CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004277
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein C-ets-1 
Protein Synonyms/Alias
 p54 
Gene Name
 ETS1 
Gene Synonyms/Alias
 EWSR2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
2******MKAAVDLKPacetylation[1]
2******MKAAVDLKPubiquitination[2, 3, 4]
8MKAAVDLKPTLTIIKacetylation[1, 4, 5]
8MKAAVDLKPTLTIIKubiquitination[3, 4]
15KPTLTIIKTEKVDLEacetylation[1, 4, 5, 6]
15KPTLTIIKTEKVDLEsumoylation[7, 8, 9]
15KPTLTIIKTEKVDLEubiquitination[3, 4]
18LTIIKTEKVDLELFPubiquitination[4]
42PLLTPSSKEMMSQALubiquitination[3, 4]
50EMMSQALKATFSGFTubiquitination[3, 4]
58ATFSGFTKEQQRLGIubiquitination[2, 3, 4]
67QQRLGIPKDPRQWTEubiquitination[3, 4]
97LKGVDFQKFCMNGAAubiquitination[3]
138ILQKEDVKPYQVNGVubiquitination[3, 4, 10]
227QNDYFAIKQEVVTPDsumoylation[7, 8]
245MGRTSRGKLGGQDSFacetylation[4, 6]
245MGRTSRGKLGGQDSFubiquitination[2, 3, 4]
299PAALPNHKPKGTFKDubiquitination[2, 3, 4]
301ALPNHKPKGTFKDYVubiquitination[3]
305HKPKGTFKDYVRDRAacetylation[1, 5]
305HKPKGTFKDYVRDRAubiquitination[2, 3, 4]
388KPKMNYEKLSRGLRYubiquitination[2, 3]
399GLRYYYDKNIIHKTAubiquitination[3, 4]
408IIHKTAGKRYVYRFVubiquitination[3]
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] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] Beads-on-a-string, characterization of ETS-1 sumoylated within its flexible N-terminal sequence.
 Macauley MS, Errington WJ, Schärpf M, Mackereth CD, Blaszczak AG, Graves BJ, McIntosh LP.
 J Biol Chem. 2006 Feb 17;281(7):4164-72. [PMID: 16319071]
 [8] PIASy-mediated repression of the Ets-1 is independent of its sumoylation.
 Nishida T, Terashima M, Fukami K.
 Biochem Biophys Res Commun. 2006 Jul 14;345(4):1536-46. [PMID: 16729975]
 [9] Regulation of the Ets-1 transcription factor by sumoylation and ubiquitinylation.
 Ji Z, Degerny C, Vintonenko N, Deheuninck J, Foveau B, Leroy C, Coll J, Tulasne D, Baert JL, Fafeur V.
 Oncogene. 2007 Jan 18;26(3):395-406. [PMID: 16862185]
 [10] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983] 
Functional Description
 Transcription factor. Directly controls the expression of cytokine and chemokine genes in a wide variety of different cellular contexts. May control the differentiation, survival and proliferation of lymphoid cells. May also regulate angiogenesis through regulation of expression of genes controlling endothelial cell migration and invasion. 
Sequence Annotation
 DOMAIN 51 136 PNT.
 DNA_BIND 335 415 ETS.
 REGION 130 243 Activation domain; required for
 MOD_RES 8 8 N6-acetyllysine.
 MOD_RES 15 15 N6-acetyllysine; alternate.
 MOD_RES 38 38 Phosphothreonine; by MAPK (By
 MOD_RES 223 223 Phosphotyrosine.
 MOD_RES 270 270 Phosphoserine.
 MOD_RES 285 285 Phosphoserine.
 MOD_RES 305 305 N6-acetyllysine.
 CROSSLNK 15 15 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 227 227 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 3D-structure; Acetylation; Alternative splicing; Complete proteome; Cytoplasm; DNA-binding; Immunity; Isopeptide bond; Nucleus; Phosphoprotein; Proto-oncogene; Reference proteome; Transcription; Transcription regulation; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 441 AA 
Protein Sequence
MKAAVDLKPT LTIIKTEKVD LELFPSPDME CADVPLLTPS SKEMMSQALK ATFSGFTKEQ 60
QRLGIPKDPR QWTETHVRDW VMWAVNEFSL KGVDFQKFCM NGAALCALGK DCFLELAPDF 120
VGDILWEHLE ILQKEDVKPY QVNGVNPAYP ESRYTSDYFI SYGIEHAQCV PPSEFSEPSF 180
ITESYQTLHP ISSEELLSLK YENDYPSVIL RDPLQTDTLQ NDYFAIKQEV VTPDNMCMGR 240
TSRGKLGGQD SFESIESYDS CDRLTQSWSS QSSFNSLQRV PSYDSFDSED YPAALPNHKP 300
KGTFKDYVRD RADLNKDKPV IPAAALAGYT GSGPIQLWQF LLELLTDKSC QSFISWTGDG 360
WEFKLSDPDE VARRWGKRKN KPKMNYEKLS RGLRYYYDKN IIHKTAGKRY VYRFVCDLQS 420
LLGYTPEELH AMLDVKPDAD E 441 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IDA:BHF-UCL.
 GO:0005667; C:transcription factor complex; IEA:Compara.
 GO:0003677; F:DNA binding; ISS:UniProtKB.
 GO:0043565; F:sequence-specific DNA binding; IEA:Compara.
 GO:0003700; F:sequence-specific DNA binding transcription factor activity; IDA:BHF-UCL.
 GO:0008134; F:transcription factor binding; NAS:UniProtKB.
 GO:0060055; P:angiogenesis involved in wound healing; IEA:Compara.
 GO:0030262; P:apoptotic nuclear changes; IDA:UniProtKB.
 GO:0048870; P:cell motility; IMP:BHF-UCL.
 GO:0070301; P:cellular response to hydrogen peroxide; IEA:Compara.
 GO:0060206; P:estrous cycle phase; IEA:Compara.
 GO:0007565; P:female pregnancy; IEA:Compara.
 GO:0021854; P:hypothalamus development; IEA:Compara.
 GO:0006955; P:immune response; TAS:ProtInc.
 GO:0045786; P:negative regulation of cell cycle; IDA:UniProtKB.
 GO:0008285; P:negative regulation of cell proliferation; TAS:ProtInc.
 GO:0021983; P:pituitary gland development; IEA:Compara.
 GO:0030578; P:PML body organization; IDA:BHF-UCL.
 GO:0045766; P:positive regulation of angiogenesis; IEA:Compara.
 GO:0008284; P:positive regulation of cell proliferation; IEA:Compara.
 GO:0010595; P:positive regulation of endothelial cell migration; IMP:UniProtKB.
 GO:0045648; P:positive regulation of erythrocyte differentiation; IDA:UniProtKB.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
 GO:0045893; P:positive regulation of transcription, DNA-dependent; IDA:UniProtKB.
 GO:0045765; P:regulation of angiogenesis; IMP:UniProtKB.
 GO:0010715; P:regulation of extracellular matrix disassembly; IEA:Compara.
 GO:0046677; P:response to antibiotic; IDA:UniProtKB.
 GO:0032355; P:response to estradiol stimulus; IEA:Compara.
 GO:0001666; P:response to hypoxia; IEA:Compara.
 GO:0070555; P:response to interleukin-1; IEA:Compara.
 GO:0034616; P:response to laminar fluid shear stress; IEA:Compara.
 GO:0009612; P:response to mechanical stimulus; IEA:Compara.
 GO:0006366; P:transcription from RNA polymerase II promoter; IDA:UniProtKB.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR000418; Ets_dom.
 IPR003118; Pointed_dom.
 IPR013761; SAM/pointed.
 IPR016311; Transform_prot_C-ets.
 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.