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 GYGGGYDNYGGGNYGSGNYND FGNYNQQPSNYGPMKSGNFG
Mouse GYGGGYDNYGGGNYGSGSYND FGNYNQQPSNYGPMKSGNFG
Rat GYGGGYDNYGGGNYGSGNYND FGNYNQQPSNYGPMKSGNFG
Bovine GYGGGYDNYGGGNYGSGNYND FGNYNQQPSNYGPMKSGNFG
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;
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.