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P15428 (PGDH_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
15-hydroxyprostaglandin dehydrogenase [NAD(+)]

Short name=15-PGDH
EC=1.1.1.141
Alternative name(s):
Prostaglandin dehydrogenase 1
Gene names
Name:HPGD
Synonyms:PGDH1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length266 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Prostaglandin inactivation. Contributes to the regulation of events that are under the control of prostaglandin levels. Catalyzes the NAD-dependent dehydrogenation of lipoxin A4 to form 15-oxo-lipoxin A4. Inhibits in vivo proliferation of colon cancer cells. Ref.11 Ref.13 Ref.14

Catalytic activity

(5Z,13E,15S)-11-alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+ = (5Z,13E)-11-alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH.

Subunit structure

Homodimer.

Subcellular location

Cytoplasm.

Tissue specificity

Detected in colon epithelium (at protein level). Ref.13

Induction

Down-regulated by cortisol, dexamethasone and betamethasone. Down-regulated in colon cancer. Up-regulated by TGFB1. Ref.12 Ref.13

Involvement in disease

Hypertrophic osteoarthropathy, primary, autosomal recessive, 1 (PHOAR1) [MIM:259100]: A disease characterized by digital clubbing, periostosis, acroosteolysis, painful joint enlargement, and variable features of pachydermia that include thickened facial skin and a thickened scalp. Other developmental anomalies include delayed closure of the cranial sutures and congenital heart disease.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16

Cranioosteoarthropathy (COA) [MIM:259100]: A form of osteoarthropathy characterized by swelling of the joints, digital clubbing, hyperhidrosis, delayed closure of the fontanels, periostosis, and variable patent ductus arteriosus. Pachydermia is not a prominent feature.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16

Isolated congenital nail clubbing (ICNC) [MIM:119900]: A rare genodermatosis characterized by enlargement of the nail plate and terminal segments of the fingers and toes, resulting from proliferation of the connective tissues between the nail matrix and the distal phalanx. It is usually symmetrical and bilateral (in some cases unilateral). In nail clubbing usually the distal end of the nail matrix is relatively high compared to the proximal end, while the nail plate is complete but its dimensions and diameter more or less vary in comparison to normal. There may be different fingers and toes involved to varying degrees. Some fingers or toes are spared, but the thumbs are almost always involved.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.19

Sequence similarities

Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Biophysicochemical properties

Kinetic parameters:

KM=3.4 µM for prostaglandin E2 Ref.14

KM=38 µM for NAD

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
Prostaglandin metabolism
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Tumor suppressor
   LigandNAD
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processarachidonic acid metabolic process

Traceable author statement. Source: Reactome

cyclooxygenase pathway

Traceable author statement. Source: Reactome

ductus arteriosus closure

Inferred from sequence or structural similarity. Source: UniProtKB

female pregnancy

Inferred from direct assay PubMed 15531523. Source: UniProtKB

lipoxin metabolic process

Traceable author statement. Source: Reactome

lipoxygenase pathway

Traceable author statement PubMed 15581601. Source: UniProtKB

negative regulation of cell cycle

Inferred from direct assay Ref.13. Source: UniProtKB

ovulation

Inferred from sequence or structural similarity. Source: UniProtKB

parturition

Inferred from direct assay PubMed 15531523. Source: UniProtKB

prostaglandin metabolic process

Inferred from direct assay Ref.14. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

thrombin receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

transforming growth factor beta receptor signaling pathway

Inferred from direct assay Ref.13. Source: UniProtKB

   Cellular_componentbasolateral plasma membrane

Inferred from electronic annotation. Source: Ensembl

cytosol

Non-traceable author statement PubMed 15581601. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 23376485. Source: UniProt

   Molecular_function15-hydroxyprostaglandin dehydrogenase (NAD+) activity

Inferred from direct assay PubMed 10198228PubMed 15581601Ref.14Ref.10. Source: UniProtKB

NAD binding

Inferred from direct assay PubMed 10198228PubMed 15581601. Source: UniProtKB

NAD+ binding

Inferred from direct assay Ref.14. Source: UniProtKB

catalytic activity

Inferred from direct assay Ref.10. Source: UniProtKB

prostaglandin E receptor activity

Inferred from direct assay PubMed 10198228. Source: UniProtKB

protein homodimerization activity

Traceable author statement Ref.10. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P15428-1)

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: P15428-2)

The sequence of this isoform differs from the canonical sequence as follows:
     167-266: LAANLMNSGV...DTTPFQAKTQ → PTIDCQWIDNTH
Isoform 3 (identifier: P15428-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-121: Missing.
Isoform 4 (identifier: P15428-4)

The sequence of this isoform differs from the canonical sequence as follows:
     140-143: AGLM → AAHH
     144-266: Missing.
Isoform 5 (identifier: P15428-5)

The sequence of this isoform differs from the canonical sequence as follows:
     73-140: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 26626615-hydroxyprostaglandin dehydrogenase [NAD(+)]
PRO_0000054744

Regions

Nucleotide binding12 – 209NAD
Nucleotide binding36 – 372NAD
Nucleotide binding63 – 653NAD
Nucleotide binding151 – 1555NAD
Nucleotide binding186 – 1883NAD

Sites

Active site1511Proton acceptor
Binding site911NAD; via carbonyl oxygen
Binding site1381Substrate Probable
Binding site1481Substrate Probable

Natural variations

Alternative sequence1 – 121121Missing in isoform 3.
VSP_045106
Alternative sequence73 – 14068Missing in isoform 5.
VSP_045579
Alternative sequence140 – 1434AGLM → AAHH in isoform 4.
VSP_045107
Alternative sequence144 – 266123Missing in isoform 4.
VSP_045108
Alternative sequence167 – 266100LAANL…QAKTQ → PTIDCQWIDNTH in isoform 2.
VSP_043032
Natural variant1401A → P in COA; inactive. Ref.16
VAR_046209
Natural variant1931S → P in ICNC. Ref.19
VAR_060792
Natural variant2171Y → C.
VAR_006972

Experimental info

Mutagenesis1481Q → A: Loss of activity. Ref.14
Mutagenesis1481Q → E, H or N: Reduced affinity for NAD and prostaglandin E2. Ref.14
Mutagenesis1511Y → A: Loss of activity. Ref.10
Sequence conflict501D → H in AAA89175. Ref.2
Sequence conflict501D → H in AAA89174. Ref.2
Sequence conflict971E → K in CAA57843. Ref.3
Sequence conflict2191I → V in BAG61916. Ref.5

Secondary structure

............................................... 266
Helix Strand Turn

Details...

Sequences

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

Last modified April 1, 1990. Version 1.
Checksum: B860D2DE80E49514

FASTA26628,977
        10         20         30         40         50         60 
MHVNGKVALV TGAAQGIGRA FAEALLLKGA KVALVDWNLE AGVQCKAALD EQFEPQKTLF 

        70         80         90        100        110        120 
IQCDVADQQQ LRDTFRKVVD HFGRLDILVN NAGVNNEKNW EKTLQINLVS VISGTYLGLD 

       130        140        150        160        170        180 
YMSKQNGGEG GIIINMSSLA GLMPVAQQPV YCASKHGIVG FTRSAALAAN LMNSGVRLNA 

       190        200        210        220        230        240 
ICPGFVNTAI LESIEKEENM GQYIEYKDHI KDMIKYYGIL DPPLIANGLI TLIEDDALNG 

       250        260 
AIMKITTSKG IHFQDYDTTP FQAKTQ 

« Hide

Isoform 2 [UniParc].

Checksum: 685B577B3CA27EE3
Show »

FASTA17819,284
Isoform 3 [UniParc].

Checksum: 7113DD63B7540112
Show »

FASTA14515,696
Isoform 4 [UniParc].

Checksum: 67C9DD0CC7E3366C
Show »

FASTA14315,534
Isoform 5 [UniParc].

Checksum: 1D571F22D8738F64
Show »

