Variant position: 913 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 1500 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 GLNSESMTEETLKRAKEIGF SDKQISKCLGLTEAQTRELRL
Mouse GLNSDSVTEETLRKAKEIGF SDKQISKCLGLTEAQTRELRL
Rat GLNSESVTEETLRQAKEIGF SDKQISKCLGLTEAQTRELRL
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
39 – 1500 Carbamoyl-phosphate synthase [ammonia], mitochondrial
896 – 896 Phosphoserine
898 – 898 Phosphoserine
905 – 905 N6-glutaryllysine
908 – 908 N6-acetyllysine; alternate
908 – 908 N6-glutaryllysine; alternate
915 – 915 N6-acetyllysine; alternate
915 – 915 N6-glutaryllysine; alternate
915 – 915 N6-succinyllysine; alternate
919 – 919 N6-acetyllysine; alternate
919 – 919 N6-glutaryllysine; alternate
919 – 919 N6-succinyllysine; alternate
Molecular defects in human carbamoyl phosphate synthetase I: mutational spectrum, diagnostic and protein structure considerations.
Haberle J.; Shchelochkov O.A.; Wang J.; Katsonis P.; Hall L.; Reiss S.; Eeds A.; Willis A.; Yadav M.; Summar S.; Lichtarge O.; Rubio V.; Wong L.J.; Summar M.;
Hum. Mutat. 32:579-589(2011)
Cited for: VARIANTS CPS1D VAL-43; ASP-58; PHE-65; GLY-71; SER-87; ASP-89; GLY-165; VAL-224; CYS-233; PRO-243; GLU-258; GLU-263; VAL-304; GLU-317; HIS-358; LEU-382; ARG-401; ARG-431; VAL-432; THR-438; GLU-450; PRO-498; GLU-531; GLY-531; MET-544; CYS-587; HIS-587; LEU-587; LEU-597; MET-622; ASP-628; ARG-632; PRO-638; TYR-648; VAL-654; LYS-674; SER-698; LYS-718; GLN-721; PRO-724; THR-726; VAL-767; HIS-780; ILE-792; SER-803; GLY-803; CYS-803; SER-805; TRP-814; ARG-816; HIS-850; GLU-911; LEU-913; HIS-914; GLY-914; THR-932; THR-949; CYS-959; CYS-962; GLU-978; VAL-982; HIS-984; THR-986; CYS-987; SER-992; SER-1016; LEU-1017; ILE-1022; GLY-1034; ARG-1045; ARG-1059; GLU-1065; CYS-1089; GLU-1155; VAL-1155; LEU-1203; GLN-1228; ASP-1255; GLN-1262; PRO-1262; HIS-1274; ARG-1327; GLU-1333; LEU-1371; MET-1391; VAL-1398; LEU-1439; TRP-1453 AND ARG-1462;
Understanding carbamoyl phosphate synthetase (CPS1) deficiency by using the recombinantly purified human enzyme: effects of CPS1 mutations that concentrate in a central domain of unknown function.
Diez-Fernandez C.; Hu L.; Cervera J.; Haeberle J.; Rubio V.;
Mol. Genet. Metab. 112:123-132(2014)
Cited for: VARIANTS CPS1D ARG-401; ARG-632; SER-843; CYS-850; HIS-850; PRO-871; VAL-911; GLU-911; LEU-913; HIS-914; GLY-914; PRO-918; THR-932; ASN-937; THR-949; PRO-958; CYS-959; CYS-962; ASP-964; ASP-1194 AND ARG-1462; VARIANT GLU-875; CHARACTERIZATION OF VARIANTS CPS1D SER-843; CYS-850; HIS-850; PRO-871; VAL-911; GLU-911; LEU-913; HIS-914; GLY-914; PRO-918; THR-932; ASN-937; THR-949; PRO-958; CYS-959; CYS-962 AND ASP-964; CATALYTIC ACTIVITY; CHARACTERIZATION OF VARIANT GLU-875;
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