CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001707
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Actin-like protein 6A 
Protein Synonyms/Alias
 53 kDa BRG1-associated factor A; Actin-related protein Baf53a; ArpNbeta; BRG1-associated factor 53A; BAF53A; INO80 complex subunit K 
Gene Name
 ACTL6A 
Gene Synonyms/Alias
 BAF53; BAF53A; INO80K 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
60LMEIDGDKGKQGGPTubiquitination[1]
62EIDGDKGKQGGPTYYubiquitination[1, 2, 3, 4]
112HTYKMHVKSEASLHPubiquitination[5]
194VLQQGIVKSPLAGDFubiquitination[5, 6, 7]
226PPYMIASKEAVREGSubiquitination[1, 6]
238EGSPANWKRKEKLPQubiquitination[5, 6, 7]
240SPANWKRKEKLPQVTubiquitination[5, 7]
242ANWKRKEKLPQVTRSubiquitination[3, 5, 7]
303DFGAERLKIPEGLFDubiquitination[1, 5, 6, 7]
371LNRELSQKTPPSMRLubiquitination[1, 5]
379TPPSMRLKLIANNTTacetylation[7]
379TPPSMRLKLIANNTTubiquitination[1, 2, 4, 5, 6, 7]
421QEYEEGGKQCVERKCubiquitination[5]
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] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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
Functional Description
 Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Required for maximal ATPase activity of SMARCA4/BRG1/BAF190A and for association of the SMARCA4/BRG1/BAF190A containing remodeling complex BAF with chromatin/nuclear matrix. Belongs to the neural progenitors- specific chromatin remodeling complex (npBAF complex) and is required for the proliferation of neural progenitors. 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). Component of the NuA4 histone acetyltransferase (HAT) complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage. 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. Putative core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair. 
Sequence Annotation
 MOD_RES 2 2 N-acetylserine.
 MOD_RES 233 233 Phosphoserine.  
Keyword
 Acetylation; Activator; Alternative splicing; Chromatin regulator; Complete proteome; Direct protein sequencing; DNA damage; DNA recombination; DNA repair; Growth regulation; Neurogenesis; Nucleus; Phosphoprotein; Reference proteome; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 429 AA 
Protein Sequence
MSGGVYGGDE VGALVFDIGS YTVRAGYAGE DCPKVDFPTA IGMVVERDDG STLMEIDGDK 60
GKQGGPTYYI DTNALRVPRE NMEAISPLKN GMVEDWDSFQ AILDHTYKMH VKSEASLHPV 120
LMSEAPWNTR AKREKLTELM FEHYNIPAFF LCKTAVLTAF ANGRSTGLIL DSGATHTTAI 180
PVHDGYVLQQ GIVKSPLAGD FITMQCRELF QEMNIELVPP YMIASKEAVR EGSPANWKRK 240
EKLPQVTRSW HNYMCNCVIQ DFQASVLQVS DSTYDEQVAA QMPTVHYEFP NGYNCDFGAE 300
RLKIPEGLFD PSNVKGLSGN TMLGVSHVVT TSVGMCDIDI RPGLYGSVIV AGGNTLIQSF 360
TDRLNRELSQ KTPPSMRLKL IANNTTVERR FSSWIGGSIL ASLGTFQQMW ISKQEYEEGG 420
KQCVERKCP 429 
Gene Ontology
 GO:0031011; C:Ino80 complex; IDA:UniProtKB.
 GO:0071564; C:npBAF complex; ISS:UniProtKB.
 GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:UniProtKB.
 GO:0005886; C:plasma membrane; IDA:LIFEdb.
 GO:0016514; C:SWI/SNF complex; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IEA:InterPro.
 GO:0003682; F:chromatin binding; TAS:ProtInc.
 GO:0003713; F:transcription coactivator activity; NAS:BHF-UCL.
 GO:0006338; P:chromatin remodeling; IDA:BHF-UCL.
 GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
 GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
 GO:0043968; P:histone H2A acetylation; IDA:UniProtKB.
 GO:0043967; P:histone H4 acetylation; IDA:UniProtKB.
 GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
 GO:0003407; P:neural retina development; IEP:BHF-UCL.
 GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
 GO:0006357; P:regulation of transcription from RNA polymerase II promoter; NAS:BHF-UCL.
 GO:0007165; P:signal transduction; TAS:ProtInc.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR004000; Actin-related.
 IPR004001; Actin_CS. 
Pfam
 PF00022; Actin 
SMART
 SM00268; ACTIN 
PROSITE
 PS00406; ACTINS_1
 PS00432; ACTINS_2 
PRINTS
 PR00190; ACTIN.