PIP5K1C
entrez
23396
canonical
uniprot
O60331
canonical
ensembl
ENSG00000186111
resolver
ensp
ENSP00000335333
resolver
ensp
ENSP00000444779
resolver
ensp
ENSP00000445992
resolver
ensp
ENSP00000466363
resolver
ensp
ENSP00000546679
resolver
ensp
ENSP00000546681
resolver
ensp
ENSP00000737918
resolver
ensp
ENSP00000737920
resolver
genesymbol
PIP5K1C
resolver
genesymbol_syn
KIAA0589
resolver
hgnc
HGNC:8996
resolver
uniprot
B7Z9E7
resolver
uniprot
C6GIJ7
resolver
uniprot
C6GIJ8
resolver
uniprot
Q7LE07
resolver
uniprot_entry
PI51C_HUMAN
resolver
uniprot_sec
B7Z9E7
resolver
uniprot_sec
C6GIJ7
resolver
uniprot_sec
C6GIJ8
resolver
uniprot_sec
Q7LE07
resolver
amino_acid_sequence
MELEVPDEAESAEAGAVPSEAAWAAESGAAAGLAQKKAAPTEVLSMTAQPGPGHGKKLGHRGVDASGETTYKKTTSSTLKGAIQLGIGYTVGHLSSKPERDVLMQDFYVVESIFFPSEGSNLTPAHHFQDFRFKTYAPVAFRYFRELFGIRPDDYLYSLCNEPLIELSNPGASGSLFYVTSDDEFIIKTVMHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQSGGKNIRVVVMNNILPRVVKMHLKFDLKGSTYKRRASKKEKEKSFPTYKDLDFMQDMPEGLLLDADTFSALVKTLQRDCLVLESFKIMDYSLLLGVHNIDQHERERQAQGAQSTSDEKRPVGQKALYSTAMESIQGGAARGEAIESDDTMGGIPAVNGRGERLLLHIGIIDILQSYRFIKKLEHTWKALVHDGDTVSVHRPSFYAERFFKFMSNTVFRKNSSLKSSPSKKGRGGALLAVKPLGPTAAFSASQIPSEREEAQYDLRGARSYPTLEDEGRPDLLPCTPPSFEEATTASIATTLSSTSLSIPERSPSETSEQPRYRRRTQSSGQDGRPQEEPPAEEDLQQITVQVEPACSVEIVVPKEEDAGVEASPAGASAAVEVETASQASDEEGAPASQASDEEDAPATDIYFPTDERSWVYSPLHYSAQAPPASDGESDT
uniprot
proteins
disease_involvement
DISEASE: Lethal congenital contracture syndrome 3 (LCCS3) [MIM:611369]: A form of lethal congenital contracture syndrome, an autosomal recessive disorder characterized by degeneration of anterior horn neurons, extreme skeletal muscle atrophy, and congenital non-progressive joint contractures (arthrogryposis). The contractures can involve the upper or lower limbs and/or the vertebral column, leading to various degrees of flexion or extension limitations evident at birth. LCCS3 patients present at birth with severe multiple joint contractures and severe muscle wasting and atrophy, mainly in the legs. Death occurs minutes to hours after birth due to respiratory insufficiency. The phenotype can be distinguished from that of LCCS1 by the absence of hydrops, fractures and multiple pterygia, and from LCCS2 by the absence of neurogenic bladder defect. {ECO:0000269|PubMed:17701898}. Note=The disease is caused by variants affecting the gene represented in this entry.
