Variant position: 264 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 503 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 YEKSVKDLKDAIEVLIAEKR RRISTEEKLEECMDFATELIL
Mouse YERSVKDLKDEIAVLVEKKR HKVSTAEKLEDCMDFATDLIF
Rat YERSVKDLKDEIEILVEKKR QKVSSAEKLEDCMDFATDLIF
Bovine YEKSVKDLKDAMEILIEEKR HRISTAEKLEDSIDFATELIF
Rabbit YEKSVKDLKDAIDILVEKKR RRISTAEKLEDHMDFATNLIF
Goat YEKSVKDLKDAMEILIEEKR HRISTAEKLEDCIDFATELIF
Sheep YEKSVKDLKDAMEILIEEKR HRISTAEKLEDCIDFATELIF
Horse HQKSIKELRDAVGILAEEKR HRIFTAEKLEDHVDFATDLIL
Chicken YEEAAKDLKGAMEILIEQKR QKLSTVEKLDEHMDFASQLIF
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.
Impact of R264C and R264H polymorphisms in human aromatase function.
Baravalle R.; Di Nardo G.; Bandino A.; Barone I.; Catalano S.; Ando S.; Gilardi G.;
J. Steroid Biochem. Mol. Biol. 167:23-32(2017)
Cited for: CHARACTERIZATION OF VARIANTS CYS-264 AND HIS-264; PHOSPHORYLATION; FUNCTION; CATALYTIC ACTIVITY; BIOPHYSICOCHEMICAL PROPERTIES;
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.