CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010860
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Friend leukemia integration 1 transcription factor 
Protein Synonyms/Alias
 Proto-oncogene Fli-1; Transcription factor ERGB 
Gene Name
 FLI1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
67QPVRVNVKREYDHMNsumoylation[1]
172KELCKMNKEDFLRATubiquitination[2, 3, 4]
217QSSRLSVKEDPSYDSubiquitination[4, 5]
240NMNSGLNKSPPLGGAacetylation[6]
252GGAQTISKNTEQRPQacetylation[6]
334KPNMNYDKLSRALRYacetylation[6]
345ALRYYYDKNIMTKVHacetylation[6]
350YDKNIMTKVHGKRYAacetylation[6]
380PTESSMYKYPSDISYacetylation[6, 7]
397SYHAHQQKVNFVPPHacetylation[6]
Reference
 [1] FLI-1 functionally interacts with PIASxalpha, a member of the PIAS E3 SUMO ligase family.
 van den Akker E, Ano S, Shih HM, Wang LC, Pironin M, Palvimo JJ, Kotaja N, Kirsh O, Dejean A, Ghysdael J.
 J Biol Chem. 2005 Nov 11;280(45):38035-46. [PMID: 16148010]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [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] 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]
 [6] Acetylation Increases EWS-FLI1 DNA Binding and Transcriptional Activity.
 Schlottmann S, Erkizan HV, Barber-Rotenberg JS, Knights C, Cheema A, Uren A, Avantaggiati ML, Toretsky JA.
 Front Oncol. 2012 Sep 7;2:107. [PMID: 22973553]
 [7] Transforming growth factor-beta regulates DNA binding activity of transcription factor Fli1 by p300/CREB-binding protein-associated factor-dependent acetylation.
 Asano Y, Czuwara J, Trojanowska M.
 J Biol Chem. 2007 Nov 30;282(48):34672-83. [PMID: 17884818
Functional Description
 Sequence-specific transcriptional activator. Recognizes the DNA sequence 5'-C[CA]GGAAGT-3'. 
Sequence Annotation
 DOMAIN 112 198 PNT.
 DNA_BIND 281 361 ETS.  
Keyword
 3D-structure; Activator; Alternative splicing; Chromosomal rearrangement; Complete proteome; DNA-binding; Nucleus; Proto-oncogene; Reference proteome; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 452 AA 
Protein Sequence
MDGTIKEALS VVSDDQSLFD SAYGAAAHLP KADMTASGSP DYGQPHKINP LPPQQEWINQ 60
PVRVNVKREY DHMNGSRESP VDCSVSKCSK LVGGGESNPM NYNSYMDEKN GPPPPNMTTN 120
ERRVIVPADP TLWTQEHVRQ WLEWAIKEYS LMEIDTSFFQ NMDGKELCKM NKEDFLRATT 180
LYNTEVLLSH LSYLRESSLL AYNTTSHTDQ SSRLSVKEDP SYDSVRRGAW GNNMNSGLNK 240
SPPLGGAQTI SKNTEQRPQP DPYQILGPTS SRLANPGSGQ IQLWQFLLEL LSDSANASCI 300
TWEGTNGEFK MTDPDEVARR WGERKSKPNM NYDKLSRALR YYYDKNIMTK VHGKRYAYKF 360
DFHGIAQALQ PHPTESSMYK YPSDISYMPS YHAHQQKVNF VPPHPSSMPV TSSSFFGAAS 420
QYWTSPTGGI YPNPNVPRHP NTHVPSHLGS YY 452 
Gene Ontology
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0003677; F:DNA binding; TAS:ProtInc.
 GO:0000980; F:RNA polymerase II distal enhancer sequence-specific DNA binding; IEA:Compara.
 GO:0003700; F:sequence-specific DNA binding transcription factor activity; TAS:ProtInc.
 GO:0008015; P:blood circulation; IEA:Compara.
 GO:0007599; P:hemostasis; TAS:ProtInc.
 GO:0009887; P:organ morphogenesis; TAS:ProtInc.
 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.