Sequence information
Variant position: 456 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 563 The length of the canonical sequence.
Location on the sequence:
KITLIIGGSYGAGNYGMCGR
A YSPRFLYIWPNARISVMGGE
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 KITLIIGGSYGAGNYGMCGRA YSPRFLYIWPNARISVMGGE
Mouse KITVIIGGSYGAGNYGMCGRA YSPRFLYMWPNARISVMGGE
Rat KITVIIGGSYGAGNYGMCGRA YSPRFLYMWPNARISVMGGE
Caenorhabditis elegans KITVLVGGSYGAGNYGMCGRG YSPRYVFMWPNSRISVMGGE
Drosophila KFTVIIGGSYGAGNYGMCGRA YSPRFLYMWPNSRISVMGGT
Slime mold KITMIIGGSFGAGNYGMCGRS YSPRFLYMWPNAKISVMGGE
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
23 – 563
Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial
Domain
309 – 555
CoA carboxyltransferase C-terminal
Region
49 – 555
Carboxyltransferase
Literature citations
3-Methylcrotonyl-CoA carboxylase deficiency: mutation analysis in 28 probands, 9 symptomatic and 19 detected by newborn screening.
Dantas M.F.; Suormala T.; Randolph A.; Coelho D.; Fowler B.; Valle D.; Baumgartner M.R.;
Hum. Mutat. 26:164-174(2005)
Cited for: VARIANTS MCC2D GLN-99; TRP-155; GLN-155; TYR-190; THR-268; ARG-282; ARG-310; PHE-375 AND VAL-456; CHARACTERIZATION OF VARIANTS TYR-190 AND ARG-352;
3-methylcrotonyl-CoA carboxylase deficiency: clinical, biochemical, enzymatic and molecular studies in 88 individuals.
Gruenert S.C.; Stucki M.; Morscher R.J.; Suormala T.; Buerer C.; Burda P.; Christensen E.; Ficicioglu C.; Herwig J.; Koelker S.; Moeslinger D.; Pasquini E.; Santer R.; Schwab K.O.; Wilcken B.; Fowler B.; Yue W.W.; Baumgartner M.R.;
Orphanet J. Rare Dis. 7:31-54(2012)
Cited for: VARIANTS MCC2D PHE-39; GLN-99; PHE-101; GLY-118 DEL; PHE-131; ASN-146; THR-152; TRP-155; ARG-167; ASP-169; LEU-173; ARG-190; TYR-190; CYS-193; HIS-193; ASN-200; THR-218; VAL-218; GLU-220; LEU-224; ASP-237; LEU-266; TYR-280; ARG-282; ARG-310; MET-339; VAL-340 ARG-352; PHE-355; PHE-375; THR-403; LEU-434; VAL-456; ARG-475; ARG-477; ARG-517; SER-520; GLY-523 AND GLU-555; CHARACTERIZATION OF VARIANTS MCC2D PHE-39; GLY-118 DEL; ASN-146; ARG-282; LEU-434; VAL-456; ARG-475 AND GLY-523;
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.