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Serum response factor (SRF)

 SRF_HUMAN               Reviewed;         508 AA.
P11831; Q5T648;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
01-OCT-1989, sequence version 1.
30-AUG-2017, entry version 195.
RecName: Full=Serum response factor;
Short=SRF;
Name=SRF;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=3203386; DOI=10.1016/0092-8674(88)90244-9;
Norman C., Runswick M., Pollock R., Treisman R.;
"Isolation and properties of cDNA clones encoding SRF, a transcription
factor that binds to the c-fos serum response element.";
Cell 55:989-1003(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung, and Lymph;
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).
[5]
PROTEIN SEQUENCE OF 210-221 AND 253-264, AND PHOSPHORYLATION AT
SER-253.
PubMed=8375385; DOI=10.1111/j.1432-1033.1993.tb18165.x;
Janknecht R., Ernst W.H., Houthaeve T., Nordheim A.;
"C-terminal phosphorylation of the serum-response factor.";
Eur. J. Biochem. 216:469-475(1993).
[6]
PHOSPHORYLATION AT SER-77; SER-79; SER-83; SER-85 AND SER-103.
PubMed=1547771;
Janknecht R., Hipskind R.A., Houthaeve T., Nordheim A.,
Stunnenberg H.G.;
"Identification of multiple SRF N-terminal phosphorylation sites
affecting DNA binding properties.";
EMBO J. 11:1045-1054(1992).
[7]
GLYCOSYLATION AT SER-277; SER-307; SER-309; SER-316 AND SER-383.
PubMed=1512232;
Reason A.J., Morris H.R., Panico M., Marais R., Treisman R.H.,
Haltiwanger R.S., Hart G.W., Kelly W.G., Dell A.;
"Localization of O-GlcNAc modification on the serum response
transcription factor.";
J. Biol. Chem. 267:16911-16921(1992).
[8]
PHOSPHORYLATION AT SER-435 AND SER-446.
PubMed=8407951;
Liu S.-H., Ma J.-T., Yueh A.Y., Lees-Miller S.P., Anderson C.W.,
Ng S.-Y.;
"The carboxyl-terminal transactivation domain of human serum response
factor contains DNA-activated protein kinase phosphorylation sites.";
J. Biol. Chem. 268:21147-21154(1993).
[9]
INTERACTION WITH MLLT7.
PubMed=16054032; DOI=10.1016/j.devcel.2005.05.017;
Liu Z.-P., Wang Z., Yanagisawa H., Olson E.N.;
"Phenotypic modulation of smooth muscle cells through interaction of
Foxo4 and myocardin.";
Dev. Cell 9:261-270(2005).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[11]
INTERACTION WITH LPXN.
PubMed=18497331; DOI=10.1161/CIRCRESAHA.107.170357;
Sundberg-Smith L.J., DiMichele L.A., Sayers R.L., Mack C.P.,
Taylor J.M.;
"The LIM protein leupaxin is enriched in smooth muscle and functions
as an serum response factor cofactor to induce smooth muscle cell gene
transcription.";
Circ. Res. 102:1502-1511(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; SER-79; SER-83;
SER-85 AND SER-224, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[13]
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).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[18]
INTERACTION WITH OLFM2.
PubMed=25298399; DOI=10.1091/mbc.E14-08-1255;
Shi N., Guo X., Chen S.Y.;
"Olfactomedin 2, a novel regulator for transforming growth factor-
beta-induced smooth muscle differentiation of human embryonic stem
cell-derived mesenchymal cells.";
Mol. Biol. Cell 25:4106-4114(2014).
[19]
X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 132-223.
PubMed=7637780; DOI=10.1038/376490a0;
Pellegrini L., Tan S., Richmond T.J.;
"Structure of serum response factor core bound to DNA.";
Nature 376:490-498(1995).
-!- 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). Required for cardiac differentiation and
maturation.
-!- SUBUNIT: Binds DNA as a multimer, probably a dimer. Interacts with
MLLT7/FOXO4, NKX3A and SSRP1. Interacts with ARID2 and SRFBP1 (By
similarity). Forms complexes with ARID2, MYOCD, NKX2-5 and SRFBP1
(By similarity). Forms a nuclear ternary complex with MKL1 and
SCAI (PubMed:19350017). 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, ECO:0000269|PubMed:16054032,
ECO:0000269|PubMed:18497331, ECO:0000269|PubMed:19350017,
ECO:0000269|PubMed:25298399}.
-!- INTERACTION:
Q969V6:MKL1; NbExp=2; IntAct=EBI-493034, EBI-493122;
Q9ULH7:MKL2; NbExp=3; IntAct=EBI-493034, EBI-493007;
Q8IZQ8:MYOCD; NbExp=2; IntAct=EBI-493034, EBI-493384;
-!- 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}.
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EMBL; J03161; AAA36647.1; -; mRNA.
EMBL; AL133375; CAI20207.1; -; Genomic_DNA.
EMBL; AL355385; CAI20207.1; JOINED; Genomic_DNA.
EMBL; AL355385; CAI13785.1; -; Genomic_DNA.
EMBL; AL133375; CAI13785.1; JOINED; Genomic_DNA.
EMBL; CH471081; EAX04161.1; -; Genomic_DNA.
EMBL; BC048211; AAH48211.1; -; mRNA.
EMBL; BC052572; AAH52572.1; -; mRNA.
CCDS; CCDS4889.1; -.
PIR; A31637; A31637.
RefSeq; NP_001278930.1; NM_001292001.1.
RefSeq; NP_003122.1; NM_003131.3.
UniGene; Hs.520140; -.
PDB; 1HBX; X-ray; 3.15 A; A/B/D/E=132-223.
PDB; 1K6O; X-ray; 3.19 A; B/C=133-235.
PDB; 1SRS; X-ray; 3.20 A; A/B=132-223.
PDBsum; 1HBX; -.
PDBsum; 1K6O; -.
PDBsum; 1SRS; -.
ProteinModelPortal; P11831; -.
SMR; P11831; -.
BioGrid; 112600; 61.
DIP; DIP-49N; -.
ELM; P11831; -.
IntAct; P11831; 6.
MINT; MINT-130058; -.
STRING; 9606.ENSP00000265354; -.
iPTMnet; P11831; -.
PhosphoSitePlus; P11831; -.
UniCarbKB; P11831; -.
BioMuta; SRF; -.
DMDM; 134876; -.
EPD; P11831; -.
MaxQB; P11831; -.
PaxDb; P11831; -.
PeptideAtlas; P11831; -.
PRIDE; P11831; -.
Ensembl; ENST00000265354; ENSP00000265354; ENSG00000112658.
GeneID; 6722; -.
KEGG; hsa:6722; -.
UCSC; uc003oui.4; human.
CTD; 6722; -.
DisGeNET; 6722; -.
GeneCards; SRF; -.
HGNC; HGNC:11291; SRF.
HPA; CAB005416; -.
HPA; HPA001819; -.
MIM; 600589; gene.
neXtProt; NX_P11831; -.
OpenTargets; ENSG00000112658; -.
PharmGKB; PA36116; -.
eggNOG; KOG0015; Eukaryota.
eggNOG; COG5068; LUCA.
GeneTree; ENSGT00400000022158; -.
HOGENOM; HOG000012380; -.
HOVERGEN; HBG014968; -.
InParanoid; P11831; -.
KO; K04378; -.
OMA; NAFPQAP; -.
OrthoDB; EOG091G0X24; -.
PhylomeDB; P11831; -.
TreeFam; TF318482; -.
Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
SignaLink; P11831; -.
SIGNOR; P11831; -.
EvolutionaryTrace; P11831; -.
GeneWiki; Serum_response_factor; -.
GenomeRNAi; 6722; -.
PMAP-CutDB; P11831; -.
PRO; PR:P11831; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000112658; -.
CleanEx; HS_SRF; -.
ExpressionAtlas; P11831; baseline and differential.
Genevisible; P11831; HS.
GO; GO:0005737; C:cytoplasm; TAS:BHF-UCL.
GO; GO:0000790; C:nuclear chromatin; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0031490; F:chromatin DNA binding; IEA:Ensembl.
GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl.
GO; GO:0070878; F:primary miRNA binding; ISS:BHF-UCL.
GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; ISS:BHF-UCL.
GO; GO:0010736; F:serum response element binding; IDA:BHF-UCL.
GO; GO:0003705; F:transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding; IEA:Ensembl.
GO; GO:0001076; F:transcription factor activity, RNA polymerase II transcription factor binding; IEA:Ensembl.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:BHF-UCL.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:UniProtKB.
GO; GO:0001228; F:transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding; ISS:BHF-UCL.
GO; GO:0060055; P:angiogenesis involved in wound healing; TAS:BHF-UCL.
GO; GO:0008306; P:associative learning; IEA:Ensembl.
GO; GO:0070830; P:bicellular tight junction assembly; IEA:Ensembl.
GO; GO:0001569; P:branching involved in blood vessel morphogenesis; IEA:Ensembl.
GO; GO:0060532; P:bronchus cartilage development; IEA:Ensembl.
GO; GO:0055003; P:cardiac myofibril assembly; IEA:Ensembl.
GO; GO:0060947; P:cardiac vascular smooth muscle cell differentiation; IEA:Ensembl.
GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; IMP:BHF-UCL.
GO; GO:0007160; P:cell-matrix adhesion; IEA:Ensembl.
GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
GO; GO:0090398; P:cellular senescence; IMP:BHF-UCL.
GO; GO:0048589; P:developmental growth; IEA:Ensembl.
GO; GO:0035912; P:dorsal aorta morphogenesis; IEA:Ensembl.
GO; GO:0090136; P:epithelial cell-cell adhesion; IEA:Ensembl.
GO; GO:0010669; P:epithelial structure maintenance; IEA:Ensembl.
GO; GO:0048821; P:erythrocyte development; IEA:Ensembl.
GO; GO:0061029; P:eyelid development in camera-type eye; IEA:Ensembl.
GO; GO:0060324; P:face development; IEA:Ensembl.
GO; GO:0007507; P:heart development; ISS:BHF-UCL.
GO; GO:0001947; P:heart looping; ISS:BHF-UCL.
GO; GO:0060347; P:heart trabecula formation; IEA:Ensembl.
GO; GO:0060218; P:hematopoietic stem cell differentiation; IEA:Ensembl.
GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
GO; GO:0060292; P:long term synaptic depression; IEA:Ensembl.
GO; GO:0007616; P:long-term memory; IEA:Ensembl.
GO; GO:0060425; P:lung morphogenesis; IEA:Ensembl.
GO; GO:0061145; P:lung smooth muscle development; IEA:Ensembl.
GO; GO:0035855; P:megakaryocyte development; IEA:Ensembl.
GO; GO:0001707; P:mesoderm formation; IEA:Ensembl.
GO; GO:0002011; P:morphogenesis of an epithelial sheet; IEA:Ensembl.
GO; GO:0042789; P:mRNA transcription from RNA polymerase II promoter; ISS:BHF-UCL.
GO; GO:0046716; P:muscle cell cellular homeostasis; ISS:BHF-UCL.
GO; GO:1900222; P:negative regulation of amyloid-beta clearance; IMP:BHF-UCL.
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; ISS:BHF-UCL.
GO; GO:0048666; P:neuron development; TAS:BHF-UCL.
GO; GO:0001764; P:neuron migration; IEA:Ensembl.
GO; GO:0031175; P:neuron projection development; IEA:Ensembl.
GO; GO:0030168; P:platelet activation; IEA:Ensembl.
GO; GO:0030220; P:platelet formation; IEA:Ensembl.
GO; GO:0045773; P:positive regulation of axon extension; IEA:Ensembl.
GO; GO:0045597; P:positive regulation of cell differentiation; IDA:MGI.
GO; GO:0051491; P:positive regulation of filopodium assembly; IEA:Ensembl.
GO; GO:1902895; P:positive regulation of pri-miRNA transcription from RNA polymerase II promoter; ISS:BHF-UCL.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IDA:BHF-UCL.
GO; GO:0045987; P:positive regulation of smooth muscle contraction; IDA:BHF-UCL.
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; IGI:BHF-UCL.
GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0010735; P:positive regulation of transcription via serum response element binding; IDA:BHF-UCL.
