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Transcription factor ETV6 (ETS translocation variant 6) (ETS-related protein Tel1) (Tel)

 ETV6_HUMAN              Reviewed;         452 AA.
P41212; A3QVP6; A8K076; Q9UMF6; Q9UMF7; Q9UMG0;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 1.
20-JUN-2018, entry version 194.
RecName: Full=Transcription factor ETV6;
AltName: Full=ETS translocation variant 6;
AltName: Full=ETS-related protein Tel1;
Short=Tel;
Name=ETV6; Synonyms=TEL, TEL1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND CHROMOSOMAL TRANSLOCATION WITH PDGFRB.
PubMed=8168137; DOI=10.1016/0092-8674(94)90322-0;
Golub T.R., Barker G.F., Lovett M., Gilliland D.G.;
"Fusion of PDGF receptor beta to a novel ets-like gene, tel, in
chronic myelomonocytic leukemia with t(5;12) chromosomal
translocation.";
Cell 77:307-316(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Urinary bladder;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 56-109; 111-336 AND 338-452.
PubMed=8743990; DOI=10.1101/gr.6.5.404;
Baens M., Peeters P., Guo C., Aerssens J., Marynen P.;
"Genomic organization of TEL: the human ETS-variant gene 6.";
Genome Res. 6:404-413(1996).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 56-452, AND CHROMOSOMAL TRANSLOCATION
WITH PAX5.
PubMed=17344859; DOI=10.1038/nature05690;
Mullighan C.G., Goorha S., Radtke I., Miller C.B., Coustan-Smith E.,
Dalton J.D., Girtman K., Mathew S., Ma J., Pounds S.B., Su X.,
Pui C.-H., Relling M.V., Evans W.E., Shurtleff S.A., Downing J.R.;
"Genome-wide analysis of genetic alterations in acute lymphoblastic
leukaemia.";
Nature 446:758-764(2007).
[7]
CHROMOSOMAL TRANSLOCATION WITH MN1.
PubMed=7731705;
Buijs A., Sherr S., van Baal S., van Bezouw S., van der Plas D.,
Geurts van Kessel A., Riegman P., Lekanne Deprez R., Zwarthoff E.,
Hagemeijer A.;
"Translocation (12;22) (p13;q11) in myeloproliferative disorders
results in fusion of the ETS-like TEL gene on 12p13 to the MN1 gene on
22q11.";
Oncogene 10:1511-1519(1995).
[8]
CHROMOSOMAL TRANSLOCATION WITH AML1.
PubMed=7761424; DOI=10.1073/pnas.92.11.4917;
Golub T.R., Barker G.F., Bohlander S.K., Hiebert S.W., Ward D.C.,
Bray-Ward P., Morgan E., Raimondi S.C., Rowley J.D., Gilliland D.G.;
"Fusion of the TEL gene on 12p13 to the AML1 gene on 21q22 in acute
lymphoblastic leukemia.";
Proc. Natl. Acad. Sci. U.S.A. 92:4917-4921(1995).
[9]
CHROMOSOMAL TRANSLOCATION WITH AML1.
PubMed=7780150;
Romana S.P., Mauchauffe M., le Coniat M., Chumakov I., le Paslier D.,
Berger R., Bernard O.A.;
"The t(12;21) of acute lymphoblastic leukemia results in a tel-AML1
gene fusion.";
Blood 85:3662-3670(1995).
[10]
CHROMOSOMAL TRANSLOCATIONS WITH JAK2.
PubMed=9326218;
Peeters P., Raynaud S.D., Cools J., Wlodarska I., Grosgeorge J.,
Philip P., Monpoux F., Van Rompaey L., Baens M., Van Den Berghe H.,
Marynen P.;
"Fusion of TEL, the ETS-variant gene 6 (ETV6), to the receptor-
associated kinase JAK2 as a result of t(9;12) in a lymphoid and
t(9;15;12) in a myeloid leukemia.";
Blood 90:2535-2540(1997).
[11]
CHROMOSOMAL TRANSLOCATION WITH ACSL6.
PubMed=10502316;
DOI=10.1002/(SICI)1098-2264(199911)26:3<192::AID-GCC2>3.0.CO;2-E;
Yagasaki F., Jinnai I., Yoshida S., Yokoyama Y., Matsuda A.,
Kusumoto S., Kobayashi H., Terasaki H., Ohyashiki K., Asou N.,
Murohashi I., Bessho M., Hirashima K.;
"Fusion of TEL/ETV6 to a novel ACS2 in myelodysplastic syndrome and
acute myelogenous leukemia with t(5;12)(q31;p13).";
Genes Chromosomes Cancer 26:192-202(1999).
[12]
CHROMOSOMAL TRANSLOCATION WITH CHIC2.
PubMed=10477709;
Cools J., Bilhou-Nabera C., Wlodarska I., Cabrol C., Talmant P.,
Bernard P., Hagemeijer A., Marynen P.;
"Fusion of a novel gene, BTL, to ETV6 in acute myeloid leukemias with
a t(4;12)(q11-q12;p13).";
Blood 94:1820-1824(1999).
[13]
PHOSPHORYLATION AT SER-22 AND SER-257, AND MUTAGENESIS OF SER-213;
SER-238 AND SER-257.
PubMed=12435397; DOI=10.1016/S0006-291X(02)02588-3;
Arai H., Maki K., Waga K., Sasaki K., Nakamura Y., Imai Y.,
Kurokawa M., Hirai H., Mitani K.;
"Functional regulation of TEL by p38-induced phosphorylation.";
Biochem. Biophys. Res. Commun. 299:116-125(2002).
[14]
CHROMOSOMAL TRANSLOCATION WITH MDS2.
PubMed=12203785; DOI=10.1002/gcc.10090;
Odero M.D., Vizmanos J.L., Roman J.P., Lahortiga I., Panizo C.,
Calasanz M.J., Zeleznik-Le N.J., Rowley J.D., Novo F.J.;
"A novel gene, MDS2, is fused to ETV6/TEL in a t(1;12)(p36.1;p13) in a
patient with myelodysplastic syndrome.";
Genes Chromosomes Cancer 35:11-19(2002).
[15]
INVOLVEMENT IN MPE, AND CHROMOSOMAL TRANSLOCATION WITH PDGFRB.
PubMed=12181402; DOI=10.1056/NEJMoa020150;
Apperley J.F., Gardembas M., Melo J.V., Russell-Jones R., Bain B.J.,
Baxter E.J., Chase A., Chessells J.M., Colombat M., Dearden C.E.,
Dimitrijevic S., Mahon F.-X., Marin D., Nikolova Z., Olavarria E.,
Silberman S., Schultheis B., Cross N.C.P., Goldman J.M.;
"Response to imatinib mesylate in patients with chronic
myeloproliferative diseases with rearrangements of the platelet-
derived growth factor receptor beta.";
N. Engl. J. Med. 347:481-487(2002).
[16]
INTERACTION WITH L3MBTL1.
PubMed=12588862; DOI=10.1074/jbc.M300592200;
Boccuni P., MacGrogan D., Scandura J.M., Nimer S.D.;
"The human L(3)MBT Polycomb group protein is a transcriptional
repressor and interacts physically and functionally with TEL (ETV6).";
J. Biol. Chem. 278:15412-15420(2003).
[17]
INTERACTION WITH HDAC9.
PubMed=12590135; DOI=10.1074/jbc.M212935200;
Petrie K., Guidez F., Howell L., Healy L., Waxman S., Greaves M.,
Zelent A.;
"The histone deacetylase 9 gene encodes multiple protein isoforms.";
J. Biol. Chem. 278:16059-16072(2003).
[18]
INVOLVEMENT IN AML, VARIANT GLY-344 INS, AND CHARACTERIZATION OF
VARIANT GLY-344 INS.
PubMed=15806161; DOI=10.1038/sj.onc.1208588;
Barjesteh van Waalwijk van Doorn-Khosrovani S., Spensberger D.,
de Knegt Y., Tang M., Loewenberg B., Delwel R.;
"Somatic heterozygous mutations in ETV6 (TEL) and frequent absence of
ETV6 protein in acute myeloid leukemia.";
Oncogene 24:4129-4137(2005).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-18 AND SER-22, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[21]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-11 AND LYS-302, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22 AND SER-213, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[25]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[26]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-11, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[27]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-11, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[28]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-11 AND LYS-288, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[29]
FUNCTION, INVOLVEMENT IN THC5, VARIANTS THC5 LEU-214; GLN-369 AND
CYS-399, AND CHARACTERIZATION OF VARIANTS THC5 LEU-214; GLN-369 AND
CYS-399.
PubMed=25581430; DOI=10.1038/ng.3177;
Zhang M.Y., Churpek J.E., Keel S.B., Walsh T., Lee M.K., Loeb K.R.,
Gulsuner S., Pritchard C.C., Sanchez-Bonilla M., Delrow J.J.,
Basom R.S., Forouhar M., Gyurkocza B., Schwartz B.S., Neistadt B.,
Marquez R., Mariani C.J., Coats S.A., Hofmann I., Lindsley R.C.,
Williams D.A., Abkowitz J.L., Horwitz M.S., King M.C., Godley L.A.,
Shimamura A.;
"Germline ETV6 mutations in familial thrombocytopenia and hematologic
malignancy.";
Nat. Genet. 47:180-185(2015).
[30]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-11; LYS-288; LYS-302;
LYS-403 AND LYS-421, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[31]
STRUCTURE BY NMR OF 338-442.
RIKEN structural genomics initiative (RSGI);
"Solution structure of ets domain transcriptional factor ETV6
protein.";
Submitted (DEC-2006) to the PDB data bank.
-!- FUNCTION: Transcriptional repressor; binds to the DNA sequence 5'-
CCGGAAGT-3'. Plays a role in hematopoiesis and malignant
transformation. {ECO:0000269|PubMed:25581430}.
-!- SUBUNIT: Can form homodimers or heterodimers with TEL2 or FLI1.
Interacts with L3MBTL1 and HDAC9. {ECO:0000269|PubMed:12588862,
ECO:0000269|PubMed:12590135}.
-!- INTERACTION:
Q9BXS5:AP1M1; NbExp=3; IntAct=EBI-1372759, EBI-541426;
A0A0S2Z4M1:AXIN1; NbExp=3; IntAct=EBI-1372759, EBI-16429430;
Q9UKV0-3:HDAC9; NbExp=3; IntAct=EBI-1372759, EBI-765476;
Q96HA8:WDYHV1; NbExp=3; IntAct=EBI-1372759, EBI-741158;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- PTM: Phosphorylation of Ser-257 by MAPK14 (p38) inhibits ETV6
transcriptional repression. {ECO:0000269|PubMed:12435397}.
-!- DISEASE: Note=A chromosomal aberration involving ETV6 is found in
a form of chronic myelomonocytic leukemia (CMML). Translocation
t(5;12)(q33;p13) with PDGFRB. It is characterized by abnormal
clonal myeloid proliferation and by progression to acute
myelogenous leukemia (AML). {ECO:0000269|PubMed:8168137}.
-!- DISEASE: Note=Chromosomal aberrations involving ETV6 are found in
acute myeloid leukemia (AML). Translocation t(12;22)(p13;q11) with
MN1 (PubMed:7731705). Translocation t(4;12)(q12;p13) with CHIC2
(PubMed:10477709). {ECO:0000269|PubMed:10477709,
ECO:0000269|PubMed:7731705}.
-!- DISEASE: Note=Chromosomal aberrations involving ETV6 are found in
childhood acute lymphoblastic leukemia (ALL). Translocations
t(12;21)(p12;q22) and t(12;21)(p13;q22) with RUNX1/AML1.
{ECO:0000269|PubMed:7761424}.
-!- DISEASE: Note=A chromosomal aberration involving ETV6 is found in
a form of pre-B acute lymphoid leukemia. Translocation
t(9;12)(p24;p13) with JAK2. {ECO:0000269|PubMed:9326218}.
-!- DISEASE: Note=A chromosomal aberration involving ETV6 and JAK2 is
found in an atypical chronic myelogenous leukemia. Translocation
t(9;15;12)(p24;q15;p13). {ECO:0000269|PubMed:9326218}.
-!- DISEASE: Note=A chromosomal aberration involving ETV6 is found in
myelodysplastic syndrome (MDS) with basophilia. Translocation
t(5;12)(q31;p13) with ACSL6. {ECO:0000269|PubMed:10502316}.
-!- DISEASE: Note=A chromosomal aberration involving ETV6 is found in
acute eosinophilic leukemia (AEL). Translocation t(5;12)(q31;p13)
with ACSL6. {ECO:0000269|PubMed:10502316}.
-!- DISEASE: Note=A chromosomal aberration involving ETV6 is found in
myelodysplastic syndrome (MDS). Translocation t(1;12)(p36.1;p13)
with MDS2. {ECO:0000269|PubMed:12203785}.
-!- DISEASE: Note=A chromosomal aberration involving ETV6 is found in
acute lymphoblastic leukemia. Translocation t(9;12)(p13;p13) with
PAX5. {ECO:0000269|PubMed:17344859}.
-!- DISEASE: Myeloproliferative disorder chronic with eosinophilia
(MPE) [MIM:131440]: A hematologic disorder characterized by
malignant eosinophils proliferation.
{ECO:0000269|PubMed:12181402}. Note=The gene represented in this
entry is involved in disease pathogenesis. A chromosomal
aberration involving ETV6 is found in many instances of
myeloproliferative disorder chronic with eosinophilia.
Translocation t(5;12) with PDGFRB on chromosome 5 creating an
ETV6-PDGFRB fusion protein. {ECO:0000269|PubMed:12181402}.
-!- DISEASE: Leukemia, acute myelogenous (AML) [MIM:601626]: A subtype
of acute leukemia, a cancer of the white blood cells. AML is a
malignant disease of bone marrow characterized by maturational
arrest of hematopoietic precursors at an early stage of
development. Clonal expansion of myeloid blasts occurs in bone
marrow, blood, and other tissue. Myelogenous leukemias develop
from changes in cells that normally produce neutrophils,
basophils, eosinophils and monocytes.
{ECO:0000269|PubMed:15806161}. Note=The gene represented in this
entry is involved in disease pathogenesis.
-!- DISEASE: Thrombocytopenia 5 (THC5) [MIM:616216]: Thrombocytopenia
is defined by a decrease in the number of platelets in circulating
blood, resulting in the potential for increased bleeding and
decreased ability for clotting. THC5 is an autosomal dominant
disorder, associated with an increased susceptibility to the
development of hematologic and solid malignancies.
{ECO:0000269|PubMed:25581430}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the ETS family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=ABI30005.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/ETV6ID38.html";
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EMBL; U11732; AAA19786.1; -; mRNA.
EMBL; AK289441; BAF82130.1; -; mRNA.
EMBL; CH471094; EAW96240.1; -; Genomic_DNA.
EMBL; BC043399; AAH43399.1; -; mRNA.
EMBL; U61375; AAC50690.1; -; Genomic_DNA.
EMBL; U63312; AAB17134.1; -; Genomic_DNA.
EMBL; U63313; AAB17135.1; -; Genomic_DNA.
EMBL; DQ841178; ABI30005.1; ALT_INIT; mRNA.
CCDS; CCDS8643.1; -.
RefSeq; NP_001978.1; NM_001987.4.
UniGene; Hs.504765; -.
PDB; 1JI7; X-ray; 1.45 A; A/B/C=47-123.
PDB; 1LKY; X-ray; 2.30 A; A/B/C/D/E/F=47-123.
PDB; 2DAO; NMR; -; A=338-442.
PDB; 2QAR; X-ray; 2.40 A; A/B/D/E=47-124.
PDB; 2QB0; X-ray; 2.56 A; A/C=47-123.
PDB; 2QB1; X-ray; 2.61 A; A/B=47-121.
PDB; 5L0P; X-ray; 2.30 A; A=47-356.
PDBsum; 1JI7; -.
PDBsum; 1LKY; -.
PDBsum; 2DAO; -.
PDBsum; 2QAR; -.
PDBsum; 2QB0; -.
PDBsum; 2QB1; -.
PDBsum; 5L0P; -.
ProteinModelPortal; P41212; -.
SMR; P41212; -.
BioGrid; 108421; 34.
DIP; DIP-17028N; -.
ELM; P41212; -.
IntAct; P41212; 16.
MINT; P41212; -.
STRING; 9606.ENSP00000379658; -.
BindingDB; P41212; -.
ChEMBL; CHEMBL2401606; -.
iPTMnet; P41212; -.
PhosphoSitePlus; P41212; -.
BioMuta; ETV6; -.
DMDM; 730927; -.
EPD; P41212; -.
MaxQB; P41212; -.
PaxDb; P41212; -.
PeptideAtlas; P41212; -.
PRIDE; P41212; -.
ProteomicsDB; 55416; -.
DNASU; 2120; -.
Ensembl; ENST00000396373; ENSP00000379658; ENSG00000139083.
GeneID; 2120; -.
KEGG; hsa:2120; -.
UCSC; uc001qzz.4; human.
CTD; 2120; -.
DisGeNET; 2120; -.
EuPathDB; HostDB:ENSG00000139083.10; -.
GeneCards; ETV6; -.
HGNC; HGNC:3495; ETV6.
HPA; HPA000264; -.
MalaCards; ETV6; -.
MIM; 131440; phenotype.
MIM; 600618; gene.
MIM; 601626; phenotype.
MIM; 616216; phenotype.
neXtProt; NX_P41212; -.
OpenTargets; ENSG00000139083; -.
Orphanet; 98823; Chronic myelomonocytic leukemia.
Orphanet; 2665; Congenital mesoblastic nephroma.
Orphanet; 2030; Fibrosarcoma.
Orphanet; 99860; Precursor B-cell acute lymphoblastic leukemia.
Orphanet; 314950; Primary hypereosinophilic syndrome.
PharmGKB; PA27909; -.
eggNOG; KOG3804; Eukaryota.
eggNOG; ENOG4111K4J; LUCA.
GeneTree; ENSGT00760000118996; -.
HOGENOM; HOG000012982; -.
HOVERGEN; HBG005617; -.
InParanoid; P41212; -.
KO; K03211; -.
OMA; HQEPYPL; -.
OrthoDB; EOG091G05Q3; -.
PhylomeDB; P41212; -.
TreeFam; TF318679; -.
SIGNOR; P41212; -.
ChiTaRS; ETV6; human.
EvolutionaryTrace; P41212; -.
GeneWiki; ETV6; -.
GenomeRNAi; 2120; -.
PRO; PR:P41212; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000139083; -.
CleanEx; HS_ETV6; -.
ExpressionAtlas; P41212; baseline and differential.
Genevisible; P41212; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0003700; F:DNA binding transcription factor activity; TAS:ProtInc.
GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISA:NTNU_SB.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II proximal promoter sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0001227; F:transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific DNA binding; IC:NTNU_SB.
GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
GO; GO:0071425; P:hematopoietic stem cell proliferation; IMP:UniProtKB.
GO; GO:0097152; P:mesenchymal cell apoptotic process; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
GO; GO:0022008; P:neurogenesis; IEA:Ensembl.
GO; GO:0007296; P:vitellogenesis; IEA:Ensembl.
Gene3D; 1.10.10.10; -; 1.
InterPro; IPR000418; Ets_dom.
InterPro; IPR003118; Pointed_dom.
InterPro; IPR013761; SAM/pointed_sf.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
Pfam; PF00178; Ets; 1.
Pfam; PF02198; SAM_PNT; 1.
PRINTS; PR00454; ETSDOMAIN.
SMART; SM00413; ETS; 1.
SMART; SM00251; SAM_PNT; 1.
SUPFAM; SSF46785; SSF46785; 1.
SUPFAM; SSF47769; SSF47769; 1.
PROSITE; PS00346; ETS_DOMAIN_2; 1.
PROSITE; PS50061; ETS_DOMAIN_3; 1.
PROSITE; PS51433; PNT; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Chromosomal rearrangement;
Complete proteome; Disease mutation; DNA-binding; Isopeptide bond;
Nucleus; Phosphoprotein; Proto-oncogene; Reference proteome;
Repressor; Transcription; Transcription regulation; Ubl conjugation.
CHAIN 1 452 Transcription factor ETV6.
/FTId=PRO_0000204121.
DOMAIN 40 124 PNT. {ECO:0000255|PROSITE-
ProRule:PRU00762}.
DNA_BIND 339 420 ETS. {ECO:0000255|PROSITE-
ProRule:PRU00237}.
SITE 11 12 Breakpoint for translocation to form
CHIC2-ETV6 in AML.
SITE 54 55 Breakpoint for translocation to form
ETV6-MDS2 in MDS.
SITE 55 56 Breakpoint for translocation to form
PAX5-ETV6.
SITE 336 337 Breakpoint for translocation to form
ETV6-AML1 in ALL.
MOD_RES 11 11 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 18 18 Phosphothreonine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 22 22 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000269|PubMed:12435397}.
MOD_RES 213 213 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 238 238 Phosphoserine.
{ECO:0000250|UniProtKB:P97360}.
MOD_RES 257 257 Phosphoserine; by MAPK14.
{ECO:0000269|PubMed:12435397}.
MOD_RES 302 302 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 323 323 Phosphoserine.
{ECO:0000250|UniProtKB:P97360}.
CROSSLNK 11 11 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 288 288 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 302 302 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 403 403 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 421 421 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VARIANT 214 214 P -> L (in THC5; abrogates DNA binding;
alters subcellular location; decreases
transcriptional repression in a dominant-
negative fashion; dbSNP:rs724159947).
{ECO:0000269|PubMed:25581430}.
/FTId=VAR_073322.
VARIANT 344 344 Y -> YG (in one individual with AML;
somatic mutation; unable to repress
transcription).
{ECO:0000269|PubMed:15806161}.
/FTId=VAR_034600.
VARIANT 369 369 R -> Q (in THC5; abrogates DNA binding;
alters subcellular location; decreases
transcriptional repression in a dominant-
negative fashion; dbSNP:rs724159946).
{ECO:0000269|PubMed:25581430}.
/FTId=VAR_073323.
VARIANT 399 399 R -> C (in THC5; abrogates DNA binding;
alters subcellular location; decreases
transcriptional repression in a dominant-
negative fashion; dbSNP:rs724159945).
{ECO:0000269|PubMed:25581430}.
/FTId=VAR_073324.
MUTAGEN 22 22 S->A: No effect.
MUTAGEN 213 213 S->A: No effect.
{ECO:0000269|PubMed:12435397}.
MUTAGEN 238 238 S->A: No effect.
{ECO:0000269|PubMed:12435397}.
MUTAGEN 257 257 S->A: No phosphorylation by MAPK14.
{ECO:0000269|PubMed:12435397}.
HELIX 12 18 {ECO:0000244|PDB:5L0P}.
TURN 20 22 {ECO:0000244|PDB:5L0P}.
HELIX 23 27 {ECO:0000244|PDB:5L0P}.
HELIX 30 38 {ECO:0000244|PDB:5L0P}.
HELIX 52 54 {ECO:0000244|PDB:1JI7}.
HELIX 58 60 {ECO:0000244|PDB:1JI7}.
HELIX 63 76 {ECO:0000244|PDB:1JI7}.
TURN 84 87 {ECO:0000244|PDB:1JI7}.
HELIX 91 94 {ECO:0000244|PDB:1JI7}.
HELIX 99 105 {ECO:0000244|PDB:1JI7}.
TURN 107 109 {ECO:0000244|PDB:1JI7}.
HELIX 110 122 {ECO:0000244|PDB:1JI7}.
HELIX 341 350 {ECO:0000244|PDB:2DAO}.
HELIX 352 354 {ECO:0000244|PDB:2DAO}.
TURN 355 357 {ECO:0000244|PDB:2DAO}.
STRAND 358 362 {ECO:0000244|PDB:2DAO}.
HELIX 363 365 {ECO:0000244|PDB:2DAO}.
STRAND 367 371 {ECO:0000244|PDB:2DAO}.
HELIX 373 383 {ECO:0000244|PDB:2DAO}.
HELIX 391 403 {ECO:0000244|PDB:2DAO}.
STRAND 406 408 {ECO:0000244|PDB:2DAO}.
STRAND 411 419 {ECO:0000244|PDB:2DAO}.
HELIX 424 426 {ECO:0000244|PDB:2DAO}.
STRAND 430 432 {ECO:0000244|PDB:2DAO}.
HELIX 434 438 {ECO:0000244|PDB:2DAO}.
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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