Variant position: 1378 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 EQSMDSNLGEAASGCESETS VSEDCSGLSSQSDILTTQQRD
Gorilla EQSMDSNLGEAASGCESETS VSEDCSGLSSQSDILTTQQRD
Rhesus macaque EQSVDSNLGEAASGYESETS VSEDCSRLSSQSEILTTQQRD
Chimpanzee EQSMDSNLGEAASGCESETS VSEDCSGLSSQSDILTTQQRD
Mouse EDSIIPD--SEASGYESETN LSEDC----SQSDILTTQQRA
Rat EDSIIPD--SVASGYESEAN LSEDC----SQSDILTTQQRA
Bovine EQSVDSDLGEAVSDHVSETS LSEDGVGLSSQSDILTTQQRD
Caenorhabditis elegans -------------------- ---------------------
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
1322 – 1387 Disordered
1354 – 1387 Polar residues
1387 – 1387 Phosphoserine; by ATM and ATR
1394 – 1394 Phosphothreonine; by ATR; in vitro
64 – 1863 Missing. In isoform 2.
1387 – 1387 S -> A. Loss of IR-induced S-phase checkpoint. Reduces in vitro phosphorylation by ATR.
1394 – 1394 T -> A. Reduces in vitro phosphorylation by ATR.
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.