Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P10515

- ODP2_HUMAN

UniProt

P10515 - ODP2_HUMAN

Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial

Gene

DLAT

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 178 (01 Oct 2014)
      Sequence version 3 (25 Nov 2008)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2, and thereby links the glycolytic pathway to the tricarboxylic cycle.

    Catalytic activityi

    Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine.

    Cofactori

    Binds 2 lipoyl cofactors covalently.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei620 – 6201Sequence Analysis
    Active sitei624 – 6241Sequence Analysis

    GO - Molecular functioni

    1. dihydrolipoyllysine-residue acetyltransferase activity Source: UniProtKB
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. cellular metabolic process Source: Reactome
    2. glucose metabolic process Source: UniProtKB-KW
    3. pyruvate metabolic process Source: Reactome
    4. regulation of acetyl-CoA biosynthetic process from pyruvate Source: Reactome
    5. small molecule metabolic process Source: Reactome
    6. tricarboxylic acid cycle Source: UniProtKB-KW

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Carbohydrate metabolism, Glucose metabolism, Tricarboxylic acid cycle

    Enzyme and pathway databases

    BioCyciMetaCyc:HS07688-MONOMER.
    ReactomeiREACT_12528. Regulation of pyruvate dehydrogenase (PDH) complex.
    REACT_2071. Pyruvate metabolism.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial (EC:2.3.1.12)
    Alternative name(s):
    70 kDa mitochondrial autoantigen of primary biliary cirrhosis
    Short name:
    PBC
    Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
    M2 antigen complex 70 kDa subunit
    Pyruvate dehydrogenase complex component E2
    Short name:
    PDC-E2
    Short name:
    PDCE2
    Gene namesi
    Name:DLAT
    Synonyms:DLTA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:2896. DLAT.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial matrix Source: Reactome
    2. mitochondrial pyruvate dehydrogenase complex Source: UniProtKB
    3. mitochondrion Source: UniProt

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    Primary biliary cirrhosis is a chronic, progressive cholestatic liver disease characterized by the presence of antimitochondrial autoantibodies in patients' serum. It manifests with inflammatory obliteration of intra-hepatic bile duct, leading to liver cell damage and cirrhosis. Patients with primary biliary cirrhosis show autoantibodies against the E2 component of pyruvate dehydrogenase complex.
    Pyruvate dehydrogenase E2 deficiency (PDHE2 deficiency) [MIM:245348]: Pyruvate dehydrogenase (PDH) deficiency is a major cause of primary lactic acidosis and neurological dysfunction in infancy and early childhood. In this form of PDH deficiency episodic dystonia is the major neurological manifestation, with other more common features of pyruvate dehydrogenase deficiency, such as hypotonia and ataxia, being less prominent.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Organism-specific databases

    MIMi245348. phenotype.
    Orphaneti79244. Pyruvate dehydrogenase E2 deficiency.
    PharmGKBiPA27350.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 8686MitochondrionAdd
    BLAST
    Chaini87 – 647561Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrialPRO_0000020479Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei132 – 1321N6-lipoyllysine1 Publication
    Modified residuei259 – 2591N6-lipoyllysine1 Publication
    Modified residuei466 – 4661N6-acetyllysine1 Publication
    Modified residuei473 – 4731N6-succinyllysineBy similarity
    Modified residuei547 – 5471N6-succinyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP10515.
    PaxDbiP10515.
    PRIDEiP10515.

    PTM databases

    PhosphoSiteiP10515.

    Expressioni

    Gene expression databases

    ArrayExpressiP10515.
    BgeeiP10515.
    CleanExiHS_DLAT.
    GenevestigatoriP10515.

    Organism-specific databases

    HPAiCAB003782.
    HPA040786.

    Interactioni

    Subunit structurei

    Part of the multimeric pyruvate dehydrogenase complex that contains multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (DLAT, E2) and lipoamide dehydrogenase (DLD, E3). These subunits are bound to an inner core composed of about 48 DLAT and 12 PDHX molecules. Interacts with PDK2 and PDK3.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PDHBP111777EBI-2959723,EBI-1035872

    Protein-protein interaction databases

    BioGridi108081. 25 interactions.
    DIPiDIP-29496N.
    IntActiP10515. 8 interactions.
    MINTiMINT-3007324.
    STRINGi9606.ENSP00000280346.

