EGR2_PIG
ID EGR2_PIG Reviewed; 471 AA.
AC A1XSY8;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 94.
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;
GN Name=EGR2;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lung;
RA Yang H.W., Yang Z.Q.;
RT "Cloning, chromosome mapping and expression characteristics of porcine
RT KLF4, KLF5, KLF7 and EGR2.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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 -!- PTM: Ubiquitinated by WWP2 leading to proteasomal degradation.
CC {ECO:0000250|UniProtKB:P08152}.
CC -!- PTM: Acetylated at Lys-246. 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; DQ665829; ABG49107.1; -; mRNA.
DR RefSeq; NP_001090957.1; NM_001097488.1.
DR AlphaFoldDB; A1XSY8; -.
DR SMR; A1XSY8; -.
DR STRING; 9823.ENSSSCP00000010899; -.
DR PaxDb; A1XSY8; -.
DR PRIDE; A1XSY8; -.
DR Ensembl; ENSSSCT00000011190; ENSSSCP00000010899; ENSSSCG00000010224.
DR Ensembl; ENSSSCT00015000019; ENSSSCP00015000009; ENSSSCG00015000015.
DR Ensembl; ENSSSCT00025106300; ENSSSCP00025047689; ENSSSCG00025076671.
DR Ensembl; ENSSSCT00030001986; ENSSSCP00030000812; ENSSSCG00030001532.
DR Ensembl; ENSSSCT00035100914; ENSSSCP00035042903; ENSSSCG00035074333.
DR Ensembl; ENSSSCT00040085127; ENSSSCP00040037202; ENSSSCG00040062455.
DR Ensembl; ENSSSCT00045054904; ENSSSCP00045038266; ENSSSCG00045032102.
DR Ensembl; ENSSSCT00050095194; ENSSSCP00050040997; ENSSSCG00050069806.
DR Ensembl; ENSSSCT00055029550; ENSSSCP00055023524; ENSSSCG00055014946.
DR Ensembl; ENSSSCT00060044958; ENSSSCP00060019234; ENSSSCG00060033163.
DR Ensembl; ENSSSCT00065095440; ENSSSCP00065041762; ENSSSCG00065069508.
DR Ensembl; ENSSSCT00070022960; ENSSSCP00070018996; ENSSSCG00070011768.
DR GeneID; 100038004; -.
DR KEGG; ssc:100038004; -.
DR CTD; 1959; -.
DR VGNC; VGNC:103939; EGR2.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000158394; -.
DR HOGENOM; CLU_043235_0_0_1; -.
DR InParanoid; A1XSY8; -.
DR OrthoDB; 1318335at2759; -.
DR TreeFam; TF318980; -.
DR Reactome; R-SSC-9031628; NGF-stimulated transcription.
DR UniPathway; UPA00886; -.
DR Proteomes; UP000008227; Chromosome 14.
DR Proteomes; UP000314985; Chromosome 14.
DR Bgee; ENSSSCG00000010224; Expressed in granulosa cell and 28 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IEA:Ensembl.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0061665; F:SUMO ligase activity; IEA:Ensembl.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0035904; P:aorta development; IEA:Ensembl.
DR GO; GO:0035284; P:brain segmentation; IEA:Ensembl.
DR GO; GO:0071310; P:cellular response to organic substance; IEA:Ensembl.
DR GO; GO:0021612; P:facial nerve structural organization; ISS:UniProtKB.
DR GO; GO:0045444; P:fat cell differentiation; IEA:Ensembl.
DR GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR GO; GO:0008045; P:motor neuron axon guidance; IEA:Ensembl.
DR GO; GO:0042552; P:myelination; IEA:Ensembl.
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:0030278; P:regulation of ossification; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0021660; P:rhombomere 3 formation; IEA:Ensembl.
DR GO; GO:0021659; P:rhombomere 3 structural organization; ISS:UniProtKB.
DR GO; GO:0021666; P:rhombomere 5 formation; IEA:Ensembl.
DR GO; GO:0021665; P:rhombomere 5 structural organization; ISS:UniProtKB.
DR GO; GO:0007622; P:rhythmic behavior; IEA:Ensembl.
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; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Transferase; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..471
FT /note="E3 SUMO-protein ligase EGR2"
FT /id="PRO_0000296388"
FT ZN_FING 335..359
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 365..387
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 393..415
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 127..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 246
FT /note="N6-acetyllysine; by EP300"
FT /evidence="ECO:0000250|UniProtKB:P08152"
SQ SEQUENCE 471 AA; 49911 MW; 9C073404B9EB86A0 CRC64;
MMTAKAVDKI PVTLSGFVHQ LSDNIYPVED LAATSVTIFP NAELGSPFDQ MNGVAGDGMI
NIDMTGEKRS LDLPYPSSFA PVSAPRNQTF TYMGKFSIDP QYPGASCYPE GIINIVSAGI
LQGVTSPAST TASSNVTSAS PNPLATGPLG VCTMSQTQPD LDHLYSPPPP PPYSGCAGDL
YQDPSAFLSA ATTSTSSSLA YPPPPSYPSP KPATDPGLFP MIPDYPGFFP SQCQRDLHGT
AGPDRKPFPC PLDSLRVPPP LTPLSTIRNF TLGGPSAGTT GPGASGGSEG PRLPGSSAAA
AAAAYNPHHL PLRPILRPRK YPNRPSKTPV HERPYPCPAE GCDRRFSRSD ELTRHIRIHT
GHKPFQCRIC MRNFSRSDHL TTHIRTHTGE KPFACDYCGR KFARSDERKR HTKIHLRQKE
RKSSAPSSSV PAASTASCTG GAQPGGPLCS SNSSTIGGGS LGPCSSRTRT P
