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:
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 VHLLARCALFVLVAPSCAYQ VCGPPLYQLGAAT------QA--RPPPHA
Mouse VYLLAHCALYLLVPPSCAYQ VCGSPLYQICATTDIWPSVSA
Rat VYLLSHCALYLLVPPSCAYQ VCGSPLYQICATTDTWSSVPA
Bovine THLLSRCALYLLVPPTCAYQ VCGPPLYDLRAAA------AA
Dog THLLARCALYLLVAPSCAYQ VCGPPLYDLCAPA------SL
Baker's yeast VDLLINYTV-IQFNGQFFTQ IVG------------------
Fission yeast HYLLSKGSIFEALPNDNYLQ ISGIPLF--------------
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 – 1132 Telomerase reverse transcriptase
1 – 230 RNA-interacting domain 1
58 – 197 GQ motif
169 – 169 Required for optimal binding of telomeric ssDNA and incorporation of nucleotides at the second position of the template
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.
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.
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.
No reference for the current variant in UniProtKB/Swiss-Prot.
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