SRF_HUMAN
ID SRF_HUMAN Reviewed; 508 AA.
AC P11831; Q5T648;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 228.
DE RecName: Full=Serum response factor;
DE Short=SRF;
GN Name=SRF;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=3203386; DOI=10.1016/0092-8674(88)90244-9;
RA Norman C., Runswick M., Pollock R., Treisman R.;
RT "Isolation and properties of cDNA clones encoding SRF, a transcription
RT factor that binds to the c-fos serum response element.";
RL Cell 55:989-1003(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Lymph;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 210-221 AND 253-264, AND PHOSPHORYLATION AT SER-253.
RX PubMed=8375385; DOI=10.1111/j.1432-1033.1993.tb18165.x;
RA Janknecht R., Ernst W.H., Houthaeve T., Nordheim A.;
RT "C-terminal phosphorylation of the serum-response factor.";
RL Eur. J. Biochem. 216:469-475(1993).
RN [6]
RP PHOSPHORYLATION AT SER-77; SER-79; SER-83; SER-85 AND SER-103.
RX PubMed=1547771; DOI=10.1002/j.1460-2075.1992.tb05143.x;
RA Janknecht R., Hipskind R.A., Houthaeve T., Nordheim A., Stunnenberg H.G.;
RT "Identification of multiple SRF N-terminal phosphorylation sites affecting
RT DNA binding properties.";
RL EMBO J. 11:1045-1054(1992).
RN [7]
RP GLYCOSYLATION AT SER-277; SER-307; SER-309; SER-316 AND SER-383.
RX PubMed=1512232; DOI=10.1016/s0021-9258(18)41871-6;
RA Reason A.J., Morris H.R., Panico M., Marais R., Treisman R.H.,
RA Haltiwanger R.S., Hart G.W., Kelly W.G., Dell A.;
RT "Localization of O-GlcNAc modification on the serum response transcription
RT factor.";
RL J. Biol. Chem. 267:16911-16921(1992).
RN [8]
RP PHOSPHORYLATION AT SER-435 AND SER-446.
RX PubMed=8407951; DOI=10.1016/s0021-9258(19)36904-2;
RA Liu S.-H., Ma J.-T., Yueh A.Y., Lees-Miller S.P., Anderson C.W., Ng S.-Y.;
RT "The carboxyl-terminal transactivation domain of human serum response
RT factor contains DNA-activated protein kinase phosphorylation sites.";
RL J. Biol. Chem. 268:21147-21154(1993).
RN [9]
RP INTERACTION WITH MRTFA AND MRTFB.
RC TISSUE=Cervix carcinoma;
RX PubMed=14565952; DOI=10.1074/jbc.m305679200;
RA Selvaraj A., Prywes R.;
RT "Megakaryoblastic leukemia-1/2, a transcriptional co-activator of serum
RT response factor, is required for skeletal myogenic differentiation.";
RL J. Biol. Chem. 278:41977-41987(2003).
RN [10]
RP INTERACTION WITH MLLT7.
RX PubMed=16054032; DOI=10.1016/j.devcel.2005.05.017;
RA Liu Z.-P., Wang Z., Yanagisawa H., Olson E.N.;
RT "Phenotypic modulation of smooth muscle cells through interaction of Foxo4
RT and myocardin.";
RL Dev. Cell 9:261-270(2005).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [12]
RP INTERACTION WITH FOXK1.
RX PubMed=17670796; DOI=10.1093/nar/gkm528;
RA Freddie C.T., Ji Z., Marais A., Sharrocks A.D.;
RT "Functional interactions between the Forkhead transcription factor FOXK1
RT and the MADS-box protein SRF.";
RL Nucleic Acids Res. 35:5203-5212(2007).
RN [13]
RP INTERACTION WITH LPXN.
RX PubMed=18497331; DOI=10.1161/circresaha.107.170357;
RA Sundberg-Smith L.J., DiMichele L.A., Sayers R.L., Mack C.P., Taylor J.M.;
RT "The LIM protein leupaxin is enriched in smooth muscle and functions as an
RT serum response factor cofactor to induce smooth muscle cell gene
RT transcription.";
RL Circ. Res. 102:1502-1511(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; SER-79; SER-83; SER-85
RP AND SER-224, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [15]
RP INTERACTION WITH MRTFA AND SCAI, AND SUBCELLULAR LOCATION.
RX PubMed=19350017; DOI=10.1038/ncb1862;
RA Brandt D.T., Baarlink C., Kitzing T.M., Kremmer E., Ivaska J., Nollau P.,
RA Grosse R.;
RT "SCAI acts as a suppressor of cancer cell invasion through the
RT transcriptional control of beta1-integrin.";
RL Nat. Cell Biol. 11:557-568(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [20]
RP INTERACTION WITH OLFM2.
RX PubMed=25298399; DOI=10.1091/mbc.e14-08-1255;
RA Shi N., Guo X., Chen S.Y.;
RT "Olfactomedin 2, a novel regulator for transforming growth factor-beta-
RT induced smooth muscle differentiation of human embryonic stem cell-derived
RT mesenchymal cells.";
RL Mol. Biol. Cell 25:4106-4114(2014).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 132-223, AND SUBUNIT.
RX PubMed=7637780; DOI=10.1038/376490a0;
RA Pellegrini L., Tan S., Richmond T.J.;
RT "Structure of serum response factor core bound to DNA.";
RL Nature 376:490-498(1995).
CC -!- FUNCTION: SRF is a transcription factor that binds to the serum
CC response element (SRE), a short sequence of dyad symmetry located 300
CC bp to the 5' of the site of transcription initiation of some genes
CC (such as FOS). Together with MRTFA transcription coactivator, controls
CC expression of genes regulating the cytoskeleton during development,
CC morphogenesis and cell migration. The SRF-MRTFA complex activity
CC responds to Rho GTPase-induced changes in cellular globular actin (G-
CC actin) concentration, thereby coupling cytoskeletal gene expression to
CC cytoskeletal dynamics. Required for cardiac differentiation and
CC maturation. {ECO:0000250|UniProtKB:Q9JM73}.
CC -!- SUBUNIT: Binds DNA as a multimer, probably a dimer (PubMed:7637780).
CC Interacts with MRTFA, forming the SRF-MRTFA nuclear complex which binds
CC the 5'-CArG-3' consensus motif (CArG box) on DNA via SRF
CC (PubMed:14565952, PubMed:19350017). Forms a nuclear ternary complex
CC with MRTFA and SCAI (PubMed:19350017). Interacts with MRTFB
CC (PubMed:14565952). Interacts with MLLT7/FOXO4, NKX3A and SSRP1
CC (PubMed:16054032). Interacts with ARID2 (By similarity). Interacts with
CC SRFBP1 (By similarity). Interacts with FOXK1 (PubMed:17670796).
CC Interacts with LPXN (PubMed:18497331). Interacts with OLFM2; the
CC interaction promotes dissociation of SRF from the transcriptional
CC repressor HEY2, facilitates binding of SRF to target genes and promotes
CC smooth muscle differentiation (PubMed:25298399). Interacts with NKX3-1
CC (By similarity). Interacts with KAT5 (By similarity).
CC {ECO:0000250|UniProtKB:Q9JM73, ECO:0000269|PubMed:14565952,
CC ECO:0000269|PubMed:16054032, ECO:0000269|PubMed:17670796,
CC ECO:0000269|PubMed:18497331, ECO:0000269|PubMed:19350017,
CC ECO:0000269|PubMed:25298399, ECO:0000269|PubMed:7637780}.
CC -!- INTERACTION:
CC P11831; P35269: GTF2F1; NbExp=2; IntAct=EBI-493034, EBI-457886;
CC P11831; Q969V6: MRTFA; NbExp=2; IntAct=EBI-493034, EBI-493122;
CC P11831; Q9ULH7: MRTFB; NbExp=3; IntAct=EBI-493034, EBI-493007;
CC P11831; Q8IZQ8: MYOCD; NbExp=2; IntAct=EBI-493034, EBI-493384;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00251,
CC ECO:0000269|PubMed:19350017}.
CC -!- PTM: Phosphorylated by PRKDC. {ECO:0000269|PubMed:1547771,
CC ECO:0000269|PubMed:8375385, ECO:0000269|PubMed:8407951}.
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DR EMBL; J03161; AAA36647.1; -; mRNA.
DR EMBL; AL133375; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL355385; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX04161.1; -; Genomic_DNA.
DR EMBL; BC048211; AAH48211.1; -; mRNA.
DR EMBL; BC052572; AAH52572.1; -; mRNA.
DR CCDS; CCDS4889.1; -.
DR PIR; A31637; A31637.
DR RefSeq; NP_001278930.1; NM_001292001.1.
DR RefSeq; NP_003122.1; NM_003131.3.
DR PDB; 1HBX; X-ray; 3.15 A; A/B/D/E=132-223.
DR PDB; 1K6O; X-ray; 3.19 A; B/C=133-235.
DR PDB; 1SRS; X-ray; 3.20 A; A/B=132-223.
DR PDBsum; 1HBX; -.
DR PDBsum; 1K6O; -.
DR PDBsum; 1SRS; -.
DR AlphaFoldDB; P11831; -.
DR SMR; P11831; -.
DR BioGRID; 112600; 67.
DR CORUM; P11831; -.
DR DIP; DIP-49N; -.
DR ELM; P11831; -.
DR IntAct; P11831; 59.
DR MINT; P11831; -.
DR STRING; 9606.ENSP00000265354; -.
DR ChEMBL; CHEMBL4523184; -.
DR GlyConnect; 561; 1 O-Linked glycan (2 sites).
DR GlyGen; P11831; 15 sites, 1 O-linked glycan (12 sites).
DR iPTMnet; P11831; -.
DR PhosphoSitePlus; P11831; -.
DR BioMuta; SRF; -.
DR DMDM; 134876; -.
DR CPTAC; CPTAC-1727; -.
DR CPTAC; CPTAC-1764; -.
DR EPD; P11831; -.
DR jPOST; P11831; -.
DR MassIVE; P11831; -.
DR MaxQB; P11831; -.
DR PaxDb; P11831; -.
DR PeptideAtlas; P11831; -.
DR PRIDE; P11831; -.
DR ProteomicsDB; 52806; -.
DR Antibodypedia; 900; 713 antibodies from 41 providers.
DR DNASU; 6722; -.
DR Ensembl; ENST00000265354.6; ENSP00000265354.4; ENSG00000112658.8.
DR GeneID; 6722; -.
DR KEGG; hsa:6722; -.
DR MANE-Select; ENST00000265354.6; ENSP00000265354.4; NM_003131.4; NP_003122.1.
DR UCSC; uc003oui.4; human.
DR CTD; 6722; -.
DR DisGeNET; 6722; -.
DR GeneCards; SRF; -.
DR HGNC; HGNC:11291; SRF.
DR HPA; ENSG00000112658; Low tissue specificity.
DR MIM; 600589; gene.
DR neXtProt; NX_P11831; -.
DR OpenTargets; ENSG00000112658; -.
DR PharmGKB; PA36116; -.
DR VEuPathDB; HostDB:ENSG00000112658; -.
DR eggNOG; KOG0015; Eukaryota.
DR GeneTree; ENSGT00400000022158; -.
DR HOGENOM; CLU_042048_1_0_1; -.
DR InParanoid; P11831; -.
DR OMA; SHAVMYA; -.
DR OrthoDB; 1125296at2759; -.
DR PhylomeDB; P11831; -.
DR TreeFam; TF318482; -.
DR PathwayCommons; P11831; -.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-9031628; NGF-stimulated transcription.
DR Reactome; R-HSA-9634638; Estrogen-dependent nuclear events downstream of ESR-membrane signaling.
DR SignaLink; P11831; -.
DR SIGNOR; P11831; -.
DR BioGRID-ORCS; 6722; 392 hits in 1111 CRISPR screens.
DR ChiTaRS; SRF; human.
DR EvolutionaryTrace; P11831; -.
DR GeneWiki; Serum_response_factor; -.
DR GenomeRNAi; 6722; -.
DR Pharos; P11831; Tbio.
DR PRO; PR:P11831; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P11831; protein.
DR Bgee; ENSG00000112658; Expressed in lower esophagus muscularis layer and 202 other tissues.
DR ExpressionAtlas; P11831; baseline and differential.
DR Genevisible; P11831; HS.
DR GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; TAS:BHF-UCL.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0031490; F:chromatin DNA binding; IEA:Ensembl.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:BHF-UCL.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl.
DR GO; GO:0070878; F:primary miRNA binding; ISS:BHF-UCL.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:GO_Central.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IEA:Ensembl.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0010736; F:serum response element binding; IDA:ARUK-UCL.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0060055; P:angiogenesis involved in wound healing; TAS:BHF-UCL.
DR GO; GO:0008306; P:associative learning; IEA:Ensembl.
DR GO; GO:0048675; P:axon extension; IEA:Ensembl.
DR GO; GO:0070830; P:bicellular tight junction assembly; IEA:Ensembl.
DR GO; GO:0001569; P:branching involved in blood vessel morphogenesis; IEA:Ensembl.
DR GO; GO:0060532; P:bronchus cartilage development; IEA:Ensembl.
DR GO; GO:0060379; P:cardiac muscle cell myoblast differentiation; IGI:BHF-UCL.
DR GO; GO:0055003; P:cardiac myofibril assembly; IEA:Ensembl.
DR GO; GO:0060947; P:cardiac vascular smooth muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; IMP:BHF-UCL.
DR GO; GO:0007160; P:cell-matrix adhesion; IEA:Ensembl.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
DR GO; GO:0090398; P:cellular senescence; IMP:BHF-UCL.
DR GO; GO:0035912; P:dorsal aorta morphogenesis; IEA:Ensembl.
DR GO; GO:0090136; P:epithelial cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0010669; P:epithelial structure maintenance; IEA:Ensembl.
DR GO; GO:0048821; P:erythrocyte development; IEA:Ensembl.
DR GO; GO:0061029; P:eyelid development in camera-type eye; IEA:Ensembl.
DR GO; GO:0060324; P:face development; IEA:Ensembl.
DR GO; GO:0046847; P:filopodium assembly; IEA:Ensembl.
DR GO; GO:0007507; P:heart development; ISS:BHF-UCL.
DR GO; GO:0001947; P:heart looping; ISS:BHF-UCL.
DR GO; GO:0060347; P:heart trabecula formation; IEA:Ensembl.
DR GO; GO:0060218; P:hematopoietic stem cell differentiation; IEA:Ensembl.
DR GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
DR GO; GO:0007616; P:long-term memory; IEA:Ensembl.
DR GO; GO:0060292; P:long-term synaptic depression; IEA:Ensembl.
DR GO; GO:0060425; P:lung morphogenesis; IEA:Ensembl.
DR GO; GO:0061145; P:lung smooth muscle development; IEA:Ensembl.
DR GO; GO:0035855; P:megakaryocyte development; IEA:Ensembl.
DR GO; GO:0001707; P:mesoderm formation; IEA:Ensembl.
DR GO; GO:0002011; P:morphogenesis of an epithelial sheet; IEA:Ensembl.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; ISS:BHF-UCL.
DR GO; GO:1900222; P:negative regulation of amyloid-beta clearance; IMP:BHF-UCL.
DR GO; GO:0030336; P:negative regulation of cell migration; IEA:Ensembl.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:1902894; P:negative regulation of miRNA transcription; ISS:BHF-UCL.
DR GO; GO:0048666; P:neuron development; TAS:BHF-UCL.
DR GO; GO:0001764; P:neuron migration; IEA:Ensembl.
DR GO; GO:0030168; P:platelet activation; IEA:Ensembl.
DR GO; GO:0030220; P:platelet formation; IEA:Ensembl.
DR GO; GO:0045773; P:positive regulation of axon extension; IEA:Ensembl.
DR GO; GO:0045597; P:positive regulation of cell differentiation; IDA:MGI.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:BHF-UCL.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; IEA:Ensembl.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; IGI:ARUK-UCL.
DR GO; GO:0045987; P:positive regulation of smooth muscle contraction; IDA:BHF-UCL.
DR GO; GO:0046016; P:positive regulation of transcription by glucose; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IDA:BHF-UCL.
DR GO; GO:0010735; P:positive regulation of transcription via serum response element binding; IEA:Ensembl.
DR GO; GO:0045059; P:positive thymic T cell selection; IEA:Ensembl.
DR GO; GO:0090009; P:primitive streak formation; IEA:Ensembl.
DR GO; GO:0030155; P:regulation of cell adhesion; IEA:Ensembl.
DR GO; GO:0051150; P:regulation of smooth muscle cell differentiation; TAS:BHF-UCL.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0033561; P:regulation of water loss via skin; IEA:Ensembl.
DR GO; GO:0034097; P:response to cytokine; IMP:BHF-UCL.
DR GO; GO:0009725; P:response to hormone; IDA:BHF-UCL.
DR GO; GO:0001666; P:response to hypoxia; IEP:BHF-UCL.
DR GO; GO:0009636; P:response to toxic substance; TAS:BHF-UCL.
