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Database: UniProt
Entry: P41212
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Original site: P41212 
ID   ETV6_HUMAN              Reviewed;         452 AA.
AC   P41212; A3QVP6; A8K076; Q9UMF6; Q9UMF7; Q9UMG0;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   07-OCT-2020, entry version 211.
DE   RecName: Full=Transcription factor ETV6;
DE   AltName: Full=ETS translocation variant 6;
DE   AltName: Full=ETS-related protein Tel1;
DE            Short=Tel;
GN   Name=ETV6; Synonyms=TEL, TEL1;
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], AND CHROMOSOMAL TRANSLOCATION WITH PDGFRB.
RX   PubMed=8168137; DOI=10.1016/0092-8674(94)90322-0;
RA   Golub T.R., Barker G.F., Lovett M., Gilliland D.G.;
RT   "Fusion of PDGF receptor beta to a novel ets-like gene, tel, in chronic
RT   myelomonocytic leukemia with t(5;12) chromosomal translocation.";
RL   Cell 77:307-316(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Urinary bladder;
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].
RA   Mural R.J., Istrail S., Sutton G.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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 56-109; 111-336 AND 338-452.
RX   PubMed=8743990; DOI=10.1101/gr.6.5.404;
RA   Baens M., Peeters P., Guo C., Aerssens J., Marynen P.;
RT   "Genomic organization of TEL: the human ETS-variant gene 6.";
RL   Genome Res. 6:404-413(1996).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 56-452, AND CHROMOSOMAL TRANSLOCATION WITH
RP   PAX5.
RX   PubMed=17344859; DOI=10.1038/nature05690;
RA   Mullighan C.G., Goorha S., Radtke I., Miller C.B., Coustan-Smith E.,
RA   Dalton J.D., Girtman K., Mathew S., Ma J., Pounds S.B., Su X., Pui C.-H.,
RA   Relling M.V., Evans W.E., Shurtleff S.A., Downing J.R.;
RT   "Genome-wide analysis of genetic alterations in acute lymphoblastic
RT   leukaemia.";
RL   Nature 446:758-764(2007).
RN   [7]
RP   CHROMOSOMAL TRANSLOCATION WITH MN1.
RX   PubMed=7731705;
RA   Buijs A., Sherr S., van Baal S., van Bezouw S., van der Plas D.,
RA   Geurts van Kessel A., Riegman P., Lekanne Deprez R., Zwarthoff E.,
RA   Hagemeijer A.;
RT   "Translocation (12;22) (p13;q11) in myeloproliferative disorders results in
RT   fusion of the ETS-like TEL gene on 12p13 to the MN1 gene on 22q11.";
RL   Oncogene 10:1511-1519(1995).
RN   [8]
RP   CHROMOSOMAL TRANSLOCATION WITH AML1.
RX   PubMed=7761424; DOI=10.1073/pnas.92.11.4917;
RA   Golub T.R., Barker G.F., Bohlander S.K., Hiebert S.W., Ward D.C.,
RA   Bray-Ward P., Morgan E., Raimondi S.C., Rowley J.D., Gilliland D.G.;
RT   "Fusion of the TEL gene on 12p13 to the AML1 gene on 21q22 in acute
RT   lymphoblastic leukemia.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:4917-4921(1995).
RN   [9]
RP   CHROMOSOMAL TRANSLOCATION WITH AML1.
RX   PubMed=7780150;
RA   Romana S.P., Mauchauffe M., le Coniat M., Chumakov I., le Paslier D.,
RA   Berger R., Bernard O.A.;
RT   "The t(12;21) of acute lymphoblastic leukemia results in a tel-AML1 gene
RT   fusion.";
RL   Blood 85:3662-3670(1995).
RN   [10]
RP   CHROMOSOMAL TRANSLOCATIONS WITH JAK2.
RX   PubMed=9326218;
RA   Peeters P., Raynaud S.D., Cools J., Wlodarska I., Grosgeorge J., Philip P.,
RA   Monpoux F., Van Rompaey L., Baens M., Van Den Berghe H., Marynen P.;
RT   "Fusion of TEL, the ETS-variant gene 6 (ETV6), to the receptor-associated
RT   kinase JAK2 as a result of t(9;12) in a lymphoid and t(9;15;12) in a
RT   myeloid leukemia.";
RL   Blood 90:2535-2540(1997).
RN   [11]
RP   CHROMOSOMAL TRANSLOCATION WITH ACSL6.
RX   PubMed=10502316;
RX   DOI=10.1002/(sici)1098-2264(199911)26:3<192::aid-gcc2>3.0.co;2-e;
RA   Yagasaki F., Jinnai I., Yoshida S., Yokoyama Y., Matsuda A., Kusumoto S.,
RA   Kobayashi H., Terasaki H., Ohyashiki K., Asou N., Murohashi I., Bessho M.,
RA   Hirashima K.;
RT   "Fusion of TEL/ETV6 to a novel ACS2 in myelodysplastic syndrome and acute
RT   myelogenous leukemia with t(5;12)(q31;p13).";
RL   Genes Chromosomes Cancer 26:192-202(1999).
RN   [12]
RP   CHROMOSOMAL TRANSLOCATION WITH CHIC2.
RX   PubMed=10477709;
RA   Cools J., Bilhou-Nabera C., Wlodarska I., Cabrol C., Talmant P.,
RA   Bernard P., Hagemeijer A., Marynen P.;
RT   "Fusion of a novel gene, BTL, to ETV6 in acute myeloid leukemias with a
RT   t(4;12)(q11-q12;p13).";
RL   Blood 94:1820-1824(1999).
RN   [13]
RP   PHOSPHORYLATION AT SER-22 AND SER-257, AND MUTAGENESIS OF SER-213; SER-238
RP   AND SER-257.
RX   PubMed=12435397; DOI=10.1016/s0006-291x(02)02588-3;
RA   Arai H., Maki K., Waga K., Sasaki K., Nakamura Y., Imai Y., Kurokawa M.,
RA   Hirai H., Mitani K.;
RT   "Functional regulation of TEL by p38-induced phosphorylation.";
RL   Biochem. Biophys. Res. Commun. 299:116-125(2002).
RN   [14]
RP   CHROMOSOMAL TRANSLOCATION WITH MDS2.
RX   PubMed=12203785; DOI=10.1002/gcc.10090;
RA   Odero M.D., Vizmanos J.L., Roman J.P., Lahortiga I., Panizo C.,
RA   Calasanz M.J., Zeleznik-Le N.J., Rowley J.D., Novo F.J.;
RT   "A novel gene, MDS2, is fused to ETV6/TEL in a t(1;12)(p36.1;p13) in a
RT   patient with myelodysplastic syndrome.";
RL   Genes Chromosomes Cancer 35:11-19(2002).
RN   [15]
RP   INVOLVEMENT IN MPE, AND CHROMOSOMAL TRANSLOCATION WITH PDGFRB.
RX   PubMed=12181402; DOI=10.1056/nejmoa020150;
RA   Apperley J.F., Gardembas M., Melo J.V., Russell-Jones R., Bain B.J.,
RA   Baxter E.J., Chase A., Chessells J.M., Colombat M., Dearden C.E.,
RA   Dimitrijevic S., Mahon F.-X., Marin D., Nikolova Z., Olavarria E.,
RA   Silberman S., Schultheis B., Cross N.C.P., Goldman J.M.;
RT   "Response to imatinib mesylate in patients with chronic myeloproliferative
RT   diseases with rearrangements of the platelet-derived growth factor receptor
RT   beta.";
RL   N. Engl. J. Med. 347:481-487(2002).
RN   [16]
RP   INTERACTION WITH L3MBTL1.
