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UniProtKB/Swiss-Prot entry Q60597


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

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Entry information
Entry name ODO1_MOUSE
Primary accession number Q60597
Secondary accession numbers Q3UDM7 Q5DTI4 Q5SVX7 Q5SVX9 Q6PFZ2 Q80Y57 Q8K0K7 Q8K2Z3 Q8R3M2 Q91WP2
Integrated into Swiss-Prot on November 1, 1997
Sequence was last modified on May 1, 2007 (Sequence version 3)
Annotations were last modified on    September 23, 2008 (Entry version 78)
Name and origin of the protein
Protein name 2-oxoglutarate dehydrogenase E1 component, mitochondrial [Precursor]
Synonyms EC 1.2.4.2
Alpha-ketoglutarate dehydrogenase
Gene name
Name: Ogdh
Synonyms: Kiaa4192
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 [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J;
TISSUE=Bone marrow;
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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Brain;
Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene. The complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries.";
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
The mouse genome sequencing consortium;
Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).
STRAIN=C57BL/6, and FVB/N;
TISSUE=Brain, Colon, Mammary tumor, and Salivary gland;
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 123-135 AND 185-204, AND MASS SPECTROMETRY.
TISSUE=Hippocampus;
Lubec G., Klug S.;
Submitted (MAR-2007) to UniProtKB.
[6]
PROTEIN SEQUENCE OF 123-135; 311-319; 561-568; 616-633 AND 916-925, AND MASS SPECTROMETRY.
STRAIN=C57BL/6;
TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 829-958 (ISOFORMS 1/2/3/4).
STRAIN=BALB/c;
PubMed=8248240 [NCBI, ExPASy, EBI, Israel, Japan]
Udaka K., Tsomides T.J., Walden P., Fukusen N., Eisen H.N.;
"A ubiquitous protein is the source of naturally occurring peptides that are recognized by a CD8+ T-cell clone.";
Proc. Natl. Acad. Sci. U.S.A. 90:11272-11276(1993).
[8]
PROTEIN SEQUENCE OF 933-939.
DOI=10.1016/0092-8674(92)90617-L; PubMed=1606619 [NCBI, ExPASy, EBI, Israel, Japan]
Udaka K., Tsomides T.J., Eisen H.N.;
"A naturally occurring peptide recognized by alloreactive CD8+ cytotoxic T lymphocytes in association with a class I MHC protein.";
Cell 69:989-998(1992).
Comments
  • FUNCTION: The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3).
  • CATALYTIC ACTIVITY: 2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2.
  • COFACTOR: Thiamine pyrophosphate.
  • ENZYME REGULATION: Catabolite repressed.
  • SUBCELLULAR LOCATION: Mitochondrion matrix.
  • ALTERNATIVE PRODUCTS: 4 named isoforms [FASTA] produced by alternative splicing.
    Name1
    Isoform IDQ60597-1
    Note: No experimental confirmation available.
    This is the isoform sequence displayed in this entry.
    Name2
    Isoform IDQ60597-2
    Features which should be applied to build the isoform sequence: VSP_024799.
    Name3
    Isoform IDQ60597-3
    Note: No experimental confirmation available.
    Features which should be applied to build the isoform sequence: VSP_024801.
    Name4
    Isoform IDQ60597-4
    Features which should be applied to build the isoform sequence: VSP_024800.
  • SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.
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
AK147289; BAE27824.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK150009; BAE29234.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK169286; BAE41044.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK220536; BAD90530.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL607152; CAI24404.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL607152; CAI24405.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL607152; CAI24406.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC025040; AAH25040.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC013670; AAH13670.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC029143; AAH29143.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC031165; AAH31165.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC049104; AAH49104.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC057354; AAH57354.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U02971; AAC52130.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR I48884; A41911.
RefSeq NP_035086.2; -.
UniGene Mm.276348
3D structure databases
ModBase Q60597.
Protein-protein interaction databases
IntAct Q60597; -.
2D gel databases
REPRODUCTION-2DPAGE Q60597; -.
Organism-specific databases
MGI MGI:1098267; Ogdh.
Gene expression databases
ArrayExpress Q60597; -.
CleanEx MM_OGDH; -.
GermOnline ENSMUSG00000020456; Mus musculus.
Ontologies
GO
GO:0031966; Cellular component: mitochondrial membrane (inferred from sequence or structural similarity from UniProtKB).
GO:0034602; Molecular function: oxoglutarate dehydrogenase (NAD+) activity (inferred from direct assay from MGI).
GO:0004591; Molecular function: oxoglutarate dehydrogenase (succinyl-transferring) activity (inferred from sequence or structural similarity from UniProtKB).
GO:0006091; Biological process: generation of precursor metabolites and energy (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR011603; 2oxoglutarate_DHase_E1.
IPR001017; DHase_E1.
IPR005475; Transketo_Cen_R.
Graphical view of domain structure.
PANTHER PTHR23152; 2oxoglutarate_DH_E1; 1.
Pfam PF00676; E1_dh; 1.
PF02779; Transket_pyr; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000157; Oxoglu_dh_E1; 1.
TIGRFAMs TIGR00239; 2oxo_dh_E1; 1.
BLOCKS Q60597.
Genome annotation databases
Ensembl ENSMUSG00000020456; Mus musculus. [Contig view]
GeneID 18293; -.
KEGG mmu:18293; -.
NMPDR fig|10090.3.peg.23245; -.
Phylogenomic databases
HOVERGEN Q60597; -.
Other
SOURCE Ogdh; Mus musculus.
ROUGE KIAA4192.
ProtoNet Q60597.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Direct protein sequencing; Glycolysis; Mitochondrion; Oxidoreductase; Thiamine pyrophosphate; Transit peptide; Ubl conjugation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
TRANSIT   1     40  40     Mitochondrion (By similarity). 
CHAIN   41   1023  983     2-oxoglutarate dehydrogenase E1 component, mitochondrial. PRO_0000020434
REGION   933    939  7     Recognized by alloreactive CD8 cytotoxic T-lymphocytes in association with a class I MHC protein. 
CROSSLNK   534    534        Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) (By similarity). 
VAR_SEQ   139    172        IRGHHVAQLDPLGILDADLDSSVPADIISSTDKL -> VRGHHIAKSCVNFDDAPVTVSSNV (in isoform 2). VSP_024799
VAR_SEQ   139    172        IRGHHVAQLDPLGILDADLDSSVPADIISSTDKL -> VRGHHIAKLDPLGISCVNFDDAPVTVSSNVDLAVFKERLR MLTVG (in isoform 4). VSP_024800
VAR_SEQ   172    172        L -> LDLAVFKERLRMLTVG (in isoform 3). VSP_024801
CONFLICT   416    416        G -> V (in Ref. 4; AAH49104). 
CONFLICT   549    549        V -> F (in Ref. 4; AAH49104). 
CONFLICT   552    552        Q -> E (in Ref. 4; AAH57354). 
CONFLICT   576    576        E -> K (in Ref. 1; BAE29234). 
Sequence information
Length: 1023 AA [This is the length of the unprocessed precursor] Molecular weight: 116449 Da [This is the MW of the unprocessed precursor] CRC64: A0F3F8D36C7A76BC [This is a checksum on the sequence]
        10         20         30         40         50         60 
MFHLRTCAAK LRPLTASQTV KTFSQNKPAA IRTFQQIRCY SAPVAAEPFL SGTSSNYVEE 

