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Protein

Prostaglandin G/H synthase 2

Gene

PTGS2

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

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Converts arachidonate to prostaglandin H2 (PGH2), a committed step in prostanoid synthesis (PubMed:26859324, PubMed:27226593). Constitutively expressed in some tissues in physiological conditions, such as the endothelium, kidney and brain, and in pathological conditions, such as in cancer. PTGS2 is responsible for production of inflammatory prostaglandins. Up-regulation of PTGS2 is also associated with increased cell adhesion, phenotypic changes, resistance to apoptosis and tumor angiogenesis. In cancer cells, PTGS2 is a key step in the production of prostaglandin E2 (PGE2), which plays important roles in modulating motility, proliferation and resistance to apoptosis.3 Publications

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 (PubMed:27710942, PubMed:26859324, PubMed:27226593). Aspirin is able to produce an irreversible inactivation of the enzyme through a serine acetylation (PubMed:26859324). 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.3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

heme b3 PublicationsNote: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.3 Publications

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by nonsteroidal anti-inflammatory drugs (NSAIDs) including aspirin, ibuprofen, flurbiprofen and celecoxib (PubMed:26859324). Inhibited by flufenamic acid, mefenamic acid and tolfenamic acid (PubMed:27226593).2 Publications

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=16.2 µM for arachidonate (in absence of sodium nitroprusside NO donor)1 Publication
  2. KM=12 µM for arachidonic acid1 Publication
  3. KM=17.0 µM for arachidonate (in presence of sodium nitroprusside NO donor)1 Publication
  1. Vmax=81.3 nmol/min/mg enzyme (in absence of sodium nitroprusside NO donor)1 Publication
  2. Vmax=132 nmol/min/mg enzyme (in absence of sodium nitroprusside NO donor)1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: prostaglandin biosynthesis

This protein is involved in the pathway prostaglandin biosynthesis, which is part of Lipid metabolism.2 Publications
View all proteins of this organism that are known to be involved in the pathway prostaglandin biosynthesis and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei106SubstrateBy similarity1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei193Proton acceptorPROSITE-ProRule annotation1
Binding sitei341SubstrateBy similarity1
Active sitei371For cyclooxygenase activityBy similarity1
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi374Iron (heme axial ligand)PROSITE-ProRule annotation1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei516Aspirin-acetylated serine1 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDioxygenase, Oxidoreductase, Peroxidase
Biological processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Prostaglandin biosynthesis, Prostaglandin metabolism
LigandHeme, Iron, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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BioCyci
MetaCyc:HS01115-MONOMER

BRENDA Comprehensive Enzyme Information System

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BRENDAi
1.14.99.1 2681

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-197264 Nicotinamide salvaging
R-HSA-2142770 Synthesis of 15-eicosatetraenoic acid derivatives
R-HSA-2162123 Synthesis of Prostaglandins (PG) and Thromboxanes (TX)
R-HSA-6783783 Interleukin-10 signaling
R-HSA-6785807 Interleukin-4 and Interleukin-13 signaling
R-HSA-9018677 Biosynthesis of DHA-derived SPMs
R-HSA-9018679 Biosynthesis of EPA-derived SPMs
R-HSA-9025094 Biosynthesis of DPAn-3 SPMs
R-HSA-9027604 Biosynthesis of electrophilic Omega-3 PUFA oxo-derivatives

SABIO-RK: Biochemical Reaction Kinetics Database

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SABIO-RKi
P35354

SIGNOR Signaling Network Open Resource

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SIGNORi
P35354

UniPathway: a resource for the exploration and annotation of metabolic pathways

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UniPathwayi
UPA00662

Protein family/group databases

PeroxiBase, a peroxidase database

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PeroxiBasei
3321 HsPGHS02

Chemistry databases

SwissLipids knowledge resource for lipid biology

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SwissLipidsi
SLP:000000830

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Prostaglandin G/H synthase 2 (EC:1.14.99.13 Publications)
Alternative name(s):
Cyclooxygenase-2
Short name:
COX-2
PHS II
Prostaglandin H2 synthase 2
Short name:
PGH synthase 2
Short name:
PGHS-2
Prostaglandin-endoperoxide synthase 2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:PTGS2
Synonyms:COX2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 1

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000073756.11

Human Gene Nomenclature Database

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HGNCi
HGNC:9605 PTGS2

Online Mendelian Inheritance in Man (OMIM)

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MIMi
600262 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P35354

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi371Y → A: Decreased protein stability. Increased decrease of protein stability; when associated with A-516. 1 Publication1
Mutagenesisi516S → A: No effect on protein stability. Increased decrease of protein stability; when associated with A-371. 1 Publication1
Mutagenesisi516S → T: Decreased enzyme activity with arachidonic acid. Loss of cyclooxygenase activity; when associated with V-519. 1 Publication1
Mutagenesisi519G → V: Loss of cyclooxygenase activity. Loss of cyclooxygenase activity; when associated with T-516. 1 Publication1
Mutagenesisi526C → S: Prevents activation by nitric oxid (NO). 1 Publication1
Mutagenesisi555C → S: Abolishes enzyme activity. 1 Publication1
Mutagenesisi561C → S: Does not affect activation by nitric oxid (NO). 1 Publication1

Organism-specific databases

DisGeNET

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DisGeNETi
5743

Open Targets

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OpenTargetsi
ENSG00000073756

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA293

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL230

Drug and drug target database

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DrugBanki
DB03477 1-Phenylsulfonamide-3-Trifluoromethyl-5-Parabromophenylpyrazole
DB00316 Acetaminophen
DB00945 Acetylsalicylic acid
DB00041 Aldesleukin
DB00233 Aminosalicylic Acid
DB01435 Antipyrine
DB01419 Antrafenine
DB01014 Balsalazide
DB00963 Bromfenac
DB00887 Bumetanide
DB06774 Capsaicin
DB00821 Carprofen
DB00482 Celecoxib
DB00856 Chlorphenesin
DB05095 Cimicoxib
DB00515 Cisplatin
DB00720 Clodronate
DB00250 Dapsone
DB05804 dehydroepiandrosterone sulfate
DB00035 Desmopressin
DB00586 Diclofenac
DB00861 Diflunisal
DB00154 Dihomo-gamma-linolenic acid
DB01395 Drospirenone
DB00005 Etanercept
DB00749 Etodolac
DB00773 Etoposide
DB01628 Etoricoxib
DB00573 Fenoprofen
DB09217 Firocoxib
DB02266 Flufenamic Acid
DB00712 Flurbiprofen
DB01404 Ginseng
DB01050 Ibuprofen
DB00159 Icosapent
DB00328 Indomethacin
DB01009 Ketoprofen
DB00465 Ketorolac
DB00480 Lenalidomide
DB04725 Licofelone
DB06725 Lornoxicam
DB01283 Lumiracoxib
DB01397 Magnesium salicylate
DB00939 Meclofenamic acid
DB00784 Mefenamic acid
DB00814 Meloxicam
DB00244 Mesalazine
DB00461 Nabumetone
DB00788 Naproxen
DB06802 Nepafenac
DB04552 Niflumic Acid
DB04743 Nimesulide
DB06804 Nonoxynol-9
DB00991 Oxaprozin
DB08439 Parecoxib
DB00812 Phenylbutazone
DB00554 Piroxicam
DB08910 Pomalidomide
DB03866 Prostaglandin G2
DB02709 Resveratrol
DB00884 Risedronate
DB00533 Rofecoxib
DB00936 Salicylic acid
DB01399 Salsalate
DB00360 Sapropterin
DB05875 substance P
DB00795 Sulfasalazine
DB00605 Sulindac
DB00870 Suprofen
DB08819 Tafluprost
DB00469 Tenoxicam
DB01041 Thalidomide
DB01600 Tiaprofenic acid
DB00500 Tolmetin
DB00620 Triamcinolone
DB01401 Trisalicylate-choline
DB00580 Valdecoxib

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
1376

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
PTGS2

Domain mapping of disease mutations (DMDM)

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DMDMi
3915797

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 17Sequence analysisAdd BLAST17
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000002387518 – 604Prostaglandin G/H synthase 2Add BLAST587

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi21 ↔ 32Combined sources3 Publications
Disulfide bondi22 ↔ 145Combined sources3 Publications
Disulfide bondi26 ↔ 42Combined sources3 Publications
Disulfide bondi44 ↔ 54Combined sources3 Publications
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi53N-linked (GlcNAc...) asparagineCombined sources2 Publications1
Glycosylationi130N-linked (GlcNAc...) asparagineCombined sources3 Publications1
Glycosylationi396N-linked (GlcNAc...) asparagineCombined sources3 Publications1
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei526S-nitrosocysteine1 Publication1
Disulfide bondi555 ↔ 561Combined sources3 Publications
Glycosylationi580N-linked (GlcNAc...) asparagine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

S-nitrosylation by NOS2 (iNOS) activates enzyme activity. S-nitrosylation may take place on different Cys residues in addition to Cys-526.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, S-nitrosylation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P35354

MaxQB - The MaxQuant DataBase

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MaxQBi
P35354

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P35354

PeptideAtlas

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PeptideAtlasi
P35354

PRoteomics IDEntifications database

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PRIDEi
P35354

ProteomicsDB human proteome resource

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ProteomicsDBi
55035

PTM databases

GlyConnect protein glycosylation platform

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GlyConnecti
1649

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P35354

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P35354

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

By cytokines and mitogens.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000073756 Expressed in 186 organ(s), highest expression level in seminal vesicle

CleanEx database of gene expression profiles

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CleanExi
HS_PTGS2

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P35354 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P35354 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB000113
HPA001335

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer.2 Publications

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
111715, 36 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P35354

Database of interacting proteins

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DIPi
DIP-28131N

Protein interaction database and analysis system

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IntActi
P35354, 2 interactors

STRING: functional protein association networks

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STRINGi
9606.ENSP00000356438

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P35354

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1604
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P35354

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P35354

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini18 – 55EGF-likePROSITE-ProRule annotationAdd BLAST38

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the prostaglandin G/H synthase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG2408 Eukaryota
ENOG410XPZ3 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00390000010743

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000013149

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG000366

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P35354

KEGG Orthology (KO)

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KOi
K11987

Identification of Orthologs from Complete Genome Data

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OMAi
KGCPFTA

Database of Orthologous Groups

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OrthoDBi
EOG091G03CD

Database for complete collections of gene phylogenies

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PhylomeDBi
P35354

TreeFam database of animal gene trees

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TreeFami
TF329675

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.640.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR029576 COX-2
IPR000742 EGF-like_dom
IPR010255 Haem_peroxidase
IPR019791 Haem_peroxidase_animal
IPR037120 Haem_peroxidase_sf

The PANTHER Classification System

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PANTHERi
PTHR11903:SF8 PTHR11903:SF8, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF03098 An_peroxidase, 1 hit
PF00008 EGF, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00457 ANPEROXIDASE

Superfamily database of structural and functional annotation

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SUPFAMi
SSF48113 SSF48113, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS50026 EGF_3, 1 hit
PS50292 PEROXIDASE_3, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

P35354-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLARALLLCA VLALSHTANP CCSHPCQNRG VCMSVGFDQY KCDCTRTGFY
60 70 80 90 100
GENCSTPEFL TRIKLFLKPT PNTVHYILTH FKGFWNVVNN IPFLRNAIMS
110 120 130 140 150
YVLTSRSHLI DSPPTYNADY GYKSWEAFSN LSYYTRALPP VPDDCPTPLG
160 170 180 190 200
VKGKKQLPDS NEIVEKLLLR RKFIPDPQGS NMMFAFFAQH FTHQFFKTDH
210 220 230 240 250
KRGPAFTNGL GHGVDLNHIY GETLARQRKL RLFKDGKMKY QIIDGEMYPP
260 270 280 290 300
TVKDTQAEMI YPPQVPEHLR FAVGQEVFGL VPGLMMYATI WLREHNRVCD
310 320 330 340 350
VLKQEHPEWG DEQLFQTSRL ILIGETIKIV IEDYVQHLSG YHFKLKFDPE
360 370 380 390 400
LLFNKQFQYQ NRIAAEFNTL YHWHPLLPDT FQIHDQKYNY QQFIYNNSIL
410 420 430 440 450
LEHGITQFVE SFTRQIAGRV AGGRNVPPAV QKVSQASIDQ SRQMKYQSFN
460 470 480 490 500
EYRKRFMLKP YESFEELTGE KEMSAELEAL YGDIDAVELY PALLVEKPRP
510 520 530 540 550
DAIFGETMVE VGAPFSLKGL MGNVICSPAY WKPSTFGGEV GFQIINTASI
560 570 580 590 600
QSLICNNVKG CPFTSFSVPD PELIKTVTIN ASSSRSGLDD INPTVLLKER

STEL
Length:604
Mass (Da):68,996
Last modified:December 15, 1998 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i72FBD699F6128519
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q6ZYK7Q6ZYK7_HUMAN
Prostaglandin G/H synthase 2
PTGS2 COX-2
163Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti165E → G in AAA58433 (PubMed:1380156).Curated1
Sequence conflicti438I → T in AAA35803 (PubMed:8473346).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_016262228R → H1 PublicationCorresponds to variant dbSNP:rs3218622Ensembl.1
Natural variantiVAR_016263428P → A1 PublicationCorresponds to variant dbSNP:rs4648279Ensembl.1
Natural variantiVAR_011980488E → G. Corresponds to variant dbSNP:rs5272Ensembl.1
Natural variantiVAR_011981511V → A2 PublicationsCorresponds to variant dbSNP:rs5273Ensembl.1
Natural variantiVAR_016264587G → R1 PublicationCorresponds to variant dbSNP:rs3218625Ensembl.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
L15326 mRNA Translation: AAA35803.1
M90100 mRNA Translation: AAA58433.1
D28235 Genomic DNA Translation: BAA05698.1
U04636 Genomic DNA Translation: AAA57317.1
AY462100 mRNA Translation: AAR23927.1
AY229989 Genomic DNA Translation: AAO38056.1
AY382629 Genomic DNA Translation: AAQ75702.1
AK292167 mRNA Translation: BAF84856.1
AL033533 Genomic DNA No translation available.
CH471067 Genomic DNA Translation: EAW91216.1
BC013734 mRNA Translation: AAH13734.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS1371.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A46150

NCBI Reference Sequences

More...
RefSeqi
NP_000954.1, NM_000963.3

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.196384

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000367468; ENSP00000356438; ENSG00000073756

Database of genes from NCBI RefSeq genomes

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GeneIDi
5743

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:5743

UCSC genome browser

More...
UCSCi
uc001gsb.4 human

Keywords - Coding sequence diversityi

Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
NIEHS-SNPs
SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L15326 mRNA Translation: AAA35803.1
M90100 mRNA Translation: AAA58433.1
D28235 Genomic DNA Translation: BAA05698.1
U04636 Genomic DNA Translation: AAA57317.1
AY462100 mRNA Translation: AAR23927.1
AY229989 Genomic DNA Translation: AAO38056.1
AY382629 Genomic DNA Translation: AAQ75702.1
AK292167 mRNA Translation: BAF84856.1
AL033533 Genomic DNA No translation available.
CH471067 Genomic DNA Translation: EAW91216.1
BC013734 mRNA Translation: AAH13734.1
CCDSiCCDS1371.1
PIRiA46150
RefSeqiNP_000954.1, NM_000963.3
UniGeneiHs.196384

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1V0Xmodel-A1-604[»]
5F19X-ray2.04A/B19-569[»]
5F1AX-ray2.38A/B19-570[»]
5IKQX-ray2.41A/B19-569[»]
5IKRX-ray2.34A/B19-569[»]
5IKTX-ray2.45A/B19-569[»]
5IKVX-ray2.51A/B19-569[»]
5KIRX-ray2.70A/B19-569[»]
ProteinModelPortaliP35354
SMRiP35354
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111715, 36 interactors
CORUMiP35354
DIPiDIP-28131N
IntActiP35354, 2 interactors
STRINGi9606.ENSP00000356438

Chemistry databases

BindingDBiP35354
ChEMBLiCHEMBL230
DrugBankiDB03477 1-Phenylsulfonamide-3-Trifluoromethyl-5-Parabromophenylpyrazole
DB00316 Acetaminophen
DB00945 Acetylsalicylic acid
DB00041 Aldesleukin
DB00233 Aminosalicylic Acid
DB01435 Antipyrine
DB01419 Antrafenine
DB01014 Balsalazide
DB00963 Bromfenac
DB00887 Bumetanide
DB06774 Capsaicin
DB00821 Carprofen
DB00482 Celecoxib
DB00856 Chlorphenesin
DB05095 Cimicoxib
DB00515 Cisplatin
DB00720 Clodronate
DB00250 Dapsone
DB05804 dehydroepiandrosterone sulfate
DB00035 Desmopressin
DB00586 Diclofenac
DB00861 Diflunisal
DB00154 Dihomo-gamma-linolenic acid
DB01395 Drospirenone
DB00005 Etanercept
DB00749 Etodolac
DB00773 Etoposide
DB01628 Etoricoxib
DB00573 Fenoprofen
DB09217 Firocoxib
DB02266 Flufenamic Acid
DB00712 Flurbiprofen
DB01404 Ginseng
DB01050 Ibuprofen
DB00159 Icosapent
DB00328 Indomethacin
DB01009 Ketoprofen
DB00465 Ketorolac
DB00480 Lenalidomide
DB04725 Licofelone
DB06725 Lornoxicam
DB01283 Lumiracoxib
DB01397 Magnesium salicylate
DB00939 Meclofenamic acid
DB00784 Mefenamic acid
DB00814 Meloxicam
DB00244 Mesalazine
DB00461 Nabumetone
DB00788 Naproxen
DB06802 Nepafenac
DB04552 Niflumic Acid
DB04743 Nimesulide
DB06804 Nonoxynol-9
DB00991 Oxaprozin
DB08439 Parecoxib
DB00812 Phenylbutazone
DB00554 Piroxicam
DB08910 Pomalidomide
DB03866 Prostaglandin G2
DB02709 Resveratrol
DB00884 Risedronate
DB00533 Rofecoxib
DB00936 Salicylic acid
DB01399 Salsalate
DB00360 Sapropterin
DB05875 substance P
DB00795 Sulfasalazine
DB00605 Sulindac
DB00870 Suprofen
DB08819 Tafluprost
DB00469 Tenoxicam
DB01041 Thalidomide
DB01600 Tiaprofenic acid
DB00500 Tolmetin
DB00620 Triamcinolone
DB01401 Trisalicylate-choline
DB00580 Valdecoxib
GuidetoPHARMACOLOGYi1376
SwissLipidsiSLP:000000830

Protein family/group databases

PeroxiBasei3321 HsPGHS02

PTM databases

GlyConnecti1649
iPTMnetiP35354
PhosphoSitePlusiP35354

Polymorphism and mutation databases

BioMutaiPTGS2
DMDMi3915797

Proteomic databases

EPDiP35354
MaxQBiP35354
PaxDbiP35354
PeptideAtlasiP35354
PRIDEiP35354
ProteomicsDBi55035

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
5743
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000367468; ENSP00000356438; ENSG00000073756
GeneIDi5743
KEGGihsa:5743
UCSCiuc001gsb.4 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5743
DisGeNETi5743
EuPathDBiHostDB:ENSG00000073756.11

GeneCards: human genes, protein and diseases

More...
GeneCardsi
PTGS2
HGNCiHGNC:9605 PTGS2
HPAiCAB000113
HPA001335
MIMi600262 gene
neXtProtiNX_P35354
OpenTargetsiENSG00000073756
PharmGKBiPA293

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG2408 Eukaryota
ENOG410XPZ3 LUCA
GeneTreeiENSGT00390000010743
HOGENOMiHOG000013149
HOVERGENiHBG000366
InParanoidiP35354
KOiK11987
OMAiKGCPFTA
OrthoDBiEOG091G03CD
PhylomeDBiP35354
TreeFamiTF329675

Enzyme and pathway databases

UniPathwayi
UPA00662

BioCyciMetaCyc:HS01115-MONOMER
BRENDAi1.14.99.1 2681
ReactomeiR-HSA-197264 Nicotinamide salvaging
R-HSA-2142770 Synthesis of 15-eicosatetraenoic acid derivatives
R-HSA-2162123 Synthesis of Prostaglandins (PG) and Thromboxanes (TX)
R-HSA-6783783 Interleukin-10 signaling
R-HSA-6785807 Interleukin-4 and Interleukin-13 signaling
R-HSA-9018677 Biosynthesis of DHA-derived SPMs
R-HSA-9018679 Biosynthesis of EPA-derived SPMs
R-HSA-9025094 Biosynthesis of DPAn-3 SPMs
R-HSA-9027604 Biosynthesis of electrophilic Omega-3 PUFA oxo-derivatives
SABIO-RKiP35354
SIGNORiP35354

Miscellaneous databases

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
Prostaglandin-endoperoxide_synthase_2
PTGS2

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
5743

Protein Ontology

More...
PROi
PR:P35354

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000073756 Expressed in 186 organ(s), highest expression level in seminal vesicle
CleanExiHS_PTGS2
ExpressionAtlasiP35354 baseline and differential
GenevisibleiP35354 HS

Family and domain databases

Gene3Di1.10.640.10, 1 hit
InterProiView protein in InterPro
IPR029576 COX-2
IPR000742 EGF-like_dom
IPR010255 Haem_peroxidase
IPR019791 Haem_peroxidase_animal
IPR037120 Haem_peroxidase_sf
PANTHERiPTHR11903:SF8 PTHR11903:SF8, 1 hit
PfamiView protein in Pfam
PF03098 An_peroxidase, 1 hit
PF00008 EGF, 1 hit
PRINTSiPR00457 ANPEROXIDASE
SUPFAMiSSF48113 SSF48113, 1 hit
PROSITEiView protein in PROSITE
PS50026 EGF_3, 1 hit
PS50292 PEROXIDASE_3, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPGH2_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P35354
Secondary accession number(s): A8K802, Q16876
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: December 15, 1998
Last modified: December 5, 2018
This is version 200 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  7. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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