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P56574 (IDHP_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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], mitochondrial

Short name=IDH
EC=1.1.1.42
Alternative name(s):
ICD-M
IDP
NADP(+)-specific ICDH
Oxalosuccinate decarboxylase
Gene names
Name:Idh2
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

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 By similarity.

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 Ref.2.

Post-translational modification

Acetylation at Lys-413 dramatically reduces catalytic activity. Deacetylated by SIRT3 By similarity.

Miscellaneous

On the 2D-gel the determined pI of this protein (spot P8) is: 9.0, its MW is: 42 kDa.

Sequence similarities

Belongs to the isocitrate and isopropylmalate dehydrogenases family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3939Mitochondrion By similarity
Chain40 – 452413Isocitrate dehydrogenase [NADP], mitochondrial
PRO_0000083581

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 residue451N6-acetyllysine By similarity
Modified residue481N6-acetyllysine By similarity
Modified residue671N6-acetyllysine By similarity
Modified residue691N6-acetyllysine By similarity
Modified residue801N6-acetyllysine; alternate By similarity
Modified residue801N6-succinyllysine; alternate By similarity
Modified residue1061N6-acetyllysine; alternate By similarity
Modified residue1061N6-succinyllysine; alternate By similarity
Modified residue1551N6-acetyllysine By similarity
Modified residue1661N6-acetyllysine; alternate By similarity
Modified residue1661N6-succinyllysine; alternate By similarity
Modified residue1801N6-acetyllysine; alternate By similarity
Modified residue1801N6-succinyllysine; alternate By similarity
Modified residue1931N6-acetyllysine; alternate By similarity
Modified residue1931N6-succinyllysine; alternate By similarity
Modified residue1991N6-acetyllysine By similarity
Modified residue2561N6-acetyllysine; alternate By similarity
Modified residue2561N6-succinyllysine; alternate By similarity
Modified residue2631N6-acetyllysine By similarity
Modified residue2721N6-acetyllysine By similarity
Modified residue2751N6-acetyllysine By similarity
Modified residue2801N6-acetyllysine By similarity
Modified residue2821N6-acetyllysine; alternate By similarity
Modified residue2821N6-succinyllysine; alternate By similarity
Modified residue3841N6-acetyllysine; alternate By similarity
Modified residue3841N6-succinyllysine; alternate By similarity
Modified residue4001N6-acetyllysine By similarity
Modified residue4131N6-acetyllysine By similarity
Modified residue4421N6-acetyllysine By similarity

Experimental info

Sequence conflict491P → K AA sequence Ref.2
Sequence conflict521E → V AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
P56574 [UniParc].

Last modified December 12, 2006. Version 2.
Checksum: 2466E1CC2C2CE9D1

FASTA45250,967
        10         20         30         40         50         60 
MAGYLRAVSS LCRASGSTRT WAPAALNVPS 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 MFKLVFTPKD GSGAKEWEVY NFPAGGVGMG MYNTDESISG FAHSCFQYSI 

       250        260        270        280        290        300 
QKKWPLYLST KNTIMKAYDG 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]"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].
Tissue: Kidney.
[2]Li X.-P., Pleissner K.-P., Scheler C., Regitz-Zagrosek V., Salikov J., Jungblut P.R.
Submitted (SEP-1998) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 40-52, SUBCELLULAR LOCATION.
Strain: Wistar.
Tissue: Heart.
[3]Lubec G., Chen W.-Q.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 61-67; 70-89; 113-122; 141-149; 181-188; 244-251; 262-272; 289-299; 341-353 AND 414-426, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Hippocampus.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC076398 mRNA. Translation: AAH76398.1.
RefSeqNP_001014183.1. NM_001014161.1.
UniGeneRn.3490.

3D structure databases

ProteinModelPortalP56574.
SMRP56574. Positions 40-452.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid262802. 1 interaction.
IntActP56574. 1 interaction.
MINTMINT-1794004.
STRING10116.ENSRNOP00000019059.

PTM databases

PhosphoSiteP56574.

Proteomic databases

PaxDbP56574.
PRIDEP56574.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000019059; ENSRNOP00000019059; ENSRNOG00000013949.
GeneID361596.
KEGGrno:361596.
UCSCRGD:1597139. rat.

Organism-specific databases

CTD3418.
RGD1597139. Idh2.

Phylogenomic databases

eggNOGCOG0538.
GeneTreeENSGT00390000012547.
HOGENOMHOG000019858.
HOVERGENHBG006119.
InParanoidP56574.
KOK00031.
OMACFQYAIG.
OrthoDBEOG7QNVKS.
PhylomeDBP56574.
TreeFamTF300428.

Enzyme and pathway databases

SABIO-RKP56574.

Gene expression databases

GenevestigatorP56574.

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

NextBio676849.
PROP56574.

Entry information

Entry nameIDHP_RAT
AccessionPrimary (citable) accession number: P56574
Secondary accession number(s): Q6DGF1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: December 12, 2006
Last modified: May 14, 2014
This is version 92 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