    Structurei

    Secondary structure

    1
    647
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi92 – 954
    Beta strandi100 – 1023
    Beta strandi105 – 1106
    Beta strandi123 – 1297
    Beta strandi134 – 1385
    Beta strandi140 – 1478
    Beta strandi156 – 1583
    Beta strandi162 – 1687
    Helixi170 – 1778
    Beta strandi181 – 1833
    Beta strandi218 – 2225
    Beta strandi229 – 2313
    Beta strandi232 – 2387
    Beta strandi251 – 2566
    Beta strandi261 – 2655
    Beta strandi270 – 2778
    Beta strandi283 – 2853
    Beta strandi289 – 2979
    Helixi301 – 3033

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FYCNMR-A212-315[»]
    1Y8NX-ray2.60B212-319[»]
    1Y8OX-ray2.48B212-319[»]
    1Y8PX-ray2.63B212-319[»]
    2DNENMR-A92-186[»]
    2PNRX-ray2.50C/G212-319[»]
    2Q8IX-ray2.60B212-319[»]
    3B8Kelectron microscopy8.80A409-647[»]
    3CRKX-ray2.30C/D214-300[»]
    3CRLX-ray2.61C/D214-300[»]
    ProteinModelPortaliP10515.
    SMRiP10515. Positions 92-182, 214-306, 409-647.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP10515.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini92 – 16675Lipoyl-binding 1Add
    BLAST
    Domaini219 – 29375Lipoyl-binding 2Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni358 – 38932E3-binding siteBy similarityAdd
    BLAST
    Regioni417 – 647231CatalyticBy similarityAdd
    BLAST

    Sequence similaritiesi

    Belongs to the 2-oxoacid dehydrogenase family.Curated
    Contains 2 lipoyl-binding domains.Curated

    Keywords - Domaini

    Lipoyl, Repeat, Transit peptide

    Phylogenomic databases

    eggNOGiCOG0508.
    HOGENOMiHOG000281566.
    HOVERGENiHBG005063.
    InParanoidiP10515.
    KOiK00627.
    OMAiPISNIRK.
    PhylomeDBiP10515.
    TreeFamiTF106145.

    Family and domain databases

    Gene3Di3.30.559.10. 1 hit.
    4.10.320.10. 1 hit.
    InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
    IPR001078. 2-oxoacid_DH_actylTfrase.
    IPR000089. Biotin_lipoyl.
    IPR023213. CAT-like_dom.
    IPR004167. E3-bd.
    IPR006257. LAT1.
    IPR011053. Single_hybrid_motif.
    [Graphical view]
    PfamiPF00198. 2-oxoacid_dh. 1 hit.
    PF00364. Biotin_lipoyl. 2 hits.
    PF02817. E3_binding. 1 hit.
    [Graphical view]
    SUPFAMiSSF47005. SSF47005. 1 hit.
    SSF51230. SSF51230. 2 hits.
    TIGRFAMsiTIGR01349. PDHac_trf_mito. 1 hit.
    PROSITEiPS50968. BIOTINYL_LIPOYL. 2 hits.
    PS00189. LIPOYL. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P10515-1 [UniParc]FASTAAdd to Basket

    « Hide

    MWRVCARRAQ NVAPWAGLEA RWTALQEVPG TPRVTSRSGP APARRNSVTT    50
    GYGGVRALCG WTPSSGATPR NRLLLQLLGS PGRRYYSLPP HQKVPLPSLS 100
    PTMQAGTIAR WEKKEGDKIN EGDLIAEVET DKATVGFESL EECYMAKILV 150
    AEGTRDVPIG AIICITVGKP EDIEAFKNYT LDSSAAPTPQ AAPAPTPAAT 200
    ASPPTPSAQA PGSSYPPHMQ VLLPALSPTM TMGTVQRWEK KVGEKLSEGD 250
    LLAEIETDKA TIGFEVQEEG YLAKILVPEG TRDVPLGTPL CIIVEKEADI 300
    SAFADYRPTE VTDLKPQVPP PTPPPVAAVP PTPQPLAPTP SAPCPATPAG 350
    PKGRVFVSPL AKKLAVEKGI DLTQVKGTGP DGRITKKDID SFVPSKVAPA 400
    PAAVVPPTGP GMAPVPTGVF TDIPISNIRR VIAQRLMQSK QTIPHYYLSI 450
    DVNMGEVLLV RKELNKILEG RSKISVNDFI IKASALACLK VPEANSSWMD 500
    TVIRQNHVVD VSVAVSTPAG LITPIVFNAH IKGVETIAND VVSLATKARE 550
    GKLQPHEFQG GTFTISNLGM FGIKNFSAII NPPQACILAI GASEDKLVPA 600
    DNEKGFDVAS MMSVTLSCDH RVVDGAVGAQ WLAEFRKYLE KPITMLL 647
    Length:647
    Mass (Da):68,997
    Last modified:November 25, 2008 - v3
    Checksum:iDD93A8E666E377C2
    GO

