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Entry version 219 (08 May 2019)
Sequence version 4 (23 Jan 2007)
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Protein

Proto-oncogene tyrosine-protein kinase Src

Gene

SRC

Organism
Gallus gallus (Chicken)
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

Non-receptor protein tyrosine kinase which is activated following engagement of many different classes of cellular receptors including immune response receptors, integrins and other adhesion receptors, receptor protein tyrosine kinases, G protein-coupled receptors as well as cytokine receptors. Participates in signaling pathways that control a diverse spectrum of biological activities including gene transcription, immune response, cell adhesion, cell cycle progression, apoptosis, migration, and transformation. Due to functional redundancy between members of the SRC kinase family, identification of the specific role of each SRC kinase is very difficult. SRC appears to be one of the primary kinases activated following engagement of receptors and plays a role in the activation of other protein tyrosine kinase (PTK) families. Receptor clustering or dimerization leads to recruitment of SRC to the receptor complexes where it phosphorylates the tyrosine residues within the receptor cytoplasmic domains. Plays an important role in the regulation of cytoskeletal organization through phosphorylation of specific substrates involved in this process (Probable). When cells adhere via focal adhesions to the extracellular matrix, signals are transmitted by integrins into the cell resulting in tyrosine phosphorylation of a number of focal adhesion proteins, including PTK2/FAK1 and paxillin (PXN) (By similarity). Also active at the sites of cell-cell contact adherens junctions and at gap junctions. Implicated in the regulation of pre-mRNA-processing (Probable). Might be involved not only in mediating the transduction of mitogenic signals at the level of the plasma membrane but also in controlling progression through the cell cycle via interaction with regulatory proteins in the nucleus (PubMed:1717492, PubMed:8550628). Involved in anchorage-independent cell growth (PubMed:19307596).By similarity3 Publications3 Publications

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

<p>This subsection of the ‘Function’ section 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

Becomes activated when its major tyrosine phosphorylation site is not phosphorylated. It can also be activated by point mutations as well as by truncations at the C-terminal end or by other mutations. Heme regulates its activity by enhancing the phosphorylation on Tyr-527 (By similarity).By similarity

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 sitei295ATP1
<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 sitei386Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi273 – 281ATPPROSITE-ProRule annotation9

<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 functionKinase, Transferase, Tyrosine-protein kinase
Biological processCell adhesion, Cell cycle, Immunity
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.10.2 1306

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-GGA-1227986 Signaling by ERBB2
R-GGA-1251985 Nuclear signaling by ERBB4
R-GGA-1257604 PIP3 activates AKT signaling
R-GGA-1295596 Spry regulation of FGF signaling
R-GGA-1433557 Signaling by SCF-KIT
R-GGA-1433559 Regulation of KIT signaling
R-GGA-186763 Downstream signal transduction
R-GGA-354192 Integrin alphaIIb beta3 signaling
R-GGA-389513 CTLA4 inhibitory signaling
R-GGA-3928662 EPHB-mediated forward signaling
R-GGA-3928663 EPHA-mediated growth cone collapse
R-GGA-3928664 Ephrin signaling
R-GGA-3928665 EPH-ephrin mediated repulsion of cells
R-GGA-418592 ADP signalling through P2Y purinoceptor 1
R-GGA-418594 G alpha (i) signalling events
R-GGA-430116 GP1b-IX-V activation signalling
R-GGA-4420097 VEGFA-VEGFR2 Pathway
R-GGA-456926 Thrombin signalling through proteinase activated receptors (PARs)
R-GGA-5663220 RHO GTPases Activate Formins
R-GGA-6811558 PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling
R-GGA-8853659 RET signaling
R-GGA-8874081 MET activates PTK2 signaling
R-GGA-8941858 Regulation of RUNX3 expression and activity
R-GGA-9009391 Non-genomic estrogen signaling

<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:
Proto-oncogene tyrosine-protein kinase Src (EC:2.7.10.2)
Alternative name(s):
Proto-oncogene c-Src
pp60c-src
Short name:
p60-Src
<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:SRC
<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>OrganismiGallus gallus (Chicken)
<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 identifieri9031 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
<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
  • UP000000539 <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 20

<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

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Endosome, Membrane, Mitochondrion, Mitochondrion inner 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

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>Mutagenesisi498C → A: Significant reduction in S-nitrosylation. 1 Publication1
Mutagenesisi527Y → F: Constitutively active. 1 Publication1

Keywords - Diseasei

Proto-oncogene

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3655

<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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedBy similarity
<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_00000881442 – 533Proto-oncogene tyrosine-protein kinase SrcAdd BLAST532

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi2N-myristoyl glycineBy similarity1
<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 residuei12Phosphoserine; by PKC1 Publication1
Modified residuei34Phosphothreonine1 Publication1
Modified residuei46Phosphothreonine1 Publication1
Modified residuei72Phosphoserine1 Publication1
Modified residuei416Phosphotyrosine; by autocatalysis2 Publications1
Modified residuei436Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei498S-nitrosocysteine1 Publication1
Modified residuei527Phosphotyrosine; by CSK1 Publication1

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

Myristoylated at Gly-2, and this is essential for targeting to membranes.By similarity
Dephosphorylated at Tyr-527 by PTPRJ. Phosphorylated on Tyr-527 by c-Src kinase (CSK). The phosphorylated form is termed pp60c-src. Dephosphorylated by PTPRJ at Tyr-416. Normally maintained in an inactive conformation with the SH2 domain engaged with Tyr-527, the SH3 domain engaged with the SH2-kinase linker, and Tyr-416 dephosphorylated. Dephosphorylation of Tyr-527 as a result of protein tyrosine phosphatase (PTP) action disrupts the intramolecular interaction between the SH2 domain and Tyr-527, Tyr-416 can then become autophosphorylated, resulting in SRC activation. Phosphorylation of Tyr-527 by CSK allows this interaction to reform, resulting in SRC inactivation (By similarity).By similarity
S-nitrosylation is important for activation of its kinase activity.1 Publication

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein, S-nitrosylation

Proteomic databases

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

More...
PaxDbi
P00523

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P00523

<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 to high levels, and with a high degree of kinase activity, in certain fully differentiated cells such as neurons, platelets and macrophages. Isoform 1 is widely expressed. Isoform 2 is expressed only in the muscle.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSGALG00000003855 Expressed in 10 organ(s), highest expression level in liver

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P00523 baseline and differential

<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

Forms a complex with polyoma virus middle T antigen. Interacts with AFAP-110. Interacts with GJA1 and PXN.3 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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
676691, 3 interactors

Database of interacting proteins

More...
DIPi
DIP-449N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...
ELMi
P00523

Protein interaction database and analysis system

More...
IntActi
P00523, 19 interactors

Molecular INTeraction database

More...
MINTi
P00523

STRING: functional protein association networks

More...
STRINGi
9031.ENSGALP00000006117

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P00523

<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

1533
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

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
1F1WX-ray2.10A145-247[»]
1F2FX-ray1.70A145-247[»]
1NLONMR-C81-140[»]
1NLPNMR-C81-140[»]
1P13X-ray1.63A/B145-246[»]
1PRLNMR-C77-140[»]
1PRMNMR-C77-140[»]
1RLPNMR-C77-140[»]
1RLQNMR-C77-140[»]
1SRLNMR-A77-140[»]
1SRMNMR-A77-140[»]
2HWOX-ray2.50A/B251-533[»]
2HWPX-ray2.48A/B251-533[»]
2OIQX-ray2.07A/B251-533[»]
2PTKX-ray2.35A81-533[»]
2QI8X-ray2.32A/B251-533[»]
2QLQX-ray2.33A/B251-533[»]
2QQ7X-ray2.38A/B251-533[»]
3D7TX-ray2.90B251-533[»]
3D7UX-ray4.11B/D260-523[»]
3DQWX-ray2.02A/B/C/D251-533[»]
3DQXX-ray2.30A/B251-533[»]
3EL7X-ray2.80A251-533[»]
3EL8X-ray2.30A/B251-533[»]
3EN4X-ray2.55A/B251-533[»]
3EN5X-ray2.66A/B251-533[»]
3EN6X-ray2.39A/B251-533[»]
3EN7X-ray2.81A/B251-533[»]
3F3TX-ray2.50A/B251-533[»]
3F3UX-ray2.50A/B251-533[»]
3F3VX-ray2.60A/B251-533[»]
3F3WX-ray2.60A/B251-533[»]
3F6XX-ray2.35A/B/C/D251-533[»]
3FJ5X-ray1.65A/B85-140[»]
3G5DX-ray2.20A/B251-533[»]
3G6GX-ray2.31A/B251-533[»]
3G6HX-ray2.35A/B251-533[»]
3GEQX-ray2.20A/B251-533[»]
3LOKX-ray2.48A/B251-533[»]
3OEZX-ray2.40A/B251-533[»]
3OF0X-ray2.70A/B251-533[»]
3QLFX-ray2.75A/B251-533[»]
3QLGX-ray2.75A/B251-533[»]
3SVVX-ray2.20A/B251-533[»]
3TZ7X-ray3.30A/B251-533[»]
3TZ8X-ray2.70A/B251-533[»]
3TZ9X-ray3.10A/B251-533[»]
3U4WX-ray1.90A259-533[»]
3U51X-ray2.24A/B259-533[»]
3UQFX-ray2.27A/B251-533[»]
3UQGX-ray2.20A/B251-533[»]
4AGWX-ray2.60A/B251-533[»]
4DGGX-ray2.65A/B251-533[»]
4FICX-ray2.50A/B251-533[»]
4HVUX-ray0.98A85-141[»]
4HVVX-ray1.10A85-140[»]
4HVWX-ray0.98A85-141[»]
4JZ3X-ray1.85A85-141[»]
4JZ4X-ray1.56A/B85-141[»]
4LE9X-ray1.34A85-141[»]
4LGGX-ray2.41A/B264-533[»]
4LGHX-ray2.84A/B257-533[»]
4MCVX-ray2.73A/B256-533[»]
4O2PX-ray2.10A/B251-533[»]
4OMLX-ray1.60A85-141[»]
4OMMX-ray1.90A85-140[»]
4OMNX-ray1.50A85-140[»]
4OMOX-ray1.04A/B85-141[»]
4OMPX-ray2.00A85-139[»]
4OMQX-ray2.00A85-140[»]
4QT7X-ray1.55A85-141[»]
4RTUX-ray2.45A85-141[»]
4RTVX-ray1.37A85-141[»]
4RTWX-ray1.24A/C85-141[»]
4RTXX-ray1.32A/B/C/D85-141[»]
4RTYX-ray1.28A85-141[»]
4RTZX-ray0.98A85-141[»]
4U5JX-ray2.26A/B251-533[»]
4YBJX-ray2.61A/B251-533[»]
4YBKX-ray2.50A251-533[»]
5BMMX-ray2.50A/B251-533[»]
5D10X-ray2.70A/B251-533[»]
5D11X-ray2.30A/B251-533[»]
5D12X-ray3.00A/B251-533[»]
5EC7X-ray1.65A/B/C85-140[»]
5ECAX-ray1.16A85-141[»]
5I11X-ray1.95A85-141[»]
5J5SX-ray2.15A/B251-533[»]
5K9IX-ray2.50A/B251-533[»]
5OAVX-ray0.95A/C85-141[»]
5OB0X-ray1.17A85-141[»]
5OB1X-ray1.17A85-141[»]
5OB2X-ray1.80A/C85-141[»]
5SWHX-ray2.50A/B252-533[»]
5SYSX-ray2.80A/B251-533[»]
5T0PX-ray2.50A/B251-533[»]
5TEHX-ray2.99A/B251-533[»]
5XP5X-ray2.10A/B251-533[»]
5XP7X-ray2.01A/B251-533[»]

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

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SMRi
P00523

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P00523

<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>Domaini81 – 142SH3PROSITE-ProRule annotationAdd BLAST62
Domaini148 – 245SH2PROSITE-ProRule annotationAdd BLAST98
Domaini267 – 520Protein kinasePROSITE-ProRule annotationAdd BLAST254

<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 protein kinase superfamily. Tyr protein kinase family. SRC subfamily.PROSITE-ProRule annotation

Keywords - Domaini

SH2 domain, SH3 domain

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0197 Eukaryota
COG0515 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000158250

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P00523

KEGG Orthology (KO)

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KOi
K05704

Identification of Orthologs from Complete Genome Data

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OMAi
NHYRKHA

Database of Orthologous Groups

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OrthoDBi
539311at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P00523

TreeFam database of animal gene trees

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TreeFami
TF351634

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.30.505.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
IPR000980 SH2
IPR036860 SH2_dom_sf
IPR036028 SH3-like_dom_sf
IPR001452 SH3_domain
IPR008266 Tyr_kinase_AS
IPR020635 Tyr_kinase_cat_dom

Pfam protein domain database

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Pfami
View protein in Pfam
PF07714 Pkinase_Tyr, 1 hit
PF00017 SH2, 1 hit
PF00018 SH3_1, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00401 SH2DOMAIN
PR00452 SH3DOMAIN
PR00109 TYRKINASE

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00252 SH2, 1 hit
SM00326 SH3, 1 hit
SM00219 TyrKc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF50044 SSF50044, 1 hit
SSF55550 SSF55550, 1 hit
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00109 PROTEIN_KINASE_TYR, 1 hit
PS50001 SH2, 1 hit
PS50002 SH3, 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>Sequences (2+)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 describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P00523-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MGSSKSKPKD PSQRRRSLEP PDSTHHGGFP ASQTPNKTAA PDTHRTPSRS
60 70 80 90 100
FGTVATEPKL FGGFNTSDTV TSPQRAGALA GGVTTFVALY DYESRTETDL
110 120 130 140 150
SFKKGERLQI VNNTEGDWWL AHSLTTGQTG YIPSNYVAPS DSIQAEEWYF
160 170 180 190 200
GKITRRESER LLLNPENPRG TFLVRESETT KGAYCLSVSD FDNAKGLNVK
210 220 230 240 250
HYKIRKLDSG GFYITSRTQF SSLQQLVAYY SKHADGLCHR LTNVCPTSKP
260 270 280 290 300
QTQGLAKDAW EIPRESLRLE VKLGQGCFGE VWMGTWNGTT RVAIKTLKPG
310 320 330 340 350
TMSPEAFLQE AQVMKKLRHE KLVQLYAVVS EEPIYIVTEY MSKGSLLDFL
360 370 380 390 400
KGEMGKYLRL PQLVDMAAQI ASGMAYVERM NYVHRDLRAA NILVGENLVC
410 420 430 440 450
KVADFGLARL IEDNEYTARQ GAKFPIKWTA PEAALYGRFT IKSDVWSFGI
460 470 480 490 500
LLTELTTKGR VPYPGMVNRE VLDQVERGYR MPCPPECPES LHDLMCQCWR
510 520 530
KDPEERPTFE YLQAFLEDYF TSTEPQYQPG ENL
Length:533
Mass (Da):60,010
Last modified:January 23, 2007 - v4
<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:iABDB036F7D63C30A
GO
Isoform 2 (identifier: P00523-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     183-193: AYCLSVSDFDN → DPCIPLPSCLC
     194-533: Missing.

Note: Membrane-bound.
Show »
Length:193
Mass (Da):21,180
Checksum:i9D1BE54C33B02D98
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 are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A1I7Q3Z0A0A1I7Q3Z0_CHICK
Tyrosine-protein kinase
SRC
539Annotation 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>
A0A1D5PAX9A0A1D5PAX9_CHICK
Tyrosine-protein kinase
SRC
557Annotation score:

Annotation score:2 out of 5

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti301T → N (PubMed:6299580).Curated1
Sequence conflicti501K → R (PubMed:6299580).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_011844183 – 193AYCLSVSDFDN → DPCIPLPSCLC in isoform 2. 1 PublicationAdd BLAST11
Alternative sequenceiVSP_011845194 – 533Missing in isoform 2. 1 PublicationAdd BLAST340

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

More...
DDBJi
Links Updated
V00402 Genomic DNA Translation: CAA23696.1
J00908 Genomic DNA No translation available.
M57290 mRNA Translation: AAA49078.1
S43604 mRNA Translation: AAD13831.1
S43616 mRNA Translation: AAD13835.1
S43587 mRNA Translation: AAD13830.1
S43609 mRNA Translation: AAD13832.1
S43614 mRNA Translation: AAD13834.1
S43579 mRNA Translation: AAB19353.2

Protein sequence database of the Protein Information Resource

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PIRi
A00630 TVCHS

NCBI Reference Sequences

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RefSeqi
NP_990788.2, NM_205457.2
XP_015151834.1, XM_015296348.1 [P00523-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSGALT00000061823; ENSGALP00000049896; ENSGALG00000003855 [P00523-1]
ENSGALT00000070498; ENSGALP00000054990; ENSGALG00000003855 [P00523-1]
ENSGALT00000093274; ENSGALP00000068298; ENSGALG00000003855 [P00523-1]

Database of genes from NCBI RefSeq genomes

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GeneIDi
396442

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
gga:396442

Keywords - Coding sequence diversityi

Alternative splicing

<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
V00402 Genomic DNA Translation: CAA23696.1
J00908 Genomic DNA No translation available.
M57290 mRNA Translation: AAA49078.1
S43604 mRNA Translation: AAD13831.1
S43616 mRNA Translation: AAD13835.1
S43587 mRNA Translation: AAD13830.1
S43609 mRNA Translation: AAD13832.1
S43614 mRNA Translation: AAD13834.1
S43579 mRNA Translation: AAB19353.2
PIRiA00630 TVCHS
RefSeqiNP_990788.2, NM_205457.2
XP_015151834.1, XM_015296348.1 [P00523-1]

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1F1WX-ray2.10A145-247[»]
1F2FX-ray1.70A145-247[»]
1NLONMR-C81-140[»]
1NLPNMR-C81-140[»]
1P13X-ray1.63A/B145-246[»]
1PRLNMR-C77-140[»]
1PRMNMR-C77-140[»]
1RLPNMR-C77-140[»]
1RLQNMR-C77-140[»]
1SRLNMR-A77-140[»]
1SRMNMR-A77-140[»]
2HWOX-ray2.50A/B251-533[»]
2HWPX-ray2.48A/B251-533[»]
2OIQX-ray2.07A/B251-533[»]
2PTKX-ray2.35A81-533[»]
2QI8X-ray2.32A/B251-533[»]
2QLQX-ray2.33A/B251-533[»]
2QQ7X-ray2.38A/B251-533[»]
3D7TX-ray2.90B251-533[»]
3D7UX-ray4.11B/D260-523[»]
3DQWX-ray2.02A/B/C/D251-533[»]
3DQXX-ray2.30A/B251-533[»]
3EL7X-ray2.80A251-533[»]
3EL8X-ray2.30A/B251-533[»]
3EN4X-ray2.55A/B251-533[»]
3EN5X-ray2.66A/B251-533[»]
3EN6X-ray2.39A/B251-533[»]
3EN7X-ray2.81A/B251-533[»]
3F3TX-ray2.50A/B251-533[»]
3F3UX-ray2.50A/B251-533[»]
3F3VX-ray2.60A/B251-533[»]
3F3WX-ray2.60A/B251-533[»]
3F6XX-ray2.35A/B/C/D251-533[»]
3FJ5X-ray1.65A/B85-140[»]
3G5DX-ray2.20A/B251-533[»]
3G6GX-ray2.31A/B251-533[»]
3G6HX-ray2.35A/B251-533[»]
3GEQX-ray2.20A/B251-533[»]
3LOKX-ray2.48A/B251-533[»]
3OEZX-ray2.40A/B251-533[»]
3OF0X-ray2.70A/B251-533[»]
3QLFX-ray2.75A/B251-533[»]
3QLGX-ray2.75A/B251-533[»]
3SVVX-ray2.20A/B251-533[»]
3TZ7X-ray3.30A/B251-533[»]
3TZ8X-ray2.70A/B251-533[»]
3TZ9X-ray3.10A/B251-533[»]
3U4WX-ray1.90A259-533[»]
3U51X-ray2.24A/B259-533[»]
3UQFX-ray2.27A/B251-533[»]
3UQGX-ray2.20A/B251-533[»]
4AGWX-ray2.60A/B251-533[»]
4DGGX-ray2.65A/B251-533[»]
4FICX-ray2.50A/B251-533[»]
4HVUX-ray0.98A85-141[»]
4HVVX-ray1.10A85-140[»]
4HVWX-ray0.98A85-141[»]
4JZ3X-ray1.85A85-141[»]
4JZ4X-ray1.56A/B85-141[»]
4LE9X-ray1.34A85-141[»]
4LGGX-ray2.41A/B264-533[»]
4LGHX-ray2.84A/B257-533[»]
4MCVX-ray2.73A/B256-533[»]
4O2PX-ray2.10A/B251-533[»]
4OMLX-ray1.60A85-141[»]
4OMMX-ray1.90A85-140[»]
4OMNX-ray1.50A85-140[»]
4OMOX-ray1.04A/B85-141[»]
4OMPX-ray2.00A85-139[»]
4OMQX-ray2.00A85-140[»]
4QT7X-ray1.55A85-141[»]
4RTUX-ray2.45A85-141[»]
4RTVX-ray1.37A85-141[»]
4RTWX-ray1.24A/C85-141[»]
4RTXX-ray1.32A/B/C/D85-141[»]
4RTYX-ray1.28A85-141[»]
4RTZX-ray0.98A85-141[»]
4U5JX-ray2.26A/B251-533[»]
4YBJX-ray2.61A/B251-533[»]
4YBKX-ray2.50A251-533[»]
5BMMX-ray2.50A/B251-533[»]
5D10X-ray2.70A/B251-533[»]
5D11X-ray2.30A/B251-533[»]
5D12X-ray3.00A/B251-533[»]
5EC7X-ray1.65A/B/C85-140[»]
5ECAX-ray1.16A85-141[»]
5I11X-ray1.95A85-141[»]
5J5SX-ray2.15A/B251-533[»]
5K9IX-ray2.50A/B251-533[»]
5OAVX-ray0.95A/C85-141[»]
5OB0X-ray1.17A85-141[»]
5OB1X-ray1.17A85-141[»]
5OB2X-ray1.80A/C85-141[»]
5SWHX-ray2.50A/B252-533[»]
5SYSX-ray2.80A/B251-533[»]
5T0PX-ray2.50A/B251-533[»]
5TEHX-ray2.99A/B251-533[»]
5XP5X-ray2.10A/B251-533[»]
5XP7X-ray2.01A/B251-533[»]
SMRiP00523
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi676691, 3 interactors
DIPiDIP-449N
ELMiP00523
IntActiP00523, 19 interactors
MINTiP00523
STRINGi9031.ENSGALP00000006117

Chemistry databases

BindingDBiP00523
ChEMBLiCHEMBL3655

PTM databases

iPTMnetiP00523

Proteomic databases

PaxDbiP00523

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSGALT00000061823; ENSGALP00000049896; ENSGALG00000003855 [P00523-1]
ENSGALT00000070498; ENSGALP00000054990; ENSGALG00000003855 [P00523-1]
ENSGALT00000093274; ENSGALP00000068298; ENSGALG00000003855 [P00523-1]
GeneIDi396442
KEGGigga:396442

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
6714

Phylogenomic databases

eggNOGiKOG0197 Eukaryota
COG0515 LUCA
GeneTreeiENSGT00940000158250
InParanoidiP00523
KOiK05704
OMAiNHYRKHA
OrthoDBi539311at2759
PhylomeDBiP00523
TreeFamiTF351634

Enzyme and pathway databases

BRENDAi2.7.10.2 1306
ReactomeiR-GGA-1227986 Signaling by ERBB2
R-GGA-1251985 Nuclear signaling by ERBB4
R-GGA-1257604 PIP3 activates AKT signaling
R-GGA-1295596 Spry regulation of FGF signaling
R-GGA-1433557 Signaling by SCF-KIT
R-GGA-1433559 Regulation of KIT signaling
R-GGA-186763 Downstream signal transduction
R-GGA-354192 Integrin alphaIIb beta3 signaling
R-GGA-389513 CTLA4 inhibitory signaling
R-GGA-3928662 EPHB-mediated forward signaling
R-GGA-3928663 EPHA-mediated growth cone collapse
R-GGA-3928664 Ephrin signaling
R-GGA-3928665 EPH-ephrin mediated repulsion of cells
R-GGA-418592 ADP signalling through P2Y purinoceptor 1
R-GGA-418594 G alpha (i) signalling events
R-GGA-430116 GP1b-IX-V activation signalling
R-GGA-4420097 VEGFA-VEGFR2 Pathway
R-GGA-456926 Thrombin signalling through proteinase activated receptors (PARs)
R-GGA-5663220 RHO GTPases Activate Formins
R-GGA-6811558 PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling
R-GGA-8853659 RET signaling
R-GGA-8874081 MET activates PTK2 signaling
R-GGA-8941858 Regulation of RUNX3 expression and activity
R-GGA-9009391 Non-genomic estrogen signaling

Miscellaneous databases

EvolutionaryTraceiP00523

Protein Ontology

More...
PROi
PR:P00523

Gene expression databases

BgeeiENSGALG00000003855 Expressed in 10 organ(s), highest expression level in liver
ExpressionAtlasiP00523 baseline and differential

Family and domain databases

Gene3Di3.30.505.10, 1 hit
InterProiView protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
IPR000980 SH2
IPR036860 SH2_dom_sf
IPR036028 SH3-like_dom_sf
IPR001452 SH3_domain
IPR008266 Tyr_kinase_AS
IPR020635 Tyr_kinase_cat_dom
PfamiView protein in Pfam
PF07714 Pkinase_Tyr, 1 hit
PF00017 SH2, 1 hit
PF00018 SH3_1, 1 hit
PRINTSiPR00401 SH2DOMAIN
PR00452 SH3DOMAIN
PR00109 TYRKINASE
SMARTiView protein in SMART
SM00252 SH2, 1 hit
SM00326 SH3, 1 hit
SM00219 TyrKc, 1 hit
SUPFAMiSSF50044 SSF50044, 1 hit
SSF55550 SSF55550, 1 hit
SSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00109 PROTEIN_KINASE_TYR, 1 hit
PS50001 SH2, 1 hit
PS50002 SH3, 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 nameiSRC_CHICK
<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: P00523
Secondary accession number(s): Q90992
, Q90993, Q91343, Q91345, Q92013, Q98915
<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: July 21, 1986
Last sequence update: January 23, 2007
Last modified: May 8, 2019
This is version 219 of the entry and version 4 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, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
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