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UniProtKB/Swiss-Prot entry P28241


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

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Entry information
Entry name IDH2_YEAST
Primary accession number P28241
Secondary accession numbers None
Integrated into Swiss-Prot on December 1, 1992
Sequence was last modified on December 1, 1992 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 80)
Name and origin of the protein
Protein name Isocitrate dehydrogenase [NAD] subunit 2, mitochondrial [Precursor]
Synonyms EC 1.1.1.41
Isocitric dehydrogenase
NAD(+)-specific ICDH
Gene name
Name: IDH2
OrderedLocusNames: YOR136W
ORFNames: O3326, YOR3326W
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1939242 [NCBI, ExPASy, EBI, Israel, Japan]
Cupp J.R., McAlister-Henn L.;
"NAD(+)-dependent isocitrate dehydrogenase. Cloning, nucleotide sequence, and disruption of the IDH2 gene from Saccharomyces cerevisiae.";
J. Biol. Chem. 266:22199-22205(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
DOI=10.1002/(SICI)1097-0061(19960315)12:3<281::AID-YEA904>3.3.CO;2-F; PubMed=8904341 [NCBI, ExPASy, EBI, Israel, Japan]
Wiemann S., Rechmann S., Benes V., Voss H., Schwager C., Vlcek C., Stegemann J., Zimmermann J., Erfle H., Paces V., Ansorge W.;
"Sequencing and analysis of 51 kb on the right arm of chromosome XV from Saccharomyces cerevisiae reveals 30 open reading frames.";
Yeast 12:281-288(1996).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1002/(SICI)1097-0061(19970615)13:7<655::AID-YEA120>3.0.CO;2-I; PubMed=9200815 [NCBI, ExPASy, EBI, Israel, Japan]
Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C., Schwager C., Paces V., Sander C., Ansorge W.;
"DNA sequencing and analysis of 130 kb from yeast chromosome XV.";
Yeast 13:655-672(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=9169874 [NCBI, ExPASy, EBI, Israel, Japan]
Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
Nature 387:98-102(1997).
[5]
PROTEIN SEQUENCE OF 16-26.
STRAIN=SG7;
PubMed=2198251 [NCBI, ExPASy, EBI, Israel, Japan]
Keys D.A., McAlister-Henn L.;
"Subunit structure, expression, and function of NAD(H)-specific isocitrate dehydrogenase in Saccharomyces cerevisiae.";
J. Bacteriol. 172:4280-4287(1990).
[6]
RNA-BINDING, AND PROTEIN SEQUENCE OF 16-34.
DOI=10.1093/nar/21.23.5328; PubMed=7505425 [NCBI, ExPASy, EBI, Israel, Japan]
Elzinga S.D.J., Bednarz A.L., van Oosterum K., Dekker P.J.T., Grivell L.A.;
"Yeast mitochondrial NAD(+)-dependent isocitrate dehydrogenase is an RNA-binding protein.";
Nucleic Acids Res. 21:5328-5331(1993).
[7]
SUBCELLULAR LOCATION.
DOI=10.1021/bi010277r; PubMed=11502169 [NCBI, ExPASy, EBI, Israel, Japan]
Grandier-Vazeille X., Bathany K., Chaignepain S., Camougrand N., Manon S., Schmitter J.-M.;
"Yeast mitochondrial dehydrogenases are associated in a supramolecular complex.";
Biochemistry 40:9758-9769(2001).
[8]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-349, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700098-MCP200; PubMed=17761666 [NCBI, ExPASy, EBI, Israel, Japan]
Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B., van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.;
"Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase.";
Mol. Cell. Proteomics 6:1896-1906(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-105; THR-153 AND SER-360, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
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
M74131; AAA34702.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X94335; CAA64054.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z75043; CAA99335.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X90518; CAA62110.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A39309; A39309.
RefSeq NP_014779.1; -.
3D structure databases
PDB
3BLV; X-ray; 3.20 A; B/D/F/H=16-369.[ExPASy / RCSB / EBI]
3BLW; X-ray; 4.30 A; B/D/F/H/J/L/N/P=16-369.[ExPASy / RCSB / EBI]
3BLX; X-ray; 2.70 A; B/D/F/H/J/L/N/P=16-369.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 3BLV; -.
3BLW; -.
3BLX; -.
ModBase P28241.
Protein-protein interaction databases
DIP DIP:4296N; -.
IntAct P28241; -.
Enzyme and pathway databases
BioCyc MetaCyc:MON-13686; -.
Organism-specific databases
CYGD YOR136w; -.
SGD S000005662; IDH2.
Yeast-GFP YOR136W.
Gene expression databases
GermOnline YOR136W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005962; Cellular component: mitochondrial isocitrate dehydrogenase complex (NAD+) (inferred from direct assay from SGD).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006537; Biological process: glutamate biosynthetic process (traceable author statement from SGD).
GO:0006102; Biological process: isocitrate metabolic process (traceable author statement from SGD).
GO:0006099; Biological process: tricarboxylic acid cycle (traceable author statement from SGD).
QuickGo view.
Family and domain databases
InterPro IPR004434; IsoCit_DHase_NAD_mit.
IPR001804; IsoCit_IM_DHase.
Graphical view of domain structure.
Gene3D G3DSA:3.40.718.10; IDH_IMDH; 1.
PANTHER PTHR11835; IDH_IMDH_dimeric; 1.
Pfam PF00180; Iso_dh; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR00175; mito_nad_idh; 1.
PROSITE PS00470; IDH_IMDH; 1.
BLOCKS P28241.
Proteomic databases
PeptideAtlas P28241; -.
Genome annotation databases
Ensembl YOR136W; Saccharomyces cerevisiae. [Contig view]
GeneID 854303; -.
GenomeReviews Y13140_GR; YOR136W.
KEGG sce:YOR136W; -.
NMPDR fig|4932.3.peg.5882; -.
Phylogenomic databases
HOGENOM P28241; -.
Other
LinkHub P28241; -.
ProtoNet P28241.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Allosteric enzyme; Complete proteome; Direct protein sequencing; Magnesium; Manganese; Metal-binding; Mitochondrion; NAD; Oxidoreductase; Phosphoprotein; RNA-binding; Transit peptide; Tricarboxylic acid cycle.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    15  15     Mitochondrion. 
CHAIN   16   369  354     Isocitrate dehydrogenase [NAD] subunit 2, mitochondrial. PRO_0000014434
METAL   237   237        Magnesium or manganese (By similarity). 
METAL   263   263        Magnesium or manganese (By similarity). 
METAL   267   267        Magnesium or manganese (By similarity). 
BINDING   119   119        Substrate (By similarity). 
BINDING   129   129        Substrate (By similarity). 
BINDING   150   150        Substrate (By similarity). 
BINDING   237   237        Substrate (By similarity). 
SITE   157   157  1     Critical for catalysis (By similarity). 
SITE   204   204  1     Critical for catalysis (By similarity). 
MOD_RES   105   105        Phosphothreonine. 
MOD_RES   153   153        Phosphothreonine. 
MOD_RES   349   349        Phosphothreonine. 
MOD_RES   360   360        Phosphoserine. 
CONFLICT   25    25        R -> G (in Ref. 5; AA sequence). 
Sequence information
Length: 369 AA [This is the length of the unprocessed precursor] Molecular weight: 39739 Da [This is the MW of the unprocessed precursor] CRC64: 3A48C999776CE373 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MLRNTFFRNT SRRFLATVKQ PSIGRYTGKP NPSTGKYTVS FIEGDGIGPE ISKSVKKIFS 

        70         80         90        100        110        120 
AANVPIEWES CDVSPIFVNG LTTIPDPAVQ SITKNLVALK GPLATPIGKG HRSLNLTLRK 

       130        140        150        160        170        180 
TFGLFANVRP AKSIEGFKTT YENVDLVLIR ENTEGEYSGI EHIVCPGVVQ SIKLITRDAS 

       190        200        210        220        230        240 
ERVIRYAFEY ARAIGRPRVI VVHKSTIQRL ADGLFVNVAK ELSKEYPDLT LETELIDNSV 

       250        260        270        280        290        300 
LKVVTNPSAY TDAVSVCPNL YGDILSDLNS GLSAGSLGLT PSANIGHKIS IFEAVHGSAP 

       310        320        330        340        350        360 
DIAGQDKANP TALLLSSVMM LNHMGLTNHA DQIQNAVLST IASGPENRTG DLAGTATTSS 


FTEAVIKRL 

P28241 in FASTA format

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