Pip5k1c
entrez
18717
canonical
uniprot
O70161
canonical
ensembl
ENSMUSG00000034902
resolver
ensp
ENSMUSP00000038225
resolver
ensp
ENSMUSP00000100964
resolver
ensp
ENSMUSP00000124155
resolver
enst
ENSMUST00000045469
resolver
genesymbol
Pip5k1c
resolver
genesymbol_syn
Kiaa0589
resolver
uniprot
F8WHW6
resolver
uniprot
Q505A1
resolver
uniprot
Q80TW9
resolver
uniprot
Q8VCU5
resolver
uniprot_entry
F8WHW6_MOUSE
resolver
uniprot_entry
PI51C_MOUSE
resolver
uniprot_sec
Q505A1
resolver
uniprot_sec
Q80TW9
resolver
uniprot_sec
Q8VCU5
resolver
activity_regulation
ACTIVITY REGULATION: Activated by phosphatidic acid. {ECO:0000269|PubMed:9535851}.
uniprot
proteins
amino_acid_sequence
MELEVPDEAESAEAGAVTAEAAWSAESGAAAGMTQKKAGLAEAPLVTGQPGPGHGKKLGHRGVDASGETTYKKTTSSTLKGAIQLGIGYTVGNLSSKPERDVLMQDFYVVESIFFPSEGSNLTPAHHFQDFRFKTYAPVAFRYFRELFGIRPDDYLYSLCNEPLIELSNPGASGSVFYVTSDDEFIIKTVMHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQSGGKNIRVVVMNNVLPRVVKMHLKFDLKGSTYKRRASKKEKEKSLPTYKDLDFMQDMPEGLLLDSDTFGALVKTLQRDCLVLESFKIMDYSLLLGVHNIDQQERERQAEGAQSKADEKRPVAQKALYSTAMESIQGGAARGEAIETDDTMGGIPAVNGRGERLLLHIGIIDILQSYRFIKKLEHTWKALVHDGDTVSVHRPSFYAERFFKFMSSTVFRKSSSLKSSPSKKGRGALLAVKPLGPTAAFSASQIPSEREDVQYDLRGARSYPTLEDEGRPDLLPCTPPSFEEATTASIATTLSSTSLSIPERSPSDTSEQPRYRRRTQSSGQDGRPQEEPHAEDLQKITVQVEPVCGVGVVPKEEGAGVEVPPCGASAAASVEIDAASQASEPASQASDEEDAPSTDIYFPTDERSWVYSPLHYSARPASDGESDT
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:14741049, PubMed:20622009, PubMed:22942276, PubMed:9535851). 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) (By similarity). PIP5K1A-mediated phosphorylation of PtdIns(4)P is the predominant pathway for PtdIns(4,5)P2 synthesis (By similarity). Together with PIP5K1A, is required for phagocytosis, both enzymes regulating different types of actin remodeling at sequential steps (PubMed:19153220). Promotes particle attachment by generating the pool of PtdIns(4,5)P2 that induces controlled actin depolymerization to facilitate Fc-gamma-R clustering. Mediates RAC1-dependent reorganization of actin filaments. Required for synaptic vesicle transport (PubMed:15386003). Controls the plasma membrane pool of PtdIns(4,5)P2 implicated in synaptic vesicle endocytosis and exocytosis (By similarity). Plays a role in endocytosis mediated by clathrin and AP-2 (adaptor protein complex 2) (PubMed:16707488). Required for clathrin-coated pits assembly at the synapse (By similarity). Participates in cell junction assembly (By similarity). Modulates adherens junctions formation by facilitating CDH1/cadherin trafficking (By similarity). Required for focal adhesion dynamics (PubMed:12422220). Modulates the targeting of talins (TLN1 and TLN2) to the plasma membrane and their efficient assembly into focal adhesions (By similarity). Regulates the interaction between talins (TLN1 and TLN2) and beta-integrins (By similarity). Required for uropodium formation and retraction of the cell rear during directed migration (PubMed:17928408). Has a role in growth factor-stimulated directional cell migration and adhesion (PubMed:17635937). Required for talin assembly into nascent adhesions forming at the leading edge toward the direction of the growth factor (PubMed:17635937). Negative regulator of T-cell activation and adhesion (PubMed:20855869). Negatively regulates integrin alpha-L/beta-2 (LFA-1) polarization and adhesion induced by T-cell receptor (PubMed:20855869). Together with PIP5K1A has a role during embryogenesis and together with PIP5K1B may have a role immediately after birth (PubMed:17609388, PubMed:20622009). {ECO:0000250|UniProtKB:O60331, ECO:0000269|PubMed:12422220, ECO:0000269|PubMed:14741049, ECO:0000269|PubMed:15386003, ECO:0000269|PubMed:16707488, ECO:0000269|PubMed:17609388, ECO:0000269|PubMed:17635937, ECO:0000269|PubMed:17928408, ECO:0000269|PubMed:19153220, ECO:0000269|PubMed:20622009, ECO:0000269|PubMed:20855869, ECO:0000269|PubMed:22942276, ECO:0000269|PubMed:9535851}.
