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Q02218

- ODO1_HUMAN

UniProt

Q02218 - ODO1_HUMAN

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Protein
2-oxoglutarate dehydrogenase, mitochondrial
Gene
OGDH
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2.

Cofactori

Thiamine pyrophosphate.

Enzyme regulationi

Calcium ions and ADP stimulate, whereas ATP and NADH reduce catalytic activity.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi154 – 1541Calcium

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi154 – 15851 Publication

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. oxoglutarate dehydrogenase (NAD+) activity Source: Ensembl
  3. oxoglutarate dehydrogenase (succinyl-transferring) activity Source: UniProtKB
  4. thiamine pyrophosphate binding Source: InterPro

GO - Biological processi

  1. 2-oxoglutarate metabolic process Source: Ensembl
  2. NADH metabolic process Source: Ensembl
  3. cellular metabolic process Source: Reactome
  4. cellular nitrogen compound metabolic process Source: Reactome
  5. cerebellar cortex development Source: Ensembl
  6. generation of precursor metabolites and energy Source: UniProtKB
  7. glycolytic process Source: UniProtKB-KW
  8. hippocampus development Source: Ensembl
  9. lysine catabolic process Source: Reactome
  10. olfactory bulb mitral cell layer development Source: Ensembl
  11. pyramidal neuron development Source: Ensembl
  12. small molecule metabolic process Source: Reactome
  13. striatum development Source: Ensembl
  14. succinyl-CoA metabolic process Source: Ensembl
  15. tangential migration from the subventricular zone to the olfactory bulb Source: Ensembl
  16. thalamus development Source: Ensembl
  17. tricarboxylic acid cycle Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Calcium, Metal-binding, Thiamine pyrophosphate

Enzyme and pathway databases

BioCyciMetaCyc:HS02832-MONOMER.
ReactomeiREACT_1298. Lysine catabolism.
REACT_1785. Citric acid cycle (TCA cycle).

Names & Taxonomyi

Protein namesi
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 namesi
Name:OGDH
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:8124. OGDH.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial matrix Source: Reactome
  2. mitochondrial membrane Source: UniProtKB
  3. mitochondrion Source: HPA
  4. oxoglutarate dehydrogenase complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi154 – 1541D → A: Six-fold decrease in sensitivity for calcium. 1 Publication

Organism-specific databases

Orphaneti31. Oxoglutaricaciduria.
PharmGKBiPA31910.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4040Mitochondrion
Add
BLAST
Chaini41 – 10239832-oxoglutarate dehydrogenase, mitochondrial
PRO_0000020432Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei74 – 741N6-succinyllysine By similarity
Modified residuei401 – 4011N6-acetyllysine By similarity
Cross-linki534 – 534Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei564 – 5641N6-succinyllysine By similarity
Modified residuei970 – 9701N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiQ02218.
PaxDbiQ02218.
PRIDEiQ02218.

2D gel databases

REPRODUCTION-2DPAGEIPI00098902.

PTM databases

PhosphoSiteiQ02218.

Miscellaneous databases

PMAP-CutDBQ02218.

Expressioni

Gene expression databases

ArrayExpressiQ02218.
BgeeiQ02218.
CleanExiHS_OGDH.
GenevestigatoriQ02218.

Organism-specific databases

HPAiHPA019514.
HPA020347.

Interactioni

Protein-protein interaction databases

BioGridi111017. 23 interactions.
IntActiQ02218. 7 interactions.
MINTiMINT-1437057.
STRINGi9606.ENSP00000222673.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ERYX-ray1.95P/Q932-940[»]
ProteinModelPortaliQ02218.
SMRiQ02218. Positions 130-1014.

Miscellaneous databases

EvolutionaryTraceiQ02218.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0567.
HOGENOMiHOG000259586.
HOVERGENiHBG001892.
InParanoidiQ02218.
KOiK00164.
PhylomeDBiQ02218.
TreeFamiTF300695.

Family and domain databases

Gene3Di3.40.50.970. 2 hits.
InterProiIPR011603. 2oxoglutarate_DH_E1.
IPR001017. DH_E1.
IPR029061. THDP-binding.
IPR005475. Transketolase-like_Pyr-bd.
[Graphical view]
PANTHERiPTHR23152. PTHR23152. 1 hit.
PfamiPF00676. E1_dh. 1 hit.
PF02779. Transket_pyr. 1 hit.
[Graphical view]
PIRSFiPIRSF000157. Oxoglu_dh_E1. 1 hit.
SMARTiSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 2 hits.
TIGRFAMsiTIGR00239. 2oxo_dh_E1. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q02218-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MFHLRTCAAK LRPLTASQTV KTFSQNRPAA ARTFQQIRCY SAPVAAEPFL     50
SGTSSNYVEE MYCAWLENPK SVHKSWDIFF RNTNAGAPPG TAYQSPLPLS 100
RGSLAAVAHA QSLVEAQPNV DKLVEDHLAV QSLIRAYQIR GHHVAQLDPL 150
GILDADLDSS VPADIISSTD KLGFYGLDES DLDKVFHLPT TTFIGGQESA 200
LPLREIIRRL EMAYCQHIGV EFMFINDLEQ CQWIRQKFET PGIMQFTNEE 250
KRTLLARLVR STRFEEFLQR KWSSEKRFGL EGCEVLIPAL KTIIDKSSEN 300
GVDYVIMGMP HRGRLNVLAN VIRKELEQIF CQFDSKLEAA DEGSGDVKYH 350
LGMYHRRINR VTDRNITLSL VANPSHLEAA DPVVMGKTKA EQFYCGDTEG 400
KKVMSILLHG DAAFAGQGIV YETFHLSDLP SYTTHGTVHV VVNNQIGFTT 450
DPRMARSSPY PTDVARVVNA PIFHVNSDDP EAVMYVCKVA AEWRSTFHKD 500
VVVDLVCYRR NGHNEMDEPM FTQPLMYKQI RKQKPVLQKY AELLVSQGVV 550
NQPEYEEEIS KYDKICEEAF ARSKDEKILH IKHWLDSPWP GFFTLDGQPR 600
SMSCPSTGLT EDILTHIGNV ASSVPVENFT IHGGLSRILK TRGEMVKNRT 650
VDWALAEYMA FGSLLKEGIH IRLSGQDVER GTFSHRHHVL HDQNVDKRTC 700
IPMNHLWPNQ APYTVCNSSL SEYGVLGFEL GFAMASPNAL VLWEAQFGDF 750
HNTAQCIIDQ FICPGQAKWV RQNGIVLLLP HGMEGMGPEH SSARPERFLQ 800
MCNDDPDVLP DLKEANFDIN QLYDCNWVVV NCSTPGNFFH VLRRQILLPF 850
RKPLIIFTPK SLLRHPEARS SFDEMLPGTH FQRVIPEDGP AAQNPENVKR 900
LLFCTGKVYY DLTRERKARD MVGQVAITRI EQLSPFPFDL LLKEVQKYPN 950
AELAWCQEEH KNQGYYDYVK PRLRTTISRA KPVWYAGRDP AAAPATGNKK 1000
THLTELQRLL DTAFDLDVFK NFS 1023
Length:1,023
Mass (Da):115,935
Last modified:November 13, 2007 - v3
Checksum:iF428DD342F232E7C
GO
Isoform 2 (identifier: Q02218-2) [UniParc]FASTAAdd to Basket

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

Note: Probably insensitive to calcium.

Show »
Length:1,019
Mass (Da):115,514
Checksum:iB416BF4EA052AC26
GO
Isoform 3 (identifier: Q02218-3) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:427
Mass (Da):48,180
Checksum:i11C89C89F2C6308E
GO

Sequence cautioni

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.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1018 – 10181V → I.
Corresponds to variant rs2070607 [ dbSNP | Ensembl ].
VAR_050435

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei139 – 17234IRGHH…STDKL → VRGHHIAKLDPLGISCVNFD DAPVTVSSNV in isoform 2.
VSP_042313Add
BLAST
Alternative sequencei404 – 42724MSILL…TFHLS → RPRERRARQIVKAPCSSMEF RSPT in isoform 3.
VSP_043628Add
BLAST
Alternative sequencei428 – 1023596Missing in isoform 3.
VSP_043629Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti730 – 7334LGFA → AGLR in BAA01393. 1 Publication
Sequence conflicti730 – 7334LGFA → AGLR in BAA06836. 1 Publication
Sequence conflicti755 – 7551Q → L in BAG65261. 1 Publication
Sequence conflicti831 – 8311N → D in BAA06836. 1 Publication
Sequence conflicti989 – 9891D → N in BAA01393. 1 Publication
Sequence conflicti989 – 9891D → N in BAA06836. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS34627.1. [Q02218-1]
CCDS47580.1. [Q02218-3]
CCDS55107.1. [Q02218-2]
PIRiA38234.
RefSeqiNP_001003941.1. NM_001003941.2. [Q02218-3]
NP_001158508.1. NM_001165036.1. [Q02218-2]
NP_002532.2. NM_002541.3. [Q02218-1]
UniGeneiHs.488181.

