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Q02218

- ODO1_HUMAN

UniProt

Q02218 - ODO1_HUMAN

Protein

2-oxoglutarate dehydrogenase, mitochondrial

Gene

OGDH

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 3 (13 Nov 2007)
      Previous versions | rss
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    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 – 1585

    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. cellular metabolic process Source: Reactome
    3. cellular nitrogen compound metabolic process Source: Reactome
    4. cerebellar cortex development Source: Ensembl
    5. generation of precursor metabolites and energy Source: UniProtKB
    6. glycolytic process Source: UniProtKB-KW
    7. hippocampus development Source: Ensembl
    8. lysine catabolic process Source: Reactome
    9. NADH metabolic process Source: Ensembl
    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

    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

    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 – 4040MitochondrionAdd
    BLAST
    Chaini41 – 10239832-oxoglutarate dehydrogenase, mitochondrialPRO_0000020432Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei74 – 741N6-succinyllysineBy similarity
    Modified residuei401 – 4011N6-acetyllysineBy similarity
    Cross-linki534 – 534Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Modified residuei564 – 5641N6-succinyllysineBy 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.
    ModBaseiSearch...
    MobiDBiSearch...

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti730 – 7334LGFA → AGLR in BAA01393. (PubMed:1542694)Curated
    Sequence conflicti730 – 7334LGFA → AGLR in BAA06836. (PubMed:7622061)Curated
    Sequence conflicti755 – 7551Q → L in BAG65261. (PubMed:14702039)Curated
    Sequence conflicti831 – 8311N → D in BAA06836. (PubMed:7622061)Curated
    Sequence conflicti989 – 9891D → N in BAA01393. (PubMed:1542694)Curated
    Sequence conflicti989 – 9891D → N in BAA06836. (PubMed:7622061)Curated

    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. 1 PublicationVSP_042313Add
    BLAST
    Alternative sequencei404 – 42724MSILL…TFHLS → RPRERRARQIVKAPCSSMEF RSPT in isoform 3. 1 PublicationVSP_043628Add
    BLAST
    Alternative sequencei428 – 1023596Missing in isoform 3. 1 PublicationVSP_043629Add
    BLAST

    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

    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: October 1, 2014
    This is version 153 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