O60701 (UGDH_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	494 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing
Ligand	NAD
Molecular function	Oxidoreductase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Allosteric enzyme Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	UDP-glucose metabolic process Traceable author statement Ref.1. Source: ProtInc UDP-glucuronate biosynthetic process Traceable author statement. Source: Reactome gastrulation with mouth forming second Inferred from electronic annotation. Source: Compara glycosaminoglycan biosynthetic process Traceable author statement Ref.1. Source: ProtInc xenobiotic metabolic process Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome
Molecular_function	NAD binding Inferred from electronic annotation. Source: InterPro UDP-glucose 6-dehydrogenase activity Traceable author statement. Source: Reactome electron carrier activity Traceable author statement Ref.1. Source: UniProtKB
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 494

494

UDP-glucose 6-dehydrogenase

PRO_0000074060

Regions

Nucleotide binding

11 – 16

6

NAD

Nucleotide binding

89 – 93

5

NAD

Nucleotide binding

130 – 131

2

NAD

Nucleotide binding

276 – 279

4

NAD

Region

161 – 165

5

Substrate binding

Region

220 – 227

8

Substrate binding

Region

260 – 273

14

Substrate binding

Region

338 – 339

2

Substrate binding

Sites

Active site

276

1

Nucleophile Ref.12 Ref.14 Ref.15

Binding site

36

1

NAD

Binding site

41

1

NAD

Binding site

165

1

NAD

Binding site

346

1

NAD

Binding site

442

1

Substrate

Amino acid modifications

Modified residue

107

1

N6-acetyllysine Ref.9

Modified residue

473

1

Phosphotyrosine By similarity

Natural variations

Alternative sequence

1 – 97

97

Missing in isoform 3.

VSP_046234

Alternative sequence

89 – 155

67

Missing in isoform 2.

VSP_042550

Experimental info

Sequence conflict

338

1

F → V in AAC05135. Ref.8

Sequence conflict

377

1

V → A in AAC05135. Ref.8

Secondary structure

1

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494

Helix Strand Turn

Details...

Beta strand

6 – 10

5

Helix

16 – 26

11

Beta strand

30 – 35

6

Helix

39 – 45

7

Beta strand

47 – 49

3

Helix

57 – 64

8

Turn

66 – 68

3

Beta strand

69 – 73

5

Helix

75 – 81

7

Beta strand

83 – 87

5

Beta strand

95 – 97

3

Turn

98 – 102

5

Helix

107 – 118

12

Beta strand

122 – 128

7

Helix

136 – 146

11

Beta strand

153 – 158

6

Helix

168 – 173

6

Beta strand

178 – 181

4

Helix

186 – 199

14

Turn

200 – 202

3

Helix

205 – 207

3

Beta strand

208 – 211

4

Helix

213 – 244

32

Helix

248 – 256

9

Turn

259 – 261

3

Beta strand

263 – 265

3

Beta strand

274 – 276

3

Helix

277 – 290

14

Helix

294 – 321

28

Turn

322 – 324

3

Beta strand

330 – 334

5

Beta strand

337 – 339

3

Helix

349 – 359

11

Beta strand

363 – 367

5

Beta strand

369 – 371

3

Helix

373 – 380

8

Helix

390 – 394

5

Beta strand

395 – 397

3

Helix

401 – 405

5

Beta strand

409 – 413

5

Helix

418 – 422

5

Helix

425 – 431

7

Beta strand

437 – 442

6

Turn

444 – 447

4

Helix

449 – 455

7

Beta strand

458 – 461

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: 9C9DA5E1227D65CC	FASTA	494	55,024
	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
	Isoform 2 [UniParc]. Checksum: DC9E41480CA48E40	FASTA	427	47,603
	10 20 30 40 50 60 MFEIKKICCI GAGYVGGPTC SVIAHMCPEI RVTVVDVNES RINAWNSPTL PIYEPGLKEV 70 80 90 100 110 120 VESCRGKNLF FSTNIDDAIK EADLVFISVL SNPEFLAEGT AIKDLKNPDR VLIGGDETPE 130 140 150 160 170 180 GQRAVQALCA VYEHWVPREK ILTTNTWSSE LSKLAANAFL AQRISSINSI SALCEATGAD 190 200 210 220 230 240 VEEVATAIGM DQRIGNKFLK ASVGFGGSCF QKDVLNLVYL CEALNLPEVA RYWQQVIDMN 250 260 270 280 290 300 DYQRRRFASR IIDSLFNTVT DKKIAILGFA FKKDTGDTRE SSSIYISKYL MDEGAHLHIY 310 320 330 340 350 360 DPKVPREQIV VDLSHPGVSE DDQVSRLVTI SKDPYEACDG AHAVVICTEW DMFKELDYER 370 380 390 400 410 420 IHKKMLKPAF IFDGRRVLDG LHNELQTIGF QIETIGKKVS SKRIPYAPSG EIPKFSLQDP PNKKPKV
	Isoform 3 [UniParc]. Checksum: 7CD01E38C0B0D6F5	FASTA	397	44,415
	10 20 30 40 50 60 MGKGRAADLK YIEACARRIV QNSNGYKIVT EKSTVPVRAA ESIRRIFDAN TKPNLNLQVL 70 80 90 100 110 120 SNPEFLAEGT AIKDLKNPDR VLIGGDETPE GQRAVQALCA VYEHWVPREK ILTTNTWSSE 130 140 150 160 170 180 LSKLAANAFL AQRISSINSI SALCEATGAD VEEVATAIGM DQRIGNKFLK ASVGFGGSCF 190 200 210 220 230 240 QKDVLNLVYL CEALNLPEVA RYWQQVIDMN DYQRRRFASR IIDSLFNTVT DKKIAILGFA 250 260 270 280 290 300 FKKDTGDTRE SSSIYISKYL MDEGAHLHIY DPKVPREQIV VDLSHPGVSE DDQVSRLVTI 310 320 330 340 350 360 SKDPYEACDG AHAVVICTEW DMFKELDYER IHKKMLKPAF IFDGRRVLDG LHNELQTIGF 370 380 390 QIETIGKKVS SKRIPYAPSG EIPKFSLQDP PNKKPKV

References

	« Hide 'large scale' referencesShow '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. , 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]	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. , 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, MASS SPECTROMETRY.
[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, ALLOSTERICITY.
[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 , 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.

IPI

IPI00031420.
IPI00956601.
IPI00964927.

PIR

JE0353.

RefSeq

NP_001171629.1. NM_001184700.1.
NP_001171630.1. NM_001184701.1.
NP_003350.1. NM_003359.3.

UniGene

Hs.572518.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

O60701.

ModBase

Search...

Protein-protein interaction databases

IntAct

O60701. 6 interactions.

MINT

MINT-5000810.

STRING

9606.ENSP00000319501.

PTM databases

PhosphoSite

O60701.

2D gel databases

REPRODUCTION-2DPAGE

O60701.

Proteomic databases

PaxDb

O60701.

PeptideAtlas

O60701.

PRIDE

O60701.

Protocols and materials databases

DNASU

7358.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000316423; ENSP00000319501; ENSG00000109814.
ENST00000501493; ENSP00000422909; ENSG00000109814.
ENST00000506179; ENSP00000421757; ENSG00000109814.
ENST00000507089; ENSP00000426560; ENSG00000109814.

GeneID

7358.

KEGG

hsa:7358.

UCSC

uc003guk.2. human.

Organism-specific databases

CTD

7358.

GeneCards

GC04M039502.

HGNC

HGNC:12525. UGDH.

HPA

CAB034444.
HPA036656.
HPA036657.

MIM

603370. gene.

neXtProt

NX_O60701.

PharmGKB

PA37170.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1004.

HOGENOM

HOG000153773.

HOVERGEN

HBG003512.

InParanoid

O60701.

KO

K00012.

OMA

QMCPEIR.

OrthoDB

EOG4N30NS.

PhylomeDB

O60701.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.

SABIO-RK

O60701.

UniPathway

UPA00038; UER00491.

Gene expression databases

ArrayExpress

O60701.

Bgee

O60701.

CleanEx

HS_UGDH.

Genevestigator

O60701.

GermOnline

ENSG00000109814. Homo sapiens.

Family and domain databases

Gene3D

3.40.50.720. 2 hits.

InterPro

IPR008927. 6-PGluconate_DH_C-like.
IPR016040. NAD(P)-bd_dom.
IPR017476. Nucleotide_sugar_DH.
IPR014027. UDP-Glc/GDP-Man_DH_C.
IPR014026. UDP-Glc/GDP-Man_DH_dimer.
IPR001732. UDP-Glc/GDP-Man_DH_N.
[Graphical view]

Pfam

PF00984. UDPG_MGDP_dh. 1 hit.
PF03720. UDPG_MGDP_dh_C. 1 hit.
PF03721. UDPG_MGDP_dh_N. 1 hit.
[Graphical view]

PIRSF

PIRSF000124. UDPglc_GDPman_dh. 1 hit.

SMART

SM00984. UDPG_MGDP_dh_C. 1 hit.
[Graphical view]

SUPFAM

SSF48179. 6DGDH_C_like. 1 hit.
SSF52413. UDP-Glc/GDP-Man_DH_C. 1 hit.

TIGRFAMs

TIGR03026. NDP-sugDHase. 1 hit.

ProtoNet

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Other

ChiTaRS

UGDH. human.

DrugBank

DB00157. NADH.

EvolutionaryTrace

O60701.

GenomeRNAi

7358.

NextBio

28812.

SOURCE

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Entry information

Entry name

UGDH_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 121 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.