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Q02218 (ODO1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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

Calcium ions and ADP stimulate, whereas ATP and NADH reduce catalytic activity. Ref.10

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 processGlycolysis
   Cellular componentMitochondrion
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainTransit peptide
   LigandCalcium
Metal-binding
Thiamine pyrophosphate
   Molecular functionOxidoreductase
   PTMAcetylation
Isopeptide bond
Ubl conjugation
   Technical term3D-structure
Complete proteome
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

cellular metabolic process

Traceable author statement. Source: Reactome

cellular nitrogen compound metabolic process

Traceable author statement. Source: Reactome

cerebellar cortex development

Inferred from electronic annotation. Source: Ensembl

generation of precursor metabolites and energy

Inferred from sequence or structural similarity. Source: UniProtKB

glycolytic process

Inferred from electronic annotation. Source: UniProtKB-KW

hippocampus development

Inferred from electronic annotation. Source: Ensembl

lysine catabolic process

Traceable author statement. Source: Reactome

olfactory bulb mitral cell layer development

Inferred from electronic annotation. Source: Ensembl

pyramidal neuron development

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

striatum development

Inferred from electronic annotation. Source: Ensembl

succinyl-CoA metabolic process

Inferred from electronic annotation. Source: Ensembl

tangential migration from the subventricular zone to the olfactory bulb

Inferred from electronic annotation. Source: Ensembl

thalamus development

Inferred from electronic annotation. Source: Ensembl

tricarboxylic acid cycle

Traceable author statement. Source: Reactome

   Cellular_componentmitochondrial matrix

Traceable author statement. Source: Reactome

mitochondrial membrane

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrion

Inferred from direct assay. Source: HPA

oxoglutarate dehydrogenase complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

oxoglutarate dehydrogenase (NAD+) activity

Inferred from electronic annotation. Source: Ensembl

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
Note: Probably insensitive to calcium.
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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4040Mitochondrion
Chain41 – 10239832-oxoglutarate dehydrogenase, mitochondrial
PRO_0000020432

Regions

Calcium binding154 – 1585 Ref.10

Sites

Metal binding1541Calcium

Amino acid modifications

Modified residue741N6-succinyllysine By similarity
Modified residue4011N6-acetyllysine By similarity
Modified residue5641N6-succinyllysine By similarity
Modified residue9701N6-acetyllysine Ref.8
Cross-link534Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.7

Natural variations

Alternative sequence139 – 17234IRGHH…STDKL → VRGHHIAKLDPLGISCVNFD DAPVTVSSNV in isoform 2.
VSP_042313
Alternative sequence404 – 42724MSILL…TFHLS → RPRERRARQIVKAPCSSMEF RSPT in isoform 3.
VSP_043628
Alternative sequence428 – 1023596Missing in isoform 3.
VSP_043629
Natural variant10181V → I.
Corresponds to variant rs2070607 [ dbSNP | Ensembl ].
VAR_050435

Experimental info

Mutagenesis1541D → A: Six-fold decrease in sensitivity for calcium. Ref.10
Sequence conflict730 – 7334LGFA → AGLR in BAA01393. Ref.1
Sequence conflict730 – 7334LGFA → AGLR in BAA06836. Ref.2
Sequence conflict7551Q → L in BAG65261. Ref.3
Sequence conflict8311N → D in BAA06836. Ref.2
Sequence conflict9891D → N in BAA01393. Ref.1
Sequence conflict9891D → N in BAA06836. Ref.2

Sequences

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

Last modified November 13, 2007. Version 3.
Checksum: F428DD342F232E7C

FASTA1,023115,935
        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 

« Hide

Isoform 2 [UniParc].

Checksum: B416BF4EA052AC26
Show »

FASTA1,019115,514
Isoform 3 [UniParc].

Checksum: 11C89C89F2C6308E
Show »

FASTA42748,180

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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.
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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]"Studies on the regulation of the human E1 subunit of the 2-oxoglutarate dehydrogenase complex, including the identification of a novel calcium-binding site."
Armstrong C.T., Anderson J.L., Denton R.M.
Biochem. J. 459:369-381(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION, CALCIUM-BINDING SITES, MUTAGENESIS OF ASP-154.
[11]"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.
CCDSCCDS34627.1. [Q02218-1]
CCDS47580.1. [Q02218-3]
CCDS55107.1. [Q02218-2]
PIRA38234.
RefSeqNP_001003941.1. NM_001003941.2. [Q02218-3]
NP_001158508.1. NM_001165036.1. [Q02218-2]
NP_002532.2. NM_002541.3. [Q02218-1]
UniGeneHs.488181.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3ERYX-ray1.95P/Q932-940[»]
ProteinModelPortalQ02218.
SMRQ02218. Positions 130-1014.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111017. 21 interactions.
IntActQ02218. 7 interactions.
MINTMINT-1437057.
STRING9606.ENSP00000222673.

Chemistry

ChEMBLCHEMBL2816.
DrugBankDB00157. NADH.

PTM databases

PhosphoSiteQ02218.

Polymorphism databases

DMDM160332299.

2D gel databases

REPRODUCTION-2DPAGEIPI00098902.

Proteomic databases

MaxQBQ02218.
PaxDbQ02218.
PRIDEQ02218.

Protocols and materials databases

DNASU4967.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000222673; ENSP00000222673; ENSG00000105953. [Q02218-1]
ENST00000443864; ENSP00000388084; ENSG00000105953. [Q02218-3]
ENST00000449767; ENSP00000392878; ENSG00000105953. [Q02218-2]
GeneID4967.
KEGGhsa:4967.
UCSCuc003tlm.3. human. [Q02218-3]
uc003tln.3. human. [Q02218-1]
uc011kbx.2. human. [Q02218-2]

Organism-specific databases

CTD4967.
GeneCardsGC07P044646.
HGNCHGNC:8124. OGDH.
HPAHPA019514.
HPA020347.
MIM613022. gene.
neXtProtNX_Q02218.
Orphanet31. Oxoglutaricaciduria.
PharmGKBPA31910.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0567.
HOGENOMHOG000259586.
HOVERGENHBG001892.
InParanoidQ02218.
KOK00164.
PhylomeDBQ02218.
TreeFamTF300695.

Enzyme and pathway databases

BioCycMetaCyc:HS02832-MONOMER.
ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressQ02218.
BgeeQ02218.
CleanExHS_OGDH.
GenevestigatorQ02218.

Family and domain databases

Gene3D3.40.50.970. 2 hits.
InterProIPR011603. 2oxoglutarate_DH_E1.
IPR001017. DH_E1.
IPR029061. THDP-binding.
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]
SUPFAMSSF52518. SSF52518. 2 hits.
TIGRFAMsTIGR00239. 2oxo_dh_E1. 1 hit.
ProtoNetSearch...

Other

ChiTaRSOGDH. human.
EvolutionaryTraceQ02218.
GeneWikiOGDH.
GenomeRNAi4967.
NextBio19110.
PMAP-CutDBQ02218.
PROQ02218.
SOURCESearch...

Entry information

Entry nameODO1_HUMAN
AccessionPrimary (citable) accession number: Q02218
Secondary accession number(s): B4E2U9 expand/collapse secondary AC list , D3DVL0, E9PBM1, Q96DD3, Q9UDX0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: November 13, 2007
Last modified: July 9, 2014
This is version 151 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM