Variant position: 208 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 504 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 TRDTARAVPPGSREVSTWNL DTL-------------AFQ---------------------ELKSELTEVPAS---------RIL
Mouse TQYPSQDMLPGSREVSQWNL DTL-------------AFQ--
Rat THHPSQDMLPGSREVSQWNL DTL-------------AFQ--
Bovine AHSSSQDVPSGSREVAKWNL ENM-------------DFQ--
Rabbit ARDTSQDVPAGSREASQWNL DTL-------------AFQ--
Cat ARGTPQDVPSGSREVSKWNV ETV-------------NFQ--
Slime mold VKHYAGDVVYEGPGMIEKNK DTLLKDHLEILQMSANNFLVG
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
33 – 504 Myocilin
33 – 226 Myocilin, N-terminal fragment
226 – 226 R -> A. Reduced processing. Impairs endoproteolytic processing; when associated with A-229 or A-230. Completely processed after 6 days of expression, and releases a C-terminal fragment with similar electrophoretic mobility to that obtained by processing wild-type myocilin; when associated with A-229 or A-230.
226 – 226 R -> Q. Slightly increases endoproteolytic processing.
227 – 227 I -> G. Reduced processing.
Novel mutations in the myocilin gene in Japanese glaucoma patients.
Kubota R.; Mashima Y.; Ohtake Y.; Tanino T.; Kimura T.; Hotta Y.; Kanai A.; Tokuoka S.; Azuma I.; Tanihara H.; Inatani M.; Inoue Y.; Kudoh J.; Oguchi Y.; Shimizu N.;
Hum. Mutat. 16:270-270(2000)
Cited for: VARIANTS GLC1A GLN-158; ASN-360 AND THR-363; VARIANTS HIS-19; LYS-76; GLU-208 AND HIS-470;
Truncations in the TIGR gene in individuals with and without primary open-angle glaucoma.
Lam D.S.C.; Leung Y.F.; Chua J.K.H.; Baum L.; Fan D.S.P.; Choy K.W.; Pang C.P.;
Invest. Ophthalmol. Vis. Sci. 41:1386-1391(2000)
Cited for: VARIANTS GLC1A GLU-208 AND ILE-353; VARIANTS ARG-12 AND LYS-76;
TIGR/MYOC gene sequence alterations in individuals with and without primary open-angle glaucoma.
Pang C.P.; Leung Y.F.; Fan B.; Baum L.; Tong W.C.; Lee W.S.; Chua J.K.H.; Fan D.S.P.; Liu Y.; Lam D.S.C.;
Invest. Ophthalmol. Vis. Sci. 43:3231-3235(2002)
Cited for: VARIANTS GLC1A LYS-300 AND CYS-471; VARIANTS ARG-12; LEU-16; SER-17; LYS-76; PRO-95; GLU-208; PRO-215; ILE-353 AND LYS-414;
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.