    Sequence cautioni

    The sequence AAA62253.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the N-terminal part.
    The sequence AAA62253.1 differs from that shown. Reason: Frameshift at positions 449, 451 and 455.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti112 – 1121E → K in CAA68787. (PubMed:3191998)Curated
    Sequence conflicti342 – 3421A → T in AAA62253. (PubMed:3174635)Curated
    Sequence conflicti358 – 3581S → D in AAA62253. (PubMed:3174635)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti43 – 431A → V.1 Publication
    Corresponds to variant rs2303436 [ dbSNP | Ensembl ].
    VAR_047410
    Natural varianti98 – 981S → F.
    Corresponds to variant rs537057 [ dbSNP | Ensembl ].
    VAR_047411
    Natural varianti99 – 991L → F.
    Corresponds to variant rs537060 [ dbSNP | Ensembl ].
    VAR_047412
    Natural varianti209 – 2091Q → R.
    Corresponds to variant rs11553595 [ dbSNP | Ensembl ].
    VAR_047413
    Natural varianti313 – 3131D → V.
    Corresponds to variant rs11553592 [ dbSNP | Ensembl ].
    VAR_047414
    Natural varianti318 – 3181V → A.1 Publication
    Corresponds to variant rs627441 [ dbSNP | Ensembl ].
    VAR_047415
    Natural varianti451 – 4511D → N.1 Publication
    Corresponds to variant rs10891314 [ dbSNP | Ensembl ].
    VAR_047416

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK223596 mRNA. Translation: BAD97316.1.
    AP000907 Genomic DNA. No translation available.
    J03866 mRNA. Translation: AAA62253.1. Sequence problems.
    Y00978 mRNA. Translation: CAA68787.1.
    CCDSiCCDS8354.1.
    PIRiA40497.
    RefSeqiNP_001922.2. NM_001931.4.
    UniGeneiHs.335551.

    Genome annotation databases

    EnsembliENST00000280346; ENSP00000280346; ENSG00000150768.
    GeneIDi1737.
    KEGGihsa:1737.
    UCSCiuc001pmo.3. human.

    Polymorphism databases

    DMDMi215274207.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK223596 mRNA. Translation: BAD97316.1 .
    AP000907 Genomic DNA. No translation available.
    J03866 mRNA. Translation: AAA62253.1 . Sequence problems.
    Y00978 mRNA. Translation: CAA68787.1 .
    CCDSi CCDS8354.1.
    PIRi A40497.
    RefSeqi NP_001922.2. NM_001931.4.
    UniGenei Hs.335551.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FYC NMR - A 212-315 [» ]
    1Y8N X-ray 2.60 B 212-319 [» ]
    1Y8O X-ray 2.48 B 212-319 [» ]
    1Y8P X-ray 2.63 B 212-319 [» ]
    2DNE NMR - A 92-186 [» ]
    2PNR X-ray 2.50 C/G 212-319 [» ]
    2Q8I X-ray 2.60 B 212-319 [» ]
    3B8K electron microscopy 8.80 A 409-647 [» ]
    3CRK X-ray 2.30 C/D 214-300 [» ]
    3CRL X-ray 2.61 C/D 214-300 [» ]
    ProteinModelPortali P10515.
    SMRi P10515. Positions 92-182, 214-306, 409-647.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108081. 25 interactions.
    DIPi DIP-29496N.
    IntActi P10515. 8 interactions.
    MINTi MINT-3007324.
    STRINGi 9606.ENSP00000280346.

    Chemistry

    DrugBanki DB00157. NADH.

    PTM databases

    PhosphoSitei P10515.

    Polymorphism databases

    DMDMi 215274207.

    Proteomic databases

    MaxQBi P10515.
    PaxDbi P10515.
    PRIDEi P10515.

    Protocols and materials databases

    DNASUi 1737.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000280346 ; ENSP00000280346 ; ENSG00000150768 .
    GeneIDi 1737.
    KEGGi hsa:1737.
    UCSCi uc001pmo.3. human.

    Organism-specific databases

    CTDi 1737.
    GeneCardsi GC11P111895.
    HGNCi HGNC:2896. DLAT.
    HPAi CAB003782.
    HPA040786.
    MIMi 245348. phenotype.
    608770. gene.
    neXtProti NX_P10515.
    Orphaneti 79244. Pyruvate dehydrogenase E2 deficiency.
    PharmGKBi PA27350.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0508.
    HOGENOMi HOG000281566.
    HOVERGENi HBG005063.
    InParanoidi P10515.
    KOi K00627.
    OMAi PISNIRK.
    PhylomeDBi P10515.
    TreeFami TF106145.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS07688-MONOMER.
    Reactomei REACT_12528. Regulation of pyruvate dehydrogenase (PDH) complex.
    REACT_2071. Pyruvate metabolism.

    Miscellaneous databases

    EvolutionaryTracei P10515.
    GeneWikii Dihydrolipoyl_transacetylase.
    GenomeRNAii 1737.
    NextBioi 7043.
    PROi P10515.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P10515.
    Bgeei P10515.
    CleanExi HS_DLAT.
    Genevestigatori P10515.

    Family and domain databases

    Gene3Di 3.30.559.10. 1 hit.
    4.10.320.10. 1 hit.
    InterProi IPR003016. 2-oxoA_DH_lipoyl-BS.
    IPR001078. 2-oxoacid_DH_actylTfrase.
    IPR000089. Biotin_lipoyl.
    IPR023213. CAT-like_dom.
    IPR004167. E3-bd.
    IPR006257. LAT1.
    IPR011053. Single_hybrid_motif.
    [Graphical view ]
    Pfami PF00198. 2-oxoacid_dh. 1 hit.
    PF00364. Biotin_lipoyl. 2 hits.
    PF02817. E3_binding. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47005. SSF47005. 1 hit.
    SSF51230. SSF51230. 2 hits.
    TIGRFAMsi TIGR01349. PDHac_trf_mito. 1 hit.
    PROSITEi PS50968. BIOTINYL_LIPOYL. 2 hits.
    PS00189. LIPOYL. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS VAL-43; ALA-318 AND ASN-451.
      Tissue: Kidney.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "Primary structure of the human M2 mitochondrial autoantigen of primary biliary cirrhosis: dihydrolipoamide acetyltransferase."
      Coppel R.L., McNeilage L.J., Surh C.D., van de Water J., Spithill T.W., Whittingham S., Gershwin M.E.
      Proc. Natl. Acad. Sci. U.S.A. 85:7317-7321(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 33-647.
      Tissue: Placenta.
    4. "Nucleotide sequence of a cDNA for the dihydrolipoamide acetyltransferase component of human pyruvate dehydrogenase complex."
      Thekkumkara T.J., Ho L., Wexler I.D., Pon G., Liu T., Patel M.S.
      FEBS Lett. 240:45-48(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 73-647, LIPOYLATION AT LYS-132 AND LYS-259.
      Tissue: Liver.
    5. "Organization of the cores of the mammalian pyruvate dehydrogenase complex formed by E2 and E2 plus the E3-binding protein and their capacities to bind the E1 and E3 components."
      Hiromasa Y., Fujisawa T., Aso Y., Roche T.E.
      J. Biol. Chem. 279:6921-6933(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    6. "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-466, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "Three-dimensional structure of the major autoantigen in primary biliary cirrhosis."
      Howard M.J., Fuller C., Broadhurst R.W., Perham R.N., Tang J.G., Quinn J., Diamond A.G., Yeaman S.J.
      Gastroenterology 115:139-146(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 214-315.
    9. "Clinical and genetic spectrum of pyruvate dehydrogenase deficiency: dihydrolipoamide acetyltransferase (E2) deficiency."
      Head R.A., Brown R.M., Zolkipli Z., Shahdadpuri R., King M.D., Clayton P.T., Brown G.K.
      Ann. Neurol. 58:234-241(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN PDHE2 DEFICIENCY.
    10. "Crystal structure of pyruvate dehydrogenase kinase 3 bound to lipoyl domain 2 of human pyruvate dehydrogenase complex."
      Kato M., Chuang J.L., Tso S.C., Wynn R.M., Chuang D.T.
      EMBO J. 24:1763-1774(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.48 ANGSTROMS) OF 212-319 IN COMPLEX WITH PDK3.
    11. "Solution structure of RSGI RUH-058, a lipoyl domain of human 2-oxoacid dehydrogenase."
      RIKEN structural genomics initiative (RSGI)
      Submitted (OCT-2006) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 92-186.
    12. "Crystal structure of an asymmetric complex of pyruvate dehydrogenase kinase 3 with lipoyl domain 2 and its biological implications."
      Devedjiev Y., Steussy C.N., Vassylyev D.G.
      J. Mol. Biol. 370:407-416(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 212-319 IN COMPLEX WITH PDK3.
    13. "Distinct structural mechanisms for inhibition of pyruvate dehydrogenase kinase isoforms by AZD7545, dichloroacetate, and radicicol."
      Kato M., Li J., Chuang J.L., Chuang D.T.
      Structure 15:992-1004(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 212-319 IN COMPLEX WITH PDK3.
    14. "Structural and functional insights into the molecular mechanisms responsible for the regulation of pyruvate dehydrogenase kinase 2."
      Green T., Grigorian A., Klyuyeva A., Tuganova A., Luo M., Popov K.M.
      J. Biol. Chem. 283:15789-15798(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 214-300 IN COMPLEX WITH PDK2.

    Entry informationi

    Entry nameiODP2_HUMAN
    AccessioniPrimary (citable) accession number: P10515
    Secondary accession number(s): Q16783, Q53EP3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: November 25, 2008
    Last modified: October 1, 2014
    This is version 178 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 11
      Human chromosome 11: 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