Variant position: 45 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 1863 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 PICLELIKEPVSTKCDHIFC KFCMLKLLNQKKGPSQCPLCK
Gorilla PICLELIKEPVSTKCDHIFC KFCMLKLLNQKKGPSQCPLCK
Rhesus macaque PICLELIKEPVSTKCDHIFC RFCMLKLLNQKKGPSQCPLCK
Chimpanzee PICLELIKEPVSTKCDHIFC KFCMLKLLNQKKGPSQCPLCK
Mouse PICLELIKEPVSTKCDHIFC KFCMLKLLNQKKGPSQCPLCK
Rat PICLELIKEPVSTQCDHIFC KFCMLKLLNQKKGPSQCPLCK
Bovine PICLELIKEPVSTKCDHIFC KFCMLKLLNQKKGPSQCPLCK
Caenorhabditis elegans GICCSTYKDPILSTCFHIFC RSCINACFERKR-KVQCPICR
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 – 1863 Breast cancer type 1 susceptibility protein
24 – 65 RING-type
1 – 47 Missing. In isoform 8.
26 – 26 I -> A. Disrupts the interaction with E2 enzymes, thereby abolishing the E3 ubiquitin-protein ligase activity.
26 – 26 I -> E. No ubiquitination of RBBP8. No restoration RBBP8-mediated focus formation or G2/M checkpoint control upon DNA damage.
A high-throughput functional complementation assay for classification of BRCA1 missense variants.
Bouwman P.; van der Gulden H.; van der Heijden I.; Drost R.; Klijn C.N.; Prasetyanti P.; Pieterse M.; Wientjens E.; Seibler J.; Hogervorst F.B.; Jonkers J.;
Cancer Discov. 3:1142-1155(2013)
Cited for: CHARACTERIZATION OF VARIANTS BC PHE-4; THR-18; GLN-45; GLY-61; GLY-64; TYR-67; LYS-132; HIS-142; PHE-147; PRO-165; TRP-170; TYR-186; ILE-191; MET-231; VAL-245; VAL-246; LEU-271; PHE-668; ASN-695; LEU-798; TYR-810; LYS-826; GLN-841; HIS-856; ASN-1101; ASN-1140; GLY-1140; LYS-1214; LYS-1236; SER-1267; VAL-1282; SER-1297 DEL; ARG-1301; LYS-1346; ILE-1378; VAL-1400; PRO-1407; THR-1411; GLY-1443; GLY-1448; CYS-1486; MET-1534; PRO-1589; THR-1628; PRO-1651; PHE-1651; PHE-1655; ARG-1686; GLN-1686; VAL-1688 DEL; ILE-1691; TRP-1699; GLN-1699; GLU-1706; ALA-1706; GLU-1708; CYS-1718; ALA-1720; LYS-1735; ALA-1736; GLY-1739; VAL-1739; GLN-1746; THR-1753; PRO-1764; SER-1767; VAL-1770; CYS-1782; THR-1789; ASP-1794; ASP-1804; ARG-1812; ARG-1837 AND LEU-1862; VARIANTS CYS-105; CYS-866; ALA-1060; LYS-1250 AND ILE-1652;
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.