UniProtKB/SwissProt variant VAR

Variant information

Variant position:

359

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

Type of variant:

LP/P [Disclaimer]

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 Arginine (R) to Tryptophan (W) at position 359 (R359W, p.Arg359Trp).

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:

Change from large size and basic (R) to large size and aromatic (W)

The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:

-3

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 DSS and CMT1D; associated with A-136 in the GJB1 gene in a DSS Korean girl; loss of DNA binding and loss of transactivation activity; loss of small and large myelinated nerve fibers; residual fibers with thin myelin sheaths.

Any additional useful information about the variant.

Other resources:

Links to websites of interest for the variant.

Variant rs104894161 [ dbSNP | Ensembl ]

Sequence information

Variant position:

359

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

Protein sequence length:

476

The length of the canonical sequence.

Location on the sequence:

PYPCPAEGCDRRFSRSDELT R HIRIHTGHKPFQCRICMRNF

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                         PYPCPAEGCDRRFSRSDELTRHIRIHTGHKPFQCRICMRNF

Mouse                         PYPCPAEGCDRRFSRSDELTRHIRIHTGHKPFQCRICMRNF

Rat                           PYPCPAEGCDRRFSRSDELTRHIRIHTGHKPFQCRICMRNF

Pig                           PYPCPAEGCDRRFSRSDELTRHIRIHTGHKPFQCRICMRNF

Xenopus laevis                PYPCPAEGCDRRFSRSDELTRHIRIHTGHKPFQCRICMRNF

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	1 – 476	E3 SUMO-protein ligase EGR2
Zinc finger	340 – 364	C2H2-type 1

Literature citations

Novel missense mutation in the early growth response 2 gene associated with Dejerine-Sottas syndrome phenotype.
Timmerman V.; De Jonghe P.; Ceuterick C.; De Vriendt E.; Lofgren A.; Nelis E.; Warner L.E.; Lupski J.R.; Martin J.-J.; Van Broeckhoven C.;
Neurology 52:1827-1832(1999)
Cited for: VARIANT DSS TRP-359;

Mutational analysis of PMP22, MPZ, GJB1, EGR2 and NEFL in Korean Charcot-Marie-Tooth neuropathy patients.
Choi B.-O.; Lee M.S.; Shin S.H.; Hwang J.H.; Choi K.-G.; Kim W.-K.; Sunwoo I.N.; Kim N.K.; Chung K.W.;
Hum. Mutat. 24:185-186(2004)
Cited for: VARIANT CMT1D TRP-359;

Two missense mutations of EGR2 R359W and GJB1 V136A in a Charcot-Marie-Tooth disease family.
Chung K.W.; Sunwoo I.N.; Kim S.M.; Park K.D.; Kim W.-K.; Kim T.S.; Koo H.; Cho M.; Lee J.; Choi B.O.;
Neurogenetics 6:159-163(2005)
Cited for: VARIANT CMT1D TRP-359;

Functional, histopathologic and natural history study of neuropathy associated with EGR2 mutations.
Szigeti K.; Wiszniewski W.; Saifi G.M.; Sherman D.L.; Sule N.; Adesina A.M.; Mancias P.; Papasozomenos S.C.; Miller G.; Keppen L.; Daentl D.; Brophy P.J.; Lupski J.R.;
Neurogenetics 8:257-262(2007)
Cited for: VARIANT DSS LYS-412; CHARACTERIZATION OF VARIANTS CHN1 ASN-268; DSS LYS-412 AND DSS/CMT1D TRP-359; FUNCTION;

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P11161: Variant p.Arg359Trp