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P15428

- PGDH_HUMAN

UniProt

P15428 - PGDH_HUMAN

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Protein

15-hydroxyprostaglandin dehydrogenase [NAD(+)]

Gene

HPGD

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

Functioni

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.3 Publications

Catalytic activityi

(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.

Kineticsi

  1. KM=3.4 µM for prostaglandin E21 Publication
  2. KM=38 µM for NAD1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei91 – 911NAD; via carbonyl oxygen1 Publication
Binding sitei138 – 1381SubstrateCurated
Binding sitei148 – 1481SubstrateCurated
Active sitei151 – 1511Proton acceptor

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi12 – 209NAD1 Publication
Nucleotide bindingi36 – 372NAD1 Publication
Nucleotide bindingi63 – 653NAD1 Publication
Nucleotide bindingi151 – 1555NAD1 Publication
Nucleotide bindingi186 – 1883NAD1 Publication

GO - Molecular functioni

  1. 15-hydroxyprostaglandin dehydrogenase (NAD+) activity Source: UniProtKB
  2. catalytic activity Source: UniProtKB
  3. NAD+ binding Source: UniProtKB
  4. NAD binding Source: UniProtKB
  5. prostaglandin E receptor activity Source: UniProtKB
  6. protein homodimerization activity Source: UniProtKB

GO - Biological processi

  1. arachidonic acid metabolic process Source: Reactome
  2. cyclooxygenase pathway Source: Reactome
  3. ductus arteriosus closure Source: UniProtKB
  4. female pregnancy Source: UniProtKB
  5. lipoxin metabolic process Source: Reactome
  6. lipoxygenase pathway Source: UniProtKB
  7. negative regulation of cell cycle Source: UniProtKB
  8. ovulation Source: UniProtKB
  9. parturition Source: UniProtKB
  10. prostaglandin metabolic process Source: UniProtKB
  11. small molecule metabolic process Source: Reactome
  12. thrombin receptor signaling pathway Source: UniProtKB
  13. transforming growth factor beta receptor signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism, Prostaglandin metabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

ReactomeiREACT_150149. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
REACT_150320. Synthesis of Lipoxins (LX).
SABIO-RKP15428.

Names & Taxonomyi

Protein namesi
Recommended name:
15-hydroxyprostaglandin dehydrogenase [NAD(+)] (EC:1.1.1.141)
Short name:
15-PGDH
Alternative name(s):
Prostaglandin dehydrogenase 1
Gene namesi
Name:HPGD
Synonyms:PGDH1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:5154. HPGD.

Subcellular locationi

GO - Cellular componenti

  1. basolateral plasma membrane Source: Ensembl
  2. cytosol Source: UniProtKB
  3. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti140 – 1401A → P in COA; inactive. 1 Publication
VAR_046209
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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti193 – 1931S → P in ICNC. 1 Publication
VAR_060792

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi148 – 1481Q → A: Loss of activity. 1 Publication
Mutagenesisi148 – 1481Q → E, H or N: Reduced affinity for NAD and prostaglandin E2. 1 Publication
Mutagenesisi151 – 1511Y → A: Loss of activity. 1 Publication

Keywords - Diseasei

Disease mutation, Tumor suppressor

Organism-specific databases

MIMi119900. phenotype.
259100. phenotype.
Orphaneti1525. Cranio-osteoarthropathy.
217059. Isolated congenital digital clubbing.
2796. Pachydermoperiostosis.
PharmGKBiPA29424.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 26626615-hydroxyprostaglandin dehydrogenase [NAD(+)]PRO_0000054744Add
BLAST

Proteomic databases

MaxQBiP15428.
PaxDbiP15428.
PRIDEiP15428.

2D gel databases

SWISS-2DPAGEP15428.

PTM databases

PhosphoSiteiP15428.

Expressioni

Tissue specificityi

Detected in colon epithelium (at protein level).1 Publication

Inductioni

Down-regulated by cortisol, dexamethasone and betamethasone. Down-regulated in colon cancer. Up-regulated by TGFB1.2 Publications

Gene expression databases

BgeeiP15428.
CleanExiHS_HPGD.
ExpressionAtlasiP15428. baseline and differential.
GenevestigatoriP15428.

Organism-specific databases

HPAiHPA004919.
HPA005679.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi109485. 1 interaction.
STRINGi9606.ENSP00000296522.

Structurei

Secondary structure

1
266
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 115
Turni12 – 143
Helixi16 – 2712
Beta strandi31 – 377
Helixi39 – 4911
Turni50 – 523
Helixi55 – 573
Beta strandi58 – 625
Helixi68 – 8215
Beta strandi87 – 904
Beta strandi97 – 993
Helixi100 – 1078
Helixi109 – 12214
Helixi124 – 1263
Beta strandi131 – 1366
Helixi139 – 1413
Helixi149 – 17224
Beta strandi176 – 1849
Beta strandi186 – 1883
Helixi189 – 1924
Helixi193 – 1953
Helixi197 – 2004
Helixi201 – 2066
Helixi207 – 21711
Helixi222 – 23413
Beta strandi242 – 2465
Turni247 – 2493
Beta strandi250 – 2534

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GDZX-ray1.65A3-256[»]
ProteinModelPortaliP15428.
SMRiP15428. Positions 3-258.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15428.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1028.
GeneTreeiENSGT00760000118868.
HOGENOMiHOG000070121.
HOVERGENiHBG107379.
InParanoidiP15428.
KOiK00069.
OMAiIHFQNYD.
OrthoDBiEOG7966HT.
PhylomeDBiP15428.
TreeFamiTF324093.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]
PfamiPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
PROSITEiPS00061. ADH_SHORT. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P15428-1) [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
MHVNGKVALV TGAAQGIGRA FAEALLLKGA KVALVDWNLE AGVQCKAALD
60 70 80 90 100
EQFEPQKTLF IQCDVADQQQ LRDTFRKVVD HFGRLDILVN NAGVNNEKNW
110 120 130 140 150
EKTLQINLVS VISGTYLGLD YMSKQNGGEG GIIINMSSLA GLMPVAQQPV
160 170 180 190 200
YCASKHGIVG FTRSAALAAN LMNSGVRLNA ICPGFVNTAI LESIEKEENM
210 220 230 240 250
GQYIEYKDHI KDMIKYYGIL DPPLIANGLI TLIEDDALNG AIMKITTSKG
260
IHFQDYDTTP FQAKTQ
Length:266
Mass (Da):28,977
Last modified:April 1, 1990 - v1
Checksum:iB860D2DE80E49514
GO
Isoform 2 (identifier: P15428-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     167-266: LAANLMNSGV...DTTPFQAKTQ → PTIDCQWIDNTH

Show »
Length:178
Mass (Da):19,284
Checksum:i685B577B3CA27EE3
GO
Isoform 3 (identifier: P15428-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-121: Missing.

Show »
Length:145
Mass (Da):15,696
Checksum:i7113DD63B7540112
GO
Isoform 4 (identifier: P15428-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     140-143: AGLM → AAHH
     144-266: Missing.

Show »
Length:143
Mass (Da):15,534
Checksum:i67C9DD0CC7E3366C
GO
Isoform 5 (identifier: P15428-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     73-140: Missing.

Note: No experimental confirmation available.

Show »
Length:198
Mass (Da):21,526
Checksum:i1D571F22D8738F64
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti50 – 501D → H in AAA89175. (PubMed:1697582)Curated
Sequence conflicti50 – 501D → H in AAA89174. (PubMed:1697582)Curated
Sequence conflicti97 – 971E → K in CAA57843. (PubMed:7557451)Curated
Sequence conflicti219 – 2191I → V in BAG61916. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti140 – 1401A → P in COA; inactive. 1 Publication
VAR_046209
Natural varianti193 – 1931S → P in ICNC. 1 Publication
VAR_060792
Natural varianti217 – 2171Y → C.
VAR_006972

