Early growth response protein 1 - Mus musculus (Mouse)

Contribute

Send feedback

Read comments (?) or add your own

P08046 (EGR1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 138. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	533 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Transcription Transcription regulation
Cellular component	Nucleus
Domain	Repeat Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Activator
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	BMP 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: Compara cellular response to cAMP Inferred from electronic annotation. Source: Compara cellular response to drug Inferred from electronic annotation. Source: Compara cellular response to follicle-stimulating hormone stimulus Inferred from electronic annotation. Source: Compara cellular response to gamma radiation Inferred from mutant phenotype PubMed 19057511. Source: BHF-UCL cellular response to growth factor stimulus Inferred from electronic annotation. Source: Compara cellular response to heparin Inferred from sequence or structural similarity. Source: UniProtKB cellular response to hyperoxia Inferred from electronic annotation. Source: Compara cellular response to hypoxia Inferred from electronic annotation. Source: Compara cellular response to insulin stimulus Inferred from electronic annotation. Source: Compara cellular response to isoquinoline alkaloid Inferred from electronic annotation. Source: Compara cellular response to mechanical stimulus Inferred from electronic annotation. Source: Compara cellular response to mycophenolic acid Inferred from sequence or structural similarity. Source: UniProtKB cellular response to steroid hormone stimulus Inferred from electronic annotation. Source: Compara circadian rhythm Inferred from electronic annotation. Source: Compara glomerular mesangial cell proliferation Inferred from sequence or structural similarity. Source: UniProtKB interleukin-1-mediated signaling pathway Inferred from electronic annotation. Source: Compara learning or memory Inferred from electronic annotation. Source: Compara long-term synaptic potentiation Inferred from electronic annotation. Source: Compara negative regulation of canonical Wnt receptor 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: Compara 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: Compara positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay PubMed 20018936. Source: BHF-UCL regulation of long-term neuronal synaptic plasticity Inferred from electronic annotation. Source: Compara regulation of protein sumoylation Inferred from electronic annotation. Source: Compara response to amphetamine Inferred from electronic annotation. Source: Compara response to carbon monoxide Inferred from electronic annotation. Source: Compara response to cocaine Inferred from electronic annotation. Source: Compara response to electrical stimulus Inferred from electronic annotation. Source: Compara response to ethanol Inferred from electronic annotation. Source: Compara response to glucose stimulus Inferred from direct assay PubMed 12689920. Source: UniProtKB response to insulin stimulus Inferred from direct assay PubMed 12689920. Source: UniProtKB response to norepinephrine stimulus Inferred from electronic annotation. Source: Compara response to nutrient levels Inferred from electronic annotation. Source: Compara skeletal muscle cell differentiation Inferred from mutant phenotype PubMed 22147266. Source: MGI
Cellular_component	cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB nucleus Inferred from direct assay PubMed 12689920. Source: UniProtKB
Molecular_function	RNA 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: Compara RNA polymerase II core promoter sequence-specific DNA binding Inferred from electronic annotation. Source: Compara double-stranded DNA binding Inferred from electronic annotation. Source: Compara transcription regulatory region DNA binding Inferred from direct assay PubMed 18281035. Source: BHF-UCL zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 533

533

Early growth response protein 1

PRO_0000047110

Regions

Zinc finger

336 – 360

C2H2-type 1

Zinc finger

366 – 388

C2H2-type 2

Zinc finger

394 – 416

C2H2-type 3

Compositional bias

57 – 81

Gly/Ser-rich

Experimental info

Sequence conflict

S → T Ref.3

Sequence conflict

S → T Ref.4

Sequence conflict

S → T Ref.3

Sequence conflict

S → T Ref.4

Secondary structure

533

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P08046 [UniParc].

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

FASTA

533

56,590

        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.

IPI

IPI00128530.

PIR

JS0304.

RefSeq

NP_031939.1. NM_007913.5.

UniGene

Mm.181959.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A1F	X-ray	2.10	A	333-421	[»]
1A1G	X-ray	1.90	A	333-421	[»]
1A1H	X-ray	1.60	A	333-421	[»]
1A1I	X-ray	1.60	A	333-421	[»]
1A1J	X-ray	2.00	A	333-421	[»]
1A1K	X-ray	1.90	A	333-421	[»]
1A1L	X-ray	2.30	A	333-421	[»]
1AAY	X-ray	1.60	A	333-421	[»]
1F2I	X-ray	2.35	G/H/I/J/K/L	334-389	[»]
1G2D	X-ray	2.20	C/F	333-421	[»]
1G2F	X-ray	2.00	C/F	333-421	[»]
1JK1	X-ray	1.90	A	333-421	[»]
1JK2	X-ray	1.65	A	333-421	[»]
1LLM	X-ray	1.50	C/D	364-412	[»]
1P47	X-ray	2.20	A/B	333-419	[»]
1ZAA	X-ray	2.10	C	332-418	[»]

ProteinModelPortal

P08046.

SMR

P08046. Positions 334-453.

ModBase

Search...

PTM databases

PhosphoSite

P08046.

Proteomic databases

PRIDE

P08046.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000064795; ENSMUSP00000069616; ENSMUSG00000038418.
ENSMUST00000165033; ENSMUSP00000126931; ENSMUSG00000038418.

GeneID

13653.

KEGG

mmu:13653.

Organism-specific databases

CTD

1958.

MGI

MGI:95295. Egr1.

Phylogenomic databases

eggNOG

COG5048.

HOGENOM

HOG000036856.

HOVERGEN

HBG003909.

InParanoid

P08046.

K09203.

OMA

PFGSFPH.

OrthoDB

EOG4BP1BT.

Gene expression databases

ArrayExpress

P08046.

Bgee

P08046.

CleanEx

MM_EGR1.

Genevestigator

P08046.

GermOnline

ENSMUSG00000038418. Mus musculus.

Family and domain databases

Gene3D

3.30.160.60. 3 hits.

InterPro

IPR021839. DUF3432.
IPR021849. DUF3446.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]

Pfam

PF11914. DUF3432. 1 hit.
PF11928. DUF3446. 1 hit.
[Graphical view]

SMART

SM00355. ZnF_C2H2. 3 hits.
[Graphical view]

PROSITE

PS00028. ZINC_FINGER_C2H2_1. 3 hits.
PS50157. ZINC_FINGER_C2H2_2. 3 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P08046.

NextBio

284384.

SOURCE

Search...

Entry information

Entry name

EGR1_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 138 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents