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Protein Page:
PIP5K1C (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
PIP5K1C a member of the type I phosphatidylinositol-4-phosphate 5-kinase family of enzymes. A similar protein in mice is found in synapses and focal adhesion plaques, and binds the FERM domain of talin through its C-terminus. Note: This description may include information from UniProtKB.
Protein type: Motility/polarity/chemotaxis; Kinase, lipid; EC 2.7.1.68; Carbohydrate Metabolism - inositol phosphate
Cellular Component: focal adhesion; endomembrane system; uropod; nucleus; cytosol; phagocytic cup
Molecular Function: 1-phosphatidylinositol-4-phosphate 5-kinase activity; ATP binding
Biological Process: axon guidance; neutrophil chemotaxis; synaptic vesicle exocytosis; cell-cell adhesion; cytoskeletal anchoring; phospholipid metabolic process; synaptic vesicle endocytosis; phosphatidylinositol biosynthetic process; actin cytoskeleton organization and biogenesis; phagocytosis
Reference #:  O60331 (UniProtKB)
Alt. Names/Synonyms: diphosphoinositide kinase; Human homolog of mouse phosphatidylinositol-4-phosphate 5-kinase I-gamma; KIAA0589; LCCS3; Phosphatidylinositol-4-phosphate 5-kinase type I gamma; Phosphatidylinositol-4-phosphate 5-kinase type-1 gamma; phosphatidylinositol-4-phosphate 5-kinase, type I, gamma; PI51C; PIP5K-GAMMA; PIP5K1-gamma; PIP5K1C; PIP5Kgamma; PIP5KIgamma; PIPKIg_v4; PtdIns(4)P-5-kinase 1 gamma; type I PIP kinase
Gene Symbols: PIP5K1C
Molecular weight: 73,260 Da
Basal Isoelectric point: 5.17  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

PIP5K1C

Protein Structure Not Found.


STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB  |  ENZYME  |  Phospho3D  |  InnateDB  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene


Sites Implicated In
cell adhesion, altered: S650‑p
cytoskeletal reorganization: S650‑p
intracellular localization: S650‑p
molecular association, regulation: Y649‑p, S650‑p
phosphorylation: Y649‑p, S650‑p

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

 
0 1 S11 EVPDEAESAEAGAVP
0 1 T47-p PTEVLSMtAQPGPGH
0 101 K97-u TVGHLSSkPERDVLM
0 9 Y136-p QDFRFKTyAPVAFRY
0 5 K200-u KEAEFLQkLLPGYYM
0 2 T215-p NLNQNPRtLLPKFYG
0 1 K414-u KKLEHTWkALVHDGD
0 1 N447 SNTVFRKNSSLKSSP
0 1 S448 NTVFRKNSSLKSSPS
0 2 S449 TVFRKNSSLKSSPSK
0 1 S452 RKNSSLKSSPSKKGR
0 2 S453 KNSSLKSSPSKKGRG
0 1 R459 SSPSKKGRGGALLAV
0 1 R459 SSPSKKGRGGALLAV
0 2 S496-p YDLRGARsYPTLEDE
0 2 S544-p ERSPSETsEQPRYRR
0 39 T553 QPRYRRRTQSsGQDG
0 28 S555 RYRRRTQSsGQDGRP
0 9 S556-p YRRRTQSsGQDGRPQ
1 0 Y639 DAPATDIYFPTDERS
0 2 - gap
6 0 Y649-p TDERSWVysPLHYSA
2 1 S650-p DERSWVysPLHYSAQ
0 4 S662 SAQAPPASDGESDT_
0 1 S666 PPASDGESDT_____
  mouse

► Hide Isoforms
 
S11-gl EVPDEAEsAEAGAVT
T47 LAEAPLVTGQPGPGH
K97-u TVGNLSSkPERDVLM
Y136 QDFRFKTYAPVAFRY
K200-u KEAEFLQkLLPGYYM
T215 NLNQNPRTLLPKFYG
K414 KKLEHTWKALVHDGD
S447-p SSTVFRKsssLKssP
S448-p STVFRKsssLKssPS
S449-p TVFRKsssLKssPSK
S452-p RKsssLKssPSKKGr
S453-p KsssLKssPSKKGrG
R459-m1 ssPSKKGrGALLAVK
R459-m2 ssPSKKGrGALLAVK
S495 YDLRGARSYPTLEDE
S543-p ERSPSDTsEQPRYRR
T552-p QPRYRRRtQssGQDG
S554-p RYRRRtQssGQDGRP
S555-p YRRRtQssGQDGRPQ
Y634-p DAPSTDIyFPTDERS
- gap
Y644-p TDERSWVysPLHYSA
S645-p DERSWVysPLHYSAR
S655-p HYSARPAsDGEsDT_
S659-p RPAsDGEsDT_____
  PIP5K1C iso2  
S11 EVPDEAESAEAGAVT
T47 LAEAPLVTGQPGPGH
K97 TVGNLSSKPERDVLM
Y136 QDFRFKTYAPVAFRY
K200 KEAEFLQKLLPGYYM
T215 NLNQNPRTLLPKFYG
K354 KKLEHTWKALVHDGD
S387 SSTVFRKSSSLKSSP
S388 STVFRKSSSLKSSPS
S389 TVFRKSSSLKSSPSK
S392 RKSSSLKSSPSKKGR
S393 KSSSLKSSPSKKGRG
R399 SSPSKKGRGALLAVK
R399 SSPSKKGRGALLAVK
S435 YDLRGARSYPTLEDE
S483 ERSPSDTSEQPRYRR
T492 QPRYRRRTQSSGQDG
S494 RYRRRTQSSGQDGRP
S495 YRRRTQSSGQDGRPQ
Y574 DAPSTDIYFFAHGRY
S585-p HGRYWLFsPRRRQLR
Y610 TDERSWVYSPLHYSA
S611 DERSWVYSPLHYSAR
S621 HYSARPASDGESDT_
S625 RPASDGESDT_____
  rat

 
S11 EVPDEAESAEAGAVT
T47 LAEAPLVTGQPGPGH
K97-u TVGNLSSkPERDVLM
Y136-p QDFRFKTyAPVAFRY
K200-u KEAEFLQkLLPGYYM
T215 NLNQNPRTLLPKFYG
K414 KKLEHTWKALVHDGD
S447 SSTVFRKSSSLKSSP
S448 STVFRKSSSLKSSPS
S449 TVFRKSSSLKSSPSK
S452 RKSSSLKSSPSKKGR
S453 KSSSLKSSPSKKGRG
R459 SSPSKKGRGALLAVK
R459 SSPSKKGRGALLAVK
S495 YDLRGARSYPTLEDE
S543 ERSPSDTSEQPRYRR
T552-p QPRYRRRtQssGQDG
S554-p RYRRRtQssGQDGRP
S555-p YRRRtQssGQDGRPQ
Y635 DAPSTDIYFFAHGRY
S646 HGRYWLFSPRRRRLR
Y671 TDGRSWVYSPLHYSA
S672 DGRSWVYSPLHYSAR
S682 HYSARPASDGESDT_
S686 RPASDGESDT_____
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