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Protein Page:
SRF (human)
rdtyret
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
SRF a transcription factor of the MADS domain family that binds to the serum response element (SRE). Regulates the transcription of immediate early genes including c-fos. Binds DNA as a multimer, probably a dimer. Note: This description may include information from UniProtKB.
Protein type: Motility/polarity/chemotaxis; Transcription factor
Chromosomal Location of Human Ortholog: 6p21.1
Cellular Component: cytoplasm; nuclear chromatin; nucleoplasm; nucleus
Molecular Function: chromatin DNA binding; histone deacetylase binding; protein binding; protein homodimerization activity; RNA polymerase II transcription factor activity, enhancer binding; transcription factor activity; transcription factor binding
Biological Process: angiogenesis involved in wound healing; associative learning; cardiac myofibril assembly; cell migration during sprouting angiogenesis; cell-matrix adhesion; developmental growth; erythrocyte development; heart development; heart looping; hippocampus development; long-term memory; mesoderm formation; morphogenesis of an epithelial sheet; mRNA transcription from RNA polymerase II promoter; muscle maintenance; negative regulation of cell migration; negative regulation of cell proliferation; neurite development; neuron development; neuron migration; patterning of blood vessels; platelet activation; platelet formation; positive regulation of axon extension; positive regulation of cell differentiation; positive regulation of filopodium formation; positive regulation of smooth muscle contraction; positive regulation of transcription by glucose; positive regulation of transcription factor activity; positive regulation of transcription from RNA polymerase II promoter; positive thymic T cell selection; regulation of cell adhesion; regulation of smooth muscle cell differentiation; regulation of water loss via skin; response to cytokine stimulus; response to hormone stimulus; response to hypoxia; response to toxin; sarcomere organization; skin morphogenesis; small GTPase mediated signal transduction; stress fiber formation; tangential migration from the subventricular zone to the olfactory bulb; thymus development; thyroid gland development; transcription from RNA polymerase II promoter; trophectodermal cell differentiation
Reference #:  P11831 (UniProtKB)
Alt. Names/Synonyms: MCM1; Serum response factor; serum response factor (c-fos serum response element-binding transcription factor); SRF
Gene Symbols: SRF
Molecular weight: 51,593 Da
Basal Isoelectric point: 7.83  Predict pI for various phosphorylation states
CST Pathways:  Growth And Differentiation Control by MAPKs
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

SRF

Protein Structure Not Found.


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Sites Implicated In
transcription, altered: S103‑p
transcription, induced: T159‑p
transcription, inhibited: T159‑p, S162‑p, S251‑p, S253‑p
activity, induced: T159‑p
molecular association, regulation: S83‑p, S85‑p, S103‑p

Modification Sites and Domains  
Click here to view other types of protein modifications

Modification Sites in Parent Protein, Orthologs, and Isoforms  
 

Show Multiple Sequence Alignment


 LTP 

LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 HTP 

HTP: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 T4‑p ____MLPtQAGAAAA
0 1 S16‑p AAALGRGsALGGsLN
0 1 S21‑p RGsALGGsLNRTPtG
0 1 T27‑p GsLNRTPtGRPGGGG
0 1 Y76 APTAGALYsGsEGDs
4 1 S77‑p PTAGALYsGsEGDsE
4 2 S79‑p AGALYsGsEGDsEsG
3 5 S83‑p YsGsEGDsEsGEEEE
3 4 S85‑p GsEGDsEsGEEEELG
1 3 S101‑p ERRGLKRsLsEMEIG
15 6 S103‑p RGLKRsLsEMEIGMV
1 0 K147‑sm TRGRVKIkMEFIDNK
2 0 T159‑p DNKLRRYtTFsKRKT
2 0 S162‑p LRRYtTFsKRKTGIM
0 1 S176‑p MKKAYELstLTGTQV
0 1 T177‑p KKAYELstLTGTQVL
0 1 T199‑p GHVYTFAtRKLQPMI
0 5 S221‑p LIQTCLNsPDsPPRs
1 32 S224‑p TCLNsPDsPPRsDPT
0 3 S228‑p sPDsPPRsDPTTDQR
1 0 S251‑p TDLTYQVsEsDSSGE
1 0 S253‑p LTYQVsEsDSSGETK
1 0 S277‑gl TNLPGTTsTIQTAPS
1 0 S313‑gl VSASVSPsAVsSANG
1 0 S316‑gl SVSPsAVsSANGTVL
0 1 S370 HQAPQQASPSRDSST
1 0 S383‑gl STDLTQTsSSGTVTL
1 0 T401‑gl IMTSSVPtTVGGHMM
1 0 S435‑p LTVLNAFsQAPSTMQ
1 0 S446‑p STMQVSHsQVQEPGG
4261 : Phospho-SRF (Ser103) Antibody
  mouse

 
S4 ____MLPSQAGAAAA
S16 AAALGRGSALGGNLN
N21 RGSALGGNLNRTPTG
T27 GNLNRTPTGRPGGGG
Y72‑p APTAGALySGSEGDs
S73 PTAGALySGSEGDsE
S75 AGALySGSEGDsEsG
S79‑p ySGSEGDsEsGEEEE
S81‑p GSEGDsEsGEEEELG
S97‑p ERRGLKRsLsEMELG
S99‑p RGLKRsLsEMELGVV
K143 TRGRVKIKMEFIDNK
T155 DNKLRRYTTFSKRKT
S158 LRRYTTFSKRKTGIM
S172 MKKAYELSTLTGTQV
T173 KKAYELSTLTGTQVL
T195 GHVYTFATRKLQPMI
S217‑p LIQTCLNsPDsPPRs
S220‑p TCLNsPDsPPRsDPT
S224‑p sPDsPPRsDPTTDQR
S247 PDLTYQVSESDSSGE
S249 LTYQVSESDSSGETK
S273 TNLPGTTSTIQTAPS
S309 VSASVSPSAVSSANG
S312 SVSPSAVSSANGTVL
S366‑p HQAPQQAsPSRDSST
S379 STDLTQTSSSGTVTL
T397 IMTSSVPTTVGGHMM
S431 LTVLNAFSQAPSTMQ
S442 STMQVSHSQVQEPGG
4261 : Phospho-SRF (Ser103) Antibody
  rat

 
S4 ____MLPSQAGAAAA
S16 AAALGRGSALGGSLN
S21 RGSALGGSLNRTPTG
T27 GSLNRTPTGRPGGSG
Y72 APTAGALYsGsEGDS
S73‑p PTAGALYsGsEGDSE
S75‑p AGALYsGsEGDSESG
S79 YsGsEGDSESGEEEE
S81 GsEGDSESGEEEELG
S97 ERRGLKRSLsEMELG
S99‑p RGLKRSLsEMELGVV
K143 TRGRVKIKMEFIDNK
T155 DNKLRRYTTFSKRKT
S158 LRRYTTFSKRKTGIM
S172 MKKAYELSTLTGTQV
T173 KKAYELSTLTGTQVL
T195 GHVYTFATRKLQPMI
S217 LIQTCLNSPDsPPRS
S220‑p TCLNSPDsPPRSDPS
S224 SPDsPPRSDPSTDQR
S247 PDLTYQVSESDSSGE
S249 LTYQVSESDSSGETK
S273 TNLPGTTSTIQTAPS
S309 VSASVSPSAVSSANG
S312 SVSPSAVSSANGTVL
S366 HQAPQQASPSRDSST
S379 STDLTQTSSSGTVTL
T397 IMTSSVPTTVGGHMM
S431 LTVLNAFSQAPSTMQ
S442 STMQVSHSQVQEPGG
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