SRF
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1HBX, 1K6O, 1SRS
Identifiers
Aliases	SRF, MCM1, serum response factor
External IDs	OMIM: 600589 MGI: 106658 HomoloGene: 31135 GeneCards: SRF
Gene location (Human) Chr. Chromosome 6 (human)[1] Band 6p21.1 Start 43,171,269 bp[1] End 43,181,506 bp[1]
Gene location (Mouse) Chr. Chromosome 17 (mouse)[2] Band 17|17 C Start 46,859,255 bp[2] End 46,867,101 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in left uterine tube popliteal artery right coronary artery saphenous vein gastric mucosa thoracic aorta ascending aorta left ventricle left coronary artery myometrium Top expressed in lip superior frontal gyrus skeletal muscle tissue secondary oocyte yolk sac esophagus thymus digastric muscle ankle triceps brachii muscle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein dimerization activity DNA-binding transcription factor activity DNA-binding transcription activator activity, RNA polymerase II-specific RNA polymerase II general transcription initiation factor activity primary miRNA binding transcription factor binding RNA polymerase II cis-regulatory region sequence-specific DNA binding protein homodimerization activity serum response element binding chromatin binding protein binding DNA binding sequence-specific DNA binding transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding chromatin DNA binding transcription factor activity, RNA polymerase II core promoter proximal region sequence-specific binding cis-regulatory region sequence-specific DNA binding DNA-binding transcription factor activity, RNA polymerase II-specific histone deacetylase binding RNA polymerase II-specific DNA-binding transcription factor binding Cellular component cytoplasm nucleus nucleoplasm Biological process dorsal aorta morphogenesis bronchus cartilage development muscle cell cellular homeostasis lung smooth muscle development regulation of water loss via skin transcription by RNA polymerase II stress fiber assembly cell migration involved in sprouting angiogenesis platelet activation cardiac myofibril assembly heart looping cellular senescence face development regulation of cell adhesion long-term depression neuron projection development morphogenesis of an epithelial sheet positive regulation of filopodium assembly primitive streak formation cellular response to glucose stimulus negative regulation of cell population proliferation response to cytokine regulation of transcription, DNA-templated heart trabecula formation actin filament organization thymus development angiogenesis involved in wound healing platelet formation neuron development in utero embryonic development transcription, DNA-templated positive regulation of transcription, DNA-templated heart development positive regulation of cell differentiation branching involved in blood vessel morphogenesis positive regulation of axon extension positive regulation of smooth muscle contraction trachea cartilage development response to toxic substance positive regulation of pri-miRNA transcription by RNA polymerase II positive regulation of transcription by glucose regulation of smooth muscle cell differentiation epithelial structure maintenance associative learning skin morphogenesis positive regulation of DNA-binding transcription factor activity epithelial cell-cell adhesion neuron migration positive regulation of transcription initiation from RNA polymerase II promoter eyelid development in camera-type eye thyroid gland development negative regulation of amyloid-beta clearance negative regulation of cell migration developmental growth hematopoietic stem cell differentiation gastrulation trophectodermal cell differentiation positive thymic T cell selection response to hormone cell-matrix adhesion sarcomere organization actin cytoskeleton organization megakaryocyte development response to hypoxia lung morphogenesis mesoderm formation cardiac vascular smooth muscle cell differentiation mRNA transcription by RNA polymerase II multicellular organism development tangential migration from the subventricular zone to the olfactory bulb long-term memory contractile actin filament bundle assembly bicellular tight junction assembly leukocyte differentiation hippocampus development positive regulation of transcription by RNA polymerase II erythrocyte development negative regulation of pri-miRNA transcription by RNA polymerase II forebrain development cell-cell adhesion Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 6722 20807 Ensembl ENSG00000112658 ENSMUSG00000015605 UniProt P11831 Q9JM73 RefSeq (mRNA) NM_003131 NM_001292001 NM_020493 RefSeq (protein) NP_001278930 NP_003122 NP_003122.1 NP_065239 Location (UCSC) Chr 6: 43.17 – 43.18 Mb Chr 17: 46.86 – 46.87 Mb PubMed search [3] [4]
Wikidata
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Serum response factor, also known as SRF, is a transcription factor protein.^[5]

Function

Serum response factor is a member of the MADS (MCM1, Agamous, Deficiens, and SRF) box superfamily of transcription factors.^[6] This protein binds to the serum response element (SRE) in the promoter region of target genes. This protein regulates the activity of many immediate early genes, for example c-fos, and thereby participates in cell cycle regulation, apoptosis, cell growth, and cell differentiation. This gene is the downstream target of many pathways; for example, the mitogen-activated protein kinase pathway (MAPK) that acts through the ternary complex factors (TCFs).^[7][8]

SRF is important during the development of the embryo, as it has been linked to the formation of mesoderm.^[9][10] In the fully developed mammal, SRF is crucial for the growth of skeletal muscle.^[11] Interaction of SRF with other proteins, such as steroid hormone receptors, may contribute to regulation of muscle growth by steroids.^[12] Interaction of SRF with other proteins such as myocardin or Elk-1 may enhance or suppress expression of genes important for growth of vascular smooth muscle.

Clinical significance

Lack of skin SRF is associated with psoriasis and other skin diseases.^[13]

Interactions

Serum response factor has been shown to interact with: