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Protein Page:
IDH2 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
IDH2 a mitochondrial oxidoreductase that catalyzes the third step of the citric acid cycle: the oxidative decarboxylation of isocitrate, consuming NADP(+), and producing alpha-ketoglutarate (alpha-KG) and CO2. Can also use oxalosuccinate as a substrate. Alpha-KG is an activator the dioxygenases that hydroxylate the transcription factor HIF and lead to its degradation by VHL. Since HIF turns on oncogenic pathways, IDH2 has apparent tumor suppressor activity. Homo-dimerization is required for activity. Each subunit binds 1 magnesium or manganese ion. May tightly associate or interact with the pyruvate dehydrogenase complex. A somatic mutation resulting in the R172K conversion results in a neomorphic enzyme activity that converts isocitrate to R(-)-2-hydroxyglutarate (2HG) occurs in a significant percentage of patients with cytogenetically normal acute myeloid leukemia (AML). Elevated levels of 2HG are also correlated with an elevated risk of malignant brain tumors. Note: This description may include information from UniProtKB.
Protein type: Mitochondrial; Carbohydrate Metabolism - citrate (TCA) cycle; EC 1.1.1.42; Other Amino Acids Metabolism - glutathione; Oxidoreductase
Cellular Component: mitochondrion; mitochondrial matrix; mitochondrial inner membrane
Molecular Function: magnesium ion binding; isocitrate dehydrogenase (NADP+) activity; NAD binding
Biological Process: isocitrate metabolic process; glyoxylate cycle; cellular metabolic process; tricarboxylic acid cycle; carbohydrate metabolic process; 2-oxoglutarate metabolic process
Reference #:  P48735 (UniProtKB)
Alt. Names/Synonyms: ICD-M; IDH; IDH2; IDHM; IDHP; IDP; IDPM; isocitrate dehydrogenase 2 (NADP+), mitochondrial; Isocitrate dehydrogenase [NADP], mitochondrial; isocitrate dehydrogenase, mitochondrial; mNADP-IDH; NADP(+)-specific ICDH; NADP+-specific ICDH; Oxalosuccinate decarboxylase
Gene Symbols: IDH2
Molecular weight: 50,909 Da
Basal Isoelectric point: 8.88  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

IDH2

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 K45 HYADKRIKVAKPVVE
0 1 K48 DKRIKVAKPVVEMDG
0 1 K48 DKRIKVAKPVVEMDG
0 1 K67-a RIIWQFIkEKLILPH
0 1 K67 RIIWQFIKEKLILPH
0 1 K69 IWQFIkEKLILPHVD
0 71 K80-a PHVDIQLkYFDLGLP
0 2 T97-p DQTDDQVtIDsALAT
0 2 S100-p DDQVtIDsALATQky
0 34 K106-a DsALATQkysVAVKC
0 1 K106 DsALATQKysVAVKC
0 6 Y107-p sALATQkysVAVKCA
0 5 S108-p ALATQkysVAVKCAt
0 1 T115-p sVAVKCAtITPDEAR
0 8 K133-a FKLKKMWkSPNGTIR
0 6 K155-a FREPIICkNIPRLVP
0 16 K166-a RLVPGWTkPITIGRH
0 2 K166-u RLVPGWTkPITIGRH
0 11 Y179-p RHAHGDQykATDFVA
0 44 K180-a HAHGDQykATDFVAD
0 1 K180 HAHGDQyKATDFVAD
0 1 K193 ADRAGTFKMVFTPKD
0 3 K199 FKMVFTPKDGSGVKE
0 1 K199 FKMVFTPKDGSGVKE
0 2 K256-a STKNTILkAYDGRFk
0 1 K256 STKNTILKAYDGRFk
0 19 K263-a kAYDGRFkDIFQEIF
0 2 K263-u kAYDGRFkDIFQEIF
0 9 K272-a IFQEIFDkHYkTDFD
0 1 K272 IFQEIFDKHYkTDFD
0 1 K275-a EIFDkHYkTDFDKNk
0 1 K280 HYkTDFDKNkIWYEH
0 2 K282-a kTDFDKNkIWYEHRL
0 1 S301-p VAQVLKSsGGFVWAC
0 5 K384-a RGLEHRGkLDGNQDL
0 1 K384 RGLEHRGKLDGNQDL
0 3 K400 RFAQMLEKVCVETVE
0 5 K413-a VESGAMTkDLAGCIH
0 4 S423-p AGCIHGLsNVKLNEH
0 6 K442-a TDFLDTIkSNLDRAL
  mouse

