Pikfyve
entrez
18711
canonical
uniprot
Q9Z1T6
canonical
ensembl
ENSMUSG00000025949
resolver
ensp
ENSMUSP00000079926
resolver
ensp
ENSMUSP00000095314
resolver
ensp
ENSMUSP00000306421
resolver
ensp
ENSMUSP00000306422
resolver
ensp
ENSMUSP00000306423
resolver
ensp
ENSMUSP00000306424
resolver
ensp
ENSMUSP00000326974
resolver
ensp
ENSMUSP00000326975
resolver
enst
ENSMUST00000081154
resolver
genesymbol
Pikfyve
resolver
genesymbol_syn
Fab1
resolver
genesymbol_syn
Kiaa0981
resolver
genesymbol_syn
Pip5k3
resolver
uniprot
D3Z5N5
resolver
uniprot
E9QL40
resolver
uniprot
Q3TNE4
resolver
uniprot
Q3UTT6
resolver
uniprot
Q69ZU1
resolver
uniprot
Q9CU94
resolver
uniprot_entry
D3Z5N5_MOUSE
resolver
uniprot_entry
FYV1_MOUSE
resolver
uniprot_sec
E9QL40
resolver
uniprot_sec
Q3TNE4
resolver
uniprot_sec
Q3UTT6
resolver
uniprot_sec
Q69ZU1
resolver
uniprot_sec
Q9CU94
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by apilimod and YM201636. {ECO:0000269|PubMed:22621786, ECO:0000269|PubMed:28779020, ECO:0000305|PubMed:11123925}.
uniprot
proteins
amino_acid_sequence
MATDDKSSPTLDSANDLPRSPASPSHLTHFKPLTPDQDEPPFKSAYSSFVNLFRFNKERGEGGQGEQQSPSSSWASPQIPSRTQSVRSPVPYKKQLNEELHRRSSVLDSRRKAEPACGGHDPRTAVQLRSLSTVLKRLKEIMEGKSQDSDLKQYWMPDSQCKECYDCSEKFTTFRRRHHCRLCGQIFCSRCCNQEIPGKFMGYTGDLRACTYCRKIALSYAHSTDSNSIGEDLNALSDSTCSVSILDPSEPRTPVGSRKASRNIFLEDDLAWQSLIHPDSSNSALSTRLVSVQEDAGKSPARNRSASITNLSLDRSGSPMVPSYETSVSPQANRNYIRTETTEDERKILLDSAQLKDLWKKICHHTSGMEFQDHRYWLRTHPNCIVGKELVNWLIRNGHIATRAQAIAIGQAMVDGRWLDCVSHHDQLFRDEYALYRPLQSTEFSETPSPDSDSVNSVEGHSEPSWFKDIKFDDSDTEQIAEEGDDNLANSASPSKRTSVSSFQSTVDSDSAASISLNVELDNVNFHIKKPSKYPHVPPHPADQKEYLVSDTGGQQLSISDAFIKESLFNRRVEEKSKELPFTPLGWHHNNLELLREENEEKQAMERLLSANHNHMMALLQQLLQNESLSSSWRDIIVSLVCQVVQTVRPDVKHQDDDMDIRQFVHIKKIPGGKKFDSVVVNGFVCTKNIAHKKMNSCIKNPKILLLKCSIEYLYREETKFTCIDPIVLQEREFLKNYVQRIVDVRPTLVLVEKTVSRIAQDMLLEHGITLVINVKSQVLERISRMTQGDLVVSMDQLLTKPHLGTCHKFYMQIFQLPNEQTKTLMFFEGCPQHLGCTIKLRGGSDYELARVKEILIFMICVAYHSQLEISFLMDEFAMPPTLMQSPSFHLLTEGRGEEGASQEQVSGSSLPQDPECPREALSSEDSTLLESRTVLEKGELDNKSIPQAVASLKHQDYTTPTCPAGIPCALFALVPESLLPLHMDQQDAVGNEQPETSQQTDEQQDPKSQMKAFRDPLQDDTGMYVTEEVTSSEDQRKTYALTFKQELKDVILCISPVITFREPFLLTEKGMRCSTRDYFPEQIYWSPLLNKEVKEMESRRKKQLLRDLSGLQGMNGSVQAKSIQVLPSHELVSTRIAEHLGDSQTLGRMLADYRARGGRIQSKHLDPFVHSKDASCTSGGKSGNKTESDEERGLIPSDVIWPTKVDCLNPANHQRLCVLFSSSSAQSSNAPSACVSPWIVTMEFYGKNDLTLGIFLERYCFRSSYQCPSMFCDTPMVHHIRRFVHGQGCVQIILKELDSPVPGYQHTILTYSWCRICKQVTPVVALSNESWSMSFAKYLELRFYGHQYTRRANAEPCGHSIHHDYHQYFSYNQMVASFSYSPIRLLEVCVPLPKIFIKRQAPLKVSLLQDLKDFFQKVSQVYLAVDERLASLKTDTFSKTREEKMEDIFAQKEMEEGEFKNWTEKMQARLMSSSVDTPQQLQSIFESLIAKKQSLCEVLQAWNSRLQDLFQQEKGRKRPSVPPSPGRLRQGEESKINAMDTSPRNISPGLHNGEKEDRFLTTLSSQSSTSSTHLQLPTPPEALAEQVVGGPTDLDSASGSEDVFDGHLLGSTDSQVKEKSTMKAIFANLLPGNSYNPIPFPFDPDKHYLMYEHERVPIAVCEKEPSSIIAFALSCKEYRNALEELSKATLRNSAEEGLPANSALDNRPKSSSPIRLPEISGGQTNRTVEAEPQPTKKASGMLSFFRGTAGKSPDLSSQKRETLRGADSAYYQVGQAGKEGLESQGLEPQDEVDGGDTQKKQLTNPHVELQFSDANAKFYCRLYYAGEFHKMREVILGSSEEEFIRSLSHSSPWQARGGKSGAAFYATEDDRFILKQMPRLEVQSFLDFAPHYFNYITNAVQQKRPTALAKILGVYRIGYKNSQNNTEKKLDLLVMENLFYGRKMAQVFDLKGSLRNRNVKTDTGKESCDVVLLDENLLKMVRDNPLYIRSHSKSVLRTSIHSDAHFLSSHLIIDYSLLVGRDDTSNELVVGIIDYIRTFTWDKKLEMVVKSTGILGGQGKMPTVVSPELYRTRFCEAMDKYFLMVPDHWTGLDLNC
uniprot
proteins
ec_number
2.7.1.150
uniprot
proteins
ec_number
2.7.11.1
uniprot
proteins
function
FUNCTION: Dual specificity kinase implicated in myriad essential cellular processes such as maintenance of endomembrane homeostasis, and endocytic-vacuolar pathway, lysosomal trafficking, nuclear transport, stress- or hormone-induced signaling and cell cycle progression (PubMed:17909029, PubMed:19037259, PubMed:22621786). The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Sole enzyme to catalyze the phosphorylation of phosphatidylinositol 3-phosphate on the fifth hydroxyl of the myo-inositol ring, to form (PtdIns(3,5)P2) (PubMed:10419465, PubMed:10567352). Also catalyzes the phosphorylation of phosphatidylinositol on the fifth hydroxyl of the myo-inositol ring, to form phosphatidylinositol 5-phosphate (PtdIns(5)P) (PubMed:10419465, PubMed:22621786). Has serine-protein kinase activity and is able to autophosphorylate and transphosphorylate. Autophosphorylation inhibits its own phosphatidylinositol 3-phosphate 5-kinase activity, stimulates FIG4 lipid phosphatase activity and down-regulates lipid product formation (By similarity) (PubMed:11123925). Involved in key endosome operations such as fission and fusion in the course of endosomal cargo transport (PubMed:22621786). Required for the maturation of early into late endosomes, phagosomes and lysosomes (By similarity). Regulates vacuole maturation and nutrient recovery following engulfment of macromolecules, initiates the redistribution of accumulated lysosomal contents back into the endosome network (PubMed:27623384). Critical regulator of the morphology, degradative activity, and protein turnover of the endolysosomal system in macrophages and platelets (PubMed:25178411, PubMed:31427458). In neutrophils, critical to perform chemotaxis, generate ROS, and undertake phagosome fusion with lysosomes (PubMed:28779020). Plays a key role in the processing and presentation of antigens by major histocompatibility complex class II (MHC class II) mediated by CTSS (By similarity). Regulates melanosome biogenesis by controlling the delivery of proteins from the endosomal compartment to the melanosome (PubMed:29584722). Essential for systemic glucose homeostasis, mediates insulin-induced signals for endosome/actin remodeling in the course of GLUT4 translocation/glucose uptake activation (PubMed:22621786, PubMed:23673157). Synthesis if (PtdIns(3,5)P2) is required for the cGAS-STING pathway (PubMed:41639454). Supports microtubule-based endosome-to-trans-Golgi network cargo transport, trhough association with SPAG9 and RABEPK (PubMed:14530284, PubMed:19056739). Mediates EGFR trafficking to the nucleus (PubMed:17909029). {ECO:0000250|UniProtKB:Q9Y2I7, ECO:0000269|PubMed:10419465, ECO:0000269|PubMed:10567352, ECO:0000269|PubMed:11123925, ECO:0000269|PubMed:14530284, ECO:0000269|PubMed:17909029, ECO:0000269|PubMed:19037259, ECO:0000269|PubMed:19056739, ECO:0000269|PubMed:22621786, ECO:0000269|PubMed:23673157, ECO:0000269|PubMed:25178411, ECO:0000269|PubMed:27623384, ECO:0000269|PubMed:28779020, ECO:0000269|PubMed:29584722, ECO:0000269|PubMed:31427458, ECO:0000269|PubMed:41639454}.
