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O60701 (UGDH_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
UDP-glucose 6-dehydrogenase

Short name=UDP-Glc dehydrogenase
Short name=UDP-GlcDH
Short name=UDPGDH
EC=1.1.1.22
Gene names
Name:UGDH
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length494 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Enzyme regulation

UDP-alpha-D-xylose (UDX) acts as a feedback inhibitor by activating an allosteric switch. Ref.13

Pathway

Nucleotide-sugar biosynthesis; UDP-alpha-D-glucuronate biosynthesis; UDP-alpha-D-glucuronate from UDP-alpha-D-glucose: step 1/1.

Subunit structure

Homohexamer. Ref.13 Ref.14 Ref.15

Tissue specificity

Widely expressed. Ref.2

Sequence similarities

Belongs to the UDP-glucose/GDP-mannose dehydrogenase family.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O60701-1)

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.
Isoform 2 (identifier: O60701-2)

The sequence of this isoform differs from the canonical sequence as follows:
     89-155: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: O60701-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-97: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 494494UDP-glucose 6-dehydrogenase
PRO_0000074060

Regions

Nucleotide binding11 – 166NAD
Nucleotide binding89 – 935NAD
Nucleotide binding130 – 1312NAD
Nucleotide binding276 – 2794NAD
Region161 – 1655Substrate binding
Region220 – 2278Substrate binding
Region260 – 27314Substrate binding
Region338 – 3392Substrate binding

Sites

Active site2761Nucleophile Ref.12 Ref.14 Ref.15
Binding site361NAD
Binding site411NAD
Binding site1651NAD
Binding site3461NAD
Binding site4421Substrate

Amino acid modifications

Modified residue1071N6-acetyllysine Ref.9

Natural variations

Alternative sequence1 – 9797Missing in isoform 3.
VSP_046234
Alternative sequence89 – 15567Missing in isoform 2.
VSP_042550

Experimental info

Sequence conflict3381F → V in AAC05135. Ref.8
Sequence conflict3771V → A in AAC05135. Ref.8

Secondary structure

...................................................................................... 494
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 9C9DA5E1227D65CC

FASTA49455,024
        10         20         30         40         50         60 
MFEIKKICCI GAGYVGGPTC SVIAHMCPEI RVTVVDVNES RINAWNSPTL PIYEPGLKEV 

        70         80         90        100        110        120 
VESCRGKNLF FSTNIDDAIK EADLVFISVN TPTKTYGMGK GRAADLKYIE ACARRIVQNS 

       130        140        150        160        170        180 
NGYKIVTEKS TVPVRAAESI RRIFDANTKP NLNLQVLSNP EFLAEGTAIK DLKNPDRVLI 

       190        200        210        220        230        240 
GGDETPEGQR AVQALCAVYE HWVPREKILT TNTWSSELSK LAANAFLAQR ISSINSISAL 

       250        260        270        280        290        300 
CEATGADVEE VATAIGMDQR IGNKFLKASV GFGGSCFQKD VLNLVYLCEA LNLPEVARYW 

       310        320        330        340        350        360 
QQVIDMNDYQ RRRFASRIID SLFNTVTDKK IAILGFAFKK DTGDTRESSS IYISKYLMDE 

       370        380        390        400        410        420 
GAHLHIYDPK VPREQIVVDL SHPGVSEDDQ VSRLVTISKD PYEACDGAHA VVICTEWDMF 

       430        440        450        460        470        480 
KELDYERIHK KMLKPAFIFD GRRVLDGLHN ELQTIGFQIE TIGKKVSSKR IPYAPSGEIP 

       490 
KFSLQDPPNK KPKV 

« Hide

Isoform 2 [UniParc].

Checksum: DC9E41480CA48E40
Show »

FASTA42747,603
Isoform 3 [UniParc].

