ETV1_HUMAN
ID ETV1_HUMAN Reviewed; 477 AA.
AC P50549; A4D118; B2R768; B7Z2I4; B7Z618; B7Z9P2; C9JT37; E9PHB1; F5GXR2;
AC O75849; Q4KMQ6; Q59GA7; Q6AI30; Q9UQ71; Q9Y636;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=ETS translocation variant 1 {ECO:0000305};
DE AltName: Full=Ets-related protein 81 {ECO:0000312|HGNC:HGNC:3490};
GN Name=ETV1 {ECO:0000312|HGNC:HGNC:3490};
GN Synonyms=ER81 {ECO:0000303|PubMed:7651741};
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 {ECO:0000312|Proteomes:UP000005640};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND CHROMOSOMAL TRANSLOCATION WITH
RP EWSR1.
RX PubMed=7700648;
RA Jeon I.-S., Davis J.N., Braun B.S., Sublett J.E., Roussel M.F., Denny C.T.,
RA Shapiro D.N.;
RT "A variant Ewing's sarcoma translocation (7;22) fuses the EWS gene to the
RT ETS gene ETV1.";
RL Oncogene 10:1229-1234(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND FUNCTION.
RC TISSUE=Kidney;
RX PubMed=7651741;
RA Monte D., Coutte L., Baert J.-L., Angeli I., Stehelin D., de Launoit Y.;
RT "Molecular characterization of the ets-related human transcription factor
RT ER81.";
RL Oncogene 11:771-779(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
RA Coutte L., Monte D., Pouilly L., Dewitte F., Vidaud M., Baert J.-L.,
RA de Launoit Y.;
RT "Characterization of the human and mouse ER81/ETV1 transcription factor
RT genes. Role of the two human alternatively spliced isoforms.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 4 AND 5), AND
RP VARIANT GLY-100.
RC TISSUE=Brain, and Trachea;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT GLY-100.
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RT "Homo sapiens protein coding cDNA.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RC TISSUE=Seminoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [10]
RP PHOSPHORYLATION AT SER-191 AND SER-216.
RX PubMed=12213813; DOI=10.1074/jbc.m205501200;
RA Wu J., Janknecht R.;
RT "Regulation of the ETS transcription factor ER81 by the 90-kDa ribosomal S6
RT kinase 1 and protein kinase A.";
RL J. Biol. Chem. 277:42669-42679(2002).
RN [11]
RP PHOSPHORYLATION AT SER-191 AND SER-216, AND MUTAGENESIS OF SER-191 AND
RP SER-216.
RX PubMed=12569367; DOI=10.1038/sj.onc.1206185;
RA Janknecht R.;
RT "Regulation of the ER81 transcription factor and its coactivators by
RT mitogen- and stress-activated protein kinase 1 (MSK1).";
RL Oncogene 22:746-755(2003).
RN [12]
RP SUMOYLATION.
RX PubMed=15561718; DOI=10.1074/jbc.m411718200;
RA Gocke C.B., Yu H., Kang J.;
RT "Systematic identification and analysis of mammalian small ubiquitin-like
RT modifier substrates.";
RL J. Biol. Chem. 280:5004-5012(2005).
RN [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-317, AND IDENTIFICATION BY MASS
RP 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 activator that binds to DNA sequences
CC containing the consensus pentanucleotide 5'-CGGA[AT]-3'
CC (PubMed:7651741). Required for olfactory dopaminergic neuron
CC differentiation; may directly activate expression of tyrosine
CC hydroxylase (TH) (By similarity). {ECO:0000250|UniProtKB:P41164,
CC ECO:0000269|PubMed:7651741}.
CC -!- INTERACTION:
CC P50549; Q8NHY2: COP1; NbExp=2; IntAct=EBI-3905068, EBI-1176214;
CC P50549; Q16236: NFE2L2; NbExp=4; IntAct=EBI-3905068, EBI-2007911;
CC P50549; P78527: PRKDC; NbExp=2; IntAct=EBI-3905068, EBI-352053;
CC P50549-1; Q8NHY2-1: COP1; NbExp=2; IntAct=EBI-15926557, EBI-9698228;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00237}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=P50549-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P50549-2; Sequence=VSP_001472;
CC Name=3;
CC IsoId=P50549-3; Sequence=VSP_043750;
CC Name=4;
CC IsoId=P50549-4; Sequence=VSP_043808, VSP_043809;
CC Name=5;
CC IsoId=P50549-5; Sequence=VSP_043808, VSP_001472;
CC Name=6;
CC IsoId=P50549-6; Sequence=VSP_043808;
CC -!- TISSUE SPECIFICITY: Very highly expressed in brain, highly expressed in
CC testis, lung and heart, moderately in spleen, small intestine, pancreas
CC and colon, weakly in liver, prostate and thymus, very weakly in
CC skeletal muscle, kidney and ovary and not in placenta and peripheral
CC blood leukocytes. {ECO:0000269|PubMed:7651741}.
CC -!- PTM: Sumoylated. {ECO:0000269|PubMed:15561718}.
CC -!- PTM: Phosphorylated at Ser-191 and Ser-216 by RPS6KA1 and RPS6KA5;
CC phosphorylation activates transcriptional activity.
CC {ECO:0000269|PubMed:12213813, ECO:0000269|PubMed:12569367}.
CC -!- DISEASE: Ewing sarcoma (ES) [MIM:612219]: A highly malignant,
CC metastatic, primitive small round cell tumor of bone and soft tissue
CC that affects children and adolescents. It belongs to the Ewing sarcoma
CC family of tumors, a group of morphologically heterogeneous neoplasms
CC that share the same cytogenetic features. They are considered neural
CC tumors derived from cells of the neural crest. Ewing sarcoma represents
CC the less differentiated form of the tumors.
CC {ECO:0000269|PubMed:7700648}. Note=The gene represented in this entry
CC is involved in disease pathogenesis. A chromosomal aberration involving
CC ETV1 is found in patients with Ewing sarcoma. Translocation
CC t(7;22)(p22;q12) with EWSR1. {ECO:0000269|PubMed:7700648}.
CC -!- SIMILARITY: Belongs to the ETS family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92439.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U17163; AAA79844.1; -; mRNA.
DR EMBL; X87175; CAA60642.1; -; mRNA.
DR EMBL; AF109632; AAD29877.1; -; Genomic_DNA.
DR EMBL; AF109621; AAD29877.1; JOINED; Genomic_DNA.
DR EMBL; AF109622; AAD29877.1; JOINED; Genomic_DNA.
DR EMBL; AF109623; AAD29877.1; JOINED; Genomic_DNA.
DR EMBL; AF109624; AAD29877.1; JOINED; Genomic_DNA.
DR EMBL; AF109625; AAD29877.1; JOINED; Genomic_DNA.
DR EMBL; AF109626; AAD29877.1; JOINED; Genomic_DNA.
DR EMBL; AF109627; AAD29877.1; JOINED; Genomic_DNA.
DR EMBL; AF109628; AAD29877.1; JOINED; Genomic_DNA.
DR EMBL; AF109629; AAD29877.1; JOINED; Genomic_DNA.
DR EMBL; AF109630; AAD29877.1; JOINED; Genomic_DNA.
DR EMBL; AF109631; AAD29877.1; JOINED; Genomic_DNA.
DR EMBL; AF109632; AAD29878.1; -; Genomic_DNA.
DR EMBL; AF109621; AAD29878.1; JOINED; Genomic_DNA.
DR EMBL; AF109622; AAD29878.1; JOINED; Genomic_DNA.
DR EMBL; AF109623; AAD29878.1; JOINED; Genomic_DNA.
DR EMBL; AF109625; AAD29878.1; JOINED; Genomic_DNA.
DR EMBL; AF109626; AAD29878.1; JOINED; Genomic_DNA.
DR EMBL; AF109627; AAD29878.1; JOINED; Genomic_DNA.
DR EMBL; AF109628; AAD29878.1; JOINED; Genomic_DNA.
DR EMBL; AF109629; AAD29878.1; JOINED; Genomic_DNA.
DR EMBL; AF109630; AAD29878.1; JOINED; Genomic_DNA.
DR EMBL; AF109631; AAD29878.1; JOINED; Genomic_DNA.
DR EMBL; AK294755; BAH11870.1; -; mRNA.
DR EMBL; AK299693; BAH13104.1; -; mRNA.
DR EMBL; AK312863; BAG35715.1; -; mRNA.
DR EMBL; AK316007; BAH14378.1; -; mRNA.
DR EMBL; AB209202; BAD92439.1; ALT_INIT; mRNA.
DR EMBL; CR627389; CAH10484.1; -; mRNA.
DR EMBL; AC004857; AAC62435.1; -; Genomic_DNA.
DR EMBL; AC004909; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236948; EAL24294.1; -; Genomic_DNA.
DR EMBL; BC098403; AAH98403.1; -; mRNA.
DR EMBL; BC106762; AAI06763.1; -; mRNA.
DR EMBL; BC106763; AAI06764.1; -; mRNA.
DR CCDS; CCDS55083.1; -. [P50549-5]
DR CCDS; CCDS55084.1; -. [P50549-4]
DR CCDS; CCDS55085.1; -. [P50549-6]
DR CCDS; CCDS55086.1; -. [P50549-2]
DR CCDS; CCDS55087.1; -. [P50549-3]
DR CCDS; CCDS55088.1; -. [P50549-1]
DR PIR; I38893; I38893.
DR RefSeq; NP_001156619.1; NM_001163147.1. [P50549-3]
DR RefSeq; NP_001156620.1; NM_001163148.1. [P50549-2]
DR RefSeq; NP_001156621.1; NM_001163149.1. [P50549-2]
DR RefSeq; NP_001156622.1; NM_001163150.1. [P50549-6]
DR RefSeq; NP_001156623.1; NM_001163151.1. [P50549-5]
DR RefSeq; NP_001156624.1; NM_001163152.1. [P50549-4]
DR RefSeq; NP_004947.2; NM_004956.4. [P50549-1]
DR RefSeq; XP_005249692.1; XM_005249635.4. [P50549-1]
DR RefSeq; XP_005249693.1; XM_005249636.4.
DR RefSeq; XP_011513470.1; XM_011515168.2. [P50549-1]
DR PDB; 4AVP; X-ray; 1.82 A; A/B/C/D=326-429.
DR PDB; 4BNC; X-ray; 2.90 A; A=326-429.
DR PDB; 5ILS; X-ray; 1.40 A; A=334-434.
DR PDBsum; 4AVP; -.
DR PDBsum; 4BNC; -.
DR PDBsum; 5ILS; -.
DR AlphaFoldDB; P50549; -.
DR SMR; P50549; -.
DR BioGRID; 108416; 30.
DR DIP; DIP-60463N; -.
DR IntAct; P50549; 9.
DR STRING; 9606.ENSP00000405327; -.
DR BindingDB; P50549; -.
DR ChEMBL; CHEMBL2010626; -.
DR GlyGen; P50549; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P50549; -.
DR PhosphoSitePlus; P50549; -.
DR BioMuta; ETV1; -.
DR DMDM; 12643411; -.
DR MassIVE; P50549; -.
DR MaxQB; P50549; -.
DR PaxDb; P50549; -.
DR PeptideAtlas; P50549; -.
DR PRIDE; P50549; -.
DR ProteomicsDB; 20494; -.
DR ProteomicsDB; 24498; -.
DR ProteomicsDB; 56244; -. [P50549-1]
DR ProteomicsDB; 56245; -. [P50549-2]
DR ProteomicsDB; 56246; -. [P50549-3]
DR ProteomicsDB; 56247; -. [P50549-4]
DR Antibodypedia; 25156; 326 antibodies from 33 providers.
DR DNASU; 2115; -.
DR Ensembl; ENST00000242066.9; ENSP00000242066.5; ENSG00000006468.14. [P50549-2]
DR Ensembl; ENST00000399357.7; ENSP00000382293.3; ENSG00000006468.14. [P50549-4]
DR Ensembl; ENST00000403527.5; ENSP00000384138.1; ENSG00000006468.14. [P50549-6]
DR Ensembl; ENST00000403685.5; ENSP00000385686.1; ENSG00000006468.14. [P50549-2]
DR Ensembl; ENST00000405192.6; ENSP00000385381.2; ENSG00000006468.14. [P50549-3]
DR Ensembl; ENST00000405218.6; ENSP00000385551.2; ENSG00000006468.14. [P50549-1]
DR Ensembl; ENST00000420159.6; ENSP00000411626.2; ENSG00000006468.14. [P50549-5]
DR Ensembl; ENST00000430479.6; ENSP00000405327.1; ENSG00000006468.14. [P50549-1]
DR GeneID; 2115; -.
DR KEGG; hsa:2115; -.
DR MANE-Select; ENST00000430479.6; ENSP00000405327.1; NM_004956.5; NP_004947.2.
DR UCSC; uc003ssw.5; human. [P50549-1]
DR CTD; 2115; -.
DR DisGeNET; 2115; -.
DR GeneCards; ETV1; -.
DR HGNC; HGNC:3490; ETV1.
DR HPA; ENSG00000006468; Tissue enhanced (brain, salivary gland).
DR MalaCards; ETV1; -.
DR MIM; 600541; gene.
DR MIM; 612219; phenotype.
DR neXtProt; NX_P50549; -.
DR OpenTargets; ENSG00000006468; -.
DR Orphanet; 319; Skeletal Ewing sarcoma.
DR PharmGKB; PA27904; -.
DR VEuPathDB; HostDB:ENSG00000006468; -.
DR eggNOG; KOG3806; Eukaryota.
DR GeneTree; ENSGT00940000157123; -.
DR HOGENOM; CLU_030025_1_0_1; -.
DR InParanoid; P50549; -.
DR OMA; DYQAESX; -.
DR PhylomeDB; P50549; -.
DR TreeFam; TF316214; -.
DR PathwayCommons; P50549; -.
DR SignaLink; P50549; -.
DR SIGNOR; P50549; -.
DR BioGRID-ORCS; 2115; 19 hits in 1099 CRISPR screens.
DR ChiTaRS; ETV1; human.
DR GeneWiki; ETV1; -.
DR GenomeRNAi; 2115; -.
DR Pharos; P50549; Tbio.
DR PRO; PR:P50549; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P50549; protein.
DR Bgee; ENSG00000006468; Expressed in cerebellar vermis and 174 other tissues.
DR ExpressionAtlas; P50549; baseline and differential.
DR Genevisible; P50549; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
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:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0007411; P:axon guidance; IEA:Ensembl.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0007638; P:mechanosensory behavior; IEA:Ensembl.
DR GO; GO:0007517; P:muscle organ development; IEA:Ensembl.
DR GO; GO:0048935; P:peripheral nervous system neuron development; TAS:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR000418; Ets_dom.
DR InterPro; IPR046328; ETS_fam.
DR InterPro; IPR006715; ETS_PEA3_N.
DR InterPro; IPR032928; ETS_V1.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11849; PTHR11849; 1.
DR PANTHER; PTHR11849:SF196; PTHR11849:SF196; 1.
DR Pfam; PF00178; Ets; 1.
