 Selaginella moellendorffii 94  
27710 D8T0S8 PAC:15407084 Selaginella moellendorffii 95  
27738 D8SZJ9 PAC:15407127 Selaginella moellendorffii 174  
89622 D8RBG4 PAC:15410886 Selaginella moellendorffii 581  
437707 D8QP09 PAC:15420447 Selaginella moellendorffii 271  
408631 D8R9F9 PAC:15423293 Selaginella moellendorffii 210  
127483 D8SYC1 PAC:15412944 Selaginella moellendorffii 199  
91219 D8RCM2 PAC:15414008 Selaginella moellendorffii 393  
36025 D8RC28 PAC:15406092 Selaginella moellendorffii 162  
91859 D8RE91 PAC:15418580 Selaginella moellendorffii 341  
91575 D8REX4 PAC:15416329 Selaginella moellendorffii 215  
evm.model.supercontig_128.70 PAC:16407498 Carica papaya 357  
evm.model.supercontig_132.48 PAC:16408144 Carica papaya 298  
evm.model.supercontig_16.19 PAC:16410040 Carica papaya 179  

8 Publications

First Author Title Year Journal Volume Pages PubMed ID
            14739250
            9818190
            14625689
            12678841
            16672235
            8948575
            9646865
            8650541