CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008380
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Transcription activator BRG1 
Protein Synonyms/Alias
 ATP-dependent helicase SMARCA4; BRG1-associated factor 190A; BAF190A; Mitotic growth and transcription activator; Protein BRG-1; Protein brahma homolog 1; SNF2-beta; SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4 
Gene Name
 SMARCA4 
Gene Synonyms/Alias
 BAF190A; BRG1; SNF2B; SNF2L4 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
188RAQIMAYKMLARGQPacetylation[1, 2]
357SRITPIQKPRGLDPVubiquitination[3]
399LAGDLRTKATIELKAubiquitination[3, 4, 5]
405TKATIELKALRLLNFubiquitination[3, 4, 5]
437LETALNAKAYKRSKRubiquitination[3, 4, 5]
455REARITEKLEKQQKIacetylation[1, 2, 5, 6]
455REARITEKLEKQQKIubiquitination[3, 5]
458RITEKLEKQQKIEQEubiquitination[3]
471QERKRRQKHQEYLNSubiquitination[4]
496YHRSVTGKIQKLTKAubiquitination[3]
502GKIQKLTKAVATYHAubiquitination[3]
626VIHVESGKILTGTDAacetylation[2, 5, 7]
626VIHVESGKILTGTDAubiquitination[4]
711RHIIENAKQDVDDEYubiquitination[3, 8]
835SVVKVSYKGSPAARRubiquitination[5]
991VEAQLPEKVEYVIKCubiquitination[5]
997EKVEYVIKCDMSALQubiquitination[3, 5]
1024LLTDGSEKDKKGKGGubiquitination[5]
1033KKGKGGTKTLMNTIMacetylation[1]
1081DLYRASGKFELLDRIubiquitination[4]
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] 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]
 [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] 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]
 [6] 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]
 [7] 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]
 [8] 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
 Transcriptional coactivator cooperating with nuclear hormone receptors to potentiate transcriptional activation. Component of the CREST-BRG1 complex, a multiprotein complex that regulates promoter activation by orchestrating a calcium-dependent release of a repressor complex and a recruitment of an activator complex. In resting neurons, transcription of the c-FOS promoter is inhibited by BRG1-dependent recruitment of a phospho-RB1-HDAC repressor complex. Upon calcium influx, RB1 is dephosphorylated by calcineurin, which leads to release of the repressor complex. At the same time, there is increased recruitment of CREBBP to the promoter by a CREST-dependent mechanism, which leads to transcriptional activation. The CREST-BRG1 complex also binds to the NR2B promoter, and activity-dependent induction of NR2B expression involves a release of HDAC1 and recruitment of CREBBP. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to post-mitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron- specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth. SMARCA4/BAF190A may promote neural stem cell self- renewal/proliferation by enhancing Notch-dependent proliferative signals, while concurrently making the neural stem cell insensitive to SHH-dependent differentiating cues (By similarity). Also involved in vitamin D-coupled transcription regulation via its association with the WINAC complex, a chromatin-remodeling complex recruited by vitamin D receptor (VDR), which is required for the ligand-bound VDR-mediated transrepression of the CYP27B1 gene. Acts as a corepressor of ZEB1 to regulate E-cadherin transcription and is required for induction of epithelial- mesenchymal transition (EMT) by ZEB1. 
Sequence Annotation
 DOMAIN 171 206 QLQ.
 DOMAIN 460 532 HSA.
 DOMAIN 766 931 Helicase ATP-binding.
 DOMAIN 1084 1246 Helicase C-terminal.
 DOMAIN 1477 1547 Bromo.
 NP_BIND 779 786 ATP (Potential).
 REGION 1 282 Necessary for interaction with
 MOTIF 881 884 DEGH box.
 MOD_RES 11 11 Phosphothreonine.
 MOD_RES 188 188 N6-acetyllysine.
 MOD_RES 353 353 Phosphothreonine.
 MOD_RES 609 609 Phosphothreonine.
 MOD_RES 610 610 Phosphoserine.
 MOD_RES 613 613 Phosphoserine.
 MOD_RES 695 695 Phosphoserine.
 MOD_RES 699 699 Phosphoserine.
 MOD_RES 1382 1382 Phosphoserine.
 MOD_RES 1452 1452 Phosphoserine.
 MOD_RES 1570 1570 Phosphoserine.
 MOD_RES 1575 1575 Phosphoserine.
 MOD_RES 1586 1586 Phosphoserine.
 MOD_RES 1627 1627 Phosphoserine.
