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P15428

- PGDH_HUMAN

UniProt

P15428 - PGDH_HUMAN

Protein

15-hydroxyprostaglandin dehydrogenase [NAD(+)]

Gene

HPGD

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 1 (01 Apr 1990)
      Previous versions | rss
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    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

    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

    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

    ArrayExpressiP15428.
    BgeeiP15428.
    CleanExiHS_HPGD.
    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.
    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

    MHVNGKVALV TGAAQGIGRA FAEALLLKGA KVALVDWNLE AGVQCKAALD    50
    EQFEPQKTLF IQCDVADQQQ LRDTFRKVVD HFGRLDILVN NAGVNNEKNW 100
    EKTLQINLVS VISGTYLGLD YMSKQNGGEG GIIINMSSLA GLMPVAQQPV 150
    YCASKHGIVG FTRSAALAAN LMNSGVRLNA ICPGFVNTAI LESIEKEENM 200
    GQYIEYKDHI KDMIKYYGIL DPPLIANGLI TLIEDDALNG AIMKITTSKG 250
    IHFQDYDTTP FQAKTQ 266
    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.
    DrugBanki DB00157. NADH.

    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.
    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

    ArrayExpressi P15428.
    Bgeei P15428.
    CleanExi HS_HPGD.
    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

    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 1, 2014
    This is version 153 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