DR Pfam; PF04621; ETS_PEA3_N; 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 3D-structure; Activator; Alternative splicing; Chromosomal rearrangement;
KW Disease variant; DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein;
KW Proto-oncogene; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..477
FT /note="ETS translocation variant 1"
FT /id="PRO_0000204110"
FT DNA_BIND 335..415
FT /note="ETS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00237"
FT REGION 128..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43268"
FT MOD_RES 191
FT /note="Phosphoserine; by RPS6KA1 and RPS6KA5"
FT /evidence="ECO:0000269|PubMed:12213813,
FT ECO:0000269|PubMed:12569367"
FT MOD_RES 216
FT /note="Phosphoserine; by RPS6KA1 and RPS6KA5"
FT /evidence="ECO:0000269|PubMed:12213813,
FT ECO:0000269|PubMed:12569367"
FT CROSSLNK 317
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..60
FT /note="MDGFYDQQVPYMVTNSQRGRNCNEKPTNVRKRKFINRDLAHDSEELFQDLSQ
FT LQETWLAE -> MLQDLSASVFFPPCSQHRTL (in isoform 4, isoform 5
FT and isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_043808"
FT VAR_SEQ 61..79
FT /note="AQVPDNDEQFVPDYQAESL -> V (in isoform 2 and isoform
FT 5)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:7651741"
FT /id="VSP_001472"
FT VAR_SEQ 122..184
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043809"
FT VAR_SEQ 268..290
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_043750"
FT VARIANT 100
FT /note="S -> G (in dbSNP:rs9639168)"
FT /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.5"
FT /id="VAR_048948"
FT MUTAGEN 191
FT /note="S->A: Loss of phosphorylation by RPS6KA5."
FT /evidence="ECO:0000269|PubMed:12569367"
FT MUTAGEN 216
FT /note="S->A: Loss of phosphorylation by RPS6KA5."
FT /evidence="ECO:0000269|PubMed:12569367"
FT CONFLICT 39
FT /note="L -> V (in Ref. 2; CAA60642)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="C -> S (in Ref. 1; AAA79844)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="K -> N (in Ref. 1; AAA79844)"
FT /evidence="ECO:0000305"
FT CONFLICT 253
FT /note="Missing (in Ref. 2; CAA60642)"
FT /evidence="ECO:0000305"
FT CONFLICT 349
FT /note="S -> A (in Ref. 2; CAA60642)"
FT /evidence="ECO:0000305"
FT CONFLICT 445
FT /note="E -> G (in Ref. 6; CAH10484)"
FT /evidence="ECO:0000305"
FT CONFLICT 471
FT /note="Y -> C (in Ref. 4; BAH13104)"
FT /evidence="ECO:0000305"
FT HELIX 337..346
FT /evidence="ECO:0007829|PDB:5ILS"
FT HELIX 348..350
FT /evidence="ECO:0007829|PDB:5ILS"
FT TURN 351..353
FT /evidence="ECO:0007829|PDB:5ILS"
FT STRAND 354..356
FT /evidence="ECO:0007829|PDB:5ILS"
FT STRAND 362..367
FT /evidence="ECO:0007829|PDB:5ILS"
FT HELIX 368..379
FT /evidence="ECO:0007829|PDB:5ILS"
FT HELIX 386..398
FT /evidence="ECO:0007829|PDB:5ILS"
FT STRAND 401..404
FT /evidence="ECO:0007829|PDB:5ILS"
FT STRAND 409..414
FT /evidence="ECO:0007829|PDB:5ILS"
FT HELIX 418..425
FT /evidence="ECO:0007829|PDB:5ILS"
SQ SEQUENCE 477 AA; 55131 MW; BE95FA3F07196F06 CRC64;
MDGFYDQQVP YMVTNSQRGR NCNEKPTNVR KRKFINRDLA HDSEELFQDL SQLQETWLAE
AQVPDNDEQF VPDYQAESLA FHGLPLKIKK EPHSPCSEIS SACSQEQPFK FSYGEKCLYN
VSAYDQKPQV GMRPSNPPTP SSTPVSPLHH ASPNSTHTPK PDRAFPAHLP PSQSIPDSSY
PMDHRFRRQL SEPCNSFPPL PTMPREGRPM YQRQMSEPNI PFPPQGFKQE YHDPVYEHNT
MVGSAASQSF PPPLMIKQEP RDFAYDSEVP SCHSIYMRQE GFLAHPSRTE GCMFEKGPRQ
FYDDTCVVPE KFDGDIKQEP GMYREGPTYQ RRGSLQLWQF LVALLDDPSN SHFIAWTGRG
MEFKLIEPEE VARRWGIQKN RPAMNYDKLS RSLRYYYEKG IMQKVAGERY VYKFVCDPEA
LFSMAFPDNQ RPLLKTDMER HINEEDTVPL SHFDESMAYM PEGGCCNPHP YNEGYVY
