P11161 (EGR2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
E3 SUMO-protein ligase EGR2
EC=6.3.2.-

Alternative name(s):
AT591
Early growth response protein 2
Short name=EGR-2
Zinc finger protein Krox-20

Gene names

Name:	EGR2
Synonyms:	KROX20

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	476 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Sequence-specific DNA-binding transcription factor. Binds to two specific DNA sites located in the promoter region of HOXA4. Ref.13 E3 SUMO-protein ligase helping SUMO1 conjugation to its coregulators NAB1 and NAB2, whose sumoylation down-regulates EGR2 own transcriptional activity. Ref.13
Pathway	Protein modification; protein sumoylation.
Subunit structure	Interacts with HCFC1. Interacts with WWP2. Interacts with UBC9. Ref.10 Ref.11 Ref.13
Subcellular location	Nucleus.
Post-translational modification	Ubiquitinated by WWP2 leading to proteasomal degradation By similarity.
Involvement in disease	Congenital hypomyelination neuropathy (CHN) [MIM:605253]: A severe degenerating neuropathy, clinically characterized by early onset of hypotonia, areflexia, distal muscle weakness, and very slow nerve conduction velocities (as low as 3m/s). Results from a congenital impairment in myelin formation. Inheritance can be autosomal dominant or recessive. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.3 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.3 Ref.14 Ref.15 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16
Sequence similarities	Belongs to the EGR C2H2-type zinc-finger protein family. Contains 3 C2H2-type zinc fingers.
Sequence caution	The sequence AAA52372.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence AAA52372.1 differs from that shown. Reason: Frameshift at position 449.

Ontologies

Keywords
Biological process	Transcription Transcription regulation Ubl conjugation pathway
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Disease	Charcot-Marie-Tooth disease Dejerine-Sottas syndrome Disease mutation Neuropathy
Domain	Repeat Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Activator Ligase
PTM	Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Schwann cell differentiation Inferred from electronic annotation. Source: Compara brain development Traceable author statement Ref.3. Source: ProtInc brain segmentation Inferred from electronic annotation. Source: Compara cellular response to organic substance Inferred from electronic annotation. Source: Compara facial nerve structural organization Inferred from electronic annotation. Source: Compara fat cell differentiation Inferred from sequence or structural similarity. Source: BHF-UCL learning or memory Inferred from electronic annotation. Source: Compara motor neuron axon guidance Inferred from electronic annotation. Source: Compara myelination Inferred from electronic annotation. Source: Compara peripheral nervous system development Traceable author statement Ref.3. Source: ProtInc positive regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara positive regulation of transcription, DNA-dependent Inferred from sequence or structural similarity. Source: UniProtKB protein export from nucleus Inferred from sequence or structural similarity. Source: UniProtKB protein sumoylation Inferred from electronic annotation. Source: UniProtKB-UniPathway regulation of neuronal synaptic plasticity Inferred from electronic annotation. Source: Compara regulation of ossification Inferred from electronic annotation. Source: Compara response to insulin stimulus Inferred from electronic annotation. Source: Compara rhombomere 3 formation Inferred from electronic annotation. Source: Compara rhombomere 5 formation Inferred from electronic annotation. Source: Compara rhythmic behavior Inferred from electronic annotation. Source: Compara transcription from RNA polymerase II promoter Inferred from sequence or structural similarity. Source: BHF-UCL
Cellular_component	cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB nucleus Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	RNA polymerase II activating transcription factor binding Inferred from sequence or structural similarity. Source: BHF-UCL chromatin binding Inferred from sequence or structural similarity. Source: UniProtKB ligase activity Inferred from electronic annotation. Source: UniProtKB-KW sequence-specific DNA binding transcription factor activity Inferred from direct assay Ref.10. Source: UniProtKB transcription regulatory region DNA binding Inferred from sequence or structural similarity. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform Long (identifier: P11161-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform Short (identifier: P11161-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-50: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 476	476	E3 SUMO-protein ligase EGR2		PRO_0000047119
Regions
	Zinc finger	340 – 364	25	C2H2-type 1
	Zinc finger	370 – 392	23	C2H2-type 2
	Zinc finger	398 – 420	23	C2H2-type 3
	Motif	162 – 165	4	HCFC1-binding-motif (HBM)
	Compositional bias	300 – 309	10	Poly-Ala
Natural variations
	Alternative sequence	1 – 50	50	Missing in isoform Short.		VSP_006863
	Natural variant	268	1	I → N in CHN. Ref.3		VAR_007735
	Natural variant	355	1	D → V in CMT1D. Ref.14 Ref.15		VAR_007736
	Natural variant	359	1	R → W in DSS and CMT1D; associated with A-136 in the GJB1 gene in a DSS Korean girl. Ref.16 Ref.20 Ref.21		VAR_009874
	Natural variant	381	1	R → C in CMT1D. Ref.18		VAR_029958
	Natural variant	381	1	R → H in CMT1D. Ref.17		VAR_009875
	Natural variant	382 – 383	2	SD → RY in CHN.		VAR_007737
	Natural variant	383	1	D → Y in CMT1D. Ref.19		VAR_029959
	Natural variant	409	1	R → W in CMT1D. Ref.3		VAR_007738
Experimental info
	Mutagenesis	162 – 165	4	DHLY → AAAA: Inhibits association with HCFC1. Ref.10
	Sequence conflict	68	1	K → R in CAH18435. Ref.5
	Sequence conflict	247	1	K → KPFPCPLDTLRVPPPLTPLS TIRK in AAH35625. Ref.8
	Sequence conflict	280	1	V → M in AAA52372. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform Long [UniParc]. Last modified July 19, 2003. Version 3. Checksum: 7810D1B1B418DF1F	FASTA	476	50,302
	10 20 30 40 50 60 MMTAKAVDKI PVTLSGFVHQ LSDNIYPVED LAATSVTIFP NAELGGPFDQ MNGVAGDGMI 70 80 90 100 110 120 NIDMTGEKRS LDLPYPSSFA PVSAPRNQTF TYMGKFSIDP QYPGASCYPE GIINIVSAGI 130 140 150 160 170 180 LQGVTSPAST TASSSVTSAS PNPLATGPLG VCTMSQTQPD LDHLYSPPPP PPPYSGCAGD 190 200 210 220 230 240 LYQDPSAFLS AATTSTSSSL AYPPPPSYPS PKPATDPGLF PMIPDYPGFF PSQCQRDLHG 250 260 270 280 290 300 TAGPDRKPFP CPLDTLRVPP PLTPLSTIRN FTLGGPSAGV TGPGASGGSE GPRLPGSSSA 310 320 330 340 350 360 AAAAAAAAAY NPHHLPLRPI LRPRKYPNRP SKTPVHERPY PCPAEGCDRR FSRSDELTRH 370 380 390 400 410 420 IRIHTGHKPF QCRICMRNFS RSDHLTTHIR THTGEKPFAC DYCGRKFARS DERKRHTKIH 430 440 450 460 470 LRQKERKSSA PSASVPAPST ASCSGGVQPG GTLCSSNSSS LGGGPLAPCS SRTRTP
	Isoform Short [UniParc]. Checksum: DD358E32D00B4353	FASTA	426	44,970
	10 20 30 40 50 60 MNGVAGDGMI NIDMTGEKRS LDLPYPSSFA PVSAPRNQTF TYMGKFSIDP QYPGASCYPE 70 80 90 100 110 120 GIINIVSAGI LQGVTSPAST TASSSVTSAS PNPLATGPLG VCTMSQTQPD LDHLYSPPPP 130 140 150 160 170 180 PPPYSGCAGD LYQDPSAFLS AATTSTSSSL AYPPPPSYPS PKPATDPGLF PMIPDYPGFF 190 200 210 220 230 240 PSQCQRDLHG TAGPDRKPFP CPLDTLRVPP PLTPLSTIRN FTLGGPSAGV TGPGASGGSE 250 260 270 280 290 300 GPRLPGSSSA AAAAAAAAAY NPHHLPLRPI LRPRKYPNRP SKTPVHERPY PCPAEGCDRR 310 320 330 340 350 360 FSRSDELTRH IRIHTGHKPF QCRICMRNFS RSDHLTTHIR THTGEKPFAC DYCGRKFARS 370 380 390 400 410 420 DERKRHTKIH LRQKERKSSA PSASVPAPST ASCSGGVQPG GTLCSSNSSS LGGGPLAPCS SRTRTP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning, sequencing, and mapping of EGR2, a human early growth response gene encoding a protein with 'zinc-binding finger' structure." 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. 85:7164-7168(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
[2]	Erratum 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) Cited for: SEQUENCE REVISION TO C-TERMINUS.
[3]	"Mutations in the early growth response 2 (EGR2) gene are associated with hereditary myelinopathies." Warner L.E., Mancias P., Butler I.J., McDonald C.M., Keppen L., Koob K.G., Lupski J.R. Nat. Genet. 18:382-384(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), VARIANTS CHN ASN-268 AND 382-ARG-TYR-383, VARIANT CMT1D TRP-409.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS LONG AND SHORT). Tissue: Brain and Testis.
[5]	"The full-ORF clone resource of the German cDNA consortium." 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. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Endometrium.
[6]	"The DNA sequence and comparative analysis of human chromosome 10." 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. Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[9]	"The serum and TPA responsive promoter and intron-exon structure of EGR2, a human early growth response gene encoding a zinc finger protein." Rangnekar V.M., Aplin A.C., Sukhatme V.P. Nucleic Acids Res. 18:2749-2757(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
[10]	"HCF-1 functions as a coactivator for the zinc finger protein Krox20." Luciano R.L., Wilson A.C. J. Biol. Chem. 278:51116-51124(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HCFC1, MUTAGENESIS OF 162-ASP--TYR-165.
[11]	"The HECT-type E3 ubiquitin ligase AIP2 inhibits activation-induced T-cell death by catalyzing EGR2 ubiquitination." Chen A., Gao B., Zhang J., McEwen T., Ye S.Q., Zhang D., Fang D. Mol. Cell. Biol. 29:5348-5356(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH WWP2.
[12]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Leukemic T-cell.
[13]	"The transcription factor Krox20 is an E3 ligase that sumoylates its Nab coregulators." Garcia-Gutierrez P., Juarez-Vicente F., Gallardo-Chamizo F., Charnay P., Garcia-Dominguez M. EMBO Rep. 12:1018-1023(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS SUMO LIGASE, INTERACTION WITH UBC9.
[14]	"EGR2 gene mutation in a patient affected with Charcot-Marie-Tooth type 1." Di Maria E., Bellone E., Soriani S., Varese A., Lamba Doria L., Grandis M., Schenone A., Levi G., Ajmar F., Mandich P. Eur. J. Hum. Genet. Suppl. 7:99-99(1999) Cited for: VARIANT CMT1D VAL-355.
[15]	"A novel mutation (D305V) in the early growth response 2 gene is associated with severe Charcot-Marie-Tooth type 1 disease." Bellone E., Di Maria E., Soriani S., Varese A., Lamba Doria L., Ajmar F., Mandich P. Hum. Mutat. 14:353-354(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CMT1D VAL-355.
[16]	"Novel missense mutation in the early growth response 2 gene associated with Dejerine-Sottas syndrome phenotype." 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. Neurology 52:1827-1832(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT DSS TRP-359.
[17]	"Cranial nerve involvement in CMT disease type 1 due to early growth response 2 gene mutation." Pareyson D., Taroni F., Botti S., Morbin M., Baratta S., Lauria G., Ciano C., Sghirlanzoni A. Neurology 54:1696-1698(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CMT1D HIS-381.
[18]	"A novel missense mutation in the early growth response 2 gene associated with late-onset Charcot-Marie-Tooth disease type 1." Yoshihara T., Kanda F., Yamamoto M., Ishihara H., Misu K., Hattori N., Chihara K., Sobue G. J. Neurol. Sci. 184:149-153(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CMT1D CYS-381.
[19]	"Screening of the early growth response 2 gene in Japanese patients with Charcot-Marie-Tooth disease type 1." Numakura C., Shirahata E., Yamashita S., Kanai M., Kijima K., Matsuki T., Hayasaka K. J. Neurol. Sci. 210:61-64(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CMT1D TYR-383.
[20]	"Mutational analysis of PMP22, MPZ, GJB1, EGR2 and NEFL in Korean Charcot-Marie-Tooth neuropathy patients." 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. Hum. Mutat. 24:185-186(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CMT1D TRP-359.
[21]	"Two missense mutations of EGR2 R359W and GJB1 V136A in a Charcot-Marie-Tooth disease family." 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. Neurogenetics 6:159-163(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CMT1D TRP-359.
+	Additional computationally mapped references.

Web resources

Inherited peripheral neuropathies mutation db

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	J04076 mRNA. Translation: AAA52372.1. Sequence problems. AF139463 mRNA. Translation: AAD24588.1. AK091399 mRNA. Translation: BAG52349.1. AK312813 mRNA. Translation: BAG35671.1. CR749641 mRNA. Translation: CAH18435.1. AL133417 Genomic DNA. Translation: CAH73827.2. CH471083 Genomic DNA. Translation: EAW54238.1. CH471083 Genomic DNA. Translation: EAW54239.1. BC035625 mRNA. Translation: AAH35625.1. X53700 Genomic DNA. No translation available.
IPI	IPI00305368. IPI00797785.
RefSeq	NP_000390.2. NM_000399.3. NP_001129649.1. NM_001136177.1. NP_001129650.1. NM_001136178.1. NP_001129651.1. NM_001136179.1.
UniGene	Hs.1395.
3D structure databases
ProteinModelPortal	P11161.
ModBase	Search...
Protein-protein interaction databases
IntAct	P11161. 9 interactions.
MINT	MINT-234172.
STRING	9606.ENSP00000242480.
PTM databases
PhosphoSite	P11161.
Polymorphism databases
DMDM	33112654.
Proteomic databases
PaxDb	P11161.
PRIDE	P11161.
Protocols and materials databases
DNASU	1959.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000242480; ENSP00000242480; ENSG00000122877. ENST00000411732; ENSP00000387634; ENSG00000122877. ENST00000439032; ENSP00000402040; ENSG00000122877.
GeneID	1959.
KEGG	hsa:1959.
UCSC	uc001jmi.3. human. uc010qio.2. human.
Organism-specific databases
CTD	1959.
GeneCards	GC10M064571.
HGNC	HGNC:3239. EGR2.
MIM	129010. gene. 145900. phenotype. 605253. phenotype. 607678. phenotype.
neXtProt	NX_P11161.
Orphanet	101084. Charcot-Marie-Tooth disease type 1D. 99951. Charcot-Marie-Tooth disease type 4E. 64748. Dejerine-Sottas syndrome.
PharmGKB	PA27674.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5048.
HOGENOM	HOG000036856.
HOVERGEN	HBG003909.
InParanoid	P11161.
KO	K12496.
OMA	GALCSSN.
OrthoDB	EOG41NTMJ.
PhylomeDB	P11161.
Enzyme and pathway databases
Pathway_Interaction_DB	nfat_tfpathway. Calcineurin-regulated NFAT-dependent transcription in lymphocytes. il4_2pathway. IL4-mediated signaling events.
UniPathway	UPA00886.
Gene expression databases
Bgee	P11161.
CleanEx	HS_EGR2.
Genevestigator	P11161.
GermOnline	ENSG00000122877. Homo sapiens.
Family and domain databases
Gene3D	3.30.160.60. 3 hits.
InterPro	IPR021849. DUF3446. IPR007087. Znf_C2H2. IPR015880. Znf_C2H2-like. IPR013087. Znf_C2H2/integrase_DNA-bd. [Graphical view]
Pfam	PF11928. DUF3446. 1 hit. [Graphical view]
SMART	SM00355. ZnF_C2H2. 3 hits. [Graphical view]
PROSITE	PS00028. ZINC_FINGER_C2H2_1. 3 hits. PS50157. ZINC_FINGER_C2H2_2. 3 hits. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	1959.
NextBio	7947.
SOURCE	Search...

Entry information

Entry name

EGR2_HUMAN

Accession

Primary (citable) accession number: P11161
Secondary accession number(s): B2R724 , B3KRD7, Q68CZ5, Q8IV26, Q9UNA6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 19, 2003
Last modified:	May 1, 2013
This is version 147 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.