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Protein

Prostaglandin G/H synthase 1

Gene

PTGS1

Organism
Ovis aries (Sheep)
Status
Reviewed-Annotation score: 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.1 Publication

Catalytic activityi

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

Cofactori

heme bNote: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei104 – 1041Not glycosylated
Active sitei207 – 2071Proton acceptor
Active sitei385 – 3851For cyclooxygenase activity1 Publication
Metal bindingi388 – 3881Iron (heme axial ligand)
Sitei530 – 5301Aspirin-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: UniProtKB-KW
  5. prostaglandin-endoperoxide synthase activity Source: UniProtKB-EC

GO - Biological processi

  1. cyclooxygenase pathway Source: InterPro
  2. inflammatory response Source: InterPro
  3. prostaglandin biosynthetic process Source: UniProtKB
  4. regulation of blood pressure Source: UniProtKB
  5. response to oxidative stress Source: InterPro
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

BRENDAi1.14.99.1. 4472.
SABIO-RKP05979.
UniPathwayiUPA00662.

Protein family/group databases

PeroxiBasei4121. OarPGHS01.

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
OrganismiOvis aries (Sheep)
Taxonomic identifieri9940 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeCaprinaeOvis
ProteomesiUP000002356: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei74 – 829Helical
Transmembranei86 – 927Helical
Transmembranei97 – 1059Helical
Transmembranei108 – 12215HelicalAdd
BLAST

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  3. integral component of membrane Source: UniProtKB-KW
  4. intracellular membrane-bounded organelle Source: UniProtKB
  5. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi385 – 3851Y → F: Abolishes cyclooxygenase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Add
BLAST
Chaini25 – 600576Prostaglandin G/H synthase 1PRO_0000023871Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi36 ↔ 47
Disulfide bondi37 ↔ 159
Disulfide bondi41 ↔ 57
Disulfide bondi59 ↔ 69
Glycosylationi68 – 681N-linked (GlcNAc...)1 Publication
Glycosylationi144 – 1441N-linked (GlcNAc...)1 Publication
Glycosylationi410 – 4101N-linked (GlcNAc...)1 Publication
Disulfide bondi569 ↔ 575

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1
600
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi35 – 384Combined sources
Beta strandi46 – 505Combined sources
Turni51 – 533Combined sources
Beta strandi54 – 585Combined sources
Beta strandi62 – 654Combined sources
Turni66 – 694Combined sources
Helixi74 – 829Combined sources
Helixi86 – 938Combined sources
Helixi97 – 1037Combined sources
Helixi108 – 12114Combined sources
Beta strandi130 – 1334Combined sources
Beta strandi134 – 1363Combined sources
Helixi139 – 1435Combined sources
Beta strandi149 – 1524Combined sources
Beta strandi159 – 1613Combined sources
Beta strandi164 – 1674Combined sources
Helixi174 – 1818Combined sources
Helixi196 – 20611Combined sources
Turni207 – 2093Combined sources
Turni214 – 2163Combined sources
Beta strandi220 – 2223Combined sources
Beta strandi227 – 2293Combined sources
Helixi231 – 2344Combined sources
Helixi238 – 2447Combined sources
Beta strandi255 – 2573Combined sources
Beta strandi260 – 2623Combined sources
Turni266 – 2683Combined sources
Helixi281 – 2833Combined sources
Beta strandi288 – 2914Combined sources
Helixi292 – 2943Combined sources
Helixi296 – 31924Combined sources
Helixi325 – 34622Combined sources
Helixi348 – 3536Combined sources
Helixi363 – 3664Combined sources
Beta strandi367 – 3693Combined sources
Helixi379 – 3846Combined sources
Helixi388 – 3903Combined sources
Beta strandi393 – 3975Combined sources
Beta strandi400 – 4023Combined sources
Helixi404 – 4074Combined sources
Helixi413 – 4175Combined sources
Helixi419 – 42810Combined sources
Beta strandi434 – 4385Combined sources
Turni442 – 4443Combined sources
Helixi445 – 45713Combined sources
Helixi463 – 4697Combined sources
Helixi478 – 4825Combined sources
Beta strandi483 – 4853Combined sources
Helixi486 – 49510Combined sources
Helixi498 – 5003Combined sources
Helixi503 – 5097Combined sources
Beta strandi517 – 5193Combined sources
Helixi520 – 53516Combined sources
Helixi538 – 5403Combined sources
Turni542 – 5443Combined sources
Helixi547 – 5504Combined sources
Helixi553 – 5608Combined sources
Helixi564 – 5696Combined sources
Beta strandi572 – 5743Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CQEX-ray3.10A/B21-600[»]
1DIYX-ray3.00A32-584[»]
1DJJmodel-A25-600[»]
1EBVX-ray3.20A33-583[»]
1EQGX-ray2.61A/B21-600[»]
1EQHX-ray2.70A/B21-600[»]
1FE2X-ray3.00A25-600[»]
1HT5X-ray2.75A/B33-583[»]
1HT8X-ray2.69A/B33-583[»]
1IGXX-ray3.10A25-600[»]
1IGZX-ray2.90A25-600[»]
1PGEX-ray3.50A/B25-600[»]
1PGFX-ray4.50A/B25-600[»]
1PGGX-ray4.50A/B25-600[»]
1PRHX-ray3.50A/B33-586[»]
1PTHX-ray3.40A/B25-600[»]
1Q4GX-ray2.00A/B32-584[»]
1U67X-ray3.10A1-600[»]
2AYLX-ray2.00A/B32-584[»]
2OYEX-ray2.85P1-600[»]
2OYUX-ray2.70P1-600[»]
3KK6X-ray2.75A/B32-584[»]
3N8VX-ray3.05A/B32-584[»]
3N8WX-ray2.75A/B32-584[»]
3N8XX-ray2.75A/B32-584[»]
3N8YX-ray2.60A/B32-584[»]
3N8ZX-ray2.90A/B32-584[»]
4O1ZX-ray2.40A/B32-600[»]
ProteinModelPortaliP05979.
SMRiP05979. Positions 32-584.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05979.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini32 – 7039EGF-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, Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG000366.
KOiK00509.

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]

Sequencei

Sequence statusi: Complete.

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

P05979-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSRQSISLRF PLLLLLLSPS PVFSADPGAP APVNPCCYYP CQHQGICVRF
60 70 80 90 100
GLDRYQCDCT RTGYSGPNCT IPEIWTWLRT TLRPSPSFIH FLLTHGRWLW
110 120 130 140 150
DFVNATFIRD TLMRLVLTVR SNLIPSPPTY NIAHDYISWE SFSNVSYYTR
160 170 180 190 200
ILPSVPRDCP TPMDTKGKKQ LPDAEFLSRR FLLRRKFIPD PQSTNLMFAF
210 220 230 240 250
FAQHFTHQFF KTSGKMGPGF TKALGHGVDL GHIYGDNLER QYQLRLFKDG
260 270 280 290 300
KLKYQMLNGE VYPPSVEEAP VLMHYPRGIP PQSQMAVGQE VFGLLPGLML
310 320 330 340 350
YATIWLREHN RVCDLLKAEH PTWGDEQLFQ TARLILIGET IKIVIEEYVQ
360 370 380 390 400
QLSGYFLQLK FDPELLFGAQ FQYRNRIAME FNQLYHWHPL MPDSFRVGPQ
410 420 430 440 450
DYSYEQFLFN TSMLVDYGVE ALVDAFSRQP AGRIGGGRNI DHHILHVAVD
460 470 480 490 500
VIKESRVLRL QPFNEYRKRF GMKPYTSFQE LTGEKEMAAE LEELYGDIDA
510 520 530 540 550
LEFYPGLLLE KCHPNSIFGE SMIEMGAPFS LKGLLGNPIC SPEYWKASTF
560 570 580 590 600
GGEVGFNLVK TATLKKLVCL NTKTCPYVSF HVPDPRQEDR PGVERPPTEL
Length:600
Mass (Da):68,861
Last modified:February 4, 2015 - v3
Checksum:i809887C7BB5A715C
GO