DR GO; GO:0045214; P:sarcomere organization; IEA:Ensembl.
DR GO; GO:0043589; P:skin morphogenesis; IEA:Ensembl.
DR GO; GO:0043149; P:stress fiber assembly; IEA:Ensembl.
DR GO; GO:0022028; P:tangential migration from the subventricular zone to the olfactory bulb; IEA:Ensembl.
DR GO; GO:0048538; P:thymus development; IEA:Ensembl.
DR GO; GO:0030878; P:thyroid gland development; IEA:Ensembl.
DR GO; GO:0060534; P:trachea cartilage development; IEA:Ensembl.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0001829; P:trophectodermal cell differentiation; IDA:MGI.
DR CDD; cd00266; MADS_SRF_like; 1.
DR Gene3D; 3.40.1810.10; -; 1.
DR IDEAL; IID00140; -.
DR InterPro; IPR033897; MADS_SRF-like.
DR InterPro; IPR002100; TF_MADSbox.
DR InterPro; IPR036879; TF_MADSbox_sf.
DR Pfam; PF00319; SRF-TF; 1.
DR PRINTS; PR00404; MADSDOMAIN.
DR SMART; SM00432; MADS; 1.
DR SUPFAM; SSF55455; SSF55455; 1.
DR PROSITE; PS00350; MADS_BOX_1; 1.
DR PROSITE; PS50066; MADS_BOX_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Developmental protein; Direct protein sequencing;
KW DNA-binding; Glycoprotein; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..508
FT /note="Serum response factor"
FT /id="PRO_0000199423"
FT DOMAIN 141..201
FT /note="MADS-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00251"
FT DNA_BIND 133..222
FT REGION 1..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..222
FT /note="Involved in dimerization"
FT REGION 219..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:1547771,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:1547771,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:1547771,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:1547771,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:1547771"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8375385"
FT MOD_RES 435
FT /note="Phosphoserine; by dsDNA kinase"
FT /evidence="ECO:0000269|PubMed:8407951"
FT MOD_RES 446
FT /note="Phosphoserine; by dsDNA kinase"
FT /evidence="ECO:0000269|PubMed:8407951"
FT CARBOHYD 277
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000269|PubMed:1512232"
FT /id="CAR_000181"
FT CARBOHYD 307
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000305|PubMed:1512232"
FT CARBOHYD 309
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000305|PubMed:1512232"
FT CARBOHYD 316
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000269|PubMed:1512232"
FT /id="CAR_000196"
FT CARBOHYD 383
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000305|PubMed:1512232"
FT HELIX 154..179
FT /evidence="ECO:0007829|PDB:1HBX"
FT STRAND 182..188
FT /evidence="ECO:0007829|PDB:1HBX"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:1K6O"
FT STRAND 194..198
FT /evidence="ECO:0007829|PDB:1HBX"
FT HELIX 200..205
FT /evidence="ECO:0007829|PDB:1HBX"
FT HELIX 209..220
FT /evidence="ECO:0007829|PDB:1HBX"
SQ SEQUENCE 508 AA; 51593 MW; 25505828D3276F44 CRC64;
MLPTQAGAAA ALGRGSALGG SLNRTPTGRP GGGGGTRGAN GGRVPGNGAG LGPGRLEREA
AAAAATTPAP TAGALYSGSE GDSESGEEEE LGAERRGLKR SLSEMEIGMV VGGPEASAAA
TGGYGPVSGA VSGAKPGKKT RGRVKIKMEF IDNKLRRYTT FSKRKTGIMK KAYELSTLTG
TQVLLLVASE TGHVYTFATR KLQPMITSET GKALIQTCLN SPDSPPRSDP TTDQRMSATG
FEETDLTYQV SESDSSGETK DTLKPAFTVT NLPGTTSTIQ TAPSTSTTMQ VSSGPSFPIT
NYLAPVSASV SPSAVSSANG TVLKSTGSGP VSSGGLMQLP TSFTLMPGGA VAQQVPVQAI
QVHQAPQQAS PSRDSSTDLT QTSSSGTVTL PATIMTSSVP TTVGGHMMYP SPHAVMYAPT
SGLGDGSLTV LNAFSQAPST MQVSHSQVQE PGGVPQVFLT ASSGTVQIPV SAVQLHQMAV
IGQQAGSSSN LTELQVVNLD TAHSTKSE
