Expasy logo

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P31483: Variant p.Glu384Lys

Cytotoxic granule associated RNA binding protein TIA1
Gene: TIA1
Feedback?
Variant information Variant position: help 384 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 Glutamate (E) to Lysine (K) at position 384 (E384K, p.Glu384Lys). 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 (E) to large size and basic (K) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 1 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 WDM; results in a mild increase of stress granule numbers compared to controls; impaired stress granule disassembly. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 384 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 386 The length of the canonical sequence.
Location on the sequence: help QGQNGSMLPNQPSGYRVAGY E TQ 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                         QGQNGSMLPNQPSGYRVAGYETQ

Mouse                         QGQNGSMLPSQPAGYRVAGYETQ

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 – 386 Cytotoxic granule associated RNA binding protein TIA1
Region 354 – 386 Disordered
Alternative sequence 215 – 386 Missing. In isoform 3.



Literature citations
Welander distal myopathy is caused by a mutation in the RNA-binding protein TIA1.
Hackman P.; Sarparanta J.; Lehtinen S.; Vihola A.; Evila A.; Jonson P.H.; Luque H.; Kere J.; Screen M.; Chinnery P.F.; Ahlberg G.; Edstrom L.; Udd B.;
Ann. Neurol. 73:500-509(2013)
Cited for: VARIANT WDM LYS-384; CHARACTERIZATION OF VARIANT WDM LYS-384; Welander distal myopathy caused by an ancient founder mutation in TIA1 associated with perturbed splicing.
Klar J.; Sobol M.; Melberg A.; Maebert K.; Ameur A.; Johansson A.C.; Feuk L.; Entesarian M.; Orlen H.; Casar-Borota O.; Dahl N.;
Hum. Mutat. 34:572-577(2013)
Cited for: VARIANT WDM LYS-384; TIA1 Mutations in Amyotrophic Lateral Sclerosis and Frontotemporal Dementia Promote Phase Separation and Alter Stress Granule Dynamics.
Mackenzie I.R.; Nicholson A.M.; Sarkar M.; Messing J.; Purice M.D.; Pottier C.; Annu K.; Baker M.; Perkerson R.B.; Kurti A.; Matchett B.J.; Mittag T.; Temirov J.; Hsiung G.R.; Krieger C.; Murray M.E.; Kato M.; Fryer J.D.; Petrucelli L.; Zinman L.; Weintraub S.; Mesulam M.; Keith J.; Zivkovic S.A.; Hirsch-Reinshagen V.; Roos R.P.; Zuechner S.; Graff-Radford N.R.; Petersen R.C.; Caselli R.J.; Wszolek Z.K.; Finger E.; Lippa C.; Lacomis D.; Stewart H.; Dickson D.W.; Kim H.J.; Rogaeva E.; Bigio E.; Boylan K.B.; Taylor J.P.; Rademakers R.;
Neuron 95:808-816.e9(2017)
Cited for: INVOLVEMENT IN ALS26; VARIANTS ALS26 MET-294; ILE-334; ARG-355; MET-360; LEU-362 AND THR-381; CHARACTERIZATION OF VARIANTS ALS26 LEU-362 AND WDM LYS-384;
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.