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 121121Missing in isoform 3. 1 PublicationVSP_045106Add
BLAST
Alternative sequencei73 – 14068Missing in isoform 5. 1 PublicationVSP_045579Add
BLAST
Alternative sequencei140 – 1434AGLM → AAHH in isoform 4. 1 PublicationVSP_045107
Alternative sequencei144 – 266123Missing in isoform 4. 1 PublicationVSP_045108Add
BLAST
Alternative sequencei167 – 266100LAANL…QAKTQ → PTIDCQWIDNTH in isoform 2. 2 PublicationsVSP_043032Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS3821.1. [P15428-1]
CCDS54821.1. [P15428-2]
CCDS58933.1. [P15428-3]
CCDS58934.1. [P15428-5]
CCDS58935.1. [P15428-4]
PIRiA35802.
RefSeqiNP_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]
UniGeneiHs.596913.

Genome annotation databases

EnsembliENST00000296521; 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]
GeneIDi3248.
KEGGihsa:3248.
UCSCiuc003itu.3. human. [P15428-1]
uc003itv.3. human. [P15428-2]
uc010irq.3. human.

Polymorphism databases

DMDMi129889.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

SeattleSNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS3821.1. [P15428-1 ]
CCDS54821.1. [P15428-2 ]
CCDS58933.1. [P15428-3 ]
CCDS58934.1. [P15428-5 ]
CCDS58935.1. [P15428-4 ]
PIRi A35802.
RefSeqi NP_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 ]
UniGenei Hs.596913.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2GDZ X-ray 1.65 A 3-256 [» ]
ProteinModelPortali P15428.
SMRi P15428. Positions 3-258.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109485. 1 interaction.
STRINGi 9606.ENSP00000296522.

Chemistry

BindingDBi P15428.
ChEMBLi CHEMBL1293255.

PTM databases

PhosphoSitei P15428.

Polymorphism databases

DMDMi 129889.

2D gel databases

SWISS-2DPAGE P15428.

Proteomic databases

MaxQBi P15428.
PaxDbi P15428.
PRIDEi P15428.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000296521 ; 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 ]
GeneIDi 3248.
KEGGi hsa:3248.
UCSCi uc003itu.3. human. [P15428-1 ]
uc003itv.3. human. [P15428-2 ]
uc010irq.3. human.

Organism-specific databases

CTDi 3248.
GeneCardsi GC04M175411.
HGNCi HGNC:5154. HPGD.
HPAi HPA004919.
HPA005679.
MIMi 119900. phenotype.
259100. phenotype.
601688. gene.
neXtProti NX_P15428.
Orphaneti 1525. Cranio-osteoarthropathy.
217059. Isolated congenital digital clubbing.
2796. Pachydermoperiostosis.
PharmGKBi PA29424.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1028.
GeneTreei ENSGT00760000118868.
HOGENOMi HOG000070121.
HOVERGENi HBG107379.
InParanoidi P15428.
KOi K00069.
OMAi IHFQNYD.
OrthoDBi EOG7966HT.
PhylomeDBi P15428.
TreeFami TF324093.

Enzyme and pathway databases

Reactomei REACT_150149. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
REACT_150320. Synthesis of Lipoxins (LX).
SABIO-RK P15428.

Miscellaneous databases

ChiTaRSi HPGD. human.
EvolutionaryTracei P15428.
GeneWikii HPGD.
GenomeRNAii 3248.
NextBioi 12913.
PROi P15428.
SOURCEi Search...

Gene expression databases

Bgeei P15428.
CleanExi HS_HPGD.
ExpressionAtlasi P15428. baseline and differential.
Genevestigatori P15428.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
InterProi IPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view ]
Pfami PF00106. adh_short. 1 hit.
[Graphical view ]
PRINTSi PR00081. GDHRDH.
PR00080. SDRFAMILY.
PROSITEi PS00061. ADH_SHORT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. Cited for: INVOLVEMENT IN PHOAR1, VARIANT COA PRO-140, CHARACTERIZATION OF VARIANT COA PRO-140.
  17. "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.
  18. "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.

Entry informationi

Entry nameiPGDH_HUMAN
AccessioniPrimary (citable) accession number: P15428
Secondary accession number(s): B4DTA4
, B4DU74, B4DV57, D3DP43, E7EV11, O00749, Q06F08, Q12998
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: October 29, 2014
This is version 154 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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3