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 103 (02 Dec 2020)
Sequence version 1 (01 Jun 2001)
Previous versions | rss
Add a publicationFeedback
Protein

Chondroitin synthase

Gene

fcbD

Organism
Pasteurella multocida (strain Pm70)
Status
Reviewed-Annotation score:

Annotation score:3 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>
-Protein inferred from homologyi <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

Glycosyltransferase that catalyzes elongation of chondroitin, a polysaccharide composed of a repeating disaccharide of N-acetylgalactosamine (GalNAc) and glucuronic acid (GlcUA) units, by alternatively transferring the GlcUA and GalNAc moiety from UDP-GlcUA and UDP-GalNAc to the non-reducing ends of the chondroitin chain. Each chondroitin unit has the composition beta-(1->4)-GlcUA-beta-(1->3)-GalNAc.

By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mn2+By similarity

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 sitei158UDP-N-acetyl-alpha-D-galactosamine; via carbonyl oxygenBy similarity1
Binding sitei162UDP-N-acetyl-alpha-D-galactosamineBy similarity1
Binding sitei189UDP-N-acetyl-alpha-D-galactosamineBy similarity1
Binding sitei218UDP-N-acetyl-alpha-D-galactosamineBy similarity1
Binding sitei224UDP-N-acetyl-alpha-D-galactosamineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi242Manganese 1By similarity1
Metal bindingi387Manganese 1; via tele nitrogenBy similarity1
Binding sitei442UDP-alpha-D-glucuronate; via amide nitrogenBy similarity1
Binding sitei470UDP-alpha-D-glucuronateBy similarity1
Metal bindingi522Manganese 2By similarity1
Binding sitei582UDP-alpha-D-glucuronate; via tele nitrogenBy similarity1
Metal bindingi632Manganese 2; via tele nitrogenBy similarity1

<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 functionGlycosyltransferase, Multifunctional enzyme, Transferase
LigandManganese, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
PMUL272843:G1FZ8-815-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.4.1.175, 4558

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
GT2, Glycosyltransferase Family 2

<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:
Chondroitin synthase
Short name:
CS
Including the following 2 domains:
Glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase (EC:2.4.1.175By similarity)
Alternative name(s):
UDP-GalNAc transferase
N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase (EC:2.4.1.226By similarity)
Alternative name(s):
UDP-GlcUA transferase
<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:fcbD
Ordered Locus Names:PM0775
<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>OrganismiPasteurella multocida (strain Pm70)
<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 identifieri272843 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaePasteurella
<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
  • UP000000809 <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

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Cell membrane, Membrane

<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_00000592581 – 965Chondroitin synthaseAdd BLAST965

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q9CMP0

<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

3D structure databases

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

More...
SMRi
Q9CMP0

Database of comparative protein structure models

More...
ModBasei
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

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>Regioni132 – 418Galactosaminyltransferase; A1 domainBy similarityAdd BLAST287
Regioni240 – 241UDP-N-acetyl-alpha-D-galactosamine bindingBy similarity2
Regioni362 – 363UDP-N-acetyl-alpha-D-galactosamine bindingBy similarity2
Regioni419 – 683Glucuronosyltransferase; A2 domainBy similarityAdd BLAST265
Regioni518 – 521UDP-alpha-D-glucuronate bindingBy similarity4
Regioni604 – 605UDP-alpha-D-glucuronate bindingBy similarity2

<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

Keywords - Domaini

Repeat

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_013018_0_0_6

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.90.550.10, 2 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001173, Glyco_trans_2-like
IPR029044, Nucleotide-diphossugar_trans

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00535, Glycos_transf_2, 2 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF53448, SSF53448, 2 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