Sequence cautioni

The sequence AAA31576.1 differs from that shown. Reason: Frameshift at positions 63 and 92. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 55MSRQS → MVQG in AAA31511. (PubMed:2831188)Curated
Sequence conflicti193 – 1931S → G in AAA31576. (PubMed:3125548)Curated
Sequence conflicti193 – 1931S → G in AAA31511. (PubMed:2831188)Curated
Sequence conflicti540 – 5401C → E AA sequence (PubMed:6414516)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti97 – 971R → H.
Natural varianti164 – 1641D → G.2 Publications
Natural varianti456 – 4561R → Q.
Natural varianti520 – 5201E → K.
Natural varianti520 – 5201E → Q.
Natural varianti525 – 5251M → I.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03599 mRNA. Translation: AAA31576.1. Frameshift.
Y00750 mRNA. Translation: CAA68719.1.
M18243 mRNA. Translation: AAA31511.1.
PIRiA28960.
A29947.
S00561.
RefSeqiNP_001009476.1. NM_001009476.1.
UniGeneiOar.445.

Genome annotation databases

GeneIDi443551.
KEGGioas:443551.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03599 mRNA. Translation: AAA31576.1. Frameshift.
Y00750 mRNA. Translation: CAA68719.1.
M18243 mRNA. Translation: AAA31511.1.
PIRiA28960.
A29947.
S00561.
RefSeqiNP_001009476.1. NM_001009476.1.
UniGeneiOar.445.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CQEX-ray3.10A/B21-600[»]
1DIYX-ray3.00A32-584[»]
1DJJmodel-A25-600[»]
1EBVX-ray3.20A33-583[»]
1EQGX-ray2.61A/B21-600[»]
1EQHX-ray2.70A/B21-600[»]
1FE2X-ray3.00A25-600[»]
1HT5X-ray2.75A/B33-583[»]
1HT8X-ray2.69A/B33-583[»]
1IGXX-ray3.10A25-600[»]
1IGZX-ray2.90A25-600[»]
1PGEX-ray3.50A/B25-600[»]
1PGFX-ray4.50A/B25-600[»]
1PGGX-ray4.50A/B25-600[»]
1PRHX-ray3.50A/B33-586[»]
1PTHX-ray3.40A/B25-600[»]
1Q4GX-ray2.00A/B32-584[»]
1U67X-ray3.10A1-600[»]
2AYLX-ray2.00A/B32-584[»]
2OYEX-ray2.85P1-600[»]
2OYUX-ray2.70P1-600[»]
3KK6X-ray2.75A/B32-584[»]
3N8VX-ray3.05A/B32-584[»]
3N8WX-ray2.75A/B32-584[»]
3N8XX-ray2.75A/B32-584[»]
3N8YX-ray2.60A/B32-584[»]
3N8ZX-ray2.90A/B32-584[»]
4O1ZX-ray2.40A/B32-600[»]
ProteinModelPortaliP05979.
SMRiP05979. Positions 32-584.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiP05979.
ChEMBLiCHEMBL2111358.

Protein family/group databases

PeroxiBasei4121. OarPGHS01.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi443551.
KEGGioas:443551.

Organism-specific databases

CTDi5742.

Phylogenomic databases

HOVERGENiHBG000366.
KOiK00509.

Enzyme and pathway databases

UniPathwayiUPA00662.
BRENDAi1.14.99.1. 4472.
SABIO-RKP05979.

Miscellaneous databases

EvolutionaryTraceiP05979.

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]
ProtoNetiSearch...

Publicationsi

  1. "Primary structure of prostaglandin G/H synthase from sheep vesicular gland determined from the complementary DNA sequence."
    Dewitt D.L., Smith W.L.
    Proc. Natl. Acad. Sci. U.S.A. 85:1412-1416(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, VARIANT GLY-164.
    Tissue: Seminal vesicle.
  2. "Primary structure of sheep prostaglandin endoperoxide synthase deduced from cDNA sequence."
    Yokoyama C., Takai T., Tanabe T.
    FEBS Lett. 231:347-351(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
  3. "Isolation and characterization of the complementary DNA for sheep seminal vesicle prostaglandin endoperoxide synthase (cyclooxygenase)."
    Merlie J., Fagan D., Mudd J., Needleman P.
    J. Biol. Chem. 263:3550-3553(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLY-164.
  4. "Isolation and covalent structure of the aspirin-modified, active-site region of prostaglandin synthetase."
    Roth G.J., Machuga E.T., Ozols J.
    Biochemistry 22:4672-4675(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 523-544.
  5. "The aspirin and heme-binding sites of ovine and murine prostaglandin endoperoxide synthases."
    Dewitt D.L., El-Harith E.A., Kraemer S.A., Andrews M.J., Yao E.F., Armstrong R.L., Smith W.L.
    J. Biol. Chem. 265:5192-5198(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: HEME-BINDING SITE.
  6. "Tyrosine 385 of prostaglandin endoperoxide synthase is required for cyclooxygenase catalysis."
    Shimokawa T., Kulmacz R.J., Dewitt D.L., Smith W.L.
    J. Biol. Chem. 265:20073-20076(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACTIVE SITE TYR-385, MUTAGENESIS OF TYR-385.
  7. "N-glycosylation of prostaglandin endoperoxide synthases-1 and -2 and their orientations in the endoplasmic reticulum."
    Otto J.C., Dewitt D.L., Smith W.L.
    J. Biol. Chem. 268:18234-18242(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT ASN-68; ASN-144 AND ASN-410, ABSENCE OF GLYCOSYLATION AT ASN-104.
  8. "Arachidonic acid oxygenation by COX-1 and COX-2. Mechanisms of catalysis and inhibition."
    Marnett L.J., Rowlinson S.W., Goodwin D.C., Kalgutkar A.S., Lanzo C.A.
    J. Biol. Chem. 274:22903-22906(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AND INHIBITION BY NSAIDS.
  9. "The X-ray crystal structure of the membrane protein prostaglandin H2 synthase-1."
    Picot D., Loll P.J., Garavito R.M.
    Nature 367:243-249(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
  10. "The structural basis of aspirin activity inferred from the crystal structure of inactivated prostaglandin H2 synthase."
    Loll P.J., Picot D., Garavito R.M.
    Nat. Struct. Biol. 2:637-643(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS).
  11. "Synthesis and use of iodinated antiinflammatory drug analogs as crystallographic probes of the prostaglandin H2 synthase cyclooxygenase active site."
    Loll P.J., Picot D., Ekabo O., Garavito R.M.
    Biochemistry 35:7330-7340(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
  12. "The productive conformation of arachidonic acid bound to prostaglandin synthase."
    Malkowski M.G., Ginell S.L., Smith W.L., Garavito R.M.
    Science 289:1933-1937(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
  13. "Mutational and X-ray crystallographic analysis of the interaction of dihomo-gamma-linolenic acid with prostaglandin endoperoxide H synthases."
    Thuresson E.D., Malkowski M.G., Lakkides K.M., Rieke C.J., Mulichak A.M., Ginell S.L., Garavito R.M., Smith W.L.
    J. Biol. Chem. 276:10358-10365(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
  14. "Structural analysis of NSAID binding by prostaglandin H2 synthase: time-dependent and time-independent inhibitors elicit identical enzyme conformations."
    Selinsky B.S., Gupta K., Sharkey C.T., Loll P.J.
    Biochemistry 40:5172-5180(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS).

Entry informationi

Entry nameiPGH1_SHEEP
AccessioniPrimary (citable) accession number: P05979
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: February 4, 2015
Last modified: February 4, 2015
This is version 141 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.