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O60701

- UGDH_HUMAN

UniProt

O60701 - UGDH_HUMAN

Protein

UDP-glucose 6-dehydrogenase

Gene

UGDH

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 1 (01 Aug 1998)
      Previous versions | rss
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    Functioni

    Involved in the biosynthesis of glycosaminoglycans; hyaluronan, chondroitin sulfate, and heparan sulfate.

    Catalytic activityi

    UDP-glucose + 2 NAD+ + H2O = UDP-glucuronate + 2 NADH.

    Enzyme regulationi

    UDP-alpha-D-xylose (UDX) acts as a feedback inhibitor by activating an allosteric switch.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei36 – 361NAD1 Publication
    Binding sitei41 – 411NAD1 Publication
    Binding sitei165 – 1651NAD1 Publication
    Active sitei276 – 2761Nucleophile3 Publications
    Binding sitei346 – 3461NAD1 Publication
    Binding sitei442 – 4421Substrate

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi11 – 166NAD1 Publication
    Nucleotide bindingi89 – 935NAD1 Publication
    Nucleotide bindingi130 – 1312NAD1 Publication
    Nucleotide bindingi276 – 2794NAD1 Publication

    GO - Molecular functioni

    1. electron carrier activity Source: UniProtKB
    2. NAD binding Source: InterPro
    3. UDP-glucose 6-dehydrogenase activity Source: Reactome

    GO - Biological processi

    1. cellular glucuronidation Source: Reactome
    2. gastrulation with mouth forming second Source: Ensembl
    3. glycosaminoglycan biosynthetic process Source: ProtInc
    4. small molecule metabolic process Source: Reactome
    5. UDP-glucose metabolic process Source: ProtInc
    6. UDP-glucuronate biosynthetic process Source: Reactome
    7. xenobiotic metabolic process Source: Reactome

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    ReactomeiREACT_6737. Formation of the active cofactor, UDP-glucuronate.
    SABIO-RKO60701.
    UniPathwayiUPA00038; UER00491.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    UDP-glucose 6-dehydrogenase (EC:1.1.1.22)
    Short name:
    UDP-Glc dehydrogenase
    Short name:
    UDP-GlcDH
    Short name:
    UDPGDH
    Gene namesi
    Name:UGDH
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:12525. UGDH.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. nucleus Source: HPA

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA37170.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 494494UDP-glucose 6-dehydrogenasePRO_0000074060Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei107 – 1071N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiO60701.
    PaxDbiO60701.
    PeptideAtlasiO60701.
    PRIDEiO60701.

    2D gel databases

    REPRODUCTION-2DPAGEO60701.

    PTM databases

    PhosphoSiteiO60701.

    Expressioni

    Tissue specificityi

    Widely expressed.1 Publication

    Gene expression databases

    ArrayExpressiO60701.
    BgeeiO60701.
    CleanExiHS_UGDH.
    GenevestigatoriO60701.

    Organism-specific databases

    HPAiCAB034444.
    HPA036656.
    HPA036657.

    Interactioni

    Subunit structurei

    Homohexamer.3 Publications

    Protein-protein interaction databases

    BioGridi113205. 26 interactions.
    IntActiO60701. 6 interactions.
    MINTiMINT-5000810.
    STRINGi9606.ENSP00000319501.

    Structurei

    Secondary structure

    1
    494
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 105
    Helixi16 – 2611
    Beta strandi30 – 356
    Helixi39 – 457
    Beta strandi47 – 493
    Helixi57 – 648
    Turni66 – 683
    Beta strandi69 – 735
    Helixi75 – 817
    Beta strandi83 – 875
    Beta strandi95 – 973
    Turni98 – 1025
    Helixi107 – 11812
    Beta strandi122 – 1287
    Helixi136 – 14611
    Beta strandi153 – 1586
    Helixi168 – 1736
    Beta strandi178 – 1814
    Helixi186 – 19914
    Turni200 – 2023
    Helixi205 – 2073
    Beta strandi208 – 2114
    Helixi213 – 24432
    Helixi248 – 2569
    Turni259 – 2613
    Beta strandi263 – 2653
    Beta strandi274 – 2763
    Helixi277 – 29014
    Helixi294 – 32128
    Turni322 – 3243
    Beta strandi330 – 3345
    Beta strandi337 – 3393
    Helixi349 – 35911
    Beta strandi363 – 3675
    Beta strandi369 – 3713
    Helixi373 – 3808
    Helixi390 – 3945
    Beta strandi395 – 3973
    Helixi401 – 4055
    Beta strandi409 – 4135
    Helixi418 – 4225
    Helixi425 – 4317
    Beta strandi437 – 4426
    Turni444 – 4474
    Helixi449 – 4557
    Beta strandi458 – 4614

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2Q3EX-ray2.00A/B/C/D/E/F/G/H/I/J/K/L1-466[»]
    2QG4X-ray2.10A/B/C/D/E/F/G/H1-466[»]
    3ITKX-ray2.40A/B/C/D/E/F1-466[»]
    3KHUX-ray2.30A/B/C/D/E/F1-466[»]
    3PRJX-ray3.10A/B/C/D/E/F1-494[»]
    3PTZX-ray2.50A/B/C/D/E/F1-494[»]
    3TDKX-ray2.80A/B/C/D/E/F/G/H/I/J/K/L1-487[»]
    3TF5X-ray2.30A/B/C1-494[»]
    4EDFX-ray2.08A/B/C/D1-494[»]
    4QEJX-ray2.65A/B/C1-494[»]
    ProteinModelPortaliO60701.
    SMRiO60701. Positions 1-466.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO60701.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni161 – 1655Substrate binding
    Regioni220 – 2278Substrate binding
    Regioni260 – 27314Substrate bindingAdd
    BLAST
    Regioni338 – 3392Substrate binding

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1004.
    HOGENOMiHOG000153773.
    HOVERGENiHBG003512.
    InParanoidiO60701.
    KOiK00012.
    OMAiAIGRSTQ.
    OrthoDBiEOG7034GP.
    PhylomeDBiO60701.
    TreeFamiTF105671.

    Family and domain databases

    Gene3Di3.40.50.720. 2 hits.
    InterProiIPR008927. 6-PGluconate_DH_C-like.
    IPR016040. NAD(P)-bd_dom.
    IPR017476. UDP-Glc/GDP-Man.
    IPR014027. UDP-Glc/GDP-Man_DH_C.
    IPR014026. UDP-Glc/GDP-Man_DH_dimer.
    IPR001732. UDP-Glc/GDP-Man_DH_N.
    IPR028356. UDPglc_DH_euk.
    [Graphical view]
    PANTHERiPTHR11374. PTHR11374. 1 hit.
    PTHR11374:SF3. PTHR11374:SF3. 1 hit.
    PfamiPF00984. UDPG_MGDP_dh. 1 hit.
    PF03720. UDPG_MGDP_dh_C. 1 hit.
    PF03721. UDPG_MGDP_dh_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF500133. UDPglc_DH_euk. 1 hit.
    PIRSF000124. UDPglc_GDPman_dh. 1 hit.
    SMARTiSM00984. UDPG_MGDP_dh_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF48179. SSF48179. 1 hit.
    SSF52413. SSF52413. 1 hit.
    TIGRFAMsiTIGR03026. NDP-sugDHase. 1 hit.

