http://rdf.ncbi.nlm.nih.gov/pubchem/conserveddomain/PSSMID340437

Outgoing Links

Predicate Object
abstract Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in 1-phosphatidylinositol-3-phosphate 5-kinase and similar proteins. 1-phosphatidylinositol-3-phosphate 5-kinase (EC 2.7.1.150) is also called FYVE finger-containing phosphoinositide kinase, PIKfyve, phosphatidylinositol 3-phosphate 5-kinase (PIP5K3), or phosphatidylinositol 3-phosphate 5-kinase type III (PIPkin-III or type III PIP kinase). It forms a complex with its regulators, the scaffolding protein Vac14 and the lipid phosphatase Fig4. The complex is responsible for synthesizing phosphatidylinositol 3,5-bisphosphate [PtdIns(3,5)P2] by catalyzing the phosphorylation of phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) on the fifth hydroxyl of the myo-inositol ring. Then phosphatidylinositol-5-phosphate (PtdIns5P) is generated directly from PtdIns(3,5)P2. PtdIns(3,5)P2 and PtdIns5P regulate endosomal trafficking and responses to extracellular stimuli. PIKfyve is vital in early embryonic development. It forms a complex with ArPIKfyve (associated regulator of PIKfyve) and SAC3 at the endomembranes, playing a role in receptor tyrosine kinase (RTK) degradation. The phosphorylation of PIKfyve by AKT can facilitate epidermal growth factor receptor (EGFR) degradation. In addition, PIKfyve may participate in the regulation of the glutamate transporters EAAT2, EAAT3 and EAAT4, and the cystic fibrosis transmembrane conductance regulator (CFTR). It is also essential for systemic glucose homeostasis and insulin-regulated glucose uptake/GLUT4 translocation in skeletal muscle. It can be activated by protein kinase B (PKB/Akt) and further up-regulates human Ether-a-go-go-Related Gene (hERG) channels. This family also includes the yeast ortholog of human PIKfyve, Fab1. PIKfyve and its orthologs share a similar architecture. They contain an N-terminal FYVE domain, a middle region related to the CCT/TCP-1/Cpn60 chaperonins that are involved in productive folding of actin and tubulin, a second middle domain that contains a number of conserved cysteine residues (CCR) unique to this family, and a C-terminal catalytic lipid kinase domain related to PtdInsP kinases (or the PIPKc domain).
title PIPKc_PIKfyve
isDiscussedBy http://rdf.ncbi.nlm.nih.gov/pubchem/reference/32754841
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/371532
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/30956524
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/3195719
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/9137751
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/1730623
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/17384707
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/27480146
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/3176698
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/14512221
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/1720391
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/13859900
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/16744778
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/33645537
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/28194245
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/24238340
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/32941164
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/7228832
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/26150621
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/14010628
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/20766623
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/28920952
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/32301218
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/24811823
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/23243235
type http://purl.obolibrary.org/obo/SO_0000417

Incoming Links

Predicate Subject
has component http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCQ9SSJ8
http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCQ9Y2I7
http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCNP_055855
http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCQ9Z1T6
http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCO96838
http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCQ9LUM0
http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCQ0WUR5
http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCB0G126
http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCQ9XID0

Total number of triples: 37.