uniprot
proteins
mass_dalton
236877
uniprot
proteins
mutagenesis
MUTAGEN 1831; /note="K->E: Loss of kinase activity. Decreases RABEPK location to membranes. Abolishes EGFR translocation to the nucleus."; /evidence="ECO:0000269|PubMed:11123925, ECO:0000269|PubMed:14530284, ECO:0000269|PubMed:17909029
uniprot
proteins
post_translational_modification
PTM: Phosphorylated in response to insulin at Ser-318 in a protein kinase B (PKB)-dependent manner (PubMed:20513353). Autophosphorylates which down-regulates lipid product formation (PubMed:11123925). {ECO:0000269|PubMed:11123925, ECO:0000269|PubMed:20513353}.; PTM: Autophosphorylates which inhibits its own phosphatidylinositol 3-phosphate 5-kinase activity, stimulates FIG4 lipid phosphatase activity and down-regulates lipid product formation (PubMed:11123925). Dephosphorylated by FIG4 in the PI(3,5)P2 regulatory complex, at Ser-48, Ser-1668 and Ser-2052 (By similarity). Phosphorylated in response to insulin at Ser-318 in a protein kinase B (PKB)-dependent manner (PubMed:20513353). {ECO:0000250|UniProtKB:Q9Y2I7, ECO:0000269|PubMed:11123925, ECO:0000269|PubMed:20513353}.
uniprot
proteins
pubmed
10419465
uniprot
proteins
pubmed
10567352
uniprot
proteins
pubmed
11123925
uniprot
proteins
pubmed
14530284
uniprot
proteins
pubmed
15368895
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17242355
uniprot
proteins
pubmed
17909029
uniprot
proteins
pubmed
17956977
uniprot
proteins
pubmed
19037259
uniprot
proteins
pubmed
19056739
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
20513353
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21349843
uniprot
proteins
pubmed
22621786
uniprot
proteins
pubmed
23673157
uniprot
proteins
pubmed
25178411
uniprot
proteins
pubmed
27623384
uniprot
proteins
pubmed
28779020
uniprot
proteins
pubmed
29584722
uniprot
proteins
pubmed
31427458
uniprot
proteins
pubmed
41639454
uniprot
proteins
pubmed
9858586
uniprot
proteins
sequence_length
2097
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endosome membrane {ECO:0000305|PubMed:19037259, ECO:0000305|PubMed:21349843}; Peripheral membrane protein {ECO:0000269|PubMed:19037259}. Early endosome membrane {ECO:0000250|UniProtKB:Q9Y2I7}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9Y2I7}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:Q9Y2I7}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9Y2I7}. Late endosome membrane {ECO:0000250|UniProtKB:Q9Y2I7}; Peripheral membrane protein {ECO:0000305}. Note=Mainly associated with membranes of the late endocytic pathway. {ECO:0000250|UniProtKB:Q9Y2I7}.
uniprot
proteins