Sequence information
Variant position: 226 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 462 The length of the canonical sequence.
Location on the sequence:
HLEQGGTKLVKDLSPGDRVL
A ADDQGRLLYSDFLTFLDRDD
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 HLEQGGTKLVKDLSPGDRVLA ADDQGRLLYSDFLTFLDRDD
Mouse HLEQGGTKLVKDLRPGDRVLA ADDQGRLLYSDFLTFLDRDE
Rat HLEQGGTKLVKDLSPGDRVLA ADDQGRLLYSDFLTFLDRDE
Chicken HLEHGGTKLVKDLSPGDRVLA ADADGRLLYSDFLTFLDRMD
Xenopus laevis MVEFGGTKAVKDLRPGDRVLS SDPQGNLLYSDFLMFIDQER
Zebrafish SLQDGGQKAVKDLNPGDKVLA ADSAGNLVFSDFIMFTDRDS
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
24 – 462
Sonic hedgehog protein
Site
243 – 243
Involved in cholesterol transfer
Literature citations
Mutations in the C-terminal domain of Sonic hedgehog cause holoprosencephaly.
Roessler E.; Belloni E.; Gaudenz K.; Vargas F.; Scherer S.W.; Tsui L.-C.; Muenke M.;
Hum. Mol. Genet. 6:1847-1853(1997)
Cited for: VARIANTS HPE3 ARG-31; GLY-117; ARG-117; GLU-224; THR-226 AND THR-383;
The mutational spectrum of holoprosencephaly-associated changes within the SHH gene in humans predicts loss-of-function through either key structural alterations of the ligand or its altered synthesis.
Roessler E.; El-Jaick K.B.; Dubourg C.; Velez J.I.; Solomon B.D.; Pineda-Alvarez D.E.; Lacbawan F.; Zhou N.; Ouspenskaia M.; Paulussen A.; Smeets H.J.; Hehr U.; Bendavid C.; Bale S.; Odent S.; David V.; Muenke M.;
Hum. Mutat. 30:E921-E935(2009)
Cited for: VARIANTS HPE3 THR-6; PRO-17; LEU-26; ALA-27; ARG-31; PRO-39; LYS-53; VAL-83; PHE-84; VAL-88; HIS-100; ARG-102; TYR-102; 106-LEU-ASN-107 DEL; PHE-109; THR-110; ASP-110; PHE-111; ASN-111; LYS-115; GLY-117; ARG-117; MET-124; LYS-136; PRO-140; GLN-140; ASP-143; PRO-144; ASN-147; ARG-150; LYS-150; ARG-156; CYS-170; HIS-171; 176-GLU--LYS-178 DEL; ARG-183; PHE-183; TYR-183; LEU-184; GLN-188; GLU-196; 196-GLY--PRO-200 DEL; VAL-197; SER-198; PHE-198; PRO-218; ASN-222; GLU-224; THR-226; VAL-231; GLY-232; PRO-234; ARG-236; ASN-236; VAL-241; LEU-241; ASN-255; 263-ARG--ALA-269 DEL; ILE-267; PRO-271; GLU-275; TRP-280; ASP-290; ALA-296; CYS-310; SER-321; ALA-332; VAL-346; ARG-347; GLN-347; LEU-347; THR-354; LEU-362; TYR-363; CYS-364; THR-373; ARG-374; ASP-376; SER-377; 378-ALA--PHE-380 DEL; PRO-381; PRO-382; THR-383; THR-391; 402-GLY--GLY-409 DEL; 405-ASP--GLY-409 DEL; GLY-411 INS; ALA-416; ALA-424; ASN-435; LEU-436 AND ARG-456;
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.