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P23219

- PGH1_HUMAN

UniProt

P23219 - PGH1_HUMAN

Protein

Prostaglandin G/H synthase 1

Gene

PTGS1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 169 (01 Oct 2014)
      Sequence version 2 (11 Jan 2011)
      Previous versions | rss
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    Functioni

    Converts arachidonate to prostaglandin H2 (PGH2), a committed step in prostanoid synthesis. Involved in the constitutive production of prostanoids in particular in the stomach and platelets. In gastric epithelial cells, it is a key step in the generation of prostaglandins, such as prostaglandin E2 (PGE2), which plays an important role in cytoprotection. In platelets, it is involved in the generation of thromboxane A2 (TXA2), which promotes platelet activation and aggregation, vasoconstriction and proliferation of vascular smooth muscle cells.

    Catalytic activityi

    Arachidonate + AH2 + 2 O2 = prostaglandin H2 + A + H2O.

    Cofactori

    Binds 1 heme B (iron-protoporphyrin IX) group per subunit.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei206 – 2061Proton acceptorPROSITE-ProRule annotation
    Active sitei384 – 3841For cyclooxygenase activityBy similarity
    Metal bindingi387 – 3871Iron (heme axial ligand)PROSITE-ProRule annotation
    Sitei529 – 5291Aspirin-acetylated serine

    GO - Molecular functioni

    1. dioxygenase activity Source: UniProtKB-KW
    2. heme binding Source: InterPro
    3. metal ion binding Source: UniProtKB-KW
    4. peroxidase activity Source: Reactome
    5. prostaglandin-endoperoxide synthase activity Source: BHF-UCL

    GO - Biological processi

    1. arachidonic acid metabolic process Source: Reactome
    2. cyclooxygenase pathway Source: BHF-UCL
    3. lipid metabolic process Source: ProtInc
    4. prostaglandin biosynthetic process Source: UniProtKB
    5. regulation of blood pressure Source: UniProtKB
    6. regulation of cell proliferation Source: Ensembl
    7. response to oxidative stress Source: InterPro
    8. small molecule metabolic process Source: Reactome
    9. xenobiotic metabolic process Source: Reactome

    Keywords - Molecular functioni

    Dioxygenase, Oxidoreductase, Peroxidase

    Keywords - Biological processi

    Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Prostaglandin biosynthesis, Prostaglandin metabolism

    Keywords - Ligandi

    Heme, Iron, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS01815-MONOMER.
    BRENDAi1.14.99.1. 2681.
    ReactomeiREACT_1396. COX reactions.
    REACT_150149. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
    UniPathwayiUPA00662.

    Protein family/group databases

    PeroxiBasei3320. HsPGHS01.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Prostaglandin G/H synthase 1 (EC:1.14.99.1)
    Alternative name(s):
    Cyclooxygenase-1
    Short name:
    COX-1
    Prostaglandin H2 synthase 1
    Short name:
    PGH synthase 1
    Short name:
    PGHS-1
    Short name:
    PHS 1
    Prostaglandin-endoperoxide synthase 1
    Gene namesi
    Name:PTGS1
    Synonyms:COX1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:9604. PTGS1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. endoplasmic reticulum membrane Source: Reactome
    3. intracellular membrane-bounded organelle Source: UniProtKB
    4. nucleus Source: UniProtKB
    5. photoreceptor outer segment Source: Ensembl

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane, Microsome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi529 – 5291S → N: Abolishes cyclooxygenase activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA24346.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323Add
    BLAST
    Chaini24 – 599576Prostaglandin G/H synthase 1PRO_0000023868Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi35 ↔ 46By similarity
    Disulfide bondi36 ↔ 158By similarity
    Disulfide bondi40 ↔ 56By similarity
    Disulfide bondi58 ↔ 68By similarity
    Glycosylationi67 – 671N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi103 – 1031N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi143 – 1431N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi568 ↔ 574By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP23219.
    PaxDbiP23219.
    PRIDEiP23219.

    PTM databases

    PhosphoSiteiP23219.

    Expressioni

    Gene expression databases

    ArrayExpressiP23219.
    BgeeiP23219.
    CleanExiHS_PTGS1.
    GenevestigatoriP23219.

    Organism-specific databases

    HPAiCAB020315.
    HPA002834.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    BioGridi111714. 7 interactions.
    IntActiP23219. 1 interaction.
    MINTiMINT-4530066.
    STRINGi9606.ENSP00000354612.

