CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000230
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 AT-rich interactive domain-containing protein 1A 
Protein Synonyms/Alias
 ARID domain-containing protein 1A; B120; BRG1-associated factor 250; BAF250; BRG1-associated factor 250a; BAF250A; Osa homolog 1; hOSA1; SWI-like protein; SWI/SNF complex protein p270; SWI/SNF-related, matrix-associated, actin-dependent regulator of chromatin subfamily F member 1; hELD 
Gene Name
 ARID1A 
Gene Synonyms/Alias
 BAF250; BAF250A; C1orf4; OSA1; SMARCF1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
71GPPQPLGKELQDGAEacetylation[1, 2]
1612PFLHSGMKMQKAGPPacetylation[3]
1662QRRRLTMKDIGTPEAubiquitination[4, 5]
1830FVVDCSDKLGRVQEFubiquitination[6]
1905PPDGPPEKRITATMDacetylation[3]
1979DWQDSLAKRCVCVSNubiquitination[6]
2020KLILLHHKHPERKQAubiquitination[6]
2146PPFSRLEKLYSTMVRubiquitination[4, 5]
Reference
 [1] 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]
 [2] 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]
 [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] 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] 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]
 [6] 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] 
Functional Description
 Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Binds DNA non-specifically. 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 1017 1108 ARID.
 MOTIF 295 299 LXXLL.
 MOTIF 1709 1713 LXXLL.
 MOTIF 1967 1971 LXXLL.
 MOTIF 2085 2089 LXXLL.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 79 79 Phosphoserine.
 MOD_RES 286 286 Phosphothreonine.
 MOD_RES 301 301 Phosphoserine.
 MOD_RES 363 363 Phosphoserine.
 MOD_RES 604 604 Phosphoserine.
 MOD_RES 696 696 Phosphoserine.
 MOD_RES 698 698 Phosphoserine.
 MOD_RES 702 702 Phosphoserine.
 MOD_RES 764 764 Phosphoserine.
 MOD_RES 772 772 Phosphoserine.
 MOD_RES 1184 1184 Phosphoserine.
 MOD_RES 1604 1604 Phosphoserine.
 MOD_RES 1612 1612 N6-acetyllysine.
 MOD_RES 1905 1905 N6-acetyllysine.
 MOD_RES 1944 1944 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Chromatin regulator; Complete proteome; Direct protein sequencing; DNA-binding; Mental retardation; Neurogenesis; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2285 AA 
Protein Sequence
MAAQVAPAAA SSLGNPPPPP PSELKKAEQQ QREEAGGEAA AAAAAERGEM KAAAGQESEG 60
PAVGPPQPLG KELQDGAESN GGGGGGGAGS GGGPGAEPDL KNSNGNAGPR PALNNNLTEP 120
PGGGGGGSSD GVGAPPHSAA AALPPPAYGF GQPYGRSPSA VAAAAAAVFH QQHGGQQSPG 180
LAALQSGGGG GLEPYAGPQQ NSHDHGFPNH QYNSYYPNRS AYPPPAPAYA LSSPRGGTPG 240
SGAAAAAGSK PPPSSSASAS SSSSSFAQQR FGAMGGGGPS AAGGGTPQPT ATPTLNQLLT 300
SPSSARGYQG YPGGDYSGGP QDGGAGKGPA DMASQCWGAA AAAAAAAAAS GGAQQRSHHA 360
PMSPGSSGGG GQPLARTPQP SSPMDQMGKM RPQPYGGTNP YSQQQGPPSG PQQGHGYPGQ 420
PYGSQTPQRY PMTMQGRAQS AMGGLSYTQQ IPPYGQQGPS GYGQQGQTPY YNQQSPHPQQ 480
QQPPYSQQPP SQTPHAQPSY QQQPQSQPPQ LQSSQPPYSQ QPSQPPHQQS PAPYPSQQST 540
TQQHPQSQPP YSQPQAQSPY QQQQPQQPAP STLSQQAAYP QPQSQQSQQT AYSQQRFPPP 600
QELSQDSFGS QASSAPSMTS SKGGQEDMNL SLQSRPSSLP DLSGSIDDLP MGTEGALSPG 660
VSTSGISSSQ GEQSNPAQSP FSPHTSPHLP GIRGPSPSPV GSPASVAQSR SGPLSPAAVP 720
GNQMPPRPPS GQSDSIMHPS MNQSSIAQDR GYMQRNPQMP QYSSPQPGSA LSPRQPSGGQ 780
IHTGMGSYQQ NSMGSYGPQG GQYGPQGGYP RQPNYNALPN ANYPSAGMAG GINPMGAGGQ 840
MHGQPGIPPY GTLPPGRMSH ASMGNRPYGP NMANMPPQVG SGMCPPPGGM NRKTQETAVA 900
MHVAANSIQN RPPGYPNMNQ GGMMGTGPPY GQGINSMAGM INPQGPPYSM GGTMANNSAG 960
MAASPEMMGL GDVKLTPATK MNNKADGTPK TESKSKKSSS STTTNEKITK LYELGGEPER 1020
KMWVDRYLAF TEEKAMGMTN LPAVGRKPLD LYRLYVSVKE IGGLTQVNKN KKWRELATNL 1080
NVGTSSSAAS SLKKQYIQCL YAFECKIERG EDPPPDIFAA ADSKKSQPKI QPPSPAGSGS 1140
MQGPQTPQST SSSMAEGGDL KPPTPASTPH SQIPPLPGMS RSNSVGIQDA FNDGSDSTFQ 1200
KRNSMTPNPG YQPSMNTSDM MGRMSYEPNK DPYGSMRKAP GSDPFMSSGQ GPNGGMGDPY 1260
SRAAGPGLGN VAMGPRQHYP YGGPYDRVRT EPGIGPEGNM STGAPQPNLM PSNPDSGMYS 1320
PSRYPPQQQQ QQQQRHDSYG NQFSTQGTPS GSPFPSQQTT MYQQQQQNYK RPMDGTYGPP 1380
AKRHEGEMYS VPYSTGQGQP QQQQLPPAQP QPASQQQAAQ PSPQQDVYNQ YGNAYPATAT 1440
AATERRPAGG PQNQFPFQFG RDRVSAPPGT NAQQNMPPQM MGGPIQASAE VAQQGTMWQG 1500
RNDMTYNYAN RQSTGSAPQG PAYHGVNRTD EMLHTDQRAN HEGSWPSHGT RQPPYGPSAP 1560
VPPMTRPPPS NYQPPPSMQN HIPQVSSPAP LPRPMENRTS PSKSPFLHSG MKMQKAGPPV 1620
PASHIAPAPV QPPMIRRDIT FPPGSVEATQ PVLKQRRRLT MKDIGTPEAW RVMMSLKSGL 1680
LAESTWALDT INILLYDDNS IMTFNLSQLP GLLELLVEYF RRCLIEIFGI LKEYEVGDPG 1740
QRTLLDPGRF SKVSSPAPME GGEEEEELLG PKLEEEEEEE VVENDEEIAF SGKDKPASEN 1800
SEEKLISKFD KLPVKIVQKN DPFVVDCSDK LGRVQEFDSG LLHWRIGGGD TTEHIQTHFE 1860
SKTELLPSRP HAPCPPAPRK HVTTAEGTPG TTDQEGPPPD GPPEKRITAT MDDMLSTRSS 1920
TLTEDGAKSS EAIKESSKFP FGISPAQSHR NIKILEDEPH SKDETPLCTL LDWQDSLAKR 1980
CVCVSNTIRS LSFVPGNDFE MSKHPGLLLI LGKLILLHHK HPERKQAPLT YEKEEEQDQG 2040
VSCNKVEWWW DCLEMLRENT LVTLANISGQ LDLSPYPESI CLPVLDGLLH WAVCPSAEAQ 2100
DPFSTLGPNA VLSPQRLVLE TLSKLSIQDN NVDLILATPP FSRLEKLYST MVRFLSDRKN 2160
PVCREMAVVL LANLAQGDSL AARAIAVQKG SIGNLLGFLE DSLAATQFQQ SQASLLHMQN 2220
PPFEPTSVDM MRRAARALLA LAKVDENHSE FTLYESRLLD ISVSPLMNSL VSQVICDVLF 2280
LIGQS 2285 
Gene Ontology
 GO:0071565; C:nBAF complex; ISS:UniProtKB.
 GO:0071564; C:npBAF complex; ISS:UniProtKB.
 GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
 GO:0016514; C:SWI/SNF complex; IDA:UniProtKB.
 GO:0003677; F:DNA binding; NAS:UniProtKB.
 GO:0003713; F:transcription coactivator activity; NAS:BHF-UCL.
 GO:0030521; P:androgen receptor signaling pathway; IDA:UniProtKB.
 GO:0048096; P:chromatin-mediated maintenance of transcription; TAS:UniProtKB.
 GO:0042921; P:glucocorticoid receptor signaling pathway; IDA:UniProtKB.
 GO:0030520; P:intracellular estrogen receptor signaling pathway; IDA:UniProtKB.
 GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
 GO:0006337; P:nucleosome disassembly; IDA:BHF-UCL.
 GO:0042766; P:nucleosome mobilization; TAS: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
 IPR001606; ARID/BRIGHT_DNA-bd.
 IPR021906; DUF3518. 
Pfam
 PF01388; ARID
 PF12031; DUF3518 
SMART
 SM00501; BRIGHT 
PROSITE
 PS51011; ARID 
PRINTS