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P54071 (IDHP_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Isocitrate dehydrogenase [NADP], mitochondrial
Short name=IDH
EC=1.1.1.42
Alternative name(s):
ICD-M
IDP
NADP(+)-specific ICDH
Oxalosuccinate decarboxylase
Gene names
Name:Idh2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length452 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 + CO2 + 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. Ref.2

Induction

By oxidative stress (at protein level). Ref.2

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3939Mitochondrion By similarity
Chain40 – 452413Isocitrate dehydrogenase [NADP], mitochondrial
PRO_0000014421

Regions

Nucleotide binding115 – 1173NADP By similarity
Nucleotide binding349 – 3546NADP By similarity
Region134 – 1407Substrate binding By similarity

Sites

Metal binding2911Magnesium or manganese By similarity
Metal binding3141Magnesium or manganese By similarity
Binding site1171Substrate By similarity
Binding site1221NADP By similarity
Binding site1491Substrate By similarity
Binding site1721Substrate By similarity
Binding site2991NADP By similarity
Binding site3671NADP; via amide nitrogen and carbonyl oxygen By similarity
Site1791Critical for catalysis By similarity
Site2511Critical for catalysis By similarity

Amino acid modifications

Modified residue671N6-acetyllysine By similarity
Modified residue1061N6-acetyllysine Ref.6
Modified residue1551N6-acetyllysine By similarity
Modified residue1661N6-acetyllysine By similarity
Modified residue1801N6-acetyllysine By similarity
Modified residue2561N6-acetyllysine By similarity
Modified residue2631N6-acetyllysine By similarity
Modified residue2721N6-acetyllysine Ref.6
Modified residue2751N6-acetyllysine By similarity
Modified residue2821N6-acetyllysine By similarity
Modified residue4421N6-acetyllysine By similarity

Experimental info

Sequence conflict1041T → A in AAC52473. Ref.1
Sequence conflict1091V → M in AAC52473. Ref.1
Sequence conflict1521I → S in AAC52473. Ref.1
Sequence conflict2001D → N in AAC52473. Ref.1
Sequence conflict2141A → G in AAC52473. Ref.1
Sequence conflict2801K → R in AAC52473. Ref.1
Sequence conflict2801K → R in AAG43538. Ref.2
Sequence conflict322 – 3232QG → SR in AAC52473. Ref.1
Sequence conflict367 – 3682NP → KG in AAC52473. Ref.1
Sequence conflict3981L → R in AAC52473. Ref.1
Sequence conflict4081Missing in AAC52473. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P54071 [UniParc].

Last modified September 11, 2007. Version 3.
Checksum: 19BB5CF78512ECAB

FASTA45250,906
        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

« Hide

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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

EMBL
GenBank
DDBJ		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.
IPIIPI00318614.
RefSeqNP_766599.2. NM_173011.2.
UniGeneMm.246432.
Mm.290925.

3D structure databases

ProteinModelPortalP54071.
SMRP54071. Positions 40-452.
ModBaseSearch...

Protein-protein interaction databases

IntActP54071. 1 interaction.
MINTMINT-4114220.

PTM databases

PhosphoSiteP54071.

Proteomic databases

PaxDbP54071.
PRIDEP54071.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000107384; ENSMUSP00000103007; ENSMUSG00000030541.
GeneID269951.
KEGGmmu:269951.
UCSCuc009hzm.2. mouse.

Organism-specific databases

CTD3418.
MGIMGI:96414. Idh2.

Phylogenomic databases

eggNOGCOG0538.
GeneTreeENSGT00390000012547.
HOGENOMHOG000019858.
HOVERGENHBG006119.
KOK00031.
OMAQHQQGKP.
OrthoDBEOG42V8G4.

Gene expression databases

ArrayExpressP54071.
BgeeP54071.
CleanExMM_IDH2.
GenevestigatorP54071.
GermOnlineENSMUSG00000030541. Mus musculus.

Family and domain databases

Gene3D3.40.718.10. 1 hit.
InterProIPR019818. IsoCit/isopropylmalate_DH_CS.
IPR004790. Isocitrate_DH_NADP.
IPR024084. IsoPropMal-DH-like_dom.
[Graphical view]
PANTHERPTHR11822. PTHR11822. 1 hit.
PfamPF00180. Iso_dh. 1 hit.
[Graphical view]
PIRSFPIRSF000108. IDH_NADP. 1 hit.
TIGRFAMsTIGR00127. nadp_idh_euk. 1 hit.
PROSITEPS00470. IDH_IMDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSIDH2. mouse.
NextBio393111.
SOURCESearch...

Entry information

Entry nameIDHP_MOUSE
AccessionPrimary (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: May 29, 2013
This is version 102 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents