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P08046 (EGR1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Early growth response protein 1

Short name=EGR-1
Alternative name(s):
Nerve growth factor-induced protein A
Short name=NGFI-A
Transcription factor Zif268
Zinc finger protein Krox-24
Gene names
Name:Egr1
Synonyms:Egr-1, Krox-24
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length533 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcriptional regulator. Recognizes and binds to the DNA sequence 5'-CGCCCCCGC-3'(EGR-site). Activates the transcription of target genes whose products are required for mitogenesis and differentiation.

Subunit structure

Interacts with SNAI1 and SP1 upon 12-O-tetradecanoylphorbol-13-acetate (TPA) induction By similarity.

Subcellular location

Nucleus.

Induction

By growth factors.

Sequence similarities

Belongs to the EGR C2H2-type zinc-finger protein family.

Contains 3 C2H2-type zinc fingers.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   DomainRepeat
Zinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionActivator
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processBMP signaling pathway

Inferred from direct assay PubMed 8769660. Source: MGI

T cell differentiation

Inferred from mutant phenotype PubMed 12165491. Source: MGI

cellular response to antibiotic

Inferred from electronic annotation. Source: Ensembl

cellular response to cAMP

Inferred from Biological aspect of Ancestor. Source: RefGenome

cellular response to drug

Inferred from electronic annotation. Source: Ensembl

cellular response to follicle-stimulating hormone stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to gamma radiation

Inferred from mutant phenotype PubMed 19057511. Source: BHF-UCL

cellular response to gonadotropin stimulus

Inferred from Biological aspect of Ancestor. Source: RefGenome

cellular response to growth factor stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to heparin

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to hyperoxia

Inferred from electronic annotation. Source: Ensembl

cellular response to hypoxia

Inferred from electronic annotation. Source: Ensembl

cellular response to insulin stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to isoquinoline alkaloid

Inferred from electronic annotation. Source: Ensembl

cellular response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to mycophenolic acid

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to organic substance

Inferred from direct assay PubMed 21357543. Source: MGI

cellular response to steroid hormone stimulus

Inferred from electronic annotation. Source: Ensembl

circadian rhythm

Inferred from electronic annotation. Source: Ensembl

glomerular mesangial cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

interleukin-1-mediated signaling pathway

Inferred from electronic annotation. Source: Ensembl

learning or memory

Inferred from electronic annotation. Source: Ensembl

long-term synaptic potentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of canonical Wnt signaling pathway

Inferred from mutant phenotype PubMed 18281035. Source: BHF-UCL

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 16033766. Source: MGI

oligodendrocyte differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of glomerular metanephric mesangial cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 20018936. Source: BHF-UCL

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 12689920PubMed 7720589. Source: UniProtKB

regulation of long-term neuronal synaptic plasticity

Inferred from Biological aspect of Ancestor. Source: RefGenome

regulation of protein sumoylation

Inferred from electronic annotation. Source: Ensembl

regulation of transcription, DNA-templated

Inferred from mutant phenotype PubMed 12165491. Source: MGI

response to amphetamine

Inferred from electronic annotation. Source: Ensembl

response to carbon monoxide

Inferred from electronic annotation. Source: Ensembl

response to cocaine

Inferred from electronic annotation. Source: Ensembl

response to electrical stimulus

Inferred from electronic annotation. Source: Ensembl

response to ethanol

Inferred from electronic annotation. Source: Ensembl

response to glucose

Inferred from direct assay PubMed 12689920. Source: UniProtKB

response to insulin

Inferred from direct assay PubMed 12689920. Source: UniProtKB

response to norepinephrine

Inferred from electronic annotation. Source: Ensembl

response to nutrient levels

Inferred from electronic annotation. Source: Ensembl

skeletal muscle cell differentiation

Inferred from mutant phenotype PubMed 22147266. Source: MGI

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 12689920. Source: UniProtKB

   Molecular_functionRNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 20018936. Source: BHF-UCL

RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription

Inferred from electronic annotation. Source: Ensembl

RNA polymerase II core promoter sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

double-stranded DNA binding

Inferred from electronic annotation. Source: Ensembl

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 12689920. Source: UniProtKB

transcription regulatory region DNA binding

Inferred from direct assay PubMed 18281035. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 533533Early growth response protein 1
PRO_0000047110

Regions

Zinc finger336 – 36025C2H2-type 1
Zinc finger366 – 38823C2H2-type 2
Zinc finger394 – 41623C2H2-type 3
Compositional bias57 – 8125Gly/Ser-rich

Experimental info

Sequence conflict761S → T Ref.3
Sequence conflict761S → T Ref.4
Sequence conflict801S → T Ref.3
Sequence conflict801S → T Ref.4

Secondary structure

..................... 533
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P08046 [UniParc].

Last modified November 1, 1990. Version 2.
Checksum: 36E3935767CEAA0F

FASTA53356,590
        10         20         30         40         50         60 
MAAAKAEMQL MSPLQISDPF GSFPHSPTMD NYPKLEEMML LSNGAPQFLG AAGTPEGSGG 

        70         80         90        100        110        120 
NSSSSTSSGG GGGGGSNSGS SAFNPQGEPS EQPYEHLTTE SFSDIALNNE KAMVETSYPS 

       130        140        150        160        170        180 
QTTRLPPITY TGRFSLEPAP NSGNTLWPEP LFSLVSGLVS MTNPPTSSSS APSPAASSSS 

       190        200        210        220        230        240 
SASQSPPLSC AVPSNDSSPI YSAAPTFPTP NTDIFPEPQS QAFPGSAGTA LQYPPPAYPA 

       250        260        270        280        290        300 
TKGGFQVPMI PDYLFPQQQG DLSLGTPDQK PFQGLENRTQ QPSLTPLSTI KAFATQSGSQ 

       310        320        330        340        350        360 
DLKALNTTYQ SQLIKPSRMR KYPNRPSKTP PHERPYACPV ESCDRRFSRS DELTRHIRIH 

       370        380        390        400        410        420 
TGQKPFQCRI CMRNFSRSDH LTTHIRTHTG EKPFACDICG RKFARSDERK RHTKIHLRQK 

       430        440        450        460        470        480 
DKKADKSVVA SPAASSLSSY PSPVATSYPS PATTSFPSPV PTSYSSPGSS TYPSPAHSGF 

       490        500        510        520        530 
PSPSVATTFA SVPPAFPTQV SSFPSAGVSS SFSTSTGLSD MTATFSPRTI EIC 

« Hide

References

[1]"A zinc finger-encoding gene coregulated with c-fos during growth and differentiation, and after cellular depolarization."
Sukhatme V.P., Cao X., Chang L.C., Tsai-Morris C.-H., Stamenkovich D., Ferreira P.C.P., Cohen D.R., Edwards S.A., Shows T.B., Curran T., le Beau M.M., Adamson E.D.
Cell 53:37-43(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"A gene activated in mouse 3T3 cells by serum growth factors encodes a protein with 'zinc finger' sequences."
Christy B.A., Lau L.F., Nathans D.
Proc. Natl. Acad. Sci. U.S.A. 85:7857-7861(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Structure, chromosome mapping and regulation of the mouse zinc-finger gene Krox-24; evidence for a common regulatory pathway for immediate-early serum-response genes."
Janssen-Timmen U., Lemaire P., Mattei M.-G., Revelant O., Charnay P.
Gene 80:325-336(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Two mouse genes encoding potential transcription factors with identical DNA-binding domains are activated by growth factors in cultured cells."
Lemaire P., Revelant O., Bravo R., Charnay P.
Proc. Natl. Acad. Sci. U.S.A. 85:4691-4695(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 50-533.
[5]"In vivo mutational analysis of the NGFI-A zinc fingers."
Wilson T.E., Day M.L., Pexton T., Padgett K.A., Johnston M., Milbrandt J.
J. Biol. Chem. 267:3718-3724(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ZINC-FINGERS.
[6]"Zinc finger-DNA recognition: crystal structure of a Zif268-DNA complex at 2.1 A."
Pavletich N.P., Pabo C.O.
Science 252:809-817(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 333-421.
[7]"High-resolution structures of variant Zif268-DNA complexes: implications for understanding zinc finger-DNA recognition."
Elrod-Erickson M., Benson T.E., Pabo C.O.
Structure 6:451-464(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 333-421 WITH VARIATIONS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M20157 mRNA. Translation: AAA37544.1.
M22326 mRNA. Translation: AAA40416.1.
M28845, M28844 Genomic DNA. Translation: AAB00468.1.
M19643 mRNA. Translation: AAA39382.1.
CCDSCCDS29136.1.
PIRJS0304.
RefSeqNP_031939.1. NM_007913.5.
UniGeneMm.181959.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A1FX-ray2.10A333-421[»]
1A1GX-ray1.90A333-421[»]
1A1HX-ray1.60A333-421[»]
1A1IX-ray1.60A333-421[»]
1A1JX-ray2.00A333-421[»]
1A1KX-ray1.90A333-421[»]
1A1LX-ray2.30A333-421[»]
1AAYX-ray1.60A333-421[»]
1F2IX-ray2.35G/H/I/J/K/L331-389[»]
1G2DX-ray2.20C/F333-421[»]
1G2FX-ray2.00C/F333-421[»]
1JK1X-ray1.90A333-421[»]
1JK2X-ray1.65A333-421[»]
1LLMX-ray1.50C/D364-412[»]
1P47X-ray2.20A/B333-419[»]
1ZAAX-ray2.10C332-418[»]
ProteinModelPortalP08046.
SMRP08046. Positions 334-453.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199404. 7 interactions.

PTM databases

PhosphoSiteP08046.

Proteomic databases

PRIDEP08046.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000064795; ENSMUSP00000069616; ENSMUSG00000038418.
ENSMUST00000165033; ENSMUSP00000126931; ENSMUSG00000038418.
GeneID13653.
KEGGmmu:13653.
UCSCuc008elt.1. mouse.

Organism-specific databases

CTD1958.
MGIMGI:95295. Egr1.

Phylogenomic databases

eggNOGCOG5048.
HOGENOMHOG000036856.
HOVERGENHBG003909.
InParanoidP08046.
KOK09203.
OMAAVTNSFS.
OrthoDBEOG7Z69C7.
PhylomeDBP08046.
TreeFamTF318980.

Gene expression databases

ArrayExpressP08046.
BgeeP08046.
CleanExMM_EGR1.
GenevestigatorP08046.

Family and domain databases

Gene3D3.30.160.60. 3 hits.
InterProIPR021839. DUF3432.
IPR021849. DUF3446.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamPF11914. DUF3432. 1 hit.
PF11928. DUF3446. 1 hit.
[Graphical view]
SMARTSM00355. ZnF_C2H2. 3 hits.
[Graphical view]
PROSITEPS00028. ZINC_FINGER_C2H2_1. 3 hits.
PS50157. ZINC_FINGER_C2H2_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP08046.
NextBio284384.
PROP08046.
SOURCESearch...

Entry information

Entry nameEGR1_MOUSE
AccessionPrimary (citable) accession number: P08046
Secondary accession number(s): Q61777
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: November 1, 1990
Last modified: July 9, 2014
This is version 149 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot