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Entry version 214 (25 May 2022)
Sequence version 2 (11 Jan 2011)
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Protein

Cytosolic phospholipase A2

Gene

PLA2G4A

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

Has primarily calcium-dependent phospholipase and lysophospholipase activities, with a major role in membrane lipid remodeling and biosynthesis of lipid mediators of the inflammatory response (PubMed:7794891, PubMed:8619991, PubMed:8702602, PubMed:9425121, PubMed:10358058, PubMed:14709560, PubMed:16617059, PubMed:17472963, PubMed:27642067, PubMed:18451993).

Plays an important role in embryo implantation and parturition through its ability to trigger prostanoid production (By similarity).

Preferentially hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity) (PubMed:7794891, PubMed:8619991, PubMed:9425121, PubMed:10358058, PubMed:17472963, PubMed:18451993).

Selectively hydrolyzes sn-2 arachidonoyl group from membrane phospholipids, providing the precursor for eicosanoid biosynthesis via the cyclooxygenase pathway (PubMed:18451993, PubMed:7794891, PubMed:9425121, PubMed:10358058, PubMed:17472963).

In an alternative pathway of eicosanoid biosynthesis, hydrolyzes sn-2 fatty acyl chain of eicosanoid lysophopholipids to release free bioactive eicosanoids (PubMed:27642067).

Hydrolyzes the ester bond of the fatty acyl group attached at sn-1 position of phospholipids (phospholipase A1 activity) only if an ether linkage rather than an ester linkage is present at the sn-2 position. This hydrolysis is not stereospecific (PubMed:7794891).

Has calcium-independent phospholipase A2 and lysophospholipase activities in the presence of phosphoinositides (PubMed:12672805).

Has O-acyltransferase activity. Catalyzes the transfer of fatty acyl chains from phospholipids to a primary hydroxyl group of glycerol (sn-1 or sn-3), potentially contributing to monoacylglycerol synthesis (PubMed:7794891).

By similarity11 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 <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

Activated by cytosolic calcium, which is necessary for binding to membrane lipids (PubMed:12672805). Activated by phosphorylation in response to mitogenic stimuli (PubMed:8381049). Activated by ceramide-1-phosphate. Binding (via C2 domain) to ceramide-1-phosphate increases the affinity for membrane lipids (PubMed:17472963). Can be activated by phosphoinositides in the absence of calcium (PubMed:12672805). Inhibited by ANXA5 in a calcium- and substrate-dependent way (PubMed:9425121).4 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. Vmax=2.7 µmol/min/mg enzyme toward 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine (phospholipase A2 activity)1 Publication
  2. Vmax=4.6 µmol/min/mg enzyme toward 1-hexadecanoyl-sn-glycero-3-phosphocholine (lysophospholipase activity)1 Publication
  3. Vmax=24.5 nmol/min/mg enzyme toward 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine (phospholipase A2 activity in the absence of ceramide-1-phosphate)1 Publication
  4. Vmax=240.5 nmol/min/mg enzyme toward 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine (phospholipase A2 activity, in the presence of ceramide-1-phosphate)1 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: glycerophospholipid metabolism

This protein is involved in the pathway glycerophospholipid metabolism, which is part of Membrane lipid metabolism.By similarity
View all proteins of this organism that are known to be involved in the pathway glycerophospholipid metabolism and in Membrane lipid metabolism.

Pathwayi: arachidonate metabolism

This protein is involved in the pathway arachidonate metabolism, which is part of Lipid metabolism.1 Publication
View all proteins of this organism that are known to be involved in the pathway arachidonate metabolism and in Lipid metabolism.

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.

Pathwayi: leukotriene B4 biosynthesis

This protein is involved in the pathway leukotriene B4 biosynthesis, which is part of Lipid metabolism.1 Publication
View all proteins of this organism that are known to be involved in the pathway leukotriene B4 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 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 bindingi40Calcium 11
Metal bindingi40Calcium 21
Metal bindingi41Calcium 1; via carbonyl oxygen1
Metal bindingi43Calcium 11
Metal bindingi43Calcium 21
Metal bindingi65Calcium 11
Metal bindingi93Calcium 21
Metal bindingi94Calcium 2; via carbonyl oxygen1
Metal bindingi95Calcium 21
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei228Nucleophile4 Publications1
Active sitei549Proton acceptor2 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 functionHydrolase
Biological processFatty acid biosynthesis, Fatty acid metabolism, Glycerol metabolism, Leukotriene biosynthesis, Lipid biosynthesis, Lipid degradation, Lipid metabolism, Phospholipid degradation, Phospholipid metabolism, Prostaglandin biosynthesis, Prostaglandin metabolism
LigandCalcium, Lipid-binding, Metal-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

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BRENDAi
3.1.1.4, 2681

Pathway Commons web resource for biological pathway data

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PathwayCommonsi
P47712

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-111995, phospho-PLA2 pathway
R-HSA-1482788, Acyl chain remodelling of PC
R-HSA-1482798, Acyl chain remodeling of CL
R-HSA-1482801, Acyl chain remodelling of PS
R-HSA-1482839, Acyl chain remodelling of PE
R-HSA-1482922, Acyl chain remodelling of PI
R-HSA-1482925, Acyl chain remodelling of PG
R-HSA-1483115, Hydrolysis of LPC
R-HSA-1483166, Synthesis of PA
R-HSA-2142753, Arachidonic acid metabolism
R-HSA-418592, ADP signalling through P2Y purinoceptor 1
R-HSA-432142, Platelet sensitization by LDL
R-HSA-6811436, COPI-independent Golgi-to-ER retrograde traffic

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
P47712

SIGNOR Signaling Network Open Resource

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SIGNORi
P47712

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

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UniPathwayi
UPA00383
UPA00662
UPA00878
UPA00940

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...
SwissLipidsi
SLP:000000565

<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:
Cytosolic phospholipase A2
Short name:
cPLA2
Alternative name(s):
Phospholipase A2 group IVA
Including the following 2 domains:
Phospholipase A2 (EC:3.1.1.46 Publications)
Alternative name(s):
Phosphatidylcholine 2-acylhydrolase
Lysophospholipase (EC:3.1.1.52 Publications)
<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:PLA2G4A
Synonyms:CPLA2, PLA2G4
<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 1

Organism-specific databases

Human Gene Nomenclature Database

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HGNCi
HGNC:9035, PLA2G4A

Online Mendelian Inheritance in Man (OMIM)

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MIMi
600522, gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P47712

Eukaryotic Pathogen, Vector and Host Database Resources

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VEuPathDBi
HostDB:ENSG00000116711

<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

Keywords - Cellular componenti

Cytoplasm, Golgi apparatus, Membrane, Nucleus

<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 provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Gastrointestinal ulceration, recurrent, with dysfunctional platelets (GURDP)3 Publications
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive disorder characterized by recurrent gastrointestinal mucosal ulcers, gastrointestinal bleeding, chronic anemia, iron deficiency, and abdominal pain. Disease features also include platelet dysfunction, and globally decreased eicosanoid synthesis.
Related information in OMIM
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_070778111S → P in GURDP; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs121434634EnsemblClinVar.1
Natural variantiVAR_070779485R → H in GURDP; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs121434635EnsemblClinVar.1
Natural variantiVAR_082091575D → H in GURDP; decreased protein expression, if any, in platelets from homozygous patients. 1 PublicationCorresponds to variant dbSNP:rs1557895416EnsemblClinVar.1

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>Mutagenesisi43D → N: Impairs phospholipase A2 and lysophospholipase activities in the absence of phosphoinositides. Has full activity in the presence of phosphoinositides. 1 Publication1
Mutagenesisi57 – 59RKR → AAA: Impairs binding to ceramide-1-phosphate. 1 Publication3
Mutagenesisi139C → A: No effect on phospholipase activity; when associated with A-141 and A-151. 1 Publication1
Mutagenesisi141C → A: No effect on phospholipase activity; when associated with A-139 and A-151. 1 Publication1
Mutagenesisi151C → A: No effect on phospholipase activity; when associated with A-139 and A-141. 1 Publication1
Mutagenesisi195S → A: 5-fold reduced phospholipase and lysophospholipase activities. 100-fold reduced phospholipase and lysophospholipase activities; when associated with A-577. 1 Publication1
Mutagenesisi200R → A or H: Abolishes phospholipase activity. 1 Publication1
Mutagenesisi200R → K: Reduces phospholipase activity 200-fold. 1 Publication1
Mutagenesisi215S → A: No effect on phospholipase or lysophospholipase activity. 1 Publication1
Mutagenesisi220C → A: No effect on phospholipase activity. 1 Publication1
Mutagenesisi228S → A, C or T: Abolishes both phospholipase and lysophospholipase activities. 3 Publications1
Mutagenesisi324C → A: No effect on phospholipase activity; when associated with A-331. 1 Publication1
Mutagenesisi331C → A: No effect on phospholipase activity; when associated with A-324. 1 Publication1
Mutagenesisi437S → A: Reduces phospholipase A2 activity; when associated with A-454; A-505 and A-727. 1 Publication1
Mutagenesisi454S → A: Reduces phospholipase A2 activity; when associated with A-437; A-505 and A-727. 1 Publication1
Mutagenesisi488K → E: Impairs phosphoinositide-stimulated phospholipase A2 activity. 1 Publication1
Mutagenesisi505S → A: Decreases agonist-stimulated release of arachidonic acid. Reduces phospholipase A2 activity; when associated with A-437; A-454 and A-727. 2 Publications1
Mutagenesisi541K → A: Impairs phosphoinositide-stimulated phospholipase A2 activity; when associated with A-543 and A-544. 1 Publication1
Mutagenesisi543K → A: Impairs phosphoinositide-stimulated phospholipase A2 activity.; when associated with A-541 and A-544. 1 Publication1
Mutagenesisi544K → A: Impairs phosphoinositide-stimulated phospholipase A2 activity.; when associated with A-541 and A-543. 1 Publication1
Mutagenesisi549D → A: Abolishes phospholipiase activity. 1 Publication1
Mutagenesisi549D → E: Reduces phospholipase activity 2000-fold. 1 Publication1
Mutagenesisi549D → N: Reduces phospholipase activity 300-fold. 1 Publication1
Mutagenesisi577S → A: 7-fold reduced phospholipase and lysophospholipase activities. 100-fold reduced phospholipase and lysophospholipase activities; when associated with A-195. 1 Publication1
Mutagenesisi620C → A: No effect on phospholipase activity; when associated with A-634. 1 Publication1
Mutagenesisi634C → A: No effect on phospholipase activity; when associated with A-620. 1 Publication1
Mutagenesisi726C → A: No effect on phospholipase activity. 1 Publication1
Mutagenesisi727S → A: Reduces phospholipase A2 activity; when associated with A-437; A-455 and A-505. 1 Publication1

Keywords - Diseasei

Disease variant

Organism-specific databases

DisGeNET

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DisGeNETi
5321

MalaCards human disease database

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MalaCardsi
PLA2G4A
MIMi618372, phenotype

Open Targets

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OpenTargetsi
ENSG00000116711

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
468635, Cryptogenic multifocal ulcerous stenosing enteritis
477787, Cytosolic phospholipase-A2 alpha deficiency associated bleeding disorder

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA271

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

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Pharosi
P47712, Tchem

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL3816

Drug and drug target database

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DrugBanki
DB00041, Aldesleukin
DB00411, Carbamoylcholine
DB00578, Carbenicillin
DB06311, Darapladib
DB00445, Epirubicin
DB13867, Fluticasone
DB00588, Fluticasone propionate
DB05029, Lancovutide
DB04552, Niflumic acid
DB01083, Orlistat
DB00721, Procaine
DB01103, Quinacrine
DB00086, Streptokinase
DB04786, Suramin
DB04827, Urethane

DrugCentral

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DrugCentrali
P47712

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
1424

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
PLA2G4A

Domain mapping of disease mutations (DMDM)

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DMDMi
317373312

<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_00001872621 – 749Cytosolic phospholipase A2Add BLAST749

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 residuei2PhosphoserineCombined sources1
Modified residuei268PhosphothreonineCombined sources1
Modified residuei434PhosphoserineBy similarity1
Modified residuei435PhosphoserineCombined sources1
Modified residuei437PhosphoserineCombined sources1
Modified residuei505Phosphoserine; by MAPK2 Publications1
Modified residuei515PhosphoserineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki541Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki606Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei727PhosphoserineCombined sources1 Publication1
Modified residuei729PhosphoserineCombined sources1

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

Phosphorylated at both Ser-505 and Ser-727 in response to mitogenic stimuli.2 Publications

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P47712

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P47712

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
P47712

MaxQB - The MaxQuant DataBase

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MaxQBi
P47712

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

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PaxDbi
P47712

PeptideAtlas

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PeptideAtlasi
P47712

PRoteomics IDEntifications database

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PRIDEi
P47712

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
55788

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P47712

MetOSite database of methionine sulfoxide sites

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MetOSitei
P47712

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

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PhosphoSitePlusi
P47712

<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

Expressed in various cells and tissues such as macrophages, neutrophils, fibroblasts and lung endothelium. Expressed in platelets (at protein level) (PubMed:25102815).1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000116711, Expressed in seminal vesicle and 204 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P47712, HS

Organism-specific databases

Human Protein Atlas

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HPAi
ENSG00000116711, Tissue enhanced (parathyroid gland, 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

Interacts with KAT5.

4 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

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BioGRIDi
111338, 41 interactors

Database of interacting proteins

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DIPi
DIP-40991N

Protein interaction database and analysis system

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IntActi
P47712, 16 interactors

Molecular INTeraction database

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MINTi
P47712

STRING: functional protein association networks

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STRINGi
9606.ENSP00000356436

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P47712

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

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RNActi
P47712, 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

1749
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

AlphaFold Protein Structure Database

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AlphaFoldDBi
P47712

Biological Magnetic Resonance Data Bank

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BMRBi
P47712

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

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SMRi
P47712

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P47712

<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%5Fand%5Fdomains%5Fsection">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>Domaini6 – 122C2PROSITE-ProRule annotationAdd BLAST117
Domaini140 – 740PLA2cPROSITE-ProRule annotationAdd BLAST601

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>Regioni1 – 178Phospholipid bindingCuratedAdd BLAST178
Regioni409 – 457DisorderedSequence analysisAdd BLAST49

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi420 – 452Basic and acidic residuesSequence analysisAdd BLAST33

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The N-terminal C2 domain associates with lipid membranes upon calcium binding. It modulates enzyme activity by presenting the active site to its substrate in response to elevations of cytosolic calcium (PubMed:9430701, PubMed:9665851, PubMed:11375391). In the presence of phosphoinositides, regulates phospholipase A2 and lysophospholipase activities in a calcium-independent way (PubMed:12672805).4 Publications

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG1012, Eukaryota
KOG1325, Eukaryota

Ensembl GeneTree

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GeneTreei
ENSGT01030000234606

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
CLU_011663_1_1_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P47712

Identification of Orthologs from Complete Genome Data

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OMAi
KFFMGKV

Database of Orthologous Groups

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OrthoDBi
302848at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P47712

TreeFam database of animal gene trees

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TreeFami
TF325228

Family and domain databases

Conserved Domains Database

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CDDi
cd04036, C2_cPLA2, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.60.40.150, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR016035, Acyl_Trfase/lysoPLipase
IPR041847, C2_cPLA2
IPR000008, C2_dom
IPR035892, C2_domain_sf
IPR002642, LysoPLipase_cat_dom

Pfam protein domain database

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Pfami
View protein in Pfam
PF00168, C2, 1 hit
PF01735, PLA2_B, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00239, C2, 1 hit
SM00022, PLAc, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF49562, SSF49562, 1 hit
SSF52151, SSF52151, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS50004, C2, 1 hit
PS51210, PLA2C, 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.

P47712-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSFIDPYQHI IVEHQYSHKF TVVVLRATKV TKGAFGDMLD TPDPYVELFI
60 70 80 90 100
STTPDSRKRT RHFNNDINPV WNETFEFILD PNQENVLEIT LMDANYVMDE
110 120 130 140 150
TLGTATFTVS SMKVGEKKEV PFIFNQVTEM VLEMSLEVCS CPDLRFSMAL
160 170 180 190 200
CDQEKTFRQQ RKEHIRESMK KLLGPKNSEG LHSARDVPVV AILGSGGGFR
210 220 230 240 250
AMVGFSGVMK ALYESGILDC ATYVAGLSGS TWYMSTLYSH PDFPEKGPEE
260 270 280 290 300
INEELMKNVS HNPLLLLTPQ KVKRYVESLW KKKSSGQPVT FTDIFGMLIG
310 320 330 340 350
ETLIHNRMNT TLSSLKEKVN TAQCPLPLFT CLHVKPDVSE LMFADWVEFS
360 370 380 390 400
PYEIGMAKYG TFMAPDLFGS KFFMGTVVKK YEENPLHFLM GVWGSAFSIL
410 420 430 440 450
FNRVLGVSGS QSRGSTMEEE LENITTKHIV SNDSSDSDDE SHEPKGTENE
460 470 480 490 500
DAGSDYQSDN QASWIHRMIM ALVSDSALFN TREGRAGKVH NFMLGLNLNT
510 520 530 540 550
SYPLSPLSDF ATQDSFDDDE LDAAVADPDE FERIYEPLDV KSKKIHVVDS
560 570 580 590 600
GLTFNLPYPL ILRPQRGVDL IISFDFSARP SDSSPPFKEL LLAEKWAKMN
610 620 630 640 650
KLPFPKIDPY VFDREGLKEC YVFKPKNPDM EKDCPTIIHF VLANINFRKY
660 670 680 690 700
RAPGVPRETE EEKEIADFDI FDDPESPFST FNFQYPNQAF KRLHDLMHFN
710 720 730 740
TLNNIDVIKE AMVESIEYRR QNPSRCSVSL SNVEARRFFN KEFLSKPKA
Length:749
Mass (Da):85,239
Last modified:January 11, 2011 - 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:iEE71CA0EBE617856
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_029276103G → R. Corresponds to variant dbSNP:rs28395828Ensembl.1
Natural variantiVAR_070778111S → P in GURDP; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs121434634EnsemblClinVar.1
Natural variantiVAR_018760224V → I1 PublicationCorresponds to variant dbSNP:rs12720588EnsemblClinVar.1
Natural variantiVAR_035826442H → Q in a breast cancer sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs370896190Ensembl.1
Natural variantiVAR_070779485R → H in GURDP; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs121434635EnsemblClinVar.1
Natural variantiVAR_082091575D → H in GURDP; decreased protein expression, if any, in platelets from homozygous patients. 1 PublicationCorresponds to variant dbSNP:rs1557895416EnsemblClinVar.1
Natural variantiVAR_062128637I → V. Corresponds to variant dbSNP:rs28395831EnsemblClinVar.1
Natural variantiVAR_018424651R → K5 PublicationsCorresponds to variant dbSNP:rs2307198Ensembl.1

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
M72393 mRNA Translation: AAB00789.1
M68874 mRNA Translation: AAA60105.1
AY552098 Genomic DNA Translation: AAS45712.1
AL022147 Genomic DNA No translation available.
AL049797 Genomic DNA No translation available.
BC114340 mRNA Translation: AAI14341.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS1372.1

Protein sequence database of the Protein Information Resource

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PIRi
A39329

NCBI Reference Sequences

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RefSeqi
NP_001298122.1, NM_001311193.1
NP_077734.1, NM_024420.2
XP_011507944.1, XM_011509642.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000367466.4; ENSP00000356436.3; ENSG00000116711.10

Database of genes from NCBI RefSeq genomes

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GeneIDi
5321

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:5321

Matched Annotation from NCBI and EMBL-EBI (MANE) - Phase one

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MANE-Selecti
ENST00000367466.4; ENSP00000356436.3; NM_024420.3; NP_077734.2

UCSC genome browser

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UCSCi
uc001gsc.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

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

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M72393 mRNA Translation: AAB00789.1
M68874 mRNA Translation: AAA60105.1
AY552098 Genomic DNA Translation: AAS45712.1
AL022147 Genomic DNA No translation available.
AL049797 Genomic DNA No translation available.
BC114340 mRNA Translation: AAI14341.1
CCDSiCCDS1372.1
PIRiA39329
RefSeqiNP_001298122.1, NM_001311193.1
NP_077734.1, NM_024420.2
XP_011507944.1, XM_011509642.2

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
1BCINMR-A1-138[»]
1CJYX-ray2.50A/B1-749[»]
1RLWX-ray2.40A17-141[»]
AlphaFoldDBiP47712
BMRBiP47712
SMRiP47712
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi111338, 41 interactors
DIPiDIP-40991N
IntActiP47712, 16 interactors
MINTiP47712
STRINGi9606.ENSP00000356436

Chemistry databases

BindingDBiP47712
ChEMBLiCHEMBL3816
DrugBankiDB00041, Aldesleukin
DB00411, Carbamoylcholine
DB00578, Carbenicillin
DB06311, Darapladib
DB00445, Epirubicin
DB13867, Fluticasone
DB00588, Fluticasone propionate
DB05029, Lancovutide
DB04552, Niflumic acid
DB01083, Orlistat
DB00721, Procaine
DB01103, Quinacrine
DB00086, Streptokinase
DB04786, Suramin
DB04827, Urethane
DrugCentraliP47712
GuidetoPHARMACOLOGYi1424
SwissLipidsiSLP:000000565

PTM databases

iPTMnetiP47712
MetOSiteiP47712
PhosphoSitePlusiP47712

Genetic variation databases

BioMutaiPLA2G4A
DMDMi317373312

Proteomic databases

EPDiP47712
jPOSTiP47712
MassIVEiP47712
MaxQBiP47712
PaxDbiP47712
PeptideAtlasiP47712
PRIDEiP47712
ProteomicsDBi55788

Protocols and materials databases

Antibodypedia a portal for validated antibodies

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Antibodypediai
4104, 406 antibodies from 37 providers

The DNASU plasmid repository

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DNASUi
5321

Genome annotation databases

EnsembliENST00000367466.4; ENSP00000356436.3; ENSG00000116711.10
GeneIDi5321
KEGGihsa:5321
MANE-SelectiENST00000367466.4; ENSP00000356436.3; NM_024420.3; NP_077734.2
UCSCiuc001gsc.4, human

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
5321
DisGeNETi5321

GeneCards: human genes, protein and diseases

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GeneCardsi
PLA2G4A
HGNCiHGNC:9035, PLA2G4A
HPAiENSG00000116711, Tissue enhanced (parathyroid gland, seminal vesicle)
MalaCardsiPLA2G4A
MIMi600522, gene
618372, phenotype
neXtProtiNX_P47712
OpenTargetsiENSG00000116711
Orphaneti468635, Cryptogenic multifocal ulcerous stenosing enteritis
477787, Cytosolic phospholipase-A2 alpha deficiency associated bleeding disorder
PharmGKBiPA271
VEuPathDBiHostDB:ENSG00000116711

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1012, Eukaryota
KOG1325, Eukaryota
GeneTreeiENSGT01030000234606
HOGENOMiCLU_011663_1_1_1
InParanoidiP47712
OMAiKFFMGKV
OrthoDBi302848at2759
PhylomeDBiP47712
TreeFamiTF325228

Enzyme and pathway databases

UniPathwayiUPA00383
UPA00662
UPA00878
UPA00940
BRENDAi3.1.1.4, 2681
PathwayCommonsiP47712
ReactomeiR-HSA-111995, phospho-PLA2 pathway
R-HSA-1482788, Acyl chain remodelling of PC
R-HSA-1482798, Acyl chain remodeling of CL
R-HSA-1482801, Acyl chain remodelling of PS
R-HSA-1482839, Acyl chain remodelling of PE
R-HSA-1482922, Acyl chain remodelling of PI
R-HSA-1482925, Acyl chain remodelling of PG
R-HSA-1483115, Hydrolysis of LPC
R-HSA-1483166, Synthesis of PA
R-HSA-2142753, Arachidonic acid metabolism
R-HSA-418592, ADP signalling through P2Y purinoceptor 1
R-HSA-432142, Platelet sensitization by LDL
R-HSA-6811436, COPI-independent Golgi-to-ER retrograde traffic
SignaLinkiP47712
SIGNORiP47712

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

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BioGRID-ORCSi
5321, 9 hits in 1076 CRISPR screens

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

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ChiTaRSi
PLA2G4A, human
EvolutionaryTraceiP47712

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
PLA2G4A

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

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GenomeRNAii
5321
PharosiP47712, Tchem

Protein Ontology

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PROi
PR:P47712
RNActiP47712, protein

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000116711, Expressed in seminal vesicle and 204 other tissues
GenevisibleiP47712, HS

Family and domain databases

CDDicd04036, C2_cPLA2, 1 hit
Gene3Di2.60.40.150, 1 hit
InterProiView protein in InterPro
IPR016035, Acyl_Trfase/lysoPLipase
IPR041847, C2_cPLA2
IPR000008, C2_dom
IPR035892, C2_domain_sf
IPR002642, LysoPLipase_cat_dom
PfamiView protein in Pfam
PF00168, C2, 1 hit
PF01735, PLA2_B, 1 hit
SMARTiView protein in SMART
SM00239, C2, 1 hit
SM00022, PLAc, 1 hit
SUPFAMiSSF49562, SSF49562, 1 hit
SSF52151, SSF52151, 1 hit
PROSITEiView protein in PROSITE
PS50004, C2, 1 hit
PS51210, PLA2C, 1 hit

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 nameiPA24A_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: P47712
Secondary accession number(s): B1AKG4, Q29R80
<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: February 1, 1996
Last sequence update: January 11, 2011
Last modified: May 25, 2022
This is version 214 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with genetic variants
    List of human entries with genetic variants
  3. Human variants curated from literature reports
    Index of human variants curated from literature reports
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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