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Protein

Serum response factor

Gene

Srf

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi129 – 218By similarityAdd BLAST90

GO - Molecular functioni

GO - Biological processi

  • actin cytoskeleton organization Source: MGI
  • actin filament organization Source: MGI
  • associative learning Source: MGI
  • bicellular tight junction assembly Source: MGI
  • bronchus cartilage development Source: MGI
  • cardiac myofibril assembly Source: MGI
  • cardiac vascular smooth muscle cell differentiation Source: MGI
  • cell-matrix adhesion Source: MGI
  • cell migration involved in sprouting angiogenesis Source: MGI
  • cellular response to glucose stimulus Source: Ensembl
  • cellular senescence Source: MGI
  • contractile actin filament bundle assembly Source: MGI
  • developmental growth Source: MGI
  • dorsal aorta morphogenesis Source: MGI
  • epithelial cell-cell adhesion Source: MGI
  • epithelial structure maintenance Source: MGI
  • erythrocyte development Source: MGI
  • eyelid development in camera-type eye Source: MGI
  • face development Source: MGI
  • forebrain development Source: MGI
  • gastrulation Source: MGI
  • heart development Source: MGI
  • heart looping Source: MGI
  • heart trabecula formation Source: MGI
  • hematopoietic stem cell differentiation Source: MGI
  • hippocampus development Source: MGI
  • in utero embryonic development Source: MGI
  • leukocyte differentiation Source: MGI
  • long-term memory Source: Ensembl
  • long term synaptic depression Source: MGI
  • lung morphogenesis Source: MGI
  • lung smooth muscle development Source: MGI
  • megakaryocyte development Source: MGI
  • mesoderm formation Source: MGI
  • morphogenesis of an epithelial sheet Source: MGI
  • mRNA transcription from RNA polymerase II promoter Source: BHF-UCL
  • muscle cell cellular homeostasis Source: MGI
  • negative regulation of beta-amyloid clearance Source: MGI
  • negative regulation of cell migration Source: Ensembl
  • negative regulation of cell proliferation Source: Ensembl
  • negative regulation of pri-miRNA transcription from RNA polymerase II promoter Source: BHF-UCL
  • neuron migration Source: MGI
  • neuron projection development Source: MGI
  • patterning of blood vessels Source: MGI
  • platelet activation Source: MGI
  • platelet formation Source: MGI
  • positive regulation of axon extension Source: MGI
  • positive regulation of cell differentiation Source: MGI
  • positive regulation of filopodium assembly Source: MGI
  • positive regulation of pri-miRNA transcription from RNA polymerase II promoter Source: BHF-UCL
  • positive regulation of sequence-specific DNA binding transcription factor activity Source: MGI
  • positive regulation of smooth muscle contraction Source: MGI
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of transcription by glucose Source: Ensembl
  • positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • positive regulation of transcription from RNA polymerase II promoter involved in myocardial precursor cell differentiation Source: BHF-UCL
  • positive regulation of transcription initiation from RNA polymerase II promoter Source: MGI
  • positive regulation of transcription via serum response element binding Source: MGI
  • positive thymic T cell selection Source: MGI
  • primitive streak formation Source: MGI
  • regulation of cell adhesion Source: MGI
  • regulation of transcription, DNA-templated Source: MGI
  • regulation of water loss via skin Source: MGI
  • response to cytokine Source: MGI
  • response to hormone Source: MGI
  • response to hypoxia Source: Ensembl
  • sarcomere organization Source: MGI
  • single organismal cell-cell adhesion Source: MGI
  • skin morphogenesis Source: MGI
  • stress fiber assembly Source: MGI
  • tangential migration from the subventricular zone to the olfactory bulb Source: MGI
  • thymus development Source: MGI
  • thyroid gland development Source: MGI
  • trachea cartilage development Source: MGI
  • transcription from RNA polymerase II promoter Source: MGI
  • trophectodermal cell differentiation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Activator, Developmental protein

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-MMU-5663220. RHO GTPases Activate Formins.

Names & Taxonomyi

Protein namesi
Recommended name:
Serum response factor
Short name:
SRF
Gene namesi
Name:Srf
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:106658. Srf.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • nuclear chromatin Source: BHF-UCL
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

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.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002452251 – 504Serum response factorAdd BLAST504

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei73PhosphoserineBy similarity1
Modified residuei75PhosphoserineBy similarity1
Modified residuei79PhosphoserineBy similarity1
Modified residuei81PhosphoserineBy similarity1
Modified residuei99PhosphoserineBy similarity1
Modified residuei220PhosphoserineCombined sources1
Modified residuei249PhosphoserineBy similarity1
Glycosylationi273O-linked (GlcNAc)By similarity1
Glycosylationi303O-linked (GlcNAc)By similarity1
Glycosylationi305O-linked (GlcNAc)By similarity1
Glycosylationi312O-linked (GlcNAc)By similarity1
Glycosylationi379O-linked (GlcNAc)By similarity1
Modified residuei431Phosphoserine; by dsDNA kinaseBy similarity1
Modified residuei442Phosphoserine; by dsDNA kinaseBy similarity1

Post-translational modificationi

Phosphorylated by PRKDC.By similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ9JM73.
PaxDbiQ9JM73.
PeptideAtlasiQ9JM73.
PRIDEiQ9JM73.

PTM databases

iPTMnetiQ9JM73.
PhosphoSitePlusiQ9JM73.

Expressioni

Gene expression databases

BgeeiENSMUSG00000015605.
CleanExiMM_SRF.
GenevisibleiQ9JM73. MM.

Interactioni

Subunit structurei

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).By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Srebf2Q3U1N23EBI-493266,EBI-645275

GO - Molecular functioni

Protein-protein interaction databases

BioGridi203497. 6 interactors.
DIPiDIP-49624N.
IntActiQ9JM73. 3 interactors.
MINTiMINT-1739318.
STRINGi10090.ENSMUSP00000015749.

Structurei

3D structure databases

ProteinModelPortaliQ9JM73.
SMRiQ9JM73.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini137 – 197MADS-boxPROSITE-ProRule annotationAdd BLAST61

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni164 – 218Involved in dimerizationBy similarityAdd BLAST55

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi13 – 138Gly-richAdd BLAST126
Compositional biasi76 – 86Asp/Glu-rich (acidic)Add BLAST11
Compositional biasi238 – 254Asp/Glu-rich (acidic)Add BLAST17

Sequence similaritiesi

Contains 1 MADS-box domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0015. Eukaryota.
COG5068. LUCA.
GeneTreeiENSGT00400000022158.
HOGENOMiHOG000012380.
HOVERGENiHBG014968.
InParanoidiQ9JM73.
KOiK04378.
OMAiNAFPQAP.
OrthoDBiEOG091G0X24.
PhylomeDBiQ9JM73.
TreeFamiTF318482.

Family and domain databases

CDDicd00266. MADS_SRF_like. 1 hit.
InterProiIPR033897. MADS_SRF-like.
IPR002100. TF_MADSbox.
[Graphical view]
PfamiPF00319. SRF-TF. 1 hit.
[Graphical view]
PRINTSiPR00404. MADSDOMAIN.
SMARTiSM00432. MADS. 1 hit.
[Graphical view]
SUPFAMiSSF55455. SSF55455. 1 hit.
PROSITEiPS00350. MADS_BOX_1. 1 hit.
PS50066. MADS_BOX_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9JM73-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLPSQAGAAA ALGRGSALGG NLNRTPTGRP GGGGGTRGAN GGRVPGNGAG
60 70 80 90 100
LGQSRLEREA AAAAAPTAGA LYSGSEGDSE SGEEEELGAE RRGLKRSLSE
110 120 130 140 150
MELGVVVGGP EAAAAAAGGY GPVSGAVSGA KPGKKTRGRV KIKMEFIDNK
160 170 180 190 200
LRRYTTFSKR KTGIMKKAYE LSTLTGTQVL LLVASETGHV YTFATRKLQP
210 220 230 240 250
MITSETGKAL IQTCLNSPDS PPRSDPTTDQ RMSATGFEEP DLTYQVSESD
260 270 280 290 300
SSGETKDTLK PAFTVTNLPG TTSTIQTAPS TSTTMQVSSG PSFPITNYLA
310 320 330 340 350
PVSASVSPSA VSSANGTVLK STGSGPVSSG GLMQLPTSFT LMPGGAVAQQ
360 370 380 390 400
VPVQAIHVHQ APQQASPSRD SSTDLTQTSS SGTVTLPATI MTSSVPTTVG
410 420 430 440 450
GHMMYPSPHA VMYAPTSGLA DGSLTVLNAF SQAPSTMQVS HSQVQEPGGV
460 470 480 490 500
PQVFLTAPSG TVQIPVSAVQ LHQMAVIGQQ AGSSSNLTEL QVVNLDATHS

TKSE
Length:504
Mass (Da):51,247
Last modified:October 1, 2000 - v1
Checksum:i26353F18A2B46F6B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB038376 Genomic DNA. Translation: BAA92314.1.
BC051950 mRNA. Translation: AAH51950.1.
CCDSiCCDS28831.1.
RefSeqiNP_065239.1. NM_020493.2.
UniGeneiMm.45044.

Genome annotation databases

EnsembliENSMUST00000015749; ENSMUSP00000015749; ENSMUSG00000015605.
GeneIDi20807.
KEGGimmu:20807.
UCSCiuc008ctg.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB038376 Genomic DNA. Translation: BAA92314.1.
BC051950 mRNA. Translation: AAH51950.1.
CCDSiCCDS28831.1.
RefSeqiNP_065239.1. NM_020493.2.
UniGeneiMm.45044.

3D structure databases

ProteinModelPortaliQ9JM73.
SMRiQ9JM73.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203497. 6 interactors.
DIPiDIP-49624N.
IntActiQ9JM73. 3 interactors.
MINTiMINT-1739318.
STRINGi10090.ENSMUSP00000015749.

PTM databases

iPTMnetiQ9JM73.
PhosphoSitePlusiQ9JM73.

Proteomic databases

MaxQBiQ9JM73.
PaxDbiQ9JM73.
PeptideAtlasiQ9JM73.
PRIDEiQ9JM73.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000015749; ENSMUSP00000015749; ENSMUSG00000015605.
GeneIDi20807.
KEGGimmu:20807.
UCSCiuc008ctg.1. mouse.

Organism-specific databases

CTDi6722.
MGIiMGI:106658. Srf.

Phylogenomic databases

eggNOGiKOG0015. Eukaryota.
COG5068. LUCA.
GeneTreeiENSGT00400000022158.
HOGENOMiHOG000012380.
HOVERGENiHBG014968.
InParanoidiQ9JM73.
KOiK04378.
OMAiNAFPQAP.
OrthoDBiEOG091G0X24.
PhylomeDBiQ9JM73.
TreeFamiTF318482.

Enzyme and pathway databases

ReactomeiR-MMU-5663220. RHO GTPases Activate Formins.

Miscellaneous databases

PROiQ9JM73.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000015605.
CleanExiMM_SRF.
GenevisibleiQ9JM73. MM.

Family and domain databases

CDDicd00266. MADS_SRF_like. 1 hit.
InterProiIPR033897. MADS_SRF-like.
IPR002100. TF_MADSbox.
[Graphical view]
PfamiPF00319. SRF-TF. 1 hit.
[Graphical view]
PRINTSiPR00404. MADSDOMAIN.
SMARTiSM00432. MADS. 1 hit.
[Graphical view]
SUPFAMiSSF55455. SSF55455. 1 hit.
PROSITEiPS00350. MADS_BOX_1. 1 hit.
PS50066. MADS_BOX_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSRF_MOUSE
AccessioniPrimary (citable) accession number: Q9JM73
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: October 1, 2000
Last modified: November 30, 2016
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.