Variant position: 74 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 354 The length of the canonical sequence.
Location on the sequence:
The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.
Residue conservation: The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human AVREPDHLQRVSLPRMVYPQ PKVLTPCRKDVLVVTPWLAPI
Mouse --------HPGAVTRNAYLQ PRVLKPTRKDVLVLTPWLAPI
Sequence annotation in neighborhood: The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:
Type: the type of sequence feature. Positions: endpoints of the sequence feature. Description: contains additional information about the feature.
Type Positions Description
1 – 354 Histo-blood group ABO system transferase
54 – 354 Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase soluble form
54 – 354 Lumenal
SeattleSNPs variation discovery resource;
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]; POLYMORPHISM; 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;
The nature of diversity and diversification at the ABO locus.
Seltsam A.; Hallensleben M.; Kollmann A.; Blasczyk R.;
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 11-354; POLYMORPHISM; VARIANTS SER-74; LEU-156; MET-163; GLY-176; TRP-198; SER-235; MET-266; ALA-268; ARG-268; ARG-288 AND MET-346;
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)
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;
Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.