PIP5K1A
entrez
8394
canonical
uniprot
Q99755
canonical
ensembl
ENSG00000143398
resolver
ensp
ENSP00000271663
resolver
ensp
ENSP00000357883
resolver
ensp
ENSP00000357885
resolver
ensp
ENSP00000386432
resolver
ensp
ENSP00000415648
resolver
ensp
ENSP00000578553
resolver
ensp
ENSP00000578554
resolver
ensp
ENSP00000578556
resolver
ensp
ENSP00000578558
resolver
ensp
ENSP00000597495
resolver
ensp
ENSP00000597502
resolver
ensp
ENSP00000665417
resolver
ensp
ENSP00000665418
resolver
ensp
ENSP00000747549
resolver
ensp
ENSP00000747553
resolver
enst
ENST00000409426
resolver
genesymbol
PIP5K1A
resolver
hgnc
HGNC:8994
resolver
uniprot
A6PW57
resolver
uniprot
A8K4Q0
resolver
uniprot
B4DIN0
resolver
uniprot
Q99754
resolver
uniprot
Q99756
resolver
uniprot_entry
A6PW57_HUMAN
resolver
uniprot_entry
PI51A_HUMAN
resolver
uniprot_sec
A8K4Q0
resolver
uniprot_sec
B4DIN0
resolver
uniprot_sec
Q99754
resolver
uniprot_sec
Q99756
resolver
activity_regulation
ACTIVITY REGULATION: Activated by diarachidonoyl phosphatidic acid (DAPA), when 1,2-dipalmitoyl-PI4P is used as a substrate. {ECO:0000269|PubMed:22942276}.
uniprot
proteins
amino_acid_sequence
MASASSGPSSSVGFSSFDPAVPSCTLSSAASGIKRPMASEVLEARQDSYISLVPYASGMPIKKIGHRSVDSSGETTYKKTTSSALKGAIQLGITHTVGSLSTKPERDVLMQDFYVVESIFFPSEGSNLTPAHHYNDFRFKTYAPVAFRYFRELFGIRPDDYLYSLCSEPLIELCSSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQAGGKNIRIVVMNNLLPRSVKMHIKYDLKGSTYKRRASQKEREKPLPTFKDLDFLQDIPDGLFLDADMYNALCKTLQRDCLVLQSFKIMDYSLLMSIHNIDHAQREPLSSETQYSVDTRRPAPQKALYSTAMESIQGEARRGGTMETDDHMGGIPARNSKGERLLLYIGIIDILQSYRFVKKLEHSWKALVHDGDTVSVHRPGFYAERFQRFMCNTVFKKIPLKPSPSKKFRSGSSFSRRAGSSGNSCITYQPSVSGEHKAQVTTKAEVEPGVHLGRPDVLPQTPPLEEISEGSPIPDPSFSPLVGETLQMLTTSTTLEKLEVAESEFTH
uniprot
proteins
ec_number
2.7.1.68
uniprot
proteins
function
FUNCTION: Catalyzes the phosphorylation of phosphatidylinositol 4-phosphate (PtdIns(4)P/PI4P) to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2/PIP2), a lipid second messenger that regulates several cellular processes such as signal transduction, vesicle trafficking, actin cytoskeleton dynamics, cell adhesion, and cell motility (PubMed:21477596, PubMed:22942276, PubMed:8955136). PtdIns(4,5)P2 can directly act as a second messenger or can be utilized as a precursor to generate other second messengers: inositol 1,4,5-trisphosphate (IP3), diacylglycerol (DAG) or phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3/PIP3) (PubMed:19158393, PubMed:20660631). PIP5K1A-mediated phosphorylation of PtdIns(4)P is the predominant pathway for PtdIns(4,5)P2 synthesis (By similarity). Can also use phosphatidylinositol (PtdIns) as substrate in vitro (PubMed:22942276). Together with PIP5K1C, is required for phagocytosis, both enzymes regulating different types of actin remodeling at sequential steps (By similarity). Promotes particle ingestion by activating the WAS GTPase-binding protein that induces Arp2/3 dependent actin polymerization at the nascent phagocytic cup (By similarity). Together with PIP5K1B, is required, after stimulation by G protein coupled receptors, for the synthesis of IP3 that will induce stable platelet adhesion (By similarity). Recruited to the plasma membrane by the E-cadherin/beta-catenin complex where it provides the substrate PtdIns(4,5)P2 for the production of PtdIns(3,4,5)P3, IP3 and DAG, that will mobilize internal calcium and drive keratinocyte differentiation (PubMed:19158393). Positively regulates insulin-induced translocation of SLC2A4 to the cell membrane in adipocytes (By similarity). Together with PIP5K1C has a role during embryogenesis (By similarity). Independently of its catalytic activity, is required for membrane ruffling formation, actin organization and focal adhesion formation during directional cell migration by controlling integrin-induced translocation of the small GTPase RAC1 to the plasma membrane (PubMed:20660631). Also functions in the nucleus where it acts as an activator of TUT1 adenylyltransferase activity in nuclear speckles, thereby regulating mRNA polyadenylation of a select set of mRNAs (PubMed:18288197). {ECO:0000250|UniProtKB:P70182, ECO:0000269|PubMed:18288197, ECO:0000269|PubMed:19158393, ECO:0000269|PubMed:20660631, ECO:0000269|PubMed:21477596, ECO:0000269|PubMed:22942276, ECO:0000269|PubMed:8955136}.
uniprot
proteins
mass_dalton
62633
uniprot
proteins
mutagenesis
MUTAGEN 215; /note="L->I: Decreased 1-phosphatidylinositol-4-phosphate 5-kinase activity with 1-octadecanoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phospho-1D-myo-inositol 4-phosphate (arachidonate-PtdIns4P) as substrate. Increased enzyme activation by diarachidonoyl phosphatidic acid (DAPA). No change in enzyme activation by 1-stearoyl-2-oleoyl phosphatidic acid (SOPA) or 1-stearoyl-2-arachidonoyl phosphatidic acid (SAPA)."; /evidence="ECO:0000269|PubMed:21477596, ECO:0000269|PubMed:22942276"; MUTAGEN 223; /note="L->I: Decreased 1-phosphatidylinositol-4-phosphate 5-kinase activity with 1-octadecanoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phospho-1D-myo-inositol 4-phosphate (arachidonate-PtdIns4P) as substrate. Increased enzyme activation by diarachidonoyl phosphatidic acid (DAPA). No change in enzyme activation by 1-stearoyl-2-oleoyl phosphatidic acid (SOPA) or 1-stearoyl-2-arachidonoyl phosphatidic acid (SAPA)."; /evidence="ECO:0000269|PubMed:22942276"; MUTAGEN 322; /note="D->A: Increased enzyme activation by diarachidonoyl phosphatidic acid (DAPA)."; /evidence="ECO:0000269|PubMed:22942276"; MUTAGEN 322; /note="D->N: Does not affect targeting of RAC1 to the plasma membrane; when associated with Q-440."; /evidence="ECO:0000269|PubMed:20660631"; MUTAGEN 440; /note="R->Q: Does not affect targeting of RAC1 to the plasma membrane; when associated with N-322."; /evidence="ECO:0000269|PubMed:20660631
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15157668
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
18288197
uniprot
proteins
pubmed
19158393
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20660631
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21477596
uniprot
proteins
pubmed
22942276
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
31091439
uniprot
proteins
pubmed
8955136
uniprot
proteins
sequence_length
562
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19158393}. Cytoplasm {ECO:0000250|UniProtKB:P70182}. Nucleus {ECO:0000269|PubMed:15157668}. Nucleus speckle {ECO:0000269|PubMed:18288197}. Cell projection, ruffle {ECO:0000269|PubMed:20660631}. Cell projection, lamellipodium {ECO:0000269|PubMed:15157668}. Note=Colocalizes with RAC1 at actin-rich membrane ruffles (PubMed:20660631). Localizes to nuclear speckles and associates with TUT1 to regulate polyadenylation of selected mRNAs (PubMed:18288197). {ECO:0000269|PubMed:18288197, ECO:0000269|PubMed:20660631}.
uniprot
proteins