uniprot
proteins
mass_dalton
72408
uniprot
proteins
mutagenesis
MUTAGEN 253; /note="D->A: Abolishes lipid kinase activity. Does not affect targeting of TLN1 to plasma membrane. Affects assembly of TLN1 into focal adhesions. Affects uropodium formation and retraction of the cell rear."; /evidence="ECO:0000269|PubMed:12422220, ECO:0000269|PubMed:17928408"; MUTAGEN 634; /note="Y->F: Cannot rescue the effect PIP5K1C knockdown on EGF-stimulated cell migration. Does not affect lipid kinase activity. Does not alter binding to tailin. Decreased tailin assembly into focal adhesions. Increased interaction with PLCG1."; /evidence="ECO:0000269|PubMed:17635937"; MUTAGEN 635; /note="F->A: Abolishes interaction with AP2B1."; /evidence="ECO:0000269|PubMed:19287005"; MUTAGEN 642; /note="W->A: Abolishes interaction with AP2B1."; /evidence="ECO:0000269|PubMed:19287005"; MUTAGEN 644; /note="Y->F: Loss of phosphorylation by CSK. Abolishes interaction with AP-2 complex. Cannot rescue the effect PIP5K1C knockdown on EGF-stimulated cell migration."; /evidence="ECO:0000269|PubMed:14691141, ECO:0000269|PubMed:16707488, ECO:0000269|PubMed:17635937, ECO:0000269|PubMed:19287005"; MUTAGEN 645; /note="S->F: Cannot rescue the effect PIP5K1C knockdown on EGF-stimulated cell migration. Decreased tailin assembly into focal adhesions."; /evidence="ECO:0000269|PubMed:17635937"; MUTAGEN 646; /note="P->F: Abolishes interaction with AP-2 complex."; /evidence="ECO:0000269|PubMed:16707488"; MUTAGEN 647; /note="L->V: Abolishes interaction with AP-2 complex."; /evidence="ECO:0000269|PubMed:16707488
uniprot
proteins
post_translational_modification
PTM: Phosphorylation on Ser-645 negatively regulates binding to TLN2 and is strongly stimulated in mitosis. Phosphorylation on Tyr-644 is necessary for targeting to focal adhesions. Phosphorylation on Ser-645 and Tyr-644 are mutually exclusive. Phosphorylated by SYK and CSK. Tyrosine phosphorylation is enhanced by PTK2 signaling. Phosphorylated at Tyr-634 upon EGF stimulation. Some studies suggest that phosphorylation on Tyr-644 enhances binding to tailins (TLN1 and TLN2); others that phosphorylation at Tyr-644 does not directly enhance binding to tailins (TLN1 and TLN2) but may act indirectly by inhibiting phosphorylation at Ser-645. {ECO:0000269|PubMed:12422220, ECO:0000269|PubMed:14691141, ECO:0000269|PubMed:16707488, ECO:0000269|PubMed:17635937, ECO:0000269|PubMed:19153220}.; PTM: Acetylation at Lys-265 and Lys-268 seems to decrease lipid kinase activity. Deacetylation of these sites by SIRT1 positively regulates the exocytosis of TSH-containing granules from pituitary cells (By similarity). {ECO:0000250}.
uniprot
proteins
pubmed
12422220
uniprot
proteins
pubmed
12693553
uniprot
proteins
pubmed
14691141
uniprot
proteins
pubmed
14741049
uniprot
proteins
pubmed
15386003
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15623515
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16707488
uniprot
proteins
pubmed
17609388
uniprot
proteins
pubmed
17635937
uniprot
proteins
pubmed
17928408
uniprot
proteins
pubmed
19144319
uniprot
proteins
pubmed
19153220
uniprot
proteins
pubmed
19287005
uniprot
proteins
pubmed
20622009
uniprot
proteins
pubmed
20855869
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
22942276
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
9535851
uniprot
proteins
sequence_length
661
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side {ECO:0000250|UniProtKB:Q5I6B8}. Endomembrane system {ECO:0000250|UniProtKB:Q5I6B8}. Cytoplasm {ECO:0000269|PubMed:19153220, ECO:0000269|PubMed:20622009}. Cell junction, focal adhesion {ECO:0000269|PubMed:12422220, ECO:0000269|PubMed:14691141}. Cell junction, adherens junction {ECO:0000250|UniProtKB:O60331}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:Q5I6B8}. Cell projection, phagocytic cup {ECO:0000269|PubMed:19153220}. Cell projection, uropodium {ECO:0000269|PubMed:17928408}. Note=During directional migration isoform 1 localized at the uropodium, and isoform 3 localized all along cell membrane including the uropodium and the leading edge.
uniprot
proteins