Genome annotation databases

EnsembliENST00000222673; ENSP00000222673; ENSG00000105953. [Q02218-1]
ENST00000443864; ENSP00000388084; ENSG00000105953. [Q02218-3]
ENST00000449767; ENSP00000392878; ENSG00000105953. [Q02218-2]
GeneIDi4967.
KEGGihsa:4967.
UCSCiuc003tlm.3. human. [Q02218-3]
uc003tln.3. human. [Q02218-1]
uc011kbx.2. human. [Q02218-2]

Polymorphism databases

DMDMi160332299.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Alpha-ketoglutarate dehydrogenase entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS34627.1. [Q02218-1 ]
CCDS47580.1. [Q02218-3 ]
CCDS55107.1. [Q02218-2 ]
PIRi A38234.
RefSeqi NP_001003941.1. NM_001003941.2. [Q02218-3 ]
NP_001158508.1. NM_001165036.1. [Q02218-2 ]
NP_002532.2. NM_002541.3. [Q02218-1 ]
UniGenei Hs.488181.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3ERY X-ray 1.95 P/Q 932-940 [» ]
ProteinModelPortali Q02218.
SMRi Q02218. Positions 130-1014.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111017. 23 interactions.
IntActi Q02218. 7 interactions.
MINTi MINT-1437057.
STRINGi 9606.ENSP00000222673.

Chemistry

ChEMBLi CHEMBL2816.
DrugBanki DB00157. NADH.

PTM databases

PhosphoSitei Q02218.

Polymorphism databases

DMDMi 160332299.

2D gel databases

REPRODUCTION-2DPAGE IPI00098902.

Proteomic databases

MaxQBi Q02218.
PaxDbi Q02218.
PRIDEi Q02218.

Protocols and materials databases

DNASUi 4967.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000222673 ; ENSP00000222673 ; ENSG00000105953 . [Q02218-1 ]
ENST00000443864 ; ENSP00000388084 ; ENSG00000105953 . [Q02218-3 ]
ENST00000449767 ; ENSP00000392878 ; ENSG00000105953 . [Q02218-2 ]
GeneIDi 4967.
KEGGi hsa:4967.
UCSCi uc003tlm.3. human. [Q02218-3 ]
uc003tln.3. human. [Q02218-1 ]
uc011kbx.2. human. [Q02218-2 ]

Organism-specific databases

CTDi 4967.
GeneCardsi GC07P044646.
HGNCi HGNC:8124. OGDH.
HPAi HPA019514.
HPA020347.
MIMi 613022. gene.
neXtProti NX_Q02218.
Orphaneti 31. Oxoglutaricaciduria.
PharmGKBi PA31910.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0567.
HOGENOMi HOG000259586.
HOVERGENi HBG001892.
InParanoidi Q02218.
KOi K00164.
PhylomeDBi Q02218.
TreeFami TF300695.

Enzyme and pathway databases

BioCyci MetaCyc:HS02832-MONOMER.
Reactomei REACT_1298. Lysine catabolism.
REACT_1785. Citric acid cycle (TCA cycle).

Miscellaneous databases

ChiTaRSi OGDH. human.
EvolutionaryTracei Q02218.
GeneWikii OGDH.
GenomeRNAii 4967.
NextBioi 19110.
PMAP-CutDB Q02218.
PROi Q02218.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q02218.
Bgeei Q02218.
CleanExi HS_OGDH.
Genevestigatori Q02218.

Family and domain databases

Gene3Di 3.40.50.970. 2 hits.
InterProi IPR011603. 2oxoglutarate_DH_E1.
IPR001017. DH_E1.
IPR029061. THDP-binding.
IPR005475. Transketolase-like_Pyr-bd.
[Graphical view ]
PANTHERi PTHR23152. PTHR23152. 1 hit.
Pfami PF00676. E1_dh. 1 hit.
PF02779. Transket_pyr. 1 hit.
[Graphical view ]
PIRSFi PIRSF000157. Oxoglu_dh_E1. 1 hit.
SMARTi SM00861. Transket_pyr. 1 hit.
[Graphical view ]
SUPFAMi SSF52518. SSF52518. 2 hits.
TIGRFAMsi TIGR00239. 2oxo_dh_E1. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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.

Entry informationi

Entry nameiODO1_HUMAN
AccessioniPrimary (citable) accession number: Q02218
Secondary accession number(s): B4E2U9
, D3DVL0, E9PBM1, Q96DD3, Q9UDX0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: November 13, 2007
Last modified: September 3, 2014
This is version 152 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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