Variant position: 572 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 SGLLVNLTTIASWLSWLQYF SIPRYGFTALQHNEFLGQNFC------------
Rhesus macaque SGLLVNLTTIASWLSWLQYF SIPRYGFTALQHNEFLGQNFC
Mouse SGLLVNLRTIGPWLSWLQYF SIPRYGFTALQYNEFLGQEFC
Rat SGLLVNLRTIGPWLSWLQYF SIPRYGFTALQHNEFLGQEFC
Pig SGLLVNLKTVVPWLSWLQYF SIPRYGFSALQYNEFLGQNFC
Bovine SGLLVNLKTVVPWLSWLQYL SIPRYGYAALQHNEFLGQNFC
Slime mold SGFMAPKRSIGGWWIWIYWI SPIKYAFEGLMSNEHHGLIYS
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
557 – 630 Extracellular
389 – 651 ABC transmembrane type-2
557 – 557 Not glycosylated
550 – 611 IFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGE -> VCWSISQPLHLGCHGFSTSAFHDMDLRLCSIMNFWDKTSAQDSMQQETILVTMQHVLAKNIW. In isoform 2.
554 – 554 L -> A. No effect on stability. Increased estrone-3 sulfate ATPase-coupled transmembrane transporter activity. Increased basal and substrate-induced ATP hydrolysis. Increased substrate transport.
555 – 555 L -> A. Loss of protein expression.
557 – 557 N -> Q. No effect.
583 – 583 H -> A. Strongly reduced binding to hemin but not to PPIX.
Functional Characterization of Clinically-Relevant Rare Variants in ABCG2 Identified in a Gout and Hyperuricemia Cohort.
Toyoda Y.; Mancikova A.; Krylov V.; Morimoto K.; Pavelcova K.; Bohata J.; Pavelka K.; Pavlikova M.; Suzuki H.; Matsuo H.; Takada T.; Stiburkova B.;
Cited for: VARIANTS TRP-147; MET-153; LYS-360 DEL; CYS-373; ALA-421; MET-434; PRO-476; ARG-572 AND ASN-620; CHARACTERIZATION OF VARIANTS LYS-141; TRP-147; MET-153; LYS-360 DEL; CYS-373; ALA-421; MET-434; PRO-476; ARG-572 AND ASN-620; FUNCTION; CATALYTIC ACTIVITY; SUBCELLULAR LOCATION;
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