Reviewed,
UniProtKB/Swiss-Prot P54071 (IDHP_MOUSE)
Last modified
November 25, 2008.
Version 68.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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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 |
| ||
| 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 | |
| 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
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
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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: 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. 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 | |
|---|---|
| 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 |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with


