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Protein

Prostaglandin G/H synthase 2

Gene

Ptgs2

Organism
Mus musculus (Mouse)
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. 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.5 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. 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.

<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 the nonsteroidal anti-inflammatory drugs aspirin, naproxen, diclofenac, meclofenamic acid, indomethacin and their analogs.2 Publications

<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.4 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 sitei106SubstrateCombined sources1 Publication1
<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 Publication1
Binding sitei341SubstrateCombined sources1 Publication1
Active sitei371For cyclooxygenase activity1 Publication1
<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)Combined sources5 Publications1
<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

<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

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.14.99.1 3474

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-197264 Nicotinamide salvaging
R-MMU-2142770 Synthesis of 15-eicosatetraenoic acid derivatives
R-MMU-2162123 Synthesis of Prostaglandins (PG) and Thromboxanes (TX)
R-MMU-9018677 Biosynthesis of DHA-derived SPMs
R-MMU-9018679 Biosynthesis of EPA-derived SPMs
R-MMU-9025094 Biosynthesis of DPAn-3 SPMs
R-MMU-9027604 Biosynthesis of electrophilic Omega-3 PUFA oxo-derivatives

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

More...
UniPathwayi
UPA00662

Protein family/group databases

PeroxiBase, a peroxidase database

More...
PeroxiBasei
3360 MmPGHS02

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...
SwissLipidsi
SLP:000001129

<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:1.14.99.1)
Alternative name(s):
Cyclooxygenase-2
Short name:
COX-2
Glucocorticoid-regulated inflammatory cyclooxygenase
Gripghs
Macrophage activation-associated marker protein P71/73
PES-2
PHS II
Prostaglandin H2 synthase 2
Short name:
PGH synthase 2
Short name:
PGHS-2
Prostaglandin-endoperoxide synthase 2
TIS10 protein
<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:Cox-2, Cox2, Pghs-b, Tis10
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:97798 Ptgs2

<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

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Mutant mice exhibit defects in colonic mucosal wound repair.1 Publication

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>Mutagenesisi517L → A, F, P or T: Slightly reduced activity. 1 Publication1
Mutagenesisi580N → A: Loss of glycosylation site. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL4321

<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 – 17Add 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_000002387618 – 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 sources7 Publications
Disulfide bondi22 ↔ 145Combined sources7 Publications
Disulfide bondi26 ↔ 42Combined sources7 Publications
Disulfide bondi44 ↔ 54Combined sources7 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>GlycosylationiCAR_00022253N-linked (GlcNAc...) asparagineCombined sources8 Publications1
GlycosylationiCAR_000223130N-linked (GlcNAc...) asparagineCombined sources8 Publications1
GlycosylationiCAR_000224396N-linked (GlcNAc...) asparagineCombined sources8 Publications1
Disulfide bondi555 ↔ 561Combined sources7 Publications
GlycosylationiCAR_000225580N-linked (GlcNAc...) asparagine2 Publications1

<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 (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei592Not glycosylated1 Publication1

Keywords - PTMi

Disulfide bond, Glycoprotein, S-nitrosylation

Proteomic databases

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

More...
PaxDbi
Q05769

PeptideAtlas

More...
PeptideAtlasi
Q05769

PRoteomics IDEntifications database

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PRIDEi
Q05769

PTM databases

GlyConnect protein glycosylation platform

More...
GlyConnecti
514

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q05769

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

More...
PhosphoSitePlusi
Q05769

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
Q05769

UniCarbKB; an annotated and curated database of glycan structures

More...
UniCarbKBi
Q05769

<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 provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Following colon injury, expressed in the wound bed mesenchyme during the first phase of repair, probably by colonic mesenchymal stem cells (at protein level).1 Publication

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

During colonic wound repair, highly up-regulated (more than 1600-fold) in the mesenchyme of the wound bed 2 days after injury as compared to uninjured mucosa. Further increase in expression is observed at day 4 following injury (close to 2200-fold). Down-regulated at day 6 (only 93-fold increase as compared to uninjured mucosa).1 Publication

<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

More...
Bgeei
ENSMUSG00000032487 Expressed in 136 organ(s), highest expression level in cumulus cell

CleanEx database of gene expression profiles

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CleanExi
MM_PTGS2

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q05769 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q05769 MM

<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.6 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
Nos1Q9Z0J44EBI-298933,EBI-397596

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
202463, 6 interactors

Database of interacting proteins

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DIPi
DIP-31082N

Protein interaction database and analysis system

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IntActi
Q05769, 2 interactors

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000035065

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
Q05769

<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
Q05769

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

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SMRi
Q05769

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...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q05769

<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
Q05769

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
Q05769

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

More...
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

More...
SUPFAMi
SSF48113 SSF48113, 1 hit

PROSITE; a protein domain and family database

More...
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

Q05769-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLFRAVLLCA ALGLSQAANP CCSNPCQNRG ECMSTGFDQY KCDCTRTGFY
60 70 80 90 100
GENCTTPEFL TRIKLLLKPT PNTVHYILTH FKGVWNIVNN IPFLRSLIMK
110 120 130 140 150
YVLTSRSYLI DSPPTYNVHY GYKSWEAFSN LSYYTRALPP VADDCPTPMG
160 170 180 190 200
VKGNKELPDS KEVLEKVLLR REFIPDPQGS NMMFAFFAQH FTHQFFKTDH
210 220 230 240 250
KRGPGFTRGL GHGVDLNHIY GETLDRQHKL RLFKDGKLKY QVIGGEVYPP
260 270 280 290 300
TVKDTQVEMI YPPHIPENLQ FAVGQEVFGL VPGLMMYATI WLREHNRVCD
310 320 330 340 350
ILKQEHPEWG DEQLFQTSRL ILIGETIKIV IEDYVQHLSG YHFKLKFDPE
360 370 380 390 400
LLFNQQFQYQ NRIASEFNTL YHWHPLLPDT FNIEDQEYSF KQFLYNNSIL
410 420 430 440 450
LEHGLTQFVE SFTRQIAGRV AGGRNVPIAV QAVAKASIDQ SREMKYQSLN
460 470 480 490 500
EYRKRFSLKP YTSFEELTGE KEMAAELKAL YSDIDVMELY PALLVEKPRP
510 520 530 540 550
DAIFGETMVE LGAPFSLKGL MGNPICSPQY WKPSTFGGEV GFKIINTASI
560 570 580 590 600
QSLICNNVKG CPFTSFNVQD PQPTKTATIN ASASHSRLDD INPTVLIKRR

STEL
Length:604
Mass (Da):69,013
Last modified:June 1, 1994 - v1
<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:iDFE1658295C92064
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
A0A087WPT2A0A087WPT2_MOUSE
Prostaglandin G/H synthase 2
Ptgs2
62Annotation score:

Annotation score:3 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 conflicti98I → T in AAA39924 (PubMed:1712772).Curated1
Sequence conflicti142A → R in AAA39918 (PubMed:1419907).Curated1
Sequence conflicti301I → L no nucleotide entry (PubMed:1744122).Curated1
Sequence conflicti585H → R in AAA39918 (PubMed:1419907).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
M64291 mRNA Translation: AAA39924.1
M94967 mRNA Translation: AAA39918.1
M82866
, M82862, M82863, M82864, M82865 Genomic DNA Translation: AAA40448.1
M88242 mRNA Translation: AAA37740.1
AK049923 mRNA Translation: BAC33986.1
AK144956 mRNA Translation: BAE26154.1
AK166221 mRNA Translation: BAE38639.1
AK172161 mRNA Translation: BAE42855.1
CH466520 Genomic DNA Translation: EDL39487.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS15353.1

Protein sequence database of the Protein Information Resource

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PIRi
A49010

NCBI Reference Sequences

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RefSeqi
NP_035328.2, NM_011198.4

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Mm.292547

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSMUST00000035065; ENSMUSP00000035065; ENSMUSG00000032487

Database of genes from NCBI RefSeq genomes

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GeneIDi
19225

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:19225

UCSC genome browser

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UCSCi
uc007cxv.1 mouse

<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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64291 mRNA Translation: AAA39924.1
M94967 mRNA Translation: AAA39918.1
M82866
, M82862, M82863, M82864, M82865 Genomic DNA Translation: AAA40448.1
M88242 mRNA Translation: AAA37740.1
AK049923 mRNA Translation: BAC33986.1
AK144956 mRNA Translation: BAE26154.1
AK166221 mRNA Translation: BAE38639.1
AK172161 mRNA Translation: BAE42855.1
CH466520 Genomic DNA Translation: EDL39487.1
CCDSiCCDS15353.1
PIRiA49010
RefSeqiNP_035328.2, NM_011198.4
UniGeneiMm.292547

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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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
1CVUX-ray2.40A/B18-569[»]
1CX2X-ray3.00A/B/C/D18-604[»]
1DCXmodel-A/B18-569[»]
1DD0model-A/B18-569[»]
1DDXX-ray3.00A/B/C/D18-569[»]
1PXXX-ray2.90A/B/C/D1-604[»]
3HS5X-ray2.10A/B20-604[»]
3HS6X-ray2.40A/B20-604[»]
3HS7X-ray2.65A/B20-604[»]
3KRKX-ray2.40A/B20-604[»]
3LN0X-ray2.20A/B/C/D18-604[»]
3LN1X-ray2.40A/B/C/D18-604[»]
3MDLX-ray2.20A/B20-599[»]
3MQEX-ray2.80A/B/C/D18-604[»]
3NT1X-ray1.73A/B18-604[»]
3NTBX-ray2.27A/B/C/D18-604[»]
3NTGX-ray2.19A/B/C/D18-569[»]
3OLTX-ray2.45A/B20-604[»]
3OLUX-ray2.35A/B20-604[»]
3PGHX-ray2.50A/B/C/D18-604[»]
3Q7DX-ray2.40A/B18-604[»]
3QH0X-ray2.10A/B1-604[»]
3QMOX-ray3.00A/B1-604[»]
3RR3X-ray2.84A/B/C/D18-577[»]
3TZIX-ray2.15A/B20-604[»]
4COXX-ray2.90A/B/C/D18-604[»]
4E1GX-ray2.10A/B1-604[»]
4FM5X-ray2.81A/B/C/D1-604[»]
4M10X-ray2.01A/B/C/D18-604[»]
4M11X-ray2.45A/B/C/D18-569[»]
4OTJX-ray2.11A/B/C/D18-604[»]
4OTYX-ray2.35A/B18-604[»]
4PH9X-ray1.81A/B20-568[»]
4RRWX-ray2.57A/B/C/D18-604[»]
4RRXX-ray2.78A/B18-604[»]
4RRYX-ray2.43A/B/C/D18-604[»]
4RRZX-ray2.57A/B/C/D18-604[»]
4RS0X-ray2.81A18-604[»]
4RUTX-ray2.16A/B/C/D18-604[»]
4Z0LX-ray2.29A/B/C/D18-604[»]
5COXX-ray3.00A/B/C/D18-604[»]
5FDQX-ray1.90A/B20-604[»]
5JVYX-ray2.36A/B20-568[»]
5JVZX-ray2.62A/B20-569[»]
5JW1X-ray2.82A/B20-569[»]
5W58X-ray2.27A18-604[»]
6COXX-ray2.80A/B18-604[»]
ProteinModelPortaliQ05769
SMRiQ05769
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202463, 6 interactors
DIPiDIP-31082N
IntActiQ05769, 2 interactors
STRINGi10090.ENSMUSP00000035065

Chemistry databases

BindingDBiQ05769
ChEMBLiCHEMBL4321
SwissLipidsiSLP:000001129

Protein family/group databases

PeroxiBasei3360 MmPGHS02

PTM databases

GlyConnecti514
iPTMnetiQ05769
PhosphoSitePlusiQ05769
SwissPalmiQ05769
UniCarbKBiQ05769

Proteomic databases

PaxDbiQ05769
PeptideAtlasiQ05769
PRIDEiQ05769

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000035065; ENSMUSP00000035065; ENSMUSG00000032487
GeneIDi19225
KEGGimmu:19225
UCSCiuc007cxv.1 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5743
MGIiMGI:97798 Ptgs2

Phylogenomic databases

eggNOGiKOG2408 Eukaryota
ENOG410XPZ3 LUCA
GeneTreeiENSGT00390000010743
HOGENOMiHOG000013149
HOVERGENiHBG000366
InParanoidiQ05769
KOiK11987
OMAiKGCPFTA
OrthoDBiEOG091G03CD
PhylomeDBiQ05769
TreeFamiTF329675

Enzyme and pathway databases

UniPathwayi
UPA00662

BRENDAi1.14.99.1 3474
ReactomeiR-MMU-197264 Nicotinamide salvaging
R-MMU-2142770 Synthesis of 15-eicosatetraenoic acid derivatives
R-MMU-2162123 Synthesis of Prostaglandins (PG) and Thromboxanes (TX)
R-MMU-9018677 Biosynthesis of DHA-derived SPMs
R-MMU-9018679 Biosynthesis of EPA-derived SPMs
R-MMU-9025094 Biosynthesis of DPAn-3 SPMs
R-MMU-9027604 Biosynthesis of electrophilic Omega-3 PUFA oxo-derivatives

Miscellaneous databases

EvolutionaryTraceiQ05769

Protein Ontology

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PROi
PR:Q05769

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000032487 Expressed in 136 organ(s), highest expression level in cumulus cell
CleanExiMM_PTGS2
ExpressionAtlasiQ05769 baseline and differential
GenevisibleiQ05769 MM

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_MOUSE
<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: Q05769
Secondary accession number(s): Q543K3
<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: June 1, 1994
Last modified: December 5, 2018
This is version 196 of the entry and version 1 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

<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, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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