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Entry version 116 (07 Oct 2020)
Sequence version 2 (10 Aug 2010)
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Protein

Ubiquitin-40S ribosomal protein S27a

Gene

RPS27A

Organism
Bos taurus (Bovine)
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

Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity).By similarity
Component of the 40S subunit of the ribosome.

Miscellaneous

Ubiquitin is encoded by 4 different genes. Uba52 and Rps27a genes code for a single copy of ubiquitin fused to the ribosomal proteins L40 and S27a, respectively. UBB and UBC genes code for a polyubiquitin precursor with exact head to tail repeats, the number of repeats differ between species and strains.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei54Activating enzyme1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei68Essential for function1
Binding sitei72Activating enzyme1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri121 – 144C4-typeAdd BLAST24

<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 functionRibonucleoprotein, Ribosomal protein
LigandMetal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-BTA-110312, Translesion synthesis by REV1
R-BTA-110314, Recognition of DNA damage by PCNA-containing replication complex
R-BTA-110320, Translesion Synthesis by POLH
R-BTA-1169091, Activation of NF-kappaB in B cells
R-BTA-1234176, Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha
R-BTA-1253288, Downregulation of ERBB4 signaling
R-BTA-1295596, Spry regulation of FGF signaling
R-BTA-1358803, Downregulation of ERBB2:ERBB3 signaling
R-BTA-156827, L13a-mediated translational silencing of Ceruloplasmin expression
R-BTA-168638, NOD1/2 Signaling Pathway
R-BTA-174048, APC/C:Cdc20 mediated degradation of Cyclin B
R-BTA-174084, Autodegradation of Cdh1 by Cdh1:APC/C
R-BTA-174154, APC/C:Cdc20 mediated degradation of Securin
R-BTA-174178, APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1
R-BTA-174184, Cdc20:Phospho-APC/C mediated degradation of Cyclin A
R-BTA-179409, APC-Cdc20 mediated degradation of Nek2A
R-BTA-1799339, SRP-dependent cotranslational protein targeting to membrane
R-BTA-182971, EGFR downregulation
R-BTA-187577, SCF(Skp2)-mediated degradation of p27/p21
R-BTA-195253, Degradation of beta-catenin by the destruction complex
R-BTA-201681, TCF dependent signaling in response to WNT
R-BTA-202424, Downstream TCR signaling
R-BTA-205043, NRIF signals cell death from the nucleus
R-BTA-209543, p75NTR recruits signalling complexes
R-BTA-209560, NF-kB is activated and signals survival
R-BTA-2122948, Activated NOTCH1 Transmits Signal to the Nucleus
R-BTA-2173788, Downregulation of TGF-beta receptor signaling
R-BTA-2173791, TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition)
R-BTA-2173795, Downregulation of SMAD2/3:SMAD4 transcriptional activity
R-BTA-2173796, SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription
R-BTA-2467813, Separation of Sister Chromatids
R-BTA-2559580, Oxidative Stress Induced Senescence
R-BTA-2559582, Senescence-Associated Secretory Phenotype (SASP)
R-BTA-2559585, Oncogene Induced Senescence
R-BTA-2565942, Regulation of PLK1 Activity at G2/M Transition
R-BTA-2672351, Stimuli-sensing channels
R-BTA-2871837, FCERI mediated NF-kB activation
R-BTA-3134975, Regulation of innate immune responses to cytosolic DNA
R-BTA-349425, Autodegradation of the E3 ubiquitin ligase COP1
R-BTA-3769402, Deactivation of the beta-catenin transactivating complex
R-BTA-382556, ABC-family proteins mediated transport
R-BTA-445989, TAK1 activates NFkB by phosphorylation and activation of IKKs complex
R-BTA-450302, activated TAK1 mediates p38 MAPK activation
R-BTA-450321, JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1
R-BTA-450408, AUF1 (hnRNP D0) binds and destabilizes mRNA
R-BTA-4608870, Asymmetric localization of PCP proteins
R-BTA-4641257, Degradation of AXIN
R-BTA-4641258, Degradation of DVL
R-BTA-4641263, Regulation of FZD by ubiquitination
R-BTA-5205685, Pink/Parkin Mediated Mitophagy
R-BTA-532668, N-glycan trimming in the ER and Calnexin/Calreticulin cycle
R-BTA-5357905, Regulation of TNFR1 signaling
R-BTA-5357956, TNFR1-induced NFkappaB signaling pathway
R-BTA-5358346, Hedgehog ligand biogenesis
R-BTA-5607761, Dectin-1 mediated noncanonical NF-kB signaling
R-BTA-5607764, CLEC7A (Dectin-1) signaling
R-BTA-5610780, Degradation of GLI1 by the proteasome
