Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

15-hydroxyprostaglandin dehydrogenase [NAD(+)]

Gene

HPGD

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

    • 15-hydroxyprostaglandin dehydrogenase (NAD+) activity Source: UniProtKB
    • catalytic activity Source: UniProtKB
    • NAD+ binding Source: UniProtKB
    • NAD binding Source: UniProtKB
    • prostaglandin E receptor activity Source: UniProtKB
    • protein homodimerization activity Source: UniProtKB

    GO - Biological processi

    • arachidonic acid metabolic process Source: Reactome
    • cyclooxygenase pathway Source: Reactome
    • ductus arteriosus closure Source: UniProtKB
    • female pregnancy Source: UniProtKB
    • lipoxin metabolic process Source: Reactome
    • lipoxygenase pathway Source: UniProtKB
    • negative regulation of cell cycle Source: UniProtKB
    • ovulation Source: UniProtKB
    • parturition Source: UniProtKB
    • prostaglandin metabolic process Source: UniProtKB
    • small molecule metabolic process Source: Reactome
    • thrombin receptor signaling pathway Source: UniProtKB
    • 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

    BRENDAi1.1.1.141. 2681.
    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
    Short chain dehydrogenase/reductase family 36C member 1
    Gene namesi
    Name:HPGD
    Synonyms:PGDH1, SDR36C1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:5154. HPGD.

    Subcellular locationi

    GO - Cellular componenti

    • basolateral plasma membrane Source: Ensembl
    • cytosol Source: UniProtKB
    • extracellular exosome Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Hypertrophic osteoarthropathy, primary, autosomal recessive, 1 (PHOAR1)1 Publication

    The disease is caused by mutations affecting the gene represented in this entry.

    Disease descriptionA 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.

    See also OMIM:259100
    Cranioosteoarthropathy (COA)1 Publication

    The disease is caused by mutations affecting the gene represented in this entry.

    Disease descriptionA 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.

    See also OMIM:259100
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti140 – 1401A → P in COA; inactive. 1 Publication
    VAR_046209
    Isolated congenital nail clubbing (ICNC)1 Publication

    The disease is caused by mutations affecting the gene represented in this entry.

    Disease descriptionA 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.

    See also OMIM:119900
    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.

    Polymorphism and mutation databases

    BioMutaiHPGD.
    DMDMi129889.

    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.
    GenevisibleiP15428. HS.

    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 – 115Combined sources
    Turni12 – 143Combined sources
    Helixi16 – 2712Combined sources
    Beta strandi31 – 377Combined sources
    Helixi39 – 4911Combined sources
    Turni50 – 523Combined sources
    Helixi55 – 573Combined sources
    Beta strandi58 – 625Combined sources
    Helixi68 – 8215Combined sources
    Beta strandi87 – 904Combined sources
    Beta strandi97 – 993Combined sources
    Helixi100 – 1078Combined sources
    Helixi109 – 12214Combined sources
    Helixi124 – 1263Combined sources
    Beta strandi131 – 1366Combined sources
    Helixi139 – 1413Combined sources
    Helixi149 – 17224Combined sources
    Beta strandi176 – 1849Combined sources
    Beta strandi186 – 1883Combined sources
    Helixi189 – 1924Combined sources
    Helixi193 – 1953Combined sources
    Helixi197 – 2004Combined sources
    Helixi201 – 2066Combined sources
    Helixi207 – 21711Combined sources
    Helixi222 – 23413Combined sources
    Beta strandi242 – 2465Combined sources
    Turni247 – 2493Combined sources
    Beta strandi250 – 2534Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    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.
    OMAiLAXMAAN.
    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. AlignAdd to basket

    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:
    EMBLi
    GenBanki
    DDBJi
    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.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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.

    3D structure databases

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

    Protein-protein interaction databases

    BioGridi109485. 1 interaction.
    STRINGi9606.ENSP00000296522.

    Chemistry

    BindingDBiP15428.
    ChEMBLiCHEMBL1293255.

    PTM databases

    PhosphoSiteiP15428.

    Polymorphism and mutation databases

    BioMutaiHPGD.
    DMDMi129889.

    2D gel databases

    SWISS-2DPAGEP15428.

    Proteomic databases

    MaxQBiP15428.
    PaxDbiP15428.
    PRIDEiP15428.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    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.

    Organism-specific databases

    CTDi3248.
    GeneCardsiGC04M175411.
    HGNCiHGNC:5154. HPGD.
    HPAiHPA004919.
    HPA005679.
    MIMi119900. phenotype.
    259100. phenotype.
    601688. gene.
    neXtProtiNX_P15428.
    Orphaneti1525. Cranio-osteoarthropathy.
    217059. Isolated congenital digital clubbing.
    2796. Pachydermoperiostosis.
    PharmGKBiPA29424.
    GenAtlasiSearch...

    Phylogenomic databases

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

    Enzyme and pathway databases

    BRENDAi1.1.1.141. 2681.
    ReactomeiREACT_150149. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
    REACT_150320. Synthesis of Lipoxins (LX).
    SABIO-RKP15428.

    Miscellaneous databases

    ChiTaRSiHPGD. human.
    EvolutionaryTraceiP15428.
    GeneWikiiHPGD.
    GenomeRNAii3248.
    NextBioi12913.
    PROiP15428.
    SOURCEiSearch...

    Gene expression databases

    BgeeiP15428.
    CleanExiHS_HPGD.
    ExpressionAtlasiP15428. baseline and differential.
    GenevisibleiP15428. HS.

    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]
    ProtoNetiSearch...

    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: June 24, 2015
    This is version 160 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.