modENCODE |  Help |  blog

Protein Domain : IPR000387

Name  Protein-tyrosine/Dual specificity phosphatase Short Name  Tyr/Dual-sp_Pase
Type  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 includes proteins of two subfamilies: Ser/Thr () and Tyr dual specificity protein phosphatase and tyrosine specific protein phosphatase (). Both of these subfamilies 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 against 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 regulatory centre [].Ser/Thr and Tyr dual specificity phosphatases are a group of enzymes with both Ser/Thr () and tyrosine specific proteinphosphatase () activity able to remove both the serine/threonine or tyrosine-bound phosphate group from a widerange 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. Tyrosine specific protein phosphatases catalyze the removal of a phosphate group attached to a tyrosine residue. They are also very important in the control of cell growth, proliferation, differentiation and transformation.This domain is common to both dual-specificity protein phosphatases and protein-tyrosine phosphatase.
Paste the following link
Lists
This ProteinDomain isn't in any lists. Upload a list.

Publication Counts Displayer

2 Child Features

DB identifier Name Short Name Type
IPR000242 Protein-tyrosine phosphatase, receptor/non-receptor type Tyr_Pase_rcpt/non-rcpt Domain
IPR020422 Dual specificity phosphatase, subgroup, catalytic domain Dual-sp_phosphatase_subgr_cat Domain

1 Contains

DB identifier Name Short Name Type
IPR016130 Protein-tyrosine phosphatase, active site Tyr_Pase_AS Active_site

1 Cross References

Identifier
Source . Name
Subject . Primary Identifier
PS50056 PROFILE IPR000387

3 Data Sets

Name URL
TrEMBL data set http://www.ebi.ac.uk/trembl/
InterPro data set  
InterPro GO Annotation data set  

20 Found In

DB identifier Name Short Name Type
IPR000340 Dual specificity phosphatase, catalytic domain Dual-sp_phosphatase_cat-dom Domain
IPR017074 mRNA capping enzyme, bifunctional mRNA_cap_enz_bifunc Family
IPR012151 Protein-tyrosine phosphatase, non-receptor type-3, -4 Tyr_Pase_non-rcpt_typ-3/4 Family
IPR020417 Atypical dual specificity phosphatase Atypical_DUSP Family
IPR016278 Dual specificity protein phosphatase 12 DUSP12 Family
IPR020405 Atypical dual specificity phosphatase, subfamily A Atypical_DUSP_famA Family
IPR012152 Protein-tyrosine phosphatase, non-receptor type-6, -11 Tyr_Pase_non-rcpt_typ-6/11 Family
IPR014392 Protein-tyrosine phosphatase, non-receptor type-14, -21 Tyr_Pase_non-rcpt_typ-14/21 Family
IPR012153 Protein-tyrosine phosphatase, non-receptor type-13 Tyr_Pase_non-rcpt_typ-13 Family
IPR016336 Receptor tyrosine-protein phosphatase, alpha/epsilon-type Tyr_Pase_rcpt_a/e-type Family
IPR016335 Leukocyte common antigen Leukocyte_common_ag Family
IPR003546 Type III secreted modular tyrosine phosphatase, SptP/YopH Tyr_Pase_SptP/YopH Family
IPR008356 Protein-tyrosine phosphatase, KIM-containing Tyr_Pase_KIM-con Family
IPR016334 Protein-tyrosine phosphatase, receptor type R/non-receptor type 5 Tyr_Pase_rcpt_R/non-rcpt_5 Family
IPR008425 Cyclin-dependent kinase inhibitor 3 CDK_inhib_3 Family
IPR012266 Protein-tyrosine phosphatase, non-receptor type-12 Ptpn_12 Family
IPR012265 Protein-tyrosine phosphatase, non-receptor type-1/2 Ptpn1/Ptpn2 Family
IPR016276 Non-receptor tyrosine-protein phosphatase, 8/22 Non-rcpt_Tyr_Pase_8/22 Family
IPR016277 Non-receptor tyrosine-protein phosphatase type 1, yeast Non-rcpt_Tyr_Pase_T1_fun Family
IPR020420 Atypical dual specificity phosphatase, subfamily B Atypical_DUSP_famB Family

2 GO Annotation


Subject . Secondary Identifier
Subject . Name
Subject . Symbol
Ontology Term . Identifier
Ontology Term . Name
Protein-tyrosine/Dual specificity phosphatase   GO:0016791 phosphatase activity
Protein-tyrosine/Dual specificity phosphatase   GO:0016311 dephosphorylation

2 Ontology Annotations


Subject . Secondary Identifier
Subject . Name
Subject . Symbol
Ontology Term . Identifier
Ontology Term . Name
Protein-tyrosine/Dual specificity phosphatase   GO:0016791 phosphatase activity
Protein-tyrosine/Dual specificity phosphatase   GO:0016311 dephosphorylation

1 Parent Features

DB identifier Name Short Name Type
IPR029021 Protein-tyrosine phosphatase-like Prot-tyrosine_phosphatase-like Domain

750 Proteins

DB identifier Primary Accession
Organism . Name
FBpp0099554 Q9W323 Drosophila melanogaster
FBpp0099555 Q9W324 Drosophila melanogaster
FBpp0099556 Q8IRM7 Drosophila melanogaster
FBpp0099558 Q8IRM6 Drosophila melanogaster
FBpp0099559 Q59E68 Drosophila melanogaster
FBpp0074510 Q9VWF4 Drosophila melanogaster
FBpp0074420 Q9VWN2 Drosophila melanogaster
FBpp0111917 A8JUQ2 Drosophila melanogaster
FBpp0083844 Q86BN8 Drosophila melanogaster
FBpp0304559 M9PAZ4 Drosophila melanogaster
FBpp0290630 Q9VPV8 Drosophila melanogaster
FBpp0290631 Q59E11 Drosophila melanogaster
FBpp0071938 Q8MLR7 Drosophila melanogaster
FBpp0071937 Q9W1Q6 Drosophila melanogaster
FBpp0070363 L7XAI0 Drosophila melanogaster
FBpp0080414 O61722 Drosophila melanogaster
FBpp0290828 Q6NN85 Drosophila melanogaster
FBpp0087183 Q8SX38 Drosophila melanogaster
FBpp0072602 Q9W0G1 Drosophila melanogaster
FBpp0072603 Q8IRH4 Drosophila melanogaster
FBpp0080801 P16621 Drosophila melanogaster
FBpp0075565 Q8IQK0 Drosophila melanogaster
FBpp0075564 Q8IQK1 Drosophila melanogaster
FBpp0075562 Q9VU80 Drosophila melanogaster
FBpp0290827 E1JIW2 Drosophila melanogaster
FBpp0074802 Q9VVW5 Drosophila melanogaster
FBpp0073369 P35992 Drosophila melanogaster
FBpp0303823 M9PEB6 Drosophila melanogaster
FBpp0303420 M9PJI5 Drosophila melanogaster
FBpp0071603 Q9W2F3 Drosophila melanogaster




© 2002 - 2013 Department of Genetics, University of Cambridge, Downing Street,
Cambridge CB2 3EH, United Kingdom