Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteprivacy & cookiesCuration ProcessContact
logos LINCs Logo Mt Sinai Logo NIH Logo NCI Logo
Protein Page:
PIP4K2B (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
PIP4K2B Participates in the biosynthesis of phosphatidylinositol 4,5-bisphosphate. Homodimer. Binds TNFRSF1A. Interacts with PIP4K2A. Interaction with PIP4K2A suppresses ubiquitination by the SPOP/ CUL3 complex. Highly expressed in brain, heart, pancreas, skeletal muscle and kidney. Detected at lower levels in placenta, lung and liver. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: EC 2.7.1.149; Kinase, lipid; Motility/polarity/chemotaxis; Carbohydrate Metabolism - inositol phosphate
Chromosomal Location of Human Ortholog: 17q12
Cellular Component: autophagic vacuole; cytosol; nucleoplasm
Molecular Function: 1-phosphatidylinositol-4-phosphate 5-kinase activity; 1-phosphatidylinositol-5-phosphate 4-kinase activity; protein binding; receptor signaling protein activity
Biological Process: cell surface receptor linked signal transduction; phosphatidylinositol biosynthetic process; regulation of autophagy; regulation of phosphoinositide 3-kinase cascade
Reference #:  P78356 (UniProtKB)
Alt. Names/Synonyms: 1-phosphatidylinositol-4-phosphate kinase; 1-phosphatidylinositol-5-phosphate 4-kinase 2-beta; Diphosphoinositide kinase 2-beta; phosphatidylinositol-4-phosphate 5-kinase, type II, beta; Phosphatidylinositol-5-phosphate 4-kinase type II beta; Phosphatidylinositol-5-phosphate 4-kinase type-2 beta; phosphatidylinositol-5-phosphate 4-kinase, type II, beta; PI(5)P 4-kinase type II beta; PI42B; PI5P4KB; PIP4K2B; PIP4KII-beta; PIP5K2B; PIP5KIIB; PIP5KIIbeta; PTDINS(4)P-5-kinase; PtdIns(5)P-4-kinase isoform 2-beta
Gene Symbols: PIP4K2B
Molecular weight: 47,378 Da
Basal Isoelectric point: 6.9  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

PIP4K2B

Protein Structure Not Found.
Download PyMol Script
Download ChimeraX Script


STRING  |  cBioPortal  |  Wikipedia  |  Reactome  |  neXtProt  |  Protein Atlas  |  BioGPS  |  Scansite  |  Pfam  |  RCSB PDB  |  ENZYME  |  Phospho3D  |  Phospho.ELM  |  NetworKIN  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene


Sites Implicated In
enzymatic activity, inhibited: S326‑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



 LTP 

LTP: 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.


 HTP 

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


       human

► Hide Isoforms
 
0 1 S7 _MSSNCTSTTAVAVA
0 1 T8 MSSNCTSTTAVAVAP
0 1 T9 SSNCTSTTAVAVAPL
0 3 S17‑p AVAVAPLsASKTKTK
0 33 Y98‑p SRFKFKEyCPMVFRN
0 2 S124‑p YQNSVTRsAPINSDS
0 4 K150‑ac YDRRFVIkTVSSEDV
0 1 Y167‑p MHNILKKyHQFIVEC
0 1 T196‑p LTVDGVEtyMVVTRN
0 1 Y197‑p TVDGVEtyMVVTRNV
0 1 S256‑p KLHVGEEsKKNFLEK
0 1 K263 sKKNFLEKLKRDVEF
0 1 S319 VGGNLLCSYGtPPDs
0 1 Y320 GGNLLCSYGtPPDsP
0 29 T322‑p NLLCSYGtPPDsPGN
1 22 S326‑p SYGtPPDsPGNLLSF
0 1 S332 DsPGNLLSFPRFFGP
0 1 Y363‑p SSPKKEVyFMAIIDI
0 1 K385‑ac KKAAHAAkTVKHGAG
  PIP4K2B iso2  
S7 _MSSNCTSTTAVAVA
T8 MSSNCTSTTAVAVAP
T9 SSNCTSTTAVAVAPL
S17 AVAVAPLSASKTKTK
Y98 SRFKFKEYCPMVFRN
S124 YQNSVTRSAPINSDS
K150 YDRRFVIKTVSSEDV
Y167 MHNILKKYHQFIVEC
T196 LTVDGVETYMVVTRN
Y197 TVDGVETYMVVTRNV
S256 KLHVGEESKKNFLEK
K263 SKKNFLEKLKRDVEE
- gap
- gap
- gap
- gap
- gap
- gap
- gap
  mouse

 
S7‑p _MSSNCTsttAVAVA
T8‑p MSSNCTsttAVAVAP
T9‑p SSNCTsttAVAVAPL
S17‑p AVAVAPLsASKTKTK
Y98‑p SRFKFKEyCPMVFRN
S124 YQNSVTRSAPINSDS
K150 YDRRFVIKTVSSEDV
Y167 MHNILKKYHQFIVEC
T196 LTVDGVETYMVVTRN
Y197 TVDGVETYMVVTRNV
S256 KLHVGEESKKNFLEK
K263 SKKNFLEKLKRDVEF
S319‑p VGGSLLCsyGtPPDs
Y320‑p GGSLLCsyGtPPDsP
T322‑p SLLCsyGtPPDsPGN
S326‑p syGtPPDsPGNLLsF
S332‑p DsPGNLLsFPRFFGP
Y363 SAPKKEVYFMAIIDI
K385 KKAAHAAKTVKHGAG
  rat

 
S7 _MSSNCTSTTAVAVA
T8 MSSNCTSTTAVAVAP
T9 SSNCTSTTAVAVAPL
S17 AVAVAPLSASKTKTK
Y98 SRFKFKEYCPMVFRN
S124 YQNSVTRSAPINSDS
K150‑ac YDRRFVIkTVSSEDV
Y167 MHNILKKYHQFIVEC
T196 LTVDGVETYMVVTRN
Y197 TVDGVETYMVVTRNV
S256 KLRVGEESKKNFLEk
K263‑ac SKKNFLEkLKRDVEF
S319 VGGGLLCSYGTPPDS
Y320 GGGLLCSYGTPPDSP
T322 GLLCSYGTPPDSPGN
S326 SYGTPPDSPGNLLSF
S332 DSPGNLLSFPRFFGP
Y363 SAPKKEVYFMAIIDI
K385 KKAAHAAKTVKHGAG
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.