UniProt functional annotation for P17679



	UniProt functional annotation for P17679

UniProt code: P17679.

Organism: Mus musculus (Mouse).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus.

Function: Transcriptional activator or repressor which probably serves as a general switch factor for erythroid development. It binds to DNA sites with the consensus sequence 5'-[AT]GATA[AG]-3' within regulatory regions of globin genes and of other genes expressed in erythroid cells. Activates the transcription of genes involved in erythroid differentiation of K562 erythroleukemia cells, including HBB, HBG1/2, ALAS2 and HMBS (By similarity). {ECO:0000250|UniProtKB:P15976, ECO:0000269|PubMed:15173587, ECO:0000269|PubMed:16888089, ECO:0000269|PubMed:2276623, ECO:0000269|PubMed:8206977, ECO:0000269|PubMed:8524811}.

Subunit: May form homodimers or heterodimers with other isoforms. Interacts (via the N-terminal zinc finger) with ZFPM1 (By similarity). Interacts with GFI1B. Interacts with PIAS4; the interaction enhances sumoylation and represses the transactivational activity in a sumoylation-independent manner. Interacts with LMCD1. Interacts with CREBBP; the interaction stimulates acetylation and transcriptional activity in vivo. Interacts with BRD3. Interacts with MED1, CCAR1 and CALCOCO1. Interacts with EP300 (By similarity). Interacts with CEBPE (By similarity). {ECO:0000250|UniProtKB:P15976, ECO:0000269|PubMed:10207073, ECO:0000269|PubMed:15173587, ECO:0000269|PubMed:15920471, ECO:0000269|PubMed:16199866, ECO:0000269|PubMed:21536911, ECO:0000269|PubMed:21555453, ECO:0000269|PubMed:24245781, ECO:0000269|PubMed:8524811}.

Subcellular location: Nucleus {ECO:0000269|PubMed:16888089}.

Tissue specificity: Erythrocytes. Expressed (at protein level) in liver. {ECO:0000269|PubMed:2725678, ECO:0000269|PubMed:8524811}.

Developmental stage: Detected at 11.5-day fetal livers (at protein level). Isoform 2 detected earlier at 8.5-day embryo. {ECO:0000269|PubMed:8524811}.

Domain: The two fingers are functionally distinct and cooperate to achieve specific, stable DNA binding. The first finger is necessary only for full specificity and stability of binding, whereas the second one is required for binding.

Ptm: Highly phosphorylated on serine residues. Phosphorylation on Ser- 310 is enhanced on erythroid differentiation. Phosphorylation on Ser- 142 promotes sumoylation on Lys-137 (By similarity). {ECO:0000250}.

Ptm: Sumoylation on Lys-137 is enhanced by phosphorylation on Ser-142 and by interaction with PIAS4. Sumoylation with SUMO1 has no effect on transcriptional activity. {ECO:0000269|PubMed:15173587, ECO:0000269|PubMed:8206977}.

Ptm: Acetylated on Lys-233, Lys-245 Lys-246 by EP300 (By similarity). Acetylated on Lys-246, Lys-252 and Lys-312 by CREBBP in vitro. Acetylation does not affect DNA-binding in vitro but is essential to induce erythroid differentiation and for binding chromatin in vivo. {ECO:0000250, ECO:0000269|PubMed:10207073, ECO:0000269|PubMed:21536911}.

Miscellaneous: [Isoform 2]: Produced by alternative initiation at Met- 84 of isoform 1. Less effective than isoform 1 in its ability to transactivate target genes. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Mus musculus (Mouse).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus.



Function:		Transcriptional activator or repressor which probably serves as a general switch factor for erythroid development. It binds to DNA sites with the consensus sequence 5'-[AT]GATA[AG]-3' within regulatory regions of globin genes and of other genes expressed in erythroid cells. Activates the transcription of genes involved in erythroid differentiation of K562 erythroleukemia cells, including HBB, HBG1/2, ALAS2 and HMBS (By similarity). {ECO:0000250\|UniProtKB:P15976, ECO:0000269\|PubMed:15173587, ECO:0000269\|PubMed:16888089, ECO:0000269\|PubMed:2276623, ECO:0000269\|PubMed:8206977, ECO:0000269\|PubMed:8524811}.


Subunit:		May form homodimers or heterodimers with other isoforms. Interacts (via the N-terminal zinc finger) with ZFPM1 (By similarity). Interacts with GFI1B. Interacts with PIAS4; the interaction enhances sumoylation and represses the transactivational activity in a sumoylation-independent manner. Interacts with LMCD1. Interacts with CREBBP; the interaction stimulates acetylation and transcriptional activity in vivo. Interacts with BRD3. Interacts with MED1, CCAR1 and CALCOCO1. Interacts with EP300 (By similarity). Interacts with CEBPE (By similarity). {ECO:0000250\|UniProtKB:P15976, ECO:0000269\|PubMed:10207073, ECO:0000269\|PubMed:15173587, ECO:0000269\|PubMed:15920471, ECO:0000269\|PubMed:16199866, ECO:0000269\|PubMed:21536911, ECO:0000269\|PubMed:21555453, ECO:0000269\|PubMed:24245781, ECO:0000269\|PubMed:8524811}.
Subcellular location:		Nucleus {ECO:0000269\|PubMed:16888089}.
Tissue specificity:		Erythrocytes. Expressed (at protein level) in liver. {ECO:0000269\|PubMed:2725678, ECO:0000269\|PubMed:8524811}.
Developmental stage:		Detected at 11.5-day fetal livers (at protein level). Isoform 2 detected earlier at 8.5-day embryo. {ECO:0000269\|PubMed:8524811}.
Domain:		The two fingers are functionally distinct and cooperate to achieve specific, stable DNA binding. The first finger is necessary only for full specificity and stability of binding, whereas the second one is required for binding.
Ptm:		Highly phosphorylated on serine residues. Phosphorylation on Ser- 310 is enhanced on erythroid differentiation. Phosphorylation on Ser- 142 promotes sumoylation on Lys-137 (By similarity). {ECO:0000250}.
Ptm:		Sumoylation on Lys-137 is enhanced by phosphorylation on Ser-142 and by interaction with PIAS4. Sumoylation with SUMO1 has no effect on transcriptional activity. {ECO:0000269\|PubMed:15173587, ECO:0000269\|PubMed:8206977}.
Ptm:		Acetylated on Lys-233, Lys-245 Lys-246 by EP300 (By similarity). Acetylated on Lys-246, Lys-252 and Lys-312 by CREBBP in vitro. Acetylation does not affect DNA-binding in vitro but is essential to induce erythroid differentiation and for binding chromatin in vivo. {ECO:0000250, ECO:0000269\|PubMed:10207073, ECO:0000269\|PubMed:21536911}.
Miscellaneous:		[Isoform 2]: Produced by alternative initiation at Met- 84 of isoform 1. Less effective than isoform 1 in its ability to transactivate target genes. {ECO:0000305}.