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Protein Page:
PIP5K1A (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
PIP5K1A Catalyzes the phosphorylation of phosphatidylinositol 4- phosphate (PtdIns4P) to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). PtdIns(4,5)P2 is involved in a variety of cellular processes and is the substrate to form phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3), another second messenger. The majority of PtdIns(4,5)P2 is thought to occur via type I phosphatidylinositol 4-phosphate 5-kinases given the abundance of PtdIns4P. Participates in a variety of cellular processes such as actin cytoskeleton organization, cell adhesion, migration and phagocytosis. Required for membrane ruffling formation, actin organization and focal adhesion formation during directional cell migration by controlling integrin-induced translocation of RAC1 to the plasma membrane. Together with PIP5K1C is required for phagocytosis, but they regulate different types of actin remodeling at sequential steps. Promotes particle ingestion by activating WAS that induces Arp2/3 dependent actin polymerization at the nascent phagocytic cup. Together with PIP5K1B is required after stimulation of G-protein coupled receptors for stable platelet adhesion. Plays a role during calcium-induced keratinocyte differentiation. 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, diacylglycerol and inositol 1,4,5-trisphosphate that mobilize internal calcium and drive keratinocyte differentiation. Together with PIP5K1C have a role during embryogenesis. Functions also in the nucleus where acts as an activator of TUT1 adenylyltransferase activity in nuclear speckles, thereby regulating mRNA polyadenylation of a select set of mRNAs. Interacts with RAC1. Interacts with TUT1. Forms a complex with CDH1/E-cadherin, CTNNB1/beta-catenin and CTNND1 at the plasma membrane upon calcium stimulation. Highly expressed in heart, placenta, skeletal muscle, kidney and pancreas. Detected at lower levels in brain, lung and liver. 4 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Carbohydrate Metabolism - inositol phosphate; Motility/polarity/chemotaxis; EC 2.7.1.68; Kinase, lipid
Cellular Component: lamellipodium; cytoplasm; plasma membrane; nucleolus; nuclear speck; mRNA cleavage and polyadenylation specificity factor complex; cytosol; nucleus
Molecular Function: protein binding; 1-phosphatidylinositol-4-phosphate 5-kinase activity; kinase binding; ATP binding
Biological Process: focal adhesion formation; keratinocyte differentiation; cell migration; activation of Rac GTPase; phosphoinositide phosphorylation; phospholipid metabolic process; actin cytoskeleton reorganization; phosphatidylinositol biosynthetic process; glycerophospholipid metabolic process; signal transduction; phagocytosis; phospholipid biosynthetic process
Reference #:  Q99755 (UniProtKB)
Alt. Names/Synonyms: 68 kDa type I phosphatidylinositol-4-phosphate 5-kinase alpha; Phosphatidylinositol-4-phosphate 5-kinase type I alpha; Phosphatidylinositol-4-phosphate 5-kinase type-1 alpha; phosphatidylinositol-4-phosphate 5-kinase, type I, alpha; PI51A; PIP5K1-alpha; PIP5K1A; PIP5KIalpha; PtdIns(4)P-5-kinase 1 alpha
Gene Symbols: PIP5K1A
Molecular weight: 62,633 Da
Basal Isoelectric point: 8.41  Predict pI for various phosphorylation states
CST Pathways:  Actin Dynamics  |  PI3K/Akt Signaling
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

