Difference between revisions of "Pseudophosphatases (obsolete)"
From PhosphataseWiki
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=== Functions === | === Functions === | ||
| + | * Receptor PTPs. Most receptor PTPs have two tandem phosphatase domains. The 2nd phosphatase domain has no or negligible activity. The 2nd domain can interact with 1st domain in both intra- and intermolecular manners <cite>denHertog02</cite>. | ||
| − | === | + | === Controversial === |
| − | + | * PTPRN (IA-2) and PTPRN2. Human PTPRN and PTPRN2 have been proposed to be enzymatically inactive due to mutations at catalytic Cx5R motif and WPD motif <cite>Kharitidi13</cite>. However, PTPRN2 has been reported to be phosphatidylinositol phosphatase <cite>Caromile10</cite>. | |
=== References === | === References === | ||
<biblio> | <biblio> | ||
| + | #Caromile10 pmid=20097759 | ||
#denHertog02 pmid=12376545 | #denHertog02 pmid=12376545 | ||
| + | #Kharitidi13 pmid=24064037 | ||
</biblio> | </biblio> | ||
Revision as of 05:27, 10 March 2015
List of pseudophosphatases
To be added.
Functions
- Receptor PTPs. Most receptor PTPs have two tandem phosphatase domains. The 2nd phosphatase domain has no or negligible activity. The 2nd domain can interact with 1st domain in both intra- and intermolecular manners [1].
Controversial
- PTPRN (IA-2) and PTPRN2. Human PTPRN and PTPRN2 have been proposed to be enzymatically inactive due to mutations at catalytic Cx5R motif and WPD motif [2]. However, PTPRN2 has been reported to be phosphatidylinositol phosphatase [3].
References
Error fetching PMID 20097759:
Error fetching PMID 12376545:
Error fetching PMID 24064037:
Error fetching PMID 12376545:
Error fetching PMID 24064037:
- Error fetching PMID 12376545:
- Error fetching PMID 24064037:
- Error fetching PMID 20097759:
