UniProt ID: A0A8M6Z8L8 |
FUNCTION: GTPase-activating protein for the ADP ribosylation factor family. {ECO:0000256|RuleBase:RU369028}. ACTIVITY REGULATION: GAP activity stimulated by phosphatidylinositol 4,5-bisphosphate (PIP2) and phosphatidic acid. {ECO:0000256|RuleBase:RU369028}. SUBCELLULAR LOCATION: Endosome membrane {ECO:0000256|RuleBase:RU369028}; Peripheral membrane protein {ECO:0000256|RuleBase:RU369028}. DOMAIN: PH domain binds phospholipids including phosphatidic acid, phosphatidylinositol 3-phosphate, phosphatidylinositol 3,5-bisphosphate (PIP2) and phosphatidylinositol 3,4,5-trisphosphate (PIP3). May mediate protein binding to PIP2 or PIP3 containing membranes. {ECO:0000256|RuleBase:RU369028}. DOMAIN: The BAR domain mediates homodimerization, it can neither bind membrane nor impart curvature, but instead requires the neighboring PH domain to achieve these functions. {ECO:0000256|RuleBase:RU369028}. |
UniProt ID: A0A8M9QLG2 |
FUNCTION: GTPase-activating protein for the ADP ribosylation factor family. {ECO:0000256|RuleBase:RU369028}. ACTIVITY REGULATION: GAP activity stimulated by phosphatidylinositol 4,5-bisphosphate (PIP2) and phosphatidic acid. {ECO:0000256|RuleBase:RU369028}. SUBCELLULAR LOCATION: Endosome membrane {ECO:0000256|RuleBase:RU369028}; Peripheral membrane protein {ECO:0000256|RuleBase:RU369028}. DOMAIN: PH domain binds phospholipids including phosphatidic acid, phosphatidylinositol 3-phosphate, phosphatidylinositol 3,5-bisphosphate (PIP2) and phosphatidylinositol 3,4,5-trisphosphate (PIP3). May mediate protein binding to PIP2 or PIP3 containing membranes. {ECO:0000256|RuleBase:RU369028}. DOMAIN: The BAR domain mediates homodimerization, it can neither bind membrane nor impart curvature, but instead requires the neighboring PH domain to achieve these functions. {ECO:0000256|RuleBase:RU369028}. |
UniProt ID: A2RUY3 |
FUNCTION: GTPase-activating protein for the ADP ribosylation factor family. {ECO:0000256|RuleBase:RU369028}. ACTIVITY REGULATION: GAP activity stimulated by phosphatidylinositol 4,5-bisphosphate (PIP2) and phosphatidic acid. {ECO:0000256|RuleBase:RU369028}. SUBCELLULAR LOCATION: Endosome membrane {ECO:0000256|RuleBase:RU369028}; Peripheral membrane protein {ECO:0000256|RuleBase:RU369028}. DOMAIN: PH domain binds phospholipids including phosphatidic acid, phosphatidylinositol 3-phosphate, phosphatidylinositol 3,5-bisphosphate (PIP2) and phosphatidylinositol 3,4,5-trisphosphate (PIP3). May mediate protein binding to PIP2 or PIP3 containing membranes. {ECO:0000256|RuleBase:RU369028}. DOMAIN: The BAR domain mediates homodimerization, it can neither bind membrane nor impart curvature, but instead requires the neighboring PH domain to achieve these functions. {ECO:0000256|RuleBase:RU369028}. |
UniProt ID: A0A8M9QCW6 |
FUNCTION: GTPase-activating protein for the ADP ribosylation factor family. {ECO:0000256|RuleBase:RU369028}. ACTIVITY REGULATION: GAP activity stimulated by phosphatidylinositol 4,5-bisphosphate (PIP2) and phosphatidic acid. {ECO:0000256|RuleBase:RU369028}. SUBCELLULAR LOCATION: Endosome membrane {ECO:0000256|RuleBase:RU369028}; Peripheral membrane protein {ECO:0000256|RuleBase:RU369028}. DOMAIN: PH domain binds phospholipids including phosphatidic acid, phosphatidylinositol 3-phosphate, phosphatidylinositol 3,5-bisphosphate (PIP2) and phosphatidylinositol 3,4,5-trisphosphate (PIP3). May mediate protein binding to PIP2 or PIP3 containing membranes. {ECO:0000256|RuleBase:RU369028}. DOMAIN: The BAR domain mediates homodimerization, it can neither bind membrane nor impart curvature, but instead requires the neighboring PH domain to achieve these functions. {ECO:0000256|RuleBase:RU369028}. |
This information was provided by UniProt through a collaboration with ZFIN. (1) |