Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 161 (02 Dec 2020)
Sequence version 2 (30 May 2000)
Previous versions | rss
Add a publicationFeedback
Protein

Prostaglandin E synthase

Gene

PTGES

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

Terminal enzyme of the cyclooxygenase (COX)-2-mediated prostaglandin E2 (PGE2) biosynthetic pathway. Catalyzes the glutathione-dependent oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to prostaglandin E2 (PGE2) in response to inflammatory stimuli (PubMed:18682561, PubMed:10377395, PubMed:12672824, PubMed:12460774, PubMed:10869354, PubMed:12244105). Plays a key role in inflammation response, fever and pain (By similarity). Catalyzes also the oxidoreduction of endocannabinoids into prostaglandin glycerol esters and PGG2 into 15-hydroperoxy-PGE2 (PubMed:12244105, PubMed:12672824). In addition, displays low glutathione transferase and glutathione-dependent peroxidase activities, toward 1-chloro-2,4-dinitrobenzene and 5-hydroperoxyicosatetraenoic acid (5-HPETE), respectively (PubMed:12672824).By similarity6 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

glutathione5 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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

Induced by interleukin IL1B.1 Publication

<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

kcat is 50 sec(-1) for prostaglandin H2 as substrate (PubMed:12672824). kcat is 75 sec(-1) for prostaglandin H2 as substrate (PubMed:12672824). kcat is 21 sec(-1) for glutathione as substrate (PubMed:12672824).1 Publication
  1. KM=75 µM for glutathione1 Publication
  2. KM=160 µM for prostaglandin H2 (at 37 degrees)1 Publication
  3. KM=71 µM for glutathione (at 37 degrees)1 Publication
  4. KM=160 µM for prostaglandin G2 (at 37 degrees)1 Publication
  5. KM=14 µM for prostaglandin H21 Publication
  6. KM=130 µM for prostaglandin H21 Publication
  1. Vmax=170 µmol/min/mg enzyme with prostaglandin H2 as substrate1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'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.1 Publication
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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei38GlutathioneCombined sources2 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>Sitei49Essential for protaglandin-E synthase activity2 Publications1
Binding sitei113GlutathioneCombined sources2 Publications1
Binding sitei117GlutathioneCombined sources2 Publications1
Sitei126Essential for protaglandin-E synthase activity2 Publications1

<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 functionIsomerase, Oxidoreductase, Transferase
Biological processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Prostaglandin biosynthesis, Prostaglandin metabolism

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:HS07518-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
5.3.99.3, 2681

Pathway Commons web resource for biological pathway data

More...
PathwayCommonsi
O14684

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-2162123, Synthesis of Prostaglandins (PG) and Thromboxanes (TX)

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
O14684

SIGNOR Signaling Network Open Resource

More...
SIGNORi
O14684

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

More...
UniPathwayi
UPA00662

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...
SwissLipidsi
SLP:000001631

<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%5Fand%5Ftaxonomy%5Fsection">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 E synthase (EC:5.3.99.37 Publications)
Alternative name(s):
Glutathione peroxidase PTGES (EC:1.11.1.-1 Publication)
Glutathione transferase PTGES (EC:2.5.1.182 Publications)
Microsomal glutathione S-transferase 1-like 11 Publication
Short name:
MGST1-L11 Publication
Microsomal prostaglandin E synthase 11 Publication
Short name:
MPGES-11 Publication
p53-induced gene 12 protein1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:PTGES
Synonyms:MGST1L11 Publication, MPGES1, PGES, PIG121 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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 9

Organism-specific databases

Eukaryotic Pathogen and Host Database Resources

More...
EuPathDBi
HostDB:ENSG00000148344.10

Human Gene Nomenclature Database

More...
HGNCi
HGNC:9599, PTGES

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
605172, gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_O14684

<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 & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 12Lumenal1 PublicationAdd BLAST12
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei13 – 41Helical1 PublicationAdd BLAST29
Topological domaini42 – 60Cytoplasmic1 PublicationAdd BLAST19
Transmembranei61 – 90Helical1 PublicationAdd BLAST30
Topological domaini91 – 95Lumenal1 Publication5
Transmembranei96 – 119Helical1 PublicationAdd BLAST24
Topological domaini120 – 123Cytoplasmic1 Publication4
Transmembranei124 – 152Helical1 PublicationAdd BLAST29

Keywords - Cellular componenti

Cytoplasm, Membrane

<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%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi36Q → E: Keeps about 40-50% of prostaglandin-E synthase activity. 1 Publication1
Mutagenesisi49D → A: Loss of prostaglandin-E synthase activity. 1 Publication1
Mutagenesisi49D → N: Loss of prostaglandin-E synthase activity. 1 Publication1
Mutagenesisi66E → A: Reduces protaglandin-E synthase activity by 50%. 1 Publication1
Mutagenesisi67R → A: Loss of prostaglandin-E synthase activity. 1 Publication1
Mutagenesisi70R → A: Slightly reduced protaglandin-E synthase activity. 1 Publication1
Mutagenesisi70R → S: No effect on protaglandin-E synthase activity. 1 Publication1
Mutagenesisi72H → A: Reduces protaglandin-E synthase activity by 70%. 1 Publication1
Mutagenesisi73R → A: Retains partial of protaglandin-E synthase activity. 1 Publication1
Mutagenesisi73R → L: Loss of protaglandin-E synthase activity. 1 Publication1
Mutagenesisi110R → A or S: Loss of protaglandin-E synthase activity. 2 Publications1
Mutagenesisi110R → T: Retains 17.8% of protaglandin-E synthase activity. 1 Publication1
Mutagenesisi114T → V: Retains 21.3% activity of protaglandin-E synthase activity. 1 Publication1
Mutagenesisi117Y → A: Loss of protaglandin-E synthase activity. 1 Publication1
Mutagenesisi117Y → F: No effect on protaglandin-E synthase activity. 2 Publications1
Mutagenesisi126R → A or L: Loss of prostaglandin-E synthase activity. 1 Publication1
Mutagenesisi126R → K: Loss of prostaglandin-E synthase activity. Transforms prostaglandin-E synthase activity to prostaglandin-F(2alpha)synthase activity. 1 Publication1
Mutagenesisi126R → Q: Loss of prostaglandin-E synthase activity. 1 Publication1
Mutagenesisi127S → A: No effect on protaglandin-E synthase activity. 2 Publications1
Mutagenesisi130Y → I: Loss of protaglandin-E synthase activity. 1 Publication1
Mutagenesisi134Q → E: Keeps about 40-50% of prostaglandin-E synthase activity. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
9536

Open Targets

More...
OpenTargetsi
ENSG00000148344

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA33948

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...
Pharosi
O14684, Tchem

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL5658

DrugCentral

More...
DrugCentrali
O14684

IUPHAR/BPS Guide to PHARMACOLOGY

More...
GuidetoPHARMACOLOGYi
1377

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
PTGES

<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 describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002177451 – 152Prostaglandin E synthaseAdd BLAST152

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
O14684

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
O14684

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...
MassIVEi
O14684

MaxQB - The MaxQuant DataBase

More...
MaxQBi
O14684

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

More...
PaxDbi
O14684

PeptideAtlas

More...
PeptideAtlasi
O14684

PRoteomics IDEntifications database

More...
PRIDEi
O14684

ProteomicsDB: a multi-organism proteome resource

More...
ProteomicsDBi
48167

Consortium for Top Down Proteomics

More...
TopDownProteomicsi
O14684

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
O14684

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

More...
PhosphoSitePlusi
O14684

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
O14684

<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

Induced by the interleukin IL1B (PubMed:10377395, PubMed:10760517). Induced By p53/TP53 (PubMed:9305847).3 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000148344, Expressed in palpebral conjunctiva and 196 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
O14684, HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
ENSG00000148344, Group enriched (ductus deferens, placenta, seminal vesicle)

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homotrimer.

2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
114912, 21 interactors

Protein interaction database and analysis system

More...
IntActi
O14684, 19 interactors

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000342385

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
O14684

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
O14684, protein

<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

1152
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
O14684

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
O14684

<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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni73 – 77Glutathione bindingCombined sources2 Publications5
Regioni126 – 130Glutathione bindingCombined sources2 Publications5

<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 MAPEG family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG502RZBK, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00390000011980

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_105467_1_1_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
O14684

Identification of Orthologs from Complete Genome Data

More...
OMAi
IKMYAVA

Database for complete collections of gene phylogenies

More...
PhylomeDBi
O14684

TreeFam database of animal gene trees

More...
TreeFami
TF105327

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.20.120.550, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR023352, MAPEG-like_dom_sf
IPR001129, Membr-assoc_MAPEG
IPR040162, MGST1-like

The PANTHER Classification System

More...
PANTHERi
PTHR10689, PTHR10689, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01124, MAPEG, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF161084, SSF161084, 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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

O14684-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPAHSLVMSS PALPAFLLCS TLLVIKMYVV AIITGQVRLR KKAFANPEDA
60 70 80 90 100
LRHGGPQYCR SDPDVERCLR AHRNDMETIY PFLFLGFVYS FLGPNPFVAW
110 120 130 140 150
MHFLVFLVGR VAHTVAYLGK LRAPIRSVTY TLAQLPCASM ALQILWEAAR

HL
Length:152
Mass (Da):17,102
Last modified:May 30, 2000 - 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:iBF9B9ED81CA67A3D
GO

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 conflicti55G → GG in AAC39534 (PubMed:9305847).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AF010316 mRNA Translation: AAC39534.1
AF027740 mRNA Translation: AAB82299.1
AJ271802, AJ271803, AJ271804 Genomic DNA Translation: CAB72099.1
AK311947 mRNA Translation: BAG34888.1
EF543149 Genomic DNA Translation: ABQ01233.1
AL590369 Genomic DNA No translation available.
AL592219 Genomic DNA No translation available.
BC008280 mRNA Translation: AAH08280.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS6927.1

NCBI Reference Sequences

More...
RefSeqi
NP_004869.1, NM_004878.4

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000340607; ENSP00000342385; ENSG00000148344

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
9536

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:9536

UCSC genome browser

More...
UCSCi
uc004byi.4, human

<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
AF010316 mRNA Translation: AAC39534.1
AF027740 mRNA Translation: AAB82299.1
AJ271802, AJ271803, AJ271804 Genomic DNA Translation: CAB72099.1
AK311947 mRNA Translation: BAG34888.1
EF543149 Genomic DNA Translation: ABQ01233.1
AL590369 Genomic DNA No translation available.
AL592219 Genomic DNA No translation available.
BC008280 mRNA Translation: AAH08280.1
CCDSiCCDS6927.1
RefSeqiNP_004869.1, NM_004878.4

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3DWWelectron microscopy3.50A/B/C1-152[»]
4AL0X-ray1.16A1-152[»]
4AL1X-ray1.95A1-152[»]
4BPMX-ray2.08A10-152[»]
4WABX-ray2.70A10-151[»]
4YK5X-ray1.42A2-152[»]
4YL0X-ray1.52A5-152[»]
4YL1X-ray1.41A5-152[»]
4YL3X-ray1.41A5-152[»]
5BQGX-ray1.44A2-152[»]
5BQHX-ray1.60A2-152[»]
5BQIX-ray1.88A2-152[»]
5K0IX-ray1.30A2-152[»]
5T36X-ray1.40A2-152[»]
5T37X-ray1.76A2-152[»]
5TL9X-ray1.20A2-152[»]
SMRiO14684
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi114912, 21 interactors
IntActiO14684, 19 interactors
STRINGi9606.ENSP00000342385

Chemistry databases

BindingDBiO14684
ChEMBLiCHEMBL5658
DrugCentraliO14684
GuidetoPHARMACOLOGYi1377
SwissLipidsiSLP:000001631

PTM databases

iPTMnetiO14684
PhosphoSitePlusiO14684
SwissPalmiO14684

Polymorphism and mutation databases

BioMutaiPTGES

Proteomic databases

EPDiO14684
jPOSTiO14684
MassIVEiO14684
MaxQBiO14684
PaxDbiO14684
PeptideAtlasiO14684
PRIDEiO14684
ProteomicsDBi48167
TopDownProteomicsiO14684

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...
Antibodypediai
17900, 209 antibodies

Genome annotation databases

EnsembliENST00000340607; ENSP00000342385; ENSG00000148344
GeneIDi9536
KEGGihsa:9536
UCSCiuc004byi.4, human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
9536
DisGeNETi9536
EuPathDBiHostDB:ENSG00000148344.10

GeneCards: human genes, protein and diseases

More...
GeneCardsi
PTGES
HGNCiHGNC:9599, PTGES
HPAiENSG00000148344, Group enriched (ductus deferens, placenta, seminal vesicle)
MIMi605172, gene
neXtProtiNX_O14684
OpenTargetsiENSG00000148344
PharmGKBiPA33948

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiENOG502RZBK, Eukaryota
GeneTreeiENSGT00390000011980
HOGENOMiCLU_105467_1_1_1
InParanoidiO14684
OMAiIKMYAVA
PhylomeDBiO14684
TreeFamiTF105327

Enzyme and pathway databases

UniPathwayiUPA00662
BioCyciMetaCyc:HS07518-MONOMER
BRENDAi5.3.99.3, 2681
PathwayCommonsiO14684
ReactomeiR-HSA-2162123, Synthesis of Prostaglandins (PG) and Thromboxanes (TX)
SABIO-RKiO14684
SIGNORiO14684

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...
BioGRID-ORCSi
9536, 2 hits in 846 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
PTGES, human
EvolutionaryTraceiO14684

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
PTGES

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

More...
GenomeRNAii
9536
PharosiO14684, Tchem

Protein Ontology

More...
PROi
PR:O14684
RNActiO14684, protein

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000148344, Expressed in palpebral conjunctiva and 196 other tissues
GenevisibleiO14684, HS

Family and domain databases

Gene3Di1.20.120.550, 1 hit
InterProiView protein in InterPro
IPR023352, MAPEG-like_dom_sf
IPR001129, Membr-assoc_MAPEG
IPR040162, MGST1-like
PANTHERiPTHR10689, PTHR10689, 1 hit
PfamiView protein in Pfam
PF01124, MAPEG, 1 hit
SUPFAMiSSF161084, SSF161084, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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 nameiPTGES_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: O14684
Secondary accession number(s): O14900, Q5SZC0
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: December 2, 2020
This is version 161 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, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again