Variant position: 431 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 655 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 AIYFGLKNDSTGIQNRAGVL FFLTTNQCFSSVSAVELFVVE
Rhesus macaque AIYFGLNNDSTGIQNRAGVL FFLTTNQCFSSVSAVELFVVE
Mouse AIYFDLKYDAAGMQNRAGVL FFLTTNQCFSSVSAVELFVVE
Rat ALYFGLKNDPTGMQNRAGVF FFLTTNQCFTSVSAVELFVVE
Pig AIFYDLKNDPSGIQNRAGVL FFLTTNQCFSSVSAVELLVVE
Bovine AIFYDLKNDPAGIQNRAGVL FFLTTNQCFSSVSAVELLVVE
Slime mold SLFYGLDLNQTDGNNRSGLI FFSLLFIVFSGMGAIAILFEQ
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 – 655 Broad substrate specificity ATP-binding cassette transporter ABCG2
429 – 449 Helical
389 – 651 ABC transmembrane type-2
418 – 418 Not glycosylated
418 – 418 N -> Q. No effect.
435 – 435 T -> A. No effect on stability. Increased estrone-3 sulfate ATPase-coupled transmembrane transporter activity. Increased substrate-induced ATP hydrolysis. Increased substrate transport.
435 – 435 T -> F. No effect on stability. Decreased estrone-3 sulfate ATPase-coupled transmembrane transporter activity. Decreased substrate-induced ATP hydrolysis. Decreased substrate transport.
436 – 436 N -> A. No effect on stability. Decreased estrone-3 sulfate ATPase-coupled transmembrane transporter activity. Decreased substrate-induced ATP hydrolysis. Decreased substrate transport.
439 – 439 F -> A. No effect on stability. Decreased estrone-3 sulfate ATPase-coupled transmembrane transporter activity. Decreased substrate-induced ATP hydrolysis. Decreased substrate transport.
423 – 439
Eight novel single nucleotide polymorphisms in ABCG2/BCRP in Japanese cancer patients administered irinotacan.
Itoda M.; Saito Y.; Shirao K.; Minami H.; Ohtsu A.; Yoshida T.; Saijo N.; Suzuki H.; Sugiyama Y.; Ozawa S.; Sawada J.;
Drug Metab. Pharmacokinet. 18:212-217(2003)
Cited for: VARIANTS LEU-431 AND LEU-489;
Genetic variation and haplotype structure of the ABC transporter gene ABCG2 in a Japanese population.
Maekawa K.; Itoda M.; Sai K.; Saito Y.; Kaniwa N.; Shirao K.; Hamaguchi T.; Kunitoh H.; Yamamoto N.; Tamura T.; Minami H.; Kubota K.; Ohtsu A.; Yoshida T.; Saijo N.; Kamatani N.; Ozawa S.; Sawada J.;
Drug Metab. Pharmacokinet. 21:109-121(2006)
Cited for: VARIANTS MET-12; LEU-13; LYS-141; GLN-160; ARG-354; LEU-431; ASN-441 AND LEU-489;
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.