UniProtKB/SwissProt variant VAR

Variant information

Variant position:

302

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

Type of variant:

Disease [Disclaimer]

The variants are classified into three categories: Disease, Polymorphism and Unclassified.

Disease: Variants implicated in disease according to literature reports.
Polymorphism: Variants not reported to be implicated in disease.
Unclassified: Variants with uncertain implication in disease according to literature reports. Evidence against or in favor of a pathogenic role is limited and/or conflicting.

Residue change:

From Aspartate (D) to Valine (V) at position 302 (D302V, p.Asp302Val).

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 medium size and acidic (D) to medium size and hydrophobic (V)

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

Involvement in disease:

Inclusion body myopathy with early-onset Paget disease with or without frontotemporal dementia 2 (IBMPFD2) [MIM:615422]: An autosomal dominant disease characterized by disabling muscle weakness clinically resembling to limb girdle muscular dystrophy, osteolytic bone lesions consistent with Paget disease, and premature frontotemporal dementia. Clinical features show incomplete penetrance. {ECO:0000269|PubMed:23455423}. Note=The disease is caused by mutations affecting the gene represented in this entry.

The name and a short description of the disease associated with the variant. For more information about the disease, the user can refer to OMIM, following the link provided after the disease acronym.

Variant description:

In IBMPFD2.

Any additional useful information about the variant.

Other resources:

Links to websites of interest for the variant.

Variant rs397515326 [ dbSNP | Ensembl ]

Sequence information

Variant position:

302

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

Protein sequence length:

353

The length of the canonical sequence.

Location on the sequence:

GYGGGYDNYGGGNYGSGNYN D FGNYNQQPSNYGPMKSGNFG

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                         GYGGGYDNYGGGNYGSGNYNDFGNYNQQPSNYGPMKSGNFG

Mouse                         GYGGGYDNYGGGNYGSGSYNDFGNYNQQPSNYGPMKSGNFG

Rat                           GYGGGYDNYGGGNYGSGNYNDFGNYNQQPSNYGPMKSGNFG

Bovine                        GYGGGYDNYGGGNYGSGNYNDFGNYNQQPSNYGPMKSGNFG

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 – 353	Heterogeneous nuclear ribonucleoproteins A2/B1
Region	193 – 353	Low complexity (LC) region
Compositional bias	202 – 353	Gly-rich
Mutagenesis	283 – 283	Y -> S. Slightly affects hydrogel-binding.
Mutagenesis	287 – 287	Y -> S. Does not affect hydrogel-binding.
Mutagenesis	290 – 290	Y -> S. Impairs hydrogel-binding.
Mutagenesis	295 – 295	Y -> S. Impairs hydrogel-binding.
Mutagenesis	300 – 300	Y -> S. Slightly affects hydrogel-binding.
Mutagenesis	303 – 303	F -> S. Impairs hydrogel-binding.
Mutagenesis	306 – 306	Y -> S. Slightly affects hydrogel-binding.
Mutagenesis	313 – 313	Y -> S. Slightly affects hydrogel-binding.
Mutagenesis	321 – 321	F -> S. Impairs hydrogel-binding.

Literature citations

Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS.
Kim H.J.; Kim N.C.; Wang Y.D.; Scarborough E.A.; Moore J.; Diaz Z.; MacLea K.S.; Freibaum B.; Li S.; Molliex A.; Kanagaraj A.P.; Carter R.; Boylan K.B.; Wojtas A.M.; Rademakers R.; Pinkus J.L.; Greenberg S.A.; Trojanowski J.Q.; Traynor B.J.; Smith B.N.; Topp S.; Gkazi A.S.; Miller J.; Shaw C.E.; Kottlors M.; Kirschner J.; Pestronk A.; Li Y.R.; Ford A.F.; Gitler A.D.; Benatar M.; King O.D.; Kimonis V.E.; Ross E.D.; Weihl C.C.; Shorter J.; Taylor J.P.;
Nature 495:467-473(2013)
Cited for: VARIANT IBMPFD2 VAL-302;

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P22626: Variant p.Asp302Val