Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Isocitrate dehydrogenase [NADP] cytoplasmic  

UniProtKB / Swiss-Prot ID :  IDHC_HUMAN

Gene Name (Synonyms) : 
IDH1, PICD  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. Peroxisome. 

Protein Function :   

Protein Sequence MSKKISGGSVVEMQGDEMTRIIWELIKEKLIFPYVELDLHSYDLGIENRDATNDQVTKDAAEAIKKHNVG...
Predicted Secondary Structure CCCCCCCCCEEEECCCCCCHHHHHHHHHHHHCCCCEEEEEEEECCHHHHHCCCCCCCHHHHHHHHHCCEE...
Protein Variant
LocationDescription
132R -> C (in colorectal cancer and gliomasamples; glioblastoma multiforme; somatic
132R -> G (in a glioma sample; glioblastomamultiforme; somatic mutation).
132R -> H (in a glioma sample; glioblastomamultiforme; somatic mutation; abolishes
132R -> L (in a glioma sample; glioblastomamultiforme; somatic mutation; abolishes
132R -> S (in a glioma sample; glioblastomamultiforme; somatic mutation; abolishes
178V -> I (in dbSNP:rs34218846). VAR_049780
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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
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
19PhosphothreonineGDEMTRIIW
CCCCCHHHH
19.37HPRD
Link
19PhosphothreonineGDEMTRIIW
CCCCCHHHH
19.37Phosphositeplus
Link
58Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DQVTKDAAE
CCCCHHHHH
46.65Phosphositeplus
Link
81N6-acetyllysineTPDEKRVEE
CCCCCCCCH
69.95HPRD
Link
81N6-acetyllysineTPDEKRVEE
CCCCCCCCH
69.95Phosphositeplus
Link
81N6-acetyllysine.TPDEKRVEE
CCCCCCCCH
69.95UniProtKB
Link
93N6-acetyllysineKQMWKSPNG
CCCCCCCCH
51.17Phosphositeplus
Link
126Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SGWVKPIII
CCCCCCCEE
24.80Phosphositeplus
Link
135PhosphotyrosineGRHAYGDQY
CCCCCCCCC
18.34Phosphositeplus
Link
151Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PGPGKVEIT
ECCCCCCEE
39.57Phosphositeplus
Link
214PhosphothreonineSTKNTILKK
EECCHHHHH
29.28HPRD
Link
214PhosphothreonineSTKNTILKK
EECCHHHHH
29.28Phosphositeplus
Link
219PhosphotyrosineILKKYDGRF
HHHHHCHHH
23.26HPRD
Link
219PhosphotyrosineILKKYDGRF
HHHHHCHHH
23.26Phosphositeplus
Link
224Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DGRFKDIFQ
CHHHHHHHH
48.86Phosphositeplus
Link
224N6-acetyllysineDGRFKDIFQ
CHHHHHHHH
48.86HPRD
Link
224N6-acetyllysineDGRFKDIFQ
CHHHHHHHH
48.86Phosphositeplus
Link
224N6-acetyllysine.DGRFKDIFQ
CHHHHHHHH
48.86UniProtKB
Link
233Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EIYDKQYKS
HHHHHHHHH
38.26Phosphositeplus
Link
321Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)RMYQKGQET
CHHHHCCCC
45.11Phosphositeplus
Link
321N6-acetyllysineRMYQKGQET
CHHHHCCCC
45.11HPRD
Link
321N6-acetyllysineRMYQKGQET
CHHHHCCCC
45.11Phosphositeplus
Link
321N6-acetyllysine.RMYQKGQET
CHHHHCCCC
45.11UniProtKB
Link
389PhosphoserineNVQRSDYLN
CCCCCCCCC
17.32Phosphositeplus
Link
391PhosphotyrosineQRSDYLNTF
CCCCCCCHH
11.78Phosphositeplus
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
ZHX1_HUMANphysical interactionEBI-732226
intact16169070
ZHX1_HUMANyeast 2-hybridHPRD:00984HPRD16169070
ACON_HUMANENSP00000260985STRING
ACON_HUMANENSP00000260985STRING
ACON_HUMANENSP00000260985STRING
IDH3G_HUMANENSP00000260985STRING
MDHC_HUMANENSP00000260985STRING
AATM_HUMANENSP00000260985STRING
AATM_HUMANENSP00000260985STRING
IDH3A_HUMANENSP00000260985STRING
PRL_HUMANENSP00000260985STRING
IREB1_HUMANENSP00000260985STRING
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Disease Reference
Kegg disease
OMIM disease
137800Glioma (GLM)
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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-81; LYS-224 AND LYS-321, ANDMASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures