Sequence information
Variant position: 244 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 392 The length of the canonical sequence.
Location on the sequence:
DKAKKKMYSRKTKPFSFYLD
I KWLANFWGCDDQPRMYHHTI
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 DKAKKKMYSRKTKPFSFYLDI KWLANFWG-----CDDQ---------PRMYHHTI
Mouse DKAKYKVYSRKTKPVSFYTDI TYLAKLWG-----CEGE---
Rat DKAKSKVYSRKTKPVSFYTDI TYLSKLWG-----CEGK---
Rabbit DKAKSKIYARKTKPFSFYMDV QLLANIWG-----CDGK---
Cat DKAKNKIYTRKTKPVSFYLDM KWLANIWG-----CDGK---
Slime mold NAACHKIATRKTPVANWYLDC NLLGGYWCPEFNLADGTIAK
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
Chain
1 – 392
Alanine--glyoxylate aminotransferase
Modified residue
225 – 225
N6-acetyllysine; alternate
Modified residue
225 – 225
N6-succinyllysine; alternate
Modified residue
234 – 234
N6-acetyllysine
Helix
244 – 250
Literature citations
Primary hyperoxaluria type 1: a cluster of new mutations in exon 7 of the AGXT gene.
von Schnakenburg C.; Rumsby G.;
J. Med. Genet. 34:489-492(1997)
Cited for: VARIANTS HP1 CYS-233; HIS-233 AND THR-244;
Primary hyperoxaluria type I: a model for multiple mutations in a monogenic disease within a distinct ethnic group.
Rinat C.; Wanders R.J.A.; Drukker A.; Halle D.; Frishberg Y.;
J. Am. Soc. Nephrol. 10:2352-2358(1999)
Cited for: VARIANTS HP1 ARG-41; ARG-156; ARG-190; THR-244; CYS-289 AND PRO-298;
Identification of 5 novel mutations in the AGXT gene.
Basmaison O.; Rolland M.-O.; Cochat P.; Bozon D.;
Hum. Mutat. 15:577-577(2000)
Cited for: VARIANTS HP1 ILE-152; ARG-170; ASN-183; CYS-233 AND THR-244;
Functional synergism between the most common polymorphism in human alanine:glyoxylate aminotransferase and four of the most common disease-causing mutations.
Lumb M.J.; Danpure C.J.;
J. Biol. Chem. 275:36415-36422(2000)
Cited for: CHARACTERIZATION OF VARIANTS HP1 ARG-41; GLU-82; ILE-152; ARG-170 AND THR-244; CHARACTERIZATION OF VARIANT LEU-11; MUTAGENESIS OF LYS-209; FUNCTION; CATALYTIC ACTIVITY; SUBCELLULAR LOCATION; COFACTOR; SUBUNIT; BIOPHYSICOCHEMICAL PROPERTIES; ACTIVITY REGULATION;
Primary hyperoxaluria type 1 in the Canary Islands: a conformational disease due to I244T mutation in the P11L-containing alanine:glyoxylate aminotransferase.
Santana A.; Salido E.; Torres A.; Shapiro L.J.;
Proc. Natl. Acad. Sci. U.S.A. 100:7277-7282(2003)
Cited for: CHARACTERIZATION OF VARIANT HP1 THR-244; FUNCTION; CATALYTIC ACTIVITY; BIOPHYSICOCHEMICAL PROPERTIES; SUBUNIT; SUBCELLULAR LOCATION;
Implications of genotype and enzyme phenotype in pyridoxine response of patients with type I primary hyperoxaluria.
Monico C.G.; Olson J.B.; Milliner D.S.;
Am. J. Nephrol. 25:183-188(2005)
Cited for: VARIANTS HP1 VAL-139 DEL; ARG-156; LEU-158; ARG-190; GLU-201; LEU-233; THR-244 AND ARG-253; VARIANT ASN-9;
Intra-familial clinical heterogeneity: absence of genotype-phenotype correlation in primary hyperoxaluria type 1 in Israel.
Frishberg Y.; Rinat C.; Shalata A.; Khatib I.; Feinstein S.; Becker-Cohen R.; Weismann I.; Wanders R.J.A.; Rumsby G.; Roels F.; Mandel H.;
Am. J. Nephrol. 25:269-275(2005)
Cited for: VARIANTS HP1 ARG-41; ARG-108; ARG-156; ARG-190; ARG-195; HIS-243; THR-244; MET-279; THR-287; CYS-289 AND PRO-298; VARIANT ASN-9;
Selected exonic sequencing of the AGXT gene provides a genetic diagnosis in 50% of patients with primary hyperoxaluria type 1.
Williams E.; Rumsby G.;
Clin. Chem. 53:1216-1221(2007)
Cited for: VARIANTS HP1 CYS-36; ARG-41; GLU-41; PRO-150; ILE-152; ARG-156; LEU-158; CYS-161; SER-161; PRO-166; ARG-170; TYR-173; CYS-233; HIS-233; THR-244 AND ARG-253; VARIANT ASN-9; CHARACTERIZATION OF VARIANTS HP1 CYS-36; GLU-41; PRO-150; ARG-156; LEU-158; CYS-161; SER-161; PRO-166; TYR-173; CYS-233; HIS-233 AND ARG-253; CHARACTERIZATION OF VARIANT ASN-9;
Four of the most common mutations in primary hyperoxaluria type 1 unmask the cryptic mitochondrial targeting sequence of alanine:glyoxylate aminotransferase encoded by the polymorphic minor allele.
Fargue S.; Lewin J.; Rumsby G.; Danpure C.J.;
J. Biol. Chem. 288:2475-2484(2013)
Cited for: CHARACTERIZATION OF VARIANTS HP1 ARG-41; ILE-152; ARG-170 AND THR-244; FUNCTION; CATALYTIC ACTIVITY; SUBCELLULAR LOCATION; SUBUNIT;
Disclaimer:
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.