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:
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 GYGGGYDNYGGGNYGSGNYN DFGNYNQQPSNYGPMKSGNFG
Mouse GYGGGYDNYGGGNYGSGSYN DFGNYNQQPSNYGPMKSGNFG
Rat GYGGGYDNYGGGNYGSGNYN DFGNYNQQPSNYGPMKSGNFG
Bovine GYGGGYDNYGGGNYGSGNYN DFGNYNQQPSNYGPMKSGNFG
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
1 – 353 Heterogeneous nuclear ribonucleoproteins A2/B1
193 – 353 Disordered
283 – 283 Y -> S. Slightly affects hydrogel-binding.
287 – 287 Y -> S. Does not affect hydrogel-binding.
290 – 290 Y -> S. Impairs hydrogel-binding.
295 – 295 Y -> S. Impairs hydrogel-binding.
300 – 300 Y -> S. Slightly affects hydrogel-binding.
303 – 303 F -> S. Impairs hydrogel-binding.
306 – 306 Y -> S. Slightly affects hydrogel-binding.
313 – 313 Y -> S. Slightly affects hydrogel-binding.
321 – 321 F -> S. Impairs hydrogel-binding.
300 – 302
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.;
Cited for: VARIANT IBMPFD2 VAL-302;
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