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P16442

- BGAT_HUMAN

UniProt

P16442 - BGAT_HUMAN

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Protein

Histo-blood group ABO system transferase

Gene

ABO

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- 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.
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.

Cofactori

Binds 1 manganese ion per subunit.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei126 – 1261UDP-N-acetyl-galactosamine
Metal bindingi211 – 2111Manganese
Metal bindingi213 – 2131Manganese
Binding sitei233 – 2331Glycoprotein fucosyl-galactosyl group
Binding sitei245 – 2451Glycoprotein fucosyl-galactosyl group
Binding sitei303 – 3031Glycoprotein fucosyl-galactosyl group
Binding sitei326 – 3261Glycoprotein fucosyl-galactosyl group

GO - Molecular functioni

  1. fucosylgalactoside 3-alpha-galactosyltransferase activity Source: UniProtKB-EC
  2. glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase activity Source: UniProtKB-EC
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. protein glycosylation Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Blood group antigen, Glycosyltransferase, Transferase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

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:2.4.1.40)
Glycoprotein-fucosylgalactoside alpha-galactosyltransferase (EC:2.4.1.37)
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
ProteomesiUP000005640: Unplaced

Organism-specific databases

HGNCiHGNC:79. ABO.

Subcellular locationi

Golgi apparatusGolgi stack membrane; Single-pass type II membrane protein. Secreted
Note: Membrane-bound form in trans cisternae of Golgi. Secreted into the body fluid.

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
  2. Golgi apparatus Source: UniProtKB-KW
  3. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi214 – 2141M → T or V: Alters substrate specificity so that both UDP-N-acetyl-D-galactosamine and UDP-galactose are utilized. 1 Publication
Mutagenesisi234 – 2341P → S: Alters substrate specificity of group B transferase.
Mutagenesisi303 – 3031E → A: Decreases specific activity of group B transferase almost to zero. 1 Publication

Organism-specific databases

MIMi110300. gene+phenotype.
PharmGKBiPA24415.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 354354Histo-blood group ABO system transferasePRO_0000012268Add
BLAST
Chaini54 – 354301Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase soluble formPRO_0000012269Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi113 – 1131N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

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

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiP16442.
PRIDEiP16442.

PTM databases

PhosphoSiteiP16442.

Expressioni

Gene expression databases

ExpressionAtlasiP16442. baseline.
GenevestigatoriP16442.

Interactioni

Protein-protein interaction databases

BioGridi106546. 1 interaction.

Structurei

Secondary structure

1
354
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi82 – 843
Beta strandi93 – 953
Helixi102 – 11110
Beta strandi115 – 1228
Helixi124 – 1296
Helixi130 – 14011
Beta strandi145 – 15410
Helixi156 – 1583
Beta strandi168 – 1747
Helixi181 – 19818
Helixi200 – 2034
Beta strandi205 – 2106
Beta strandi212 – 2165
Helixi222 – 2243
Beta strandi226 – 2327
Turni234 – 2385
Helixi241 – 2433
Beta strandi269 – 2735
Helixi274 – 29320
Turni299 – 3013
Helixi302 – 31211
Beta strandi316 – 3194
Helixi321 – 3233
Helixi327 – 3304
Beta strandi341 – 3433
Helixi348 – 3514

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
DisProtiDP00339.
ProteinModelPortaliP16442.
SMRiP16442. Positions 64-354.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16442.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3232CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini54 – 354301LumenalSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei33 – 5321Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni121 – 1233UDP-N-acetyl-galactosamine binding
Regioni211 – 2133UDP-N-acetyl-galactosamine binding

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

eggNOGiNOG43612.
HOVERGENiHBG003563.
InParanoidiP16442.
KOiK00709.
OrthoDBiEOG7BZVSQ.
PhylomeDBiP16442.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR005076. Glyco_trans_6.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERiPTHR10462. PTHR10462. 1 hit.
PfamiPF03414. Glyco_transf_6. 1 hit.
[Graphical view]
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

The sequence shown is that of the A transferase. The B form differs by a few residues substitutions. The O phenotype results from a single base frameshift in the N-terminal extremity of the gene, resulting in a severly truncated protein without catalytic activity.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti35 – 351G → R.1 Publication
Corresponds to variant rs8176696 [ dbSNP | Ensembl ].
VAR_019147
Natural varianti36 – 361V → F.1 Publication
Corresponds to variant rs688976 [ dbSNP | Ensembl ].
VAR_019148
Natural varianti63 – 631R → H.1 Publication
Corresponds to variant rs549446 [ dbSNP | Ensembl ].
VAR_019149
Natural varianti74 – 741P → S.2 Publications
Corresponds to variant rs512770 [ dbSNP | Ensembl ].
VAR_019150
Natural varianti80 – 812CR → W.
VAR_003408
Natural varianti156 – 1561P → L in allele A2. 5 Publications
Corresponds to variant rs1053878 [ dbSNP | Ensembl ].
VAR_003409
Natural varianti161 – 1611R → H.1 Publication
Corresponds to variant rs8176738 [ dbSNP | Ensembl ].
VAR_019151
Natural varianti163 – 1631T → M in allele Aw08. 1 Publication
Corresponds to variant rs55756402 [ dbSNP | Ensembl ].
VAR_036738
Natural varianti176 – 1761R → G in group B transferase. 7 Publications
Corresponds to variant rs7853989 [ dbSNP | Ensembl ].
VAR_003410
Natural varianti198 – 1981R → W in allele Aw07.
Corresponds to variant rs56223957 [ dbSNP | Ensembl ].
VAR_036739
Natural varianti199 – 1991R → C.1 Publication
Corresponds to variant rs8176739 [ dbSNP | Ensembl ].
VAR_019152
Natural varianti214 – 2141M → R in allele Bel01; loss of manganese binding and reduced catalytic activity. 1 Publication
Corresponds to variant rs55827808 [ dbSNP | Ensembl ].
VAR_036740
Natural varianti216 – 2161F → I.2 Publications
Corresponds to variant rs8176740 [ dbSNP | Ensembl ].
VAR_019153
Natural varianti223 – 2231E → D in allele B106. 1 Publication
VAR_036741
Natural varianti230 – 2301G → R in group B transferase; lower-level protein expression and intracellular cytoplasmic mislocation. 1 Publication
VAR_055227
Natural varianti235 – 2351G → S in group B transferase. 8 Publications
Corresponds to variant rs8176743 [ dbSNP | Ensembl ].
VAR_003411
Natural varianti257 – 2571P → L.
Corresponds to variant rs8176745 [ dbSNP | Ensembl ].
VAR_033540
Natural varianti266 – 2661L → M in group B transferase; important for the specificity. 8 Publications
Corresponds to variant rs8176746 [ dbSNP | Ensembl ].
VAR_003412
Natural varianti268 – 2681G → A in group B transferase; important for the specificity. 7 Publications
Corresponds to variant rs8176747 [ dbSNP | Ensembl ].
VAR_003413
Natural varianti268 – 2681G → R.1 Publication
Corresponds to variant rs8176747 [ dbSNP | Ensembl ].
VAR_033541
Natural varianti277 – 2771V → M.2 Publications
Corresponds to variant rs8176748 [ dbSNP | Ensembl ].
VAR_019154
Natural varianti288 – 2881M → R.1 Publication
VAR_036742
Natural varianti291 – 2911D → N in allele B104. 1 Publication
VAR_036743
Natural varianti346 – 3461K → M in allele Bw08. 2 Publications
VAR_036744
Natural varianti352 – 3521R → G in allele A107. 1 Publication
VAR_036745
Natural varianti352 – 3521R → W in allele A106 and allele B3. 1 Publication
VAR_003414

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
UCSCiuc004cda.1. human.

Polymorphism databases

DMDMi114949.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

GGDB

GlycoGene database

SeattleSNPs
Functional Glycomics Gateway - GTase

Histo-blood group ABO system transferase

Functional Glycomics Gateway - GTase

Histo-blood group ABO system transferase

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
PIRi PC1165.
RefSeqi NP_065202.2. NM_020469.2.
UniGenei Hs.654423.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1LZ0 X-ray 1.80 A 64-354 [» ]
1LZ7 X-ray 1.65 A 64-354 [» ]
1LZI X-ray 1.35 A 64-354 [» ]
1LZJ X-ray 1.32 A 64-354 [» ]
1R7T X-ray 2.09 A 64-345 [» ]
1R7U X-ray 1.61 A 64-345 [» ]
1R7V X-ray 2.09 A 64-345 [» ]
1R7X X-ray 1.97 A 64-345 [» ]
1R7Y X-ray 1.75 A 64-345 [» ]
1R80 X-ray 1.65 A 64-345 [» ]
1R81 X-ray 1.75 A 64-345 [» ]
1R82 X-ray 1.55 A 64-345 [» ]
1WSZ X-ray 1.59 A 64-354 [» ]
1WT0 X-ray 1.80 A 64-354 [» ]
1WT1 X-ray 1.55 A 64-354 [» ]
1WT2 X-ray 1.90 A 64-354 [» ]
1WT3 X-ray 1.80 A 64-354 [» ]
1XZ6 X-ray 1.55 A 64-354 [» ]
1ZHJ X-ray 1.59 A 64-354 [» ]
1ZI1 X-ray 1.57 A 64-354 [» ]
1ZI3 X-ray 1.69 A 64-354 [» ]
1ZI4 X-ray 1.85 A 64-354 [» ]
1ZI5 X-ray 1.55 A 64-354 [» ]
1ZIZ X-ray 1.49 A 64-354 [» ]
1ZJ0 X-ray 1.67 A 64-354 [» ]
1ZJ1 X-ray 1.65 A 64-354 [» ]
1ZJ2 X-ray 1.69 A 64-354 [» ]
1ZJ3 X-ray 1.69 A 64-354 [» ]
1ZJO X-ray 1.64 A 64-354 [» ]
1ZJP X-ray 1.59 A 64-354 [» ]
2A8U X-ray 1.69 A 64-354 [» ]
2A8W X-ray 1.59 A 64-354 [» ]
2I7B X-ray 1.99 A 64-354 [» ]
2O1F X-ray 1.99 A 64-354 [» ]
2O1G X-ray 1.71 A 64-354 [» ]
2O1H X-ray 1.67 A 64-354 [» ]
2PGV X-ray 1.79 A 64-354 [» ]
2PGY X-ray 2.39 A 64-354 [» ]
2RIT X-ray 1.43 A 64-354 [» ]
2RIX X-ray 1.75 A 64-354 [» ]
2RIY X-ray 1.55 A 64-354 [» ]
2RIZ X-ray 1.45 A 64-354 [» ]
2RJ0 X-ray 1.52 A 64-354 [» ]
2RJ1 X-ray 1.55 A 64-354 [» ]
2RJ4 X-ray 1.47 A 64-354 [» ]
2RJ5 X-ray 1.45 A 64-354 [» ]
2RJ6 X-ray 1.41 A 64-354 [» ]
2RJ7 X-ray 1.70 A 64-354 [» ]
2RJ8 X-ray 1.69 A 64-354 [» ]
2RJ9 X-ray 1.69 A 64-354 [» ]
2Y7A X-ray 2.06 A/B/C/D 64-354 [» ]
3I0C X-ray 1.55 A 69-354 [» ]
3I0D X-ray 1.90 A 69-354 [» ]
3I0E X-ray 1.81 A 69-354 [» ]
3I0F X-ray 1.56 A 69-354 [» ]
3I0G X-ray 1.40 A 69-354 [» ]
3I0H X-ray 2.00 A 69-354 [» ]
3I0I X-ray 1.90 X 69-354 [» ]
3I0J X-ray 1.48 A 69-354 [» ]
3I0K X-ray 2.20 A 69-354 [» ]
3I0L X-ray 1.60 A 69-354 [» ]
3IOH X-ray 1.25 A 64-354 [» ]
3IOI X-ray 1.45 A 64-354 [» ]
3IOJ X-ray 1.65 A/B 64-354 [» ]
3SX3 X-ray 1.45 A 64-354 [» ]
3SX5 X-ray 1.43 A 64-354 [» ]
3SX7 X-ray 1.42 A 64-354 [» ]
3SX8 X-ray 1.47 A 64-354 [» ]
3SXA X-ray 1.50 A 64-354 [» ]
3SXB X-ray 1.49 A 64-354 [» ]
3SXC X-ray 1.90 A 64-354 [» ]
3SXD X-ray 1.55 A 64-354 [» ]
3SXE X-ray 1.49 A 64-354 [» ]
3SXG X-ray 1.86 A 64-354 [» ]
3U0X X-ray 1.85 A/B 64-354 [» ]
3U0Y X-ray 1.60 A/B 64-354 [» ]
3V0L X-ray 1.75 A 64-354 [» ]
3V0M X-ray 1.68 A/B 64-354 [» ]
3V0N X-ray 1.75 A/B 64-354 [» ]
3V0O X-ray 1.65 A/B 64-354 [» ]
3V0P X-ray 1.90 A/B 64-354 [» ]
3V0Q X-ray 1.80 A/B 64-354 [» ]
3ZGF X-ray 1.70 A/B 64-354 [» ]
3ZGG X-ray 1.90 A 64-354 [» ]
4C2S X-ray 2.48 A/B 64-354 [» ]
4FQW X-ray 2.02 A 64-354 [» ]
4FRA X-ray 1.43 A 64-354 [» ]
4FRB X-ray 1.54 A 64-354 [» ]
4FRD X-ray 1.55 A 64-354 [» ]
4FRE X-ray 1.85 A 64-354 [» ]
4FRH X-ray 1.80 A 64-354 [» ]
4FRL X-ray 1.90 A 64-354 [» ]
4FRM X-ray 1.90 A 64-354 [» ]
4FRO X-ray 1.75 A 64-354 [» ]
4FRP X-ray 2.00 A 64-354 [» ]
4FRQ X-ray 2.35 A 64-354 [» ]
4GBP X-ray 2.15 A 64-354 [» ]
4KC1 X-ray 1.50 A 64-346 [» ]
4KC2 X-ray 1.70 A 64-346 [» ]
4KC4 X-ray 1.60 A 64-346 [» ]
4KXO X-ray 2.00 A 64-354 [» ]
DisProti DP00339.
ProteinModelPortali P16442.
SMRi P16442. Positions 64-354.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106546. 1 interaction.

Chemistry

ChEMBLi CHEMBL2321639.

Protein family/group databases

CAZyi GT6. Glycosyltransferase Family 6.

PTM databases

PhosphoSitei P16442.

Polymorphism databases

DMDMi 114949.

Proteomic databases

PaxDbi P16442.
PRIDEi P16442.

Protocols and materials databases

DNASUi 28.
Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 28.
KEGGi hsa:28.
UCSCi uc004cda.1. human.

Organism-specific databases

CTDi 28.
GeneCardsi GC09M136130.
HGNCi HGNC:79. ABO.
MIMi 110300. gene+phenotype.
neXtProti NX_P16442.
PharmGKBi PA24415.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG43612.
HOVERGENi HBG003563.
InParanoidi P16442.
KOi K00709.
OrthoDBi EOG7BZVSQ.
PhylomeDBi P16442.

Enzyme and pathway databases

UniPathwayi UPA00378 .

Miscellaneous databases

EvolutionaryTracei P16442.
GeneWikii ABO_(gene).
GenomeRNAii 28.
NextBioi 97.
PROi P16442.
SOURCEi Search...

Gene expression databases

ExpressionAtlasi P16442. baseline.
Genevestigatori P16442.

Family and domain databases

Gene3Di 3.90.550.10. 1 hit.
InterProi IPR005076. Glyco_trans_6.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view ]
PANTHERi PTHR10462. PTHR10462. 1 hit.
Pfami PF03414. Glyco_transf_6. 1 hit.
[Graphical view ]
SUPFAMi SSF53448. SSF53448. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of DNA complementary to human UDP-GalNAc: Fuc alpha 1-->2Gal alpha 1-->3GalNAc transferase (histo-blood group A transferase) mRNA."
    Yamamoto F., Marken J., Tsuji T., White T., Clausen H., Hakomori S.
    J. Biol. Chem. 265:1146-1151(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
  2. "Molecular genetic basis of the histo-blood group ABO system."
    Yamamoto F., Clausen H., White T., Marken J., Hakomori S.
    Nature 345:229-233(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LEU-156.
  4. "Human histo-blood group ABO gene locus alleles."
    Yamamoto F.
    Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANTS LEU-156; GLY-176; SER-235 AND MET-266.
  5. "A weak blood group A phenotype caused by a translation-initiator mutation in the ABO gene."
    Seltsam A., Das Gupta C., Bade-Doeding C., Blasczyk R.
    Transfusion 46:434-440(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Peripheral blood.
  6. "Weak blood group B phenotypes may be caused by variations in the CCAAT-binding factor/NF-Y enhancer region of the ABO gene."
    Seltsam A., Wagner F.F., Gruger D., Gupta C.D., Bade-Doeding C., Blasczyk R.
    Transfusion 47:2330-2335(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Peripheral blood.
  7. "Aberrant intracellular trafficking of a variant B glycosyltransferase."
    Seltsam A., Gruger D., Just B., Figueiredo C., Gupta C.D., Deluca D.S., Blasczyk R.
    Transfusion 48:1898-1905(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-230; SER-235; MET-266 AND ALA-268.
    Tissue: Peripheral blood.
  8. SeattleSNPs variation discovery resource
    Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-35; PHE-36; HIS-63; SER-74; LEU-156; HIS-161; GLY-176; CYS-199; ILE-216; SER-235; MET-266; ALA-268 AND MET-277.
  9. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS GLY-176; SER-235; MET-266 AND ALA-268.
  10. "The nature of diversity and diversification at the ABO locus."
    Seltsam A., Hallensleben M., Kollmann A., Blasczyk R.
    Blood 102:3035-3042(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 11-354, VARIANTS SER-74; LEU-156; MET-163; GLY-176; SER-235; MET-266; ALA-268; ARG-268; ARG-288 AND MET-346.
  11. "Molecular genetic analysis of variant phenotypes of the ABO blood group system."
    Ogasawara K., Yabe R., Uchikawa M., Saitou N., Bannai M., Nakata K., Takenaka M., Fujisawa K., Ishikawa Y., Juji T., Tokunaga K.
    Blood 88:2732-2737(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 81-354, VARIANTS LEU-156; GLY-176; ARG-214; ILE-216; ASP-223; SER-235; MET-266; ALA-268; MET-277; ASN-291; GLY-352 AND TRP-352.
  12. "Heterogeneity of the blood group Ax allele: genetic recombination of common alleles can result in the Ax phenotype."
    Olsson M.L., Chester M.A.
    Transfus. Med. 8:231-238(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 81-354.
  13. "Evolution of the O alleles of the human ABO blood group gene."
    Roubinet F., Despiau S., Calafell F., Jin F., Bertanpetit J., Saitou N., Blancher A.
    Transfusion 44:707-715(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 11-354, VARIANTS GLY-176; SER-235; MET-266 AND ALA-268.
  14. "A novel B Transferase."
    Seltsam A., Hallensleben M., Salama A., Blasczyk R.
    Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 126-354, VARIANTS GLY-176; SER-235 AND MET-346.
  15. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 146-334, VARIANTS MET-266 AND ALA-268.
  16. "Sugar-nucleotide donor specificity of histo-blood group A and B transferases is based on amino acid substitutions."
    Yamamoto F., Hakomori S.
    J. Biol. Chem. 265:19257-19262(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  17. "The structural basis for specificity in human ABO(H) blood group biosynthesis."
    Patenaude S.I., Seto N.O.L., Borisova S.N., Szpacenko A., Marcus S.L., Palcic M.M., Evans S.V.
    Nat. Struct. Biol. 9:685-690(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 64-354, METAL-BINDING, MUTAGENESIS OF GLU-303.
  18. "A single point mutation reverses the donor specificity of human blood group B-synthesizing galactosyltransferase."
    Marcus S.L., Polakowski R., Seto N.O.L., Leinala E., Borisova S., Blancher A., Roubinet F., Evans S.V., Palcic M.M.
    J. Biol. Chem. 278:12403-12405(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 64-345 OF MUTANT SER-234 IN COMPLEX WITH GLYCOPROTEIN FUCOSYL-GALACTOSE ANALOG.
  19. "The influence of an intramolecular hydrogen bond in differential recognition of inhibitory acceptor analogs by human ABO(H) blood group A and B glycosyltransferases."
    Nguyen H.P., Seto N.O.L., Cai Y., Leinala E.K., Borisova S.N., Palcic M.M., Evans S.V.
    J. Biol. Chem. 278:49191-49195(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 64-345 IN COMPLEXES WITH UDP; UDP-N-ACETYL-GALACTOSAMINE; UDP-GALACTOSE AND GLYCOPROTEIN FUCOSYL-GALACTOSE ANALOGS.
  20. "Structural basis for the inactivity of human blood group O2 glycosyltransferase."
    Lee H.J., Barry C.H., Borisova S.N., Seto N.O.L., Zheng R.B., Blancher A., Evans S.V., Palcic M.M.
    J. Biol. Chem. 280:525-529(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS) OF 64-354 OF MUTANTS SER-74 AND ARG-268 IN COMPLEXES WITH GLYCOPROTEIN FUCOSYL-GALACTOSE ANALOG AND UDP-N-ACETYL-GALACTOSAMINE.
  21. "Differential recognition of the type I and II H antigen acceptors by the human ABO(H) blood group A and B glycosyltransferases."
    Letts J.A., Rose N.L., Fang Y.R., Barry C.H., Borisova S.N., Seto N.O.L., Palcic M.M., Evans S.V.
    J. Biol. Chem. 281:3625-3632(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS) OF 64-354 OF HISTO-BLOOD GROUP GROUP A TRANSFERASE AND HISTO-BLOOD GROUP GROUP B TRANSFERASE IN COMPLEXES WITH GLYCOPROTEIN FUCOSYL-GALACTOSE ANALOGS.
  22. "Structural effects of naturally occurring human blood group B galactosyltransferase mutations adjacent to the DXD motif."
    Persson M., Letts J.A., Hosseini-Maaf B., Borisova S.N., Palcic M.M., Evans S.V., Olsson M.L.
    J. Biol. Chem. 282:9564-9570(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) OF 64-354 OF MUTANTS ARG-214 AND THR-214, COFACTOR, CHARACTERIZATION OF VARIANT ARG-214, MUTAGENESIS OF MET-214.

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 historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: December 1, 1992
Last modified: October 29, 2014
This is version 165 of the entry and version 2 of the sequence. [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

External Data

Dasty 3