FASTA19821,526

References

« Hide 'large scale' references
[1]"Purification and structural characterization of placental NAD(+)-linked 15-hydroxyprostaglandin dehydrogenase. The primary structure reveals the enzyme to belong to the short-chain alcohol dehydrogenase family."
Krook M., Marekov L., Joernvall H.
Biochemistry 29:738-743(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Placenta.
[2]"Cloning and sequence analysis of the cDNA for human placental NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase."
Ensor C.M., Yang J.Y., Okita R.T., Tai H.-H.
J. Biol. Chem. 265:14888-14891(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Placenta.
[3]"Sequence of a novel mRNA coding for a C-terminal-truncated form of human NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase."
Pichaud F., Frendo J.L., Delage-Mourroux R., de Vernejoul M.C., Moukhtar M.S., Jullienne A.
Gene 162:319-322(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Leukemia.
[4]"Cloning and sequencing of a new 15-hydroxyprostaglandin dehydrogenase related mRNA."
Delage-Mourroux R., Pichaud F., Frendo J.L., Pidoux E., Guliana J.M., Moukhtar M.S., Jullienne A.
Gene 188:143-148(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
[5]"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 1; 2; 3 AND 5).
Tissue: Colon, Placenta and Prostate.
[6]SeattleSNPs variation discovery resource
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]"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].
[8]Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"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: Pancreas.
[10]"Site-directed mutagenesis of the conserved tyrosine 151 of human placental NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase yields a catalytically inactive enzyme."
Ensor C.M., Tai H.-H.
Biochem. Biophys. Res. Commun. 176:840-845(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF TYR-151.
[11]"Oxidoreductases in lipoxin A4 metabolic inactivation: a novel role for 15-onoprostaglandin 13-reductase/leukotriene B4 12-hydroxydehydrogenase in inflammation."
Clish C.B., Levy B.D., Chiang N., Tai H.-H., Serhan C.N.
J. Biol. Chem. 275:25372-25380(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"Mechanism of cortisol/progesterone antagonism in the regulation of 15-hydroxyprostaglandin dehydrogenase activity and messenger ribonucleic acid levels in human chorion and placental trophoblast cells at term."
Patel F.A., Funder J.W., Challis J.R.G.
J. Clin. Endocrinol. Metab. 88:2922-2933(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[13]"15-Hydroxyprostaglandin dehydrogenase, a COX-2 oncogene antagonist, is a TGF-beta-induced suppressor of human gastrointestinal cancers."
Yan M., Rerko R.M., Platzer P., Dawson D., Willis J., Tong M., Lawrence E., Lutterbaugh J., Lu S., Willson J.K.V., Luo G., Hensold J., Tai H.-H., Wilson K., Markowitz S.D.
Proc. Natl. Acad. Sci. U.S.A. 101:17468-17473(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION, TISSUE SPECIFICITY.
[14]"Role of glutamine 148 of human 15-hydroxyprostaglandin dehydrogenase in catalytic oxidation of prostaglandin E2."
Cho H., Huang L., Hamza A., Gao D., Zhan C.-G., Tai H.-H.
Bioorg. Med. Chem. 14:6486-6491(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF GLN-148, BIOPHYSICOCHEMICAL PROPERTIES, 3D-STRUCTURE MODELING.
[15]"Three-dimensional model of NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase and relationships to the NADP(+)-dependent enzyme (carbonyl reductase)."
Krook M., Ghosh D., Duax W.L., Joernvall H.
FEBS Lett. 322:139-142(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING.
[16]"Mutations in 15-hydroxyprostaglandin dehydrogenase cause primary hypertrophic osteoarthropathy."
Uppal S., Diggle C.P., Carr I.M., Fishwick C.W.G., Ahmed M., Ibrahim G.H., Helliwell P.S., Latos-Bielenska A., Phillips S.E.V., Markham A.F., Bennett C.P., Bonthron D.T.
Nat. Genet. 40:789-793(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN PHOAR1, VARIANT COA PRO-140, CHARACTERIZATION OF VARIANT COA PRO-140.
[17]Erratum
Uppal S., Diggle C.P., Carr I.M., Fishwick C.W.G., Ahmed M., Ibrahim G.H., Helliwell P.S., Latos-Bielenska A., Phillips S.E.V., Markham A.F., Bennett C.P., Bonthron D.T.
Nat. Genet. 40:927-927(2008)
[18]"High-affinity inhibitors of human NAD-dependent 15-hydroxyprostaglandin dehydrogenase: mechanisms of inhibition and structure-activity relationships."
Niesen F.H., Schultz L., Jadhav A., Bhatia C., Guo K., Maloney D.J., Pilka E.S., Wang M., Oppermann U., Heightman T.D., Simeonov A.
PLoS ONE 5:E13719-E13719(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 3-256 IN COMPLEX WITH NAD.
[19]"Mutation in the HPGD gene encoding NAD+ dependent 15-hydroxyprostaglandin dehydrogenase underlies isolated congenital nail clubbing (ICNC)."
Tariq M., Azeem Z., Ali G., Chishti M.S., Ahmad W.
J. Med. Genet. 46:14-20(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ICNC PRO-193.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L76465 mRNA. Translation: AAA89175.1.
J05594 mRNA. Translation: AAA89174.1.
X82460 mRNA. Translation: CAA57843.1.
U63296 mRNA. Translation: AAB53034.1.
AK296642 mRNA. Translation: BAH12408.1.
AK300125 mRNA. Translation: BAG61916.1.
AK300524 mRNA. Translation: BAG62236.1.
AK300940 mRNA. Translation: BAG62569.1.
AK314624 mRNA. Translation: BAG37190.1.
DQ903072 Genomic DNA. Translation: ABI75347.1.
AC096751 Genomic DNA. No translation available.
CH471056 Genomic DNA. Translation: EAX04734.1.
CH471056 Genomic DNA. Translation: EAX04735.1.
CH471056 Genomic DNA. Translation: EAX04736.1.
CH471056 Genomic DNA. Translation: EAX04737.1.
BC018986 mRNA. Translation: AAH18986.1.
CCDSCCDS3821.1. [P15428-1]
CCDS54821.1. [P15428-2]
CCDS58933.1. [P15428-3]
CCDS58934.1. [P15428-5]
CCDS58935.1. [P15428-4]
PIRA35802.
RefSeqNP_000851.2. NM_000860.5. [P15428-1]
NP_001139288.1. NM_001145816.2. [P15428-2]
NP_001243230.1. NM_001256301.1. [P15428-3]
NP_001243234.1. NM_001256305.1. [P15428-4]
NP_001243235.1. NM_001256306.1. [P15428-5]
NP_001243236.1. NM_001256307.1. [P15428-3]
UniGeneHs.596913.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2GDZX-ray1.65A3-256[»]
ProteinModelPortalP15428.
SMRP15428. Positions 3-258.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109485. 1 interaction.
STRING9606.ENSP00000296522.

