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P52209

- 6PGD_HUMAN

UniProt

P52209 - 6PGD_HUMAN

Protein

6-phosphogluconate dehydrogenase, decarboxylating

Gene

PGD

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO2, with concomitant reduction of NADP to NADPH.By similarity

    Catalytic activityi

    6-phospho-D-gluconate + NADP+ = D-ribulose 5-phosphate + CO2 + NADPH.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei103 – 1031NADP1 Publication
    Binding sitei103 – 1031SubstrateBy similarity
    Active sitei184 – 1841Proton acceptorBy similarity
    Active sitei191 – 1911Proton donorBy similarity
    Binding sitei192 – 1921SubstrateBy similarity
    Binding sitei261 – 2611Substrate; via amide nitrogenBy similarity
    Binding sitei288 – 2881SubstrateBy similarity
    Binding sitei447 – 4471Substrate; shared with dimeric partnerBy similarity
    Binding sitei453 – 4531Substrate; shared with dimeric partnerBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi10 – 156NADP1 Publication
    Nucleotide bindingi33 – 353NADP1 Publication
    Nucleotide bindingi75 – 773NADP1 Publication
    Nucleotide bindingi478 – 4814NADP; shared with dimeric partner1 Publication

    GO - Molecular functioni

    1. NADP binding Source: InterPro
    2. phosphogluconate dehydrogenase (decarboxylating) activity Source: UniProtKB

    GO - Biological processi

    1. carbohydrate metabolic process Source: Reactome
    2. D-gluconate metabolic process Source: UniProtKB-KW
    3. oxidation-reduction process Source: UniProtKB
    4. pentose biosynthetic process Source: Ensembl
    5. pentose-phosphate shunt Source: UniProtKB
    6. pentose-phosphate shunt, oxidative branch Source: UniProtKB
    7. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Gluconate utilization, Pentose shunt

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BioCyciMetaCyc:HS06949-MONOMER.
    ReactomeiREACT_1859. Pentose phosphate pathway (hexose monophosphate shunt).
    SABIO-RKP52209.
    UniPathwayiUPA00115; UER00410.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    6-phosphogluconate dehydrogenase, decarboxylating (EC:1.1.1.44)
    Gene namesi
    Name:PGD
    Synonyms:PGDH
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:8891. PGD.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. extracellular vesicular exosome Source: UniProt
    3. nucleus Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33229.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 4834826-phosphogluconate dehydrogenase, decarboxylatingPRO_0000090063Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei38 – 381N6-acetyllysineBy similarity
    Modified residuei59 – 591N6-acetyllysine1 Publication
    Modified residuei257 – 2571PhosphoserineBy similarity
    Modified residuei263 – 2631PhosphothreonineBy similarity
    Modified residuei267 – 2671PhosphothreonineBy similarity
    Modified residuei270 – 2701PhosphoserineBy similarity
    Modified residuei309 – 3091N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP52209.
    PaxDbiP52209.
    PeptideAtlasiP52209.
    PRIDEiP52209.

    PTM databases

    PhosphoSiteiP52209.

    Expressioni

    Gene expression databases

    ArrayExpressiP52209.
    BgeeiP52209.
    CleanExiHS_PGD.
    GenevestigatoriP52209.

    Organism-specific databases

    HPAiHPA031314.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi111247. 36 interactions.
    IntActiP52209. 6 interactions.
    MINTiMINT-1415782.
    STRINGi9606.ENSP00000270776.

    Structurei

    Secondary structure

    1
    483
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 96
    Helixi13 – 2412
    Beta strandi29 – 324
    Helixi37 – 448
    Turni45 – 495
    Helixi58 – 636
    Beta strandi70 – 734
    Helixi79 – 8810
    Helixi89 – 913
    Beta strandi97 – 1004
    Helixi106 – 11813
    Beta strandi122 – 1309
    Helixi131 – 1377
    Beta strandi140 – 1456
    Helixi147 – 1493
    Helixi150 – 16011
    Turni165 – 1673
    Beta strandi169 – 1713
    Helixi179 – 20729
    Helixi213 – 22311
    Turni224 – 2285
    Helixi231 – 24111
    Beta strandi247 – 2504
    Helixi251 – 2533
    Helixi265 – 27410
    Helixi279 – 29214
    Helixi294 – 3018
    Helixi316 – 34934
    Helixi355 – 3617
    Helixi371 – 38212
    Helixi389 – 3913
    Helixi393 – 41624
    Helixi421 – 43313
    Helixi440 – 45112
    Beta strandi455 – 4573
    Beta strandi460 – 4656

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2JKVX-ray2.53A/B/C/D/E/F1-483[»]
    4GWGX-ray1.39A2-483[»]
    4GWKX-ray1.53A2-483[»]
    ProteinModelPortaliP52209.
    SMRiP52209. Positions 2-470.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP52209.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni129 – 1313Substrate bindingBy similarity
    Regioni187 – 1882Substrate bindingBy similarity

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0362.
    HOGENOMiHOG000255147.
    HOVERGENiHBG000029.
    InParanoidiP52209.
    KOiK00033.
    OMAiRTPERTK.
    PhylomeDBiP52209.
    TreeFamiTF300386.

    Family and domain databases

    Gene3Di1.10.1040.10. 1 hit.
    1.20.5.320. 1 hit.
    3.40.50.720. 1 hit.
    InterProiIPR008927. 6-PGluconate_DH_C-like.
    IPR006114. 6PGDH_C.
    IPR006113. 6PGDH_decarbox.
    IPR006115. 6PGDH_NADP-bd.
    IPR006184. 6PGdom_BS.
    IPR013328. DH_multihelical.
    IPR012284. Fibritin/6PGD_C-extension.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF00393. 6PGD. 1 hit.
    PF03446. NAD_binding_2. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000109. 6PGD. 1 hit.
    SUPFAMiSSF48179. SSF48179. 1 hit.
    TIGRFAMsiTIGR00873. gnd. 1 hit.
    PROSITEiPS00461. 6PGD. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P52209-1) [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

    MAQADIALIG LAVMGQNLIL NMNDHGFVVC AFNRTVSKVD DFLANEAKGT    50
    KVVGAQSLKE MVSKLKKPRR IILLVKAGQA VDDFIEKLVP LLDTGDIIID 100
    GGNSEYRDTT RRCRDLKAKG ILFVGSGVSG GEEGARYGPS LMPGGNKEAW 150
    PHIKTIFQGI AAKVGTGEPC CDWVGDEGAG HFVKMVHNGI EYGDMQLICE 200
    AYHLMKDVLG MAQDEMAQAF EDWNKTELDS FLIEITANIL KFQDTDGKHL 250
    LPKIRDSAGQ KGTGKWTAIS ALEYGVPVTL IGEAVFARCL SSLKDERIQA 300
    SKKLKGPQKF QFDGDKKSFL EDIRKALYAS KIISYAQGFM LLRQAATEFG 350
    WTLNYGGIAL MWRGGCIIRS VFLGKIKDAF DRNPELQNLL LDDFFKSAVE 400
    NCQDSWRRAV STGVQAGIPM PCFTTALSFY DGYRHEMLPA SLIQAQRDYF 450
    GAHTYELLAK PGQFIHTNWT GHGGTVSSSS YNA 483
    Length:483
    Mass (Da):53,140
    Last modified:January 23, 2007 - v3
    Checksum:i6CEFC0077D1283E3
    GO
    Isoform 2 (identifier: P52209-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-13: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:470
    Mass (Da):51,872
    Checksum:i9099E0CF2995B8AD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti118 – 1181A → G in AAA75302. (PubMed:8978909)Curated
    Sequence conflicti135 – 1351A → P in AAA75302. (PubMed:8978909)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti268 – 2681A → S.
    Corresponds to variant rs11547610 [ dbSNP | Ensembl ].
    VAR_048104

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 1313Missing in isoform 2. 1 PublicationVSP_055767Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U30255 mRNA. Translation: AAA75302.1.
    AK290404 mRNA. Translation: BAF83093.1.
    AK298830 mRNA. Translation: BAG60960.1.
    AL139424 Genomic DNA. Translation: CAI95751.1.
    CH471130 Genomic DNA. Translation: EAW71648.1.
    BC000368 mRNA. Translation: AAH00368.1.
    CCDSiCCDS113.1.
    PIRiG01922.
    RefSeqiNP_002622.2. NM_002631.2.
    UniGeneiHs.464071.

    Genome annotation databases

    EnsembliENST00000270776; ENSP00000270776; ENSG00000142657. [P52209-1]
    GeneIDi5226.
    KEGGihsa:5226.
    UCSCiuc001arc.3. human.

