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Early growth response protein 1 (EGR-1) (Nerve growth factor-induced protein A) (NGFI-A) (Transcription factor Zif268) (Zinc finger protein Krox-24)

 EGR1_RAT                Reviewed;         508 AA.
P08154; Q53YM5;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
01-JAN-1990, sequence version 2.
22-NOV-2017, entry version 144.
RecName: Full=Early growth response protein 1;
Short=EGR-1;
AltName: Full=Nerve growth factor-induced protein A {ECO:0000303|PubMed:2492104};
Short=NGFI-A {ECO:0000303|PubMed:2492104};
AltName: Full=Transcription factor Zif268;
AltName: Full=Zinc finger protein Krox-24;
Name=Egr1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3672127; DOI=10.1126/science.3672127;
Milbrandt J.;
"A nerve growth factor-induced gene encodes a possible transcriptional
regulatory factor.";
Science 238:797-799(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION BY GROWTH FACTORS.
PubMed=2492104; DOI=10.1073/pnas.86.1.377;
Changelian P.S., Feng P., King T.C., Milbrandt J.;
"Structure of the NGFI-A gene and detection of upstream sequences
responsible for its transcriptional induction by nerve growth
factor.";
Proc. Natl. Acad. Sci. U.S.A. 86:377-381(1989).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Midbrain;
Ju S.K.;
"Cloning and sequencing of cDNA encoding EGR1 from rat.";
Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
[4]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION BY ISCHEMIA.
PubMed=1859855;
Bonventre J.V., Sukhatme V.P., Bamberger M., Ouellette A.J., Brown D.;
"Localization of the protein product of the immediate early growth
response gene, Egr-1, in the kidney after ischemia and reperfusion.";
Cell Regul. 2:251-260(1991).
[5]
FUNCTION, AND MUTAGENESIS OF ILE-265.
PubMed=8413279; DOI=10.1128/MCB.13.11.6858;
Russo M.W., Matheny C., Milbrandt J.;
"Transcriptional activity of the zinc finger protein NGFI-A is
influenced by its interaction with a cellular factor.";
Mol. Cell. Biol. 13:6858-6865(1993).
-!- FUNCTION: Transcriptional regulator (PubMed:8413279). Recognizes
and binds to the DNA sequence 5'-GCG(T/G)GGGCG-3'(EGR-site) in the
promoter region of target genes (By similarity). Binds double-
stranded target DNA, irrespective of the cytosine methylation
status (By similarity). Regulates the transcription of numerous
target genes, and thereby plays an important role in regulating
the response to growth factors, DNA damage, and ischemia. Plays a
role in the regulation of cell survival, proliferation and cell
death. Activates expression of p53/TP53 and TGFB1, and thereby
helps prevent tumor formation. Required for normal progress
through mitosis and normal proliferation of hepatocytes after
partial hepatectomy. Mediates responses to ischemia and hypoxia;
regulates the expression of proteins such as IL1B and CXCL2 that
are involved in inflammatory processes and development of tissue
damage after ischemia. Regulates biosynthesis of luteinizing
hormone (LHB) in the pituitary (By similarity).
{ECO:0000250|UniProtKB:P08046, ECO:0000250|UniProtKB:P18146,
ECO:0000269|PubMed:8413279}.
-!- SUBUNIT: Interacts with SNAI1 and SP1 upon 12-O-
tetradecanoylphorbol-13-acetate (TPA) induction.
{ECO:0000250|UniProtKB:P18146}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:1859855}.
Cytoplasm {ECO:0000250|UniProtKB:P18146}.
-!- TISSUE SPECIFICITY: Detected in kidney thick ascending limbs and
collecting ducts (at protein level). {ECO:0000269|PubMed:1859855}.
-!- INDUCTION: By growth factors (PubMed:2492104). Rapidly and
transiently up-regulated in response to oschemia (PubMed:1859855).
{ECO:0000269|PubMed:1859855, ECO:0000269|PubMed:2492104}.
-!- DOMAIN: Binds to DNA motifs with the sequence 5'-GCG(T/G)GGGCG-3'
via its C2H2-type zinc fingers. The first, most N-terminal zinc
finger binds to the 3'-GCG motif, the middle zinc finger interacts
with the central TGG motif, and the C-terminal zinc finger binds
to the 5'-GCG motif. Binds double-stranded target DNA,
irrespective of the cytosine methylation status. Has reduced
affinity for target DNA where the cytosines have been oxidized to
5-hydroxymethylcytosine. Does not bind target DNA where the
cytosines have been oxidized to 5-formylcytosine or 5-
carboxylcytosine. {ECO:0000250|UniProtKB:P18146}.
-!- SIMILARITY: Belongs to the EGR C2H2-type zinc-finger protein
family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M18416; AAA61927.1; -; mRNA.
EMBL; J04154; AAA60740.1; -; Genomic_DNA.
EMBL; AY551092; AAS58455.1; -; mRNA.
PIR; A32225; A32225.
