Reviewed, UniProtKB/Swiss-Prot P54071 (IDHP_MOUSE)

Names and origin

Protein names

Recommended name:
    Isocitrate dehydrogenase [NADP], mitochondrial
      Short name=IDH
    EC=1.1.1.42
Alternative name(s):
    Oxalosuccinate decarboxylase
    NADP(+)-specific ICDH
    IDP
    ICD-M

Gene names

Name:

Idh2

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	452 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Plays a role in intermediary metabolism and energy production. It may tightly associate or interact with the pyruvate dehydrogenase complex.
Catalytic activity	Isocitrate + NADP(+) = 2-oxoglutarate + CO(2) + NADPH. Oxalosuccinate + NADP(+) = 2-oxoglutarate + CO(2) + NADPH.
Cofactor	Binds 1 magnesium or manganese ion per subunit By similarity.
Subunit structure	Homodimer By similarity.
Subcellular location	Mitochondrion.
Tissue specificity	Heart > kidney >> other tissues.
Induction	By oxidative stress (at protein level).
Sequence similarities	Belongs to the isocitrate and isopropylmalate dehydrogenases family.
Sequence caution	The sequence AAC52473.1 differs from that shown. Reason: Frameshift at positions 5 and 11.

Ontologies

Keywords
Biological process	Glyoxylate bypass Stress response Tricarboxylic acid cycle
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Magnesium Manganese Metal-binding NADP
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	glyoxylate cycle Inferred from electronic annotation. Source: UniProtKB-KW isocitrate metabolic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW response to stress Inferred from electronic annotation. Source: UniProtKB-KW tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial inner membrane Inferred from direct assay. Source: MGI
Molecular function	isocitrate dehydrogenase (NADP+) activity Inferred from direct assay. Source: MGI magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 39	39	Mitochondrion By similarity
	Chain	40 – 452	413	Isocitrate dehydrogenase [NADP], mitochondrial		PRO_0000014421
Regions
	Nucleotide binding	115 – 117	3	NADP By similarity
	Nucleotide binding	349 – 354	6	NADP By similarity
	Region	134 – 140	7	Substrate binding By similarity
Sites
	Metal binding	291	1	Magnesium or manganese By similarity
	Metal binding	314	1	Magnesium or manganese By similarity
	Binding site	117	1	Substrate By similarity
	Binding site	122	1	NADP By similarity
	Binding site	149	1	Substrate By similarity
	Binding site	172	1	Substrate By similarity
	Binding site	299	1	NADP By similarity
	Binding site	367	1	NADP; via amide nitrogen and carbonyl oxygen By similarity
	Site	179	1	Critical for catalysis By similarity
	Site	251	1	Critical for catalysis By similarity
Amino acid modifications
	Modified residue	106	1	N6-acetyllysine
	Modified residue	272	1	N6-acetyllysine
Experimental info
	Sequence conflict	104	1	T → A in AAC52473. Ref.1
	Sequence conflict	109	1	V → M in AAC52473. Ref.1
	Sequence conflict	152	1	I → S in AAC52473. Ref.1
	Sequence conflict	200	1	D → N in AAC52473. Ref.1
	Sequence conflict	214	1	A → G in AAC52473. Ref.1
	Sequence conflict	280	1	K → R in AAC52473. Ref.1
	Sequence conflict	280	1	K → R in AAG43538. Ref.2
	Sequence conflict	322 – 323	2	QG → SR in AAC52473. Ref.1
	Sequence conflict	367 – 368	2	NP → KG in AAC52473. Ref.1
	Sequence conflict	398	1	L → R in AAC52473. Ref.1
	Sequence conflict	408	1	Missing in AAC52473. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P54071-1 [UniParc]. Last modified September 11, 2007. Version 3. Checksum: 19BB5CF78512ECAB	FASTA	452	50,906