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:12422219, PubMed:22942276). 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) (Probable). 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 (By similarity). 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 (By similarity). Controls the plasma membrane pool of PtdIns(4,5)P2 implicated in synaptic vesicle endocytosis and exocytosis (PubMed:12847086). Plays a role in endocytosis mediated by clathrin and AP-2 (adaptor protein complex 2) (PubMed:12847086). Required for clathrin-coated pits assembly at the synapse (PubMed:17261850). Participates in cell junction assembly (PubMed:17261850). Modulates adherens junctions formation by facilitating CDH1/cadherin trafficking (PubMed:17261850). Required for focal adhesion dynamics. Modulates the targeting of talins (TLN1 and TLN2) to the plasma membrane and their efficient assembly into focal adhesions (PubMed:12422219). Regulates the interaction between talins (TLN1 and TLN2) and beta-integrins (PubMed:12422219). Required for uropodium formation and retraction of the cell rear during directed migration (By similarity). Has a role in growth factor-stimulated directional cell migration and adhesion (By similarity). 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 (By similarity). Negatively regulates integrin alpha-L/beta-2 (LFA-1) polarization and adhesion induced by T-cell receptor (By similarity). Together with PIP5K1A has a role during embryogenesis and together with PIP5K1B may have a role immediately after birth (By similarity). {ECO:0000250|UniProtKB:O70161, ECO:0000250|UniProtKB:P70182, ECO:0000269|PubMed:12422219, ECO:0000269|PubMed:12847086, ECO:0000269|PubMed:17261850, ECO:0000269|PubMed:17635937, ECO:0000269|PubMed:22942276, ECO:0000305|PubMed:19889969}.
uniprot
proteins
mass_dalton
73260
uniprot
proteins
mutagenesis
MUTAGEN 650; /note="S->D: Abolishes binding to TLN2. Affects localization to focal adhesions."; /evidence="ECO:0000269|PubMed:15738269"; MUTAGEN 650; /note="S->N: Does not affect binding to TLN2 and localization to focal adhesions."; /evidence="ECO:0000269|PubMed:15738269
uniprot
proteins
post_translational_modification
PTM: Phosphorylation on Ser-650 negatively regulates binding to TLN2 and is strongly stimulated in mitosis. Phosphorylation on Tyr-649 is necessary for targeting to focal adhesions. Phosphorylation on Ser-650 and Tyr-649 are mutually exclusive. Phosphorylated by SYK and CSK (By similarity). Tyrosine phosphorylation is enhanced by PTK2 signaling. Phosphorylated at Tyr-639 upon EGF stimulation. Some studies suggest that phosphorylation on Tyr-649 enhances binding to tailins (TLN1 and TLN2). According to PubMed:15738269 phosphorylation at Tyr-649 does not directly enhance binding to tailins (TLN1 and TLN2) but may act indirectly by inhibiting phosphorylation at Ser-650. {ECO:0000250, ECO:0000269|PubMed:15738269}.; PTM: Acetylation at Lys-265 and Lys-268 seems to decrease lipid 1-phosphatidylinositol-4-phosphate 5-kinase activity. Deacetylation of these sites by SIRT1 positively regulates the exocytosis of TSH-containing granules from pituitary cells. {ECO:0000269|PubMed:20668706}.
uniprot
proteins
pubmed
12422219
uniprot
proteins
pubmed
12847086
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15057824
uniprot
proteins
pubmed
15738269
uniprot
proteins
pubmed
17261850
uniprot
proteins
pubmed
17635937
uniprot
proteins
pubmed
17701898
uniprot
proteins
pubmed
19548880
uniprot
proteins
pubmed
19889969
uniprot
proteins
pubmed
20668706
uniprot
proteins
pubmed
22942276
uniprot
proteins
pubmed
25588945
uniprot
proteins
pubmed
9628581
uniprot
proteins
sequence_length
668
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:0000250|UniProtKB:O70161}. Cell junction, focal adhesion {ECO:0000269|PubMed:12422219}. Cell junction, adherens junction {ECO:0000269|PubMed:17261850}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:Q5I6B8}. Cell projection, phagocytic cup {ECO:0000250|UniProtKB:O70161}. Cell projection, uropodium {ECO:0000250|UniProtKB:O70161}. Note=Detected in plasma membrane invaginations. Isoform 3 is detected in intracellular vesicle-like structures.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. Nucleus.
uniprot
proteins