    Structurei

    3D structure databases

    ProteinModelPortaliP23219.
    SMRiP23219. Positions 31-583.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini31 – 6939EGF-likePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the prostaglandin G/H synthase family.Curated
    Contains 1 EGF-like domain.PROSITE-ProRule annotation

    Keywords - Domaini

    EGF-like domain, Signal

    Phylogenomic databases

    eggNOGiNOG39991.
    HOGENOMiHOG000013149.
    HOVERGENiHBG000366.
    InParanoidiP23219.
    KOiK00509.
    OMAiFKTSGKM.
    OrthoDBiEOG7RFTHC.
    PhylomeDBiP23219.
    TreeFamiTF329675.

    Family and domain databases

    Gene3Di1.10.640.10. 1 hit.
    InterProiIPR029580. COX-1.
    IPR000742. EG-like_dom.
    IPR010255. Haem_peroxidase.
    IPR019791. Haem_peroxidase_animal.
    [Graphical view]
    PANTHERiPTHR11903:SF6. PTHR11903:SF6. 1 hit.
    PfamiPF03098. An_peroxidase. 1 hit.
    [Graphical view]
    PRINTSiPR00457. ANPEROXIDASE.
    SMARTiSM00181. EGF. 1 hit.
    [Graphical view]
    SUPFAMiSSF48113. SSF48113. 1 hit.
    PROSITEiPS50026. EGF_3. 1 hit.
    PS50292. PEROXIDASE_3. 1 hit.
    [Graphical view]

    Sequences (6)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 6 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P23219-1) [UniParc]FASTAAdd to Basket

    Also known as: Long

    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

    MSRSLLLWFL LFLLLLPPLP VLLADPGAPT PVNPCCYYPC QHQGICVRFG    50
    LDRYQCDCTR TGYSGPNCTI PGLWTWLRNS LRPSPSFTHF LLTHGRWFWE 100
    FVNATFIREM LMRLVLTVRS NLIPSPPTYN SAHDYISWES FSNVSYYTRI 150
    LPSVPKDCPT PMGTKGKKQL PDAQLLARRF LLRRKFIPDP QGTNLMFAFF 200
    AQHFTHQFFK TSGKMGPGFT KALGHGVDLG HIYGDNLERQ YQLRLFKDGK 250
    LKYQVLDGEM YPPSVEEAPV LMHYPRGIPP QSQMAVGQEV FGLLPGLMLY 300
    ATLWLREHNR VCDLLKAEHP TWGDEQLFQT TRLILIGETI KIVIEEYVQQ 350
    LSGYFLQLKF DPELLFGVQF QYRNRIAMEF NHLYHWHPLM PDSFKVGSQE 400
    YSYEQFLFNT SMLVDYGVEA LVDAFSRQIA GRIGGGRNMD HHILHVAVDV 450
    IRESREMRLQ PFNEYRKRFG MKPYTSFQEL VGEKEMAAEL EELYGDIDAL 500
    EFYPGLLLEK CHPNSIFGES MIEIGAPFSL KGLLGNPICS PEYWKPSTFG 550
    GEVGFNIVKT ATLKKLVCLN TKTCPYVSFR VPDASQDDGP AVERPSTEL 599
    Length:599
    Mass (Da):68,686
    Last modified:January 11, 2011 - v2
    Checksum:i1F4F734BCD00346D
    GO
    Isoform 2 (identifier: P23219-2) [UniParc]FASTAAdd to Basket

    Also known as: Short

    The sequence of this isoform differs from the canonical sequence as follows:
         396-432: Missing.

    Show »
    Length:562
    Mass (Da):64,513
    Checksum:i7AB78D6FD94F5FF1
    GO
    Isoform 3 (identifier: P23219-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-32: MSRSLLLWFLLFLLLLPPLPVLLADPGAPTPV → MRKPRLM
         396-432: Missing.