PIP5K1A

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

► Hide Isoforms
 
0 4 S39 GIKRPMASEVLEARQ
0 18 Y55-p SYISLVPyASGMPIK
0 2 S57 ISLVPyASGMPIKKI
0 1 S68-p IKKIGHRsVDSSGET
0 128 K103-u TVGSLSTkPERDVLM
0 6 Y142-p NDFRFKTyAPVAFRY
0 4 K206-u KEAEFLQkLLPGYYM
0 43 Y346-p PLSSETQySVDTRRP
0 70 Y360-p PAPQKALySTAMESI
0 1 K413 LQSYRFVKKLEHSWK
0 3 S458-p KKIPLKPsPsKKFRS
0 2 S460-p IPLKPsPsKKFRSGS
0 2 A473 GSSFSRRAGsSGNsC
0 10 S475-p SFSRRAGsSGNsCIt
0 2 S479-p RAGsSGNsCItyQPs
0 3 T482-p sSGNsCItyQPsVSG
0 149 Y483-p SGNsCItyQPsVSGE
0 1 S486-p sCItyQPsVSGEHKA
0 5 T516-p RPDVLPQtPPLEEIs
0 1 S523-p tPPLEEIsEGSPIPD
0 1 S534-p PIPDPSFsPLVGEtL
0 1 T540-p FsPLVGEtLQMLTTS
  PIP5K1A iso2  
S38-p GIKRPMAsEVPyAsG
Y42-p PMAsEVPyAsGMPIK
S44-p AsEVPyAsGMPIKKI
S55 IKKIGHRSVDSSGET
K90 TVGSLSTKPERDVLM
Y129-p NDFRFKTyAPVAFRY
K193 KEAEFLQKLLPGYYM
Y333-p PLSSETQySVDTRRP
Y347 PAPQKALYSTAMESI
K400 LQSYRFVKKLEHSWK
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
T454 RPDVLPQTPPLEEIS
S461 TPPLEEISEGSPIPD
S472 PIPDPSFSPLVGETL
T478 FSPLVGETLQMLTTS
  PIP5K1A iso4  
S39-p GIKRPMAsEVPyAsG
Y43-p PMAsEVPyAsGMPIK
S45-p AsEVPyAsGMPIKKI
S56 IKKIGHRSVDSSGET
K91 TVGSLSTKPERDVLM
Y130 NDFRFKTYAPVAFRY
K194 KEAEFLQKLLPGYYM
Y334 PLSSETQYSVDTRRP
Y348 PAPQKALYSTAMESI
K373-u ETDDQFVkKLEHSWK
S418 KKIPLKPSPSKKFRS
S420 IPLKPSPSKKFRSGS
A433 GSSFSRRAGSSGNSC
S435 SFSRRAGSSGNSCIT
S439 RAGSSGNSCITYQPS
T442 SSGNSCITYQPSVSG
Y443 SGNSCITYQPSVSGE
S446 SCITYQPSVSGEHKA
T476 RPDVLPQTPPLEEIS
S483 TPPLEEISEGSPIPD
S494 PIPDPSFSPLVGETL
T500 FSPLVGETLQMLTTS
  mouse

 
S36-p GIKRATVsEGPsAsV
S40-p ATVsEGPsAsVMPVK
S42-p VsEGPsAsVMPVKKI
S53 VKKIGHRSVDSSGET
K88-u TVGSLSTkPERDVLM
Y127 NDFRFKTYAPVAFRY
K191-u KEAEFLQkLLPGYYM
Y331 PTSNDTQYSADTRRP
Y345 PAPQKALYSTAMESI
K398 LQSYRFVKKLEHSWK
S443 KKIPLKPSPTKKFRS
T445 IPLKPSPTKKFRSGP
S458-p GPSFSRRsGPSGNSC
P460 SFSRRsGPSGNSCTS
S464 RsGPSGNSCTSQLMA
T466 GPSGNSCTSQLMASG
S467 PSGNSCTSQLMASGE
M470 NSCTSQLMASGEHRA
T500 RPDVLPQTPPLEEIS
S507 TPPLEEISEGSPVPG
S518 PVPGPSFSPVVGQPL
P524 FSPVVGQPLQILNLS
  rat

 
S35 GIKRGTVSEGPYASL
Y39 GTVSEGPYASLMPVK
S41 VSEGPYASLMPVKKI
S52 VKKIGHRSVDSSGET
K87 TVGSLSTKPERDVLM
Y126 NDFRFKTYAPVAFRY
K190 KEAEFLQKLLPGYYM
Y330 PMNSETQYSIDTRRP
Y344 PAPQKALYSTAMESI
K397 LQSYRFVKKLEHSWK
S442 KKIPLKPSPTKKFRS
T444 IPLKPSPTKKFRSGP
S457 GPSFSRRSGPSGNSC
P459 SFSRRSGPSGNSCTP
S463 RSGPSGNSCTPSQPT
T465 GPSGNSCTPSQPTAS
S467 SGNSCTPSQPTASGE
T470 SCTPSQPTASGEHKA
T500 RPDVLPQTPPLEEIS
S507 TPPLEEISEGSPVPG
S518 PVPGPSFSPAVGQPL
P524 FSPAVGQPLQILNLS
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