Sequence information
Variant position: 75 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 142 The length of the canonical sequence.
Location on the sequence:
QVKGHGKKVADALTNAVAHV
D DMPNALSALSDLHAHKLRVD
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 QVKGHGKKVADALTNAVAHVD DMPNALSALSDLHAHKLRVD
Gorilla QVKGHGKKVADALTNAVAHVD DMPNALSALSDLHAHKLRVD
QVKAHGKKVADALTTAVAHLD DLPGALSALSDLHAYKLRVD
Rhesus macaque QVKGHGKKVADALTLAVGHVD DMPNALSALSDLHAHKLRVD
Chimpanzee QVKGHGKKVADALTNAVAHVD DMPNALSALSDLHAHKLRVD
Mouse QVKGHGKKVADALASAAGHLD DLPGALSALSDLHAHKLRVD
Rat QVKAHGKKVADALAKAADHVE DLPGALSTLSDLHAHKLRVD
Pig QVKAHGQKVADALTKAVGHLD DLPGALSALSDLHAHKLRVD
Bovine QVKGHGAKVAAALTKAVEHLD DLPGALSELSDLHAHKLRVD
Rabbit QIKAHGKKVSEALTKAVGHLD DLPGALSTLSDLHAHKLRVD
Sheep QVKGHGEKVAAALTKAVGHLD DLPGTLSDLSDLHAHKLRVD
Cat QVKAHGQKVADALTQAVAHMD DLPTAMSALSDLHAYKLRVD
Horse QVKAHGKKVGDALTLAVGHLD DLPGALSNLSDLHAHKLRVD
Chicken QIKGHGKKVVAALIEAANHID DIAGTLSKLSDLHAHKLRVD
Xenopus tropicalis HILAHGKKVSDALNEACNHLD NIAGCLSKLSDLHAYDLRVD
Zebrafish PVKKHGKTIMGAVGEAISKID DLVGGLAALSELHAFKLRVD
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
Chain
2 – 142
Hemoglobin subunit alpha
Metal binding
59 – 59
Iron (heme b distal ligand)
Metal binding
88 – 88
Iron (heme b proximal ligand)
Site
57 – 57
Not glycated
Site
61 – 61
Not glycated
Site
91 – 91
Not glycated
Glycosylation
62 – 62
N-linked (Glc) (glycation) lysine
Turn
73 – 75
Literature citations
Structural characterizations of hemoglobins J-Buda (alpha 61 (E10) Lys-to-Asn) and G-Pest (alpha 74 (EF3) Asp-to-Asn).
Brimhall B.J.; Duerst M.; Hollan S.R.; Stenzel P.; Szelenyi J.; Jones R.T.;
Cited for: VARIANTS J-BUDA ASN-62 AND G-PEST ASN-75;
Disclaimer:
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.