    Show »
    Length:537
    Mass (Da):61,930
    Checksum:i9AD6A32F6FE7CF05
    GO
    Isoform 4 (identifier: P23219-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-109: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:490
    Mass (Da):56,085
    Checksum:i8C340B40B682E98C
    GO
    Isoform 5 (identifier: P23219-5) [UniParc]FASTAAdd to Basket

    Also known as: 1b3

    The sequence of this isoform differs from the canonical sequence as follows:
         1-3: MSR → MSRECDPGARWGIFLASGGALNARLSPSSLSSAG

    Show »
    Length:630
    Mass (Da):71,717
    Checksum:iB70763422AC0C249
    GO
    Isoform 6 (identifier: P23219-6) [UniParc]FASTAAdd to Basket

    Also known as: 1b2

    The sequence of this isoform differs from the canonical sequence as follows:
         1-3: MSR → MSRECDPGARWGIFLASWWSLECQLSPSSLSSAG

    Show »
    Length:630
    Mass (Da):72,010
    Checksum:i7A7080D69D5583C1
    GO

    Sequence cautioni

    The sequence CAI14716.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti12 – 121F → L in AAA36439. (PubMed:2512924)Curated
    Sequence conflicti113 – 1131R → L in AAA36439. (PubMed:2512924)Curated
    Sequence conflicti378 – 3781M → T in AAA36439. (PubMed:2512924)Curated
    Sequence conflicti423 – 4231D → G in BAG65237. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti8 – 81W → R.9 Publications
    Corresponds to variant rs1236913 [ dbSNP | Ensembl ].
    VAR_013451
    Natural varianti17 – 171P → L.2 Publications
    Corresponds to variant rs3842787 [ dbSNP | Ensembl ].
    VAR_013452
    Natural varianti53 – 531R → H.1 Publication
    Corresponds to variant rs3842789 [ dbSNP | Ensembl ].
    VAR_019161
    Natural varianti149 – 1491R → L.1 Publication
    Corresponds to variant rs10306140 [ dbSNP | Ensembl ].
    VAR_019162
    Natural varianti185 – 1851K → T.
    Corresponds to variant rs3842792 [ dbSNP | Ensembl ].
    VAR_056663
    Natural varianti237 – 2371L → M.2 Publications
    Corresponds to variant rs5789 [ dbSNP | Ensembl ].
    VAR_019163
    Natural varianti341 – 3411K → R.
    Corresponds to variant rs3842799 [ dbSNP | Ensembl ].
    VAR_056664
    Natural varianti359 – 3591K → R.
    Corresponds to variant rs5791 [ dbSNP | Ensembl ].
    VAR_013453
    Natural varianti443 – 4431I → V.
    Corresponds to variant rs5792 [ dbSNP | Ensembl ].
    VAR_013454
    Natural varianti481 – 4811V → I.1 Publication
    Corresponds to variant rs5794 [ dbSNP | Ensembl ].
    VAR_028017

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 109109Missing in isoform 4. 1 PublicationVSP_046932Add
    BLAST
    Alternative sequencei1 – 3232MSRSL…APTPV → MRKPRLM in isoform 3. 1 PublicationVSP_053936Add
    BLAST
    Alternative sequencei1 – 33MSR → MSRECDPGARWGIFLASGGA LNARLSPSSLSSAG in isoform 5. 1 PublicationVSP_054862
    Alternative sequencei1 – 33MSR → MSRECDPGARWGIFLASWWS LECQLSPSSLSSAG in isoform 6. 1 PublicationVSP_054863
    Alternative sequencei396 – 43237Missing in isoform 2 and isoform 3. 2 PublicationsVSP_004673Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M31822
    , M31812, M31813, M31814, M31815, M31816, M31817, M31818, M31819, M31820, M31821 Genomic DNA. Translation: AAA36439.1.
    M59979 mRNA. Translation: AAA03630.1.
    S78220 mRNA. Translation: AAB21215.1.
    S36219 mRNA. Translation: AAB22216.1.
    S36271 mRNA. Translation: AAB22217.1.
    DQ180741 mRNA. Translation: ABA60098.1.
    DQ180742 mRNA. Translation: ABA60099.1.
    AF440204 Genomic DNA. Translation: AAL33601.1.
    AK290022 mRNA. Translation: BAF82711.1.
    AK295221 mRNA. Translation: BAG58214.1.
    AK304403 mRNA. Translation: BAG65237.1.
    AY449688 Genomic DNA. Translation: AAR08907.1.
    AL162424, AL359636 Genomic DNA. Translation: CAI14714.1.
    AL162424, AL359636 Genomic DNA. Translation: CAI14715.1.
    AL162424 Genomic DNA. Translation: CAI14716.1. Sequence problems.
    AL359636, AL162424 Genomic DNA. Translation: CAM45740.1.
    AL359636, AL162424 Genomic DNA. Translation: CAM45741.1.
    CH471090 Genomic DNA. Translation: EAW87530.1.
    BC029840 mRNA. Translation: AAH29840.1.
    CCDSiCCDS59520.1. [P23219-3]
    CCDS59521.1. [P23219-4]
    CCDS6842.1. [P23219-1]
    CCDS6843.1. [P23219-2]
    PIRiJH0259.
    RefSeqiNP_000953.2. NM_000962.3. [P23219-1]
    NP_001258094.1. NM_001271165.1. [P23219-4]
    NP_001258095.1. NM_001271166.1.
    NP_001258297.1. NM_001271368.1. [P23219-3]
    NP_542158.1. NM_080591.2. [P23219-2]
    XP_006717255.1. XM_006717192.1. [P23219-3]
    UniGeneiHs.201978.

