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Q60597 (ODO1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
2-oxoglutarate dehydrogenase, mitochondrial

EC=1.2.4.2
Alternative name(s):
2-oxoglutarate dehydrogenase complex component E1
Short name=OGDC-E1
Alpha-ketoglutarate dehydrogenase
Gene names
Name:Ogdh
Synonyms:Kiaa4192
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1023 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO2. 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.

Sequence similarities

Belongs to the alpha-ketoglutarate dehydrogenase family.

Sequence caution

The sequence AAH31165.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAD90530.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentMitochondrion
   Coding sequence diversityAlternative splicing
   DomainTransit peptide
   LigandThiamine pyrophosphate
   Molecular functionOxidoreductase
   PTMAcetylation
Isopeptide bond
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_process2-oxoglutarate metabolic process

Inferred from electronic annotation. Source: Ensembl

NADH metabolic process

Inferred from electronic annotation. Source: Ensembl

cerebellar cortex development

Inferred from expression pattern PubMed 16901643. Source: UniProtKB

generation of precursor metabolites and energy

Inferred from sequence or structural similarity. Source: UniProtKB

glycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

hippocampus development

Inferred from expression pattern PubMed 16901643. Source: UniProtKB

olfactory bulb mitral cell layer development

Inferred from expression pattern PubMed 16901643. Source: UniProtKB

pyramidal neuron development

Inferred from expression pattern PubMed 16901643. Source: UniProtKB

striatum development

Inferred from expression pattern PubMed 16901643. Source: UniProtKB

succinyl-CoA metabolic process

Inferred from electronic annotation. Source: Ensembl

tangential migration from the subventricular zone to the olfactory bulb

Inferred from expression pattern PubMed 16901643. Source: UniProtKB

thalamus development

Inferred from expression pattern PubMed 16901643. Source: UniProtKB

tricarboxylic acid cycle

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrial membrane

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrion

Inferred from direct assay PubMed 14651853PubMed 17322295PubMed 18614015. Source: MGI

oxoglutarate dehydrogenase complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionoxoglutarate dehydrogenase (NAD+) activity

Inferred from direct assay PubMed 17322295. Source: MGI

oxoglutarate dehydrogenase (succinyl-transferring) activity

Inferred from sequence or structural similarity. Source: UniProtKB

thiamine pyrophosphate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q60597-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q60597-2)

The sequence of this isoform differs from the canonical sequence as follows:
     139-172: IRGHHVAQLDPLGILDADLDSSVPADIISSTDKL → VRGHHIAKSCVNFDDAPVTVSSNV
Isoform 3 (identifier: Q60597-3)

The sequence of this isoform differs from the canonical sequence as follows:
     172-172: L → LDLAVFKERLRMLTVG
Note: No experimental confirmation available.
Isoform 4 (identifier: Q60597-4)

The sequence of this isoform differs from the canonical sequence as follows:
     139-172: IRGHHVAQLDPLGILDADLDSSVPADIISSTDKL → VRGHHIAKLD...KERLRMLTVG

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4040Mitochondrion By similarity
Chain41 – 10239832-oxoglutarate dehydrogenase, mitochondrial
PRO_0000020434

Regions

Region933 – 9397Recognized by alloreactive CD8 cytotoxic T-lymphocytes in association with a class I MHC protein

Amino acid modifications

Modified residue741N6-succinyllysine Ref.8
Modified residue4011N6-acetyllysine Ref.9
Modified residue5641N6-succinyllysine Ref.8
Modified residue9701N6-acetyllysine By similarity
Cross-link534Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Natural variations

Alternative sequence139 – 17234IRGHH…STDKL → VRGHHIAKSCVNFDDAPVTV SSNV in isoform 2.
VSP_024799
Alternative sequence139 – 17234IRGHH…STDKL → VRGHHIAKLDPLGISCVNFD DAPVTVSSNVDLAVFKERLR MLTVG in isoform 4.
VSP_024800
Alternative sequence1721L → LDLAVFKERLRMLTVG in isoform 3.
VSP_024801

Experimental info

Sequence conflict4161G → V in AAH49104. Ref.4
Sequence conflict5491V → F in AAH49104. Ref.4
Sequence conflict5521Q → E in AAH57354. Ref.4
Sequence conflict5761E → K in BAE29234. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 2007. Version 3.
Checksum: A0F3F8D36C7A76BC

FASTA1,023116,449
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 64CBC6F0E46B5D5F
Show »

FASTA1,013115,419
Isoform 3 [UniParc].

Checksum: 7DC3C47068B12D2C
Show »

FASTA1,038118,179
Isoform 4 [UniParc].

