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Serum response factor (SRF)

 SRF_MOUSE               Reviewed;         504 AA.
Q9JM73;
11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
07-NOV-2018, entry version 142.
RecName: Full=Serum response factor;
Short=SRF;
Name=Srf;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Miwa T.;
"Serum response factor.";
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
FUNCTION, AND INTERACTION WITH MRTFA.
PubMed=12732141;
Miralles F., Posern G., Zaromytidou A.I., Treisman R.;
"Actin dynamics control SRF activity by regulation of its coactivator
MAL.";
Cell 113:329-342(2003).
[4]
INTERACTION WITH SRFBP1, AND SUBUNIT.
PubMed=15492011; DOI=10.1074/jbc.M405945200;
Zhang X., Azhar G., Zhong Y., Wei J.Y.;
"Identification of a novel serum response factor cofactor in cardiac
gene regulation.";
J. Biol. Chem. 279:55626-55632(2004).
[5]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=15169892; DOI=10.1128/MCB.24.12.5281-5289.2004;
Parlakian A., Tuil D., Hamard G., Tavernier G., Hentzen D.,
Concordet J.-P., Paulin D., Li Z., Daegelen D.;
"Targeted inactivation of serum response factor in the developing
heart results in myocardial defects and embryonic lethality.";
Mol. Cell. Biol. 24:5281-5289(2004).
[6]
INTERACTION WITH ARID2, AND SUBUNIT.
PubMed=16782067; DOI=10.1016/j.bbrc.2006.05.211;
Zhang X., Azhar G., Zhong Y., Wei J.Y.;
"Zipzap/p200 is a novel zinc finger protein contributing to cardiac
gene regulation.";
Biochem. Biophys. Res. Commun. 346:794-801(2006).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[9]
FUNCTION, INTERACTION WITH MRTFA AND SCAI, AND SUBCELLULAR LOCATION.
PubMed=19350017; DOI=10.1038/ncb1862;
Brandt D.T., Baarlink C., Kitzing T.M., Kremmer E., Ivaska J.,
Nollau P., Grosse R.;
"SCAI acts as a suppressor of cancer cell invasion through the
transcriptional control of beta1-integrin.";
Nat. Cell Biol. 11:557-568(2009).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[11]
FUNCTION.
PubMed=24732378; DOI=10.1101/gad.239327.114;
Esnault C., Stewart A., Gualdrini F., East P., Horswell S.,
Matthews N., Treisman R.;
"Rho-actin signaling to the MRTF coactivators dominates the immediate
transcriptional response to serum in fibroblasts.";
Genes Dev. 28:943-958(2014).
-!- 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) (PubMed:24732378). Together with MRTFA
transcription coactivator, controls expression of genes regulating
the cytoskeleton during development, morphogenesis and cell
migration (PubMed:12732141, PubMed:19350017, PubMed:24732378). 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
(PubMed:24732378). Required for cardiac differentiation and
maturation (PubMed:15169892). {ECO:0000269|PubMed:12732141,
ECO:0000269|PubMed:15169892, ECO:0000269|PubMed:19350017,
ECO:0000269|PubMed:24732378}.
-!- SUBUNIT: Binds DNA as a multimer, probably a dimer
(PubMed:15492011, PubMed:16782067). Interacts with MRTFA, forming
the SRF-MRTFA nuclear complex which binds the 5'-CArG-3' consensus
motif (CArG box) on DNA via SRF (PubMed:12732141,
PubMed:19350017). Forms a nuclear ternary complex with MRTFA and
SCAI (PubMed:19350017). Interacts with MRTFB (By similarity).
Interacts with MLLT7/FOXO4, NKX3A and SSRP1 (By similarity).
Interacts with ARID2 (PubMed:16782067). Interacts with SRFBP1
(PubMed:15492011). Interacts with LPXN (By similarity). 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 (By
similarity). {ECO:0000250|UniProtKB:P11831,
ECO:0000269|PubMed:12732141, ECO:0000269|PubMed:15492011,
ECO:0000269|PubMed:16782067, ECO:0000269|PubMed:19350017}.
-!- INTERACTION:
Q3U1N2:Srebf2; NbExp=3; IntAct=EBI-493266, EBI-645275;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00251, ECO:0000269|PubMed:19350017}.
-!- PTM: Phosphorylated by PRKDC. {ECO:0000250|UniProtKB:P11831}.
-!- DISRUPTION PHENOTYPE: Mice lacking Srf in cardiac tissue display
lethal cardiac defects between E10.5 and E13.5 characterized by
abnormally thin myocardium, dilated cardiac chambers, poor
trabeculation and a disorganised interventricular septum.
{ECO:0000269|PubMed:15169892}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AB038376; BAA92314.1; -; Genomic_DNA.
EMBL; BC051950; AAH51950.1; -; mRNA.
CCDS; CCDS28831.1; -.
RefSeq; NP_065239.1; NM_020493.2.
UniGene; Mm.45044; -.
ProteinModelPortal; Q9JM73; -.
SMR; Q9JM73; -.
BioGrid; 203497; 6.
CORUM; Q9JM73; -.
DIP; DIP-49624N; -.
IntAct; Q9JM73; 4.
STRING; 10090.ENSMUSP00000015749; -.
iPTMnet; Q9JM73; -.
PhosphoSitePlus; Q9JM73; -.
MaxQB; Q9JM73; -.
PaxDb; Q9JM73; -.
PeptideAtlas; Q9JM73; -.
PRIDE; Q9JM73; -.
Ensembl; ENSMUST00000015749; ENSMUSP00000015749; ENSMUSG00000015605.
GeneID; 20807; -.
KEGG; mmu:20807; -.
UCSC; uc008ctg.1; mouse.
CTD; 6722; -.
MGI; MGI:106658; Srf.
eggNOG; KOG0015; Eukaryota.
eggNOG; COG5068; LUCA.
GeneTree; ENSGT00400000022158; -.
HOGENOM; HOG000012380; -.
HOVERGEN; HBG014968; -.
InParanoid; Q9JM73; -.
KO; K04378; -.
OMA; TSTSMQV; -.
OrthoDB; EOG091G0X24; -.
PhylomeDB; Q9JM73; -.
TreeFam; TF318482; -.
Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
PRO; PR:Q9JM73; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000015605; Expressed in 287 organ(s), highest expression level in ascending aorta.
CleanEx; MM_SRF; -.
Genevisible; Q9JM73; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0031490; F:chromatin DNA binding; IDA:MGI.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:BHF-UCL.
GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
GO; GO:0070878; F:primary miRNA binding; IDA:BHF-UCL.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0001077; F:proximal promoter DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:BHF-UCL.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:BHF-UCL.
GO; GO:0061629; F:RNA polymerase II sequence-specific DNA-binding transcription factor binding; IPI:BHF-UCL.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
GO; GO:0010736; F:serum response element binding; IDA:UniProtKB.
GO; GO:0000983; F:transcription factor activity, RNA polymerase II core promoter sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0003705; F:transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding; IDA:MGI.
GO; GO:0000982; F:transcription factor activity, RNA polymerase II proximal promoter sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0008134; F:transcription factor binding; ISO:MGI.
GO; GO:0044212; F:transcription regulatory region DNA binding; IBA:GO_Central.
GO; GO:0030036; P:actin cytoskeleton organization; IDA:UniProtKB.
GO; GO:0007015; P:actin filament organization; IMP:MGI.
GO; GO:0008306; P:associative learning; IMP:MGI.
GO; GO:0070830; P:bicellular tight junction assembly; IMP:MGI.
GO; GO:0001569; P:branching involved in blood vessel morphogenesis; IMP:MGI.
GO; GO:0060532; P:bronchus cartilage development; IMP:MGI.
GO; GO:0055003; P:cardiac myofibril assembly; IMP:MGI.
GO; GO:0060947; P:cardiac vascular smooth muscle cell differentiation; IMP:MGI.
GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; IMP:MGI.
GO; GO:0098609; P:cell-cell adhesion; IMP:MGI.
GO; GO:0007160; P:cell-matrix adhesion; IMP:MGI.
GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
GO; GO:0090398; P:cellular senescence; ISO:MGI.
GO; GO:0030038; P:contractile actin filament bundle assembly; IMP:MGI.
GO; GO:0048589; P:developmental growth; IMP:MGI.
GO; GO:0035912; P:dorsal aorta morphogenesis; IMP:MGI.