    Genome annotation databases

    EnsembliENST00000223423; ENSP00000223423; ENSG00000095303. [P23219-2]
    ENST00000362012; ENSP00000354612; ENSG00000095303. [P23219-1]
    ENST00000373698; ENSP00000362802; ENSG00000095303. [P23219-4]
    ENST00000540753; ENSP00000437709; ENSG00000095303. [P23219-3]
    GeneIDi5742.
    KEGGihsa:5742.
    UCSCiuc004bmf.2. human. [P23219-2]
    uc004bmg.2. human. [P23219-1]

    Polymorphism databases

    DMDMi317373262.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M31822
    , M31812 , M31813 , M31814 , M31815 , M31816 , M31817 , M31818 , M31819 , M31820 , M31821 Genomic DNA. Translation: AAA36439.1 .
    M59979 mRNA. Translation: AAA03630.1 .
    S78220 mRNA. Translation: AAB21215.1 .
    S36219 mRNA. Translation: AAB22216.1 .
    S36271 mRNA. Translation: AAB22217.1 .
    DQ180741 mRNA. Translation: ABA60098.1 .
    DQ180742 mRNA. Translation: ABA60099.1 .
    AF440204 Genomic DNA. Translation: AAL33601.1 .
    AK290022 mRNA. Translation: BAF82711.1 .
    AK295221 mRNA. Translation: BAG58214.1 .
    AK304403 mRNA. Translation: BAG65237.1 .
    AY449688 Genomic DNA. Translation: AAR08907.1 .
    AL162424 , AL359636 Genomic DNA. Translation: CAI14714.1 .
    AL162424 , AL359636 Genomic DNA. Translation: CAI14715.1 .
    AL162424 Genomic DNA. Translation: CAI14716.1 . Sequence problems.
    AL359636 , AL162424 Genomic DNA. Translation: CAM45740.1 .
    AL359636 , AL162424 Genomic DNA. Translation: CAM45741.1 .
    CH471090 Genomic DNA. Translation: EAW87530.1 .
    BC029840 mRNA. Translation: AAH29840.1 .
    CCDSi CCDS59520.1. [P23219-3 ]
    CCDS59521.1. [P23219-4 ]
    CCDS6842.1. [P23219-1 ]
    CCDS6843.1. [P23219-2 ]
    PIRi JH0259.
    RefSeqi NP_000953.2. NM_000962.3. [P23219-1 ]
    NP_001258094.1. NM_001271165.1. [P23219-4 ]
    NP_001258095.1. NM_001271166.1.
    NP_001258297.1. NM_001271368.1. [P23219-3 ]
    NP_542158.1. NM_080591.2. [P23219-2 ]
    XP_006717255.1. XM_006717192.1. [P23219-3 ]
    UniGenei Hs.201978.

    3D structure databases

    ProteinModelPortali P23219.
    SMRi P23219. Positions 31-583.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111714. 7 interactions.
    IntActi P23219. 1 interaction.
    MINTi MINT-4530066.
    STRINGi 9606.ENSP00000354612.

    Chemistry

    BindingDBi P23219.
    ChEMBLi CHEMBL221.
    DrugBanki DB00316. Acetaminophen.
    DB00945. Aspirin.
    DB01014. Balsalazide.
    DB00963. Bromfenac.
    DB01188. Ciclopirox.
    DB00586. Diclofenac.
    DB00861. Diflunisal.
    DB04817. Dipyrone.
    DB00749. Etodolac.
    DB00573. Fenoprofen.
    DB00712. Flurbiprofen.
    DB00154. gamma-Homolinolenic acid.
    DB01050. Ibuprofen.
    DB00159. Icosapent.
    DB00328. Indomethacin.
    DB01009. Ketoprofen.
    DB00465. Ketorolac.
    DB01283. Lumiracoxib.
    DB00939. Meclofenamic acid.
    DB00784. Mefenamic acid.
    DB00244. Mesalazine.
    DB00350. Minoxidil.
    DB00461. Nabumetone.
    DB00788. Naproxen.
    DB03783. Phenacetin.
    DB00554. Piroxicam.
    DB00533. Rofecoxib.
    DB00936. Salicyclic acid.
    DB01399. Salsalate.
    DB00605. Sulindac.
    DB00870. Suprofen.
    DB00469. Tenoxicam.
    DB00500. Tolmetin.
    GuidetoPHARMACOLOGYi 1375.