Checksum: 7023215EEEE9516B
Show »

FASTA1,034117,758

References

« Hide 'large scale' references
[1]"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. expand/collapse author list , 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.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: C57BL/6J.
Tissue: Bone marrow.
[2]"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."
Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O., Koga H.
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Brain.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).
Strain: C57BL/6 and FVB/N.
Tissue: Brain, Colon, Mammary tumor and Salivary gland.
[5]Lubec G., Klug S., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 123-135; 185-204; 311-319; 561-568; 616-633 AND 916-925, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain and Hippocampus.
[6]"A ubiquitous protein is the source of naturally occurring peptides that are recognized by a CD8+ T-cell clone."
Udaka K., Tsomides T.J., Walden P., Fukusen N., Eisen H.N.
Proc. Natl. Acad. Sci. U.S.A. 90:11272-11276(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 829-958 (ISOFORMS 1/2/3/4).
Strain: BALB/c.
[7]"A naturally occurring peptide recognized by alloreactive CD8+ cytotoxic T lymphocytes in association with a class I MHC protein."
Udaka K., Tsomides T.J., Eisen H.N.
Cell 69:989-998(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 933-939.
[8]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-74 AND LYS-564, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[9]"Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-401, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK147289 mRNA. Translation: BAE27824.1.
AK150009 mRNA. Translation: BAE29234.1.
AK169286 mRNA. Translation: BAE41044.1.
AK220536 mRNA. Translation: BAD90530.1. Different initiation.
AL607152 Genomic DNA. Translation: CAI24404.1.
AL607152 Genomic DNA. Translation: CAI24405.1.
AL607152 Genomic DNA. Translation: CAI24406.1.
BC025040 mRNA. Translation: AAH25040.1.
BC013670 mRNA. Translation: AAH13670.1.
BC029143 mRNA. Translation: AAH29143.1.
BC031165 mRNA. Translation: AAH31165.1. Different initiation.
BC049104 mRNA. Translation: AAH49104.1.
BC057354 mRNA. Translation: AAH57354.1.
U02971 mRNA. Translation: AAC52130.1.
PIRA41911. I48884.
RefSeqNP_001239211.1. NM_001252282.1.
NP_001239212.1. NM_001252283.1.
NP_001239216.1. NM_001252287.1.
NP_001239217.1. NM_001252288.1.
NP_035086.2. NM_010956.4.
XP_006514645.1. XM_006514582.1.
XP_006514646.1. XM_006514583.1.
XP_006514647.1. XM_006514584.1.
XP_006514648.1. XM_006514585.1.
UniGeneMm.276348.
Mm.479411.
Mm.490272.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3E2HX-ray3.80Q932-940[»]
3TF7X-ray2.75B/F932-940[»]
ProteinModelPortalQ60597.
SMRQ60597. Positions 130-1014.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ60597. 5 interactions.
MINTMINT-1860288.

Chemistry

ChEMBLCHEMBL2176831.

PTM databases

PhosphoSiteQ60597.

2D gel databases

REPRODUCTION-2DPAGEQ60597.

Proteomic databases

PaxDbQ60597.
PRIDEQ60597.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000003461; ENSMUSP00000003461; ENSMUSG00000020456. [Q60597-1]
ENSMUST00000093350; ENSMUSP00000091041; ENSMUSG00000020456. [Q60597-4]
ENSMUST00000101554; ENSMUSP00000099090; ENSMUSG00000020456. [Q60597-1]
GeneID18293.
KEGGmmu:18293.
UCSCuc007hyf.2. mouse. [Q60597-1]
uc007hyg.2. mouse. [Q60597-3]
uc007hyh.2. mouse. [Q60597-4]

Organism-specific databases

CTD4967.
MGIMGI:1098267. Ogdh.
RougeSearch...

Phylogenomic databases

eggNOGCOG0567.
GeneTreeENSGT00530000063092.
HOVERGENHBG001892.
KOK00164.
OMANEGVANE.
OrthoDBEOG7FXZXH.
PhylomeDBQ60597.
TreeFamTF300695.

Gene expression databases

ArrayExpressQ60597.
BgeeQ60597.
CleanExMM_OGDH.
GenevestigatorQ60597.

Family and domain databases

InterProIPR011603. 2oxoglutarate_DH_E1.
IPR001017. DH_E1.
IPR005475. Transketolase-like_Pyr-bd.
[Graphical view]
PANTHERPTHR23152. PTHR23152. 1 hit.
PfamPF00676. E1_dh. 1 hit.
PF02779. Transket_pyr. 1 hit.
[Graphical view]
PIRSFPIRSF000157. Oxoglu_dh_E1. 1 hit.
SMARTSM00861. Transket_pyr. 1 hit.
[Graphical view]
TIGRFAMsTIGR00239. 2oxo_dh_E1. 1 hit.
ProtoNetSearch...

Other

ChiTaRSOGDH. mouse.
NextBio293740.
PROQ60597.
SOURCESearch...

Entry information

Entry nameODO1_MOUSE
AccessionPrimary (citable) accession number: Q60597
Secondary accession number(s): Q3UDM7 expand/collapse secondary AC list , Q5DTI4, Q5SVX7, Q5SVX9, Q6PFZ2, Q80Y57, Q8K0K7, Q8K2Z3, Q8R3M2, Q91WP2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 1, 2007
Last modified: April 16, 2014
This is version 132 of the entry and version 3 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot