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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P22626: Variant p.Asp302Val

Heterogeneous nuclear ribonucleoproteins A2/B1
Gene: HNRNPA2B1
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Variant information Variant position: help 302 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help 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: help 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: help 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: help -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: help In IBMPFD2. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 302 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 353 The length of the canonical sequence.
Location on the sequence: help 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: help 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: help 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 1 – 353 Heterogeneous nuclear ribonucleoproteins A2/B1
Region 193 – 353 Disordered
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.
Beta strand 300 – 302



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;
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.