background:
The phosphorylation of proteins at tyrosine residues has long been recognized as an important regulatory component of signal transduction. This is a reversible process, involving both enzymes that phosphorylate proteins on tyrosine residues as well as a rapidly expanding family of protein tyrosine phosphatases. These latter enzymes bear little resemblance to either the protein serine and protein threonine phosphatases or to the acid and alkaline phosphatases. In most tissues, the major PTPase is a vanadate- and molybdate-sensitive protein. PTP-H1 shares homology with the cytoskeletal-associated proteins band 4.1, ezrin, and talin and has been shown to contain a PDZ and band 4.1 domain. These domains are responsible for targeting proteins to the cytoskeleton-membrane interface, as well as mediating protein-protein interactions, recognizing SLCterminal valine residues and binding to other PDZ domains. Overexpression of PTP-H1 may reverse transformation induced by oncogenic protein-tyrosine kinases, such as the members of the src family.
Function:
May act at junctions between the membrane and the cytoskeleton. Possesses tyrosine phosphatase activity.
Subcellular Location:
Cell membrane. Cytoplasm. cytoskeleton.
Similarity:
Belongs to the protein-tyrosine phosphatase family. Non-receptor class subfamily.
Contains 1 FERM domain.
Contains 1 PDZ (DHR) domain.
Contains 1 tyrosine-protein phosphatase domain.
Database links:
Entrez Gene: 5774 Human
Entrez Gene: 545622 Mouse
Omim: 176877 Human
SwissProt: P26045 Human
SwissProt: A2ALK8 Mouse
Unigene: 436429 Human
Unigene: 246552 Mouse
Important Note:
This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
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