Variant position: 139 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 453 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 NATAAMKNQVARFNDLRFVG RSGRGKSFTLTITVFTNPPQV
Mouse NATAAMKNQVARFNDLRFVG RSGRGKSFTLTITVFTNPPQV
Rat NATAAMKNQVARFNDLRFVG RSGRGKSFTLTITVFTNPPQV
Xenopus laevis NATAAMKSQVARFNDLRFVG RSGRGKSFTLTITVFTNPPQV
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 – 453 Runt-related transcription factor 1
50 – 178 Runt
135 – 143 Interaction with DNA
139 – 139 Chloride 2
137 – 242 VGRSGRGKSFTLTITVFTNPPQVATYHRAIKITVDGPREPRRHRQKLDDQTKPGSLSFSERLSELEQLRRTAMRVSPHHPAPTPNPRASLNHSTAFNPQPQSQMQD -> VDGPREPRRHRQKLDDQTKPGSLSFSERLSELEQLRRTAMRVSPHHPAPTPNPRASLNHSTAFNPQPQSQMQDTRQIQPSPPWSYDQSYQYLGSIASPSVHPATPI. In isoform AML-1FC.
135 – 135 R -> A. Strongly reduces DNA-binding.
139 – 139 R -> A. Strongly reduces DNA-binding.
140 – 140 S -> G. Disrupts AML1-MTG8/ETO DNA-binding, decreases AML1-MTG8/ETO transforming activity.
142 – 142 R -> A. Strongly reduces DNA-binding.
Haploinsufficiency of CBFA2 causes familial thrombocytopenia with propensity to develop acute myelogenous leukaemia.
Song W.-J.; Sullivan M.G.; Legare R.D.; Hutchings S.; Tan X.; Kufrin D.; Ratajczak J.; Resende I.C.; Haworth C.; Hock R.; Loh M.; Felix C.; Roy D.-C.; Busque L.; Kurnit D.; Willman C.; Gewirtz A.M.; Speck N.A.; Bushweller J.H.; Li F.P.; Gardiner K.; Poncz M.; Maris J.M.; Gilliland D.G.;
Nat. Genet. 23:166-175(1999)
Cited for: VARIANTS FPDMM GLN-139 AND GLN-174;
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.