CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018876
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 SWI/SNF complex subunit SMARCC1 
Protein Synonyms/Alias
 BRG1-associated factor 155; BAF155; SWI/SNF complex 155 kDa subunit; SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily C member 1 
Gene Name
 SMARCC1 
Gene Synonyms/Alias
 BAF155 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
41KDGGPATKFWESPETubiquitination[1, 2, 3]
129LGAAYKYKNEQGWRRubiquitination[2]
179LIPDIDLKLANKLKDubiquitination[2, 4]
185LKLANKLKDIIKRHQubiquitination[2]
189NKLKDIIKRHQGTFTubiquitination[2]
345ESRKKSGKKGQASLYacetylation[5]
346SRKKSGKKGQASLYGacetylation[5, 6]
354GQASLYGKRRSQKEEacetylation[5, 6, 7, 8]
359YGKRRSQKEEDEQEDacetylation[5, 8]
387IEEVVLPKNVNLKKDacetylation[8]
421ETVTAGGKEDEDPAKubiquitination[1]
428KEDEDPAKGDQSRSVubiquitination[1, 3]
480EFFNGKNKSKTPEIYubiquitination[2]
482FNGKNKSKTPEIYLAubiquitination[2]
588QMLNFPEKNKEKPVDacetylation[6]
588QMLNFPEKNKEKPVDubiquitination[1, 3, 9]
590LNFPEKNKEKPVDLQubiquitination[2, 6]
592FPEKNKEKPVDLQNFubiquitination[1, 2, 6, 9]
608LRTDIYSKKTLAKSKacetylation[5]
716RVASAAAKAALEEFSubiquitination[1, 2, 3, 4, 6, 9, 10, 11, 12]
740LVEAHVKKVQEAARAubiquitination[2]
792PDGQQPEKAENKVENacetylation[7]
796QPEKAENKVENETDEacetylation[7]
829SEVSEDTKSEEKETEubiquitination[1]
856ESDTGKKKVEHEISEubiquitination[2]
880ALASAATKAKHLAAVubiquitination[1, 2, 3, 6, 12]
882ASAATKAKHLAAVEEubiquitination[1, 2, 12]
905LLVETQMKKLEIKLRubiquitination[1]
906LVETQMKKLEIKLRHubiquitination[2]
910QMKKLEIKLRHFEELubiquitination[2]
925ETIMDREKEALEQQRubiquitination[1, 6]
948NFHMEQLKYAELRARacetylation[5]
948NFHMEQLKYAELRARubiquitination[2, 9]
Reference
 [1] 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]
 [2] 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]
 [3] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [4] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] 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]
 [9] 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]
 [10] A data set of human endogenous protein ubiquitination sites.
 Shi Y, Chan DW, Jung SY, Malovannaya A, Wang Y, Qin J.
 Mol Cell Proteomics. 2011 May;10(5):M110.002089. [PMID: 20972266]
 [11] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [12] 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] 
Functional Description
 Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). May stimulate the ATPase activity of the catalytic subunit of the complex. 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 449 546 SWIRM.
 DOMAIN 618 669 SANT.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 301 301 Phosphoserine (By similarity).
 MOD_RES 310 310 Phosphoserine.
 MOD_RES 328 328 Phosphoserine.
 MOD_RES 330 330 Phosphoserine.
 MOD_RES 335 335 Phosphothreonine.
 MOD_RES 337 337 Phosphothreonine (By similarity).
 MOD_RES 345 345 N6-acetyllysine.
 MOD_RES 346 346 N6-acetyllysine.
 MOD_RES 350 350 Phosphoserine.
 MOD_RES 354 354 N6-acetyllysine.
 MOD_RES 357 357 Phosphoserine.
 MOD_RES 359 359 N6-acetyllysine.
 MOD_RES 398 398 Phosphothreonine.
 MOD_RES 573 573 Phosphoserine.
 MOD_RES 822 822 Phosphoserine.
 MOD_RES 825 825 Phosphoserine.
 MOD_RES 948 948 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Chromatin regulator; Coiled coil; Complete proteome; Direct protein sequencing; Neurogenesis; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1105 AA 
Protein Sequence
MAAAAGGGGP GTAVGATGSG IAAAAAGLAV YRRKDGGPAT KFWESPETVS QLDSVRVWLG 60
KHYKKYVHAD APTNKTLAGL VVQLLQFQED AFGKHVTNPA FTKLPAKCFM DFKAGGALCH 120
ILGAAYKYKN EQGWRRFDLQ NPSRMDRNVE MFMNIEKTLV QNNCLTRPNI YLIPDIDLKL 180
ANKLKDIIKR HQGTFTDEKS KASHHIYPYS SSQDDEEWLR PVMRKEKQVL VHWGFYPDSY 240
DTWVHSNDVD AEIEDPPIPE KPWKVHVKWI LDTDIFNEWM NEEDYEVDEN RKPVSFRQRI 300
STKNEEPVRS PERRDRKASA NARKRKHSPS PPPPTPTESR KKSGKKGQAS LYGKRRSQKE 360
EDEQEDLTKD MEDPTPVPNI EEVVLPKNVN LKKDSENTPV KGGTVADLDE QDEETVTAGG 420
KEDEDPAKGD QSRSVDLGED NVTEQTNHII IPSYASWFDY NCIHVIERRA LPEFFNGKNK 480
SKTPEIYLAY RNFMIDTYRL NPQEYLTSTA CRRNLTGDVC AVMRVHAFLE QWGLVNYQVD 540
PESRPMAMGP PPTPHFNVLA DTPSGLVPLH LRSPQVPAAQ QMLNFPEKNK EKPVDLQNFG 600
LRTDIYSKKT LAKSKGASAG REWTEQETLL LLEALEMYKD DWNKVSEHVG SRTQDECILH 660
FLRLPIEDPY LENSDASLGP LAYQPVPFSQ SGNPVMSTVA FLASVVDPRV ASAAAKAALE 720
EFSRVREEVP LELVEAHVKK VQEAARASGK VDPTYGLESS CIAGTGPDEP EKLEGAEEEK 780
MEADPDGQQP EKAENKVENE TDEGDKAQDG ENEKNSEKEQ DSEVSEDTKS EEKETEENKE 840
LTDTCKERES DTGKKKVEHE ISEGNVATAA AAALASAATK AKHLAAVEER KIKSLVALLV 900
ETQMKKLEIK LRHFEELETI MDREKEALEQ QRQQLLTERQ NFHMEQLKYA ELRARQQMEQ 960
QQHGQNPQQA HQHSGGPGLA PLGAAGHPGM MPHQQPPPYP LMHHQMPPPH PPQPGQIPGP 1020
GSMMPGQHMP GRMIPTVAAN IHPSGSGPTP PGMPPMPGNI LGPRVPLTAP NGMYPPPPQQ 1080
QPPPPPPADG VPPPPAPGPP ASAAP 1105 
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:0071778; C:WINAC complex; IDA:BHF-UCL.
 GO:0001741; C:XY body; IEA:Compara.
 GO:0003682; F:chromatin binding; IEA:Compara.
 GO:0003677; F:DNA binding; IEA:InterPro.
 GO:0003713; F:transcription coactivator activity; NAS:BHF-UCL.
 GO:0006338; P:chromatin remodeling; IDA:UniProtKB.
 GO:0008286; P:insulin receptor signaling pathway; IEA:Compara.
 GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
 GO:0006337; P:nucleosome disassembly; IDA:BHF-UCL.
 GO:0009887; P:organ morphogenesis; IEA:Compara.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Compara.
 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