Checksum: 7CD01E38C0B0D6F5
Show »

FASTA39744,415

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"Structural basis of cooperativity in human UDP-glucose dehydrogenase."
Rajakannan V., Lee H.S., Chong S.H., Ryu H.B., Bae J.Y., Whang E.Y., Huh J.W., Cho S.W., Kang L.W., Choe H., Robinson R.C.
PLoS ONE 6:E25226-E25226(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-487 IN COMPLEX WITH UDP-GLUCOSE, SUBUNIT, ACTIVE SITE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF061016 mRNA. Translation: AAC36095.1.
AJ007702 mRNA. Translation: CAA07609.1.
AJ272274 expand/collapse EMBL AC list , 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.
CCDSCCDS3455.1. [O60701-1]
CCDS54757.1. [O60701-3]
CCDS54758.1. [O60701-2]
PIRJE0353.
RefSeqNP_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]
UniGeneHs.572518.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalO60701.
SMRO60701. Positions 1-466.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113205. 26 interactions.
IntActO60701. 6 interactions.
MINTMINT-5000810.
STRING9606.ENSP00000319501.

Chemistry

DrugBankDB00157. NADH.

PTM databases

PhosphoSiteO60701.

2D gel databases

REPRODUCTION-2DPAGEO60701.

Proteomic databases

MaxQBO60701.
PaxDbO60701.
PeptideAtlasO60701.
PRIDEO60701.

Protocols and materials databases

DNASU7358.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000316423; ENSP00000319501; ENSG00000109814. [O60701-1]
ENST00000501493; ENSP00000422909; ENSG00000109814. [O60701-2]
ENST00000506179; ENSP00000421757; ENSG00000109814. [O60701-1]
ENST00000507089; ENSP00000426560; ENSG00000109814. [O60701-3]
GeneID7358.
KEGGhsa:7358.
UCSCuc003guk.2. human. [O60701-1]
uc003gul.2. human. [O60701-2]

Organism-specific databases

CTD7358.
GeneCardsGC04M039502.
HGNCHGNC:12525. UGDH.
HPACAB034444.
HPA036656.
HPA036657.
MIM603370. gene.
neXtProtNX_O60701.
PharmGKBPA37170.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1004.
HOGENOMHOG000153773.
HOVERGENHBG003512.
InParanoidO60701.
KOK00012.
OMAAIGRSTQ.
OrthoDBEOG7034GP.
PhylomeDBO60701.
TreeFamTF105671.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
SABIO-RKO60701.
UniPathwayUPA00038; UER00491.

Gene expression databases

ArrayExpressO60701.
BgeeO60701.
CleanExHS_UGDH.
GenevestigatorO60701.

Family and domain databases

Gene3D3.40.50.720. 2 hits.
InterProIPR008927. 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]
PANTHERPTHR11374. PTHR11374. 1 hit.
PTHR11374:SF3. PTHR11374:SF3. 1 hit.
PfamPF00984. UDPG_MGDP_dh. 1 hit.
PF03720. UDPG_MGDP_dh_C. 1 hit.
PF03721. UDPG_MGDP_dh_N. 1 hit.
[Graphical view]
PIRSFPIRSF500133. UDPglc_DH_euk. 1 hit.
PIRSF000124. UDPglc_GDPman_dh. 1 hit.
SMARTSM00984. UDPG_MGDP_dh_C. 1 hit.
[Graphical view]
SUPFAMSSF48179. SSF48179. 1 hit.
SSF52413. SSF52413. 1 hit.
TIGRFAMsTIGR03026. NDP-sugDHase. 1 hit.
ProtoNetSearch...

Other

ChiTaRSUGDH. human.
EvolutionaryTraceO60701.
GeneWikiUGDH.
GenomeRNAi7358.
NextBio28812.
PROO60701.
SOURCESearch...

Entry information

Entry nameUGDH_HUMAN
AccessionPrimary (citable) accession number: O60701
Secondary accession number(s): B3KUU2, B4DN25, O60589
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: August 1, 1998
Last modified: July 9, 2014
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM