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E3 SUMO-protein ligase EGR2 (EC 6.3.2.-) (Early growth response protein 2) (EGR-2) (Zinc finger protein Krox-20)

 EGR2_MOUSE              Reviewed;         470 AA.
P08152;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 3.
22-NOV-2017, entry version 173.
RecName: Full=E3 SUMO-protein ligase EGR2;
EC=6.3.2.-;
AltName: Full=Early growth response protein 2;
Short=EGR-2;
AltName: Full=Zinc finger protein Krox-20;
Name=Egr2; Synonyms=Egr-2, Krox-20, Zfp-25;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS LONG AND SHORT).
PubMed=2496302; DOI=10.1128/MCB.9.2.787;
Chavrier P., Janssen-Timmen U., Mattei M.-G., Zerial M., Bravo R.,
Charnay P.;
"Structure, chromosome location, and expression of the mouse zinc
finger gene Krox-20: multiple gene products and coregulation with the
proto-oncogene c-fos.";
Mol. Cell. Biol. 9:787-797(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
PubMed=3129290;
Chavrier P., Zerial M., Lemaire P., Almendral J., Bravo R.,
Charnay P.;
"A gene encoding a protein with zinc fingers is activated during G0/G1
transition in cultured cells.";
EMBO J. 7:29-35(1988).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
STRAIN=FVB/N; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 339-417.
PubMed=2452975; DOI=10.1128/MCB.8.3.1319;
Chavrier P., Lemaire P., Revelant O., Bravo R., Charnay P.;
"Characterization of a mouse multigene family that encodes zinc finger
structures.";
Mol. Cell. Biol. 8:1319-1326(1988).
[5]
FUNCTION.
PubMed=1969796;
Chavrier P., Vesque C., Galliot B., Vigneron M., Dolle P., Duboule D.,
Charnay P.;
"The segment-specific gene Krox-20 encodes a transcription factor with
binding sites in the promoter region of the Hox-1.4 gene.";
EMBO J. 9:1209-1218(1990).
[6]
FUNCTION.
PubMed=1674431; DOI=10.1016/0300-9084(91)90079-G;
Gilardi P., Schneider-Maunoury S., Charnay P.;
"Krox-20: a candidate gene for the regulation of pattern formation in
the hindbrain.";
Biochimie 73:85-91(1991).
[7]
DOMAINS.
PubMed=1598206; DOI=10.1093/nar/20.10.2485;
Vesque C., Charnay P.;
"Mapping functional regions of the segment-specific transcription
factor Krox-20.";
Nucleic Acids Res. 20:2485-2492(1992).
[8]
FUNCTION, INTERACTION WITH CITED1 AND SFN, MUTAGENESIS OF SER-377,
DNA-BINDING, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=17938205; DOI=10.1128/MCB.00866-07;
Dillon R.L., Brown S.T., Ling C., Shioda T., Muller W.J.;
"An EGR2/CITED1 transcription factor complex and the 14-3-3sigma tumor
suppressor are involved in regulating ErbB2 expression in a
transgenic-mouse model of human breast cancer.";
Mol. Cell. Biol. 27:8648-8657(2007).
[9]
UBIQUITINATION, INTERACTION WITH WWP2, AND MUTAGENESIS OF TYR-174 AND
TYR-208.
PubMed=19651900; DOI=10.1128/MCB.00407-09;
Chen A., Gao B., Zhang J., McEwen T., Ye S.Q., Zhang D., Fang D.;
"The HECT-type E3 ubiquitin ligase AIP2 inhibits activation-induced T-
cell death by catalyzing EGR2 ubiquitination.";
Mol. Cell. Biol. 29:5348-5356(2009).
-!- FUNCTION: Sequence-specific DNA-binding transcription factor.
Binds to two specific DNA sites located in the promoter region of
HOXA4. Binds to the promoter region of ERBB2. May play a role in
the regulation of hindbrain segmentation, might act in combination
with the Hox network to specify odd and even rhombomeres, and
might participate in the control of the expression of some of the
homeobox containing genes. {ECO:0000269|PubMed:1674431,
ECO:0000269|PubMed:17938205, ECO:0000269|PubMed:1969796}.
