EGR2_RAT
ID EGR2_RAT Reviewed; 470 AA.
AC P51774; Q54AG4;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=E3 SUMO-protein ligase EGR2;
DE EC=2.3.2.- {ECO:0000250|UniProtKB:P11161};
DE AltName: Full=E3 SUMO-protein transferase ERG2 {ECO:0000305};
DE AltName: Full=Early growth response protein 2;
DE Short=EGR-2;
DE AltName: Full=Zinc finger protein Krox-20;
GN Name=Egr2; Synonyms=Egr-2, Krox-20, Krox20;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Zaharic T., Durtschi B.A., Mason-Parker S.E., Abraham W.C., Tate W.P.;
RT "cDNA for rat krox20.";
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
RC STRAIN=Wistar; TISSUE=Hippocampus;
RX PubMed=8619872; DOI=10.1006/bbrc.1996.0612;
RA Inokuchi K., Murayama A., Ozawa F.;
RT "mRNA differential display reveals Krox-20 as a neural plasticity-regulated
RT gene in the rat hippocampus.";
RL Biochem. Biophys. Res. Commun. 221:430-436(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
RC STRAIN=Sprague-Dawley;
RX PubMed=10970821; DOI=10.1165/ajrcmb.23.3.4112;
RA Hirano S., Anuradha C.D., Kanno S.;
RT "Transcription of krox-20/egr-2 is upregulated after exposure to fibrous
RT particles and adhesion in rat alveolar macrophages.";
RL Am. J. Respir. Cell Mol. Biol. 23:313-319(2000).
CC -!- FUNCTION: Sequence-specific DNA-binding transcription factor (By
CC similarity). Plays a role in hindbrain segmentation by regulating the
CC expression of a subset of homeobox containing genes and in Schwann cell
CC myelination by regulating the expression of genes involved in the
CC formation and maintenance of myelin (By similarity). Binds to two EGR2-
CC consensus sites EGR2A (5'-CTGTAGGAG-3') and EGR2B (5'-ATGTAGGTG-3') in
CC the HOXB3 enhancer and promotes HOXB3 transcriptional activation (By
CC similarity). Binds to specific DNA sites located in the promoter region
CC of HOXA4, HOXB2 and ERBB2 (By similarity). Regulates hindbrain
CC segmentation by controlling the expression of Hox genes, such as HOXA4,
CC HOXB3 and HOXB2, and thereby specifying odd and even rhombomeres (By
CC similarity). Promotes the expression of HOXB3 in the rhombomere r5 in
CC the hindbrain (By similarity). Regulates myelination in the peripheral
CC nervous system after birth, possibly by regulating the expression of
CC myelin proteins, such as MPZ, and by promoting the differentiation of
CC Schwann cells (By similarity). Involved in the development of the jaw
CC openener musculature, probably by playing a role in its innervation
CC through trigeminal motor neurons (By similarity). May play a role in
CC adipogenesis, possibly by regulating the expression of CEBPB (By
CC similarity). {ECO:0000250|UniProtKB:P08152}.
CC -!- FUNCTION: E3 SUMO-protein ligase helping SUMO1 conjugation to its
CC coregulators NAB1 and NAB2, whose sumoylation down-regulates EGR2
CC transcriptional activity. {ECO:0000250|UniProtKB:P11161}.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC -!- SUBUNIT: Interacts with HCFC1 (By similarity). Interacts with WWP2 (By
CC similarity). Interacts with UBC9 (By similarity). Interacts with CITED1
CC (By similarity). Interacts (via phosphorylated form) with SFN (By
CC similarity). {ECO:0000250|UniProtKB:P08152,
CC ECO:0000250|UniProtKB:P11161}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P08152}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=P51774-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P51774-2; Sequence=VSP_006865;
CC -!- PTM: Ubiquitinated by WWP2 leading to proteasomal degradation.
CC {ECO:0000250|UniProtKB:P08152}.
CC -!- PTM: Acetylated at Lys-247. May be deacetylated by HDAC6, HDAC10 or
CC SIRT1. {ECO:0000250|UniProtKB:P08152}.
CC -!- SIMILARITY: Belongs to the EGR C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
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DR EMBL; U78102; AAB36783.1; -; mRNA.
DR EMBL; D83508; BAA11932.1; -; mRNA.
DR EMBL; AB032420; BAA89319.1; -; mRNA.
DR PIR; JC4716; JC4716.
DR RefSeq; NP_446085.1; NM_053633.1. [P51774-1]
DR RefSeq; XP_017457019.1; XM_017601530.1. [P51774-2]
DR AlphaFoldDB; P51774; -.
DR SMR; P51774; -.
DR STRING; 10116.ENSRNOP00000000792; -.
DR PaxDb; P51774; -.
DR Ensembl; ENSRNOT00000000792; ENSRNOP00000000792; ENSRNOG00000000640. [P51774-1]
DR GeneID; 114090; -.
