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Protein

Histo-blood group ABO system transferase

Gene

ABO

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

This protein is the basis of the ABO blood group system. The histo-blood group ABO involves three carbohydrate antigens: A, B, and H. A, B, and AB individuals express a glycosyltransferase activity that converts the H antigen to the A antigen (by addition of UDP-GalNAc) or to the B antigen (by addition of UDP-Gal), whereas O individuals lack such activity.

Catalytic activityi

UDP-N-acetyl-alpha-beta-D-galactosamine + glycoprotein-alpha-L-fucosyl-(1->2)-D-galactose = UDP + glycoprotein-N-acetyl-alpha-D-galactosaminyl-(1->3)-(alpha-L-fucosyl-(1->2))-beta-D-galactose.2 Publications
UDP-alpha-D-galactose + alpha-L-fucosyl-(1->2)-D-galactosyl-R = UDP + alpha-D-galactosyl-(1->3)-(alpha-L-fucosyl-(1->2))-D-galactosyl-R.2 Publications

Cofactori

Mn2+1 PublicationNote: Binds 1 Mn2+ ion per subunit.1 Publication

Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.Curated
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei126UDP-N-acetyl-galactosamineCombined sources5 Publications1
Metal bindingi211ManganeseCombined sources4 Publications1
Metal bindingi213ManganeseCombined sources4 Publications1
Binding sitei233Glycoprotein fucosyl-galactosyl groupCombined sources1 Publication1
Binding sitei245Glycoprotein fucosyl-galactosyl groupCombined sources3 Publications1
Active sitei303NucleophileBy similarity1
Binding sitei303Glycoprotein fucosyl-galactosyl groupCombined sources3 Publications1
Binding sitei326Glycoprotein fucosyl-galactosyl groupCombined sources2 Publications1

GO - Molecular functioni

  • antigen binding Source: CAFA
  • fucosylgalactoside 3-alpha-galactosyltransferase activity Source: UniProtKB-EC
  • glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase activity Source: UniProtKB-EC
  • manganese ion binding Source: CAFA
  • nucleotide binding Source: CAFA
  • transferase activity, transferring glycosyl groups Source: GO_Central

GO - Biological processi

Keywordsi

Molecular functionBlood group antigen, Glycosyltransferase, Transferase
LigandManganese, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS10887-MONOMER
BRENDAi2.4.1.37 2681
2.4.1.40 2681
UniPathwayiUPA00378

Protein family/group databases

CAZyiGT6 Glycosyltransferase Family 6

Names & Taxonomyi

Protein namesi
Recommended name:
Histo-blood group ABO system transferase
Alternative name(s):
Fucosylglycoprotein 3-alpha-galactosyltransferase
Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase
Glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase (EC:2.4.1.402 Publications)
Glycoprotein-fucosylgalactoside alpha-galactosyltransferase (EC:2.4.1.372 Publications)
Histo-blood group A transferase
Short name:
A transferase
Histo-blood group B transferase
Short name:
B transferase
NAGAT
Cleaved into the following chain:
Gene namesi
Name:ABO
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Unplaced

Organism-specific databases

HGNCiHGNC:79 ABO
MIMi110300 gene
neXtProtiNX_P16442

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; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 32CytoplasmicSequence analysisAdd BLAST32
Transmembranei33 – 53Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
Topological domaini54 – 354LumenalSequence analysisAdd BLAST301

Keywords - Cellular componenti

Golgi apparatus, Membrane, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi214M → T or V: Alters substrate specificity so that both UDP-N-acetyl-D-galactosamine and UDP-galactose are utilized. 1 Publication1
Mutagenesisi234P → S: Alters substrate specificity of group B transferase. 1
Mutagenesisi303E → A: Decreases specific activity of group B transferase almost to zero. 1 Publication1

Organism-specific databases

DisGeNETi28
MIMi616093 phenotype
PharmGKBiPA24415

Chemistry databases

ChEMBLiCHEMBL2321639
DrugBankiDB04681 BETA-METHYLLACTOSIDE
DB04680 GALACTOSE GREASE
DB03501 Galactose-uridine-5'-diphosphate
DB04679 H TYPE I TRISACCHARIDE
DB04678 H TYPE II TRISACCHARIDE
DB07633 octyl 3-deoxy-2-O-(6-deoxy-alpha-L-galactopyranosyl)-beta-D-xylo-hexopyranoside
DB03435 Uridine-5'-Diphosphate
DB02196 Uridine-Diphosphate-N-Acetylgalactosamine

Polymorphism and mutation databases

BioMutaiABO
DMDMi114949

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000122681 – 354Histo-blood group ABO system transferaseAdd BLAST354
ChainiPRO_000001226954 – 354Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase soluble formAdd BLAST301

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi113N-linked (GlcNAc...) asparagineSequence analysis1

Post-translational modificationi

The soluble form derives from the membrane form by proteolytic processing.

Keywords - PTMi

Glycoprotein

Proteomic databases

PeptideAtlasiP16442
PRIDEiP16442

PTM databases

iPTMnetiP16442
PhosphoSitePlusiP16442

Interactioni

Protein-protein interaction databases

BioGridi106546, 3 interactors

Chemistry databases

BindingDBiP16442

Structurei

Secondary structure

1354
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi82 – 84Combined sources3
Beta strandi93 – 95Combined sources3
Helixi102 – 111Combined sources10
Beta strandi115 – 122Combined sources8
Helixi124 – 129Combined sources6
Helixi130 – 140Combined sources11
Beta strandi145 – 154Combined sources10
Helixi156 – 158Combined sources3
Beta strandi168 – 174Combined sources7
Helixi181 – 198Combined sources18
Helixi200 – 203Combined sources4
Beta strandi205 – 210Combined sources6
Beta strandi212 – 216Combined sources5
Helixi222 – 224Combined sources3
Beta strandi226 – 232Combined sources7
Turni234 – 238Combined sources5
Helixi241 – 243Combined sources3
Beta strandi269 – 273Combined sources5
Helixi274 – 293Combined sources20
Helixi301 – 312Combined sources12
Beta strandi316 – 319Combined sources4
Helixi321 – 323Combined sources3
Helixi327 – 330Combined sources4
Beta strandi341 – 343Combined sources3
Helixi348 – 351Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LZ0X-ray1.80A64-354[»]
1LZ7X-ray1.65A64-354[»]
1LZIX-ray1.35A64-354[»]
1LZJX-ray1.32A64-354[»]
1R7TX-ray2.09A64-345[»]
1R7UX-ray1.61A64-345[»]
1R7VX-ray2.09A64-345[»]
1R7XX-ray1.97A64-345[»]
1R7YX-ray1.75A64-345[»]
1R80X-ray1.65A64-345[»]
1R81X-ray1.75A64-345[»]
1R82X-ray1.55A64-345[»]
1WSZX-ray1.59A64-354[»]
1WT0X-ray1.80A64-354[»]
1WT1X-ray1.55A64-354[»]
1WT2X-ray1.90A64-354[»]
1WT3X-ray1.80A64-354[»]
1XZ6X-ray1.55A64-354[»]
1ZHJX-ray1.59A64-354[»]
1ZI1X-ray1.57A64-354[»]
1ZI3X-ray1.69A64-354[»]
1ZI4X-ray1.85A64-354[»]
1ZI5X-ray1.55A64-354[»]
1ZIZX-ray1.49A64-354[»]
1ZJ0X-ray1.67A64-354[»]
1ZJ1X-ray1.65A64-354[»]
1ZJ2X-ray1.69A64-354[»]
1ZJ3X-ray1.69A64-354[»]
1ZJOX-ray1.64A64-354[»]
1ZJPX-ray1.59A64-354[»]
2A8UX-ray1.69A64-354[»]
2A8WX-ray1.59A64-354[»]
2I7BX-ray1.99A64-354[»]
2O1FX-ray1.99A64-354[»]
2O1GX-ray1.71A64-354[»]
2O1HX-ray1.67A64-354[»]
2PGVX-ray1.79A64-354[»]
2PGYX-ray2.39A64-354[»]
2RITX-ray1.43A64-354[»]
2RIXX-ray1.75A64-354[»]
2RIYX-ray1.55A64-354[»]
2RIZX-ray1.45A64-354[»]
2RJ0X-ray1.52A64-354[»]
2RJ1X-ray1.55A64-354[»]
2RJ4X-ray1.47A64-354[»]
2RJ5X-ray1.45A64-354[»]
2RJ6X-ray1.41A64-354[»]
2RJ7X-ray1.70A64-354[»]
2RJ8X-ray1.69A64-354[»]
2RJ9X-ray1.69A64-354[»]
2Y7AX-ray2.06A/B/C/D64-354[»]
3I0CX-ray1.55A69-354[»]
3I0DX-ray1.90A69-354[»]
3I0EX-ray1.81A69-354[»]
3I0FX-ray1.56A69-354[»]
3I0GX-ray1.40A69-354[»]
3I0HX-ray2.00A69-354[»]
3I0IX-ray1.90X69-354[»]
3I0JX-ray1.48A69-354[»]
3I0KX-ray2.20A69-354[»]
3I0LX-ray1.60A69-354[»]
3IOHX-ray1.25A64-354[»]
3IOIX-ray1.45A64-354[»]
3IOJX-ray1.65A/B64-354[»]
3SX3X-ray1.45A64-354[»]
3SX5X-ray1.43A64-354[»]
3SX7X-ray1.42A64-354[»]
3SX8X-ray1.47A64-354[»]
3SXAX-ray1.50A64-354[»]
3SXBX-ray1.49A64-354[»]
3SXCX-ray1.90A64-354[»]
3SXDX-ray1.55A64-354[»]
3SXEX-ray1.49A64-354[»]
3SXGX-ray1.86A64-354[»]
3U0XX-ray1.85A/B64-354[»]
3U0YX-ray1.60A/B64-354[»]
3V0LX-ray1.75A64-354[»]
3V0MX-ray1.68A/B64-354[»]
3V0NX-ray1.75A/B64-354[»]
3V0OX-ray1.65A/B64-354[»]
3V0PX-ray1.90A/B64-354[»]
3V0QX-ray1.80A/B64-354[»]
3ZGFX-ray1.70A/B64-354[»]
3ZGGX-ray1.90A64-354[»]
4C2SX-ray2.48A/B64-354[»]
4FQWX-ray2.02A64-354[»]
4FRAX-ray1.43A64-354[»]
4FRBX-ray1.54A64-354[»]
4FRDX-ray1.55A64-354[»]
4FREX-ray1.85A64-354[»]
4FRHX-ray1.80A64-354[»]
4FRLX-ray1.90A64-354[»]
4FRMX-ray1.90A64-354[»]
4FROX-ray1.75A64-354[»]
4FRPX-ray2.00A64-354[»]
4FRQX-ray2.35A64-354[»]
4GBPX-ray2.15A64-354[»]
4KC1X-ray1.50A64-346[»]
4KC2X-ray1.70A64-346[»]
4KC4X-ray1.60A64-346[»]
4KXOX-ray2.00A64-354[»]
4Y62X-ray1.60A1-354[»]
4Y63X-ray1.30A1-354[»]
4Y64X-ray1.60A1-354[»]
5BXCX-ray1.40A64-354[»]
5C1GX-ray1.46A64-354[»]
5C1HX-ray1.55A64-354[»]
5C1LX-ray1.40A64-354[»]
5C36X-ray1.55A64-354[»]
5C38X-ray1.45A64-354[»]
5C3AX-ray1.33A64-354[»]
5C3BX-ray1.40A64-354[»]
5C3DX-ray1.39A64-354[»]
5C47X-ray1.39A64-354[»]
5C48X-ray1.46A64-354[»]
5C49X-ray1.49A64-354[»]
5C4BX-ray1.54A64-354[»]
5C4CX-ray1.43A64-354[»]
5C4DX-ray1.40A64-354[»]
5C4EX-ray1.55A64-354[»]
5C4FX-ray1.41A64-354[»]
5C8RX-ray1.45A64-354[»]
5CMFX-ray1.95X64-345[»]
5CMGX-ray1.83X64-354[»]
5CMHX-ray1.61A64-354[»]
5CMIX-ray1.85A64-354[»]
5CMJX-ray1.73A64-354[»]
5CQLX-ray1.69X64-354[»]
5CQMX-ray1.65X64-354[»]
5CQNX-ray1.61X64-354[»]
5CQOX-ray1.69A64-354[»]
5CQPX-ray1.83A64-354[»]
5M79X-ray1.30A64-354[»]
5M7AX-ray1.30A64-354[»]
5M7BX-ray1.50A64-354[»]
5M7CX-ray1.60A/B64-354[»]
5M7DX-ray1.20A64-354[»]
5TJKX-ray1.45A64-354[»]
5TJLX-ray1.89A64-354[»]
5TJNX-ray1.47A64-354[»]
5TJOX-ray1.57A64-354[»]
DisProtiDP00339
ProteinModelPortaliP16442
SMRiP16442
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16442

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni121 – 123UDP-N-acetyl-galactosamine bindingCombined sources5 Publications3
Regioni211 – 213UDP-N-acetyl-galactosamine bindingCombined sources5 Publications3

Domaini

The conserved DXD motif is involved in cofactor binding. The manganese ion interacts with the beta-phosphate group of UDP and may also have a role in catalysis.

Sequence similaritiesi

Belongs to the glycosyltransferase 6 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG003563
InParanoidiP16442
KOiK00709
PhylomeDBiP16442

Family and domain databases

Gene3Di3.90.550.10, 1 hit
InterProiView protein in InterPro
IPR005076 Glyco_trans_6
IPR029044 Nucleotide-diphossugar_trans
PANTHERiPTHR10462 PTHR10462, 1 hit
PfamiView protein in Pfam
PF03414 Glyco_transf_6, 1 hit
SUPFAMiSSF53448 SSF53448, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P16442-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEVLRTLAG KPKCHALRPM ILFLIMLVLV LFGYGVLSPR SLMPGSLERG
60 70 80 90 100
FCMAVREPDH LQRVSLPRMV YPQPKVLTPC RKDVLVVTPW LAPIVWEGTF
110 120 130 140 150
NIDILNEQFR LQNTTIGLTV FAIKKYVAFL KLFLETAEKH FMVGHRVHYY
160 170 180 190 200
VFTDQPAAVP RVTLGTGRQL SVLEVRAYKR WQDVSMRRME MISDFCERRF
210 220 230 240 250
LSEVDYLVCV DVDMEFRDHV GVEILTPLFG TLHPGFYGSS REAFTYERRP
260 270 280 290 300
QSQAYIPKDE GDFYYLGGFF GGSVQEVQRL TRACHQAMMV DQANGIEAVW
310 320 330 340 350
HDESHLNKYL LRHKPTKVLS PEYLWDQQLL GWPAVLRKLR FTAVPKNHQA

VRNP
Length:354
Mass (Da):40,934
Last modified:December 1, 1992 - v2
Checksum:iA03DA16E630C1608
GO

Polymorphismi

Genetic variations in ABO define the ABO blood group system [MIMi:616093]. The ABO blood group system is the most important blood group system in blood transfusion. The sequence shown here is that of the A transferase. The B form differs by a few residues substitution. Residues 266 and 268 are important for specificity. The reference genome assembly (GRCh38/hg38) describes a non-functional O-type ABO allele. The O-type ABO allele results in a guanine deletion (NM_020469.2: c.286delG). This deletion induces a frameshift and creates a premature stop codon resulting in a truncated (117 amino acids) protein deprived of any glycosyltransferase activity (PubMed:2333095).13 Publications

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01914735G → R1 PublicationCorresponds to variant dbSNP:rs8176696Ensembl.1
Natural variantiVAR_01914836V → F1 PublicationCorresponds to variant dbSNP:rs688976Ensembl.1
Natural variantiVAR_01914963R → H1 PublicationCorresponds to variant dbSNP:rs549446Ensembl.1
Natural variantiVAR_01915074P → S2 PublicationsCorresponds to variant dbSNP:rs512770Ensembl.1
Natural variantiVAR_00340880 – 81CR → W. 2
Natural variantiVAR_003409156P → L in allele A2. 5 PublicationsCorresponds to variant dbSNP:rs1053878EnsemblClinVar.1
Natural variantiVAR_019151161R → H1 PublicationCorresponds to variant dbSNP:rs8176738Ensembl.1
Natural variantiVAR_036738163T → M in allele Aw08. 1 PublicationCorresponds to variant dbSNP:rs55756402Ensembl.1
Natural variantiVAR_003410176R → G in allele Aw08 and allele Bw08. 7 PublicationsCorresponds to variant dbSNP:rs7853989Ensembl.1
Natural variantiVAR_036739198R → W in allele Aw07. 1 Publication1
Natural variantiVAR_019152199R → C1 PublicationCorresponds to variant dbSNP:rs8176739Ensembl.1
Natural variantiVAR_036740214M → R in allele Bel01; loss of manganese binding and reduced catalytic activity. 2 Publications1
Natural variantiVAR_019153216F → I2 PublicationsCorresponds to variant dbSNP:rs8176740Ensembl.1
Natural variantiVAR_036741223E → D in allele B106. 1 Publication1
Natural variantiVAR_055227230G → R in group B transferase; lower-level protein expression and intracellular cytoplasmic mislocation. 1 Publication1
Natural variantiVAR_072628234P → A in allele B(A). 1 Publication1
Natural variantiVAR_003411235G → S in allele Bw08. 8 PublicationsCorresponds to variant dbSNP:rs8176743Ensembl.1
Natural variantiVAR_033540257P → L. Corresponds to variant dbSNP:rs8176745Ensembl.1
Natural variantiVAR_003412266L → M in allele Bw08. 8 PublicationsCorresponds to variant dbSNP:rs8176746Ensembl.1
Natural variantiVAR_003413268G → A in allele Bw08. 7 PublicationsCorresponds to variant dbSNP:rs8176747EnsemblClinVar.1
Natural variantiVAR_033541268G → R in allele Aw08. 1 PublicationCorresponds to variant dbSNP:rs41302905Ensembl.1
Natural variantiVAR_019154277V → M2 PublicationsCorresponds to variant dbSNP:rs8176748Ensembl.1
Natural variantiVAR_036742288M → R1 Publication1
Natural variantiVAR_036743291D → N in allele B104. 1 Publication1
Natural variantiVAR_036744346K → M in allele Bw08. 2 Publications1
Natural variantiVAR_036745352R → G in allele A107. 1 Publication1
Natural variantiVAR_003414352R → W in allele A106 and allele B3. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05175 mRNA Translation: AAA36792.1
X84746
, X84747, X84748, X84749, X84750, X84751, X84752 Genomic DNA Translation: CAA59233.1
AF134412 mRNA Translation: AAD26572.1
AF134413 mRNA Translation: AAD26573.1
AF134414 mRNA Translation: AAD26574.1
AH007586 Genomic DNA Translation: AAD26575.1
AH007587 Genomic DNA Translation: AAD26576.1
AH007592 Genomic DNA Translation: AAD26581.1
AJ920329 Genomic DNA Translation: CAI79116.1
AM423110 Genomic DNA Translation: CAM28424.1
AM492698 Genomic DNA Translation: CAM34526.1
AM492699 Genomic DNA Translation: CAM34527.1
AY268591 Genomic DNA Translation: AAP03430.1
BC069595 mRNA Translation: AAH69595.1
BC111575 mRNA Translation: AAI11576.1
AJ536135 Genomic DNA Translation: CAD60222.1
AJ536136 Genomic DNA Translation: CAD60223.1
D82842 Genomic DNA Translation: BAA11591.2
D82843 Genomic DNA Translation: BAA11592.2
AF016622 Genomic DNA Translation: AAB86462.1
AF448199 Genomic DNA Translation: AAQ04662.1
AF448200 Genomic DNA Translation: AAQ04663.1
AJ276689 Genomic DNA Translation: CAB81779.1
PIRiPC1165
RefSeqiNP_065202.2, NM_020469.2
UniGeneiHs.654423

Genome annotation databases

GeneIDi28
KEGGihsa:28

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiBGAT_HUMAN
AccessioniPrimary (citable) accession number: P16442
Secondary accession number(s): B0JDB9
, O14758, Q14490, Q53I57, Q6ISD4, Q6KFZ2, Q70V27, Q99484, Q99485, Q9NY01, Q9UQ68, Q9UQ69
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: December 1, 1992
Last modified: March 28, 2018
This is version 197 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Blood group antigen proteins
    Nomenclature of blood group antigens and list of entries
  2. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  7. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  8. SIMILARITY comments
    Index of protein domains and families

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