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 gamma  

UniProtKB / Swiss-Prot ID :  PI42C_HUMAN

Gene Name (Synonyms) : 
PIP4K2C, PIP5K2C  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. Membrane. Note=Mostly found in the cytosol and surrounding plasma membrane. However, its presence in the endoplasmic reticulum seems to be a prerequisite for PIP2 synthesis (By similarity). 

Protein Function :  May play an important role in the production of Phosphatidylinositol bisphosphate (PIP2), in the endoplasmic reticulum (By similarity). 

Protein Sequence MASSSVPPATVSAATAGPGPGFGFASKTKKKHFVQQKVKVFRAADPLVGVFLWGVAHSINELSQVPPPVM...
Predicted Secondary Structure  -
Protein Variant
LocationDescription
84V -> A (in dbSNP:rs17550713). VAR_032049
241K -> R (in dbSNP:rs17852569). VAR_032050
300A -> G (in dbSNP:rs2277319). VAR_032051
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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.---MASSSV
---
20.37UniProtKB
Link-
26PhosphoserineFGFASKTKK
38.30HPRD
Link-
26PhosphoserineFGFASKTKK
38.30Phosphositeplus
Link-
26Phosphoserine.FGFASKTKK
38.30UniProtKB
Link-
208PhosphoserineRNMFSHRLP
9.27HPRD
Link
208PhosphoserineRNMFSHRLP
9.27Phosphositeplus
Link
281PhosphotyrosineKIMDYSLLL
5.48HPRD
Link
328PhosphoserineSYGTSPEGI
19.32HPRD
Link-
349PhosphoserineGEFESFIDV
32.59HPRD
Link-
349PhosphoserineGEFESFIDV
32.59Phosphositeplus
Link-
349Phosphoserine.GEFESFIDV
32.59UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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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.
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 SER-26 AND SER-349, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures