P70318 · TIAR_MOUSE

  • Protein
    Nucleolysin TIAR
  • Gene
    Tial1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

RNA-binding protein involved in alternative pre-RNA splicing and in cytoplasmic stress granules formation (By similarity).
Shows a preference for uridine-rich RNAs (By similarity).
Activates splicing of alternative exons with weak 5' splice sites followed by a U-rich stretch on its own pre-mRNA and on TIA1 mRNA (PubMed:11514562).
Promotes the inclusion of TIA1 exon 5 to give rise to the long isoform (isoform a) of TIA1 (PubMed:17488725).
Acts downstream of the stress-induced phosphorylation of EIF2S1/EIF2A to promote the recruitment of untranslated mRNAs to cytoplasmic stress granules (SG) (By similarity).
Possesses nucleolytic activity against cytotoxic lymphocyte target cells (By similarity).
May be involved in apoptosis (By similarity).

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytolytic granule
Cellular Componentcytoplasm
Cellular Componentcytoplasmic stress granule
Cellular Componentcytosol
Cellular Componentnucleoplasm
Cellular Componentnucleus
Cellular Componentribonucleoprotein complex
Molecular FunctionDNA binding
Molecular FunctionmRNA 3'-UTR AU-rich region binding
Molecular Functionprotein-RNA adaptor activity
Biological Processapoptotic process
Biological Processgerm cell development
Biological Processnegative regulation of cell population proliferation
Biological Processpositive regulation of hippo signaling
Biological Processpositive regulation of miRNA-mediated gene silencing
Biological Processpositive regulation of stem cell proliferation
Biological Processstem cell division
Biological Processstem cell proliferation

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Nucleolysin TIAR
  • Alternative names
    • TIA-1-related protein

Gene names

    • Name
      Tial1

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    P70318

Proteomes

Organism-specific databases

Subcellular Location

Nucleus
Cytoplasm
Cytolytic granule
Note: Nuclear import seems to be coupled to RNA polymerase II transcription and may be dependent on RNA-binding (PubMed:16278295).
Accumulates in cytoplasmic stress granules (SG) following cellular damage (By similarity).

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis117-121Impairs nuclear localization.
Mutagenesis156-160Impairs nuclear localization.
Mutagenesis225-229Abolishes nuclear export.
Mutagenesis258-264Abolishes nuclear export.
Mutagenesis293-300No effect on nuclear localization.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 12 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00000819791-392Nucleolysin TIAR
Modified residue139N6-acetyllysine
Modified residue218Phosphoserine

Post-translational modification

Phosphorylated by MAPK14 following DNA damage, releasing TIAR from GADD45A mRNA.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed both in primordial germ cells (PGCs) and in neighboring somatic cells.

Gene expression databases

Interaction

Subunit

Interacts with FASTK.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY P70318Ddx21 Q8K2L42EBI-299820, EBI-7977861
BINARY P70318Hnrnpm Q3THB32EBI-299820, EBI-4282050
BINARY P70318Srsf1 Q6PDM23EBI-299820, EBI-2550360

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain9-102RRM 1
Domain114-192RRM 2
Domain222-294RRM 3
Region363-392Disordered

Domain

The RRM 2 domain is required for the binding to target RNA, and the RRM 1 and RRM 3 domains seem to contribute to the affinity of the interaction with RNA.
The RRM2 domain and the C-terminal residues 290-339 contribute to nuclear localization.
The RRM3 domain mediates nuclear export and cytoplasmic localization in a manner dependent on RNA- binding.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    392
  • Mass (Da)
    43,389
  • Last updated
    1997-02-01 v1
  • Checksum
    66E6AF14B9EBE77A
MMEDDGQPRTLYVGNLSRDVTEVLILQLFSQIGPCKSCKMITEQPDSRRVNSSVGFSVLQHTSNDPYCFVEFYEHRDAAAALAAMNGRKILGKEVKVNWATTPSSQKKDTSNHFHVFVGDLSPEITTEDIKSAFAPFGKISDARVVKDMATGKSKGYGFVSFYNKLDAENAIVHMGGQWLGGRQIRTNWATRKPPAPKSTQETNTKQLRFEDVVNQSSPKNCTVYCGGIASGLTDQLMRQTFSPFGQIMEIRVFPEKGYSFVRFSTHESAAHAIVSVNGTTIEGHVVKCYWGKESPDMTKNFQQVDYSQWGQWSQVYGNPQQYGQYMANGWQVPPYGVYGQPWNQQGFGVDQSPSAAWMGGFGAQPPQGQAPPPVIPPPNQAGYGMASFPTQ

Computationally mapped potential isoform sequences

There are 8 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A0U1RPL4A0A0U1RPL4_MOUSETial142
A0A0U1RPD3A0A0U1RPD3_MOUSETial1244
A0A0U1RPE1A0A0U1RPE1_MOUSETial1106
A0A0U1RPB0A0A0U1RPB0_MOUSETial1140
A0A0U1RP00A0A0U1RP00_MOUSETial1107
D3Z3Y4D3Z3Y4_MOUSETial1336
D6RGU1D6RGU1_MOUSETial1135
Q921W2Q921W2_MOUSETial1375

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U55861
EMBL· GenBank· DDBJ
AAC52870.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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