GO; GO:0090136; P:epithelial cell-cell adhesion; IMP:MGI.
GO; GO:0010669; P:epithelial structure maintenance; IMP:MGI.
GO; GO:0048821; P:erythrocyte development; IMP:MGI.
GO; GO:0061029; P:eyelid development in camera-type eye; IMP:MGI.
GO; GO:0060324; P:face development; IMP:MGI.
GO; GO:0030900; P:forebrain development; IMP:MGI.
GO; GO:0007369; P:gastrulation; IMP:MGI.
GO; GO:0007507; P:heart development; IMP:MGI.
GO; GO:0001947; P:heart looping; IMP:MGI.
GO; GO:0060347; P:heart trabecula formation; IMP:MGI.
GO; GO:0060218; P:hematopoietic stem cell differentiation; IMP:MGI.
GO; GO:0021766; P:hippocampus development; IMP:MGI.
GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
GO; GO:0002521; P:leukocyte differentiation; IMP:MGI.
GO; GO:0007616; P:long-term memory; ISO:MGI.
GO; GO:0060292; P:long-term synaptic depression; IMP:MGI.
GO; GO:0060425; P:lung morphogenesis; IMP:MGI.
GO; GO:0061145; P:lung smooth muscle development; IMP:MGI.
GO; GO:0035855; P:megakaryocyte development; IMP:MGI.
GO; GO:0001707; P:mesoderm formation; IMP:MGI.
GO; GO:0002011; P:morphogenesis of an epithelial sheet; IMP:MGI.
GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IDA:BHF-UCL.
GO; GO:0007275; P:multicellular organism development; IBA:GO_Central.
GO; GO:0046716; P:muscle cell cellular homeostasis; IMP:MGI.
GO; GO:1900222; P:negative regulation of amyloid-beta clearance; ISO:MGI.
GO; GO:0030336; P:negative regulation of cell migration; ISO:MGI.
GO; GO:0008285; P:negative regulation of cell proliferation; ISO:MGI.
GO; GO:1902894; P:negative regulation of pri-miRNA transcription by RNA polymerase II; IDA:BHF-UCL.
GO; GO:0001764; P:neuron migration; IMP:MGI.
GO; GO:0031175; P:neuron projection development; IMP:MGI.
GO; GO:0030168; P:platelet activation; IMP:MGI.
GO; GO:0030220; P:platelet formation; IMP:MGI.
GO; GO:0045773; P:positive regulation of axon extension; IMP:MGI.
GO; GO:0045597; P:positive regulation of cell differentiation; ISO:MGI.
GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISO:MGI.
GO; GO:0051491; P:positive regulation of filopodium assembly; IMP:MGI.
GO; GO:1902895; P:positive regulation of pri-miRNA transcription by RNA polymerase II; IDA:BHF-UCL.
GO; GO:0045987; P:positive regulation of smooth muscle contraction; ISO:MGI.
GO; GO:0046016; P:positive regulation of transcription by glucose; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
GO; GO:0003257; P:positive regulation of transcription from RNA polymerase II promoter involved in myocardial precursor cell differentiation; IMP:BHF-UCL.
GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; ISO:MGI.
GO; GO:0010735; P:positive regulation of transcription via serum response element binding; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0045059; P:positive thymic T cell selection; IMP:MGI.
GO; GO:0090009; P:primitive streak formation; IMP:MGI.
GO; GO:0030155; P:regulation of cell adhesion; IMP:MGI.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0033561; P:regulation of water loss via skin; IMP:MGI.
GO; GO:0034097; P:response to cytokine; ISO:MGI.
GO; GO:0009725; P:response to hormone; ISO:MGI.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0045214; P:sarcomere organization; IMP:MGI.
GO; GO:0043589; P:skin morphogenesis; IMP:MGI.
GO; GO:0043149; P:stress fiber assembly; IMP:MGI.
GO; GO:0022028; P:tangential migration from the subventricular zone to the olfactory bulb; IMP:MGI.
GO; GO:0048538; P:thymus development; IMP:MGI.
GO; GO:0030878; P:thyroid gland development; IMP:MGI.
GO; GO:0060534; P:trachea cartilage development; IMP:MGI.
GO; GO:0006366; P:transcription by RNA polymerase II; ISO:MGI.
GO; GO:0001829; P:trophectodermal cell differentiation; ISO:MGI.
CDD; cd00266; MADS_SRF_like; 1.
Gene3D; 3.40.1810.10; -; 1.
InterPro; IPR033897; MADS_SRF-like.
InterPro; IPR002100; TF_MADSbox.
InterPro; IPR036879; TF_MADSbox_sf.
Pfam; PF00319; SRF-TF; 1.
PRINTS; PR00404; MADSDOMAIN.
SMART; SM00432; MADS; 1.
SUPFAM; SSF55455; SSF55455; 1.
PROSITE; PS00350; MADS_BOX_1; 1.
PROSITE; PS50066; MADS_BOX_2; 1.
1: Evidence at protein level;
Activator; Complete proteome; Developmental protein; DNA-binding;
Glycoprotein; Nucleus; Phosphoprotein; Reference proteome;
Transcription; Transcription regulation.
CHAIN 1 504 Serum response factor.
/FTId=PRO_0000245225.
DOMAIN 137 197 MADS-box. {ECO:0000255|PROSITE-
ProRule:PRU00251}.
DNA_BIND 129 218 {ECO:0000250}.
REGION 164 218 Involved in dimerization. {ECO:0000250}.
COMPBIAS 13 138 Gly-rich.
COMPBIAS 76 86 Asp/Glu-rich (acidic).
COMPBIAS 238 254 Asp/Glu-rich (acidic).
MOD_RES 73 73 Phosphoserine.
{ECO:0000250|UniProtKB:P11831}.
MOD_RES 75 75 Phosphoserine.
{ECO:0000250|UniProtKB:P11831}.
MOD_RES 79 79 Phosphoserine.
{ECO:0000250|UniProtKB:P11831}.
MOD_RES 81 81 Phosphoserine.
{ECO:0000250|UniProtKB:P11831}.
MOD_RES 99 99 Phosphoserine.
{ECO:0000250|UniProtKB:P11831}.
MOD_RES 220 220 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:21183079}.
MOD_RES 249 249 Phosphoserine.
{ECO:0000250|UniProtKB:P11831}.
MOD_RES 431 431 Phosphoserine; by dsDNA kinase.
{ECO:0000250|UniProtKB:P11831}.
MOD_RES 442 442 Phosphoserine; by dsDNA kinase.
{ECO:0000250|UniProtKB:P11831}.
CARBOHYD 273 273 O-linked (GlcNAc) serine. {ECO:0000250}.
CARBOHYD 303 303 O-linked (GlcNAc) serine. {ECO:0000250}.
CARBOHYD 305 305 O-linked (GlcNAc) serine. {ECO:0000250}.
CARBOHYD 312 312 O-linked (GlcNAc) serine. {ECO:0000250}.
CARBOHYD 379 379 O-linked (GlcNAc) serine. {ECO:0000250}.
SEQUENCE 504 AA; 51247 MW; 26353F18A2B46F6B CRC64;
MLPSQAGAAA ALGRGSALGG NLNRTPTGRP GGGGGTRGAN GGRVPGNGAG LGQSRLEREA
AAAAAPTAGA LYSGSEGDSE SGEEEELGAE RRGLKRSLSE MELGVVVGGP EAAAAAAGGY
GPVSGAVSGA KPGKKTRGRV KIKMEFIDNK LRRYTTFSKR KTGIMKKAYE LSTLTGTQVL
LLVASETGHV YTFATRKLQP MITSETGKAL IQTCLNSPDS PPRSDPTTDQ RMSATGFEEP
DLTYQVSESD SSGETKDTLK PAFTVTNLPG TTSTIQTAPS TSTTMQVSSG PSFPITNYLA
PVSASVSPSA VSSANGTVLK STGSGPVSSG GLMQLPTSFT LMPGGAVAQQ VPVQAIHVHQ
APQQASPSRD SSTDLTQTSS SGTVTLPATI MTSSVPTTVG GHMMYPSPHA VMYAPTSGLA
DGSLTVLNAF SQAPSTMQVS HSQVQEPGGV PQVFLTAPSG TVQIPVSAVQ LHQMAVIGQQ
AGSSSNLTEL QVVNLDATHS TKSE


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