    Protein family/group databases

    PeroxiBasei 3320. HsPGHS01.

    PTM databases

    PhosphoSitei P23219.

    Polymorphism databases

    DMDMi 317373262.

    Proteomic databases

    MaxQBi P23219.
    PaxDbi P23219.
    PRIDEi P23219.

    Protocols and materials databases

    DNASUi 5742.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000223423 ; ENSP00000223423 ; ENSG00000095303 . [P23219-2 ]
    ENST00000362012 ; ENSP00000354612 ; ENSG00000095303 . [P23219-1 ]
    ENST00000373698 ; ENSP00000362802 ; ENSG00000095303 . [P23219-4 ]
    ENST00000540753 ; ENSP00000437709 ; ENSG00000095303 . [P23219-3 ]
    GeneIDi 5742.
    KEGGi hsa:5742.
    UCSCi uc004bmf.2. human. [P23219-2 ]
    uc004bmg.2. human. [P23219-1 ]

    Organism-specific databases

    CTDi 5742.
    GeneCardsi GC09P125133.
    HGNCi HGNC:9604. PTGS1.
    HPAi CAB020315.
    HPA002834.
    MIMi 176805. gene.
    neXtProti NX_P23219.
    PharmGKBi PA24346.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG39991.
    HOGENOMi HOG000013149.
    HOVERGENi HBG000366.
    InParanoidi P23219.
    KOi K00509.
    OMAi FKTSGKM.
    OrthoDBi EOG7RFTHC.
    PhylomeDBi P23219.
    TreeFami TF329675.

    Enzyme and pathway databases

    UniPathwayi UPA00662 .
    BioCyci MetaCyc:HS01815-MONOMER.
    BRENDAi 1.14.99.1. 2681.
    Reactomei REACT_1396. COX reactions.
    REACT_150149. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).

    Miscellaneous databases

    ChiTaRSi PTGS1. human.
    GeneWikii PTGS1.
    GenomeRNAii 5742.
    NextBioi 22352.
    PROi P23219.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P23219.
    Bgeei P23219.
    CleanExi HS_PTGS1.
    Genevestigatori P23219.

