Sequence information
Variant position: 267 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:
GAKKVFYVIETREPRERLLL
T AAHLLFVAPHNDSATGEPEA
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 GAKKVFYVIETREPRERLLLT AAHLLFVAPHNDSATGEPEA
Mouse GAKKVFYVIETLEPRERLLLT AAHLLFVAPHND--------
Rat GAKKVFYVIETREPRERLLLT AAHLLFVAPHND--------
Chicken SSRKLFYVIETRQPRARLLLT AAHLLFVAPQHNQSE-----
Xenopus laevis DVKKLFYVIETSQRKIR--LT AAHLLFVAQTK---------
Zebrafish TTRRVFYVIETQEPVEKITLT AAHLLFVLDNS---------
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
267 – 267
Involved in auto-cleavage
Site
270 – 270
Essential for auto-cleavage
Glycosylation
278 – 278
N-linked (GlcNAc...) asparagine
Literature citations
Wide phenotypic variability in families with holoprosencephaly and a sonic hedgehog mutation.
Hehr U.; Gross C.; Diebold U.; Wahl D.; Beudt U.; Heidemann P.; Hehr A.; Mueller D.;
Eur. J. Pediatr. 163:347-352(2004)
Cited for: VARIANTS HPE3 ALA-27; ILE-267 AND THR-373;
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.