RefSeq; NP_036683.1; NM_012551.2.
UniGene; Rn.9096; -.
ProteinModelPortal; P08154; -.
SMR; P08154; -.
STRING; 10116.ENSRNOP00000026303; -.
PhosphoSitePlus; P08154; -.
PaxDb; P08154; -.
GeneID; 24330; -.
KEGG; rno:24330; -.
UCSC; RGD:2544; rat.
CTD; 1958; -.
RGD; 2544; Egr1.
eggNOG; KOG1721; Eukaryota.
eggNOG; COG5048; LUCA.
HOGENOM; HOG000036856; -.
HOVERGEN; HBG003909; -.
InParanoid; P08154; -.
KO; K09203; -.
OrthoDB; EOG091G06VX; -.
PhylomeDB; P08154; -.
PRO; PR:P08154; -.
Proteomes; UP000002494; Unplaced.
Genevisible; P08154; RN.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; ISO:RGD.
GO; GO:0003690; F:double-stranded DNA binding; IDA:RGD.
GO; GO:0010385; F:double-stranded methylated DNA binding; ISO:RGD.
GO; GO:0044729; F:hemi-methylated DNA-binding; ISO:RGD.
GO; GO:0035035; F:histone acetyltransferase binding; ISO:RGD.
GO; GO:1990841; F:promoter-specific chromatin binding; IDA:RGD.
GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IDA:RGD.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:RGD.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD.
GO; GO:0000982; F:transcription factor activity, RNA polymerase II core promoter proximal region sequence-specific binding; ISO:RGD.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IMP:RGD.
GO; GO:0008134; F:transcription factor binding; IPI:RGD.
GO; GO:0044212; F:transcription regulatory region DNA binding; ISO:RGD.
GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; ISO:RGD.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:RGD.
GO; GO:0008270; F:zinc ion binding; ISO:RGD.
GO; GO:0030509; P:BMP signaling pathway; ISO:RGD.
GO; GO:0071236; P:cellular response to antibiotic; IEP:RGD.
GO; GO:0071320; P:cellular response to cAMP; IEP:RGD.
GO; GO:0035690; P:cellular response to drug; IEP:RGD.
GO; GO:0071372; P:cellular response to follicle-stimulating hormone stimulus; IEP:RGD.
GO; GO:0071480; P:cellular response to gamma radiation; ISO:RGD.
GO; GO:0071371; P:cellular response to gonadotropin stimulus; IEP:RGD.
GO; GO:0071363; P:cellular response to growth factor stimulus; IEP:RGD.
GO; GO:0071504; P:cellular response to heparin; IDA:UniProtKB.
GO; GO:0071455; P:cellular response to hyperoxia; IEP:RGD.
GO; GO:0071456; P:cellular response to hypoxia; IEP:RGD.
GO; GO:0032869; P:cellular response to insulin stimulus; IEP:RGD.
GO; GO:0098759; P:cellular response to interleukin-8; ISS:UniProtKB.
GO; GO:0071317; P:cellular response to isoquinoline alkaloid; IEP:RGD.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:RGD.
GO; GO:0071506; P:cellular response to mycophenolic acid; IDA:UniProtKB.
GO; GO:0071310; P:cellular response to organic substance; ISO:RGD.
GO; GO:0071383; P:cellular response to steroid hormone stimulus; IEP:RGD.
GO; GO:0007623; P:circadian rhythm; IEP:RGD.
GO; GO:0044849; P:estrous cycle; ISS:UniProtKB.
GO; GO:0072110; P:glomerular mesangial cell proliferation; IMP:UniProtKB.
GO; GO:0070498; P:interleukin-1-mediated signaling pathway; ISO:RGD.
GO; GO:0007611; P:learning or memory; IMP:RGD.
GO; GO:0007616; P:long-term memory; IMP:RGD.
GO; GO:0060291; P:long-term synaptic potentiation; IEP:RGD.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISO:RGD.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISO:RGD.
GO; GO:0048709; P:oligodendrocyte differentiation; IEP:RGD.
GO; GO:0010942; P:positive regulation of cell death; IMP:RGD.
GO; GO:0045080; P:positive regulation of chemokine biosynthetic process; ISS:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; IMP:RGD.
GO; GO:0072303; P:positive regulation of glomerular metanephric mesangial cell proliferation; IMP:UniProtKB.
GO; GO:0046886; P:positive regulation of hormone biosynthetic process; ISS:UniProtKB.
GO; GO:0050725; P:positive regulation of interleukin-1 beta biosynthetic process; ISS:UniProtKB.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IMP:RGD.
GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IMP:RGD.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IMP:RGD.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:RGD.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:RGD.
GO; GO:0042981; P:regulation of apoptotic process; ISO:RGD.
GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IMP:RGD.
GO; GO:2000182; P:regulation of progesterone biosynthetic process; ISS:UniProtKB.
GO; GO:0033233; P:regulation of protein sumoylation; ISO:RGD.
GO; GO:0061418; P:regulation of transcription from RNA polymerase II promoter in response to hypoxia; ISO:RGD.
GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:RGD.
GO; GO:0001975; P:response to amphetamine; IEP:RGD.
GO; GO:0034465; P:response to carbon monoxide; IEP:RGD.
GO; GO:0042220; P:response to cocaine; IEP:RGD.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0051602; P:response to electrical stimulus; IEP:RGD.
GO; GO:0045471; P:response to ethanol; IEP:RGD.
GO; GO:0032354; P:response to follicle-stimulating hormone; IEP:RGD.
GO; GO:0009749; P:response to glucose; ISO:RGD.
GO; GO:0034698; P:response to gonadotropin; IEP:RGD.
GO; GO:0001666; P:response to hypoxia; ISS:UniProtKB.
GO; GO:0032868; P:response to insulin; ISO:RGD.
GO; GO:0002931; P:response to ischemia; IDA:UniProtKB.
GO; GO:0071873; P:response to norepinephrine; IEP:RGD.
GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
GO; GO:0035914; P:skeletal muscle cell differentiation; ISO:RGD.
GO; GO:0030217; P:T cell differentiation; ISO:RGD.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; ISO:RGD.
GO; GO:0042060; P:wound healing; IEP:RGD.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR021849; EGR.
InterPro; IPR021839; EGR1_C.
InterPro; IPR036236; Znf_C2H2_sf.
InterPro; IPR013087; Znf_C2H2_type.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
Pfam; PF11914; DUF3432; 1.
Pfam; PF11928; DUF3446; 1.
SMART; SM00355; ZnF_C2H2; 3.
SUPFAM; SSF57667; SSF57667; 2.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
1: Evidence at protein level;
Activator; Complete proteome; Cytoplasm; DNA-binding; Isopeptide bond;
Metal-binding; Nucleus; Reference proteome; Repeat; Transcription;
Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 508 Early growth response protein 1.
/FTId=PRO_0000047111.
REPEAT 413 420 1.
REPEAT 421 428 2.
REPEAT 429 436 3.
REPEAT 437 444 4.
REPEAT 445 452 5.
REPEAT 453 460 6.
REPEAT 462 468 7.
ZN_FING 311 335 C2H2-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 341 363 C2H2-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 369 391 C2H2-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
REGION 413 468 7 X 8 AA tandem repeats of [TS](2)-[FY]-
[PS]-S-P-[GSAV]-X.
COMPBIAS 29 56 Gly/Ser-rich.
SITE 309 309 Interaction with DNA.
{ECO:0000250|UniProtKB:P18146}.
SITE 320 320 Interaction with DNA.
{ECO:0000250|UniProtKB:P08046}.
SITE 324 324 Interaction with DNA.
{ECO:0000250|UniProtKB:P08046}.
SITE 330 330 Interaction with DNA.
{ECO:0000250|UniProtKB:P18146}.
SITE 348 348 Interaction with DNA.
{ECO:0000250|UniProtKB:P08046}.
SITE 352 352 Interaction with DNA.
{ECO:0000250|UniProtKB:P18146}.
SITE 376 376 Interaction with DNA.
{ECO:0000250|UniProtKB:P18146}.
SITE 380 380 Interaction with DNA.
{ECO:0000250|UniProtKB:P18146}.
SITE 386 386 Interaction with DNA.
{ECO:0000250|UniProtKB:P18146}.
CROSSLNK 278 278 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P18146}.
MUTAGEN 265 265 I->F: Increases transcriptional activity.
{ECO:0000269|PubMed:8413279}.
SEQUENCE 508 AA; 53935 MW; 3947BBA871BB8FA8 CRC64;
MDNYPKLEEM MLLSNGAPQF LGAAGTPEGS GGNNSSSSSS SSSGGGGGGG SNSGSSAFNP
QGEPSEQPYE HLTTESFSDI ALNNEKALVE TSYPSQTTRL PPITYTGRFS LEPAPNSGNT
LWPEPLFSLV SGLVSMTNPP TSSSSAPSPA ASSSSSASQS PPLSCAVPSN DSSPIYSAAP
TFPTPNTDIF PEPQSQAFPG SAGTALQYPP PAYPATKGGF QVPMIPDYLF PQQQGDLSLG
TPDQKPFQGL ENRTQQPSLT PLSTIKAFAT QSGSQDLKAL NNTYQSQLIK PSRMRKYPNR
PSKTPPHERP YACPVESCDR RFSRSDELTR HIRIHTGQKP FQCRICMRNF SRSDHLTTHI
RTHTGEKPFA CDICGRKFAR SDERKRHTKI HLRQKDKKAD KSVVASSAAS SLSSYPSPVA
TSYPSPATTS FPSPVPTSYS SPGSSTYPSP AHSGFPSPSV ATTYASVPPA FPAQVSTFQS
AGVSNSFSTS TGLSDMTATF SPRTIEIC


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