 
K45-a HYAEKRIkVEkPVVE
K48-a EKRIkVEkPVVEMDG
K48-u EKRIkVEkPVVEMDG
K67 RIIWQFIKEkLILPH
K67-u RIIWQFIkEkLILPH
K69-a IWQFIkEkLILPHVD
K80-a PHVDVQLkYFDLGLP
T97 DQTNDQVTIDSALAT
S100 NDQVTIDSALATQkY
K106-a DSALATQkYSVAVKC
K106-u DSALATQkYSVAVKC
Y107 SALATQkYSVAVKCA
S108 ALATQkYSVAVKCAT
T115 SVAVKCATITPDEAR
K133-a FKLKKMWkSPNGTIR
K155-a FREPIICkNIPRLVP
K166-a RLVPGWTkPITIGRH
K166-u RLVPGWTkPITIGRH
Y179 RHAHGDQYkATDFVV
K180-a HAHGDQYkATDFVVD
K180-u HAHGDQYkATDFVVD
K193-a VDRAGTFkLVFTPkD
K199-a FkLVFTPkDGSSAKE
K199-u FkLVFTPkDGSSAKE
K256-a STKNTILkAYDGRFk
K256-u STKNTILkAYDGRFk
K263-a kAYDGRFkDIFQEIF
K263-u kAYDGRFkDIFQEIF
K272-a IFQEIFDkHYKTDFD
K272-u IFQEIFDkHYKTDFD
K275 EIFDkHYKTDFDkNk
K280-a HYKTDFDkNkIWYEH
K282-a KTDFDkNkIWYEHRL
S301-p VAQVLKSsGGFVWAC
K384-a RGLEHRGkLDGNQDL
K384-u RGLEHRGkLDGNQDL
K400-a RFAQTLEkVCVQTVE
K413-a VESGAMTkDLAGCIH
S423-p AGCIHGLsNVKLNEH
K442-a TDFLDTIkSNLDRAL
  rat

 
K45 HYAEKRIKVEKPVVE
K48 EKRIKVEKPVVEMDG
K48 EKRIKVEKPVVEMDG
K67 RIIWQFIKEKLILPH
K67 RIIWQFIKEKLILPH
K69 IWQFIKEKLILPHVD
K80 PHVDVQLKYFDLGLP
T97 DQTNDQVTIDSALAT
S100 NDQVTIDSALATQKY
K106 DSALATQKYSVAVKC
K106 DSALATQKYSVAVKC
Y107 SALATQKYSVAVKCA
S108 ALATQKYSVAVKCAT
T115 SVAVKCATITPDEAR
K133 FKLKKMWKSPNGTIR
K155 FREPIICKNIPRLVP
K166 RLVPGWTKPITIGRH
K166 RLVPGWTKPITIGRH
Y179-p RHAHGDQyKATDFVV
K180 HAHGDQyKATDFVVD
K180 HAHGDQyKATDFVVD
K193 VDRAGMFKLVFTPKD
K199 FKLVFTPKDGSGAKE
K199 FKLVFTPKDGSGAKE
K256 STKNTIMKAYDGRFk
K256 STKNTIMKAYDGRFk
K263-a KAYDGRFkDIFQEIF
K263 KAYDGRFKDIFQEIF
K272 IFQEIFDKHYKTDFD
K272 IFQEIFDKHYKTDFD
K275 EIFDKHYKTDFDKNK
K280 HYKTDFDKNKIWYEH
K282 KTDFDKNKIWYEHRL
S301 VAQVLKSSGGFVWAC
K384 RGLEHRGKLDGNQDL
K384 RGLEHRGKLDGNQDL
K400 RFAQTLEKVCVQTVE
K413 VESGAMTKDLAGCIH
S423 AGCIHGLSNVKLNEH
K442 TDFLDTIKSNLDRAL
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