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O60701-1) [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

    MFEIKKICCI GAGYVGGPTC SVIAHMCPEI RVTVVDVNES RINAWNSPTL    50
    PIYEPGLKEV VESCRGKNLF FSTNIDDAIK EADLVFISVN TPTKTYGMGK 100
    GRAADLKYIE ACARRIVQNS NGYKIVTEKS TVPVRAAESI RRIFDANTKP 150
    NLNLQVLSNP EFLAEGTAIK DLKNPDRVLI GGDETPEGQR AVQALCAVYE 200
    HWVPREKILT TNTWSSELSK LAANAFLAQR ISSINSISAL CEATGADVEE 250
    VATAIGMDQR IGNKFLKASV GFGGSCFQKD VLNLVYLCEA LNLPEVARYW 300
    QQVIDMNDYQ RRRFASRIID SLFNTVTDKK IAILGFAFKK DTGDTRESSS 350
    IYISKYLMDE GAHLHIYDPK VPREQIVVDL SHPGVSEDDQ VSRLVTISKD 400
    PYEACDGAHA VVICTEWDMF KELDYERIHK KMLKPAFIFD GRRVLDGLHN 450
    ELQTIGFQIE TIGKKVSSKR IPYAPSGEIP KFSLQDPPNK KPKV 494
    Length:494
    Mass (Da):55,024
    Last modified:August 1, 1998 - v1
    Checksum:i9C9DA5E1227D65CC
    GO
    Isoform 2 (identifier: O60701-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         89-155: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:427
    Mass (Da):47,603
    Checksum:iDC9E41480CA48E40
    GO
    Isoform 3 (identifier: O60701-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-97: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:397
    Mass (Da):44,415
    Checksum:i7CD01E38C0B0D6F5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti338 – 3381F → V in AAC05135. 1 PublicationCurated
    Sequence conflicti377 – 3771V → A in AAC05135. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 9797Missing in isoform 3. 1 PublicationVSP_046234Add
    BLAST
    Alternative sequencei89 – 15567Missing in isoform 2. 1 PublicationVSP_042550Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF061016 mRNA. Translation: AAC36095.1.
    AJ007702 mRNA. Translation: CAA07609.1.
    AJ272274
    , AJ272275, AJ272276, AJ272277, AJ272278, AJ272279, AJ272280, AJ272281 Genomic DNA. Translation: CAB75891.1.
    AK097930 mRNA. Translation: BAG53554.1.
    AK297737 mRNA. Translation: BAG60087.1.
    AC021148 Genomic DNA. No translation available.
    CH471069 Genomic DNA. Translation: EAW92937.1.
    BC022781 mRNA. Translation: AAH22781.1.
    AF049126 mRNA. Translation: AAC05135.1.
    CCDSiCCDS3455.1. [O60701-1]
    CCDS54757.1. [O60701-3]
    CCDS54758.1. [O60701-2]
    PIRiJE0353.
    RefSeqiNP_001171629.1. NM_001184700.1. [O60701-2]
    NP_001171630.1. NM_001184701.1. [O60701-3]
    NP_003350.1. NM_003359.3. [O60701-1]
    XP_006714092.1. XM_006714029.1. [O60701-1]
    UniGeneiHs.572518.

    Genome annotation databases

    EnsembliENST00000316423; ENSP00000319501; ENSG00000109814. [O60701-1]
    ENST00000501493; ENSP00000422909; ENSG00000109814. [O60701-2]
    ENST00000506179; ENSP00000421757; ENSG00000109814. [O60701-1]
    ENST00000507089; ENSP00000426560; ENSG00000109814. [O60701-3]
    GeneIDi7358.
    KEGGihsa:7358.
    UCSCiuc003guk.2. human. [O60701-1]
    uc003gul.2. human. [O60701-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF061016 mRNA. Translation: AAC36095.1 .
    AJ007702 mRNA. Translation: CAA07609.1 .
    AJ272274
    , AJ272275 , AJ272276 , AJ272277 , AJ272278 , AJ272279 , AJ272280 , AJ272281 Genomic DNA. Translation: CAB75891.1 .
    AK097930 mRNA. Translation: BAG53554.1 .
    AK297737 mRNA. Translation: BAG60087.1 .
    AC021148 Genomic DNA. No translation available.
    CH471069 Genomic DNA. Translation: EAW92937.1 .
    BC022781 mRNA. Translation: AAH22781.1 .
    AF049126 mRNA. Translation: AAC05135.1 .
    CCDSi CCDS3455.1. [O60701-1 ]
    CCDS54757.1. [O60701-3 ]
    CCDS54758.1. [O60701-2 ]
    PIRi JE0353.
    RefSeqi NP_001171629.1. NM_001184700.1. [O60701-2 ]
    NP_001171630.1. NM_001184701.1. [O60701-3 ]
    NP_003350.1. NM_003359.3. [O60701-1 ]
    XP_006714092.1. XM_006714029.1. [O60701-1 ]
    UniGenei Hs.572518.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2Q3E X-ray 2.00 A/B/C/D/E/F/G/H/I/J/K/L 1-466 [» ]
    2QG4 X-ray 2.10 A/B/C/D/E/F/G/H 1-466 [» ]
    3ITK X-ray 2.40 A/B/C/D/E/F 1-466 [» ]
    3KHU X-ray 2.30 A/B/C/D/E/F 1-466 [» ]
    3PRJ X-ray 3.10 A/B/C/D/E/F 1-494 [» ]
    3PTZ X-ray 2.50 A/B/C/D/E/F 1-494 [» ]
    3TDK X-ray 2.80 A/B/C/D/E/F/G/H/I/J/K/L 1-487 [» ]
    3TF5 X-ray 2.30 A/B/C 1-494 [» ]
    4EDF X-ray 2.08 A/B/C/D 1-494 [» ]
    4QEJ X-ray 2.65 A/B/C 1-494 [» ]
    ProteinModelPortali O60701.
    SMRi O60701. Positions 1-466.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113205. 26 interactions.
    IntActi O60701. 6 interactions.
    MINTi MINT-5000810.
    STRINGi 9606.ENSP00000319501.

    Chemistry

    DrugBanki DB00157. NADH.

    PTM databases

    PhosphoSitei O60701.

    2D gel databases

    REPRODUCTION-2DPAGE O60701.

    Proteomic databases

    MaxQBi O60701.
    PaxDbi O60701.
    PeptideAtlasi O60701.
    PRIDEi O60701.

    Protocols and materials databases

    DNASUi 7358.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000316423 ; ENSP00000319501 ; ENSG00000109814 . [O60701-1 ]
    ENST00000501493 ; ENSP00000422909 ; ENSG00000109814 . [O60701-2 ]
    ENST00000506179 ; ENSP00000421757 ; ENSG00000109814 . [O60701-1 ]
    ENST00000507089 ; ENSP00000426560 ; ENSG00000109814 . [O60701-3 ]
    GeneIDi 7358.
    KEGGi hsa:7358.
    UCSCi uc003guk.2. human. [O60701-1 ]
    uc003gul.2. human. [O60701-2 ]

    Organism-specific databases

    CTDi 7358.
    GeneCardsi GC04M039502.
    HGNCi HGNC:12525. UGDH.
    HPAi CAB034444.
    HPA036656.
    HPA036657.
    MIMi 603370. gene.
    neXtProti NX_O60701.
    PharmGKBi PA37170.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1004.
    HOGENOMi HOG000153773.
    HOVERGENi HBG003512.
    InParanoidi O60701.
    KOi K00012.
    OMAi AIGRSTQ.
    OrthoDBi EOG7034GP.
    PhylomeDBi O60701.
    TreeFami TF105671.

    Enzyme and pathway databases

    UniPathwayi UPA00038 ; UER00491 .
    Reactomei REACT_6737. Formation of the active cofactor, UDP-glucuronate.
    SABIO-RK O60701.