DR KEGG; rno:114090; -.
DR UCSC; RGD:621608; rat. [P51774-1]
DR CTD; 1959; -.
DR RGD; 621608; Egr2.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000158394; -.
DR HOGENOM; CLU_043235_0_0_1; -.
DR InParanoid; P51774; -.
DR OMA; PQCQREL; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; P51774; -.
DR TreeFam; TF318980; -.
DR Reactome; R-RNO-9031628; NGF-stimulated transcription.
DR UniPathway; UPA00886; -.
DR PRO; PR:P51774; -.
DR Proteomes; UP000002494; Chromosome 20.
DR Bgee; ENSRNOG00000000640; Expressed in thymus and 13 other tissues.
DR Genevisible; P51774; RN.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISO:RGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISS:UniProtKB.
DR GO; GO:0071837; F:HMG box domain binding; IPI:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:RGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR GO; GO:0061665; F:SUMO ligase activity; ISO:RGD.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR GO; GO:0035904; P:aorta development; ISO:RGD.
DR GO; GO:0035284; P:brain segmentation; ISO:RGD.
DR GO; GO:0071310; P:cellular response to organic substance; ISO:RGD.
DR GO; GO:0021612; P:facial nerve structural organization; ISS:UniProtKB.
DR GO; GO:0045444; P:fat cell differentiation; ISO:RGD.
DR GO; GO:0010467; P:gene expression; ISO:RGD.
DR GO; GO:0007611; P:learning or memory; IEP:RGD.
DR GO; GO:0008045; P:motor neuron axon guidance; ISO:RGD.
DR GO; GO:0042552; P:myelination; ISO:RGD.
DR GO; GO:0031643; P:positive regulation of myelination; ISS:UniProtKB.
DR GO; GO:0014040; P:positive regulation of Schwann cell differentiation; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006611; P:protein export from nucleus; ISS:UniProtKB.
DR GO; GO:0016925; P:protein sumoylation; ISO:RGD.
DR GO; GO:0048168; P:regulation of neuronal synaptic plasticity; IEP:RGD.
DR GO; GO:0030278; P:regulation of ossification; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0032868; P:response to insulin; IMP:RGD.
DR GO; GO:0021569; P:rhombomere 3 development; ISO:RGD.
DR GO; GO:0021660; P:rhombomere 3 formation; ISO:RGD.
DR GO; GO:0021659; P:rhombomere 3 structural organization; ISS:UniProtKB.
DR GO; GO:0021666; P:rhombomere 5 formation; ISO:RGD.
DR GO; GO:0021665; P:rhombomere 5 structural organization; ISS:UniProtKB.
DR GO; GO:0007622; P:rhythmic behavior; ISO:RGD.
DR GO; GO:0014037; P:Schwann cell differentiation; ISS:UniProtKB.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; ISS:UniProtKB.
DR InterPro; IPR021849; EGR_N.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF11928; DUF3446; 1.
DR Pfam; PF00096; zf-C2H2; 3.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 2: Evidence at transcript level;
KW Acetylation; Activator; Alternative splicing; DNA-binding; Metal-binding;
KW Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..470
FT /note="E3 SUMO-protein ligase EGR2"
FT /id="PRO_0000047121"
FT ZN_FING 337..361
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 367..389
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 395..417
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 126..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 159..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 275..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 247
FT /note="N6-acetyllysine; by EP300"
FT /evidence="ECO:0000250|UniProtKB:P08152"
FT VAR_SEQ 1..50
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:8619872"
FT /id="VSP_006865"
SQ SEQUENCE 470 AA; 49849 MW; 2B28185752A91F76 CRC64;
MMTAKAVDKI PVTLSGFMHQ LPDSLYPVED LAAPSVTIFP NGELGGPFDQ MNGVAGDGMI
NIDMTGEKRP LDLPYPSSFA PISAPRNQTF TYMGKFSIDP QYPGASCYPE GIINIVSAGI
LQGVTPPAST TASSSVTSAS PNPLATGPLG VCTMSQTQPE LDHLYSPPPP PPPYSGCTGD
LYQDPSAFLS PPPTTSTSSL AYQPPPSYPS PKPAMDPGLI PMIPDYPGFF PSPCQRDPHG
AAGPDRKPFP CPLDSLRVPP PLTPLSTIRN FTLGGPSAGV TGPGASGGGE GPRLPGSGSA
AVTATPYNPH HLPLRPILRP RKYPNRPSKT PVHERPYPCP AEGCDRRFSR SDELTRHIRI
HTGHKPFQCR ICMRNFSRSD HLTTHIRTHT GEKPFACDYC GRKFARSDER KRHTKIHLRQ
KERKSSAPSS SASAQSSASG PGGSQAGGSL CGNSAIGGPL ASCTSRTRTP