	10 20 30 40 50 60 MAGYLRAVSS LCRASGSART WAPAALTVPS WPEQPRRHYA EKRIKVEKPV VEMDGDEMTR 70 80 90 100 110 120 IIWQFIKEKL ILPHVDVQLK YFDLGLPNRD QTNDQVTIDS ALATQKYSVA VKCATITPDE 130 140 150 160 170 180 ARVEEFKLKK MWKSPNGTIR NILGGTVFRE PIICKNIPRL VPGWTKPITI GRHAHGDQYK 190 200 210 220 230 240 ATDFVVDRAG TFKLVFTPKD GSSAKEWEVY NFPAGGVGMG MYNTDESISG FAHSCFQYSI 250 260 270 280 290 300 QKKWPLYLST KNTILKAYDG RFKDIFQEIF DKHYKTDFDK NKIWYEHRLI DDMVAQVLKS 310 320 330 340 350 360 SGGFVWACKN YDGDVQSDIL AQGFGSLGLM TSVLVCPDGK TIEAEAAHGT VTRHYREHQK 370 380 390 400 410 420 GRPTSTNPIA SIFAWTRGLE HRGKLDGNQD LIRFAQTLEK VCVQTVESGA MTKDLAGCIH 430 440 450 GLSNVKLNEH FLNTTDFLDT IKSNLDRALG KQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of the cDNA of mouse mitochondrial NADP-dependent isocitrate dehydrogenase and the expression of the gene during lymphocyte activation." Yang L., Luo H., Vinay P., Wu J. J. Cell. Biochem. 60:400-410(1996) [PubMed: 8867815] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: BALB/c. Tissue: Heart.
[2]	"Control of mitochondrial redox balance and cellular defense against oxidative damage by mitochondrial NADP+-dependent isocitrate dehydrogenase." Jo S.-H., Son M.-K., Koh H.-J., Lee S.-M., Song I.-H., Kim Y.-O., Lee Y.-S., Jeong K.-S., Kim W.B., Park J.-W., Song B.J., Huhe T.-L. J. Biol. Chem. 276:16168-16176(2001) [PubMed: 11278619] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION.
[3]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and NOD. Tissue: Embryo, Heart and Thymus.
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N-3. Tissue: Mammary tumor.
[5]	Lubec G., Kang S.U. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 44-60 AND 81-89, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain.
[6]	"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-106 AND LYS-272, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U51167 mRNA. Translation: AAC52473.1. Frameshift. AF212319 mRNA. Translation: AAG43538.1. AK088110 mRNA. Translation: BAC40149.1. AK145753 mRNA. Translation: BAE26628.1. AK161640 mRNA. Translation: BAE36505.1. AK169395 mRNA. Translation: BAE41142.1. BC060030 mRNA. Translation: AAH60030.1.
RefSeq	NP_766599.1.
UniGene	Mm.246432
3D structure databases
HSSP	HSSP built from PDB template 1LWD based on UniProtKB P33198.
SMR	P54071. Positions 112-524.
ModBase	Search...
PTM databases
PhosphoSite	P54071.
Genome annotation databases
Ensembl	ENSMUSG00000030541. Mus musculus. [Contig view]
GeneID	269951.
KEGG	mmu:269951.
Organism-specific databases
MGI	MGI:96414. Idh2.
Phylogenomic databases
HOGENOM	P54071.
HOVERGEN	P54071.
Gene expression databases
ArrayExpress	P54071.
CleanEx	MM_IDH2.
GermOnline	ENSMUSG00000030541. Mus musculus.
Family and domain databases
InterPro	IPR004790. IsoCit_DHase_NADP-dep_euk. IPR001804. IsoCit_IM_DHase. [Graphical view]
Gene3D	G3DSA:3.40.718.10. IDH_IMDH. 1 hit.
PANTHER	PTHR11822. IDH_NADP_euk. 1 hit.
Pfam	PF00180. Iso_dh. 1 hit. [Graphical view]
PIRSF	PIRSF000108. IDH_NADP. 1 hit.
TIGRFAMs	TIGR00127. nadp_idh_euk. 1 hit.
PROSITE	PS00470. IDH_IMDH. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	393111.
SOURCE	Search...

Entry information

Entry name

IDHP_MOUSE

Accession

Primary (citable) accession number: P54071
Secondary accession number(s): Q8C2R9, Q9EQK1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	September 11, 2007
Last modified:	November 25, 2008
This is version 68 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)