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P23219

- PGH1_HUMAN

UniProt

P23219 - PGH1_HUMAN

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Protein
Prostaglandin G/H synthase 1
Gene
PTGS1, COX1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 acceptor By similarity
Active sitei384 – 3841For cyclooxygenase activity By similarity
Metal bindingi387 – 3871Iron (heme axial ligand) By similarity
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
Complete GO annotation...

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
Complete GO annotation...

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
Complete GO annotation...

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 – 2323
Add
BLAST
Chaini24 – 599576Prostaglandin G/H synthase 1
PRO_0000023868Add
BLAST

Amino acid modifications

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini31 – 6939EGF-like
Add
BLAST

Sequence similaritiesi

Contains 1 EGF-like domain.

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.

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.
VSP_046932Add
BLAST
Alternative sequencei1 – 3232MSRSL…APTPV → MRKPRLM in isoform 3.
VSP_053936Add
BLAST
Alternative sequencei1 – 33MSR → MSRECDPGARWGIFLASGGA LNARLSPSSLSSAG in isoform 5.
VSP_054862
Alternative sequencei1 – 33MSR → MSRECDPGARWGIFLASWWS LECQLSPSSLSSAG in isoform 6.
VSP_054863
Alternative sequencei396 – 43237Missing in isoform 2 and isoform 3.
VSP_004673Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 121F → L in AAA36439. 1 Publication
Sequence conflicti113 – 1131R → L in AAA36439. 1 Publication
Sequence conflicti378 – 3781M → T in AAA36439. 1 Publication
Sequence conflicti423 – 4231D → G in BAG65237. 1 Publication

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]
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...

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 ]
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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 168 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

Dasty 3

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