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UniProtKB/Swiss-Prot entry P54071


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name IDHP_MOUSE
Primary accession number P54071
Secondary accession numbers Q8C2R9 Q9EQK1
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on September 11, 2007 (Sequence version 3)
Annotations were last modified on    July 22, 2008 (Entry version 65)
Name and origin of the protein
Protein name Isocitrate dehydrogenase [NADP], mitochondrial [Precursor]
Synonyms IDH
EC 1.1.1.42
Oxalosuccinate decarboxylase
NADP(+)-specific ICDH
IDP
ICD-M
Gene name
Name: Idh2
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/c;
TISSUE=Heart;
DOI=10.1002/(SICI)1097-4644(19960301)60:3<400::AID-JCB11>3.3.CO;2-2; PubMed=8867815 [NCBI, ExPASy, EBI, Israel, Japan]
Yang L., Luo H., Vinay P., Wu J.;
"Molecular cloning of the cDNA of mouse mitochondrial NADP-dependent isocitrate dehydrogenase and the expression of the gene during lymphocyte activation.";
J. Cell. Biochem. 60:400-410(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
DOI=10.1074/jbc.M010120200; PubMed=11278619 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Control of mitochondrial redox balance and cellular defense against oxidative damage by mitochondrial NADP+-dependent isocitrate dehydrogenase.";
J. Biol. Chem. 276:16168-16176(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD;
TISSUE=Embryo, Heart, and Thymus;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N-3;
TISSUE=Mammary tumor;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 44-60 AND 81-89, AND MASS SPECTROMETRY.
STRAIN=C57BL/6;
TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[6]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-106 AND LYS-272, AND MASS SPECTROMETRY.
TISSUE=Liver;
DOI=10.1016/j.molcel.2006.06.026; PubMed=16916647 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.";
Mol. Cell 23:607-618(2006).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U51167; AAC52473.1; ALT_FRAME; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF212319; AAG43538.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK088110; BAC40149.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK145753; BAE26628.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK161640; BAE36505.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK169395; BAE41142.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC060030; AAH60030.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_766599.1; -.
UniGene Mm.246432
3D structure databases
HSSP P33198; 1LWD. [HSSP ENTRY / PDB]
SMR P54071; 112-524.
ModBase P54071.
Protein-protein interaction databases
IntAct P54071; -.
PTM databases
PhosphoSite P54071; -.
Organism-specific databases
MGI MGI:96414; Idh2.
Gene expression databases
ArrayExpress P54071; -.
CleanEx MM_IDH2; -.
GermOnline ENSMUSG00000030541; Mus musculus.
Ontologies
GO
GO:0005743; Cellular component: mitochondrial inner membrane (inferred from direct assay from MGI).
GO:0004450; Molecular function: isocitrate dehydrogenase (NADP+) activity (inferred from direct assay from MGI).
QuickGo view.
Family and domain databases
InterPro IPR004790; IsoCit_DHase_NADP-dep_euk.
IPR001804; IsoCit_IM_DHase.
Graphical view of domain structure.
Gene3D G3DSA:3.40.718.10; IDH_IMDH; 1.
PANTHER PTHR11822; IDH_NADP_euk; 1.
Pfam PF00180; Iso_dh; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000108; IDH_NADP; 1.
TIGRFAMs TIGR00127; nadp_idh_euk; 1.
PROSITE PS00470; IDH_IMDH; 1.
BLOCKS P54071.
Genome annotation databases
Ensembl ENSMUSG00000030541; Mus musculus. [Contig view]
GeneID 269951; -.
KEGG mmu:269951; -.
Phylogenomic databases
HOGENOM P54071; -.
HOVERGEN P54071; -.
Other
SOURCE Idh2; Mus musculus.
ProtoNet P54071.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Direct protein sequencing; Glyoxylate bypass; Magnesium; Manganese; Metal-binding; Mitochondrion; NADP; Oxidoreductase; Stress response; Transit peptide; Tricarboxylic acid cycle.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
TRANSIT   1    39  39     Mitochondrion (By similarity). 
CHAIN   40   452  413     Isocitrate dehydrogenase [NADP], mitochondrial. PRO_0000014421
NP_BIND   115   117  3     NADP (By similarity). 
NP_BIND   349   354  6     NADP (By similarity). 
REGION   134   140  7     Substrate binding (By similarity). 
METAL   291   291        Magnesium or manganese (By similarity). 
METAL   314   314        Magnesium or manganese (By similarity). 
BINDING   117   117        Substrate (By similarity). 
BINDING   122   122        NADP (By similarity). 
BINDING   149   149        Substrate (By similarity). 
BINDING   172   172        Substrate (By similarity). 
BINDING   299   299        NADP (By similarity). 
BINDING   367   367        NADP; via amide nitrogen and carbonyl oxygen (By similarity). 
SITE   179   179  1     Critical for catalysis (By similarity). 
SITE   251   251  1     Critical for catalysis (By similarity). 
MOD_RES   106   106        N6-acetyllysine. 
MOD_RES   272   272        N6-acetyllysine. 
CONFLICT   104   104        T -> A (in Ref. 1; AAC52473). 
CONFLICT   109   109        V -> M (in Ref. 1; AAC52473). 
CONFLICT   152   152        I -> S (in Ref. 1; AAC52473). 
CONFLICT   200   200        D -> N (in Ref. 1; AAC52473). 
CONFLICT   214   214        A -> G (in Ref. 1; AAC52473). 
CONFLICT   280   280        K -> R (in Ref. 1; AAC52473 and 2; AAG43538). 
CONFLICT   322   323        QG -> SR (in Ref. 1; AAC52473). 
CONFLICT   367   368        NP -> KG (in Ref. 1; AAC52473). 
CONFLICT   398   398        L -> R (in Ref. 1; AAC52473). 
CONFLICT   408   408        Missing (in Ref. 1; AAC52473). 
Sequence information
Length: 452 AA [This is the length of the unprocessed precursor] Molecular weight: 50906 Da [This is the MW of the unprocessed precursor] CRC64: 19BB5CF78512ECAB [This is a checksum on the sequence]
        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 

P54071 in FASTA format

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