-!- FUNCTION: E3 SUMO-protein ligase helping SUMO1 conjugation to its
coregulators NAB1 and NAB2, whose sumoylation down-regulates EGR2
own transcriptional activity. {ECO:0000250}.
-!- PATHWAY: Protein modification; protein sumoylation.
-!- SUBUNIT: Interacts with HCFC1. Interacts with UBC9 (By
similarity). Interacts with WWP2. Interacts with CITED1. Interacts
(via phosphorylated form) with SFN. {ECO:0000250,
ECO:0000269|PubMed:17938205, ECO:0000269|PubMed:19651900}.
-!- INTERACTION:
Q8C5D8-1:Pias2; NbExp=5; IntAct=EBI-7070449, EBI-8064899;
P63280:Ube2i; NbExp=2; IntAct=EBI-7070449, EBI-80180;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17938205}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Long;
IsoId=P08152-1; Sequence=Displayed;
Name=Short;
IsoId=P08152-2; Sequence=VSP_006864;
-!- TISSUE SPECIFICITY: Expressed in mammary tumors (at protein
level). Expressed mainly in adult thymus and embryonic nervous
system. {ECO:0000269|PubMed:17938205}.
-!- INDUCTION: Activated during G0/G1 transition in cultured cells.
-!- PTM: Ubiquitinated by WWP2 leading to proteasomal degradation.
{ECO:0000269|PubMed:19651900}.
-!- SIMILARITY: Belongs to the EGR C2H2-type zinc-finger protein
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M24377; AAA39379.1; -; Genomic_DNA.
EMBL; M24376; AAA39379.1; JOINED; Genomic_DNA.
EMBL; M24377; AAA39380.1; -; Genomic_DNA.
EMBL; M24376; AAA39380.1; JOINED; Genomic_DNA.
EMBL; X06746; CAA29921.1; -; mRNA.
EMBL; BC009093; AAH09093.1; -; mRNA.
EMBL; M20759; AAA39381.1; -; Genomic_DNA.
CCDS; CCDS35927.2; -. [P08152-1]
CCDS; CCDS83706.1; -. [P08152-2]
PIR; A30136; A30136.
PIR; S00256; S00256.
RefSeq; NP_001334387.1; NM_001347458.1. [P08152-2]
RefSeq; NP_034248.2; NM_010118.3. [P08152-1]
RefSeq; XP_006513272.1; XM_006513209.2. [P08152-2]
RefSeq; XP_006513273.1; XM_006513210.2. [P08152-2]
RefSeq; XP_006513274.1; XM_006513211.2. [P08152-2]
RefSeq; XP_006513276.1; XM_006513213.3. [P08152-2]
RefSeq; XP_011241670.1; XM_011243368.2. [P08152-2]
UniGene; Mm.290421; -.
ProteinModelPortal; P08152; -.
SMR; P08152; -.
BioGrid; 199405; 6.
ELM; P08152; -.
IntAct; P08152; 5.
MINT; MINT-2828823; -.
STRING; 10090.ENSMUSP00000041053; -.
iPTMnet; P08152; -.
PhosphoSitePlus; P08152; -.
PaxDb; P08152; -.
PRIDE; P08152; -.
Ensembl; ENSMUST00000048289; ENSMUSP00000041053; ENSMUSG00000037868. [P08152-1]
Ensembl; ENSMUST00000105438; ENSMUSP00000101078; ENSMUSG00000037868. [P08152-2]
GeneID; 13654; -.
KEGG; mmu:13654; -.
UCSC; uc007flx.1; mouse. [P08152-1]
CTD; 1959; -.
MGI; MGI:95296; Egr2.
eggNOG; KOG1721; Eukaryota.
eggNOG; COG5048; LUCA.
GeneTree; ENSGT00550000074455; -.
HOGENOM; HOG000036856; -.
HOVERGEN; HBG003909; -.
InParanoid; P08152; -.
KO; K12496; -.
OMA; FPPQCQR; -.
OrthoDB; EOG091G06VX; -.
PhylomeDB; P08152; -.
TreeFam; TF318980; -.
Reactome; R-MMU-442533; Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.
UniPathway; UPA00886; -.
PRO; PR:P08152; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000037868; -.
CleanEx; MM_EGR2; -.
