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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.
25-OCT-2017, entry version 134.
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]
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).
[4]
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).
[5]
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).
[6]
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).
[7]
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).
[8]
INTERACTION WITH MKL1 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).
[9]
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).
-!- 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) (By similarity). Required for cardiac
differentiation and maturation. {ECO:0000250}.
-!- SUBUNIT: Binds DNA as a multimer, probably a dimer. Interacts with
MLLT7/FOXO4, NKX3A and SSRP1 (By similarity). Interacts with ARID2
(PubMed:16782067). Interacts with SRFBP1 (PubMed:15492011). Forms
complexes with ARID2, MYOCD, NKX2-5 and SRFBP1. Forms a nuclear
ternary complex with MKL1 and SCAI (PubMed:19350017). 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: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}.
-!- 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-NoDerivs 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.
MINT; MINT-1739318; -.
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; NAFPQAP; -.
OrthoDB; EOG091G0X24; -.
PhylomeDB; Q9JM73; -.
TreeFam; TF318482; -.
Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
PRO; PR:Q9JM73; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000015605; -.
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:0042826; F:histone deacetylase binding; IEA:Ensembl.
GO; GO:0070878; F:primary miRNA binding; IDA:BHF-UCL.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:BHF-UCL.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
GO; GO:0010736; F:serum response element binding; IDA:MGI.
GO; GO:0000983; F:transcription factor activity, RNA polymerase II core promoter sequence-specific; IEA:Ensembl.
GO; GO:0003705; F:transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding; IDA:MGI.
GO; GO:0001076; F:transcription factor activity, RNA polymerase II transcription factor binding; IDA:BHF-UCL.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:MGI.
GO; GO:0008134; F:transcription factor binding; ISO:MGI.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:BHF-UCL.
GO; GO:0001228; F:transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding; IDA:BHF-UCL.
GO; GO:0030036; P:actin cytoskeleton organization; IMP:MGI.
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:0060292; P:long term synaptic depression; IMP:MGI.
GO; GO:0007616; P:long-term memory; IEA:Ensembl.
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 from RNA polymerase II promoter; IDA:BHF-UCL.
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; IEA:Ensembl.
GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl.
GO; GO:1902894; P:negative regulation of pri-miRNA transcription from RNA polymerase II promoter; 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:0051491; P:positive regulation of filopodium assembly; IMP:MGI.
GO; GO:1902895; P:positive regulation of pri-miRNA transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; ISO:MGI.
GO; GO:0045987; P:positive regulation of smooth muscle contraction; ISO:MGI.
GO; GO:0046016; P:positive regulation of transcription by glucose; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; 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; ISO:MGI.
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 from RNA polymerase II promoter; 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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