UniProt functional annotation for Q9H7E2



	UniProt functional annotation for Q9H7E2

UniProt code: Q9H7E2.

Organism: Homo sapiens (Human).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.

Function: Scaffolding protein that specifically recognizes and binds dimethylarginine-containing proteins. In nucleus, acts as a coactivator: recognizes and binds asymmetric dimethylation on the core histone tails associated with transcriptional activation (H3R17me2a and H4R3me2a) and recruits proteins at these arginine-methylated loci. In cytoplasm, may play a role in the assembly and/or disassembly of mRNA stress granules and in the regulation of translation of target mRNAs by binding Arg/Gly-rich motifs (GAR) in dimethylarginine-containing proteins. {ECO:0000269|PubMed:15955813, ECO:0000269|PubMed:18632687, ECO:0000269|PubMed:21172665}.

Subunit: Component of mRNA stress granules. Interacts with FMR1, FXR1, FXR2, EWSR1, FUS, SERBP1, EEF1A1 and DDX3X or DDX3Y, and with the small nuclear ribonucleoprotein-associated proteins SNRPB and SNRPN. Interacts with 'Lys-48'-linked tetra-ubiquitin, but not with monoubiquitin or 'Lys-63'-linked ubiquitin chains. May interact with the exon junction complex (EJC) composed at least of CASC3, EIF4A3, MAGOH and RBM8A. Interacts with POLR2A (via the C-terminal domain (CTD)). {ECO:0000269|PubMed:15955813, ECO:0000269|PubMed:18632687, ECO:0000269|PubMed:18664458, ECO:0000269|PubMed:20930030, ECO:0000269|PubMed:26700805}.

Subcellular location: Cytoplasm {ECO:0000269|PubMed:18632687}. Nucleus {ECO:0000269|PubMed:21172665}. Note=Predominantly cytoplasmic. Associated with actively translating polyribosomes and with mRNA stress granules. {ECO:0000269|PubMed:18632687, ECO:0000269|PubMed:18664458}.

Tissue specificity: Detected in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. {ECO:0000269|PubMed:18664458}.

Domain: The Tudor domain specifically recognizes and binds asymmetric dimethylation of histone H3 'Arg-17' (H3R17me2a) and histones H4 'Arg- 3', 2 tags for epigenetic transcriptional activation. {ECO:0000269|PubMed:21172665}.

Annotations taken from UniProtKB at the EBI.


Organism:		Homo sapiens (Human).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.



Function:		Scaffolding protein that specifically recognizes and binds dimethylarginine-containing proteins. In nucleus, acts as a coactivator: recognizes and binds asymmetric dimethylation on the core histone tails associated with transcriptional activation (H3R17me2a and H4R3me2a) and recruits proteins at these arginine-methylated loci. In cytoplasm, may play a role in the assembly and/or disassembly of mRNA stress granules and in the regulation of translation of target mRNAs by binding Arg/Gly-rich motifs (GAR) in dimethylarginine-containing proteins. {ECO:0000269\|PubMed:15955813, ECO:0000269\|PubMed:18632687, ECO:0000269\|PubMed:21172665}.


Subunit:		Component of mRNA stress granules. Interacts with FMR1, FXR1, FXR2, EWSR1, FUS, SERBP1, EEF1A1 and DDX3X or DDX3Y, and with the small nuclear ribonucleoprotein-associated proteins SNRPB and SNRPN. Interacts with 'Lys-48'-linked tetra-ubiquitin, but not with monoubiquitin or 'Lys-63'-linked ubiquitin chains. May interact with the exon junction complex (EJC) composed at least of CASC3, EIF4A3, MAGOH and RBM8A. Interacts with POLR2A (via the C-terminal domain (CTD)). {ECO:0000269\|PubMed:15955813, ECO:0000269\|PubMed:18632687, ECO:0000269\|PubMed:18664458, ECO:0000269\|PubMed:20930030, ECO:0000269\|PubMed:26700805}.
Subcellular location:		Cytoplasm {ECO:0000269\|PubMed:18632687}. Nucleus {ECO:0000269\|PubMed:21172665}. Note=Predominantly cytoplasmic. Associated with actively translating polyribosomes and with mRNA stress granules. {ECO:0000269\|PubMed:18632687, ECO:0000269\|PubMed:18664458}.
Tissue specificity:		Detected in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. {ECO:0000269\|PubMed:18664458}.
Domain:		The Tudor domain specifically recognizes and binds asymmetric dimethylation of histone H3 'Arg-17' (H3R17me2a) and histones H4 'Arg- 3', 2 tags for epigenetic transcriptional activation. {ECO:0000269\|PubMed:21172665}.