ETV5_HUMAN
ID ETV5_HUMAN Reviewed; 510 AA.
AC P41161; A6NH46; B7Z7D7; Q6IBN5;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=ETS translocation variant 5;
DE AltName: Full=Ets-related protein ERM;
GN Name=ETV5; Synonyms=ERM;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=8152800;
RA Monte D., Baert J.-L., Defossez P.-A., de Launoit Y., Stehelin D.;
RT "Molecular cloning and characterization of human ERM, a new member of the
RT Ets family closely related to mouse PEA3 and ER81 transcription factors.";
RL Oncogene 9:1397-1406(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8661127; DOI=10.1006/geno.1996.0345;
RA Monte D., Coutte L., Dewitte F., Defossez P.-A., le Coniat D., Stehelin R.,
RA Berger Y., de Launoit Y.;
RT "Genomic organization of the human ERM (ETV5) gene, a PEA3 group member of
RT ETS transcription factors.";
RL Genomics 35:236-240(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [7]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skin;
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 [9]
RP MASS SPECTROMETRY.
RC TISSUE=Mammary cancer;
RX PubMed=11840567;
RX DOI=10.1002/1615-9861(200202)2:2<212::aid-prot212>3.0.co;2-h;
RA Harris R.A., Yang A., Stein R.C., Lucy K., Brusten L., Herath A.,
RA Parekh R., Waterfield M.D., O'Hare M.J., Neville M.A., Page M.J.,
RA Zvelebil M.J.;
RT "Cluster analysis of an extensive human breast cancer cell line protein
RT expression map database.";
RL Proteomics 2:212-223(2002).
RN [10]
RP INTERACTION WITH ZMYM5.
RX PubMed=17126306; DOI=10.1016/j.brainres.2006.10.056;
RA Pastorcic M., Das H.K.;
RT "Analysis of transcriptional modulation of the presenilin 1 gene promoter
RT by ZNF237, a candidate binding partner of the Ets transcription factor
RT ERM.";
RL Brain Res. 1128:21-32(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, AND IDENTIFICATION BY
RP 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 [12]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-350, AND IDENTIFICATION BY MASS
RP 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 [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-350, 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: Binds to DNA sequences containing the consensus nucleotide
CC core sequence 5'-GGAA.-3'. {ECO:0000269|PubMed:8152800}.
CC -!- SUBUNIT: Interacts (via C-terminal) with ZMYM5 (via N-terminal 120
CC amino acid region). {ECO:0000269|PubMed:17126306}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P41161-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P41161-2; Sequence=VSP_055489;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- MASS SPECTROMETRY: Mass=57837.98; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:11840567};
CC -!- SIMILARITY: Belongs to the ETS family. {ECO:0000305}.
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DR EMBL; X76184; CAA53778.1; -; mRNA.
DR EMBL; X96381; CAA65246.1; -; Genomic_DNA.
DR EMBL; X96380; CAA65246.1; JOINED; Genomic_DNA.
DR EMBL; X96382; CAA65246.1; JOINED; Genomic_DNA.
DR EMBL; X96379; CAA65246.1; JOINED; Genomic_DNA.
DR EMBL; X96378; CAA65246.1; JOINED; Genomic_DNA.
DR EMBL; X96377; CAA65246.1; JOINED; Genomic_DNA.
DR EMBL; X96376; CAA65246.1; JOINED; Genomic_DNA.
DR EMBL; X96375; CAA65246.1; JOINED; Genomic_DNA.
DR EMBL; AK301878; BAH13573.1; -; mRNA.
DR EMBL; CR456767; CAG33048.1; -; mRNA.
DR EMBL; BT006713; AAP35359.1; -; mRNA.
DR EMBL; AC108671; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC112649; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC131156; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW78200.1; -; Genomic_DNA.
DR EMBL; BC007333; AAH07333.1; -; mRNA.
DR CCDS; CCDS33906.1; -. [P41161-1]
DR PIR; S43692; S43692.
DR RefSeq; NP_004445.1; NM_004454.2. [P41161-1]
DR PDB; 4UNO; X-ray; 1.95 A; A=365-462.
DR PDB; 5ILV; X-ray; 1.80 A; A=366-457.
DR PDBsum; 4UNO; -.
DR PDBsum; 5ILV; -.
DR AlphaFoldDB; P41161; -.
DR SMR; P41161; -.
DR BioGRID; 108420; 34.
DR IntAct; P41161; 23.
DR STRING; 9606.ENSP00000306894; -.
DR GlyGen; P41161; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P41161; -.
DR PhosphoSitePlus; P41161; -.
DR BioMuta; ETV5; -.
DR DMDM; 729441; -.
DR jPOST; P41161; -.
DR MassIVE; P41161; -.
DR PaxDb; P41161; -.
DR PeptideAtlas; P41161; -.
DR PRIDE; P41161; -.
DR ProteomicsDB; 55407; -. [P41161-1]
DR ProteomicsDB; 6857; -.
DR Antibodypedia; 34851; 361 antibodies from 34 providers.
DR DNASU; 2119; -.
DR Ensembl; ENST00000306376.10; ENSP00000306894.5; ENSG00000244405.8. [P41161-1]
DR Ensembl; ENST00000434744.5; ENSP00000413755.1; ENSG00000244405.8. [P41161-1]
DR GeneID; 2119; -.
DR KEGG; hsa:2119; -.
DR MANE-Select; ENST00000306376.10; ENSP00000306894.5; NM_004454.3; NP_004445.1.
DR UCSC; uc003fpz.4; human. [P41161-1]
DR CTD; 2119; -.
DR DisGeNET; 2119; -.
DR GeneCards; ETV5; -.
DR HGNC; HGNC:3494; ETV5.
DR HPA; ENSG00000244405; Low tissue specificity.
DR MIM; 601600; gene.
DR neXtProt; NX_P41161; -.
DR OpenTargets; ENSG00000244405; -.
DR PharmGKB; PA27908; -.
DR VEuPathDB; HostDB:ENSG00000244405; -.
DR eggNOG; KOG3806; Eukaryota.
DR GeneTree; ENSGT00940000160680; -.
DR HOGENOM; CLU_030025_1_0_1; -.
DR InParanoid; P41161; -.
DR OMA; SYCAYDR; -.
DR OrthoDB; 536648at2759; -.
DR PhylomeDB; P41161; -.
DR TreeFam; TF316214; -.
DR PathwayCommons; P41161; -.
DR SignaLink; P41161; -.
DR SIGNOR; P41161; -.
DR BioGRID-ORCS; 2119; 20 hits in 1101 CRISPR screens.
DR ChiTaRS; ETV5; human.
DR GenomeRNAi; 2119; -.
DR Pharos; P41161; Tbio.
DR PRO; PR:P41161; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P41161; protein.
DR Bgee; ENSG00000244405; Expressed in buccal mucosa cell and 176 other tissues.
DR ExpressionAtlas; P41161; baseline and differential.
DR Genevisible; P41161; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IMP:NTNU_SB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IMP:NTNU_SB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:NTNU_SB.
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; IPR006715; ETS_PEA3_N.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11849; PTHR11849; 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; Alternative splicing; DNA-binding; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..510
FT /note="ETS translocation variant 5"
FT /id="PRO_0000204118"
FT DNA_BIND 368..448
FT /note="ETS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00237"
FT REGION 131..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..158
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..203
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 350
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1
FT /note="M -> MSERRCPPEHREGVNDTGGSLFPQKLLNAETSQSGIRDAESTM (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055489"
FT VARIANT 348
FT /note="K -> R (in dbSNP:rs2228269)"
FT /id="VAR_048951"
FT HELIX 370..378
FT /evidence="ECO:0007829|PDB:5ILV"
FT HELIX 381..383
FT /evidence="ECO:0007829|PDB:5ILV"
FT TURN 384..386
FT /evidence="ECO:0007829|PDB:5ILV"
FT STRAND 387..389
FT /evidence="ECO:0007829|PDB:5ILV"
FT STRAND 395..400
FT /evidence="ECO:0007829|PDB:5ILV"
FT HELIX 401..412
FT /evidence="ECO:0007829|PDB:5ILV"
FT HELIX 419..431
FT /evidence="ECO:0007829|PDB:5ILV"
FT STRAND 434..437
FT /evidence="ECO:0007829|PDB:5ILV"
FT STRAND 442..449
FT /evidence="ECO:0007829|PDB:5ILV"
FT HELIX 453..455
FT /evidence="ECO:0007829|PDB:5ILV"
SQ SEQUENCE 510 AA; 57838 MW; B7CE40A33927F46E CRC64;
MDGFYDQQVP FMVPGKSRSE ECRGRPVIDR KRKFLDTDLA HDSEELFQDL SQLQEAWLAE
AQVPDDEQFV PDFQSDNLVL HAPPPTKIKR ELHSPSSELS SCSHEQALGA NYGEKCLYNY
CAYDRKPPSG FKPLTPPTTP LSPTHQNPLF PPPQATLPTS GHAPAAGPVQ GVGPAPAPHS
LPEPGPQQQT FAVPRPPHQP LQMPKMMPEN QYPSEQRFQR QLSEPCHPFP PQPGVPGDNR
PSYHRQMSEP IVPAAPPPPQ GFKQEYHDPL YEHGVPGMPG PPAHGFQSPM GIKQEPRDYC
VDSEVPNCQS SYMRGGYFSS SHEGFSYEKD PRLYFDDTCV VPERLEGKVK QEPTMYREGP
PYQRRGSLQL WQFLVTLLDD PANAHFIAWT GRGMEFKLIE PEEVARRWGI QKNRPAMNYD
KLSRSLRYYY EKGIMQKVAG ERYVYKFVCD PDALFSMAFP DNQRPFLKAE SECHLSEEDT
LPLTHFEDSP AYLLDMDRCS SLPYAEGFAY
