EGR3_HUMAN
ID EGR3_HUMAN Reviewed; 387 AA.
AC Q06889; A8K8U9; B4DHJ5; E7EW38; Q2M3W2;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Early growth response protein 3;
DE Short=EGR-3;
DE AltName: Full=Zinc finger protein pilot;
GN Name=EGR3; Synonyms=PILOT;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Peripheral blood T-cell;
RX PubMed=8443122; DOI=10.1093/intimm/5.1.63;
RA Mages H.W., Stamminger T., Rilke O., Bravo R., Kroczek R.A.;
RT "Expression of PILOT, a putative transcription factor, requires two signals
RT and is cyclosporin A sensitive in T cells.";
RL Int. Immunol. 5:63-70(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=1906159;
RA Patwardhan S., Gashler A., Siegel M.G., Chang L.C., Joseph L.J.,
RA Shows T.B., le Beau M.M., Sukhatme V.P.;
RT "EGR3, a novel member of the Egr family of genes encoding immediate-early
RT transcription factors.";
RL Oncogene 6:917-928(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Probable transcription factor involved in muscle spindle
CC development.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q06889-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q06889-2; Sequence=VSP_045954;
CC -!- DEVELOPMENTAL STAGE: In T-cells, expressed 20 minutes following
CC activation.
CC -!- SIMILARITY: Belongs to the EGR C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
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DR EMBL; X63741; CAA45275.1; -; mRNA.
DR EMBL; S40832; AAB19317.1; -; mRNA.
DR EMBL; AK292464; BAF85153.1; -; mRNA.
DR EMBL; AK295134; BAG58157.1; -; mRNA.
DR EMBL; AK313604; BAG36369.1; -; mRNA.
DR EMBL; AC105046; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC104765; AAI04766.1; -; mRNA.
DR EMBL; BC112279; AAI12280.1; -; mRNA.
DR CCDS; CCDS56528.1; -. [Q06889-2]
DR CCDS; CCDS6033.1; -. [Q06889-1]
DR PIR; S60519; S19885.
DR RefSeq; NP_001186809.1; NM_001199880.1. [Q06889-2]
DR RefSeq; NP_001186810.1; NM_001199881.1.
DR RefSeq; NP_004421.2; NM_004430.2. [Q06889-1]
DR RefSeq; XP_005273483.1; XM_005273426.3. [Q06889-2]
DR AlphaFoldDB; Q06889; -.
DR SMR; Q06889; -.
DR IntAct; Q06889; 3.
DR STRING; 9606.ENSP00000318057; -.
DR GlyConnect; 2036; 1 N-Linked glycan (1 site).
DR GlyGen; Q06889; 1 site, 1 N-linked glycan (1 site).
DR iPTMnet; Q06889; -.
DR PhosphoSitePlus; Q06889; -.
DR BioMuta; EGR3; -.
DR DMDM; 730328; -.
DR MassIVE; Q06889; -.
DR PaxDb; Q06889; -.
DR PeptideAtlas; Q06889; -.
DR PRIDE; Q06889; -.
DR ProteomicsDB; 18765; -.
DR ProteomicsDB; 58487; -. [Q06889-1]
DR TopDownProteomics; Q06889-1; -. [Q06889-1]
DR Antibodypedia; 22692; 240 antibodies from 28 providers.
DR DNASU; 1960; -.
DR Ensembl; ENST00000317216.3; ENSP00000318057.2; ENSG00000179388.9. [Q06889-1]
DR Ensembl; ENST00000522910.1; ENSP00000430310.1; ENSG00000179388.9. [Q06889-2]
DR GeneID; 1960; -.
DR KEGG; hsa:1960; -.
DR MANE-Select; ENST00000317216.3; ENSP00000318057.2; NM_004430.3; NP_004421.2.
DR UCSC; uc003xcm.2; human. [Q06889-1]
DR CTD; 1960; -.
DR DisGeNET; 1960; -.
DR GeneCards; EGR3; -.
DR HGNC; HGNC:3240; EGR3.
DR HPA; ENSG00000179388; Tissue enhanced (brain).
DR MIM; 602419; gene.
DR neXtProt; NX_Q06889; -.
DR OpenTargets; ENSG00000179388; -.
DR PharmGKB; PA27675; -.
DR VEuPathDB; HostDB:ENSG00000179388; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000160355; -.
DR HOGENOM; CLU_043235_0_0_1; -.
DR InParanoid; Q06889; -.
DR OMA; GEVEPMY; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q06889; -.
DR TreeFam; TF318980; -.
DR PathwayCommons; Q06889; -.
DR Reactome; R-HSA-9031628; NGF-stimulated transcription.
DR SignaLink; Q06889; -.
DR SIGNOR; Q06889; -.
DR BioGRID-ORCS; 1960; 13 hits in 1094 CRISPR screens.
DR ChiTaRS; EGR3; human.
DR GeneWiki; EGR3; -.
DR GenomeRNAi; 1960; -.
DR Pharos; Q06889; Tbio.
DR PRO; PR:Q06889; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q06889; protein.
DR Bgee; ENSG00000179388; Expressed in upper leg skin and 171 other tissues.
DR ExpressionAtlas; Q06889; baseline and differential.
DR Genevisible; Q06889; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0045202; C:synapse; IEA:GOC.
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; TAS:ProtInc.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
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:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; IDA:BHF-UCL.
DR GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IMP:BHF-UCL.
DR GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; IMP:BHF-UCL.
DR GO; GO:0007623; P:circadian rhythm; TAS:ProtInc.
DR GO; GO:0035767; P:endothelial cell chemotaxis; IMP:BHF-UCL.
DR GO; GO:0007517; P:muscle organ development; TAS:ProtInc.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:BHF-UCL.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; IEA:Ensembl.
DR GO; GO:0007422; P:peripheral nervous system development; IEA:Ensembl.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IMP:BHF-UCL.
DR GO; GO:0033089; P:positive regulation of T cell differentiation in thymus; IEA:Ensembl.
DR GO; GO:0045586; P:regulation of gamma-delta T cell differentiation; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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 Alternative splicing; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..387
FT /note="Early growth response protein 3"
FT /id="PRO_0000047125"
FT ZN_FING 275..299
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 305..327
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 333..355
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 241..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..283
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..51
FT /note="MTGKLAEKLPVTMSSLLNQLPDNLYPEEIPSALNLFSGSSDSVVHYNQMAT
FT -> MEPCAAWSPRGGR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045954"
FT CONFLICT 102
FT /note="I -> T (in Ref. 3; BAG58157)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="I -> T (in Ref. 2; AAB19317)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 387 AA; 42613 MW; 77FAF7D5A278C68E CRC64;
MTGKLAEKLP VTMSSLLNQL PDNLYPEEIP SALNLFSGSS DSVVHYNQMA TENVMDIGLT
NEKPNPELSY SGSFQPAPGN KTVTYLGKFA FDSPSNWCQD NIISLMSAGI LGVPPASGAL
STQTSTASMV QPPQGDVEAM YPALPPYSNC GDLYSEPVSF HDPQGNPGLA YSPQDYQSAK
PALDSNLFPM IPDYNLYHHP NDMGSIPEHK PFQGMDPIRV NPPPITPLET IKAFKDKQIH
PGFGSLPQPP LTLKPIRPRK YPNRPSKTPL HERPHACPAE GCDRRFSRSD ELTRHLRIHT
GHKPFQCRIC MRSFSRSDHL TTHIRTHTGE KPFACEFCGR KFARSDERKR HAKIHLKQKE
KKAEKGGAPS ASSAPPVSLA PVVTTCA
