Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2  

UniProtKB / Swiss-Prot ID :  VIP2_HUMAN

Gene Name (Synonyms) : 
PPIP5K2, HISPPD1, KIAA0433, VIP2  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm, cytosol. 

Protein Function :  Bifunctional inositol kinase that catalyzes the formation of diphosphoinositol pentakisphosphate (InsP7 or PP- InsP5) and bi-diphosphoinositol tetrakisphosphate (InsP8 or PP2- InsP4). Converts inositolitol hexakisphosphate (InsP6) to InsP7. Also able to convert InsP7 to InsP8. Probably specifically mediates the formation of 4PP-InsP5 and 6PP-InsP5 InsP7 isomers but not of 5PP-IP5 InsP7 isomer. 

Protein Sequence MSEAPRFFVGPEDTEINPGNYRHFFHHADEDDEEEDDSPPERQIVVGICSMAKKSKSKPMKEILERISLF...
Predicted Secondary Structure  -
Protein Variant
LocationDescription
944A -> G (in dbSNP:rs17155115). VAR_038276
985E -> K (in dbSNP:rs12519525). VAR_038277
1003R -> K (in dbSNP:rs12520040). VAR_038278
1206P -> Q (in dbSNP:rs17155138). VAR_038279
1232T -> M (in dbSNP:rs17155147). VAR_038280
- top -

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
- top -

Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
21PhosphotyrosineNPGNYRHFF
16.04Phosphositeplus
Link-
38PhosphoserineEEDDSPPER
55.46HPRD
Link-
38PhosphoserineEEDDSPPER
55.46Phosphositeplus
Link-
38PhosphoserineEEDDSPPER
55.46SysPTM
Link-
38Phosphoserine.EEDDSPPER
55.46UniProtKB
Link-
248N6-acetyllysineGTDVKVYTV
32.13Phosphositeplus
Link
270N6-acetyllysineALDGKVERD
40.36Phosphositeplus
Link
491PhosphothreonineGCPKTSSEE
23.72HPRD
Link-
492PhosphoserineCPKTSSEEE
41.71HPRD
Link-
493PhosphoserinePKTSSEEED
55.01Phosphositeplus
Link-
498PhosphoserineEEEDSRREE
36.20Phosphositeplus
Link-
504PhosphoserineREEPSLLLV
34.62HPRD
Link-
504Phosphoserine.REEPSLLLV
34.62UniProtKB
Link-
694PhosphoserineQLYHSETLE
20.79HPRD
Link-
1006PhosphoserineRRRRSGEQI
44.89HPRD
Link-
1006PhosphoserineRRRRSGEQI
44.89Phosphositeplus
Link-
1006PhosphoserineRRRRSGEQI
44.89SysPTM
Link-
1006Phosphoserine.RRRRSGEQI
44.89UniProtKB
Link-
1011PhosphothreonineGEQITSSPV
23.89Phosphositeplus
Link-
1012PhosphoserineEQITSSPVS
33.98HPRD
Link-
1013PhosphoserineQITSSPVSP
22.22SysPTM
Link-
1016PhosphoserineSSPVSPKSL
29.96HPRD
Link-
1016PhosphoserineSSPVSPKSL
29.96Phosphositeplus
Link-
1016PhosphoserineSSPVSPKSL
29.96SysPTM
Link-
1016Phosphoserine.SSPVSPKSL
29.96UniProtKB
Link-
1172PhosphoserineALRSSPIMR
16.41Phosphositeplus
Link-
1172PhosphoserineALRSSPIMR
16.41SysPTM
Link-
1172Phosphoserine.ALRSSPIMR
16.41UniProtKB
Link-
1185PhosphothreonineLNTYTPAKI
18.09Phosphositeplus
Link-
1185PhosphothreonineLNTYTPAKI
18.09SysPTM
Link-
1185Phosphothreonine.LNTYTPAKI
18.09UniProtKB
Link-
- top -

Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
- top -

Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
- top -
Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-504, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38; SER-1006; SER-1016AND SER-1172, AND MASS SPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38 AND SER-1006, ANDMASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1185, AND MASSSPECTROMETRY.
- top -
Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures