Variant position: 3 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 484 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 MA AGGDHGSP------DSYRSPLASRY-AS
Mouse MA ASGDPGSA------ESYRSPL
Bovine MA AAGDRGGREAACGHDSYRSPL
Chicken MA TPCAEEDP-----LARYRSPL
Caenorhabditis elegans -- ----MASE------DKFESVL
Slime mold MS TTTNIQLN-----NLTAISPI
Baker's yeast -- ----MPDY------DNYTTPL
Fission yeast -- ----MEDY------GSYSTPL
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 – 1 Removed
2 – 484 Adenylosuccinate lyase
2 – 2 N-acetylalanine
Human adenylosuccinate lyase (ADSL), cloning and characterization of full-length cDNA and its isoform, gene structure and molecular basis for ADSL deficiency in six patients.
Kmoch S.; Hartmannova H.; Stiburkova B.; Krijt J.; Zikanova M.; Sebesta I.;
Hum. Mol. Genet. 9:1501-1513(2000)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2); FUNCTION; VARIANTS ADSLD VAL-3; HIS-114; GLN-190; CYS-194; ASN-268; HIS-426 AND ASN-430;
Screening for adenylosuccinate lyase deficiency: clinical, biochemical and molecular findings in four patients.
Castro M.; Perez-Cerda C.; Merinero B.; Garcia M.J.; Bernar J.; Gil Nagel A.; Torres J.; Bermudez M.; Garavito P.; Marie S.; Vincent F.; Van den Berghe G.; Ugarte M.;
Cited for: VARIANTS ADSLD VAL-311; MET-364; HIS-396 AND PRO-452;
Biochemical and biophysical analysis of five disease-associated human adenylosuccinate lyase mutants.
Ariyananda Lde Z.; Lee P.; Antonopoulos C.; Colman R.F.;
Cited for: CHARACTERIZATION OF VARIANTS ADSLD CYS-194; GLU-246; VAL-311; CYS-396 AND HIS-396; ACTIVITY REGULATION;
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