UniProt Accession

 IDHP_HUMAN; P48735; B2R6L6; Q96GT3 

Genbank Protein ID

 X69433; AK312627; CH471101; BC009244; BC071828 

Genbank Nucleotide ID

 CAA49208.1; BAG35513.1; EAX02082.1; AAH09244.1; AAH71828.1 

Protein Name

 Isocitrate dehydrogenase [NADP], mitochondrial 

Protein Synonyms/Alias

 IDH; ICD-M; IDP; NADP(+)-specific ICDH; Oxalosuccinate decarboxylase 

Gene Name

 IDH2 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
67	RIIWQFIKEKLILPH	acetylation	[1]
67	RIIWQFIKEKLILPH	ubiquitination	[2]
80	PHVDIQLKYFDLGLP	acetylation	[1]
106	DSALATQKYSVAVKC	acetylation	[1, 3]
112	QKYSVAVKCATITPD	ubiquitination	[2]
155	FREPIICKNIPRLVP	acetylation	[1]
166	RLVPGWTKPITIGRH	acetylation	[1]
166	RLVPGWTKPITIGRH	ubiquitination	[2, 4, 5, 6]
180	HAHGDQYKATDFVAD	acetylation	[1]
180	HAHGDQYKATDFVAD	ubiquitination	[2, 5]
193	ADRAGTFKMVFTPKD	ubiquitination	[2]
256	STKNTILKAYDGRFK	acetylation	[1]
263	KAYDGRFKDIFQEIF	acetylation	[1]
263	KAYDGRFKDIFQEIF	ubiquitination	[4, 6]
272	IFQEIFDKHYKTDFD	acetylation	[1]
272	IFQEIFDKHYKTDFD	ubiquitination	[2, 4, 6]
275	EIFDKHYKTDFDKNK	acetylation	[1]
280	HYKTDFDKNKIWYEH	ubiquitination	[5]
282	KTDFDKNKIWYEHRL	acetylation	[1]
282	KTDFDKNKIWYEHRL	ubiquitination	[5]
384	RGLEHRGKLDGNQDL	ubiquitination	[2]
413	VESGAMTKDLAGCIH	acetylation	[1]
413	VESGAMTKDLAGCIH	ubiquitination	[2]
442	TDFLDTIKSNLDRAL	acetylation	[1]

Reference

 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [5] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [6] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789] 

Functional Description

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

Sequence Annotation

 NP_BIND 115 117 NADP (By similarity).
 NP_BIND 349 354 NADP (By similarity).
 REGION 134 140 Substrate binding (By similarity).
 METAL 291 291 Magnesium or manganese (By similarity).
 METAL 314 314 Magnesium or manganese (By similarity).
 BINDING 117 117 Substrate (By similarity).
 BINDING 122 122 NADP (By similarity).
 BINDING 149 149 Substrate (By similarity).
 BINDING 172 172 Substrate (By similarity).
 BINDING 299 299 NADP (By similarity).
 BINDING 367 367 NADP; via amide nitrogen and carbonyl
 MOD_RES 67 67 N6-acetyllysine.
 MOD_RES 106 106 N6-acetyllysine.
 MOD_RES 155 155 N6-acetyllysine.
 MOD_RES 166 166 N6-acetyllysine.
 MOD_RES 180 180 N6-acetyllysine.
 MOD_RES 256 256 N6-acetyllysine.
 MOD_RES 263 263 N6-acetyllysine.
 MOD_RES 272 272 N6-acetyllysine.
 MOD_RES 275 275 N6-acetyllysine.
 MOD_RES 282 282 N6-acetyllysine.
 MOD_RES 442 442 N6-acetyllysine.  

Keyword

 3D-structure; Acetylation; Complete proteome; Disease mutation; Glyoxylate bypass; Magnesium; Manganese; Metal-binding; Mitochondrion; NADP; Oxidoreductase; Reference proteome; Transit peptide; Tricarboxylic acid cycle. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 452 AA 

Protein Sequence

Gene Ontology

 GO:0005743; C:mitochondrial inner membrane; IEA:Compara.
 GO:0005759; C:mitochondrial matrix; TAS:Reactome.
 GO:0004450; F:isocitrate dehydrogenase (NADP+) activity; ISS:UniProtKB.
 GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
 GO:0051287; F:NAD binding; IEA:InterPro.
 GO:0006103; P:2-oxoglutarate metabolic process; ISS:UniProtKB.
 GO:0005975; P:carbohydrate metabolic process; NAS:ProtInc.
 GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-KW.
 GO:0006102; P:isocitrate metabolic process; ISS:UniProtKB.
 GO:0006099; P:tricarboxylic acid cycle; TAS:Reactome. 

Interpro

 IPR019818; IsoCit/isopropylmalate_DH_CS.
 IPR004790; Isocitrate_DH_NADP.
 IPR024084; IsoPropMal-DH-like_dom. 

Pfam

 PF00180; Iso_dh 

SMART

  

PROSITE

 PS00470; IDH_IMDH 

PRINTS