UniProt Accession

 SMCA2_HUMAN; P51531; B1ALG3; B1ALG4; D3DRH4; D3DRH5 

Genbank Protein ID

 X72889; D26155; AL359076; AL138755; AL359076; AL138755; AL138755; AL359076; AL138755; AL359076; CH471071; CH471071; CH471071; CH471071 

Genbank Nucleotide ID

 CAA51407.1; BAA05142.1; CAI12967.1; CAI12967.1; CAI12968.1; CAI12968.1; CAI14599.1; CAI14599.1; CAI14600.1; CAI14600.1; EAW58811.1; EAW58813.1; EAW58814.1; EAW58815.1 

Protein Name

 Probable global transcription activator SNF2L2 

Protein Synonyms/Alias

 ATP-dependent helicase SMARCA2; BRG1-associated factor 190B; BAF190B; Protein brahma homolog; hBRM; SNF2-alpha; SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2 

Gene Name

 SMARCA2 

Gene Synonyms/Alias

 BAF190B; BRM; SNF2A; SNF2L2 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
413	LETALNSKAYKRSKR	ubiquitination	[1, 2]
463	LQHAKDFKEYHRSVA	ubiquitination	[3]
604	VTHTETGKVLFGPEA	acetylation	[4, 5, 6]
604	VTHTETGKVLFGPEA	ubiquitination	[1, 2]
672	NSEEVSEKDAKQIIE	acetylation	[6]
997	DGSEKDKKGKGGAKT	acetylation	[4]
999	SEKDKKGKGGAKTLM	acetylation	[4]
1051	ELYRASGKFELLDRI	ubiquitination	[1, 3, 7, 8, 9]
1183	TVNSVEEKILAAAKY	ubiquitination	[3]
1189	EKILAAAKYKLNVDQ	ubiquitination	[3]
1191	ILAAAKYKLNVDQKV	ubiquitination	[3]
1207	QAGMFDQKSSSHERR	ubiquitination	[3]
1323	YSDALTEKQWLRAIE	ubiquitination	[1, 2]
1434	FIQLPSRKELPEYYE	ubiquitination	[10]
1551	KDDKGRDKGKGKKRP	acetylation	[11, 12]
1553	DKGRDKGKGKKRPNR	acetylation	[11, 12, 13]
1555	GRDKGKGKKRPNRGK	acetylation	[11, 12, 13]
1556	RDKGKGKKRPNRGKA	acetylation	[13]

Reference

 [1] 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]
 [2] 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]
 [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] 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]
 [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] 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]
 [8] 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]
 [9] 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]
 [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]
 [11] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
 Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
 Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647]
 [12] Proteome-wide prediction of acetylation substrates.
 Basu A, Rose KL, Zhang J, Beavis RC, Ueberheide B, Garcia BA, Chait B, Zhao Y, Hunt DF, Segal E, Allis CD, Hake SB.
 Proc Natl Acad Sci U S A. 2009 Aug 18;106(33):13785-90. [PMID: 19666589]
 [13] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786] 

Functional Description

 Transcriptional coactivator cooperating with nuclear hormone receptors to potentiate transcriptional activation. 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. 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 (By similarity). 

Sequence Annotation

 DOMAIN 173 208 QLQ.
 DOMAIN 436 508 HSA.
 DOMAIN 736 901 Helicase ATP-binding.
 DOMAIN 1054 1216 Helicase C-terminal.
 DOMAIN 1419 1489 Bromo.
 NP_BIND 749 756 ATP (Potential).
 MOTIF 851 854 DEGH box.
 MOD_RES 175 175 Phosphoserine.
 MOD_RES 329 329 Phosphoserine.
 MOD_RES 997 997 N6-acetyllysine.
 MOD_RES 999 999 N6-acetyllysine.
 MOD_RES 1512 1512 Phosphoserine.
 MOD_RES 1516 1516 Phosphoserine.
 MOD_RES 1528 1528 Phosphoserine.
 MOD_RES 1568 1568 Phosphoserine.
 MOD_RES 1572 1572 Phosphoserine.  

Keyword

 3D-structure; Acetylation; Activator; Alternative splicing; ATP-binding; Bromodomain; Complete proteome; Disease mutation; DNA-binding; Helicase; Hydrolase; Hypotrichosis; Mental retardation; Neurogenesis; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Transcription; Transcription regulation. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 1590 AA 

Protein Sequence

Gene Ontology

 GO:0045111; C:intermediate filament cytoskeleton; IDA:HPA.
 GO:0071565; C:nBAF complex; ISS:UniProtKB.
 GO:0071564; C:npBAF complex; ISS:UniProtKB.
 GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
 GO:0005654; C:nucleoplasm; TAS:ProtInc.
 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:0008094; F:DNA-dependent ATPase activity; TAS:BHF-UCL.
 GO:0004386; F:helicase activity; TAS:ProtInc.
 GO:0001105; F:RNA polymerase II transcription coactivator activity; IDA:UniProtKB.
 GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
 GO:0035887; P:aortic smooth muscle cell differentiation; IEA:Compara.
 GO:0006338; P:chromatin remodeling; TAS:BHF-UCL.
 GO:0030308; P:negative regulation of cell growth; IMP:BHF-UCL.
 GO:0008285; P:negative regulation of cell proliferation; IEA:Compara.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; TAS:BHF-UCL.
 GO:0007399; P:nervous system development; IEA:UniProtKB-KW. 

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.