ETV3_HUMAN
ID ETV3_HUMAN Reviewed; 512 AA.
AC P41162; B4E3M7; Q8TAC8; Q9BX30;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=ETS translocation variant 3;
DE AltName: Full=ETS domain transcriptional repressor PE1;
DE Short=PE-1;
DE AltName: Full=Mitogenic Ets transcriptional suppressor;
GN Name=ETV3; Synonyms=METS, PE1;
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 2), AND FUNCTION.
RX PubMed=12007404; DOI=10.1016/s0092-8674(02)00714-6;
RA Klappacher G.W., Lunyak V.V., Sykes D.B., Sawka-Verhelle D., Sage J.,
RA Brard G., Ngo S.D., Gangadharan D., Jacks T., Kamps M.P., Rose D.W.,
RA Rosenfeld M.G., Glass C.K.;
RT "An induced Ets repressor complex regulates growth arrest during terminal
RT macrophage differentiation.";
RL Cell 109:169-180(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Uterus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Bone marrow;
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).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-262 (ISOFORM 1).
RX PubMed=8020980; DOI=10.1006/geno.1994.1169;
RA Klemsz M., Hromas R., Raskind W., Bruno E., Hoffman R.;
RT "PE-1, a novel ETS oncogene family member, localizes to chromosome 1q21-
RT q23.";
RL Genomics 20:291-294(1994).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-388, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139 AND SER-159, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-381, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [11]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-381, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [12]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-381 AND LYS-388, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Transcriptional repressor that contribute to growth arrest
CC during terminal macrophage differentiation by repressing target genes
CC involved in Ras-dependent proliferation. Represses MMP1 promoter
CC activity. {ECO:0000269|PubMed:12007404}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00237}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Long;
CC IsoId=P41162-1; Sequence=Displayed;
CC Name=2; Synonyms=Short;
CC IsoId=P41162-2; Sequence=VSP_013351, VSP_013352;
CC -!- SIMILARITY: Belongs to the ETS family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA60949.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF218540; AAK56846.1; -; mRNA.
DR EMBL; AK304789; BAG65539.1; -; mRNA.
DR EMBL; AK316274; BAH14645.1; -; mRNA.
DR EMBL; AL157713; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW52888.1; -; Genomic_DNA.
DR EMBL; BC022868; AAH22868.1; -; mRNA.
DR EMBL; L16464; AAA60949.1; ALT_FRAME; mRNA.
DR CCDS; CCDS1164.1; -. [P41162-2]
DR CCDS; CCDS44250.1; -. [P41162-1]
DR PIR; A54308; A54308.
DR RefSeq; NP_001138784.1; NM_001145312.1. [P41162-1]
DR RefSeq; NP_005231.1; NM_005240.1. [P41162-2]
DR RefSeq; XP_006711273.1; XM_006711210.2. [P41162-1]
DR AlphaFoldDB; P41162; -.
DR SMR; P41162; -.
DR BioGRID; 108418; 141.
DR IntAct; P41162; 71.
DR MINT; P41162; -.
DR STRING; 9606.ENSP00000357175; -.
DR iPTMnet; P41162; -.
DR PhosphoSitePlus; P41162; -.
DR BioMuta; ETV3; -.
DR DMDM; 62512143; -.
DR EPD; P41162; -.
DR jPOST; P41162; -.
DR MassIVE; P41162; -.
DR MaxQB; P41162; -.
DR PaxDb; P41162; -.
DR PeptideAtlas; P41162; -.
DR PRIDE; P41162; -.
DR ProteomicsDB; 55408; -. [P41162-1]
DR ProteomicsDB; 55409; -. [P41162-2]
DR Antibodypedia; 1438; 65 antibodies from 18 providers.
DR DNASU; 2117; -.
DR Ensembl; ENST00000326786.4; ENSP00000327316.4; ENSG00000117036.12. [P41162-2]
DR Ensembl; ENST00000368192.9; ENSP00000357175.4; ENSG00000117036.12. [P41162-1]
DR GeneID; 2117; -.
DR KEGG; hsa:2117; -.
DR MANE-Select; ENST00000368192.9; ENSP00000357175.4; NM_001145312.3; NP_001138784.1.
DR UCSC; uc001fqr.3; human. [P41162-1]
DR CTD; 2117; -.
DR DisGeNET; 2117; -.
DR GeneCards; ETV3; -.
DR HGNC; HGNC:3492; ETV3.
DR HPA; ENSG00000117036; Low tissue specificity.
DR MIM; 164873; gene.
DR neXtProt; NX_P41162; -.
DR OpenTargets; ENSG00000117036; -.
DR PharmGKB; PA27906; -.
DR VEuPathDB; HostDB:ENSG00000117036; -.
DR eggNOG; KOG3806; Eukaryota.
DR GeneTree; ENSGT00940000160963; -.
DR HOGENOM; CLU_023454_1_0_1; -.
DR InParanoid; P41162; -.
DR OMA; GIYPDPH; -.
DR OrthoDB; 677533at2759; -.
DR PhylomeDB; P41162; -.
DR TreeFam; TF351065; -.
DR PathwayCommons; P41162; -.
DR SignaLink; P41162; -.
DR SIGNOR; P41162; -.
DR BioGRID-ORCS; 2117; 12 hits in 1102 CRISPR screens.
DR ChiTaRS; ETV3; human.
DR GenomeRNAi; 2117; -.
DR Pharos; P41162; Tbio.
DR PRO; PR:P41162; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P41162; protein.
DR Bgee; ENSG00000117036; Expressed in upper arm skin and 185 other tissues.
DR Genevisible; P41162; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0090571; C:RNA polymerase II transcription repressor complex; IEA:Ensembl.
DR GO; GO:0017151; F:DEAD/H-box RNA helicase binding; IEA:Ensembl.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0097011; P:cellular response to granulocyte macrophage colony-stimulating factor stimulus; IEA:Ensembl.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR000418; Ets_dom.
DR InterPro; IPR046328; ETS_fam.
DR InterPro; IPR032929; ETV3.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11849; PTHR11849; 1.
DR PANTHER; PTHR11849:SF30; PTHR11849:SF30; 1.
DR Pfam; PF00178; Ets; 1.
DR PRINTS; PR00454; ETSDOMAIN.
DR SMART; SM00413; ETS; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS00345; ETS_DOMAIN_1; 1.
DR PROSITE; PS00346; ETS_DOMAIN_2; 1.
DR PROSITE; PS50061; ETS_DOMAIN_3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; DNA-binding; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..512
FT /note="ETS translocation variant 3"
FT /id="PRO_0000204114"
FT DNA_BIND 35..116
FT /note="ETS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00237"
FT REGION 136..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 336..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..420
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..490
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R4Z4"
FT MOD_RES 388
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT CROSSLNK 381
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 388
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 135..143
FT /note="VVPQSAPPV -> KIQTLLVGN (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12007404,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_013351"
FT VAR_SEQ 144..512
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12007404,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_013352"
SQ SEQUENCE 512 AA; 57001 MW; 3E50323BF9910062 CRC64;
MKAGCSIVEK PEGGGGYQFP DWAYKTESSP GSRQIQLWHF ILELLQKEEF RHVIAWQQGE
YGEFVIKDPD EVARLWGRRK CKPQMNYDKL SRALRYYYNK RILHKTKGKR FTYKFNFNKL
VMPNYPFINI RSSGVVPQSA PPVPTASSRF HFPPLDTHSP TNDVQPGRFS ASSLTASGQE
SSNGTDRKTE LSELEDGSAA DWRRGVDPVS SRNAIGGGGI GHQKRKPDIM LPLFARPGMY
PDPHSPFAVS PIPGRGGVLN VPISPALSLT PTIFSYSPSP GLSPFTSSSC FSFNPEEMKH
YLHSQACSVF NYHLSPRTFP RYPGLMVPPL QCQMHPEEST QFSIKLQPPP VGRKNRERVE
SSEESAPVTT PTMASIPPRI KVEPASEKDP ESLRQSAREK EEHTQEEGTV PSRTIEEEKG
TIFARPAAPP IWPSVPISTP SGEPLEVTED SEDRPGKEPS APEKKEDALM PPKLRLKRRW
NDDPEARELS KSGKFLWNGS GPQGLATAAA DA