Q9CMP0-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNTLSQAIKA YNSNDYELAL KLFEKSAETY GRKIVEFQII KCKEKLSTNS
60 70 80 90 100
YVSEDKKNSV CDSSLDIATQ LLLSNVKKLT LSESEKNSLK NKWKSITGKK
110 120 130 140 150
SENAEIRKVE LVPKDFPKDL VLAPLPDHVN DFTWYKNRKK SLGIKPVNKN
160 170 180 190 200
IGLSIIIPTF NRSRILDITL ACLVNQKTNY PFEVVVADDG SKENLLTIVQ
210 220 230 240 250
KYEQKLDIKY VRQKDYGYQL CAVRNLGLRT AKYDFVSILD CDMAPQQLWV
260 270 280 290 300
HSYLTELLED NDIVLIGPRK YVDTHNITAE QFLNDPYLIE SLPETATNNN
310 320 330 340 350
PSITSKGNIS LDWRLEHFKK TDNLRLCDSP FRYFSCGNVA FSKEWLNKVG
360 370 380 390 400
WFDEEFNHWG GEDVEFGYRL FAKGCFFRVI DGGMAYHQEP PGKENETDRE
410 420 430 440 450
AGKSITLKIV KEKVPYIYRK LLPIEDSHIH RIPLVSIYIP AYNCANYIQR
460 470 480 490 500
CVDSALNQTV VDLEVCICND GSTDNTLEVI NKLYGNNPRV RIMSKPNGGI
510 520 530 540 550
ASASNAAVSF AKGYYIGQLD SDDYLEPDAV ELCLKEFLKD KTLACVYTTN
560 570 580 590 600
RNVNPDGSLI ANGYNWPEFS REKLTTAMIA HHFRMFTIRA WHLTDGFNEK
610 620 630 640 650
IENAVDYDMF LKLSEVGKFK HLNKICYNRV LHGDNTSIKN LDTQKKNHFV
660 670 680 690 700
VVNQSLNRQR VSNYNYDEFD NLDESRKYIF NKTADYQEEI DILKDIKIVQ
710 720 730 740 750
RKDAKVAISI FYPNRLDGLV KKLNNIIEYN KNVLIIVLHI DKNHLTSDIK
760 770 780 790 800
KEILEFHNKN QINILLNNDV SYYTNNRLIK TKAHLSNMNK LRQLNLNLEY
810 820 830 840 850
IIFDNHDSLF IKNDSYNHIK KYDIGMNFSS LTNDWINKIN AHSPFKNLIK
860 870 880 890 900
KYFNDNDLKT INMKGASQGM FIKYTLAHDI ATIMKEVITL CQSTDSVPEY
910 920 930 940 950
NTEDIWFQFA LLILEKKTGH VFNKTSTLTY MPWERKLQWT NEQIESAKRG
960
ENIPVNKFII NSITL
Length:965
Mass (Da):111,601
Last modified:June 1, 2001 - v1
<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:i9C4B2CF80E1A6BD7
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 conflicti157I → T in AAK17921 (PubMed:11230405).Curated1
Sequence conflicti170L → S in AAK17921 (PubMed:11230405).Curated1
Sequence conflicti600K → N in AAF97500 (PubMed:10818104).Curated1
Sequence conflicti640 – 643NLDT → KLGI in AAF97500 (PubMed:10818104).Curated4
Sequence conflicti660 – 663RVSN → GINY in AAF97500 (PubMed:10818104).Curated4
Sequence conflicti668E → K in AAF97500 (PubMed:10818104).Curated1
Sequence conflicti671N → D in AAF97500 (PubMed:10818104).Curated1
Sequence conflicti685D → E in AAF97500 (PubMed:10818104).Curated1
Sequence conflicti690I → M in AAF97500 (PubMed:10818104).Curated1
Sequence conflicti696 – 701IKIVQR → LKLIQN in AAF97500 (PubMed:10818104).Curated6
Sequence conflicti706 – 708VAI → IAV in AAF97500 (PubMed:10818104).Curated3
Sequence conflicti715 – 717RLD → TLN in AAF97500 (PubMed:10818104).Curated3
Sequence conflicti733 – 740VLIIVLHI → IFVIILHV in AAF97500 (PubMed:10818104).Curated8
Sequence conflicti747S → P in AAF97500 (PubMed:10818104).Curated1
Sequence conflicti755 – 762EFHNKNQI → AFYHKHQV in AAF97500 (PubMed:10818104).Curated8
Sequence conflicti770V → I in AAF97500 (PubMed:10818104).Curated1
Sequence conflicti775N → S in AAF97500 (PubMed:10818104).Curated1
Sequence conflicti782K → E in AAF97500 (PubMed:10818104).Curated1
Sequence conflicti788M → I in AAF97500 (PubMed:10818104).Curated1
Sequence conflicti792R → S in AAF97500 (PubMed:10818104).Curated1
Sequence conflicti798L → C in AAF97500 (PubMed:10818104).Curated1
Sequence conflicti811I → V in AAF97500 (PubMed:10818104).Curated1
Sequence conflicti817 – 819NHI → AYM in AAF97500 (PubMed:10818104).Curated3
Sequence conflicti824I → V in AAF97500 (PubMed:10818104).Curated1
Sequence conflicti830S → A in AAF97500 (PubMed:10818104).Curated1
Sequence conflicti833N → H in AAF97500 (PubMed:10818104).Curated1
Sequence conflicti837N → E in AAF97500 (PubMed:10818104).Curated1
Sequence conflicti843S → P in AAF97500 (PubMed:10818104).Curated1
Sequence conflicti847N → K in AAF97500 (PubMed:10818104).Curated1
Sequence conflicti851K → T in AAF97500 (PubMed:10818104).Curated1
Sequence conflicti859 – 863KTINM → RSMNV in AAF97500 (PubMed:10818104).Curated5
Sequence conflicti872I → M in AAF97500 (PubMed:10818104).Curated1
Sequence conflicti875 – 884TLAHDIATIM → ALPHELLTII in AAF97500 (PubMed:10818104).Curated10
Sequence conflicti890L → S in AAF97500 (PubMed:10818104).Curated1
Sequence conflicti894T → I in AAF97500 (PubMed:10818104).Curated1
Sequence conflicti910A → V in AAT10183 (Ref. 4) Curated1
Sequence conflicti945E → Q in AAF97500 (PubMed:10818104).Curated1
Sequence conflicti949R → K in AAF97500 (PubMed:10818104).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
AF195517 Genomic DNA Translation: AAF97500.2
AF302467 Genomic DNA Translation: AAK17921.1
AY604234 Genomic DNA Translation: AAT10183.1
AE004439 Genomic DNA Translation: AAK02859.1

NCBI Reference Sequences

More...
RefSeqi
WP_010906847.1, NC_002663.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAK02859; AAK02859; PM0775

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
pmu:PM0775

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|272843.6.peg.784

<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
AF195517 Genomic DNA Translation: AAF97500.2
AF302467 Genomic DNA Translation: AAK17921.1
AY604234 Genomic DNA Translation: AAT10183.1
AE004439 Genomic DNA Translation: AAK02859.1
RefSeqiWP_010906847.1, NC_002663.1

3D structure databases

SMRiQ9CMP0
ModBaseiSearch...

Protein family/group databases

CAZyiGT2, Glycosyltransferase Family 2

Proteomic databases

PRIDEiQ9CMP0

Genome annotation databases

EnsemblBacteriaiAAK02859; AAK02859; PM0775
KEGGipmu:PM0775
PATRICifig|272843.6.peg.784

Phylogenomic databases

HOGENOMiCLU_013018_0_0_6

Enzyme and pathway databases

BioCyciPMUL272843:G1FZ8-815-MONOMER
BRENDAi2.4.1.175, 4558

Family and domain databases

Gene3Di3.90.550.10, 2 hits
InterProiView protein in InterPro
IPR001173, Glyco_trans_2-like
IPR029044, Nucleotide-diphossugar_trans
PfamiView protein in Pfam
PF00535, Glycos_transf_2, 2 hits
SUPFAMiSSF53448, SSF53448, 2 hits

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 nameiCHS_PASMU
<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: Q9CMP0
Secondary accession number(s): Q6PKM8, Q9AHL6, Q9KJ99
<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: April 26, 2005
Last sequence update: June 1, 2001
Last modified: December 2, 2020
This is version 103 of the entry and version 1 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 programProkaryotic 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

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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

Do not show this banner again