IMPA1_RAT - dbPTM
IMPA1_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IMPA1_RAT
UniProt AC P97697
Protein Name Inositol monophosphatase 1
Gene Name Impa1
Organism Rattus norvegicus (Rat).
Sequence Length 277
Subcellular Localization Cytoplasm .
Protein Description Responsible for the provision of inositol required for synthesis of phosphatidylinositol and polyphosphoinositides and has been implicated as the pharmacological target for lithium action in brain. Has broad substrate specificity and can use myo-inositol 1,3-diphosphate, myo-inositol 1,4-diphosphate, scyllo-inositol-phosphate, glucose-1-phosphate, glucose-6-phosphate, fructose-1-phosphate, beta-glycerophosphate, and 2'-AMP as substrates (By similarity). Is equally active with myo-inositol monophosphate and D-galactose 1-phosphate..
Protein Sequence MADPWQECMDYAVILARQAGEMIREALKNKMDVMIKSSPADLVTVTDQKVEKMLMSSIKEKYPYHSFIGEESVASGEKTVFTEQPTWIIDPIDGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKGAFCNGQKLRVSQQEDITKSLLVTELGSSRKPETLRIVLSNMERLCSIPIHGIRSVGTAAVNMCLVATGGADAYYEMGIHCWDMAGAGIIVIEAGGVLLDVTGGPFDLMSRRIIAASNIALAERIAKELEIIPLQRDDES
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
30AcetylationIREALKNKMDVMIKS
HHHHHHCCCCEEEEC
34.5822902405
37PhosphorylationKMDVMIKSSPADLVT
CCCEEEECCCCCEEE
30.5428432305
38PhosphorylationMDVMIKSSPADLVTV
CCEEEECCCCCEEEE
21.0728432305
49AcetylationLVTVTDQKVEKMLMS
EEEECHHHHHHHHHH
55.9922902405
52AcetylationVTDQKVEKMLMSSIK
ECHHHHHHHHHHHHH
40.0822902405
59AcetylationKMLMSSIKEKYPYHS
HHHHHHHHHHCCCCC
50.5322902405
62PhosphorylationMSSIKEKYPYHSFIG
HHHHHHHCCCCCCCC
15.3225575281
64PhosphorylationSIKEKYPYHSFIGEE
HHHHHCCCCCCCCCC
13.6525575281
66PhosphorylationKEKYPYHSFIGEESV
HHHCCCCCCCCCCCC
16.8325575281
72PhosphorylationHSFIGEESVASGEKT
CCCCCCCCCCCCCCE
20.7725575281
75PhosphorylationIGEESVASGEKTVFT
CCCCCCCCCCCEEEE
45.3825575281
145AcetylationGAFCNGQKLRVSQQE
CCCCCCCCCEECCHH
39.3922902405
156AcetylationSQQEDITKSLLVTEL
CCHHHHHHHHHHHHC
39.1722902405
161PhosphorylationITKSLLVTELGSSRK
HHHHHHHHHCCCCCC
26.0130181290
165PhosphorylationLLVTELGSSRKPETL
HHHHHCCCCCCCHHH
39.3328432305
166PhosphorylationLVTELGSSRKPETLR
HHHHCCCCCCCHHHH
42.3928432305
264AcetylationALAERIAKELEIIPL
HHHHHHHHHCCCEEC
61.5322902405

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of IMPA1_RAT !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IMPA1_RAT !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of IMPA1_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of IMPA1_RAT !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of IMPA1_RAT

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Related Literatures of Post-Translational Modification

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