RX   PubMed=12588862; DOI=10.1074/jbc.m300592200;
RA   Boccuni P., MacGrogan D., Scandura J.M., Nimer S.D.;
RT   "The human L(3)MBT Polycomb group protein is a transcriptional repressor
RT   and interacts physically and functionally with TEL (ETV6).";
RL   J. Biol. Chem. 278:15412-15420(2003).
RN   [17]
RP   INTERACTION WITH HDAC9.
RX   PubMed=12590135; DOI=10.1074/jbc.m212935200;
RA   Petrie K., Guidez F., Howell L., Healy L., Waxman S., Greaves M.,
RA   Zelent A.;
RT   "The histone deacetylase 9 gene encodes multiple protein isoforms.";
RL   J. Biol. Chem. 278:16059-16072(2003).
RN   [18]
RP   INVOLVEMENT IN AML, VARIANT GLY-344 INS, AND CHARACTERIZATION OF VARIANT
RP   GLY-344 INS.
RX   PubMed=15806161; DOI=10.1038/sj.onc.1208588;
RA   Barjesteh van Waalwijk van Doorn-Khosrovani S., Spensberger D.,
RA   de Knegt Y., Tang M., Loewenberg B., Delwel R.;
RT   "Somatic heterozygous mutations in ETV6 (TEL) and frequent absence of ETV6
RT   protein in acute myeloid leukemia.";
RL   Oncogene 24:4129-4137(2005).
RN   [19]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [20]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-18 AND SER-22, AND
RP   IDENTIFICATION BY 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   [21]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-11 AND LYS-302, AND
RP   IDENTIFICATION BY MASS 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   [22]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [23]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22 AND SER-213, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [24]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [25]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=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   [26]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-11, 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   [27]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-11, 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   [28]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-11 AND LYS-288, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA   Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA   Vertegaal A.C.;
RT   "System-wide analysis of SUMOylation dynamics in response to replication
RT   stress reveals novel small ubiquitin-like modified target proteins and
RT   acceptor lysines relevant for genome stability.";
RL   Mol. Cell. Proteomics 14:1419-1434(2015).
RN   [29]
RP   FUNCTION, INVOLVEMENT IN THC5, VARIANTS THC5 LEU-214; GLN-369 AND CYS-399,
RP   AND CHARACTERIZATION OF VARIANTS THC5 LEU-214; GLN-369 AND CYS-399.
RX   PubMed=25581430; DOI=10.1038/ng.3177;
RA   Zhang M.Y., Churpek J.E., Keel S.B., Walsh T., Lee M.K., Loeb K.R.,
RA   Gulsuner S., Pritchard C.C., Sanchez-Bonilla M., Delrow J.J., Basom R.S.,
RA   Forouhar M., Gyurkocza B., Schwartz B.S., Neistadt B., Marquez R.,
RA   Mariani C.J., Coats S.A., Hofmann I., Lindsley R.C., Williams D.A.,
RA   Abkowitz J.L., Horwitz M.S., King M.C., Godley L.A., Shimamura A.;
RT   "Germline ETV6 mutations in familial thrombocytopenia and hematologic
RT   malignancy.";
RL   Nat. Genet. 47:180-185(2015).
RN   [30]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-11; LYS-288; LYS-302; LYS-403 AND
RP   LYS-421, AND 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).
RN   [31]
RP   STRUCTURE BY NMR OF 338-442.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of ets domain transcriptional factor ETV6 protein.";
RL   Submitted (DEC-2006) to the PDB data bank.
CC   -!- FUNCTION: Transcriptional repressor; binds to the DNA sequence 5'-
CC       CCGGAAGT-3'. Plays a role in hematopoiesis and malignant
CC       transformation. {ECO:0000269|PubMed:25581430}.
CC   -!- SUBUNIT: Can form homodimers or heterodimers with TEL2 or FLI1.
CC       Interacts with L3MBTL1 and HDAC9. {ECO:0000269|PubMed:12588862,
CC       ECO:0000269|PubMed:12590135}.
CC   -!- INTERACTION:
CC       P41212; Q9BXS5: AP1M1; NbExp=3; IntAct=EBI-1372759, EBI-541426;
CC       P41212; A0A0S2Z4M1: AXIN1; NbExp=3; IntAct=EBI-1372759, EBI-16429430;
CC       P41212; Q9UKV0-3: HDAC9; NbExp=3; IntAct=EBI-1372759, EBI-765476;
CC       P41212; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-1372759, EBI-741158;
CC       P41212; Q13526: PIN1; NbExp=3; IntAct=EBI-1372759, EBI-714158;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- PTM: Phosphorylation of Ser-257 by MAPK14 (p38) inhibits ETV6
CC       transcriptional repression. {ECO:0000269|PubMed:12435397}.
CC   -!- DISEASE: Note=A chromosomal aberration involving ETV6 is found in a
CC       form of chronic myelomonocytic leukemia (CMML). Translocation
CC       t(5;12)(q33;p13) with PDGFRB. It is characterized by abnormal clonal
CC       myeloid proliferation and by progression to acute myelogenous leukemia
CC       (AML). {ECO:0000269|PubMed:8168137}.
CC   -!- DISEASE: Note=Chromosomal aberrations involving ETV6 are found in acute
CC       myeloid leukemia (AML). Translocation t(12;22)(p13;q11) with MN1
CC       (PubMed:7731705). Translocation t(4;12)(q12;p13) with CHIC2
CC       (PubMed:10477709). {ECO:0000269|PubMed:10477709,
CC       ECO:0000269|PubMed:7731705}.
CC   -!- DISEASE: Note=Chromosomal aberrations involving ETV6 are found in
CC       childhood acute lymphoblastic leukemia (ALL). Translocations
CC       t(12;21)(p12;q22) and t(12;21)(p13;q22) with RUNX1/AML1.
CC       {ECO:0000269|PubMed:7761424}.
CC   -!- DISEASE: Note=A chromosomal aberration involving ETV6 is found in a
CC       form of pre-B acute lymphoid leukemia. Translocation t(9;12)(p24;p13)
CC       with JAK2. {ECO:0000269|PubMed:9326218}.
CC   -!- DISEASE: Note=A chromosomal aberration involving ETV6 and JAK2 is found
CC       in an atypical chronic myelogenous leukemia. Translocation
CC       t(9;15;12)(p24;q15;p13). {ECO:0000269|PubMed:9326218}.
CC   -!- DISEASE: Note=A chromosomal aberration involving ETV6 is found in
CC       myelodysplastic syndrome (MDS) with basophilia. Translocation
CC       t(5;12)(q31;p13) with ACSL6. {ECO:0000269|PubMed:10502316}.
CC   -!- DISEASE: Note=A chromosomal aberration involving ETV6 is found in acute
CC       eosinophilic leukemia (AEL). Translocation t(5;12)(q31;p13) with ACSL6.
CC       {ECO:0000269|PubMed:10502316}.
CC   -!- DISEASE: Note=A chromosomal aberration involving ETV6 is found in
CC       myelodysplastic syndrome (MDS). Translocation t(1;12)(p36.1;p13) with
CC       MDS2. {ECO:0000269|PubMed:12203785}.
CC   -!- DISEASE: Note=A chromosomal aberration involving ETV6 is found in acute
CC       lymphoblastic leukemia. Translocation t(9;12)(p13;p13) with PAX5.
CC       {ECO:0000269|PubMed:17344859}.
CC   -!- DISEASE: Myeloproliferative disorder chronic with eosinophilia (MPE)
CC       [MIM:131440]: A hematologic disorder characterized by malignant
CC       eosinophils proliferation. {ECO:0000269|PubMed:12181402}. Note=The gene
CC       represented in this entry is involved in disease pathogenesis. A
CC       chromosomal aberration involving ETV6 is found in many instances of
CC       myeloproliferative disorder chronic with eosinophilia. Translocation
CC       t(5;12) with PDGFRB on chromosome 5 creating an ETV6-PDGFRB fusion
CC       protein. {ECO:0000269|PubMed:12181402}.
CC   -!- DISEASE: Leukemia, acute myelogenous (AML) [MIM:601626]: A subtype of
CC       acute leukemia, a cancer of the white blood cells. AML is a malignant
CC       disease of bone marrow characterized by maturational arrest of
CC       hematopoietic precursors at an early stage of development. Clonal
CC       expansion of myeloid blasts occurs in bone marrow, blood, and other
CC       tissue. Myelogenous leukemias develop from changes in cells that
CC       normally produce neutrophils, basophils, eosinophils and monocytes.
CC       {ECO:0000269|PubMed:15806161}. Note=The gene represented in this entry
CC       is involved in disease pathogenesis.
CC   -!- DISEASE: Thrombocytopenia 5 (THC5) [MIM:616216]: Thrombocytopenia is
CC       defined by a decrease in the number of platelets in circulating blood,
CC       resulting in the potential for increased bleeding and decreased ability
CC       for clotting. THC5 is an autosomal dominant disorder, associated with
CC       an increased susceptibility to the development of hematologic and solid
CC       malignancies. {ECO:0000269|PubMed:25581430}. Note=The disease is caused
CC       by mutations affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the ETS family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABI30005.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/ETV6ID38.html";
DR   EMBL; U11732; AAA19786.1; -; mRNA.
DR   EMBL; AK289441; BAF82130.1; -; mRNA.
DR   EMBL; CH471094; EAW96240.1; -; Genomic_DNA.
DR   EMBL; BC043399; AAH43399.1; -; mRNA.
DR   EMBL; U61375; AAC50690.1; -; Genomic_DNA.
DR   EMBL; U63312; AAB17134.1; -; Genomic_DNA.
DR   EMBL; U63313; AAB17135.1; -; Genomic_DNA.
DR   EMBL; DQ841178; ABI30005.1; ALT_INIT; mRNA.
DR   CCDS; CCDS8643.1; -.
DR   RefSeq; NP_001978.1; NM_001987.4.
DR   PDB; 1JI7; X-ray; 1.45 A; A/B/C=47-123.
DR   PDB; 1LKY; X-ray; 2.30 A; A/B/C/D/E/F=47-123.
DR   PDB; 2DAO; NMR; -; A=338-442.
DR   PDB; 2QAR; X-ray; 2.40 A; A/B/D/E=47-124.
DR   PDB; 2QB0; X-ray; 2.56 A; A/C=47-123.
DR   PDB; 2QB1; X-ray; 2.61 A; A/B=47-121.
DR   PDB; 5L0P; X-ray; 2.30 A; A=47-356.
DR   PDBsum; 1JI7; -.
DR   PDBsum; 1LKY; -.
DR   PDBsum; 2DAO; -.
DR   PDBsum; 2QAR; -.
DR   PDBsum; 2QB0; -.
DR   PDBsum; 2QB1; -.
DR   PDBsum; 5L0P; -.
DR   BMRB; P41212; -.
DR   SMR; P41212; -.
DR   BioGRID; 108421; 45.
DR   DIP; DIP-17028N; -.
DR   ELM; P41212; -.
DR   IntAct; P41212; 24.
DR   MINT; P41212; -.
DR   STRING; 9606.ENSP00000379658; -.
DR   BindingDB; P41212; -.
DR   ChEMBL; CHEMBL2401606; -.
DR   DrugCentral; P41212; -.
DR   iPTMnet; P41212; -.
DR   PhosphoSitePlus; P41212; -.
DR   BioMuta; ETV6; -.
DR   DMDM; 730927; -.
DR   EPD; P41212; -.
DR   jPOST; P41212; -.
DR   MassIVE; P41212; -.
DR   MaxQB; P41212; -.
DR   PaxDb; P41212; -.
DR   PeptideAtlas; P41212; -.
DR   PRIDE; P41212; -.
DR   ProteomicsDB; 55416; -.
DR   Antibodypedia; 634; 377 antibodies.
DR   DNASU; 2120; -.
DR   Ensembl; ENST00000396373; ENSP00000379658; ENSG00000139083.
DR   GeneID; 2120; -.
DR   KEGG; hsa:2120; -.
DR   UCSC; uc001qzz.4; human.
DR   CTD; 2120; -.
DR   DisGeNET; 2120; -.
DR   EuPathDB; HostDB:ENSG00000139083.10; -.
DR   GeneCards; ETV6; -.
DR   HGNC; HGNC:3495; ETV6.
DR   HPA; ENSG00000139083; Low tissue specificity.
DR   MalaCards; ETV6; -.
DR   MIM; 131440; phenotype.
DR   MIM; 600618; gene.
DR   MIM; 601626; phenotype.
DR   MIM; 616216; phenotype.
DR   neXtProt; NX_P41212; -.
DR   OpenTargets; ENSG00000139083; -.
DR   Orphanet; 98823; Chronic myelomonocytic leukemia.
DR   Orphanet; 2665; Congenital mesoblastic nephroma.
DR   Orphanet; 146; Differentiated thyroid carcinoma.
DR   Orphanet; 71290; Familial platelet disorder with associated myeloid malignancy.
DR   Orphanet; 2030; Fibrosarcoma.
DR   Orphanet; 99860; Precursor B-cell acute lymphoblastic leukemia.
DR   Orphanet; 314950; Primary hypereosinophilic syndrome.
DR   PharmGKB; PA27909; -.
DR   eggNOG; KOG3804; Eukaryota.
DR   GeneTree; ENSGT00940000159508; -.
DR   HOGENOM; CLU_037998_1_0_1; -.
DR   InParanoid; P41212; -.
DR   KO; K03211; -.
DR   OMA; CIKQERI; -.
DR   OrthoDB; 559763at2759; -.
DR   PhylomeDB; P41212; -.
DR   TreeFam; TF318679; -.
DR   PathwayCommons; P41212; -.
DR   Reactome; R-HSA-9673768; Signaling by membrane-tethered fusions of PDGFRA or PDGFRB.
DR   SIGNOR; P41212; -.
DR   BioGRID-ORCS; 2120; 20 hits in 897 CRISPR screens.
DR   ChiTaRS; ETV6; human.
DR   EvolutionaryTrace; P41212; -.
DR   GeneWiki; ETV6; -.
DR   GenomeRNAi; 2120; -.
DR   Pharos; P41212; Tbio.
DR   PRO; PR:P41212; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; P41212; protein.
DR   Bgee; ENSG00000139083; Expressed in mammary gland and 206 other tissues.
DR   ExpressionAtlas; P41212; baseline and differential.
DR   Genevisible; P41212; HS.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0042025; C:host cell nucleus; IEA:InterPro.
DR   GO; GO:0000790; C:nuclear chromatin; ISA:NTNU_SB.
DR   GO; GO:0005730; C:nucleolus; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR   GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0071425; P:hematopoietic stem cell proliferation; IMP:UniProtKB.
DR   GO; GO:0097152; P:mesenchymal cell apoptotic process; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR   GO; GO:0022008; P:neurogenesis; IEA:Ensembl.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0007296; P:vitellogenesis; IEA:Ensembl.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 1.10.150.50; -; 1.
DR   InterPro; IPR000418; Ets_dom.
DR   InterPro; IPR003118; Pointed_dom.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF00178; Ets; 1.
DR   Pfam; PF02198; SAM_PNT; 1.
DR   PRINTS; PR00454; ETSDOMAIN.
DR   SMART; SM00413; ETS; 1.
DR   SMART; SM00251; SAM_PNT; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF47769; SSF47769; 1.
DR   PROSITE; PS00346; ETS_DOMAIN_2; 1.
DR   PROSITE; PS50061; ETS_DOMAIN_3; 1.
DR   PROSITE; PS51433; PNT; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Chromosomal rearrangement; Disease mutation;
KW   DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein; Proto-oncogene;
KW   Reference proteome; Repressor; Transcription; Transcription regulation;
KW   Ubl conjugation.
FT   CHAIN           1..452
FT                   /note="Transcription factor ETV6"
FT                   /id="PRO_0000204121"
FT   DOMAIN          40..124
FT                   /note="PNT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00762"
FT   DNA_BIND        339..420
FT                   /note="ETS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00237"
FT   SITE            11..12
FT                   /note="Breakpoint for translocation to form CHIC2-ETV6 in
FT                   AML"
FT   SITE            54..55
FT                   /note="Breakpoint for translocation to form ETV6-MDS2 in
FT                   MDS"
FT   SITE            55..56
FT                   /note="Breakpoint for translocation to form PAX5-ETV6"
FT   SITE            336..337
FT                   /note="Breakpoint for translocation to form ETV6-AML1 in
FT                   ALL"
FT   MOD_RES         11
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000244|PubMed:19608861"
FT   MOD_RES         18
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000244|PubMed:19690332"
FT   MOD_RES         22
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:19690332, ECO:0000244|PubMed:20068231,
FT                   ECO:0000244|PubMed:21406692, ECO:0000269|PubMed:12435397"
FT   MOD_RES         213
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:21406692"
FT   MOD_RES         238
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P97360"
FT   MOD_RES         257
FT                   /note="Phosphoserine; by MAPK14"
FT                   /evidence="ECO:0000269|PubMed:12435397"
FT   MOD_RES         302
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000244|PubMed:19608861"
FT   MOD_RES         323
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P97360"
FT   CROSSLNK        11
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000244|PubMed:25218447,
FT                   ECO:0000244|PubMed:25755297, ECO:0000244|PubMed:25772364,
FT                   ECO:0000244|PubMed:28112733"
FT   CROSSLNK        288
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000244|PubMed:25755297,
FT                   ECO:0000244|PubMed:28112733"
FT   CROSSLNK        302
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000244|PubMed:28112733"
FT   CROSSLNK        403
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000244|PubMed:28112733"
FT   CROSSLNK        421
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000244|PubMed:28112733"
FT   VARIANT         214
FT                   /note="P -> L (in THC5; abrogates DNA binding; alters
FT                   subcellular location; decreases transcriptional repression
FT                   in a dominant-negative fashion; dbSNP:rs724159947)"
FT                   /evidence="ECO:0000269|PubMed:25581430"
FT                   /id="VAR_073322"
FT   VARIANT         344
FT                   /note="Y -> YG (in one individual with AML; somatic
FT                   mutation; unable to repress transcription)"
FT                   /evidence="ECO:0000269|PubMed:15806161"
FT                   /id="VAR_034600"
FT   VARIANT         369
FT                   /note="R -> Q (in THC5; abrogates DNA binding; alters
FT                   subcellular location; decreases transcriptional repression
FT                   in a dominant-negative fashion; dbSNP:rs724159946)"
FT                   /evidence="ECO:0000269|PubMed:25581430"
FT                   /id="VAR_073323"
FT   VARIANT         399
FT                   /note="R -> C (in THC5; abrogates DNA binding; alters
FT                   subcellular location; decreases transcriptional repression
FT                   in a dominant-negative fashion; dbSNP:rs724159945)"
FT                   /evidence="ECO:0000269|PubMed:25581430"
FT                   /id="VAR_073324"
FT   MUTAGEN         22
FT                   /note="S->A: No effect."
FT   MUTAGEN         213
FT                   /note="S->A: No effect."
FT                   /evidence="ECO:0000269|PubMed:12435397"
FT   MUTAGEN         238
FT                   /note="S->A: No effect."
FT                   /evidence="ECO:0000269|PubMed:12435397"
FT   MUTAGEN         257
FT                   /note="S->A: No phosphorylation by MAPK14."
FT                   /evidence="ECO:0000269|PubMed:12435397"
FT   HELIX           12..18
FT                   /evidence="ECO:0000244|PDB:5L0P"
FT   TURN            20..22
FT                   /evidence="ECO:0000244|PDB:5L0P"
FT   HELIX           23..27
FT                   /evidence="ECO:0000244|PDB:5L0P"
FT   HELIX           30..38
FT                   /evidence="ECO:0000244|PDB:5L0P"
FT   HELIX           52..54
FT                   /evidence="ECO:0000244|PDB:1JI7"
FT   HELIX           58..60
FT                   /evidence="ECO:0000244|PDB:1JI7"
FT   HELIX           63..76
FT                   /evidence="ECO:0000244|PDB:1JI7"
FT   TURN            84..87
FT                   /evidence="ECO:0000244|PDB:1JI7"
FT   HELIX           91..94
FT                   /evidence="ECO:0000244|PDB:1JI7"
FT   HELIX           99..105
FT                   /evidence="ECO:0000244|PDB:1JI7"
FT   TURN            107..109
FT                   /evidence="ECO:0000244|PDB:1JI7"
FT   HELIX           110..122
FT                   /evidence="ECO:0000244|PDB:1JI7"
FT   HELIX           341..350
FT                   /evidence="ECO:0000244|PDB:2DAO"
FT   HELIX           352..354
FT                   /evidence="ECO:0000244|PDB:2DAO"
FT   TURN            355..357
FT                   /evidence="ECO:0000244|PDB:2DAO"
FT   STRAND          358..362
FT                   /evidence="ECO:0000244|PDB:2DAO"
FT   HELIX           363..365
FT                   /evidence="ECO:0000244|PDB:2DAO"
FT   STRAND          367..371
FT                   /evidence="ECO:0000244|PDB:2DAO"
FT   HELIX           373..383
FT                   /evidence="ECO:0000244|PDB:2DAO"
FT   HELIX           391..403
FT                   /evidence="ECO:0000244|PDB:2DAO"
FT   STRAND          406..408
FT                   /evidence="ECO:0000244|PDB:2DAO"
FT   STRAND          411..419
FT                   /evidence="ECO:0000244|PDB:2DAO"
FT   HELIX           424..426
FT                   /evidence="ECO:0000244|PDB:2DAO"
FT   STRAND          430..432
FT                   /evidence="ECO:0000244|PDB:2DAO"
FT   HELIX           434..438
FT                   /evidence="ECO:0000244|PDB:2DAO"
SQ   SEQUENCE   452 AA;  53000 MW;  DEC45682ECADECBB CRC64;
     MSETPAQCSI KQERISYTPP ESPVPSYASS TPLHVPVPRA LRMEEDSIRL PAHLRLQPIY
     WSRDDVAQWL KWAENEFSLR PIDSNTFEMN GKALLLLTKE DFRYRSPHSG DVLYELLQHI
     LKQRKPRILF SPFFHPGNSI HTQPEVILHQ NHEEDNCVQR TPRPSVDNVH HNPPTIELLH
     RSRSPITTNH RPSPDPEQRP LRSPLDNMIR RLSPAERAQG PRPHQENNHQ ESYPLSVSPM
     ENNHCPASSE SHPKPSSPRQ ESTRVIQLMP SPIMHPLILN PRHSVDFKQS RLSEDGLHRE
     GKPINLSHRE DLAYMNHIMV SVSPPEEHAM PIGRIADCRL LWDYVYQLLS DSRYENFIRW
     EDKESKIFRI VDPNGLARLW GNHKNRTNMT YEKMSRALRH YYKLNIIRKE PGQRLLFRFM
     KTPDEIMSGR TDRLEHLESQ ELDEQIYQED EC
//
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