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P11161 (EGR2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 157. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length476 AA.
Sequence statusComplete.
Protein existenceEvidence 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

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.
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 (Ref.14). Ref.3 Ref.14

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.15 Ref.16 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22

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.17

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 processTranscription
Transcription regulation
Ubl conjugation pathway
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DiseaseCharcot-Marie-Tooth disease
Dejerine-Sottas syndrome
Disease mutation
Neurodegeneration
Neuropathy
   DomainRepeat
Zinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionActivator
Ligase
   PTMUbl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processSchwann cell differentiation

Inferred from electronic annotation. Source: Ensembl

brain development

Traceable author statement Ref.3. Source: ProtInc

brain segmentation

Inferred from electronic annotation. Source: Ensembl

cellular response to cAMP

Inferred from Biological aspect of Ancestor. Source: RefGenome

cellular response to gonadotropin stimulus

Inferred from Biological aspect of Ancestor. Source: RefGenome

facial nerve structural organization

Inferred from electronic annotation. Source: Ensembl

fat cell differentiation

Inferred from sequence or structural similarity. Source: BHF-UCL

learning or memory

Inferred from electronic annotation. Source: Ensembl

motor neuron axon guidance

Inferred from electronic annotation. Source: Ensembl

myelination

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of apoptotic process

Inferred from Biological aspect of Ancestor. Source: RefGenome

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: Ensembl

positive regulation of transcription, DNA-templated

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 Biological aspect of Ancestor. Source: RefGenome

regulation of ossification

Inferred from electronic annotation. Source: Ensembl

response to insulin

Inferred from electronic annotation. Source: Ensembl

rhombomere 3 formation

Inferred from electronic annotation. Source: Ensembl

rhombomere 5 formation

Inferred from electronic annotation. Source: Ensembl

rhythmic behavior

Inferred from electronic annotation. Source: Ensembl

skeletal muscle cell differentiation

Inferred from Biological aspect of Ancestor. Source: RefGenome

transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: BHF-UCL

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionRNA 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

metal ion binding

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

ubiquitin protein ligase binding

Inferred from physical interaction Ref.11. Source: UniProtKB

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 476476E3 SUMO-protein ligase EGR2
PRO_0000047119

Regions

Zinc finger340 – 36425C2H2-type 1
Zinc finger370 – 39223C2H2-type 2
Zinc finger398 – 42023C2H2-type 3
Motif162 – 1654HCFC1-binding-motif (HBM)
Compositional bias300 – 30910Poly-Ala

Natural variations

Alternative sequence1 – 5050Missing in isoform Short.
VSP_006863
Natural variant2681I → N in CHN. Ref.3
VAR_007735
Natural variant3551D → V in CMT1D. Ref.15 Ref.16
VAR_007736
Natural variant3591R → W in DSS and CMT1D; associated with A-136 in the GJB1 gene in a DSS Korean girl. Ref.17 Ref.21 Ref.22
VAR_009874
Natural variant3811R → C in CMT1D. Ref.19
VAR_029958
Natural variant3811R → H in CMT1D. Ref.18
VAR_009875
Natural variant382 – 3832SD → RY in CHN.
VAR_007737
Natural variant3831D → Y in CMT1D. Ref.20
VAR_029959
Natural variant4091R → W in CMT1D. Ref.3
VAR_007738

Experimental info

Mutagenesis162 – 1654DHLY → AAAA: Inhibits association with HCFC1. Ref.10
Sequence conflict681K → R in CAH18435. Ref.5
Sequence conflict2471K → KPFPCPLDTLRVPPPLTPLS TIRK in AAH35625. Ref.8
Sequence conflict2801V → M in AAA52372. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform Long [UniParc].

Last modified July 19, 2003. Version 3.
Checksum: 7810D1B1B418DF1F

FASTA47650,302
        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 

« Hide

Isoform Short [UniParc].

Checksum: DD358E32D00B4353
Show »

FASTA42644,970

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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]"Homozygous deletion of an EGR2 enhancer in congenital amyelinating neuropathy."
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.
Ann. Neurol. 71:719-723(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN CHN.
[15]"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.
[16]"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.
[17]"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.
[18]"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.
[19]"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.
[20]"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.
[21]"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.
[22]"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.

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.
RefSeqNP_000390.2. NM_000399.3.
NP_001129649.1. NM_001136177.1.
NP_001129650.1. NM_001136178.1.
NP_001129651.1. NM_001136179.1.
UniGeneHs.1395.

3D structure databases

ProteinModelPortalP11161.
SMRP11161. Positions 338-463.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108279. 16 interactions.
IntActP11161. 10 interactions.
MINTMINT-234172.
STRING9606.ENSP00000242480.

PTM databases

PhosphoSiteP11161.

Polymorphism databases

DMDM33112654.

Proteomic databases

PaxDbP11161.
PRIDEP11161.

Protocols and materials databases

DNASU1959.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000242480; ENSP00000242480; ENSG00000122877. [P11161-1]
ENST00000411732; ENSP00000387634; ENSG00000122877. [P11161-2]
ENST00000439032; ENSP00000402040; ENSG00000122877. [P11161-1]
GeneID1959.
KEGGhsa:1959.
UCSCuc001jmi.3. human. [P11161-1]
uc010qio.2. human. [P11161-2]

Organism-specific databases

CTD1959.
GeneCardsGC10M064571.
HGNCHGNC:3239. EGR2.
MIM129010. gene.
145900. phenotype.
605253. phenotype.
607678. phenotype.
neXtProtNX_P11161.
Orphanet101084. Charcot-Marie-Tooth disease type 1D.
99951. Charcot-Marie-Tooth disease type 4E.
64748. Dejerine-Sottas syndrome.
PharmGKBPA27674.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5048.
HOGENOMHOG000036856.
HOVERGENHBG003909.
InParanoidP11161.
KOK12496.
OMANPEGVIN.
OrthoDBEOG7Z69C7.
PhylomeDBP11161.
TreeFamTF318980.

Enzyme and pathway databases

SignaLinkP11161.
UniPathwayUPA00886.

Gene expression databases

BgeeP11161.
CleanExHS_EGR2.
GenevestigatorP11161.

Family and domain databases

Gene3D3.30.160.60. 3 hits.
InterProIPR021849. DUF3446.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamPF11928. DUF3446. 1 hit.
[Graphical view]
SMARTSM00355. ZnF_C2H2. 3 hits.
[Graphical view]
PROSITEPS00028. ZINC_FINGER_C2H2_1. 3 hits.
PS50157. ZINC_FINGER_C2H2_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiEGR2.
GenomeRNAi1959.
NextBio7947.
PROP11161.
SOURCESearch...

Entry information

Entry nameEGR2_HUMAN
AccessionPrimary (citable) accession number: P11161
Secondary accession number(s): B2R724 expand/collapse secondary AC list , B3KRD7, Q68CZ5, Q8IV26, Q9UNA6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 19, 2003
Last modified: April 16, 2014
This is version 157 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM