TIA1
entrez
7072
canonical
uniprot
P31483
canonical
ensembl
ENSG00000116001
resolver
ensp
ENSP00000282574
resolver
ensp
ENSP00000401371
resolver
ensp
ENSP00000404023
resolver
ensp
ENSP00000413751
resolver
ensp
ENSP00000430969
resolver
ensp
ENSP00000551417
resolver
ensp
ENSP00000551420
resolver
ensp
ENSP00000675033
resolver
ensp
ENSP00000675036
resolver
ensp
ENSP00000757991
resolver
ensp
ENSP00000757993
resolver
ensp
ENSP00000757995
resolver
ensp
ENSP00000768211
resolver
enst
ENST00000282574
resolver
enst
ENST00000474809
resolver
genesymbol
TIA1
resolver
hgnc
HGNC:11802
resolver
uniprot
E5RGV5
resolver
uniprot
F8W8I6
resolver
uniprot
Q53SS9
resolver
uniprot
Q96B58
resolver
uniprot_entry
E5RGV5_HUMAN
resolver
uniprot_entry
F8W8I6_HUMAN
resolver
uniprot_entry
TIA1_HUMAN
resolver
uniprot_sec
Q53SS9
resolver
uniprot_sec
Q96B58
resolver
amino_acid_sequence
MEDEMPKTLYVGNLSRDVTEALILQLFSQIGPCKNCKMIMDTAGNDPYCFVEFHEHRHAAAALAAMNGRKIMGKEVKVNWATTPSSQKKDTSSSTVVSTQRSQDHFHVFVGDLSPEITTEDIKAAFAPFGRISDARVVKDMATGKSKGYGFVSFFNKWDAENAIQQMGGQWLGGRQIRTNWATRKPPAPKSTYESNTKQLSYDEVVNQSSPSNCTVYCGGVTSGLTEQLMRQTFSPFGQIMEIRVFPDKGYSFVRFNSHESAAHAIVSVNGTTIEGHVVKCYWGKETLDMINPVQQQNQIGYPQPYGQWGQWYGNAQQIGQYMPNGWQVPAYGMYGQAWNQQGFNQTQSSAPWMGPNYGVQPPQGQNGSMLPNQPSGYRVAGYETQ
uniprot
proteins
disease_involvement
DISEASE: Welander distal myopathy (WDM) [MIM:604454]: An autosomal dominant disorder characterized by adult onset of distal muscle weakness predominantly affecting the distal long extensors of the hands, with slow progression to involve all small hand muscles and the lower legs. Skeletal muscle biopsy shows myopathic changes and prominent rimmed vacuoles. Rare homozygous patients showed earlier onset, faster progression, and proximal muscle involvement. {ECO:0000269|PubMed:23348830, ECO:0000269|PubMed:23401021}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Amyotrophic lateral sclerosis 26, with or without frontotemporal dementia (ALS26) [MIM:619133]: A form of amyotrophic lateral sclerosis, a neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of the cases. ALS26 inheritance is autosomal dominant. Some patients may develop frontotemporal dementia. {ECO:0000269|PubMed:28817800}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: RNA-binding protein involved in the regulation of alternative pre-RNA splicing and mRNA translation by binding to uridine-rich (U-rich) RNA sequences (PubMed:11106748, PubMed:12486009, PubMed:17488725, PubMed:8576255). Binds to U-rich sequences immediately downstream from a 5' splice sites in a uridine-rich small nuclear ribonucleoprotein (U snRNP)-dependent fashion, thereby modulating alternative pre-RNA splicing (PubMed:11106748, PubMed:8576255). Preferably binds to the U-rich IAS1 sequence in a U1 snRNP-dependent manner; this binding is optimal if a 5' splice site is adjacent to IAS1 (By similarity). Activates the use of heterologous 5' splice sites; the activation depends on the intron sequence downstream from the 5' splice site, with a preference for a downstream U-rich sequence (PubMed:11106748). By interacting with SNRPC/U1-C, promotes recruitment and binding of spliceosomal U1 snRNP to 5' splice sites followed by U-rich sequences, thereby facilitating atypical 5' splice site recognition by U1 snRNP (PubMed:11106748, PubMed:12486009, PubMed:17488725). Activates splicing of alternative exons with weak 5' splice sites followed by a U-rich stretch on its own pre-mRNA and on TIAR mRNA (By similarity). Acts as a modulator of alternative splicing for the apoptotic FAS receptor, thereby promoting apoptosis (PubMed:11106748, PubMed:17488725, PubMed:1934064). Binds to the 5' splice site region of FAS intron 5 to promote accumulation of transcripts that include exon 6 at the expense of transcripts in which exon 6 is skipped, thereby leading to the transcription of a membrane-bound apoptotic FAS receptor, which promotes apoptosis (PubMed:11106748, PubMed:17488725, PubMed:1934064). Binds to a conserved AU-rich cis element in COL2A1 intron 2 and modulates alternative splicing of COL2A1 exon 2 (PubMed:17580305). Also binds to the equivalent AT-rich element in COL2A1 genomic DNA, and may thereby be involved in the regulation of transcription (PubMed:17580305). Binds specifically to a polypyrimidine-rich controlling element (PCE) located between the weak 5' splice site and the intronic splicing silencer of CFTR mRNA to promote exon 9 inclusion, thereby antagonizing PTB1 and its role in exon skipping of CFTR exon 9 (PubMed:14966131). Involved in the repression of mRNA translation by binding to AU-rich elements (AREs) located in mRNA 3' untranslated regions (3' UTRs), including target ARE-bearing mRNAs encoding TNF and PTGS2 (By similarity). Also participates in the cellular response to environmental stress, by acting downstream of the stress-induced phosphorylation of EIF2S1/EIF2A to promote the recruitment of untranslated mRNAs to cytoplasmic stress granules (SGs), leading to stress-induced translational arrest (PubMed:10613902). Formation and recruitment to SGs is regulated by Zn(2+) (By similarity). Possesses nucleolytic activity against cytotoxic lymphocyte target cells (PubMed:1934064). {ECO:0000250|UniProtKB:P52912, ECO:0000269|PubMed:10613902, ECO:0000269|PubMed:11106748, ECO:0000269|PubMed:12486009, ECO:0000269|PubMed:14966131, ECO:0000269|PubMed:17488725, ECO:0000269|PubMed:17580305, ECO:0000269|PubMed:1934064, ECO:0000269|PubMed:8576255}.; FUNCTION: [Isoform Short]: Displays enhanced splicing regulatory activity compared with TIA isoform Long. {ECO:0000269|PubMed:17488725}.
uniprot
proteins
mass_dalton
42963
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by FASTK; phosphorylation occurs after FAS ligation in FAS-mediated apoptosis and before DNA fragmentation. {ECO:0000269|PubMed:7544399}.
uniprot
proteins
pubmed
10613902
uniprot
proteins
pubmed
11106748
uniprot
proteins
pubmed
12486009
uniprot
proteins
pubmed
14966131
uniprot
proteins
pubmed
15371533
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
17135269
uniprot
proteins
pubmed
17488725
uniprot
proteins
pubmed
17580305
uniprot
proteins
pubmed
17984221
uniprot
proteins
pubmed
18201561
uniprot
proteins
pubmed
1934064
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23348830
uniprot
proteins
pubmed
23401021
uniprot
proteins
pubmed
28817800
uniprot
proteins
pubmed
7544399
uniprot
proteins
pubmed
8176212
uniprot
proteins
pubmed
8576255
uniprot
proteins
sequence_length
386
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10613902, ECO:0000269|PubMed:15371533, ECO:0000269|PubMed:17984221, ECO:0000305|PubMed:18201561}. Cytoplasm {ECO:0000269|PubMed:17488725}. Cytoplasm, Stress granule {ECO:0000269|PubMed:10613902, ECO:0000269|PubMed:15371533, ECO:0000269|PubMed:17984221}. Note=Accumulates in cytoplasmic stress granules (SG) following cellular damage (PubMed:10613902, PubMed:15371533). Recruitment to SG is induced by Zn(2+) (By similarity). {ECO:0000250|UniProtKB:P52912, ECO:0000269|PubMed:10613902, ECO:0000269|PubMed:15371533}.
uniprot
proteins