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Literature summary for 3.1.3.48 extracted from

  • Granot-Attas, S.; Elson, A.
    Protein tyrosine phosphatases in osteoclast differentiation, adhesion, and bone resorption (2008), Eur. J. Cell Biol., 87, 479-490.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in U-937 cells Oryctolagus cuniculus

Inhibitors

Inhibitors Comment Organism Structure
additional information inhibition of PTP-PEST by RNAi reduces formation of podosomal structures at the cell periphery and reduces bone resorption indicating a positive functional role for this PTP in promoting osteoclast activity Mus musculus

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
Mus musculus 5829
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
88000
-
-
Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Mus musculus PTP-PEST most likely also participates in regulating osteoclast differentiation and adhesion to bone matrix ?
-
?
additional information Mus musculus SHP-1 is a negative regulator of osteoclastogenic signalling ?
-
?

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-
Oryctolagus cuniculus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
Oryctolagus cuniculus
-
hematopoietic cell
-
Mus musculus
-
hematopoietic cell
-
Oryctolagus cuniculus
-
kidney
-
Oryctolagus cuniculus
-
osteoclast
-
Mus musculus
-
osteoclast cyt-PTPepsilon is expressed strongly in osteoclasts and is virtually absent from osteoblasts, RPTPepsilon is not expressed in either cell type, function of cyt-PTPepsilon is critical for proper organization of podosomes in osteoclasts Mus musculus
-
osteoclast PTP-oc is expressed quite strongly in osteoclasts and positively regulates osteoclast production and activity Oryctolagus cuniculus
-
RAW-264.7 cell
-
Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information PTP-PEST most likely also participates in regulating osteoclast differentiation and adhesion to bone matrix Mus musculus ?
-
?
additional information SHP-1 is a negative regulator of osteoclastogenic signalling Mus musculus ?
-
?
phosphorylated c-Src + H2O dephosphorylation activates c-Src Mus musculus c-Src + phosphate
-
?
phosphorylated c-Src + H2O dephosphorylation occurs at Tyr-527 Oryctolagus cuniculus c-Src + phosphate
-
?
phosphorylated proline serine threonine-rich phosphatase interacting protein + H2O
-
Mus musculus proline serine threonine-rich phosphatase interacting protein + phosphate
-
?

Synonyms

Synonyms Comment Organism
Cryp-2
-
Oryctolagus cuniculus
cyt-PTPepsilon non-receptor-type isoform of PTPepsilon Mus musculus
GLEPP-1
-
Oryctolagus cuniculus
p65 PTPepsilon
-
Mus musculus
p67 PTPepsilon
-
Mus musculus
protein tyrosine phosphatase
-
Mus musculus
protein tyrosine phosphatase
-
Oryctolagus cuniculus
PTP
-
Mus musculus
PTP
-
Oryctolagus cuniculus
PTP-F
-
Oryctolagus cuniculus
PTP-oc the protein is produced from the distal promotor, PTP-oc is identical to PTPRO, except that its extracellular domain is extremely short with eight amino acids in all Oryctolagus cuniculus
PTP-PEST a non-receptor protein tyrosine phosphatase Mus musculus
PTP-U2
-
Oryctolagus cuniculus
PTPepsilon belongs to the receptor-type branch of the PTP family Mus musculus
PTPepsilonC non-receptor-type isoform of PTPepsilon Mus musculus
PTPepsilonM receptor-type isoform of PTPepsilon Mus musculus
PTPRO a receptor-type PTP, the protein is produced from the distal promotor Oryctolagus cuniculus
PTPRO, truncated the protein is produced from the proximal promotor Oryctolagus cuniculus
PTPRO-FL
-
Oryctolagus cuniculus
PTPROt the protein is produced from the proximal promotor Oryctolagus cuniculus
RPTP-BK
-
Oryctolagus cuniculus
RPTPepsilon receptor-type isoform of PTPepsilon Mus musculus
SHP-1
-
Mus musculus
Src homology 2 domain-containing phosphatase-1
-
Mus musculus