InterPro : 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.
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

4 Contains

Id Name Short Name Type
IPR000980 SH2 domain SH2 Domain
IPR000242 Protein-tyrosine phosphatase, receptor/non-receptor type Tyr_Pase_rcpt/non-rcpt Domain
IPR000387 Protein-tyrosine/Dual specificity phosphatase Tyr/Dual-sp_Pase Domain
IPR016130 Protein-tyrosine phosphatase, active site Tyr_Pase_AS Active_site

0 Found In

0 Parent Features

9 Publications

First Author Title Year Journal Volume Pages
Denu JM Protein tyrosine phosphatases: mechanisms of catalysis and regulation. 1998 Curr Opin Chem Biol 2 633-41
Paul S Receptor and nonreceptor protein tyrosine phosphatases in the nervous system. 2003 Cell Mol Life Sci 60 2465-82
Wang WQ An overview of the protein tyrosine phosphatase superfamily. 2003 Curr Top Med Chem 3 739-48
Eswaran J The crystal structure of human receptor protein tyrosine phosphatase kappa phosphatase domain 1. 2006 Protein Sci 15 1500-5
Perkins LA The nonreceptor protein tyrosine phosphatase corkscrew functions in multiple receptor tyrosine kinase pathways in Drosophila. 1996 Dev Biol 180 63-81
Barford D The structure and mechanism of protein phosphatases: insights into catalysis and regulation. 1998 Annu Rev Biophys Biomol Struct 27 133-64
Ono M Deletion of SHIP or SHP-1 reveals two distinct pathways for inhibitory signaling. 1997 Cell 90 293-301
Hof P Crystal structure of the tyrosine phosphatase SHP-2. 1998 Cell 92 441-50
Yamauchi K Protein-tyrosine-phosphatase SHPTP2 is a required positive effector for insulin downstream signaling. 1995 Proc Natl Acad Sci U S A 92 664-8



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)