ID TIAR_MOUSE Reviewed; 392 AA. AC P70318; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 09-DEC-2015, entry version 119. DE RecName: Full=Nucleolysin TIAR; DE AltName: Full=TIA-1-related protein; GN Name=Tial1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=8871565; DOI=10.1093/nar/24.19.3829; RA Beck A.R.P., Medley O.G., O'Brien S., Anderson P., Streuli M.; RT "Structure, tissue distribution and genomic organization of the murine RT RRM-type RNA binding proteins TIA-1 and TIAR."; RL Nucleic Acids Res. 24:3829-3836(1996). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Lung, Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and RT expression."; RL Cell 143:1174-1189(2010). RN [3] RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=19861488; DOI=10.1530/REP-09-0373; RA Yamaji M., Tanaka T., Shigeta M., Chuma S., Saga Y., Saitou M.; RT "Functional reconstruction of NANOS3 expression in the germ cell RT lineage by a novel transgenic reporter reveals distinct subcellular RT localizations of NANOS3."; RL Reproduction 139:381-393(2010). CC -!- FUNCTION: RNA-binding protein. Possesses nucleolytic activity CC against cytotoxic lymphocyte target cells. May be involved in CC apoptosis (By similarity). {ECO:0000250}. CC -!- INTERACTION: CC Q8K2L4:Ddx21; NbExp=2; IntAct=EBI-299820, EBI-7977861; CC Q3THB3:Hnrnpm; NbExp=2; IntAct=EBI-299820, EBI-4282050; CC Q6PDM2:Srsf1; NbExp=3; IntAct=EBI-299820, EBI-2550360; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19861488}. CC Nucleus {ECO:0000269|PubMed:19861488}. Cytoplasmic granule CC {ECO:0000269|PubMed:19861488}. Note=The cytoplasmic granules are CC stress granules which are a dense aggregation in the cytosol CC composed of proteins and RNAs that appear when the cell is under CC stress. Colocalizes with NANOS3 in the stress granules. CC -!- TISSUE SPECIFICITY: Expressed both in primordial germ cells (PGCs) CC and in neighboring somatic cells. {ECO:0000269|PubMed:19861488}. CC -!- PTM: Phosphorylated by MAPK14 following DNA damage, releasing TIAR CC from GADD45A mRNA. {ECO:0000250}. CC -!- SIMILARITY: Contains 3 RRM (RNA recognition motif) domains. CC {ECO:0000255|PROSITE-ProRule:PRU00176}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U55861; AAC52870.1; -; mRNA. DR CCDS; CCDS21897.1; -. DR PIR; S72436; S72436. DR RefSeq; NP_033409.1; NM_009383.2. DR UniGene; Mm.242072; -. DR ProteinModelPortal; P70318; -. DR SMR; P70318; 1-299. DR BioGrid; 204192; 3. DR IntAct; P70318; 28. DR MINT; MINT-4137828; -. DR STRING; 10090.ENSMUSP00000101833; -. DR PhosphoSite; P70318; -. DR MaxQB; P70318; -. DR PaxDb; P70318; -. DR PRIDE; P70318; -. DR Ensembl; ENSMUST00000106226; ENSMUSP00000101833; ENSMUSG00000030846. DR GeneID; 21843; -. DR KEGG; mmu:21843; -. DR UCSC; uc009jyy.1; mouse. DR CTD; 7073; -. DR MGI; MGI:107913; Tial1. DR eggNOG; KOG0148; Eukaryota. DR eggNOG; ENOG410XQ8U; LUCA. DR HOGENOM; HOG000206748; -. DR HOVERGEN; HBG105006; -. DR InParanoid; P70318; -. DR KO; K13201; -. DR OMA; CKMITEM; -. DR OrthoDB; EOG7XH6QJ; -. DR PhylomeDB; P70318; -. DR TreeFam; TF312915; -. DR ChiTaRS; Tial1; mouse. DR NextBio; 301310; -. DR PRO; PR:P70318; -. DR Proteomes; UP000000589; Chromosome 7. DR Bgee; P70318; -. DR ExpressionAtlas; P70318; baseline. DR Genevisible; P70318; MM. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0017091; F:AU-rich element binding; IDA:MGI. DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro. DR GO; GO:0044822; F:poly(A) RNA binding; ISO:MGI. DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW. DR GO; GO:0007281; P:germ cell development; IMP:MGI. DR GO; GO:0008284; P:positive regulation of cell proliferation; IMP:MGI. DR GO; GO:0017145; P:stem cell division; IMP:MGI. DR Gene3D; 3.30.70.330; -; 3. DR InterPro; IPR012677; Nucleotide-bd_a/b_plait. DR InterPro; IPR000504; RRM_dom. DR Pfam; PF00076; RRM_1; 4. DR SMART; SM00360; RRM; 3. DR PROSITE; PS50102; RRM; 3. PE 1: Evidence at protein level; KW Acetylation; Apoptosis; Complete proteome; Cytoplasm; Nucleus; KW Phosphoprotein; Reference proteome; Repeat; RNA-binding. FT CHAIN 1 392 Nucleolysin TIAR. FT /FTId=PRO_0000081979. FT DOMAIN 9 102 RRM 1. {ECO:0000255|PROSITE- FT ProRule:PRU00176}. FT DOMAIN 114 192 RRM 2. {ECO:0000255|PROSITE- FT ProRule:PRU00176}. FT DOMAIN 222 294 RRM 3. {ECO:0000255|PROSITE- FT ProRule:PRU00176}. FT MOD_RES 139 139 N6-acetyllysine. FT {ECO:0000250|UniProtKB:Q01085}. FT MOD_RES 218 218 Phosphoserine. FT {ECO:0000250|UniProtKB:Q01085}. SQ SEQUENCE 392 AA; 43389 MW; 66E6AF14B9EBE77A CRC64; MMEDDGQPRT LYVGNLSRDV TEVLILQLFS QIGPCKSCKM ITEQPDSRRV NSSVGFSVLQ HTSNDPYCFV EFYEHRDAAA ALAAMNGRKI LGKEVKVNWA TTPSSQKKDT SNHFHVFVGD LSPEITTEDI KSAFAPFGKI SDARVVKDMA TGKSKGYGFV SFYNKLDAEN AIVHMGGQWL GGRQIRTNWA TRKPPAPKST QETNTKQLRF EDVVNQSSPK NCTVYCGGIA SGLTDQLMRQ TFSPFGQIME IRVFPEKGYS FVRFSTHESA AHAIVSVNGT TIEGHVVKCY WGKESPDMTK NFQQVDYSQW GQWSQVYGNP QQYGQYMANG WQVPPYGVYG QPWNQQGFGV DQSPSAAWMG GFGAQPPQGQ APPPVIPPPN QAGYGMASFP TQ //