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Field | Value |
---|---|
Namespace | Molecular function |
Short description | Phosphatidylinositol-3-phosphate binding |
Full defintion | Interacting selectively and non-covalently with phosphatidylinositol-3-phosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 3' position. |
Subterm of |
The relationship of GO:0032266 with other GO terms.
Relationship type | GO terms |
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Is a | |
Regulates | n.a. |
Part of | n.a. |
Positively regulates | n.a. |
Negatively regulates | n.a. |
A force layout showing the ancestor tree for GO:0032266, and its immediate children. If you wish to explore the tree dynamically, please use the GO Explorer.
This table contains additional metadata associated with the GO entry's definition field.
Field | Value |
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GOC | bf |
PMID | All phox homology (PX) domains from Saccharomyces cerevisiae specifically recognize phosphatidylinositol 3-phosphate. J Biol Chem. 2001 Nov 23; 276 (47): 44179–84.PMID: 11557775 Phox homology (PX) domains are named for a 130-amino acid region of homology shared with part of two components of the phagocyte NADPH oxidase (phox) complex. They are found in proteins involved in vesicular trafficking, protein sorting, and lipid modification. It was recently reported that certain PX domains specifically recognize phosphatidylinositol 3-phosphate (PtdIns-3-P) and drive recruitment of their host proteins to the cytoplasmic leaflet of endosomal and/or vacuolar membranes where this phosphoinositide is enriched. We have analyzed phosphoinositide binding by all 15 PX domains encoded by the Saccharomyces cerevisiae genome. All yeast PX domains specifically recognize PtdIns-3-P in protein-lipid overlay experiments, with just one exception (a significant sequence outlier). In surface plasmon resonance studies, four of the yeast PX domains bind PtdIns-3-P with high (micromolar range) affinity. Although the remaining PX domains specifically recognize PtdIns-3-P, they bind this lipid with only low affinity. Interestingly, many proteins with "low affinity" PX domains are known to form large multimeric complexes, which may increase the overall avidity for membranes. Our results establish that PtdIns-3-P, and not other phosphoinositides, is the target of all PX domains in S. cerevisiae and suggest a role for PX domains in assembly of multiprotein complexes at specific membrane surfaces. |
GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on , while the GO metadata was last updated on .
Transcript | Name | Description | GO terms | GO count |
---|---|---|---|---|
– | PREDICTED: vacuolar protein sorting-associated protein 36-like [Cicer arietinum] gi|502158471|ref|XP_004511164.1| | 2 | ||
– | Vacuolar protein sorting-associated protein 36; TAIR: AT5G04920.1 EAP30/Vps36 family protein; Swiss-Prot: sp|Q9FF81|VPS36_ARATH Vacuolar protein sorting-associated protein 36; TrEMBL-Plants: tr|V7AJ01|V7AJ01_PHAVU Uncharacterized protein; Found in the gene: LotjaGi3g1v0303100 | 2 | ||
– | Vacuolar protein sorting-associated protein 36; TAIR: AT5G04920.1 EAP30/Vps36 family protein; Swiss-Prot: sp|Q9FF81|VPS36_ARATH Vacuolar protein sorting-associated protein 36; TrEMBL-Plants: tr|V7AJ01|V7AJ01_PHAVU Uncharacterized protein; Found in the gene: LotjaGi3g1v0303100 | 2 | ||
– | Vacuolar protein sorting-associated protein 36; TAIR: AT5G04920.1 EAP30/Vps36 family protein; Swiss-Prot: sp|Q9FF81|VPS36_ARATH Vacuolar protein sorting-associated protein 36; TrEMBL-Plants: tr|V7AJ01|V7AJ01_PHAVU Uncharacterized protein; Found in the gene: LotjaGi3g1v0303100 | 2 |
A list of co-occurring GO terms within the L. japonicus gene space:
GO term | Namespace | Name | Observations | Saturation (%) |
---|---|---|---|---|
Molecular function | Ubiquitin binding | 1 | 25.00 |