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O60701

- UGDH_HUMAN

UniProt

O60701 - UGDH_HUMAN

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Protein

UDP-glucose 6-dehydrogenase

Gene

UGDH

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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. extracellular vesicular exosome Source: UniProtKB
  3. nucleus Source: HPA
Complete GO annotation...

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

BgeeiO60701.
CleanExiHS_UGDH.
ExpressionAtlasiO60701. baseline and differential.
GenevestigatoriO60701.

Organism-specific databases

HPAiCAB034444.
HPA036656.
HPA036657.

Interactioni

Subunit structurei

Homohexamer.3 Publications

Protein-protein interaction databases

BioGridi113205. 32 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 – 105Combined sources
Helixi16 – 2611Combined sources
Beta strandi30 – 356Combined sources
Helixi39 – 457Combined sources
Beta strandi47 – 493Combined sources
Helixi57 – 648Combined sources
Turni66 – 683Combined sources
Beta strandi69 – 735Combined sources
Helixi75 – 817Combined sources
Beta strandi83 – 875Combined sources
Beta strandi95 – 973Combined sources
Turni98 – 1025Combined sources
Helixi107 – 11812Combined sources
Beta strandi122 – 1287Combined sources
Helixi136 – 14611Combined sources
Beta strandi153 – 1586Combined sources
Helixi168 – 1736Combined sources
Beta strandi178 – 1814Combined sources
Helixi186 – 19914Combined sources
Turni200 – 2023Combined sources
Helixi205 – 2073Combined sources
Beta strandi208 – 2114Combined sources
Helixi213 – 24432Combined sources
Helixi248 – 2569Combined sources
Turni259 – 2613Combined sources
Beta strandi263 – 2653Combined sources
Beta strandi274 – 2763Combined sources
Helixi277 – 29014Combined sources
Helixi294 – 32128Combined sources
Turni322 – 3243Combined sources
Beta strandi330 – 3345Combined sources
Beta strandi337 – 3393Combined sources
Helixi349 – 35911Combined sources
Beta strandi363 – 3675Combined sources
Beta strandi369 – 3713Combined sources
Helixi373 – 3808Combined sources
Helixi390 – 3945Combined sources
Beta strandi395 – 3973Combined sources
Helixi401 – 4055Combined sources
Beta strandi409 – 4135Combined sources
Helixi418 – 4225Combined sources
Helixi425 – 4317Combined sources
Beta strandi437 – 4426Combined sources
Turni444 – 4474Combined sources
Helixi449 – 4557Combined sources
Beta strandi458 – 4614Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000015355.
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

        10         20         30         40         50
MFEIKKICCI GAGYVGGPTC SVIAHMCPEI RVTVVDVNES RINAWNSPTL
60 70 80 90 100
PIYEPGLKEV VESCRGKNLF FSTNIDDAIK EADLVFISVN TPTKTYGMGK
110 120 130 140 150
GRAADLKYIE ACARRIVQNS NGYKIVTEKS TVPVRAAESI RRIFDANTKP
160 170 180 190 200
NLNLQVLSNP EFLAEGTAIK DLKNPDRVLI GGDETPEGQR AVQALCAVYE
210 220 230 240 250
HWVPREKILT TNTWSSELSK LAANAFLAQR ISSINSISAL CEATGADVEE
260 270 280 290 300
VATAIGMDQR IGNKFLKASV GFGGSCFQKD VLNLVYLCEA LNLPEVARYW
310 320 330 340 350
QQVIDMNDYQ RRRFASRIID SLFNTVTDKK IAILGFAFKK DTGDTRESSS
360 370 380 390 400
IYISKYLMDE GAHLHIYDPK VPREQIVVDL SHPGVSEDDQ VSRLVTISKD
410 420 430 440 450
PYEACDGAHA VVICTEWDMF KELDYERIHK KMLKPAFIFD GRRVLDGLHN
460 470 480 490
ELQTIGFQIE TIGKKVSSKR IPYAPSGEIP KFSLQDPPNK KPKV
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 32 interactions.
IntActi O60701. 6 interactions.
MINTi MINT-5000810.
STRINGi 9606.ENSP00000319501.

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.
GeneTreei ENSGT00390000015355.
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

Bgeei O60701.
CleanExi HS_UGDH.
ExpressionAtlasi O60701. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 139 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