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], mitochondrial  

UniProtKB / Swiss-Prot ID :  IDHP_HUMAN

Gene Name (Synonyms) : 
IDH2  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Mitochondrion. 

Protein Function :  Plays a role in intermediary metabolism and energy production. It may tightly associate or interact with the pyruvate dehydrogenase complex. 

Protein Sequence MAGYLRVVRSLCRASGSRPAWAPAALTAPTSQEQPRRHYADKRIKVAKPVVEMDGDEMTRIIWQFIKEKL...
Predicted Secondary Structure CHHHHHHHHHHHHHHHCCCCCCHHHHHCCCCHHHHHHHCCCEEECCCCCEEEECCCCHHHHHHHHHHHHH...
Protein Variant
LocationDescription
140R -> G (in D2HGA2). VAR_065174
140R -> Q (in D2HGA2). VAR_065175
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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
67N6-acetyllysineWQFIKEKLI
HHHHHHHHC
50.51HPRD
Link
67N6-acetyllysineWQFIKEKLI
HHHHHHHHC
50.51Phosphositeplus
Link
67N6-acetyllysine.WQFIKEKLI
HHHHHHHHC
50.51UniProtKB
Link
80N6-acetyllysineDIQLKYFDL
CCCEEEEEC
27.74HPRD
Link
80N6-acetyllysineDIQLKYFDL
CCCEEEEEC
27.74Phosphositeplus
Link
80N6-acetyllysine.DIQLKYFDL
CCCEEEEEC
27.74UniProtKB
Link
106N6-acetyllysineLATQKYSVA
HHHHHCCEE
34.83HPRD
Link
106N6-acetyllysineLATQKYSVA
HHHHHCCEE
34.83Phosphositeplus
Link
106N6-acetyllysine.LATQKYSVA
HHHHHCCEE
34.83UniProtKB
Link
108PhosphoserineTQKYSVAVK
HHHCCEEEE
15.61HPRD
Link
108PhosphoserineTQKYSVAVK
HHHCCEEEE
15.61Phosphositeplus
Link
115PhosphothreonineVKCATITPD
EECCCCCCC
34.55HPRD
Link
115PhosphothreonineVKCATITPD
EECCCCCCC
34.55Phosphositeplus
Link
133N6-acetyllysineKKMWKSPNG
CCCCCCHHH
53.16HPRD
Link
133N6-acetyllysineKKMWKSPNG
CCCCCCHHH
53.16Phosphositeplus
Link
133N6-acetyllysine.KKMWKSPNG
CCCCCCHHH
53.16UniProtKB
Link
155N6-acetyllysinePIICKNIPR
EEEECCCCC
47.72HPRD
Link
155N6-acetyllysinePIICKNIPR
EEEECCCCC
47.72Phosphositeplus
Link
155N6-acetyllysine.PIICKNIPR
EEEECCCCC
47.72UniProtKB
Link
166Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PGWTKPITI
CCCCCCEEE
28.10Phosphositeplus
Link
166N6-acetyllysinePGWTKPITI
CCCCCCEEE
28.10HPRD
Link
166N6-acetyllysinePGWTKPITI
CCCCCCEEE
28.10Phosphositeplus
Link
166N6-acetyllysine.PGWTKPITI
CCCCCCEEE
28.10UniProtKB
Link
180N6-acetyllysineGDQYKATDF
CCEEECCCE
38.89HPRD
Link
180N6-acetyllysineGDQYKATDF
CCEEECCCE
38.89Phosphositeplus
Link
180N6-acetyllysine.GDQYKATDF
CCEEECCCE
38.89UniProtKB
Link
256N6-acetyllysineNTILKAYDG
HHHHHHHCH
40.84HPRD
Link
256N6-acetyllysineNTILKAYDG
HHHHHHHCH
40.84Phosphositeplus
Link
256N6-acetyllysine.NTILKAYDG
HHHHHHHCH
40.84UniProtKB
Link
263Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DGRFKDIFQ
CHHHHHHHH
48.86Phosphositeplus
Link
263N6-acetyllysineDGRFKDIFQ
CHHHHHHHH
48.86HPRD
Link
263N6-acetyllysineDGRFKDIFQ
CHHHHHHHH
48.86Phosphositeplus
Link
263N6-acetyllysine.DGRFKDIFQ
CHHHHHHHH
48.86UniProtKB
Link
272N6-acetyllysineEIFDKHYKT
HHHHHHHHC
37.78HPRD
Link
272N6-acetyllysineEIFDKHYKT
HHHHHHHHC
37.78Phosphositeplus
Link
272N6-acetyllysine.EIFDKHYKT
HHHHHHHHC
37.78UniProtKB
Link
275N6-acetyllysineDKHYKTDFD
HHHHHCCCC
41.14HPRD
Link
275N6-acetyllysineDKHYKTDFD
HHHHHCCCC
41.14Phosphositeplus
Link
275N6-acetyllysine.DKHYKTDFD
HHHHHCCCC
41.14UniProtKB
Link
282N6-acetyllysineFDKNKIWYE
CCCCCCEEH
40.12HPRD
Link
282N6-acetyllysineFDKNKIWYE
CCCCCCEEH
40.12Phosphositeplus
Link
282N6-acetyllysine.FDKNKIWYE
CCCCCCEEH
40.12UniProtKB
Link
413N6-acetyllysineGAMTKDLAG
CCCCHHHCC
37.35HPRD
Link
442N6-acetyllysineLDTIKSNLD
HHHHHHHHH
35.07HPRD
Link
442N6-acetyllysineLDTIKSNLD
HHHHHHHHH
35.07Phosphositeplus
Link
442N6-acetyllysine.LDTIKSNLD
HHHHHHHHH
35.07UniProtKB
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
ACON_HUMANENSP00000331897STRING
ACON_HUMANENSP00000331897STRING
ACON_HUMANENSP00000331897STRING
IDH3G_HUMANENSP00000331897STRING
AATM_HUMANENSP00000331897STRING
AATM_HUMANENSP00000331897STRING
IDH3A_HUMANENSP00000331897STRING
IREB1_HUMANENSP00000331897STRING
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Disease Reference
Kegg disease
OMIM disease
613657D-2-hydroxyglutaric aciduria 2 (D2HGA2)
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-67; LYS-80; LYS-106;LYS-133; LYS-155; LYS-166; LYS-180; LYS-256; LYS-263; LYS-272;LYS-275; LYS-282 AND LYS-442, AND MASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures