{{Rsnum
|rsid=35213748
|Chromosome=16
|Orientation=plus
|geno1=(C;C)
|geno2=(C;T)
|geno3=(T;T)
|Gene=HBA2
|position=177008
|Assembly=GRCh38
|GenomeBuild=38.1
|dbSNPBuild=141
|Gene_s=HBA1
}}{{omim
|id=141800
|rsnum=35213748
|variant=0092
}}{{ClinVar
|rsid=35213748
|Reversed=0
|FwdREF=C
|FwdALT=T
|REF=C
|ALT=T
|RSPOS=227007
|CHROM=16
|dbSNPBuildID=126
|SSR=0
|SAO=1
|VP=0x050368000a01000002110100
|GENEINFO=HBA1:3039
|GENE_NAME=HBA1
|GENE_ID=3039
|WGT=1
|VC=SNV
|CLNALLE=1
|CLNHGVS=NC_000016.9:g.227007C>T
|CLNORIGIN=1
|CLNSIG=1
|Tags=PM;PMC;S3D;SLO;NSM;REF;OTHERKG;LSD;OM
}}{{PMID Auto
|PMID=235745
|Title=High cooperativity of haemoglobin M Boston in the completely reduced state.
}}

{{PMID Auto
|PMID=4521212
|Title=Structure of hemoglobin M Boston, a variant with a five-coordinated ferric heme.
|OA=1
}}

{{PMID Auto
|PMID=6255985
|Title=Proton nuclear magnetic resonance studies of hemoglobins M Boston (alpha 58E7 His leads to Tyr) and M Milwaukee (beta 67E11 Val leads to Glu): spectral assignments of hyperfine-shifted proton resonances and of proximal histidine (E7) NH resonances to the alpha and beta chains of normal human adult hemoglobin.
}}