Q02218 (ODO1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1023 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	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 BAA01393.1 differs from that shown. Reason: Frameshift at position 1003. The sequence BAA06836.1 differs from that shown. Reason: Frameshift at position 1003.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Mitochondrion
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Transit peptide
Ligand	Thiamine pyrophosphate
Molecular function	Oxidoreductase
PTM	Acetylation Isopeptide bond Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	2-oxoglutarate metabolic process Inferred from electronic annotation. Source: Compara NADH metabolic process Inferred from electronic annotation. Source: Compara cellular nitrogen compound metabolic process Traceable author statement. Source: Reactome cerebellar cortex development Inferred from electronic annotation. Source: Compara glycolysis Inferred from electronic annotation. Source: UniProtKB-KW hippocampus development Inferred from electronic annotation. Source: Compara lysine catabolic process Traceable author statement. Source: Reactome olfactory bulb mitral cell layer development Inferred from electronic annotation. Source: Compara pyramidal neuron development Inferred from electronic annotation. Source: Compara striatum development Inferred from electronic annotation. Source: Compara succinyl-CoA metabolic process Inferred from electronic annotation. Source: Compara tangential migration from the subventricular zone to the olfactory bulb Inferred from electronic annotation. Source: Compara thalamus development Inferred from electronic annotation. Source: Compara tricarboxylic acid cycle Traceable author statement. Source: Reactome
Cellular_component	mitochondrial matrix Traceable author statement. Source: Reactome mitochondrial membrane Inferred from sequence or structural similarity. Source: UniProtKB oxoglutarate dehydrogenase complex Inferred from electronic annotation. Source: Compara
Molecular_function	oxoglutarate dehydrogenase (NAD+) activity Inferred from electronic annotation. Source: Compara 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 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q02218-1)

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: Q02218-2)

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

Isoform 3 (identifier: Q02218-3)

The sequence of this isoform differs from the canonical sequence as follows:
     404-427: MSILLHGDAAFAGQGIVYETFHLS → RPRERRARQIVKAPCSSMEFRSPT
     428-1023: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 40	40	Mitochondrion
	Chain	41 – 1023	983	2-oxoglutarate dehydrogenase, mitochondrial		PRO_0000020432
Amino acid modifications
	Modified residue	970	1	N6-acetyllysine Ref.8
	Cross-link	534		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.7
Natural variations
	Alternative sequence	139 – 172	34	IRGHH…STDKL → VRGHHIAKLDPLGISCVNFD DAPVTVSSNV in isoform 2.		VSP_042313
	Alternative sequence	404 – 427	24	MSILL…TFHLS → RPRERRARQIVKAPCSSMEF RSPT in isoform 3.		VSP_043628
	Alternative sequence	428 – 1023	596	Missing in isoform 3.		VSP_043629
	Natural variant	1018	1	V → I. Corresponds to variant rs2070607 [ dbSNP | Ensembl ].		VAR_050435
Experimental info
	Sequence conflict	730 – 733	4	LGFA → AGLR in BAA01393. Ref.1
	Sequence conflict	730 – 733	4	LGFA → AGLR in BAA06836. Ref.2
	Sequence conflict	755	1	Q → L in BAG65261. Ref.3
	Sequence conflict	831	1	N → D in BAA06836. Ref.2
	Sequence conflict	989	1	D → N in BAA01393. Ref.1
	Sequence conflict	989	1	D → N in BAA06836. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 13, 2007. Version 3. Checksum: F428DD342F232E7C	FASTA	1,023	115,935
	10 20 30 40 50 60 MFHLRTCAAK LRPLTASQTV KTFSQNRPAA ARTFQQIRCY SAPVAAEPFL SGTSSNYVEE 70 80 90 100 110 120 MYCAWLENPK SVHKSWDIFF RNTNAGAPPG TAYQSPLPLS RGSLAAVAHA QSLVEAQPNV 130 140 150 160 170 180 DKLVEDHLAV QSLIRAYQIR GHHVAQLDPL GILDADLDSS VPADIISSTD KLGFYGLDES 190 200 210 220 230 240 DLDKVFHLPT TTFIGGQESA LPLREIIRRL EMAYCQHIGV EFMFINDLEQ CQWIRQKFET 250 260 270 280 290 300 PGIMQFTNEE KRTLLARLVR STRFEEFLQR KWSSEKRFGL EGCEVLIPAL KTIIDKSSEN 310 320 330 340 350 360 GVDYVIMGMP HRGRLNVLAN VIRKELEQIF CQFDSKLEAA DEGSGDVKYH 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 AEWRSTFHKD VVVDLVCYRR NGHNEMDEPM FTQPLMYKQI RKQKPVLQKY 550 560 570 580 590 600 AELLVSQGVV NQPEYEEEIS KYDKICEEAF ARSKDEKILH IKHWLDSPWP GFFTLDGQPR 610 620 630 640 650 660 SMSCPSTGLT EDILTHIGNV ASSVPVENFT IHGGLSRILK TRGEMVKNRT VDWALAEYMA 670 680 690 700 710 720 FGSLLKEGIH IRLSGQDVER GTFSHRHHVL HDQNVDKRTC IPMNHLWPNQ APYTVCNSSL 730 740 750 760 770 780 SEYGVLGFEL GFAMASPNAL VLWEAQFGDF HNTAQCIIDQ FICPGQAKWV RQNGIVLLLP 790 800 810 820 830 840 HGMEGMGPEH SSARPERFLQ MCNDDPDVLP DLKEANFDIN QLYDCNWVVV NCSTPGNFFH 850 860 870 880 890 900 VLRRQILLPF RKPLIIFTPK SLLRHPEARS SFDEMLPGTH FQRVIPEDGP AAQNPENVKR 910 920 930 940 950 960 LLFCTGKVYY DLTRERKARD MVGQVAITRI EQLSPFPFDL LLKEVQKYPN AELAWCQEEH 970 980 990 1000 1010 1020 KNQGYYDYVK PRLRTTISRA KPVWYAGRDP AAAPATGNKK THLTELQRLL DTAFDLDVFK NFS
	Isoform 2 [UniParc]. Checksum: B416BF4EA052AC26	FASTA	1,019	115,514
	10 20 30 40 50 60 MFHLRTCAAK LRPLTASQTV KTFSQNRPAA ARTFQQIRCY SAPVAAEPFL SGTSSNYVEE 70 80 90 100 110 120 MYCAWLENPK SVHKSWDIFF RNTNAGAPPG TAYQSPLPLS RGSLAAVAHA QSLVEAQPNV 130 140 150 160 170 180 DKLVEDHLAV QSLIRAYQVR GHHIAKLDPL GISCVNFDDA PVTVSSNVGF YGLDESDLDK 190 200 210 220 230 240 VFHLPTTTFI GGQESALPLR EIIRRLEMAY CQHIGVEFMF INDLEQCQWI RQKFETPGIM 250 260 270 280 290 300 QFTNEEKRTL LARLVRSTRF EEFLQRKWSS EKRFGLEGCE VLIPALKTII DKSSENGVDY 310 320 330 340 350 360 VIMGMPHRGR LNVLANVIRK ELEQIFCQFD SKLEAADEGS GDVKYHLGMY HRRINRVTDR 370 380 390 400 410 420 NITLSLVANP SHLEAADPVV MGKTKAEQFY CGDTEGKKVM SILLHGDAAF AGQGIVYETF 430 440 450 460 470 480 HLSDLPSYTT HGTVHVVVNN QIGFTTDPRM ARSSPYPTDV ARVVNAPIFH VNSDDPEAVM 490 500 510 520 530 540 YVCKVAAEWR STFHKDVVVD LVCYRRNGHN EMDEPMFTQP LMYKQIRKQK PVLQKYAELL 550 560 570 580 590 600 VSQGVVNQPE YEEEISKYDK ICEEAFARSK DEKILHIKHW LDSPWPGFFT LDGQPRSMSC 610 620 630 640 650 660 PSTGLTEDIL THIGNVASSV PVENFTIHGG LSRILKTRGE MVKNRTVDWA LAEYMAFGSL 670 680 690 700 710 720 LKEGIHIRLS GQDVERGTFS HRHHVLHDQN VDKRTCIPMN HLWPNQAPYT VCNSSLSEYG 730 740 750 760 770 780 VLGFELGFAM ASPNALVLWE AQFGDFHNTA QCIIDQFICP GQAKWVRQNG IVLLLPHGME 790 800 810 820 830 840 GMGPEHSSAR PERFLQMCND DPDVLPDLKE ANFDINQLYD CNWVVVNCST PGNFFHVLRR 850 860 870 880 890 900 QILLPFRKPL IIFTPKSLLR HPEARSSFDE MLPGTHFQRV IPEDGPAAQN PENVKRLLFC 910 920 930 940 950 960 TGKVYYDLTR ERKARDMVGQ VAITRIEQLS PFPFDLLLKE VQKYPNAELA WCQEEHKNQG 970 980 990 1000 1010 YYDYVKPRLR TTISRAKPVW YAGRDPAAAP ATGNKKTHLT ELQRLLDTAF DLDVFKNFS
	Isoform 3 [UniParc]. Checksum: 11C89C89F2C6308E	FASTA	427	48,180
	10 20 30 40 50 60 MFHLRTCAAK LRPLTASQTV KTFSQNRPAA ARTFQQIRCY SAPVAAEPFL SGTSSNYVEE 70 80 90 100 110 120 MYCAWLENPK SVHKSWDIFF RNTNAGAPPG TAYQSPLPLS RGSLAAVAHA QSLVEAQPNV 130 140 150 160 170 180 DKLVEDHLAV QSLIRAYQIR GHHVAQLDPL GILDADLDSS VPADIISSTD KLGFYGLDES 190 200 210 220 230 240 DLDKVFHLPT TTFIGGQESA LPLREIIRRL EMAYCQHIGV EFMFINDLEQ CQWIRQKFET 250 260 270 280 290 300 PGIMQFTNEE KRTLLARLVR STRFEEFLQR KWSSEKRFGL EGCEVLIPAL KTIIDKSSEN 310 320 330 340 350 360 GVDYVIMGMP HRGRLNVLAN VIRKELEQIF CQFDSKLEAA DEGSGDVKYH LGMYHRRINR 370 380 390 400 410 420 VTDRNITLSL VANPSHLEAA DPVVMGKTKA EQFYCGDTEG KKVRPRERRA RQIVKAPCSS MEFRSPT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and nucleotide sequence of the cDNA encoding human 2-oxoglutarate dehydrogenase (lipoamide)." Koike K., Urata Y., Goto S. Proc. Natl. Acad. Sci. U.S.A. 89:1963-1967(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Liver.
[2]	"The gene encoding human 2-oxoglutarate dehydrogenase: structural organization and mapping to chromosome 7p13-p14." Koike K. Gene 159:261-266(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SEQUENCE REVISION.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Trachea.
[4]	"The DNA sequence of human chromosome 7." Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K. Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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 AND 3). Tissue: Bone marrow and Muscle.
[7]	"Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry." Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D. Proteomics 7:868-874(2007) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-534, MASS SPECTROMETRY. Tissue: Mammary cancer.
[8]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-970, MASS SPECTROMETRY.
[9]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]	"Different thermodynamic binding mechanisms and peptide fine specificities associated with a panel of structurally similar high-affinity T cell receptors." Jones L.L., Colf L.A., Bankovich A.J., Stone J.D., Gao Y.G., Chan C.M., Huang R.H., Garcia K.C., Kranz D.M. Biochemistry 47:12398-12408(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 932-940 IN COMPLEX WITH H-2 CLASS I HISTOCOMPATIBILITY COMPLEX.
+	Additional computationally mapped references.

Web resources

Wikipedia

Alpha-ketoglutarate dehydrogenase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D10523 mRNA. Translation: BAA01393.1. Frameshift.
D32064 Genomic DNA. Translation: BAA06836.1. Frameshift.
AK304439 mRNA. Translation: BAG65261.1.
AC004859 Genomic DNA. Translation: AAQ96884.1.
AC004859 Genomic DNA. Translation: AAQ96885.1.
AC011894 Genomic DNA. No translation available.
CH471128 Genomic DNA. Translation: EAW61086.1.
CH471128 Genomic DNA. Translation: EAW61087.1.
CH471128 Genomic DNA. Translation: EAW61089.1.
BC004964 mRNA. Translation: AAH04964.1.
BC009580 mRNA. Translation: AAH09580.1.
BC014617 mRNA. Translation: AAH14617.1.

IPI

IPI00098902.
IPI00386497.

PIR

A38234.

RefSeq

NP_001003941.1. NM_001003941.2.
NP_001158508.1. NM_001165036.1.
NP_002532.2. NM_002541.3.

UniGene

Hs.488181.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3ERY	X-ray	1.95	P/Q	932-940	[»]

ProteinModelPortal

Q02218.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q02218. 7 interactions.

STRING

9606.ENSP00000222673.

PTM databases

PhosphoSite

Q02218.

Polymorphism databases

DMDM

160332299.

2D gel databases

REPRODUCTION-2DPAGE

IPI00098902.

Proteomic databases

PaxDb

Q02218.

PRIDE

Q02218.

Protocols and materials databases

DNASU

4967.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000222673; ENSP00000222673; ENSG00000105953.
ENST00000443864; ENSP00000388084; ENSG00000105953.
ENST00000449767; ENSP00000392878; ENSG00000105953.

GeneID

4967.

KEGG

hsa:4967.

UCSC

uc003tln.3. human.

Organism-specific databases

CTD

4967.

GeneCards

GC07P044646.

HGNC

HGNC:8124. OGDH.

HPA

HPA019514.
HPA020347.

MIM

613022. gene.

neXtProt

NX_Q02218.

Orphanet

31. Oxoglutaricaciduria.

PharmGKB

PA31910.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0567.

HOGENOM

HOG000259586.

HOVERGEN

HBG001892.

InParanoid

Q02218.

KO

K00164.

PhylomeDB

Q02218.

Enzyme and pathway databases

BioCyc

MetaCyc:HS02832-MONOMER.

Reactome

REACT_111217. Metabolism.

Gene expression databases

ArrayExpress

Q02218.

Bgee

Q02218.

CleanEx

HS_OGDH.

Genevestigator

Q02218.

GermOnline

ENSG00000105953. Homo sapiens.

Family and domain databases

InterPro

IPR011603. 2oxoglutarate_DH_E1.
IPR001017. DH_E1.
IPR005475. Transketolase-like_Pyr-bd.
[Graphical view]

PANTHER

PTHR23152. PTHR23152. 1 hit.

Pfam

PF00676. E1_dh. 1 hit.
PF02779. Transket_pyr. 1 hit.
[Graphical view]

PIRSF

PIRSF000157. Oxoglu_dh_E1. 1 hit.

SMART

SM00861. Transket_pyr. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00239. 2oxo_dh_E1. 1 hit.

ProtoNet

Search...

Other

ChEMBL

CHEMBL2816.

ChiTaRS

OGDH. human.

DrugBank

DB00157. NADH.

EvolutionaryTrace

Q02218.

GenomeRNAi

4967.

NextBio

19110.

PMAP-CutDB

Q02218.

SOURCE

Search...

Entry information

Entry name

ODO1_HUMAN

Accession

Primary (citable) accession number: Q02218
Secondary accession number(s): B4E2U9 , D3DVL0, E9PBM1, Q96DD3, Q9UDX0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	November 13, 2007
Last modified:	April 3, 2013
This is version 138 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.