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Nucleolysin TIAR (TIA-1-related protein)

 TIAR_MOUSE              Reviewed;         392 AA.
P70318;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-FEB-1997, sequence version 1.
25-OCT-2017, entry version 134.
RecName: Full=Nucleolysin TIAR;
AltName: Full=TIA-1-related protein;
Name=Tial1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8871565; DOI=10.1093/nar/24.19.3829;
Beck A.R.P., Medley O.G., O'Brien S., Anderson P., Streuli M.;
"Structure, tissue distribution and genomic organization of the murine
RRM-type RNA binding proteins TIA-1 and TIAR.";
Nucleic Acids Res. 24:3829-3836(1996).
[2]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[3]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=19861488; DOI=10.1530/REP-09-0373;
Yamaji M., Tanaka T., Shigeta M., Chuma S., Saga Y., Saitou M.;
"Functional reconstruction of NANOS3 expression in the germ cell
lineage by a novel transgenic reporter reveals distinct subcellular
localizations of NANOS3.";
Reproduction 139:381-393(2010).
-!- FUNCTION: RNA-binding protein. Possesses nucleolytic activity
against cytotoxic lymphocyte target cells. May be involved in
apoptosis (By similarity). {ECO:0000250}.
-!- INTERACTION:
Q8K2L4:Ddx21; NbExp=2; IntAct=EBI-299820, EBI-7977861;
Q3THB3:Hnrnpm; NbExp=2; IntAct=EBI-299820, EBI-4282050;
Q6PDM2:Srsf1; NbExp=3; IntAct=EBI-299820, EBI-2550360;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19861488}.
Nucleus {ECO:0000269|PubMed:19861488}. Cytoplasmic granule
{ECO:0000269|PubMed:19861488}. Note=The cytoplasmic granules are
stress granules which are a dense aggregation in the cytosol
composed of proteins and RNAs that appear when the cell is under
stress. Colocalizes with NANOS3 in the stress granules.
-!- TISSUE SPECIFICITY: Expressed both in primordial germ cells (PGCs)
and in neighboring somatic cells. {ECO:0000269|PubMed:19861488}.
-!- PTM: Phosphorylated by MAPK14 following DNA damage, releasing TIAR
from GADD45A mRNA. {ECO:0000250}.
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EMBL; U55861; AAC52870.1; -; mRNA.
CCDS; CCDS21897.1; -.
PIR; S72436; S72436.
RefSeq; NP_033409.1; NM_009383.2.
UniGene; Mm.242072; -.
ProteinModelPortal; P70318; -.
SMR; P70318; -.
BioGrid; 204192; 3.
IntAct; P70318; 28.
MINT; MINT-4137828; -.
STRING; 10090.ENSMUSP00000101833; -.
iPTMnet; P70318; -.
PhosphoSitePlus; P70318; -.
EPD; P70318; -.
PaxDb; P70318; -.
PeptideAtlas; P70318; -.
PRIDE; P70318; -.
Ensembl; ENSMUST00000106226; ENSMUSP00000101833; ENSMUSG00000030846.
GeneID; 21843; -.
KEGG; mmu:21843; -.
UCSC; uc009jyy.1; mouse.
CTD; 7073; -.
MGI; MGI:107913; Tial1.
eggNOG; KOG0148; Eukaryota.
eggNOG; ENOG410XQ8U; LUCA.
GeneTree; ENSGT00870000136413; -.
HOGENOM; HOG000206748; -.
HOVERGEN; HBG105006; -.
InParanoid; P70318; -.
KO; K13201; -.
OMA; GSQRHTF; -.
OrthoDB; EOG091G0FH8; -.
PhylomeDB; P70318; -.
TreeFam; TF312915; -.
Reactome; R-MMU-6803529; FGFR2 alternative splicing.
ChiTaRS; Tial1; mouse.
PRO; PR:P70318; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000030846; -.
ExpressionAtlas; P70318; baseline and differential.
Genevisible; P70318; MM.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0017091; F:AU-rich element binding; IDA:MGI.
GO; GO:0003677; F:DNA binding; IEA:InterPro.
GO; GO:0003723; F:RNA binding; ISO:MGI.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0007281; P:germ cell development; IMP:MGI.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:MGI.
GO; GO:0017145; P:stem cell division; IMP:MGI.
CDD; cd12616; RRM1_TIAR; 1.
CDD; cd12617; RRM2_TIAR; 1.
CDD; cd12620; RRM3_TIAR; 1.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
InterPro; IPR003954; RRM_dom_euk.
InterPro; IPR034492; TIAR_RRM1.
InterPro; IPR034494; TIAR_RRM2.
InterPro; IPR034496; TIAR_RRM3.
Pfam; PF00076; RRM_1; 3.
SMART; SM00360; RRM; 3.
SMART; SM00361; RRM_1; 3.
SUPFAM; SSF54928; SSF54928; 3.
PROSITE; PS50102; RRM; 3.
1: Evidence at protein level;
Acetylation; Apoptosis; Complete proteome; Cytoplasm; Nucleus;
Phosphoprotein; Reference proteome; Repeat; RNA-binding.
CHAIN 1 392 Nucleolysin TIAR.
/FTId=PRO_0000081979.
DOMAIN 9 102 RRM 1. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 114 192 RRM 2. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 222 294 RRM 3. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
MOD_RES 139 139 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q01085}.
MOD_RES 218 218 Phosphoserine.
{ECO:0000250|UniProtKB:Q01085}.
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


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