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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P09651: Variant p.Asp314Val

Heterogeneous nuclear ribonucleoprotein A1
Gene: HNRNPA1
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Variant information Variant position: help 314 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 314 (D314V, p.Asp314Val). 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 IBMPFD3; reduces binding to UBQLN2. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 314 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 372 The length of the canonical sequence.
Location on the sequence: help GGGGFGGGSGSNFGGGGSYN D FGNYNNQSSNFGPMKGGNFG 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                         GGGGFGGGSGSNFGGGGSY-----NDFGNYNNQSSN-FGPMK-GGNF-G

Rhesus macaque                ---------GSNFGGGGSY-----NDFGNYNNQSSN-FGPM

Chimpanzee                    ---------GSNFGGGGSY-----NDFGNYNNQSSN-FGPM

Mouse                         ---------GSNFGGGGSY-----NDFGNYNNQSSN-FGPM

Rat                           ---------GSNFGGGGSY-----NDFGNYNNQSSN-FGPM

Bovine                        ---------GSNFGGGGSY-----NDFGNYNNQSSN-FGPM

Xenopus laevis                -----FSGSGGNFGSSGGY-----NDFGNYNSQSSSNFGPM

Caenorhabditis elegans        ---------GGGQGGWG----------GPQQQQQGGWGGPQ

Drosophila                    ---------GGNFGGGGNNWNNGGNDFGGYQQNYGG--GPQ

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 – 372 Heterogeneous nuclear ribonucleoprotein A1
Chain 2 – 372 Heterogeneous nuclear ribonucleoprotein A1, N-terminally processed
Mutagenesis 326 – 326 G -> A. No nuclear import nor export.
Mutagenesis 327 – 327 P -> A. No nuclear import nor export.
Beta strand 312 – 314



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 IBMPFD3 VAL-314; VARIANTS ALS20 ASN-314 AND SER-319; INVOLVEMENT IN IBMPFD3; INVOLVEMENT IN ALS20; ALS-linked mutations in ubiquilin-2 or hnRNPA1 reduce interaction between ubiquilin-2 and hnRNPA1.
Gilpin K.M.; Chang L.; Monteiro M.J.;
Hum. Mol. Genet. 24:2565-2577(2015)
Cited for: CHARACTERIZATION OF VARIANT IBMPFD3 VAL-314; INTERACTION WITH UBQLN2;
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.