Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 167 (18 Sep 2019)
Sequence version 2 (01 Oct 1996)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

DNA-directed RNA polymerase I subunit RPA49

Gene

RPA49

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
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

DNA-dependent RNA polymerases catalyze the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase I (Pol I) which synthesizes ribosomal RNA precursors. Besides, RNA polymerase I has intrinsic RNA cleavage activity. The heterodimer formed by RPA34 and RPA49 stimulates transcript elongation by Pol I. Subunit RPA49 can bind both single-stranded and double-stranded DNA.4 Publications

<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 functionDNA-binding, Nucleotidyltransferase, Transferase
Biological processRibosome biogenesis, Transcription

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-33245-MONOMER

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-73762 RNA Polymerase I Transcription Initiation
R-SCE-73772 RNA Polymerase I Promoter Escape

<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:
DNA-directed RNA polymerase I subunit RPA49
Short name:
A49
Alternative name(s):
DNA-directed RNA polymerase I 49 kDa polypeptide
<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:RPA49
Synonyms:RRN13
Ordered Locus Names:YNL248C
ORF Names:N0880
<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>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<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 identifieri559292 [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 lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<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
  • UP000002311 <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 XIV

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YNL248C

Saccharomyces Genome Database

More...
SGDi
S000005192 RPA49

<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 Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

DNA-directed RNA polymerase, 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>Mutagenesisi325 – 326ED → AA: No effect on DNA binding. 1 Publication2
Mutagenesisi356K → A: Loss of DNA binding; when associated with A-358. 1 Publication1
Mutagenesisi358S → A: Loss of DNA binding; when associated with A-356. 1 Publication1
Mutagenesisi359K → A: Loss of DNA binding. 1 Publication1
Mutagenesisi365R → A: Loss of DNA binding. 1 Publication1
Mutagenesisi393K → A: Loss of DNA binding. 1 Publication1

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000739551 – 415DNA-directed RNA polymerase I subunit RPA49Add BLAST415

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 residuei34PhosphoserineCombined sources1
Modified residuei151PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q01080

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

More...
PaxDbi
Q01080

PRoteomics IDEntifications database

More...
PRIDEi
Q01080

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q01080

<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

Component of the RNA polymerase I (Pol I) complex consisting of 14 subunits: RPA135, RPA190, RPC40, RPA14, RPB5, RPO26, RPA43, RPB8, RPA12, RPB10, RPC19, RPC10, RPA49 and RPA34. The complex is composed of a horseshoe-shaped core containing ten subunits (RPA135, RPA190, RPB5, RPO26, RPB8, RPB10, RPC10, RPA12, RPC19 and RPC40) where RPA135 and RPA190 form the DNA-binding cleft. Outside of the core, RPA14 and RPA43 form the stalk that mediates interactions with transcription initiation factors and newly synthesized RNA.

Forms a TFIIF-like heterodimer with RPA34; the heterodimer formed by RPA34 and RPA49 can be dissociated from the Pol I core giving rise to a 12 subunit form A* of Pol I (formerly called pol A) that shows impaired transcript elongation activity and increased sensitivity to alpha-amanitin. The heterodimer formed by RPA34 and RPA49 stabilizes subunit RPA12 and stimulates RPA12-dependent RNA cleavage.

6 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
35591, 493 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-1664 DNA-directed RNA Polymerase I complex

Database of interacting proteins

More...
DIPi
DIP-6577N

Protein interaction database and analysis system

More...
IntActi
Q01080, 16 interactors

Molecular INTeraction database

More...
MINTi
Q01080

STRING: functional protein association networks

More...
STRINGi
4932.YNL248C

<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

1415
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
Q01080

Database of comparative protein structure models

More...
ModBasei
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q01080

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni322 – 415Interaction with DNAAdd BLAST94

<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

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000057118

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q01080

KEGG Orthology (KO)

More...
KOi
K03005

Identification of Orthologs from Complete Genome Data

More...
OMAi
LQNPGNM

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR009668 RNA_pol-assoc_fac_A49-like

The PANTHER Classification System

More...
PANTHERi
PTHR14440 PTHR14440, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF06870 RNA_pol_I_A49, 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>. 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_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.

Q01080-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSVKRSVSEI EIESVQDQPS VAVGSFFKGF RAPSDTTFDL YKKKKSEKDE
60 70 80 90 100
FVLHGENERL EYEGYTDSSS QASNQYVVGL FNPEKKSIQL YKAPVLVSKV
110 120 130 140 150
VSKSSKNLRG PKIKSKSDTR PSALRNALGE AFGTKKAKKA IADLERNRID
160 170 180 190 200
SDKLTDSAID IVDSVRTASK DLPTRAQLDE ITSNDRPTPL ANIDATDVEQ
210 220 230 240 250
IYPIESIIPK KELQFIRVSS ILKEADKEKK LELFPYQNNS KYVAKKLDSL
260 270 280 290 300
TQPSQMTKLQ LLYYLSLLLG VYENRRVNNK TKLLERLNSP PEILVDGILS
310 320 330 340 350
RFTVIKPGQF GRSKDRSYFI DPQNEDKILC YILAIIMHLD NFIVEITPLA
360 370 380 390 400
HELNLKPSKV VSLFRVLGAI VKGATVAQAE AFGIPKSTAA SYKIATMKVP
410
FKLPEMTRRG RGPRR
Length:415
Mass (Da):46,651
Last modified:October 1, 1996 - 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:i3D9BF05440D26021
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti66T → P in AAA34380 (PubMed:1409638).Curated1
Sequence conflicti157S → C in AAA34380 (PubMed:1409638).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M96600 Genomic DNA Translation: AAA34380.1
X96722 Genomic DNA Translation: CAA65496.1
Z71524 Genomic DNA Translation: CAA96155.1
AY558027 Genomic DNA Translation: AAS56353.1
BK006947 Genomic DNA Translation: DAA10311.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S63221

NCBI Reference Sequences

More...
RefSeqi
NP_014151.1, NM_001183086.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YNL248C_mRNA; YNL248C; YNL248C

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
855473

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YNL248C

<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
M96600 Genomic DNA Translation: AAA34380.1
X96722 Genomic DNA Translation: CAA65496.1
Z71524 Genomic DNA Translation: CAA96155.1
AY558027 Genomic DNA Translation: AAS56353.1
BK006947 Genomic DNA Translation: DAA10311.1
PIRiS63221
RefSeqiNP_014151.1, NM_001183086.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3NFHX-ray2.17A/B154-399[»]
3NFIX-ray1.90A/B/C/D/E171-403[»]
4C2MX-ray2.802/M1-415[»]
4C3HX-ray3.27M1-415[»]
4C3IX-ray3.0M1-415[»]
4C3JX-ray3.35M1-415[»]
4YM7X-ray5.50AM/BM/CM/DM/EM/FM1-415[»]
5G5Lelectron microscopy4.80M1-415[»]
5LMXelectron microscopy4.90M1-415[»]
5M3Felectron microscopy3.80M1-415[»]
5M3Melectron microscopy4.00M1-415[»]
5M5Welectron microscopy3.80M1-415[»]
5M5Xelectron microscopy4.00M1-415[»]
5M5Yelectron microscopy4.00M1-415[»]
5M64electron microscopy4.60M1-415[»]
5N5Yelectron microscopy7.70M1-415[»]
5N5Zelectron microscopy7.70M1-415[»]
5N60electron microscopy7.70M1-415[»]
5N61electron microscopy3.40M1-415[»]
5OA1electron microscopy4.40M1-415[»]
5W5Yelectron microscopy3.80M1-415[»]
5W64electron microscopy4.20M1-415[»]
5W65electron microscopy4.30M1-415[»]
5W66electron microscopy3.90M1-415[»]
6H67electron microscopy3.60M1-415[»]
6H68electron microscopy4.60M1-415[»]
6HKOelectron microscopy3.42M1-415[»]
SMRiQ01080
ModBaseiSearch...

Protein-protein interaction databases

BioGridi35591, 493 interactors
ComplexPortaliCPX-1664 DNA-directed RNA Polymerase I complex
DIPiDIP-6577N
IntActiQ01080, 16 interactors
MINTiQ01080
STRINGi4932.YNL248C

PTM databases

iPTMnetiQ01080

Proteomic databases

MaxQBiQ01080
PaxDbiQ01080
PRIDEiQ01080

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYNL248C_mRNA; YNL248C; YNL248C
GeneIDi855473
KEGGisce:YNL248C

Organism-specific databases

EuPathDBiFungiDB:YNL248C
SGDiS000005192 RPA49

Phylogenomic databases

HOGENOMiHOG000057118
InParanoidiQ01080
KOiK03005
OMAiLQNPGNM

Enzyme and pathway databases

BioCyciYEAST:G3O-33245-MONOMER
ReactomeiR-SCE-73762 RNA Polymerase I Transcription Initiation
R-SCE-73772 RNA Polymerase I Promoter Escape

Miscellaneous databases

EvolutionaryTraceiQ01080

Protein Ontology

More...
PROi
PR:Q01080

Family and domain databases

InterProiView protein in InterPro
IPR009668 RNA_pol-assoc_fac_A49-like
PANTHERiPTHR14440 PTHR14440, 1 hit
PfamiView protein in Pfam
PF06870 RNA_pol_I_A49, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiRPA49_YEAST
<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: Q01080
Secondary accession number(s): D6W0U5
<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: April 1, 1993
Last sequence update: October 1, 1996
Last modified: September 18, 2019
This is version 167 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 programFungal 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. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast chromosome XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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

Do not show this banner again