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UniProtKB/Swiss-Prot Q99972: Variant p.Asp208Glu

Myocilin
Gene: MYOC
Variant information

Variant position:  208
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  US
The variants are classified into three categories: LP/P, LB/B and US.
  • LP/P: likely pathogenic or pathogenic.
  • LB/B: likely benign or benign.
  • US: uncertain significance

Residue change:  From Aspartate (D) to Glutamate (E) at position 208 (D208E, p.Asp208Glu).
Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.

Physico-chemical properties:  Similar physico-chemical property. Both residues are medium size and acidic.
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  2
The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:
  • Lowest score: -4 (low probability of substitution).
  • Highest score: 11 (high probability of substitution).
More information can be found on the following page

Variant description:  In GLC1A; unknown pathological significance.
Any additional useful information about the variant.

Other resources:  
Links to websites of interest for the variant.



Sequence information

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:   TRDTARAVPPGSREVSTWNL  D TLAFQELKSELTEVPASRIL
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                         TRDTARAVPPGSREVSTWNLDTL-------------AFQ---------------------ELKSELTEVPAS---------RIL

                              AHSSSQDVPAGSREVSKWNVETV-------------NFQ--

Mouse                         TQYPSQDMLPGSREVSQWNLDTL-------------AFQ--

Rat                           THHPSQDMLPGSREVSQWNLDTL-------------AFQ--

Bovine                        AHSSSQDVPSGSREVAKWNLENM-------------DFQ--

Rabbit                        ARDTSQDVPAGSREASQWNLDTL-------------AFQ--

Cat                           ARGTPQDVPSGSREVSKWNVETV-------------NFQ--

Slime mold                    VKHYAGDVVYEGPGMIEKNKDTLLKDHLEILQMSANNFLVG

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.

TypePositionsDescription
Chain 33 – 504 Myocilin
Chain 33 – 226 Myocilin, N-terminal fragment
Mutagenesis 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.
Mutagenesis 226 – 226 R -> Q. Slightly increases endoproteolytic processing.
Mutagenesis 227 – 227 I -> G. Reduced processing.


Literature citations

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;

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.