PIKFYVE
entrez
200576
canonical
uniprot
Q9Y2I7
canonical
ensembl
ENSG00000115020
resolver
ensp
ENSP00000264380
resolver
ensp
ENSP00000376038
resolver
ensp
ENSP00000384356
resolver
ensp
ENSP00000405736
resolver
ensp
ENSP00000579857
resolver
ensp
ENSP00000593169
resolver
ensp
ENSP00000593170
resolver
ensp
ENSP00000593171
resolver
ensp
ENSP00000593172
resolver
ensp
ENSP00000593173
resolver
ensp
ENSP00000593174
resolver
ensp
ENSP00000593175
resolver
ensp
ENSP00000630215
resolver
ensp
ENSP00000630216
resolver
ensp
ENSP00000630217
resolver
genesymbol
PIKFYVE
resolver
genesymbol_syn
KIAA0981
resolver
genesymbol_syn
PIP5K3
resolver
hgnc
HGNC:23785
resolver
uniprot
Q08AR7
resolver
uniprot
Q08AR8
resolver
uniprot
Q53ST3
resolver
uniprot
Q53T36
resolver
uniprot
Q8N5H0
resolver
uniprot
Q8NB67
resolver
uniprot_entry
FYV1_HUMAN
resolver
uniprot_sec
Q08AR7
resolver
uniprot_sec
Q08AR8
resolver
uniprot_sec
Q53ST3
resolver
uniprot_sec
Q53T36
resolver
uniprot_sec
Q8N5H0
resolver
uniprot_sec
Q8NB67
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by apilimod and YM201636. {ECO:0000269|PubMed:22621786, ECO:0000269|PubMed:29584722, ECO:0000269|PubMed:30612035, ECO:0000269|PubMed:32221306}.
uniprot
proteins
amino_acid_sequence
MATDDKTSPTLDSANDLPRSPTSPSHLTHFKPLTPDQDEPPFKSAYSSFVNLFRFNKERAEGGQGEQQPLSGSWTSPQLPSRTQSVRSPTPYKKQLNEELQRRSSALDTRRKAEPTFGGHDPRTAVQLRSLSTVLKRLKEIMEGKSQDSDLKQYWMPDSQCKECYDCSEKFTTFRRRHHCRLCGQIFCSRCCNQEIPGKFMGYTGDLRACTYCRKIALSYAHSTDSNSIGEDLNALSDSACSVSVLDPSEPRTPVGSRKASRNIFLEDDLAWQSLIHPDSSNTPLSTRLVSVQEDAGKSPARNRSASITNLSLDRSGSPMVPSYETSVSPQANRTYVRTETTEDERKILLDSVQLKDLWKKICHHSSGMEFQDHRYWLRTHPNCIVGKELVNWLIRNGHIATRAQAIAIGQAMVDGRWLDCVSHHDQLFRDEYALYRPLQSTEFSETPSPDSDSVNSVEGHSEPSWFKDIKFDDSDTEQIAEEGDDNLANSASPSKRTSVSSFQSTVDSDSAASISLNVELDNVNFHIKKPSKYPHVPPHPADQKEYLISDTGGQQLSISDAFIKESLFNRRVEEKSKELPFTPLGWHHNNLELLREENGEKQAMERLLSANHNHMMALLQQLLHSDSLSSSWRDIIVSLVCQVVQTVRPDVKNQDDDMDIRQFVHIKKIPGGKKFDSVVVNGFVCTKNIAHKKMSSCIKNPKILLLKCSIEYLYREETKFTCIDPIVLQEREFLKNYVQRIVDVRPTLVLVEKTVSRIAQDMLLEHGITLVINVKSQVLERISRMTQGDLVMSMDQLLTKPHLGTCHKFYMQIFQLPNEQTKTLMFFEGCPQHLGCTIKLRGGSDYELARVKEILIFMICVAYHSQLEISFLMDEFAMPPTLMQNPSFHSLIEGRGHEGAVQEQYGGGSIPWDPDIPPESLPCDDSSLLELRIVFEKGEQENKNLPQAVASVKHQEHSTTACPAGLPCAFFAPVPESLLPLPVDDQQDALGSEQPETLQQTVVLQDPKSQIRAFRDPLQDDTGLYVTEEVTSSEDKRKTYSLAFKQELKDVILCISPVITFREPFLLTEKGMRCSTRDYFAEQVYWSPLLNKEFKEMENRRKKQLLRDLSGLQGMNGSIQAKSIQVLPSHELVSTRIAEHLGDSQSLGRMLADYRARGGRIQPKNSDPFAHSKDASSTSSGQSGSKNEGDEERGLILSDAVWSTKVDCLNPINHQRLCVLFSSSSAQSSNAPSACVSPWIVTMEFYGKNDLTLGIFLERYCFRPSYQCPSMFCDTPMVHHIRRFVHGQGCVQIILKELDSPVPGYQHTILTYSWCRICKQVTPVVALSNESWSMSFAKYLELRFYGHQYTRRANAEPCGHSIHHDYHQYFSYNQMVASFSYSPIRLLEVCVPLPKIFIKRQAPLKVSLLQDLKDFFQKVSQVYVAIDERLASLKTDTFSKTREEKMEDIFAQKEMEEGEFKNWIEKMQARLMSSSVDTPQQLQSVFESLIAKKQSLCEVLQAWNNRLQDLFQQEKGRKRPSVPPSPGRLRQGEESKISAMDASPRNISPGLQNGEKEDRFLTTLSSQSSTSSTHLQLPTPPEVMSEQSVGGPPELDTASSSEDVFDGHLLGSTDSQVKEKSTMKAIFANLLPGNSYNPIPFPFDPDKHYLMYEHERVPIAVCEKEPSSIIAFALSCKEYRNALEELSKATQWNSAEEGLPTNSTSDSRPKSSSPIRLPEMSGGQTNRTTETEPQPTKKASGMLSFFRGTAGKSPDLSSQKRETLRGADSAYYQVGQTGKEGTENQGVEPQDEVDGGDTQKKQLINPHVELQFSDANAKFYCRLYYAGEFHKMREVILDSSEEDFIRSLSHSSPWQARGGKSGAAFYATEDDRFILKQMPRLEVQSFLDFAPHYFNYITNAVQQKRPTALAKILGVYRIGYKNSQNNTEKKLDLLVMENLFYGRKMAQVFDLKGSLRNRNVKTDTGKESCDVVLLDENLLKMVRDNPLYIRSHSKAVLRTSIHSDSHFLSSHLIIDYSLLVGRDDTSNELVVGIIDYIRTFTWDKKLEMVVKSTGILGGQGKMPTVVSPELYRTRFCEAMDKYFLMVPDHWTGLGLNC
uniprot
proteins
disease_involvement
DISEASE: Corneal dystrophy, fleck (CFD) [MIM:121850]: A form of stromal corneal dystrophy characterized by numerous small white flecks scattered in all levels of the stroma, with configurations varying from semicircular to wreath-like, curvilinear, or punctate. Although CFD may occasionally cause mild photophobia, patients are typically asymptomatic and have normal vision. {ECO:0000269|PubMed:15902656}. Note=The disease is caused by variants affecting the gene represented in this entry.
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:23086417). The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) (PubMed:17556371, PubMed:41639454). 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:17556371, PubMed:41639454). Also catalyzes the phosphorylation of phosphatidylinositol on the fifth hydroxyl of the myo-inositol ring, to form phosphatidylinositol 5-phosphate (PtdIns(5)P) (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 (PubMed:33098764). 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 (PubMed:30612035). 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 (By similarity). 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 (PubMed:30612035). 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 (By similarity). 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, through association with SPAG9 and RABEPK (By similarity). Mediates EGFR trafficking to the nucleus (PubMed:17909029). {ECO:0000250|UniProtKB:Q9Z1T6, ECO:0000269|PubMed:17556371, ECO:0000269|PubMed:17909029, ECO:0000269|PubMed:22621786, ECO:0000269|PubMed:27623384, ECO:0000269|PubMed:28779020, ECO:0000269|PubMed:29584722, ECO:0000269|PubMed:30612035, ECO:0000269|PubMed:33098764, ECO:0000269|PubMed:41639454, ECO:0000303|PubMed:23086417}.; FUNCTION: (Microbial infection) Required for cell entry of coronaviruses SARS-CoV and SARS-CoV-2, as well as human coronavirus EMC (HCoV-EMC) by endocytosis. {ECO:0000269|PubMed:32221306}.
uniprot
proteins
mass_dalton
237136
uniprot
proteins
mutagenesis
MUTAGEN 1877; /note="K->E: Loss of autophosphorylation. Loss of phosphatidylinositol 3-phosphate 5-kinase activity."; /evidence="ECO:0000269|PubMed:33098764"; MUTAGEN 2053; /note="S->A: No effect on phosphatidylinositol 3-phosphate 5-kinase activity."; /evidence="ECO:0000269|PubMed:33098764"; MUTAGEN 2053; /note="S->E: Reduces 2-folds phosphatidylinositol 3-phosphate 5-kinase activity."; /evidence="ECO:0000269|PubMed:33098764
uniprot
proteins
post_translational_modification
PTM: Autophosphorylates which inhibits its own phosphatidylinositol 3-phosphate 5-kinase activity, stimulates FIG4 lipid phosphatase activity and down-regulates lipid product formation (PubMed:33098764). Dephosphorylated by FIG4 in the PI(3,5)P2 regulatory complex, at Ser-48, Ser-1669 and Ser-2053 (PubMed:33098764). Phosphorylated in response to insulin at Ser-318 in a protein kinase B (PKB)-dependent manner (PubMed:20513353). {ECO:0000269|PubMed:20513353, ECO:0000269|PubMed:33098764}.
uniprot
proteins
pubmed
10231032
uniprot
proteins
pubmed
11706043
uniprot
proteins
pubmed
14530284
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15144186
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15592455
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
15902656
uniprot
proteins
pubmed
17556371
uniprot
proteins
pubmed
17909029
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
18950639
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
20513353
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22621786
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23086417
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
27623384
uniprot
proteins
pubmed
28779020
uniprot
proteins
pubmed
29584722
uniprot
proteins
pubmed
30612035
uniprot
proteins
pubmed
32221306
uniprot
proteins
pubmed
33098764
uniprot
proteins
pubmed
41639454
uniprot
proteins
sequence_length
2098
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:11706043, ECO:0000269|PubMed:17556371}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9Z1T6}. Early endosome membrane {ECO:0000269|PubMed:30612035}; Peripheral membrane protein. Cytoplasmic vesicle, phagosome membrane {ECO:0000269|PubMed:30612035}; Peripheral membrane protein {ECO:0000305}. Late endosome membrane {ECO:0000269|PubMed:11706043}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9Z1T6}. Note=Mainly associated with membranes of the late endocytic pathway. {ECO:0000269|PubMed:11706043}.
uniprot
proteins