    Miscellaneous databases

    ChiTaRSi UGDH. human.
    EvolutionaryTracei O60701.
    GeneWikii UGDH.
    GenomeRNAii 7358.
    NextBioi 28812.
    PROi O60701.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O60701.
    Bgeei O60701.
    CleanExi HS_UGDH.
    Genevestigatori O60701.

    Family and domain databases

    Gene3Di 3.40.50.720. 2 hits.
    InterProi IPR008927. 6-PGluconate_DH_C-like.
    IPR016040. NAD(P)-bd_dom.
    IPR017476. UDP-Glc/GDP-Man.
    IPR014027. UDP-Glc/GDP-Man_DH_C.
    IPR014026. UDP-Glc/GDP-Man_DH_dimer.
    IPR001732. UDP-Glc/GDP-Man_DH_N.
    IPR028356. UDPglc_DH_euk.
    [Graphical view ]
    PANTHERi PTHR11374. PTHR11374. 1 hit.
    PTHR11374:SF3. PTHR11374:SF3. 1 hit.
    Pfami PF00984. UDPG_MGDP_dh. 1 hit.
    PF03720. UDPG_MGDP_dh_C. 1 hit.
    PF03721. UDPG_MGDP_dh_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF500133. UDPglc_DH_euk. 1 hit.
    PIRSF000124. UDPglc_GDPman_dh. 1 hit.
    SMARTi SM00984. UDPG_MGDP_dh_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48179. SSF48179. 1 hit.
    SSF52413. SSF52413. 1 hit.
    TIGRFAMsi TIGR03026. NDP-sugDHase. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and characterization of the human and mouse UDP-glucose dehydrogenase genes."
      Spicer A.P., Kaback L.A., Smith T.J., Seldin M.F.
      J. Biol. Chem. 273:25117-25124(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Placenta.
    2. "cDNA cloning and expression analysis of the human UDPglucose dehydrogenase."
      Peng H.L., Lou M.D., Chang M.L., Chang H.Y.
      Proc. Natl. Sci. Counc. Repub. China, B, Life Sci. 22:166-172(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: Liver.
    3. "Characterization of human gene encoding UDP-glucose dehydrogenase."
      Chang M.L., Chang H.Y., Peng H.L.
      Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "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 2 AND 3).
      Tissue: Thymus.
    5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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: Skin.
    8. Raghuram V., Foskett J.K.
      Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 214-388 (ISOFORM 1/2/3).
    9. "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-107, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Structural and kinetic evidence that catalytic reaction of human UDP-glucose 6-dehydrogenase involves covalent thiohemiacetal and thioester enzyme intermediates."
      Egger S., Chaikuad A., Klimacek M., Kavanagh K.L., Oppermann U., Nidetzky B.
      J. Biol. Chem. 287:2119-2129(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 1-466, ACTIVE SITE.
    13. "Conformational flexibility in the allosteric regulation of human UDP-alpha-D-glucose 6-dehydrogenase."
      Sennett N.C., Kadirvelraj R., Wood Z.A.
      Biochemistry 50:9651-9663(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), SUBUNIT, ENZYME REGULATION, ALLOSTERIC REGULATION.
    14. "Structure and mechanism of human UDP-glucose 6-dehydrogenase."
      Egger S., Chaikuad A., Kavanagh K.L., Oppermann U., Nidetzky B.
      J. Biol. Chem. 286:23877-23887(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-466 IN COMPLEX WITH NAD; UDP-GLUCOSE AND UDP-GLUCURONATE, SUBUNIT, ACTIVE SITE.
    15. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-487 IN COMPLEX WITH UDP-GLUCOSE, SUBUNIT, ACTIVE SITE.

    Entry informationi

    Entry nameiUGDH_HUMAN
    AccessioniPrimary (citable) accession number: O60701
    Secondary accession number(s): B3KUU2, B4DN25, O60589
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: August 1, 1998
    Last modified: October 1, 2014
    This is version 137 of the entry and version 1 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, Allosteric enzyme, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3