    Polymorphism databases

    DMDMi20981679.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U30255 mRNA. Translation: AAA75302.1 .
    AK290404 mRNA. Translation: BAF83093.1 .
    AK298830 mRNA. Translation: BAG60960.1 .
    AL139424 Genomic DNA. Translation: CAI95751.1 .
    CH471130 Genomic DNA. Translation: EAW71648.1 .
    BC000368 mRNA. Translation: AAH00368.1 .
    CCDSi CCDS113.1.
    PIRi G01922.
    RefSeqi NP_002622.2. NM_002631.2.
    UniGenei Hs.464071.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2JKV X-ray 2.53 A/B/C/D/E/F 1-483 [» ]
    4GWG X-ray 1.39 A 2-483 [» ]
    4GWK X-ray 1.53 A 2-483 [» ]
    ProteinModelPortali P52209.
    SMRi P52209. Positions 2-470.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111247. 36 interactions.
    IntActi P52209. 6 interactions.
    MINTi MINT-1415782.
    STRINGi 9606.ENSP00000270776.

    Chemistry

    BindingDBi P52209.
    ChEMBLi CHEMBL3404.
    DrugBanki DB00851. Dacarbazine.
    DB00695. Furosemide.
    DB00789. Gadopentetate dimeglumine.
    DB00920. Ketotifen.
    DB00814. Meloxicam.
    DB00563. Methotrexate.
    DB00867. Ritodrine.

    PTM databases

    PhosphoSitei P52209.

    Polymorphism databases

    DMDMi 20981679.

    Proteomic databases

    MaxQBi P52209.
    PaxDbi P52209.
    PeptideAtlasi P52209.
    PRIDEi P52209.

    Protocols and materials databases

    DNASUi 5226.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000270776 ; ENSP00000270776 ; ENSG00000142657 . [P52209-1 ]
    GeneIDi 5226.
    KEGGi hsa:5226.
    UCSCi uc001arc.3. human.

    Organism-specific databases

    CTDi 5226.
    GeneCardsi GC01P010458.
    HGNCi HGNC:8891. PGD.
    HPAi HPA031314.
    MIMi 172200. gene.
    neXtProti NX_P52209.
    PharmGKBi PA33229.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0362.
    HOGENOMi HOG000255147.
    HOVERGENi HBG000029.
    InParanoidi P52209.
    KOi K00033.
    OMAi RTPERTK.
    PhylomeDBi P52209.
    TreeFami TF300386.

    Enzyme and pathway databases

    UniPathwayi UPA00115 ; UER00410 .
    BioCyci MetaCyc:HS06949-MONOMER.
    Reactomei REACT_1859. Pentose phosphate pathway (hexose monophosphate shunt).
    SABIO-RK P52209.

    Miscellaneous databases

    ChiTaRSi PGD. human.
    EvolutionaryTracei P52209.
    GenomeRNAii 5226.
    NextBioi 20204.
    PROi P52209.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P52209.
    Bgeei P52209.
    CleanExi HS_PGD.
    Genevestigatori P52209.

    Family and domain databases

    Gene3Di 1.10.1040.10. 1 hit.
    1.20.5.320. 1 hit.
    3.40.50.720. 1 hit.
    InterProi IPR008927. 6-PGluconate_DH_C-like.
    IPR006114. 6PGDH_C.
    IPR006113. 6PGDH_decarbox.
    IPR006115. 6PGDH_NADP-bd.
    IPR006184. 6PGdom_BS.
    IPR013328. DH_multihelical.
    IPR012284. Fibritin/6PGD_C-extension.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    Pfami PF00393. 6PGD. 1 hit.
    PF03446. NAD_binding_2. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000109. 6PGD. 1 hit.
    SUPFAMi SSF48179. SSF48179. 1 hit.
    TIGRFAMsi TIGR00873. gnd. 1 hit.
    PROSITEi PS00461. 6PGD. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of a cDNA encoding 6-phosphogluconate dehydrogenase from a human heart cDNA library."
      Tsui S.K.W., Chan J.Y., Waye M.M.Y., Fung K.-P., Lee C.-Y.
      Biochem. Genet. 34:367-373(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Heart.
    2. "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] (ISOFORMS 1 AND 2).
      Tissue: Umbilical cord blood.
    3. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORM 1).
      Tissue: Lung.
    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-59 AND LYS-309, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "Structure of human phosphogluconate dehydrogenase in complex with NADPH at 2.53 A."
      Structural genomics consortium (SGC)
      Submitted (SEP-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.53 ANGSTROMS) IN COMPLEX WITH NADP, SUBUNIT.

    Entry informationi

    Entry namei6PGD_HUMAN
    AccessioniPrimary (citable) accession number: P52209
    Secondary accession number(s): A8K2Y9, B4DQJ8, Q9BWD8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 147 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 1
      Human chromosome 1: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3