Variant position: 373 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 SGGEKKKKITVFKEISYTTS FCHQLRWVSKRSFKNLLGNPQ
Rhesus macaque SGG-EKKKITVFKEISYTTS FCHQLRWVSKRSFKNLLGNPQ
Mouse PGAQEKKGTSAFKEPVYVTS FCHQLRWIARRSFKNLLGNPQ
Rat PVAQKKKGSSAFREPVYVTS FCHQLRWIARRSFKNLLGNPQ
Pig SGGRKKKKSSVYKEVTYTTS FCHQLRWISRRSFKNLLGNPQ
Bovine SGDQRRKKLPSYKEVTYATS FCHQLKWISRRSFKNLLGNPQ
Slime mold QPDLTFCKDSSHL-PKYPTP LSYQIRLASIRAFKMLISSQV
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
1 – 395 Cytoplasmic
362 – 362 Phosphothreonine; by PIM1
362 – 362 T -> A. Loss of phosphorylation by PIM1. Decreased localization to the plasma membrane. Decreased homooligomerization. Loss of function in resistance to drug treatment.
362 – 362 T -> D. Loss of phosphorylation by PIM1. Constitutive drug resistance independent of PIM1.
383 – 383 R -> C. Loss of protein expression.
373 – 390
Cellular expression and function of naturally occurring variants of the human ABCG2 multidrug transporter.
Zambo B.; Mozner O.; Bartos Z.; Toeroek G.; Varady G.; Telbisz A.; Homolya L.; Orban T.I.; Sarkadi B.;
Cell. Mol. Life Sci. 0:0-0(2019)
Cited for: FUNCTION; CATALYTIC ACTIVITY; SUBCELLULAR LOCATION; CHARACTERIZATION OF VARIANT LYS-141; TRP-147; MET-153; LYS-360 DEL; CYS-373; MET-434 AND PRO-476; MUTAGENESIS OF MET-71; LYS-86 AND ARG-383;
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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