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O88844 (IDHC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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

Names and origin

Protein namesRecommended name:
Isocitrate dehydrogenase [NADP] cytoplasmic

Short name=IDH
EC=1.1.1.42
Alternative name(s):
Cytosolic NADP-isocitrate dehydrogenase
IDP
NADP(+)-specific ICDH
Oxalosuccinate decarboxylase
Gene names
Name:Idh1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length414 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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

Cytoplasm.

Post-translational modification

Acetylation at Lys-374 dramatically reduces catalytic activity By similarity.

Sequence similarities

Belongs to the isocitrate and isopropylmalate dehydrogenases family.

Ontologies

Keywords
   Biological processGlyoxylate bypass
Tricarboxylic acid cycle
   Cellular componentCytoplasm
   LigandMagnesium
Manganese
Metal-binding
NADP
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_process2-oxoglutarate metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

female gonad development

Inferred from electronic annotation. Source: Ensembl

glutathione metabolic process

Inferred from mutant phenotype PubMed 12031902. Source: MGI

glyoxylate cycle

Inferred from electronic annotation. Source: UniProtKB-KW

isocitrate metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

response to oxidative stress

Inferred from direct assay PubMed 12031902. Source: MGI

response to steroid hormone

Inferred from electronic annotation. Source: Ensembl

tricarboxylic acid cycle

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytosol

Inferred from direct assay PubMed 12031902. Source: MGI

mitochondrion

Inferred from direct assay PubMed 18614015. Source: MGI

peroxisome

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionNAD binding

Inferred from electronic annotation. Source: InterPro

NADP binding

Inferred from electronic annotation. Source: Ensembl

isocitrate dehydrogenase (NADP+) activity

Inferred from sequence or structural similarity. Source: UniProtKB

magnesium ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 414413Isocitrate dehydrogenase [NADP] cytoplasmic
PRO_0000083578

Regions

Nucleotide binding75 – 773NADP By similarity
Nucleotide binding310 – 3156NADP By similarity
Region94 – 1007Substrate binding By similarity

Sites

Metal binding2521Magnesium or manganese By similarity
Metal binding2751Magnesium or manganese By similarity
Binding site771Substrate By similarity
Binding site821NADP By similarity
Binding site1091Substrate By similarity
Binding site1321Substrate By similarity
Binding site2601NADP By similarity
Binding site3281NADP; via amide nitrogen and carbonyl oxygen By similarity
Site1391Critical for catalysis By similarity
Site2121Critical for catalysis By similarity

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue811N6-acetyllysine Ref.6
Modified residue1261N6-succinyllysine Ref.5
Modified residue2241N6-acetyllysine Ref.6
Modified residue2331N6-acetyllysine Ref.6
Modified residue2431N6-acetyllysine Ref.6
Modified residue3211N6-acetyllysine By similarity
Modified residue4001N6-succinyllysine Ref.5

Experimental info

Sequence conflict2431K → N in AAD02919. Ref.1

Secondary structure

................................................................ 414
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O88844 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: C7FEF315D042C44C

FASTA41446,674
        10         20         30         40         50         60 
MSRKIQGGSV VEMQGDEMTR IIWELIKEKL ILPYVELDLH SYDLGIENRD ATNDQVTKDA 

        70         80         90        100        110        120 
AEAIKKYNVG VKCATITPDE KRVEEFKLKQ MWKSPNGTIR NILGGTVFRE AIICKNIPRL 

       130        140        150        160        170        180 
VTGWVKPIII GRHAYGDQYR ATDFVVPGPG KVEITYTPKD GTQKVTYMVH DFEEGGGVAM 

       190        200        210        220        230        240 
GMYNQDKSIE DFAHSSFQMA LSKGWPLYLS TKNTILKKYD GRFKDIFQEI YDKKYKSQFE 

       250        260        270        280        290        300 
AQKICYEHRL IDDMVAQAMK SEGGFIWACK NYDGDVQSDS VAQGYGSLGM MTSVLICPDG 

       310        320        330        340        350        360 
KTVEAEAAHG TVTRHYRMYQ KGQETSTNPI ASIFAWSRGL AHRAKLDNNT ELSFFAKALE 

       370        380        390        400        410 
DVCIETIEAG FMTKDLAACI KGLPNVQRSD YLNTFEFMDK LGENLKAKLA QAKL 

« Hide

References

« Hide 'large scale' references
[1]"Cytosolic isocitrate dehydrogenase in humans, mice, and voles and phylogenetic analysis of the enzyme family."
Nekrutenko A., Hillis D.M., Patton J.C., Bradley R.D., Baker R.J.
Mol. Biol. Evol. 15:1674-1684(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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.
Tissue: Bone marrow, Embryo and Sympathetic ganglion.
[3]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Lubec G., Yang J.W., Zigmond M.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 30-49.
Tissue: Brain.
[5]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-126 AND LYS-400, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast and Liver.
[6]"Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-81; LYS-224; LYS-233 AND LYS-243, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF020039 mRNA. Translation: AAD02919.1.
AK149019 mRNA. Translation: BAE28720.1.
AK151212 mRNA. Translation: BAE30207.1.
AK159173 mRNA. Translation: BAE34873.1.
AK160896 mRNA. Translation: BAE36075.1.
AK167158 mRNA. Translation: BAE39299.1.
CH466548 Genomic DNA. Translation: EDL00223.1.
CH466548 Genomic DNA. Translation: EDL00225.1.
CCDSCCDS15016.1.
RefSeqNP_001104790.1. NM_001111320.1.
NP_034627.3. NM_010497.3.
UniGeneMm.9925.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CMJX-ray1.99A/B4-413[»]
2CMVX-ray2.52A/B4-413[»]
ProteinModelPortalO88844.
SMRO88844. Positions 4-413.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActO88844. 5 interactions.
MINTMINT-1859161.

PTM databases

PhosphoSiteO88844.

2D gel databases

COMPLUYEAST-2DPAGEO88844.
REPRODUCTION-2DPAGEO88844.
SWISS-2DPAGEO88844.

Proteomic databases

MaxQBO88844.
PaxDbO88844.
PRIDEO88844.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000097709; ENSMUSP00000095316; ENSMUSG00000025950.
ENSMUST00000169032; ENSMUSP00000127307; ENSMUSG00000025950.
GeneID15926.
KEGGmmu:15926.
UCSCuc007bhn.2. mouse.

Organism-specific databases

CTD3417.
MGIMGI:96413. Idh1.

Phylogenomic databases

eggNOGCOG0538.
GeneTreeENSGT00390000012547.
HOGENOMHOG000019858.
HOVERGENHBG006119.
KOK00031.
OMASCGGVAM.
OrthoDBEOG7QNVKS.
TreeFamTF300428.

Gene expression databases

ArrayExpressO88844.
BgeeO88844.
CleanExMM_IDH1.
GenevestigatorO88844.

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

EvolutionaryTraceO88844.
NextBio288640.
PROO88844.
SOURCESearch...

Entry information

Entry nameIDHC_MOUSE
AccessionPrimary (citable) accession number: O88844
Secondary accession number(s): Q3UAV7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

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