CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007465
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Transcription factor ETV6 
Protein Synonyms/Alias
 ETS translocation variant 6; ETS-related protein Tel1; Tel 
Gene Name
 ETV6 
Gene Synonyms/Alias
 TEL; TEL1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
11TPAQCSIKQERISYTacetylation[1, 2]
11TPAQCSIKQERISYTsumoylation[3, 4]
99KALLLLTKEDFRYRSsumoylation[5, 6]
288PRHSVDFKQSRLSEDubiquitination[7]
302DGLHREGKPINLSHRacetylation[1, 2, 8, 9]
302DGLHREGKPINLSHRubiquitination[2]
403RALRHYYKLNIIRKEubiquitination[10]
Reference
 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [3] Identification of a new site of sumoylation on Tel (ETV6) uncovers a PIAS-dependent mode of regulating Tel function.
 Roukens MG, Alloul-Ramdhani M, Vertegaal AC, Anvarian Z, Balog CI, Deelder AM, Hensbergen PJ, Baker DA.
 Mol Cell Biol. 2008 Apr;28(7):2342-57. [PMID: 18212042]
 [4] Downregulation of vertebrate Tel (ETV6) and Drosophila Yan is facilitated by an evolutionarily conserved mechanism of F-box-mediated ubiquitination.
 Roukens MG, Alloul-Ramdhani M, Moghadasi S, Op den Brouw M, Baker DA.
 Mol Cell Biol. 2008 Jul;28(13):4394-406. [PMID: 18426905]
 [5] Small ubiquitin-like modifier conjugation regulates nuclear export of TEL, a putative tumor suppressor.
 Wood LD, Irvin BJ, Nucifora G, Luce KS, Hiebert SW.
 Proc Natl Acad Sci U S A. 2003 Mar 18;100(6):3257-62. [PMID: 12626745]
 [6] SUMO modification is required for in vivo Hox gene regulation by the Caenorhabditis elegans Polycomb group protein SOP-2.
 Zhang H, Smolen GA, Palmer R, Christoforou A, van den Heuvel S, Haber DA.
 Nat Genet. 2004 May;36(5):507-11. [PMID: 15107848]
 [7] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [8] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [9] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [10] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965
Functional Description
 Transcriptional repressor; binds to the DNA sequence 5'- CCGGAAGT-3'. 
Sequence Annotation
 DOMAIN 40 124 PNT.
 DNA_BIND 339 420 ETS.
 MOD_RES 2 2 N-acetylserine.
 MOD_RES 11 11 N6-acetyllysine.
 MOD_RES 18 18 Phosphothreonine.
 MOD_RES 22 22 Phosphoserine.
 MOD_RES 213 213 Phosphoserine.
 MOD_RES 257 257 Phosphoserine; by MAPK14.
 MOD_RES 302 302 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Chromosomal rearrangement; Complete proteome; Disease mutation; DNA-binding; Nucleus; Phosphoprotein; Proto-oncogene; Reference proteome; Repressor; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 452 AA 
Protein Sequence
MSETPAQCSI KQERISYTPP ESPVPSYASS TPLHVPVPRA LRMEEDSIRL PAHLRLQPIY 60
WSRDDVAQWL KWAENEFSLR PIDSNTFEMN GKALLLLTKE DFRYRSPHSG DVLYELLQHI 120
LKQRKPRILF SPFFHPGNSI HTQPEVILHQ NHEEDNCVQR TPRPSVDNVH HNPPTIELLH 180
RSRSPITTNH RPSPDPEQRP LRSPLDNMIR RLSPAERAQG PRPHQENNHQ ESYPLSVSPM 240
ENNHCPASSE SHPKPSSPRQ ESTRVIQLMP SPIMHPLILN PRHSVDFKQS RLSEDGLHRE 300
GKPINLSHRE DLAYMNHIMV SVSPPEEHAM PIGRIADCRL LWDYVYQLLS DSRYENFIRW 360
EDKESKIFRI VDPNGLARLW GNHKNRTNMT YEKMSRALRH YYKLNIIRKE PGQRLLFRFM 420
KTPDEIMSGR TDRLEHLESQ ELDEQIYQED EC 452 
Gene Ontology
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
 GO:0003700; F:sequence-specific DNA binding transcription factor activity; TAS:ProtInc.
 GO:0030154; P:cell differentiation; IEA:Compara.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR000418; Ets_dom.
 IPR003118; Pointed_dom.
 IPR013761; SAM/pointed.
 IPR011991; WHTH_DNA-bd_dom. 
Pfam
 PF00178; Ets
 PF02198; SAM_PNT 
SMART
 SM00413; ETS
 SM00251; SAM_PNT 
PROSITE
 PS00345; ETS_DOMAIN_1
 PS00346; ETS_DOMAIN_2
 PS50061; ETS_DOMAIN_3
 PS51433; PNT 
PRINTS
 PR00454; ETSDOMAIN.