Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Phosphatidylinositol 5-phosphate 4-kinase type-2 alpha  

UniProtKB / Swiss-Prot ID :  PI42A_HUMAN

Gene Name (Synonyms) : 
PIP4K2A, PIP5K2, PIP5K2A  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cell membrane (By similarity). Nucleus. Cytoplasm. Note=May translocate from the cytosol to the cell membrane upon activation of tyrosine phosphorylation. May translocate from the inner to the outer segments of the rod photoreceptor cells in response to  

Protein Function :  Catalyzes the phosphorylation of phosphatidylinositol 5- phosphate (PtdIns5P) on the fourth hydroxyl of the myo-inositol ring, to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). May exert its function by regulating the levels of PtdIns5P, which functions in the cytosol by increasing AKT activity and in the nucleus signals through ING2. May regulate the pool of cytosolic PtdIns5P in response to the activation of tyrosine phosphorylation. May negatively regulate insulin- stimulated glucose uptake by lowering the levels of PtdIns5P. May be involved in thrombopoiesis, and the terminal maturation of megakaryocytes and regulation of their size. 

Protein Sequence MATPGNLGSSVLASKTKTKKKHFVAQKVKLFRASDPLLSVLMWGVNHSINELSHVQIPVMLMPDDFKAYS...
Predicted Secondary Structure  -
Protein Variant
LocationDescription
7L -> I (in dbSNP:rs11813789). VAR_059764
251N -> S (in dbSNP:rs10828317). VAR_024565
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MATPGN
---
23.62UniProtKB
Link-
3Phosphothreonine--MATPGNL
--
30.36HPRD
Link-
3Phosphothreonine--MATPGNL
--
30.36Phosphositeplus
Link-
3Phosphothreonine--MATPGNL
--
30.36SysPTM
Link-
3Phosphothreonine.--MATPGNL
--
30.36UniProtKB
Link-
9PhosphoserineGNLGSSVLA
22.05HPRD
Link-
9Phosphoserine.GNLGSSVLA
22.05UniProtKB
Link-
10PhosphoserineNLGSSVLAS
21.25Phosphositeplus
Link-
14PhosphoserineSVLASKTKT
36.38HPRD
Link-
14PhosphoserineSVLASKTKT
36.38Phosphositeplus
Link-
14PhosphoserineSVLASKTKT
36.38SysPTM
Link-
14Phosphoserine.SVLASKTKT
36.38UniProtKB
Link-
89N6-acetyllysinePSHFKFKEY
50.53HPRD
Link
89N6-acetyllysinePSHFKFKEY
50.53Phosphositeplus
Link
89N6-acetyllysine.PSHFKFKEY
50.53UniProtKB
Link
93PhosphotyrosineKFKEYCPMV
11.48PhosphoELM
Link
93PhosphotyrosineKFKEYCPMV
11.48Phosphositeplus
Link
93Phosphotyrosine.KFKEYCPMV
11.48UniProtKB
Link
145N6-acetyllysineRYIIKTITS
25.06HPRD
Link
145N6-acetyllysineRYIIKTITS
25.06Phosphositeplus
Link
145N6-acetyllysine.RYIIKTITS
25.06UniProtKB
Link
246PhosphotyrosineGQKIYIDDN
12.82Phosphositeplus
Link
304PhosphoserineEEGESDGTH
52.80Phosphositeplus
Link-
304Phosphoserine (CK2_alpha)EEGESDGTH
52.80PhosphoELM
Link-
304Phosphoserine.EEGESDGTH
52.80UniProtKB
Link-
312Phosphothreonine.HPVGTPPDS
31.70UniProtKB
Link-
316Phosphoserine.TPPDSPGNT
40.24UniProtKB
Link-
320Phosphothreonine.SPGNTLNSS
32.98UniProtKB
Link-
376PhosphothreonineHAAKTVKHG
30.02Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
RAC1_HUMANin vitro
in vivo
HPRD:11931HPRD7629060
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-89 AND LYS-145, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3 AND SER-14, AND MASSSPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3; SER-9; SER-14;SER-304; THR-312; SER-316 AND THR-320, AND MASS SPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-93, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures