UniProt functional annotation for P11831



	UniProt functional annotation for P11831

UniProt code: P11831.

Organism: Homo sapiens (Human).

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

Function: SRF is a transcription factor that binds to the serum response element (SRE), a short sequence of dyad symmetry located 300 bp to the 5' of the site of transcription initiation of some genes (such as FOS). Together with MRTFA transcription coactivator, controls expression of genes regulating the cytoskeleton during development, morphogenesis and cell migration. The SRF-MRTFA complex activity responds to Rho GTPase-induced changes in cellular globular actin (G- actin) concentration, thereby coupling cytoskeletal gene expression to cytoskeletal dynamics. Required for cardiac differentiation and maturation. {ECO:0000250|UniProtKB:Q9JM73}.

Subunit: Binds DNA as a multimer, probably a dimer (PubMed:7637780). Interacts with MRTFA, forming the SRF-MRTFA nuclear complex which binds the 5'-CArG-3' consensus motif (CArG box) on DNA via SRF (PubMed:14565952, PubMed:19350017). Forms a nuclear ternary complex with MRTFA and SCAI (PubMed:19350017). Interacts with MRTFB (PubMed:14565952). Interacts with MLLT7/FOXO4, NKX3A and SSRP1 (PubMed:16054032). Interacts with ARID2 (By similarity). Interacts with SRFBP1 (By similarity). Interacts with FOXK1 (PubMed:17670796). Interacts with LPXN (PubMed:18497331). Interacts with OLFM2; the interaction promotes dissociation of SRF from the transcriptional repressor HEY2, facilitates binding of SRF to target genes and promotes smooth muscle differentiation (PubMed:25298399). {ECO:0000250|UniProtKB:Q9JM73, ECO:0000269|PubMed:14565952, ECO:0000269|PubMed:16054032, ECO:0000269|PubMed:17670796, ECO:0000269|PubMed:18497331, ECO:0000269|PubMed:19350017, ECO:0000269|PubMed:25298399, ECO:0000269|PubMed:7637780}.

Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00251, ECO:0000269|PubMed:19350017}.

Ptm: Phosphorylated by PRKDC. {ECO:0000269|PubMed:1547771, ECO:0000269|PubMed:8375385, ECO:0000269|PubMed:8407951}.

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:		SRF is a transcription factor that binds to the serum response element (SRE), a short sequence of dyad symmetry located 300 bp to the 5' of the site of transcription initiation of some genes (such as FOS). Together with MRTFA transcription coactivator, controls expression of genes regulating the cytoskeleton during development, morphogenesis and cell migration. The SRF-MRTFA complex activity responds to Rho GTPase-induced changes in cellular globular actin (G- actin) concentration, thereby coupling cytoskeletal gene expression to cytoskeletal dynamics. Required for cardiac differentiation and maturation. {ECO:0000250\|UniProtKB:Q9JM73}.


Subunit:		Binds DNA as a multimer, probably a dimer (PubMed:7637780). Interacts with MRTFA, forming the SRF-MRTFA nuclear complex which binds the 5'-CArG-3' consensus motif (CArG box) on DNA via SRF (PubMed:14565952, PubMed:19350017). Forms a nuclear ternary complex with MRTFA and SCAI (PubMed:19350017). Interacts with MRTFB (PubMed:14565952). Interacts with MLLT7/FOXO4, NKX3A and SSRP1 (PubMed:16054032). Interacts with ARID2 (By similarity). Interacts with SRFBP1 (By similarity). Interacts with FOXK1 (PubMed:17670796). Interacts with LPXN (PubMed:18497331). Interacts with OLFM2; the interaction promotes dissociation of SRF from the transcriptional repressor HEY2, facilitates binding of SRF to target genes and promotes smooth muscle differentiation (PubMed:25298399). {ECO:0000250\|UniProtKB:Q9JM73, ECO:0000269\|PubMed:14565952, ECO:0000269\|PubMed:16054032, ECO:0000269\|PubMed:17670796, ECO:0000269\|PubMed:18497331, ECO:0000269\|PubMed:19350017, ECO:0000269\|PubMed:25298399, ECO:0000269\|PubMed:7637780}.
Subcellular location:		Nucleus {ECO:0000255\|PROSITE-ProRule:PRU00251, ECO:0000269\|PubMed:19350017}.
Ptm:		Phosphorylated by PRKDC. {ECO:0000269\|PubMed:1547771, ECO:0000269\|PubMed:8375385, ECO:0000269\|PubMed:8407951}.