Variant position: 274 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 558 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 CVTGKPISQGGIHGRISATG RGVFHGIENFINEASYMSILG
Mouse CVTGKPISQGGIHGRISATG RGVFHGIENFINEASYMSILG
Rat CVTGKPISQGGIHGRISATG RGVFHGIENFINEASYMSILG
Pig CVTGKPISQGGIHGRISATG RGVFHGIENFINEASYMSILG
Bovine CVTGKPISQGGIHGRISATG RGVFHGIENFINEASYMSILG
Drosophila CVTGKPINQGGIHGRVSATG RGVFHGLENFINEANYMSQIG
Slime mold CVTGKPISSGGIRGRTEATG LGVFYGIREFLSYEEVLKKTG
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.
Novel missense mutations outside the allosteric domain of glutamate dehydrogenase are prevalent in European patients with the congenital hyperinsulinism-hyperammonemia syndrome.
Santer R.; Kinner M.; Passarge M.; Superti-Furga A.; Mayatepek E.; Meissner T.; Schneppenheim R.; Schaub J.;
Hum. Genet. 108:66-71(2001)
Cited for: VARIANTS HHF6 CYS-274 AND HIS-322;
Hyperinsulinism/hyperammonemia syndrome in children with regulatory mutations in the inhibitory guanosine triphosphate-binding domain of glutamate dehydrogenase.
MacMullen C.; Fang J.; Hsu B.Y.L.; Kelly A.; de Lonlay-Debeney P.; Saudubray J.-M.; Ganguly A.; Smith T.J.; Stanley C.A.; Brown R.; Buist N.; Dasouki M.; Fefferman R.; Grange D.; Karaviti L.; Luedke C.; Marriage B.; McLaughlin J.; Perlman K.; Seashore M.; van Vliet G.;
J. Clin. Endocrinol. Metab. 86:1782-1787(2001)
Cited for: VARIANTS HHF6 CYS-270; CYS-274; THR-318; CYS-319; CYS-322 AND HIS-322; CHARACTERIZATION OF VARIANTS HHF6 CYS-270; CYS-274; THR-318; CYS-322 AND HIS-322; FUNCTION; ACTIVITY REGULATION;
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.