Proteins
Curated comments from UniProt
Type | Comment | Proteins |
---|---|---|
DSP2_ARATH | function | Cleaves the beta-phosphate at the 5-position of soluble inositol pyrophosphates (PubMed:35640071). Has highest activity on 5-diphosphoinositol 1,2,3,4,6-pentakisphosphate (5-InsP(7)), 1,5-bis-diphosphoinositol 2,3,4,6-tetrakisphosphate (1,5-InsP(8)) and 3,5-InsP(8) (PubMed:35640071). Possesses phosphotyrosine phosphatase activity in vitro (PubMed:21409566). Dephosphorylates the phosphoinositides PI(3,5)P2 (PubMed:21409566). Hydrolyzes para-nitrophenyl phosphate and O-methylfluorescein phosphate in vitro (PubMed:17976645, PubMed:21409566). |
DSP2_ARATH | similarity | Belongs to the protein-tyrosine phosphatase family. Atypical dual-specificity phosphatase Siw14-like subfamily. |
DSP2_ARATH | tissue specificity | Expressed in roots, leaves, stems, flowers and siliques. |
Function
Gene Ontology
cellular component | |
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No terms in this category. | |
molecular function | |
protein tyrosine phosphatase activity | ECO |
identical protein binding | ECO |
inositol-3,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 5-diphosphatase activity | ECO |
phosphatase activity | ECO |
inositol-5-diphosphate-1,2,3,4,6-pentakisphosphate diphosphatase activity | ECO |
inositol-1,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 5-diphosphatase activity | ECO |
biological process | |
protein dephosphorylation | ECO |
Interactions
Interaction Network
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