CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022380
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Bcl-2-associated transcription factor 1 
Protein Synonyms/Alias
 Btf 
Gene Name
 BCLAF1 
Gene Synonyms/Alias
 BTF; KIAA0164 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
152RSSSPYSKSPVSKRRacetylation[1]
332GGDQETAKTGKFLKRubiquitination[2, 3]
335QETAKTGKFLKRFTDacetylation[1]
421SVLADQGKSFATASHacetylation[1]
421SVLADQGKSFATASHubiquitination[3, 4]
437NTEEEGLKYKSKVSLacetylation[1]
437NTEEEGLKYKSKVSLubiquitination[3]
517DYSPPLHKNLDAREKubiquitination[4]
567NRPASLTKDRLLASTubiquitination[4]
593RSIFDHIKLPQASKSubiquitination[4, 5]
622HVKEQYFKSAAMTLNubiquitination[4]
637ERFTSYQKATEEHSTacetylation[1]
637ERFTSYQKATEEHSTubiquitination[3]
831TTFQKRPKEEEWDPEsumoylation[6, 7]
845EYTPKSKKYFLHDDRubiquitination[4]
891SPKWTHDKYQGDGIVacetylation[8]
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] 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]
 [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] 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]
 [5] 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]
 [6] Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif.
 Matic I, Schimmel J, Hendriks IA, van Santen MA, van de Rijke F, van Dam H, Gnad F, Mann M, Vertegaal AC.
 Mol Cell. 2010 Aug 27;39(4):641-52. [PMID: 20797634]
 [7] Targeted identification of SUMOylation sites in human proteins using affinity enrichment and paralog-specific reporter ions.
 Lamoliatte F, Bonneil E, Durette C, Caron-Lizotte O, Wildemann D, Zerweck J, Wenschuh H, Thibault P.
 Mol Cell Proteomics. 2013 Jun 7;. [PMID: 23750026]
 [8] Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome.
 Morselli E, Mariño G, Bennetzen MV, Eisenberg T, Megalou E, Schroeder S, Cabrera S, Bénit P, Rustin P, Criollo A, Kepp O, Galluzzi L, Shen S, Malik SA, Maiuri MC, Horio Y, López-Otín C, Andersen JS, Tavernarakis N, Madeo F, Kroemer G.
 J Cell Biol. 2011 Feb 21;192(4):615-29. [PMID: 21339330] 
Functional Description
 Death-promoting transcriptional repressor. May be involved in cyclin-D1/CCND1 mRNA stability through the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA. 
Sequence Annotation
 MOD_RES 102 102 Phosphoserine.
 MOD_RES 104 104 Phosphoserine.
 MOD_RES 119 119 Phosphoserine (By similarity).
 MOD_RES 122 122 Phosphoserine (By similarity).
 MOD_RES 125 125 Phosphoserine (By similarity).
 MOD_RES 152 152 N6-acetyllysine.
 MOD_RES 177 177 Phosphoserine.
 MOD_RES 181 181 Phosphoserine.
 MOD_RES 196 196 Phosphoserine.
 MOD_RES 198 198 Phosphoserine.
 MOD_RES 222 222 Phosphoserine.
 MOD_RES 264 264 Phosphoserine.
 MOD_RES 268 268 Phosphoserine.
 MOD_RES 284 284 Phosphotyrosine.
 MOD_RES 285 285 Phosphoserine.
 MOD_RES 287 287 Phosphoserine (By similarity).
 MOD_RES 290 290 Phosphoserine.
 MOD_RES 297 297 Phosphoserine.
 MOD_RES 341 341 Phosphothreonine.
 MOD_RES 385 385 Phosphoserine.
 MOD_RES 389 389 Phosphoserine.
 MOD_RES 397 397 Phosphoserine.
 MOD_RES 402 402 Phosphothreonine.
 MOD_RES 437 437 N6-acetyllysine.
 MOD_RES 472 472 Phosphoserine.