        70         80         90        100        110        120 
MYCAWLENPK SVHKSWDIFF RNTNAGAPPG TAYQSPLSLS RSSLATMAHA QSLVEAQPNV 

       130        140        150        160        170        180 
DKLVEDHLAV QSLIRAYQIR GHHVAQLDPL GILDADLDSS VPADIISSTD KLGFYGLHES 

       190        200        210        220        230        240 
DLDKVFHLPT TTFIGGQEPA LPLREIIRRL EMAYCQHIGV EFMFINDLEQ CQWIRQKFET 

       250        260        270        280        290        300 
PGIMQFTNEE KRTLLARLVR STRFEEFLQR KWSSEKRFGL EGCEVLIPAL KTIIDMSSAN 

       310        320        330        340        350        360 
GVDYVIMGMP HRGRLNVLAN VIRKELEQIF CQFDSKLEAA DEGSGDMKYH LGMYHRRINR 

       370        380        390        400        410        420 
VTDRNITLSL VANPSHLEAA DPVVMGKTKA EQFYCGDTEG KKVMSILLHG DAAFAGQGIV 

       430        440        450        460        470        480 
YETFHLSDLP SYTTHGTVHV VVNNQIGFTT DPRMARSSPY PTDVARVVNA PIFHVNSDDP 

       490        500        510        520        530        540 
EAVMYVCKVA AEWRNTFHKD VVVDLVCYRR NGHNEMDEPM FTQPLMYKQI RKQKPVLQKY 

       550        560        570        580        590        600 
AELLVSQGVV NQPEYEEEIS KYDKICEEAF TRSKDEKILH IKHWLDSPWP GFFTLDGQPR 

       610        620        630        640        650        660 
SMTCPSTGLE EDVLFHIGKV ASSVPVENFT IHGGLSRILK TRRELVTNRT VDWALAEYMA 

       670        680        690        700        710        720 
FGSLLKEGIH VRLSGQDVER GTFSHRHHVL HDQNVDKRTC IPMNHLWPNQ APYTVCNSSL 

       730        740        750        760        770        780 
SEYGVLGFEL GFAMASPNAL VLWEAQFGDF NNMAQCIIDQ FICPGQAKWV RQNGIVLLLP 

       790        800        810        820        830        840 
HGMEGMGPEH SSARPERFLQ MCNDDPDVLP DLQEENFDIN QLYDCNWIVV NCSTPGNFFH 

       850        860        870        880        890        900 
VLRRQILLPF RKPLIVFTPK SLLRHPEART SFDEMLPGTH FQRVIPENGP AAQDPHKVKR 

       910        920        930        940        950        960 
LLFCTGKVYY DLTRERKARN MEEEVAITRI EQLSPFPFDL LLKEAQKYPN AELAWCQEEH 

       970        980        990       1000       1010       1020 
KNQGYYDYVK PRLRTTIDRA KPVWYAGRDP AAAPATGNKK THLTELQRFL DTAFDLDAFK 


KFS 

Q60597 in FASTA format

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View entry in raw text format (no links)
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