ExpressionAtlas; P08152; baseline and differential.
Genevisible; P08152; MM.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0071837; F:HMG box domain binding; IEA:Ensembl.
GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0001102; F:RNA polymerase II activating transcription factor binding; IPI:BHF-UCL.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; ISO:MGI.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; ISO:MGI.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:0035284; P:brain segmentation; IMP:MGI.
GO; GO:0071310; P:cellular response to organic substance; IDA:MGI.
GO; GO:0021612; P:facial nerve structural organization; IGI:MGI.
GO; GO:0045444; P:fat cell differentiation; IMP:BHF-UCL.
GO; GO:0007611; P:learning or memory; IEA:Ensembl.
GO; GO:0008045; P:motor neuron axon guidance; IGI:MGI.
GO; GO:0042552; P:myelination; IMP:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0006611; P:protein export from nucleus; IDA:UniProtKB.
GO; GO:0016925; P:protein sumoylation; IEA:UniProtKB-UniPathway.
GO; GO:0048168; P:regulation of neuronal synaptic plasticity; IEA:Ensembl.
GO; GO:0030278; P:regulation of ossification; IMP:MGI.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:MGI.
GO; GO:0032868; P:response to insulin; IEA:Ensembl.
GO; GO:0021569; P:rhombomere 3 development; IGI:MGI.
GO; GO:0021660; P:rhombomere 3 formation; IMP:MGI.
GO; GO:0021666; P:rhombomere 5 formation; IMP:MGI.
GO; GO:0007622; P:rhythmic behavior; IDA:MGI.
GO; GO:0014037; P:Schwann cell differentiation; IMP:MGI.
GO; GO:0035914; P:skeletal muscle cell differentiation; IMP:MGI.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; IDA:BHF-UCL.
InterPro; IPR021849; EGR.
InterPro; IPR036236; Znf_C2H2_sf.
InterPro; IPR013087; Znf_C2H2_type.
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; Alternative splicing; Complete proteome; DNA-binding;
Ligase; Metal-binding; Nucleus; Reference proteome; Repeat;
Transcription; Transcription regulation; Ubl conjugation;
Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 470 E3 SUMO-protein ligase EGR2.
/FTId=PRO_0000047120.
ZN_FING 337 361 C2H2-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 367 389 C2H2-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 395 417 C2H2-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
COMPBIAS 167 173 Poly-Pro.
VAR_SEQ 1 50 Missing (in isoform Short).
{ECO:0000303|PubMed:3129290}.
/FTId=VSP_006864.
MUTAGEN 174 174 Y->F: Abolishes interaction with WWP2; if
associated with F-208.
{ECO:0000269|PubMed:19651900}.
MUTAGEN 208 208 Y->F: Abolishes interaction with WWP2; if
associated with F-174.
{ECO:0000269|PubMed:19651900}.
MUTAGEN 377 377 S->A: Inhibits interaction with SFN.
{ECO:0000269|PubMed:17938205}.
SEQUENCE 470 AA; 49819 MW; 67712733C77960F0 CRC64;
MMTAKAVDKI PVTLSGFMHQ LPDSLYPVED LAASSVTIFP NGELGGPFDQ MNGVAGDGMI
NIDMTGEKRP LDLPYPSSFA PISAPRNQTF TYMGKFSIDP QYPGASCYPE GIINIVSAGI
LQGVTPPAST TASSSVTSAS PNPLATGPLG VCTMSQTQPE LDHLYSPPPP PPPYSGCTGD
LYQDPSAFLS PPSTTSTSSL AYQPPPSYPS PKPAMDPGLI PMIPDYPGFF PSPCQRDPHG
AAGPDRKPFP CPLDSLRVPP PLTPLSTIRN FTLGGPGAGV TGPGASGGGE GPRLPGSGSA
AVTATPYNPH HLPLRPILRP RKYPNRPSKT PVHERPYPCP AEGCDRRFSR SDELTRHIRI
HTGHKPFQCR ICMRNFSRSD HLTTHIRTHT GEKPFACDYC GRKFARSDER KRHTKIHLRQ
KERKSSAPSA PPSAQSSASG PGGSQAGGSL CGNSAIGGPL ASCTSRTRTP


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