R-BTA-5610785, GLI3 is processed to GLI3R by the proteasome
R-BTA-5632684, Hedgehog 'on' state
R-BTA-5654726, Negative regulation of FGFR1 signaling
R-BTA-5654727, Negative regulation of FGFR2 signaling
R-BTA-5654732, Negative regulation of FGFR3 signaling
R-BTA-5654733, Negative regulation of FGFR4 signaling
R-BTA-5655862, Translesion synthesis by POLK
R-BTA-5656121, Translesion synthesis by POLI
R-BTA-5656169, Termination of translesion DNA synthesis
R-BTA-5658442, Regulation of RAS by GAPs
R-BTA-5668541, TNFR2 non-canonical NF-kB pathway
R-BTA-5675221, Negative regulation of MAPK pathway
R-BTA-5675482, Regulation of necroptotic cell death
R-BTA-5676590, NIK-->noncanonical NF-kB signaling
R-BTA-5684264, MAP3K8 (TPL2)-dependent MAPK1/3 activation
R-BTA-5685942, HDR through Homologous Recombination (HRR)
R-BTA-5687128, MAPK6/MAPK4 signaling
R-BTA-5689603, UCH proteinases
R-BTA-5689877, Josephin domain DUBs
R-BTA-5689880, Ub-specific processing proteases
R-BTA-5689896, Ovarian tumor domain proteases
R-BTA-5689901, Metalloprotease DUBs
R-BTA-5693565, Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks
R-BTA-5696394, DNA Damage Recognition in GG-NER
R-BTA-5696395, Formation of Incision Complex in GG-NER
R-BTA-5696397, Gap-filling DNA repair synthesis and ligation in GG-NER
R-BTA-5696400, Dual Incision in GG-NER
R-BTA-6781823, Formation of TC-NER Pre-Incision Complex
R-BTA-6782135, Dual incision in TC-NER
R-BTA-6782210, Gap-filling DNA repair synthesis and ligation in TC-NER
R-BTA-6783310, Fanconi Anemia Pathway
R-BTA-6791226, Major pathway of rRNA processing in the nucleolus and cytosol
R-BTA-6804756, Regulation of TP53 Activity through Phosphorylation
R-BTA-6804757, Regulation of TP53 Degradation
R-BTA-6804760, Regulation of TP53 Activity through Methylation
R-BTA-68827, CDT1 association with the CDC6:ORC:origin complex
R-BTA-69017, CDK-mediated phosphorylation and removal of Cdc6
R-BTA-69231, Cyclin D associated events in G1
R-BTA-69481, G2/M Checkpoints
R-BTA-69541, Stabilization of p53
R-BTA-69601, Ubiquitin Mediated Degradation of Phosphorylated Cdc25A
R-BTA-72649, Translation initiation complex formation
R-BTA-72689, Formation of a pool of free 40S subunits
R-BTA-72702, Ribosomal scanning and start codon recognition
R-BTA-72706, GTP hydrolysis and joining of the 60S ribosomal subunit
R-BTA-75815, Ubiquitin-dependent degradation of Cyclin D
R-BTA-8849469, PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1
R-BTA-8852276, The role of GTSE1 in G2/M progression after G2 checkpoint
R-BTA-8854050, FBXL7 down-regulates AURKA during mitotic entry and in early mitosis
R-BTA-8856825, Cargo recognition for clathrin-mediated endocytosis
R-BTA-8856828, Clathrin-mediated endocytosis
R-BTA-8863795, Downregulation of ERBB2 signaling
R-BTA-8866652, Synthesis of active ubiquitin: roles of E1 and E2 enzymes
R-BTA-8866654, E3 ubiquitin ligases ubiquitinate target proteins
R-BTA-8939236, RUNX1 regulates transcription of genes involved in differentiation of HSCs
R-BTA-8939902, Regulation of RUNX2 expression and activity
R-BTA-8941858, Regulation of RUNX3 expression and activity
R-BTA-8948747, Regulation of PTEN localization
R-BTA-8948751, Regulation of PTEN stability and activity
R-BTA-8951664, Neddylation
R-BTA-901032, ER Quality Control Compartment (ERQC)
R-BTA-9010553, Regulation of expression of SLITs and ROBOs
R-BTA-9013507, NOTCH3 Activation and Transmission of Signal to the Nucleus
R-BTA-9020702, Interleukin-1 signaling
R-BTA-9033241, Peroxisomal protein import
R-BTA-912631, Regulation of signaling by CBL
R-BTA-917729, Endosomal Sorting Complex Required For Transport (ESCRT)
R-BTA-917937, Iron uptake and transport
R-BTA-936440, Negative regulators of DDX58/IFIH1 signaling
R-BTA-937039, IRAK1 recruits IKK complex
R-BTA-937042, IRAK2 mediated activation of TAK1 complex
R-BTA-937072, TRAF6-mediated induction of TAK1 complex within TLR4 complex
R-BTA-9645460, Alpha-protein kinase 1 signaling pathway
R-BTA-9646399, Aggrephagy
R-BTA-9664873, Pexophagy
R-BTA-975110, TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling
R-BTA-975144, IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation
R-BTA-975163, IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation
R-BTA-975956, Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC)
R-BTA-975957, Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC)
R-BTA-983168, Antigen processing: Ubiquitination & Proteasome degradation

<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:
Ubiquitin-40S ribosomal protein S27a
Alternative name(s):
Ubiquitin carboxyl extension protein 80
Cleaved into the following 2 chains:
<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:RPS27A
Synonyms:UBA80, UBCEP1
<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>OrganismiBos taurus (Bovine)
<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 identifieri9913 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaArtiodactylaRuminantiaPecoraBovidaeBovinaeBos
<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
  • UP000009136 <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 11

Organism-specific databases

Vertebrate Gene Nomenclature Database

More...
VGNCi
VGNC:34135, RPS27A

<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

Cytoplasm, Nucleus

<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_00003964741 – 76UbiquitinAdd BLAST76
ChainiPRO_000013766077 – 15640S ribosomal protein S27aAdd BLAST80

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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-linki6Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki27Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki29Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki48Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki63Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
<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 residuei65Phosphoserine; by PINK1By similarity1
Modified residuei76ADP-ribosylglycineBy similarity1
Cross-linki76Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)
Modified residuei104N6-acetyllysineBy similarity1
Modified residuei113N6-acetyllysineBy similarity1
Modified residuei152N6-acetyllysineBy similarity1

<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 Ser-65 by PINK1 during mitophagy. Phosphorylated ubiquitin specifically binds and activates parkin (PRKN), triggering mitophagy. Phosphorylation does not affect E1-mediated E2 charging of ubiquitin but affects discharging of E2 enzymes to form polyubiquitin chains. It also affects deubiquitination by deubiquitinase enzymes such as USP30.By similarity
Mono-ADP-ribosylated at the C-terminus by PARP9, a component of the PPAR9-DTX3L complex. ADP-ribosylation requires processing by E1 and E2 enzymes and prevents ubiquitin conjugation to substrates such as histones.By similarity

Keywords - PTMi

Acetylation, ADP-ribosylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

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

More...
PaxDbi
P62992

PRoteomics IDEntifications database

More...
PRIDEi
P62992

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSBTAG00000015473, Expressed in endometrium and 18 other tissues

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P62992, 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%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

Ribosomal protein S27a is part of the 40S ribosomal subunit.

By similarity

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

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BioGRIDi
159949, 3 interactors

STRING: functional protein association networks

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STRINGi
9913.ENSBTAP00000033015

<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

1156
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

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SMRi
P62992

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...

<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>Domaini1 – 76Ubiquitin-likePROSITE-ProRule annotationAdd BLAST76

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 amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi77 – 99Lys-rich (highly basic)Add BLAST23
Compositional biasi78 – 107Lys-richAdd BLAST30

<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

In the N-terminal section; belongs to the ubiquitin family.Curated
In the C-terminal section; belongs to the eukaryotic ribosomal protein eS31 family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri121 – 144C4-typeAdd BLAST24

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0004, Eukaryota

Ensembl GeneTree

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GeneTreei
ENSGT00940000165870

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
CLU_010412_2_0_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P62992

KEGG Orthology (KO)

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KOi
K02977

Identification of Orthologs from Complete Genome Data

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OMAi
FMAQHAN

Database of Orthologous Groups

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OrthoDBi
1536766at2759

TreeFam database of animal gene trees

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TreeFami
TF300036

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.20.25.660, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR002906, Ribosomal_S27a
IPR011332, Ribosomal_zn-bd
IPR038582, S27a-like_sf
IPR000626, Ubiquitin-like_dom
IPR029071, Ubiquitin-like_domsf
IPR019954, Ubiquitin_CS
IPR019956, Ubiquitin_dom

Pfam protein domain database

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Pfami
View protein in Pfam
PF01599, Ribosomal_S27, 1 hit
PF00240, ubiquitin, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00348, UBIQUITIN

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM01402, Ribosomal_S27, 1 hit
SM00213, UBQ, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF54236, SSF54236, 1 hit
SSF57829, SSF57829, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00299, UBIQUITIN_1, 1 hit
PS50053, UBIQUITIN_2, 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>Sequence (1+)i

<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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

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

P62992-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL
60 70 80 90 100
EDGRTLSDYN IQKESTLHLV LRLRGGAKKR KKKSYTTPKK NKHKRKKVKL
110 120 130 140 150
AVLKYYKVDE NGKISRLRRE CPSDECGAGV FMASHFDRHY CGKCCLTYCF

NKPEDK
Length:156
Mass (Da):17,965
Last modified:August 10, 2010 - 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:i617BC63DF3A904F7
GO

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

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A3Q1MYD8A0A3Q1MYD8_BOVIN
40S ribosomal protein S27a
RPS27A
194Annotation 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 conflicti141 – 156CGKCC…KPEDK → VANVV in BAC56381 (PubMed:12658628).CuratedAdd BLAST16

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
AF058700 mRNA Translation: AAC77907.1
AB098891 mRNA Translation: BAC56381.1
BC102491 mRNA Translation: AAI02492.2

Protein sequence database of the Protein Information Resource

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PIRi
A28144

NCBI Reference Sequences

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RefSeqi
NP_777203.1, NM_174778.1
XP_005212615.1, XM_005212558.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSBTAT00000033091; ENSBTAP00000033015; ENSBTAG00000015473

Database of genes from NCBI RefSeq genomes

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GeneIDi
286839

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
bta:286839

<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
AF058700 mRNA Translation: AAC77907.1
AB098891 mRNA Translation: BAC56381.1
BC102491 mRNA Translation: AAI02492.2
PIRiA28144
RefSeqiNP_777203.1, NM_174778.1
XP_005212615.1, XM_005212558.2

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4M0WX-ray1.40B1-76[»]
4Y1HX-ray1.40A1-76[»]
4Z9SX-ray2.30A/B/C/D1-76[»]
5BZ0X-ray2.10B1-76[»]
5FERX-ray2.34C/F1-76[»]
5JQSX-ray2.65D1-76[»]
5MN9X-ray2.05A/B1-76[»]
5XU8X-ray1.81B1-76[»]
5XVEX-ray1.24B1-76[»]
6DJWX-ray3.80B1-74[»]
6DJXX-ray4.80B1-76[»]
6E2BX-ray1.45A/C/E/G/I/P1-76[»]
6Q01X-ray0.85A/B1-76[»]
SMRiP62992
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi159949, 3 interactors
STRINGi9913.ENSBTAP00000033015

Proteomic databases

PaxDbiP62992
PRIDEiP62992

Genome annotation databases

EnsembliENSBTAT00000033091; ENSBTAP00000033015; ENSBTAG00000015473
GeneIDi286839
KEGGibta:286839

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
6233
VGNCiVGNC:34135, RPS27A

Phylogenomic databases

eggNOGiKOG0004, Eukaryota
GeneTreeiENSGT00940000165870
HOGENOMiCLU_010412_2_0_1
InParanoidiP62992
KOiK02977
OMAiFMAQHAN
OrthoDBi1536766at2759
TreeFamiTF300036

Enzyme and pathway databases

ReactomeiR-BTA-110312, Translesion synthesis by REV1
R-BTA-110314, Recognition of DNA damage by PCNA-containing replication complex
R-BTA-110320, Translesion Synthesis by POLH
R-BTA-1169091, Activation of NF-kappaB in B cells
R-BTA-1234176, Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha
R-BTA-1253288, Downregulation of ERBB4 signaling
R-BTA-1295596, Spry regulation of FGF signaling
R-BTA-1358803, Downregulation of ERBB2:ERBB3 signaling
R-BTA-156827, L13a-mediated translational silencing of Ceruloplasmin expression
R-BTA-168638, NOD1/2 Signaling Pathway
R-BTA-174048, APC/C:Cdc20 mediated degradation of Cyclin B
R-BTA-174084, Autodegradation of Cdh1 by Cdh1:APC/C
R-BTA-174154, APC/C:Cdc20 mediated degradation of Securin
R-BTA-174178, APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1
R-BTA-174184, Cdc20:Phospho-APC/C mediated degradation of Cyclin A
R-BTA-179409, APC-Cdc20 mediated degradation of Nek2A
R-BTA-1799339, SRP-dependent cotranslational protein targeting to membrane
R-BTA-182971, EGFR downregulation
R-BTA-187577, SCF(Skp2)-mediated degradation of p27/p21
R-BTA-195253, Degradation of beta-catenin by the destruction complex
R-BTA-201681, TCF dependent signaling in response to WNT
R-BTA-202424, Downstream TCR signaling
R-BTA-205043, NRIF signals cell death from the nucleus
R-BTA-209543, p75NTR recruits signalling complexes
R-BTA-209560, NF-kB is activated and signals survival
R-BTA-2122948, Activated NOTCH1 Transmits Signal to the Nucleus
R-BTA-2173788, Downregulation of TGF-beta receptor signaling
R-BTA-2173791, TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition)
R-BTA-2173795, Downregulation of SMAD2/3:SMAD4 transcriptional activity
R-BTA-2173796, SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription
R-BTA-2467813, Separation of Sister Chromatids
R-BTA-2559580, Oxidative Stress Induced Senescence
R-BTA-2559582, Senescence-Associated Secretory Phenotype (SASP)
R-BTA-2559585, Oncogene Induced Senescence
R-BTA-2565942, Regulation of PLK1 Activity at G2/M Transition
R-BTA-2672351, Stimuli-sensing channels
R-BTA-2871837, FCERI mediated NF-kB activation
R-BTA-3134975, Regulation of innate immune responses to cytosolic DNA
R-BTA-349425, Autodegradation of the E3 ubiquitin ligase COP1
R-BTA-3769402, Deactivation of the beta-catenin transactivating complex
R-BTA-382556, ABC-family proteins mediated transport
R-BTA-445989, TAK1 activates NFkB by phosphorylation and activation of IKKs complex
R-BTA-450302, activated TAK1 mediates p38 MAPK activation
R-BTA-450321, JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1
R-BTA-450408, AUF1 (hnRNP D0) binds and destabilizes mRNA
R-BTA-4608870, Asymmetric localization of PCP proteins
R-BTA-4641257, Degradation of AXIN
R-BTA-4641258, Degradation of DVL
R-BTA-4641263, Regulation of FZD by ubiquitination
R-BTA-5205685, Pink/Parkin Mediated Mitophagy
R-BTA-532668, N-glycan trimming in the ER and Calnexin/Calreticulin cycle
R-BTA-5357905, Regulation of TNFR1 signaling
R-BTA-5357956, TNFR1-induced NFkappaB signaling pathway
R-BTA-5358346, Hedgehog ligand biogenesis
R-BTA-5607761, Dectin-1 mediated noncanonical NF-kB signaling
R-BTA-5607764, CLEC7A (Dectin-1) signaling
R-BTA-5610780, Degradation of GLI1 by the proteasome
R-BTA-5610785, GLI3 is processed to GLI3R by the proteasome
R-BTA-5632684, Hedgehog 'on' state
R-BTA-5654726, Negative regulation of FGFR1 signaling
R-BTA-5654727, Negative regulation of FGFR2 signaling
R-BTA-5654732, Negative regulation of FGFR3 signaling
R-BTA-5654733, Negative regulation of FGFR4 signaling
R-BTA-5655862, Translesion synthesis by POLK
R-BTA-5656121, Translesion synthesis by POLI
R-BTA-5656169, Termination of translesion DNA synthesis
R-BTA-5658442, Regulation of RAS by GAPs
R-BTA-5668541, TNFR2 non-canonical NF-kB pathway
R-BTA-5675221, Negative regulation of MAPK pathway
R-BTA-5675482, Regulation of necroptotic cell death
R-BTA-5676590, NIK-->noncanonical NF-kB signaling
R-BTA-5684264, MAP3K8 (TPL2)-dependent MAPK1/3 activation
R-BTA-5685942, HDR through Homologous Recombination (HRR)
R-BTA-5687128, MAPK6/MAPK4 signaling
R-BTA-5689603, UCH proteinases
R-BTA-5689877, Josephin domain DUBs
R-BTA-5689880, Ub-specific processing proteases
R-BTA-5689896, Ovarian tumor domain proteases
R-BTA-5689901, Metalloprotease DUBs
R-BTA-5693565, Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks
R-BTA-5696394, DNA Damage Recognition in GG-NER
R-BTA-5696395, Formation of Incision Complex in GG-NER
R-BTA-5696397, Gap-filling DNA repair synthesis and ligation in GG-NER
R-BTA-5696400, Dual Incision in GG-NER
R-BTA-6781823, Formation of TC-NER Pre-Incision Complex
R-BTA-6782135, Dual incision in TC-NER
R-BTA-6782210, Gap-filling DNA repair synthesis and ligation in TC-NER
R-BTA-6783310, Fanconi Anemia Pathway
R-BTA-6791226, Major pathway of rRNA processing in the nucleolus and cytosol
R-BTA-6804756, Regulation of TP53 Activity through Phosphorylation
R-BTA-6804757, Regulation of TP53 Degradation
R-BTA-6804760, Regulation of TP53 Activity through Methylation
R-BTA-68827, CDT1 association with the CDC6:ORC:origin complex
R-BTA-69017, CDK-mediated phosphorylation and removal of Cdc6
R-BTA-69231, Cyclin D associated events in G1
R-BTA-69481, G2/M Checkpoints
R-BTA-69541, Stabilization of p53
R-BTA-69601, Ubiquitin Mediated Degradation of Phosphorylated Cdc25A
R-BTA-72649, Translation initiation complex formation
R-BTA-72689, Formation of a pool of free 40S subunits
R-BTA-72702, Ribosomal scanning and start codon recognition
R-BTA-72706, GTP hydrolysis and joining of the 60S ribosomal subunit
R-BTA-75815, Ubiquitin-dependent degradation of Cyclin D
R-BTA-8849469, PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1
R-BTA-8852276, The role of GTSE1 in G2/M progression after G2 checkpoint
R-BTA-8854050, FBXL7 down-regulates AURKA during mitotic entry and in early mitosis
R-BTA-8856825, Cargo recognition for clathrin-mediated endocytosis
R-BTA-8856828, Clathrin-mediated endocytosis
R-BTA-8863795, Downregulation of ERBB2 signaling
R-BTA-8866652, Synthesis of active ubiquitin: roles of E1 and E2 enzymes
R-BTA-8866654, E3 ubiquitin ligases ubiquitinate target proteins
R-BTA-8939236, RUNX1 regulates transcription of genes involved in differentiation of HSCs
R-BTA-8939902, Regulation of RUNX2 expression and activity
R-BTA-8941858, Regulation of RUNX3 expression and activity
R-BTA-8948747, Regulation of PTEN localization
R-BTA-8948751, Regulation of PTEN stability and activity
R-BTA-8951664, Neddylation
R-BTA-901032, ER Quality Control Compartment (ERQC)
R-BTA-9010553, Regulation of expression of SLITs and ROBOs
R-BTA-9013507, NOTCH3 Activation and Transmission of Signal to the Nucleus
R-BTA-9020702, Interleukin-1 signaling
R-BTA-9033241, Peroxisomal protein import
R-BTA-912631, Regulation of signaling by CBL
R-BTA-917729, Endosomal Sorting Complex Required For Transport (ESCRT)
R-BTA-917937, Iron uptake and transport
R-BTA-936440, Negative regulators of DDX58/IFIH1 signaling
R-BTA-937039, IRAK1 recruits IKK complex
R-BTA-937042, IRAK2 mediated activation of TAK1 complex
R-BTA-937072, TRAF6-mediated induction of TAK1 complex within TLR4 complex
R-BTA-9645460, Alpha-protein kinase 1 signaling pathway
R-BTA-9646399, Aggrephagy
R-BTA-9664873, Pexophagy
R-BTA-975110, TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling
R-BTA-975144, IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation
R-BTA-975163, IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation
R-BTA-975956, Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC)
R-BTA-975957, Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC)
R-BTA-983168, Antigen processing: Ubiquitination & Proteasome degradation

Gene expression databases

BgeeiENSBTAG00000015473, Expressed in endometrium and 18 other tissues
ExpressionAtlasiP62992, baseline and differential

Family and domain databases

Gene3Di2.20.25.660, 1 hit
InterProiView protein in InterPro
IPR002906, Ribosomal_S27a
IPR011332, Ribosomal_zn-bd
IPR038582, S27a-like_sf
IPR000626, Ubiquitin-like_dom
IPR029071, Ubiquitin-like_domsf
IPR019954, Ubiquitin_CS
IPR019956, Ubiquitin_dom
PfamiView protein in Pfam
PF01599, Ribosomal_S27, 1 hit
PF00240, ubiquitin, 1 hit
PRINTSiPR00348, UBIQUITIN
SMARTiView protein in SMART
SM01402, Ribosomal_S27, 1 hit
SM00213, UBQ, 1 hit
SUPFAMiSSF54236, SSF54236, 1 hit
SSF57829, SSF57829, 1 hit
PROSITEiView protein in PROSITE
PS00299, UBIQUITIN_1, 1 hit
PS50053, UBIQUITIN_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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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 nameiRS27A_BOVIN
<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: P62992
Secondary accession number(s): O97577
, P02248, P02249, P02250, P0CG52, P62990, P80169, Q01235, Q24K23, Q28169, Q28170, Q29120, Q3T0V5, Q3ZCE3, Q862C1, Q862F4, Q862M4, Q862T5, Q862X8, Q91887, Q91888
<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: August 31, 2004
Last sequence update: August 10, 2010
Last modified: October 7, 2020
This is version 116 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

<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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Ribosomal proteins
    Ribosomal proteins families and list of entries
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