Chemistry

BindingDBP15428.
ChEMBLCHEMBL1293255.
DrugBankDB00157. NADH.

PTM databases

PhosphoSiteP15428.

Polymorphism databases

DMDM129889.

2D gel databases

SWISS-2DPAGEP15428.

Proteomic databases

MaxQBP15428.
PaxDbP15428.
PRIDEP15428.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000296521; ENSP00000296521; ENSG00000164120. [P15428-2]
ENST00000296522; ENSP00000296522; ENSG00000164120. [P15428-1]
ENST00000422112; ENSP00000398720; ENSG00000164120. [P15428-5]
ENST00000510901; ENSP00000422418; ENSG00000164120. [P15428-3]
ENST00000541923; ENSP00000438017; ENSG00000164120. [P15428-3]
ENST00000542498; ENSP00000443644; ENSG00000164120. [P15428-4]
GeneID3248.
KEGGhsa:3248.
UCSCuc003itu.3. human. [P15428-1]
uc003itv.3. human. [P15428-2]
uc010irq.3. human.

Organism-specific databases

CTD3248.
GeneCardsGC04M175411.
HGNCHGNC:5154. HPGD.
HPAHPA004919.
HPA005679.
MIM119900. phenotype.
259100. phenotype.
601688. gene.
neXtProtNX_P15428.
Orphanet1525. Cranio-osteoarthropathy.
217059. Isolated congenital digital clubbing.
2796. Pachydermoperiostosis.
PharmGKBPA29424.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1028.
HOGENOMHOG000070121.
HOVERGENHBG107379.
InParanoidP15428.
KOK00069.
OMAIHFQNYD.
OrthoDBEOG7966HT.
PhylomeDBP15428.
TreeFamTF324093.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
SABIO-RKP15428.

Gene expression databases

ArrayExpressP15428.
BgeeP15428.
CleanExHS_HPGD.
GenevestigatorP15428.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]
PfamPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSPR00081. GDHRDH.
PR00080. SDRFAMILY.
PROSITEPS00061. ADH_SHORT. 1 hit.
[Graphical view]
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Other

ChiTaRSHPGD. human.
EvolutionaryTraceP15428.
GeneWikiHPGD.
GenomeRNAi3248.
NextBio12913.
PROP15428.
SOURCESearch...

Entry information

Entry namePGDH_HUMAN
AccessionPrimary (citable) accession number: P15428
Secondary accession number(s): B4DTA4 expand/collapse secondary AC list , B4DU74, B4DV57, D3DP43, E7EV11, O00749, Q06F08, Q12998
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: July 9, 2014
This is version 151 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

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

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