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E3 SUMO-protein ligase EGR2 (EC 6.3.2.-) (AT591) (Early growth response protein 2) (EGR-2) (Zinc finger protein Krox-20)

 EGR2_HUMAN              Reviewed;         476 AA.
P11161; B2R724; B3KRD7; Q68CZ5; Q8IV26; Q9UNA6;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
19-JUL-2003, sequence version 3.
22-NOV-2017, entry version 191.
RecName: Full=E3 SUMO-protein ligase EGR2;
EC=6.3.2.-;
AltName: Full=AT591;
AltName: Full=Early growth response protein 2;
Short=EGR-2;
AltName: Full=Zinc finger protein Krox-20;
Name=EGR2; Synonyms=KROX20;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
PubMed=3140236; DOI=10.1073/pnas.85.19.7164;
Joseph L.J., le Beau M.M., Jamieson G.A. Jr., Acharya S., Shows T.B.,
Rowley J.D., Sukhatme V.P.;
"Molecular cloning, sequencing, and mapping of EGR2, a human early
growth response gene encoding a protein with 'zinc-binding finger'
structure.";
Proc. Natl. Acad. Sci. U.S.A. 85:7164-7168(1988).
[2]
ERRATUM, AND SEQUENCE REVISION TO C-TERMINUS.
Joseph L.J., le Beau M.M., Jamieson G.A. Jr., Acharya S., Shows T.B.,
Rowley J.D., Sukhatme V.P.;
Proc. Natl. Acad. Sci. U.S.A. 86:515-515(1989).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), VARIANTS CHN ASN-268 AND
382-ARG-TYR-383, AND VARIANT CMT1D TRP-409.
PubMed=9537424; DOI=10.1038/ng0498-382;
Warner L.E., Mancias P., Butler I.J., McDonald C.M., Keppen L.,
Koob K.G., Lupski J.R.;
"Mutations in the early growth response 2 (EGR2) gene are associated
with hereditary myelinopathies.";
Nat. Genet. 18:382-384(1998).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS LONG AND SHORT).
TISSUE=Brain, and Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Endometrium;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
PubMed=2111009; DOI=10.1093/nar/18.9.2749;
Rangnekar V.M., Aplin A.C., Sukhatme V.P.;
"The serum and TPA responsive promoter and intron-exon structure of
EGR2, a human early growth response gene encoding a zinc finger
protein.";
Nucleic Acids Res. 18:2749-2757(1990).
[10]
INTERACTION WITH HCFC1, AND MUTAGENESIS OF 162-ASP--TYR-165.
PubMed=14532282; DOI=10.1074/jbc.M303470200;
Luciano R.L., Wilson A.C.;
"HCF-1 functions as a coactivator for the zinc finger protein
Krox20.";
J. Biol. Chem. 278:51116-51124(2003).
[11]
INTERACTION WITH WWP2.
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).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[13]
FUNCTION AS SUMO LIGASE, AND INTERACTION WITH UBC9.
PubMed=21836637; DOI=10.1038/embor.2011.152;
Garcia-Gutierrez P., Juarez-Vicente F., Gallardo-Chamizo F.,
Charnay P., Garcia-Dominguez M.;
"The transcription factor Krox20 is an E3 ligase that sumoylates its
Nab coregulators.";
EMBO Rep. 12:1018-1023(2011).
[14]
INVOLVEMENT IN CHN.
PubMed=22522483; DOI=10.1002/ana.23527;
Funalot B., Topilko P., Arroyo M.A., Sefiani A., Hedley-Whyte E.T.,
Yoldi M.E., Richard L., Touraille E., Laurichesse M., Khalifa E.,
Chauzeix J., Ouedraogo A., Cros D., Magdelaine C., Sturtz F.G.,
Urtizberea J.A., Charnay P., Bragado F.G., Vallat J.M.;
"Homozygous deletion of an EGR2 enhancer in congenital amyelinating
neuropathy.";
Ann. Neurol. 71:719-723(2012).
[15]
VARIANT CMT1D VAL-355.
Di Maria E., Bellone E., Soriani S., Varese A., Lamba Doria L.,
Grandis M., Schenone A., Levi G., Ajmar F., Mandich P.;
"EGR2 gene mutation in a patient affected with Charcot-Marie-Tooth
type 1.";
Eur. J. Hum. Genet. Suppl. 7:99-99(1999).
[16]
VARIANT CMT1D VAL-355.
PubMed=10502832;
DOI=10.1002/(SICI)1098-1004(199910)14:4<353::AID-HUMU17>3.3.CO;2-W;
Bellone E., Di Maria E., Soriani S., Varese A., Lamba Doria L.,
Ajmar F., Mandich P.;
"A novel mutation (D305V) in the early growth response 2 gene is
associated with severe Charcot-Marie-Tooth type 1 disease.";
Hum. Mutat. 14:353-354(1999).
[17]
VARIANT DSS TRP-359.
PubMed=10371530; DOI=10.1212/WNL.52.9.1827;
Timmerman V., De Jonghe P., Ceuterick C., De Vriendt E., Lofgren A.,
Nelis E., Warner L.E., Lupski J.R., Martin J.-J., Van Broeckhoven C.;
"Novel missense mutation in the early growth response 2 gene
associated with Dejerine-Sottas syndrome phenotype.";
Neurology 52:1827-1832(1999).
[18]
VARIANT CMT1D HIS-381.
PubMed=10762521; DOI=10.1212/WNL.54.8.1696;
Pareyson D., Taroni F., Botti S., Morbin M., Baratta S., Lauria G.,
Ciano C., Sghirlanzoni A.;
"Cranial nerve involvement in CMT disease type 1 due to early growth
response 2 gene mutation.";
Neurology 54:1696-1698(2000).
[19]
VARIANT CMT1D CYS-381.
PubMed=11239949; DOI=10.1016/S0022-510X(00)00504-9;
Yoshihara T., Kanda F., Yamamoto M., Ishihara H., Misu K., Hattori N.,
Chihara K., Sobue G.;
"A novel missense mutation in the early growth response 2 gene
associated with late-onset Charcot-Marie-Tooth disease type 1.";
J. Neurol. Sci. 184:149-153(2001).
[20]
VARIANT CMT1D TYR-383.
PubMed=12736090; DOI=10.1016/S0022-510X(03)00028-5;
Numakura C., Shirahata E., Yamashita S., Kanai M., Kijima K.,
Matsuki T., Hayasaka K.;
"Screening of the early growth response 2 gene in Japanese patients
with Charcot-Marie-Tooth disease type 1.";
J. Neurol. Sci. 210:61-64(2003).
[21]
VARIANT CMT1D TRP-359.
PubMed=15241803; DOI=10.1002/humu.9261;
Choi B.-O., Lee M.S., Shin S.H., Hwang J.H., Choi K.-G., Kim W.-K.,
Sunwoo I.N., Kim N.K., Chung K.W.;
"Mutational analysis of PMP22, MPZ, GJB1, EGR2 and NEFL in Korean
Charcot-Marie-Tooth neuropathy patients.";
Hum. Mutat. 24:185-186(2004).
[22]
VARIANT CMT1D TRP-359.
PubMed=15947997; DOI=10.1007/s10048-005-0217-4;
Chung K.W., Sunwoo I.N., Kim S.M., Park K.D., Kim W.-K., Kim T.S.,
Koo H., Cho M., Lee J., Choi B.O.;
"Two missense mutations of EGR2 R359W and GJB1 V136A in a Charcot-
Marie-Tooth disease family.";
Neurogenetics 6:159-163(2005).
-!- FUNCTION: Sequence-specific DNA-binding transcription factor.
Binds to two specific DNA sites located in the promoter region of
HOXA4. {ECO:0000269|PubMed:21836637}.
-!- FUNCTION: E3 SUMO-protein ligase helping SUMO1 conjugation to its
coregulators NAB1 and NAB2, whose sumoylation down-regulates EGR2
own transcriptional activity. {ECO:0000269|PubMed:21836637}.
-!- PATHWAY: Protein modification; protein sumoylation.
-!- SUBUNIT: Interacts with HCFC1. Interacts with WWP2. Interacts with
UBC9. {ECO:0000269|PubMed:14532282, ECO:0000269|PubMed:19651900,
ECO:0000269|PubMed:21836637}.
-!- SUBCELLULAR LOCATION: Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Long;
IsoId=P11161-1; Sequence=Displayed;
Name=Short;
IsoId=P11161-2; Sequence=VSP_006863;
Note=No experimental confirmation available.;
-!- PTM: Ubiquitinated by WWP2 leading to proteasomal degradation.
{ECO:0000250}.
-!- DISEASE: Neuropathy, congenital hypomyelinating or amyelinating
(CHN) [MIM:605253]: A severe degenerating neuropathy that results
from a congenital impairment in myelin formation. It is clinically
characterized by early onset of hypotonia, areflexia, distal
muscle weakness, and very slow nerve conduction velocities (as low
as 3m/s). Some patients manifest nearly complete absence of
spontaneous limb movements, respiratory distress at birth, and
complete absence of myelin shown by electron microscopy of
peripheral nerves. Inheritance can be autosomal dominant or
recessive. {ECO:0000269|PubMed:22522483,
ECO:0000269|PubMed:9537424}. Note=The disease is caused by
mutations affecting the gene represented in this entry. Patients
affected by the amyelinating form carry a causative, homozygous
deletion encompassing a myelin-specific enhancer of EGR2
(PubMed:22522483). {ECO:0000269|PubMed:22522483}.
-!- DISEASE: Charcot-Marie-Tooth disease 1D (CMT1D) [MIM:607678]: A
dominant demyelinating form of Charcot-Marie-Tooth disease, a
disorder of the peripheral nervous system, characterized by
progressive weakness and atrophy, initially of the peroneal
muscles and later of the distal muscles of the arms. Charcot-
Marie-Tooth disease is classified in two main groups on the basis
of electrophysiologic properties and histopathology: primary
peripheral demyelinating neuropathies (designated CMT1 when they
are dominantly inherited) and primary peripheral axonal
neuropathies (CMT2). Demyelinating neuropathies are characterized
by severely reduced nerve conduction velocities (less than 38
m/sec), segmental demyelination and remyelination with onion bulb
formations on nerve biopsy, slowly progressive distal muscle
atrophy and weakness, absent deep tendon reflexes, and hollow
feet. {ECO:0000269|PubMed:10502832, ECO:0000269|PubMed:10762521,
ECO:0000269|PubMed:11239949, ECO:0000269|PubMed:12736090,
ECO:0000269|PubMed:15241803, ECO:0000269|PubMed:15947997,
ECO:0000269|PubMed:9537424, ECO:0000269|Ref.15}. Note=The disease
is caused by mutations affecting the gene represented in this
entry.
-!- DISEASE: Dejerine-Sottas syndrome (DSS) [MIM:145900]: A severe
degenerating neuropathy of the demyelinating Charcot-Marie-Tooth
disease category, with onset by age 2 years. Characterized by
motor and sensory neuropathy with very slow nerve conduction
velocities, increased cerebrospinal fluid protein concentrations,
hypertrophic nerve changes, delayed age of walking as well as
areflexia. There are both autosomal dominant and autosomal
recessive forms of Dejerine-Sottas syndrome.
{ECO:0000269|PubMed:10371530}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the EGR C2H2-type zinc-finger protein
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA52372.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAA52372.1; Type=Frameshift; Positions=449; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Inherited peripheral neuropathies mutation db;
URL="http://www.molgen.ua.ac.be/CMTMutations/";
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EMBL; J04076; AAA52372.1; ALT_SEQ; mRNA.
EMBL; AF139463; AAD24588.1; -; mRNA.
EMBL; AK091399; BAG52349.1; -; mRNA.
EMBL; AK312813; BAG35671.1; -; mRNA.
EMBL; CR749641; CAH18435.1; -; mRNA.
EMBL; AL133417; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471083; EAW54238.1; -; Genomic_DNA.
EMBL; CH471083; EAW54239.1; -; Genomic_DNA.
EMBL; BC035625; AAH35625.1; -; mRNA.
EMBL; X53700; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS44409.1; -. [P11161-2]
CCDS; CCDS7267.1; -. [P11161-1]
RefSeq; NP_000390.2; NM_000399.4. [P11161-1]
RefSeq; NP_001129649.1; NM_001136177.2. [P11161-1]
RefSeq; NP_001129650.1; NM_001136178.1. [P11161-1]
RefSeq; NP_001129651.1; NM_001136179.2. [P11161-2]
RefSeq; NP_001307966.1; NM_001321037.1. [P11161-2]
UniGene; Hs.1395; -.
ProteinModelPortal; P11161; -.
SMR; P11161; -.
BioGrid; 108279; 17.
IntAct; P11161; 10.
MINT; MINT-234172; -.
STRING; 9606.ENSP00000242480; -.
iPTMnet; P11161; -.
PhosphoSitePlus; P11161; -.
BioMuta; EGR2; -.
DMDM; 33112654; -.
PaxDb; P11161; -.
PeptideAtlas; P11161; -.
PRIDE; P11161; -.
DNASU; 1959; -.
Ensembl; ENST00000242480; ENSP00000242480; ENSG00000122877. [P11161-1]
Ensembl; ENST00000411732; ENSP00000387634; ENSG00000122877. [P11161-2]
Ensembl; ENST00000439032; ENSP00000402040; ENSG00000122877. [P11161-1]
GeneID; 1959; -.
KEGG; hsa:1959; -.
UCSC; uc001jmi.4; human. [P11161-1]
CTD; 1959; -.
DisGeNET; 1959; -.
EuPathDB; HostDB:ENSG00000122877.13; -.
GeneCards; EGR2; -.
GeneReviews; EGR2; -.
HGNC; HGNC:3239; EGR2.
HPA; HPA031165; -.
MalaCards; EGR2; -.
MIM; 129010; gene.
MIM; 145900; phenotype.
MIM; 605253; phenotype.
MIM; 607678; phenotype.
neXtProt; NX_P11161; -.
OpenTargets; ENSG00000122877; -.
Orphanet; 101084; Charcot-Marie-Tooth disease type 1D.
Orphanet; 99951; Charcot-Marie-Tooth disease type 4E.
Orphanet; 64748; Dejerine-Sottas syndrome.
PharmGKB; PA27674; -.
eggNOG; KOG1721; Eukaryota.
eggNOG; COG5048; LUCA.
GeneTree; ENSGT00550000074455; -.
HOGENOM; HOG000036856; -.
HOVERGEN; HBG003909; -.
InParanoid; P11161; -.
KO; K12496; -.
OMA; FPPQCQR; -.
OrthoDB; EOG091G06VX; -.
PhylomeDB; P11161; -.
TreeFam; TF318980; -.
Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis.
SignaLink; P11161; -.
SIGNOR; P11161; -.
UniPathway; UPA00886; -.
GeneWiki; EGR2; -.
GenomeRNAi; 1959; -.
PRO; PR:P11161; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000122877; -.
CleanEx; HS_EGR2; -.
ExpressionAtlas; P11161; baseline and differential.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
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; ISS:BHF-UCL.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0044212; F:transcription regulatory region DNA binding; ISS:UniProtKB.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:NTNU_SB.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0007420; P:brain development; TAS:ProtInc.
GO; GO:0035284; P:brain segmentation; IEA:Ensembl.
GO; GO:0071310; P:cellular response to organic substance; IEA:Ensembl.
GO; GO:0021612; P:facial nerve structural organization; IEA:Ensembl.
GO; GO:0045444; P:fat cell differentiation; ISS:BHF-UCL.
GO; GO:0007611; P:learning or memory; IEA:Ensembl.
GO; GO:0008045; P:motor neuron axon guidance; IEA:Ensembl.
GO; GO:0042552; P:myelination; IEA:Ensembl.
GO; GO:0007422; P:peripheral nervous system development; TAS:ProtInc.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:NTNU_SB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0006611; P:protein export from nucleus; ISS: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; IEA:Ensembl.
GO; GO:0032868; P:response to insulin; IEA:Ensembl.
GO; GO:0021660; P:rhombomere 3 formation; IEA:Ensembl.
GO; GO:0021666; P:rhombomere 5 formation; IEA:Ensembl.
GO; GO:0007622; P:rhythmic behavior; IEA:Ensembl.
GO; GO:0014037; P:Schwann cell differentiation; IEA:Ensembl.
GO; GO:0035914; P:skeletal muscle cell differentiation; IEA:Ensembl.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; ISS:BHF-UCL.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR021849; EGR.
InterPro; IPR036236; Znf_C2H2_sf.
InterPro; IPR013087; Znf_C2H2_type.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
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; Charcot-Marie-Tooth disease;
Complete proteome; Dejerine-Sottas syndrome; Disease mutation;
DNA-binding; Ligase; Metal-binding; Neurodegeneration; Neuropathy;
Nucleus; Reference proteome; Repeat; Transcription;
Transcription regulation; Ubl conjugation; Ubl conjugation pathway;
Zinc; Zinc-finger.
CHAIN 1 476 E3 SUMO-protein ligase EGR2.
/FTId=PRO_0000047119.
ZN_FING 340 364 C2H2-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 370 392 C2H2-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 398 420 C2H2-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
MOTIF 162 165 HCFC1-binding-motif (HBM).
COMPBIAS 300 309 Poly-Ala.
VAR_SEQ 1 50 Missing (in isoform Short).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_006863.
VARIANT 268 268 I -> N (in CHN; dbSNP:rs104894158).
{ECO:0000269|PubMed:9537424}.
/FTId=VAR_007735.
VARIANT 355 355 D -> V (in CMT1D).
{ECO:0000269|PubMed:10502832,
ECO:0000269|Ref.15}.
/FTId=VAR_007736.
VARIANT 359 359 R -> W (in DSS and CMT1D; associated with
A-136 in the GJB1 gene in a DSS Korean
girl; dbSNP:rs104894161).
{ECO:0000269|PubMed:10371530,
ECO:0000269|PubMed:15241803,
ECO:0000269|PubMed:15947997}.
/FTId=VAR_009874.
VARIANT 381 381 R -> C (in CMT1D).
{ECO:0000269|PubMed:11239949}.
/FTId=VAR_029958.
VARIANT 381 381 R -> H (in CMT1D; dbSNP:rs281865137).
{ECO:0000269|PubMed:10762521}.
/FTId=VAR_009875.
VARIANT 382 383 SD -> RY (in CHN).
/FTId=VAR_007737.
VARIANT 383 383 D -> Y (in CMT1D; dbSNP:rs104894160).
{ECO:0000269|PubMed:12736090}.
/FTId=VAR_029959.
VARIANT 409 409 R -> W (in CMT1D; dbSNP:rs104894159).
{ECO:0000269|PubMed:9537424}.
/FTId=VAR_007738.
MUTAGEN 162 165 DHLY->AAAA: Inhibits association with
HCFC1. {ECO:0000269|PubMed:14532282}.
CONFLICT 68 68 K -> R (in Ref. 5; CAH18435).
{ECO:0000305}.
CONFLICT 247 247 K -> KPFPCPLDTLRVPPPLTPLSTIRK (in Ref. 8;
AAH35625). {ECO:0000305}.
CONFLICT 280 280 V -> M (in Ref. 1; AAA52372).
{ECO:0000305}.
SEQUENCE 476 AA; 50302 MW; 7810D1B1B418DF1F CRC64;
MMTAKAVDKI PVTLSGFVHQ LSDNIYPVED LAATSVTIFP NAELGGPFDQ MNGVAGDGMI
NIDMTGEKRS LDLPYPSSFA PVSAPRNQTF TYMGKFSIDP QYPGASCYPE GIINIVSAGI
LQGVTSPAST TASSSVTSAS PNPLATGPLG VCTMSQTQPD LDHLYSPPPP PPPYSGCAGD
LYQDPSAFLS AATTSTSSSL AYPPPPSYPS PKPATDPGLF PMIPDYPGFF PSQCQRDLHG
TAGPDRKPFP CPLDTLRVPP PLTPLSTIRN FTLGGPSAGV TGPGASGGSE GPRLPGSSSA
AAAAAAAAAY NPHHLPLRPI LRPRKYPNRP SKTPVHERPY PCPAEGCDRR FSRSDELTRH
IRIHTGHKPF QCRICMRNFS RSDHLTTHIR THTGEKPFAC DYCGRKFARS DERKRHTKIH
LRQKERKSSA PSASVPAPST ASCSGGVQPG GTLCSSNSSS LGGGPLAPCS SRTRTP


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