UniProt functional annotation for Q7KZF4



	UniProt functional annotation for Q7KZF4

UniProt code: Q7KZF4.

Organism: Homo sapiens (Human).

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

Function: Endonuclease that mediates miRNA decay of both protein-free and AGO2-loaded miRNAs (PubMed:28546213, PubMed:18453631). As part of its function in miRNA decay, regulates mRNAs involved in G1-to-S phase transition (PubMed:28546213). Functions as a bridging factor between STAT6 and the basal transcription factor (PubMed:12234934). Plays a role in PIM1 regulation of MYB activity (PubMed:9809063). Functions as a transcriptional coactivator for STAT5 (By similarity). {ECO:0000250|UniProtKB:Q78PY7, ECO:0000269|PubMed:12234934, ECO:0000269|PubMed:18453631, ECO:0000269|PubMed:28546213, ECO:0000269|PubMed:9809063}.

Function: (Microbial infection) Functions as a transcriptional coactivator for the Epstein-Barr virus nuclear antigen 2 (EBNA2). {ECO:0000269|PubMed:7651391}.

Catalytic activity: Reaction=Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'- phosphooligonucleotide end-products.; EC=3.1.31.1; Evidence={ECO:0000269|PubMed:18453631, ECO:0000269|PubMed:28546213};

Subunit: Forms a ternary complex with STAT6 and POLR2A (PubMed:12234934). Associates with the RNA-induced silencing complex (RISC) (PubMed:14508492, PubMed:28546213). Interacts with the RISC components AGO2, FMR1 and TNRC6A (PubMed:14508492, PubMed:28546213). Interacts with GTF2E1 and GTF2E2 (PubMed:7651391). Interacts with PIM1 (PubMed:9809063). Interacts with STAT5 (By similarity). Interacts with SYT11 (via C2 2 domain); the interaction with SYT11 is direct (By similarity). {ECO:0000250|UniProtKB:Q78PY7, ECO:0000269|PubMed:12234934, ECO:0000269|PubMed:14508492, ECO:0000269|PubMed:28546213, ECO:0000269|PubMed:7651391, ECO:0000269|PubMed:9809063}.

Subunit: (Microbial infection) Interacts with EAV NSP1 (PubMed:12917451). Binds to acidic transactivation domain of EBNA2 (PubMed:7651391). {ECO:0000269|PubMed:12917451, ECO:0000269|PubMed:7651391}.

Subcellular location: Cytoplasm {ECO:0000269|PubMed:14508492, ECO:0000269|PubMed:17081065}. Nucleus {ECO:0000269|PubMed:12234934, ECO:0000269|PubMed:14508492, ECO:0000269|PubMed:17081065, ECO:0000269|PubMed:7651391}. Melanosome {ECO:0000269|PubMed:17081065}. Note=In IL-4 stimulated cells colocalizes with STAT6 in the nucleus (PubMed:12234934). Identified by mass spectrometry in melanosome fractions from stage I to stage IV (PubMed:17081065). {ECO:0000269|PubMed:12234934, ECO:0000269|PubMed:17081065}.

Tissue specificity: Ubiquitously expressed. {ECO:0000269|PubMed:7651391}.

Ptm: Phosphorylated by PIM1 in vitro. {ECO:0000269|PubMed:9809063}.

Sequence caution: Sequence=AAA80488.1; Type=Frameshift; Note=The frameshift leads to wrong initiation.; Evidence={ECO:0000305};

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:		Endonuclease that mediates miRNA decay of both protein-free and AGO2-loaded miRNAs (PubMed:28546213, PubMed:18453631). As part of its function in miRNA decay, regulates mRNAs involved in G1-to-S phase transition (PubMed:28546213). Functions as a bridging factor between STAT6 and the basal transcription factor (PubMed:12234934). Plays a role in PIM1 regulation of MYB activity (PubMed:9809063). Functions as a transcriptional coactivator for STAT5 (By similarity). {ECO:0000250\|UniProtKB:Q78PY7, ECO:0000269\|PubMed:12234934, ECO:0000269\|PubMed:18453631, ECO:0000269\|PubMed:28546213, ECO:0000269\|PubMed:9809063}.



Function:		(Microbial infection) Functions as a transcriptional coactivator for the Epstein-Barr virus nuclear antigen 2 (EBNA2). {ECO:0000269\|PubMed:7651391}.


Catalytic activity:		Reaction=Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'- phosphooligonucleotide end-products.; EC=3.1.31.1; Evidence={ECO:0000269\|PubMed:18453631, ECO:0000269\|PubMed:28546213};
Subunit:		Forms a ternary complex with STAT6 and POLR2A (PubMed:12234934). Associates with the RNA-induced silencing complex (RISC) (PubMed:14508492, PubMed:28546213). Interacts with the RISC components AGO2, FMR1 and TNRC6A (PubMed:14508492, PubMed:28546213). Interacts with GTF2E1 and GTF2E2 (PubMed:7651391). Interacts with PIM1 (PubMed:9809063). Interacts with STAT5 (By similarity). Interacts with SYT11 (via C2 2 domain); the interaction with SYT11 is direct (By similarity). {ECO:0000250\|UniProtKB:Q78PY7, ECO:0000269\|PubMed:12234934, ECO:0000269\|PubMed:14508492, ECO:0000269\|PubMed:28546213, ECO:0000269\|PubMed:7651391, ECO:0000269\|PubMed:9809063}.
Subunit:		(Microbial infection) Interacts with EAV NSP1 (PubMed:12917451). Binds to acidic transactivation domain of EBNA2 (PubMed:7651391). {ECO:0000269\|PubMed:12917451, ECO:0000269\|PubMed:7651391}.
Subcellular location:		Cytoplasm {ECO:0000269\|PubMed:14508492, ECO:0000269\|PubMed:17081065}. Nucleus {ECO:0000269\|PubMed:12234934, ECO:0000269\|PubMed:14508492, ECO:0000269\|PubMed:17081065, ECO:0000269\|PubMed:7651391}. Melanosome {ECO:0000269\|PubMed:17081065}. Note=In IL-4 stimulated cells colocalizes with STAT6 in the nucleus (PubMed:12234934). Identified by mass spectrometry in melanosome fractions from stage I to stage IV (PubMed:17081065). {ECO:0000269\|PubMed:12234934, ECO:0000269\|PubMed:17081065}.
Tissue specificity:		Ubiquitously expressed. {ECO:0000269\|PubMed:7651391}.
Ptm:		Phosphorylated by PIM1 in vitro. {ECO:0000269\|PubMed:9809063}.
Sequence caution:		Sequence=AAA80488.1; Type=Frameshift; Note=The frameshift leads to wrong initiation.; Evidence={ECO:0000305};