GO; GO:0045059; P:positive thymic T cell selection; IEA:Ensembl.
GO; GO:0090009; P:primitive streak formation; IEA:Ensembl.
GO; GO:0030155; P:regulation of cell adhesion; IEA:Ensembl.
GO; GO:0051150; P:regulation of smooth muscle cell differentiation; TAS:BHF-UCL.
GO; GO:0033561; P:regulation of water loss via skin; IEA:Ensembl.
GO; GO:0034097; P:response to cytokine; IMP:BHF-UCL.
GO; GO:0009725; P:response to hormone; IDA:BHF-UCL.
GO; GO:0001666; P:response to hypoxia; IEP:BHF-UCL.
GO; GO:0009636; P:response to toxic substance; TAS:BHF-UCL.
GO; GO:0045214; P:sarcomere organization; IEA:Ensembl.
GO; GO:0043589; P:skin morphogenesis; IEA:Ensembl.
GO; GO:0043149; P:stress fiber assembly; IEA:Ensembl.
GO; GO:0022028; P:tangential migration from the subventricular zone to the olfactory bulb; IEA:Ensembl.
GO; GO:0048538; P:thymus development; IEA:Ensembl.
GO; GO:0030878; P:thyroid gland development; IEA:Ensembl.
GO; GO:0060534; P:trachea cartilage development; IEA:Ensembl.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0001829; P:trophectodermal cell differentiation; IDA:MGI.
CDD; cd00266; MADS_SRF_like; 1.
Gene3D; 3.40.1810.10; -; 1.
InterPro; IPR033897; MADS_SRF-like.
InterPro; IPR002100; TF_MADSbox.
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;
3D-structure; Activator; Complete proteome; Developmental protein;
Direct protein sequencing; DNA-binding; Glycoprotein; Nucleus;
Phosphoprotein; Reference proteome; Transcription;
Transcription regulation.
CHAIN 1 508 Serum response factor.
/FTId=PRO_0000199423.
DOMAIN 141 201 MADS-box. {ECO:0000255|PROSITE-
ProRule:PRU00251}.
DNA_BIND 133 222
REGION 168 222 Involved in dimerization.
COMPBIAS 13 142 Gly-rich.
COMPBIAS 80 90 Asp/Glu-rich (acidic).
COMPBIAS 242 258 Asp/Glu-rich (acidic).
MOD_RES 77 77 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000269|PubMed:1547771}.
MOD_RES 79 79 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000269|PubMed:1547771}.
MOD_RES 83 83 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000269|PubMed:1547771}.
MOD_RES 85 85 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000269|PubMed:1547771}.
MOD_RES 103 103 Phosphoserine.
{ECO:0000269|PubMed:1547771}.
MOD_RES 224 224 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 253 253 Phosphoserine.
{ECO:0000269|PubMed:8375385}.
MOD_RES 435 435 Phosphoserine; by dsDNA kinase.
{ECO:0000269|PubMed:8407951}.
MOD_RES 446 446 Phosphoserine; by dsDNA kinase.
{ECO:0000269|PubMed:8407951}.
CARBOHYD 277 277 O-linked (GlcNAc) serine.
{ECO:0000269|PubMed:1512232}.
/FTId=CAR_000181.
CARBOHYD 307 307 O-linked (GlcNAc) serine.
{ECO:0000305|PubMed:1512232}.
CARBOHYD 309 309 O-linked (GlcNAc) serine.
{ECO:0000305|PubMed:1512232}.
CARBOHYD 316 316 O-linked (GlcNAc) serine.
{ECO:0000269|PubMed:1512232}.
/FTId=CAR_000196.
CARBOHYD 383 383 O-linked (GlcNAc) serine.
{ECO:0000305|PubMed:1512232}.
HELIX 154 179 {ECO:0000244|PDB:1HBX}.
STRAND 182 188 {ECO:0000244|PDB:1HBX}.
STRAND 190 192 {ECO:0000244|PDB:1K6O}.
STRAND 194 198 {ECO:0000244|PDB:1HBX}.
HELIX 200 205 {ECO:0000244|PDB:1HBX}.
HELIX 209 220 {ECO:0000244|PDB:1HBX}.
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


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