modENCODE |  Help |  blog

Protein Domain : IPR000242

Name  Protein-tyrosine phosphatase, receptor/non-receptor type Short Name  Tyr_Pase_rcpt/non-rcpt
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 thatcontain 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 repesents several receptor and non-receptor protein-tyrosine phosphatases.Structurally, all known receptor PTPases, are made up of a variable lengthextracellular domain, followed by a transmembrane region and a C-terminalcatalytic cytoplasmic domain. Some of the receptor PTPases contain fibronectintype III (FN-III) repeats, immunoglobulin-like domains, MAM domains orcarbonic anhydrase-like domains in their extracellular region. The cytoplasmicregion generally contains two copies of the PTPase domain. The first seems tohave enzymatic activity, while the second is inactive. The inactive domains of tandem phosphatases can be divided 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 []. PTPase domains consist of about 300 amino acids. There are two conserved cysteines, the second one has been shown to be absolutely required for activity. Furthermore, a number of conserved residues in its immediate vicinity have also been shown to be important.
Paste the following link
Lists
This ProteinDomain isn't in any lists. Upload a list.

Publication Counts Displayer

1 Child Features

DB identifier Name Short Name Type
IPR003595 Protein-tyrosine phosphatase, catalytic Tyr_Pase_cat Domain

1 Contains

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

4 Cross References

Identifier
Source . Name
Subject . Primary Identifier
PF00102 PFAM IPR000242
PR00700 PRINTS IPR000242
PS50055 PROFILE IPR000242
SM00194 SMART IPR000242

3 Data Sets

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

11 Found In

DB identifier Name Short Name Type
IPR012151 Protein-tyrosine phosphatase, non-receptor type-3, -4 Tyr_Pase_non-rcpt_typ-3/4 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
IPR016334 Protein-tyrosine phosphatase, receptor type R/non-receptor type 5 Tyr_Pase_rcpt_R/non-rcpt_5 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

2 GO Annotation


Subject . Secondary Identifier
Subject . Name
Subject . Symbol
Ontology Term . Identifier
Ontology Term . Name
Protein-tyrosine phosphatase, receptor/non-receptor type   GO:0004725 protein tyrosine phosphatase activity
Protein-tyrosine phosphatase, receptor/non-receptor type   GO:0006470 protein dephosphorylation

2 Ontology Annotations


Subject . Secondary Identifier
Subject . Name
Subject . Symbol
Ontology Term . Identifier
Ontology Term . Name
Protein-tyrosine phosphatase, receptor/non-receptor type   GO:0004725 protein tyrosine phosphatase activity
Protein-tyrosine phosphatase, receptor/non-receptor type   GO:0006470 protein dephosphorylation

1 Parent Features

DB identifier Name Short Name Type
IPR000387 Protein-tyrosine/Dual specificity phosphatase Tyr/Dual-sp_Pase Domain

688 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
FBpp0304559 M9PAZ4 Drosophila melanogaster
FBpp0290630 Q9VPV8 Drosophila melanogaster
FBpp0290631 Q59E11 Drosophila melanogaster
FBpp0070363 L7XAI0 Drosophila melanogaster
FBpp0072602 Q9W0G1 Drosophila melanogaster
FBpp0072603 Q8IRH4 Drosophila melanogaster
FBpp0080801 P16621 Drosophila melanogaster
FBpp0073369 P35992 Drosophila melanogaster
FBpp0303823 M9PEB6 Drosophila melanogaster
FBpp0303420 M9PJI5 Drosophila melanogaster
FBpp0071603 Q9W2F3 Drosophila melanogaster
FBpp0078914 Q9V3V3 Drosophila melanogaster
FBpp0075645 P16620 Drosophila melanogaster
FBpp0070692 Q9W4F5 Drosophila melanogaster
FBpp0070693 Q8IRS0 Drosophila melanogaster
FBpp0080614 Q9VJ95 Drosophila melanogaster
FBpp0310132 E1JJE4 Drosophila melanogaster
FBpp0303681 M9PD76 Drosophila melanogaster
FBpp0303683 M9PDF7 Drosophila melanogaster
FBpp0303684 M9PG93 Drosophila melanogaster
FBpp0303682 M9PDR3 Drosophila melanogaster
FBpp0111712 A8DZ18 Drosophila melanogaster
FBpp0297092 M9NCY3 Drosophila melanogaster
FBpp0289067 Q0KI81 Drosophila melanogaster
FBpp0288423 A1ZAB3 Drosophila melanogaster




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