 MOD_RES 1631 1631 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Activator; Alternative splicing; ATP-binding; Bromodomain; Chromatin regulator; Complete proteome; Disease mutation; Helicase; Hydrolase; Mental retardation; Neurogenesis; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repressor; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1647 AA 
Protein Sequence
MSTPDPPLGG TPRPGPSPGP GPSPGAMLGP SPGPSPGSAH SMMGPSPGPP SAGHPIPTQG 60
PGGYPQDNMH QMHKPMESMH EKGMSDDPRY NQMKGMGMRS GGHAGMGPPP SPMDQHSQGY 120
PSPLGGSEHA SSPVPASGPS SGPQMSSGPG GAPLDGADPQ ALGQQNRGPT PFNQNQLHQL 180
RAQIMAYKML ARGQPLPDHL QMAVQGKRPM PGMQQQMPTL PPPSVSATGP GPGPGPGPGP 240
GPGPAPPNYS RPHGMGGPNM PPPGPSGVPP GMPGQPPGGP PKPWPEGPMA NAAAPTSTPQ 300
KLIPPQPTGR PSPAPPAVPP AASPVMPPQT QSPGQPAQPA PMVPLHQKQS RITPIQKPRG 360
LDPVEILQER EYRLQARIAH RIQELENLPG SLAGDLRTKA TIELKALRLL NFQRQLRQEV 420
VVCMRRDTAL ETALNAKAYK RSKRQSLREA RITEKLEKQQ KIEQERKRRQ KHQEYLNSIL 480
QHAKDFKEYH RSVTGKIQKL TKAVATYHAN TEREQKKENE RIEKERMRRL MAEDEEGYRK 540
LIDQKKDKRL AYLLQQTDEY VANLTELVRQ HKAAQVAKEK KKKKKKKKAE NAEGQTPAIG 600
PDGEPLDETS QMSDLPVKVI HVESGKILTG TDAPKAGQLE AWLEMNPGYE VAPRSDSEES 660
GSEEEEEEEE EEQPQAAQPP TLPVEEKKKI PDPDSDDVSE VDARHIIENA KQDVDDEYGV 720
SQALARGLQS YYAVAHAVTE RVDKQSALMV NGVLKQYQIK GLEWLVSLYN NNLNGILADE 780
MGLGKTIQTI ALITYLMEHK RINGPFLIIV PLSTLSNWAY EFDKWAPSVV KVSYKGSPAA 840
RRAFVPQLRS GKFNVLLTTY EYIIKDKHIL AKIRWKYMIV DEGHRMKNHH CKLTQVLNTH 900
YVAPRRLLLT GTPLQNKLPE LWALLNFLLP TIFKSCSTFE QWFNAPFAMT GEKVDLNEEE 960
TILIIRRLHK VLRPFLLRRL KKEVEAQLPE KVEYVIKCDM SALQRVLYRH MQAKGVLLTD 1020
GSEKDKKGKG GTKTLMNTIM QLRKICNHPY MFQHIEESFS EHLGFTGGIV QGLDLYRASG 1080
KFELLDRILP KLRATNHKVL LFCQMTSLMT IMEDYFAYRG FKYLRLDGTT KAEDRGMLLK 1140
TFNEPGSEYF IFLLSTRAGG LGLNLQSADT VIIFDSDWNP HQDLQAQDRA HRIGQQNEVR 1200
VLRLCTVNSV EEKILAAAKY KLNVDQKVIQ AGMFDQKSSS HERRAFLQAI LEHEEQDESR 1260
HCSTGSGSAS FAHTAPPPAG VNPDLEEPPL KEEDEVPDDE TVNQMIARHE EEFDLFMRMD 1320
LDRRREEARN PKRKPRLMEE DELPSWIIKD DAEVERLTCE EEEEKMFGRG SRHRKEVDYS 1380
DSLTEKQWLK AIEEGTLEEI EEEVRQKKSS RKRKRDSDAG SSTPTTSTRS RDKDDESKKQ 1440
KKRGRPPAEK LSPNPPNLTK KMKKIVDAVI KYKDSSSGRQ LSEVFIQLPS RKELPEYYEL 1500
IRKPVDFKKI KERIRNHKYR SLNDLEKDVM LLCQNAQTFN LEGSLIYEDS IVLQSVFTSV 1560
RQKIEKEDDS EGEESEEEEE GEEEGSESES RSVKVKIKLG RKEKAQDRLK GGRRRPSRGS 1620
RAKPVVSDDD SEEEQEEDRS GSGSEED 1647 
Gene Ontology
 GO:0000792; C:heterochromatin; IEA:Compara.
 GO:0071565; C:nBAF complex; ISS:UniProtKB.
 GO:0071564; C:npBAF complex; ISS:UniProtKB.
 GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
 GO:0005719; C:nuclear euchromatin; IEA:Compara.
 GO:0005726; C:perichromatin fibrils; IEA:Compara.
 GO:0016514; C:SWI/SNF complex; IDA:UniProtKB.
 GO:0071778; C:WINAC complex; IDA:BHF-UCL.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0003682; F:chromatin binding; IEA:Compara.
 GO:0008094; F:DNA-dependent ATPase activity; IGI:BHF-UCL.
 GO:0004386; F:helicase activity; TAS:ProtInc.
 GO:0070577; F:histone acetyl-lysine binding; IDA:BHF-UCL.
 GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IEA:Compara.
 GO:0001105; F:RNA polymerase II transcription coactivator activity; IDA:BHF-UCL.
 GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
 GO:0035887; P:aortic smooth muscle cell differentiation; IEA:Compara.
 GO:0001832; P:blastocyst growth; IEA:Compara.
 GO:0001835; P:blastocyst hatching; IEA:Compara.
 GO:0000902; P:cell morphogenesis; IEA:Compara.
 GO:0006338; P:chromatin remodeling; IDA:BHF-UCL.
 GO:0060318; P:definitive erythrocyte differentiation; IEA:Compara.
 GO:0010424; P:DNA methylation on cytosine within a CG sequence; IEA:Compara.
 GO:0035116; P:embryonic hindlimb morphogenesis; IEA:Compara.
 GO:0048562; P:embryonic organ morphogenesis; IEA:Compara.
 GO:0048730; P:epidermis morphogenesis; IEA:Compara.
 GO:0030198; P:extracellular matrix organization; IEA:Compara.
 GO:0030900; P:forebrain development; IEA:Compara.
 GO:0007403; P:glial cell fate determination; IEA:Compara.
 GO:0060347; P:heart trabecula formation; IEA:Compara.
 GO:0030902; P:hindbrain development; IEA:Compara.
 GO:0043966; P:histone H3 acetylation; IEA:Compara.
 GO:0030216; P:keratinocyte differentiation; IEA:Compara.
 GO:0001889; P:liver development; IEA:Compara.
 GO:0006346; P:methylation-dependent chromatin silencing; IEA:Compara.
 GO:0060766; P:negative regulation of androgen receptor signaling pathway; IMP:BHF-UCL.
 GO:0030308; P:negative regulation of cell growth; IMP:BHF-UCL.
 GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; TAS:BHF-UCL.
 GO:0007070; P:negative regulation of transcription from RNA polymerase II promoter during mitosis; TAS:BHF-UCL.
 GO:0003407; P:neural retina development; IEP:BHF-UCL.
 GO:0006337; P:nucleosome disassembly; IDA:BHF-UCL.
 GO:0043923; P:positive regulation by host of viral transcription; IMP:BHF-UCL.
 GO:0043388; P:positive regulation of DNA binding; IEA:Compara.
 GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IDA:BHF-UCL.
 GO:0019827; P:stem cell maintenance; IEA:Compara.
 GO:0001570; P:vasculogenesis; IEA:Compara. 
Interpro
 IPR006576; BRK_domain.
 IPR001487; Bromodomain.
 IPR018359; Bromodomain_CS.
 IPR014978; Gln-Leu-Gln_QLQ.
 IPR013999; HAS_subgr.
 IPR014012; Helicase/SANT-assoc_DNA-bd.
 IPR014001; Helicase_ATP-bd.
 IPR001650; Helicase_C.
 IPR006562; HSA.
 IPR027417; P-loop_NTPase.
 IPR000330; SNF2_N. 
Pfam
 PF07533; BRK
 PF00439; Bromodomain
 PF00271; Helicase_C
 PF07529; HSA
 PF08880; QLQ
 PF00176; SNF2_N 
SMART
 SM00592; BRK
 SM00297; BROMO
 SM00487; DEXDc
 SM00490; HELICc
 SM00573; HSA
 SM00951; QLQ 
PROSITE
 PS00633; BROMODOMAIN_1
 PS50014; BROMODOMAIN_2
 PS51192; HELICASE_ATP_BIND_1
 PS51194; HELICASE_CTER
 PS51204; HSA
 PS51666; QLQ 
PRINTS
 PR00503; BROMODOMAIN.