CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-017927
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 SWI/SNF complex subunit SMARCC2 
Protein Synonyms/Alias
 BRG1-associated factor 170; BAF170; SWI/SNF complex 170 kDa subunit; SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily C member 2 
Gene Name
 SMARCC2 
Gene Synonyms/Alias
 BAF170 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
275RRKKISAKTLTDEVNubiquitination[1, 2]
326GPSTPYTKSKRGHREacetylation[3]
564QMLNFPDKGKEKPTDacetylation[4]
564QMLNFPDKGKEKPTDubiquitination[1, 2, 5]
568FPDKGKEKPTDMQNFubiquitination[1, 2]
694RVASAAAKSALEEFSubiquitination[1, 2]
702SALEEFSKMKEEVPTubiquitination[1, 2]
872ALAAAAVKAKHLAAVubiquitination[1, 2, 5]
874AAAAVKAKHLAAVEEubiquitination[1, 2, 5]
885AVEERKIKSLVALLVubiquitination[1, 2]
897LLVETQMKKLEIKLRubiquitination[5]
898LVETQMKKLEIKLRHubiquitination[1, 2]
902QMKKLEIKLRHFEELubiquitination[1, 2]
940AFHMEQLKYAEMRARubiquitination[1, 2]
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] 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]
 [4] 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]
 [5] 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
 Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Can stimulate the ATPase activity of the catalytic subunit of these complexes. May be required for CoREST dependent repression of neuronal specific gene promoters in non-neuronal cells. 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 424 521 SWIRM.
 DOMAIN 596 647 SANT.
 MOD_RES 283 283 Phosphoserine.
 MOD_RES 286 286 Phosphoserine.
 MOD_RES 302 302 Phosphoserine.
 MOD_RES 304 304 Phosphoserine.
 MOD_RES 306 306 Phosphoserine.
 MOD_RES 326 326 N6-acetyllysine.
 MOD_RES 347 347 Phosphoserine.
 MOD_RES 548 548 Phosphothreonine.
 MOD_RES 806 806 Phosphoserine (By similarity).
 MOD_RES 810 810 Phosphoserine (By similarity).
 MOD_RES 813 813 Phosphoserine.  
Keyword
 Acetylation; Alternative splicing; Chromatin regulator; Coiled coil; Complete proteome; Neurogenesis; Nucleus; Phosphoprotein; Reference proteome; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1214 AA 
Protein Sequence
MAVRKKDGGP NVKYYEAADT VTQFDNVRLW LGKNYKKYIQ AEPPTNKSLS SLVVQLLQFQ 60
EEVFGKHVSN APLTKLPIKC FLDFKAGGSL CHILAAAYKF KSDQGWRRYD FQNPSRMDRN 120
VEMFMTIEKS LVQNNCLSRP NIFLCPEIEP KLLGKLKDII KRHQGTVTED KNNASHVVYP 180
VPGNLEEEEW VRPVMKRDKQ VLLHWGYYPD SYDTWIPASE IEASVEDAPT PEKPRKVHAK 240
WILDTDTFNE WMNEEDYEVN DDKNPVSRRK KISAKTLTDE VNSPDSDRRD KKGGNYKKRK 300
RSPSPSPTPE AKKKNAKKGP STPYTKSKRG HREEEQEDLT KDMDEPSPVP NVEEVTLPKT 360
VNTKKDSESA PVKGGTMTDL DEQEDESMET TGKDEDENST GNKGEQTKNP DLHEDNVTEQ 420
THHIIIPSYA AWFDYNSVHA IERRALPEFF NGKNKSKTPE IYLAYRNFMI DTYRLNPQEY 480
LTSTACRRNL AGDVCAIMRV HAFLEQWGLI NYQVDAESRP TPMGPPPTSH FHVLADTPSG 540
LVPLQPKTPQ QTSASQQMLN FPDKGKEKPT DMQNFGLRTD MYTKKNVPSK SKAAASATRE 600
WTEQETLLLL EALEMYKDDW NKVSEHVGSR TQDECILHFL RLPIEDPYLE DSEASLGPLA 660
YQPIPFSQSG NPVMSTVAFL ASVVDPRVAS AAAKSALEEF SKMKEEVPTA LVEAHVRKVE 720
EAAKVTGKAD PAFGLESSGI AGTTSDEPER IEESGNDEAR VEGQATDEKK EPKEPREGGG 780
AIEEEAKEKT SEAPKKDEEK GKEGDSEKES EKSDGDPIVD PEKEKEPKEG QEEVLKEVVE 840
SEGERKTKVE RDIGEGNLST AAAAALAAAA VKAKHLAAVE ERKIKSLVAL LVETQMKKLE 900
IKLRHFEELE TIMDREREAL EYQRQQLLAD RQAFHMEQLK YAEMRARQQH FQQMHQQQQQ 960
PPPALPPGSQ PIPPTGAAGP PAVHGLAVAP ASVVPAPAGS GAPPGSLGPS EQIGQAGSTA 1020
GPQQQQPAGA PQPGAVPPGV PPPGPHGPSP FPNQQTPPSM MPGAVPGSGH PGVAGNAPLG 1080
LPFGMPPPPP PPAPSIIPFG SLADSISINL PAPPNLHGHH HHLPFAPGTL PPPNLPVSMA 1140
NPLHPNLPAT TTMPSSLPLG PGLGSAAAQS PAIVAAVQGN LLPSASPLPD PGTPLPPDPT 1200
APSPGTVTPV PPPQ 1214 
Gene Ontology
 GO:0071565; C:nBAF complex; ISS:UniProtKB.
 GO:0071564; C:npBAF complex; ISS:UniProtKB.
 GO:0016514; C:SWI/SNF complex; IDA:UniProtKB.
 GO:0003682; F:chromatin binding; IEA:InterPro.
 GO:0003677; F:DNA binding; IEA:InterPro.
 GO:0003713; F:transcription coactivator activity; NAS:BHF-UCL.
 GO:0006338; P:chromatin remodeling; IDA:UniProtKB.
 GO:0045892; P:negative regulation of transcription, DNA-dependent; IDA:UniProtKB.
 GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
 GO:0006337; P:nucleosome disassembly; IDA:BHF-UCL.
 GO:0045893; P:positive regulation of transcription, DNA-dependent; IDA:UniProtKB.
 GO:0006357; P:regulation of transcription from RNA polymerase II promoter; NAS:BHF-UCL.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR001357; BRCT_dom.
 IPR000953; Chromo_domain/shadow.
 IPR009057; Homeodomain-like.
 IPR001005; SANT/Myb.
 IPR017884; SANT_dom.
 IPR007526; SWIRM.
 IPR011991; WHTH_DNA-bd_dom. 
Pfam
 PF00249; Myb_DNA-binding
 PF04433; SWIRM 
SMART
 SM00298; CHROMO
 SM00717; SANT 
PROSITE
 PS51293; SANT
 PS50934; SWIRM 
PRINTS