    Family and domain databases

    Gene3Di 1.10.640.10. 1 hit.
    InterProi IPR029580. COX-1.
    IPR000742. EG-like_dom.
    IPR010255. Haem_peroxidase.
    IPR019791. Haem_peroxidase_animal.
    [Graphical view ]
    PANTHERi PTHR11903:SF6. PTHR11903:SF6. 1 hit.
    Pfami PF03098. An_peroxidase. 1 hit.
    [Graphical view ]
    PRINTSi PR00457. ANPEROXIDASE.
    SMARTi SM00181. EGF. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48113. SSF48113. 1 hit.
    PROSITEi PS50026. EGF_3. 1 hit.
    PS50292. PEROXIDASE_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of human gene encoding prostaglandin endoperoxide synthase and primary structure of the enzyme."
      Yokoyama C., Tanabe T.
      Biochem. Biophys. Res. Commun. 165:888-894(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANT ARG-8.
    2. "Human platelet/erythroleukemia cell prostaglandin G/H synthase: cDNA cloning, expression, and gene chromosomal assignment."
      Funk C.D., Funk L.B., Kennedy M.E., Pong A.S., Fitzgerald G.A.
      FASEB J. 5:2304-2312(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS OF SER-529, VARIANT ARG-8.
    3. "Immunoaffinity purification and cDNA cloning of human platelet prostaglandin endoperoxide synthase (cyclooxygenase)."
      Takahashi Y., Ueda N., Yoshimoto T., Yamamoto S., Yokoyama C., Miyata A., Tanabe T., Fuse I., Hattori A., Shibata A.
      Biochem. Biophys. Res. Commun. 182:433-438(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ARG-8.
      Tissue: Platelet.
    4. "Alternative splicing of human prostaglandin G/H synthase mRNA and evidence of differential regulation of the resulting transcripts by transforming growth factor beta 1, interleukin 1 beta, and tumor necrosis factor alpha."
      Diaz A., Reginato A.M., Jimenez S.A.
      J. Biol. Chem. 267:10816-10822(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), VARIANT ARG-8.
      Tissue: Lung fibroblast.
    5. "Cloning, expression, and functional characterization of human cyclooxygenase-1 splicing variants: evidence for intron 1 retention."
      Qin N., Zhang S.P., Reitz T.L., Mei J.M., Flores C.M.
      J. Pharmacol. Exp. Ther. 315:1298-1305(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5 AND 6).
    6. "Characterization of the human prostaglandin H synthase 1 gene (PTGS1): exclusion by genetic linkage analysis as a second modifier gene in familial thrombosis."
      Scott B.T., Hasstedt S.J., Bovill E.G., Callas P.W., Valliere J.E., Wang L.-H., Wu K.K., Long G.L.
      Blood Coagul. Fibrinolysis 13:519-531(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANTS ARG-8 AND LEU-17.
    7. "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; 3 AND 4), VARIANT ARG-8.
      Tissue: Caudate nucleus, Hippocampus and Trachea.
    8. SeattleSNPs variation discovery resource
      Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANTS ARG-8; LEU-17; HIS-53; LEU-149 AND MET-237.
    9. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ARG-8.
    11. "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), VARIANT ARG-8.
      Tissue: Brain.
    12. "Cyclooxygenases: structural, cellular, and molecular biology."
      Smith W.L., DeWitt D.L., Garavito R.M.
      Annu. Rev. Biochem. 69:145-182(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION; TISSUE SPECIFICITY AND INHIBITION BY NSAIDS.
    13. "Aspirin, cyclooxygenase inhibition and colorectal cancer."
      Sostres C., Gargallo C.J., Lanas A.
      World J. Gastrointest. Pharmacol. Ther. 5:40-49(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION; INHIBITION BY ASPIRIN AND INVOLVEMENT IN COLORECTAL CANCER.
    14. "Arachidonate lipoxygenase (ALOX) and cyclooxygenase (COX) polymorphisms and colon cancer risk."
      Goodman J.E., Bowman E.D., Chanock S.J., Alberg A.J., Harris C.C.
      Carcinogenesis 25:2467-2472(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS MET-237 AND ILE-481.

    Entry informationi

    Entry nameiPGH1_HUMAN
    AccessioniPrimary (citable) accession number: P23219
    Secondary accession number(s): A8K1V7
    , B4DHQ2, B4E2S5, Q15122, Q3HY28, Q3HY29, Q5T7T6, Q5T7T7, Q5T7T8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 169 of the entry and version 2 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

    Miscellaneous

    The conversion of arachidonate to prostaglandin H2 is a 2 step reaction: a cyclooxygenase (COX) reaction which converts arachidonate to prostaglandin G2 (PGG2) and a peroxidase reaction in which PGG2 is reduced to prostaglandin H2 (PGH2). The cyclooxygenase reaction occurs in a hydrophobic channel in the core of the enzyme. The peroxidase reaction occurs at a heme-containing active site located near the protein surface. The nonsteroidal anti-inflammatory drugs (NSAIDs) binding site corresponds to the cyclooxygenase active site.
    Conversion of arachidonate to prostaglandin H2 is mediated by 2 different isozymes: the constitutive PTGS1 and the inducible PTGS2. PGHS1 is expressed constitutively and generally produces prostanoids acutely in response to hormonal stimuli to fine-tune physiological processes requiring instantaneous, continuous regulation (e.g. hemostasis). PGHS2 is inducible and typically produces prostanoids that mediate responses to physiological stresses such as infection and inflammation.
    PTGS1 and PTGS2 are the targets of nonsteroidal anti-inflammatory drugs (NSAIDs) including aspirin and ibuprofen. Aspirin is able to produce an irreversible inactivation of the enzyme through a serine acetylation. Inhibition of the PGHSs with NSAIDs acutely reduces inflammation, pain, and fever, and long-term use of these drugs reduces fatal thrombotic events, as well as the development of colon cancer and Alzheimer's disease. PTGS2 is the principal isozyme responsible for production of inflammatory prostaglandins. New generation PTGSs inhibitors strive to be selective for PTGS2, to avoid side effects such as gastrointestinal complications and ulceration.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

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