 MOD_RES 494 494 Phosphothreonine.
 MOD_RES 496 496 Phosphoserine.
 MOD_RES 502 502 Phosphoserine.
 MOD_RES 512 512 Phosphoserine.
 MOD_RES 531 531 Phosphoserine.
 MOD_RES 566 566 Phosphothreonine.
 MOD_RES 578 578 Phosphoserine.
 MOD_RES 648 648 Phosphoserine.
 MOD_RES 658 658 Phosphoserine.
 MOD_RES 660 660 Phosphoserine.
 MOD_RES 690 690 Phosphoserine.
 MOD_RES 760 760 Phosphoserine.
 MOD_RES 840 840 Phosphothreonine (By similarity).  
Keyword
 Acetylation; Alternative splicing; Complete proteome; Cytoplasm; Direct protein sequencing; DNA-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repressor; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 920 AA 
Protein Sequence
MGRSNSRSHS SRSKSRSQSS SRSRSRSHSR KKRYSSRSRS RTYSRSRSRD RMYSRDYRRD 60
YRNNRGMRRP YGYRGRGRGY YQGGGGRYHR GGYRPVWNRR HSRSPRRGRS RSRSPKRRSV 120
SSQRSRSRSR RSYRSSRSPR SSSSRSSSPY SKSPVSKRRG SQEKQTKKAE GEPQEESPLK 180
SKSQEEPKDT FEHDPSESID EFNKSSATSG DIWPGLSAYD NSPRSPHSPS PIATPPSQSS 240
SCSDAPMLST VHSAKNTPSQ HSHSIQHSPE RSGSGSVGNG SSRYSPSQNS PIHHIPSRRS 300
PAKTIAPQNA PRDESRGRSS FYPDGGDQET AKTGKFLKRF TDEESRVFLL DRGNTRDKEA 360
SKEKGSEKGR AEGEWEDQEA LDYFSDKESG KQKFNDSEGD DTEETEDYRQ FRKSVLADQG 420
KSFATASHRN TEEEGLKYKS KVSLKGNRES DGFREEKNYK LKETGYVVER PSTTKDKHKE 480
EDKNSERITV KKETQSPEQV KSEKLKDLFD YSPPLHKNLD AREKSTFREE SPLRIKMIAS 540
DSHRPEVKLK MAPVPLDDSN RPASLTKDRL LASTLVHSVK KEQEFRSIFD HIKLPQASKS 600
TSESFIQHIV SLVHHVKEQY FKSAAMTLNE RFTSYQKATE EHSTRQKSPE IHRRIDISPS 660
TLRKHTRLAG EERVFKEENQ KGDKKLRCDS ADLRHDIDRR RKERSKERGD SKGSRESSGS 720
RKQEKTPKDY KEYKSYKDDS KHKREQDHSR SSSSSASPSS PSSREEKESK KEREEEFKTH 780
HEMKEYSGFA GVSRPRGTFF RIRGRGRARG VFAGTNTGPN NSNTTFQKRP KEEEWDPEYT 840
PKSKKYFLHD DRDDGVDYWA KRGRGRGTFQ RGRGRFNFKK SGSSPKWTHD KYQGDGIVED 900
EEETMENNEE KKDRRKEEKE 920 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005730; C:nucleolus; IDA:HPA.
 GO:0003677; F:DNA binding; IDA:MGI.
 GO:0006917; P:induction of apoptosis; TAS:UniProtKB.
 GO:0045892; P:negative regulation of transcription, DNA-dependent; TAS:UniProtKB.
 GO:2000144; P:positive regulation of DNA-dependent transcription, initiation; IMP:UniProtKB.
 GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IMP:UniProtKB.
 GO:2001022; P:positive regulation of response to DNA damage stimulus; IMP:UniProtKB.
 GO:0043620; P:regulation of DNA-dependent transcription in response to stress; IMP:UniProtKB.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR026668; Bcl-2_assoc_TF1. 
Pfam
  
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