Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  1-phosphatidylinositol 3-phosphate 5-kinase  

UniProtKB / Swiss-Prot ID :  FYV1_MOUSE

Gene Name (Synonyms) : 
Pikfyve, Kiaa0981, Pip5k3  

Species :  Mus musculus (Mouse). 

Subcellular Localization :  Cytoplasmic vesicle membrane; Peripheral membrane protein. Endosome membrane (By similarity). Note=Associated with vesicle structures. Displays a peripheral vesicular punctate pattern. Mainly associated with membranes of the late endocytic pathway (By si 

Protein Function :  The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Catalyzes the phosphorylation of phosphatidylinositol 3-phosphate on the fifth hydroxyl of the myo- inositol ring, to form phosphatidylinositol 3,5-bisphosphate. Required for endocytic-vacuolar pathway and nuclear migration. The product of the reaction it catalyzes functions as an important regulator of vacuole homeostasis perhaps by controlling membrane flux to and/or from the vacuole. 

Protein Sequence MATDDKSSPTLDSANDLPRSPASPSHLTHFKPLTPDQDEPPFKSAYSSFVNLFRFNKERGEGGQGEQQSP...
Predicted Secondary Structure CCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCHHHHHHHHHHHHHHHHHHHHHCCCCCCCC...
Protein Variant -
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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
Predicted PTM Sites
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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
105PhosphoserineHRRSSVLDS
CCCCCHHHC
25.53Phosphositeplus
Link-
305PhosphoserineARNRSASIT
HHHHHHCCC
29.89SysPTM
Link-
307PhosphoserineNRSASITNL
HHHHCCCCC
31.06SysPTM
Link-
307Phosphoserine.NRSASITNL
HHHHCCCCC
31.06UniProtKB
Link-
318PhosphoserineDRSGSPMVP
CCCCCCCCC
15.86PhosphoELM
Link-
475PhosphoserineKFDDSDTEQ
CCCCCCCCC
48.56Phosphositeplus
Link-
493PhosphoserineANSASPSKR
HHHHHHHCC
29.53Phosphositeplus
Link-
495PhosphoserineSASPSKRTS
HHHHHCCHH
32.07Phosphositeplus
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
Drug Reference
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures