Sequence information
Variant position: 170 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 1132 The length of the canonical sequence.
Location on the sequence:
VHLLARCALFVLVAPSCAYQ
V CGPPLYQLGAATQARPPPHA
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 VHLLARCALFVLVAPSCAYQV CGPPLYQLGAAT------QA--RPPPHA
THLLARCALYLLVAPSCAYQV CGPPLYDLCAPA------SL
Mouse VYLLAHCALYLLVPPSCAYQV CGSPLYQICATTDIWPSVSA
Rat VYLLSHCALYLLVPPSCAYQV CGSPLYQICATTDTWSSVPA
Bovine THLLSRCALYLLVPPTCAYQV CGPPLYDLRAAA------AA
Baker's yeast VDLLINYTV-IQFNGQFFTQI VG------------------
Fission yeast HYLLSKGSIFEALPNDNYLQI SGIPLF--------------
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
1 – 1132
Telomerase reverse transcriptase
Region
1 – 230
RNA-interacting domain 1
Region
58 – 197
GQ motif
Site
169 – 169
Required for optimal binding of telomeric ssDNA and incorporation of nucleotides at the second position of the template
Mutagenesis
169 – 169
Q -> A. About 80% loss of enzymatic activity. Greatly reduced incorporation of second nucleotide. Altered strength of binding to ssDNA. Little effect on repeat addition processivity, nor on TR interaction nor on protein levels.
Mutagenesis
169 – 169
Q -> N. About 85% loss of enzymatic activity. Greatly reduced incorporation of second nucleotide. Altered strength of binding to ssDNA. No effect on protein levels nor on TR interaction.
Mutagenesis
169 – 169
Q -> T. About 90% loss of enzymatic activity. Greatly reduced incorporation of second nucleotide. Altered strength of binding to ssDNA. No effect on protein levels nor on TR interaction.
Literature citations
Syndrome complex of bone marrow failure and pulmonary fibrosis predicts germline defects in telomerase.
Parry E.M.; Alder J.K.; Qi X.; Chen J.J.; Armanios M.;
Blood 117:5607-5611(2011)
Cited for: VARIANTS PFBMFT1 MET-170; THR-716; PHE-841; ARG-902 AND PHE-1025; CHARACTERIZATION OF VARIANTS PFBMFT1 MET-170; THR-716; PHE-841 AND PHE-1025;
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.