CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022076
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Bromodomain adjacent to zinc finger domain protein 1A 
Protein Synonyms/Alias
 ATP-dependent chromatin-remodeling protein; ATP-utilizing chromatin assembly and remodeling factor 1; hACF1; CHRAC subunit ACF1; Williams syndrome transcription factor-related chromatin-remodeling factor 180; WCRF180; hWALp1 
Gene Name
 BAZ1A 
Gene Synonyms/Alias
 ACF1; WCRF180; HSPC317 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
73EALESEKKARQNLQSubiquitination[1]
113DDIFAYVKDRYFVEEubiquitination[1]
181CSFQNGKKKDAIDPLubiquitination[1]
182SFQNGKKKDAIDPLLubiquitination[1]
191AIDPLLFKYKVQPTKubiquitination[1, 2, 3]
208LHESAIVKATQISRRubiquitination[1]
229DKLKLFLKQHCEPQDubiquitination[1]
294QEDNVANKQTLASYRubiquitination[1]
324MKSLAFEKAKLKREKubiquitination[1]
326SLAFEKAKLKREKADubiquitination[1]
342LEAKKKEKEDKEKKRacetylation[4]
345KKKEKEDKEKKREELacetylation[4]
347KEKEDKEKKREELKKacetylation[4]
348EKEDKEKKREELKKIacetylation[4]
387KLREEKRKYVEYLKQubiquitination[1, 2, 3, 5]
540LHQGCSLKSLDLDSCubiquitination[1]
570DVTSANAKYRYQKRGubiquitination[1, 2, 3]
598LSNPSLVKKLSSTSVubiquitination[1, 6]
919GHRESALKETLLQEKubiquitination[1, 5]
926KETLLQEKSRICAQLubiquitination[1]
973PSQMCAEKQLELRLRacetylation[5]
973PSQMCAEKQLELRLRubiquitination[1]
999QGTLGAIKVTDRHIWubiquitination[1]
1023ELLSEENKENGIIKTubiquitination[1]
1097GIERRFLKAPLDASDubiquitination[1, 5]
1156ARCKICRKKGDAENMubiquitination[1]
1157RCKICRKKGDAENMVubiquitination[1]
1277LPVKTRGKLSSSFSSacetylation[5]
1327SAPPTETKSLRIASRacetylation[5]
1362RRKRRGRKSANNTPEubiquitination[1]
1383NFRVIATKSSEQSRSubiquitination[1]
1396RSVNIASKLSLQESEacetylation[5]
1396RSVNIASKLSLQESEubiquitination[1]
1471PDYYDIIKKPIALNIubiquitination[1]
1553STPPAAKKSRI****ubiquitination[1]
Reference
 [1] 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]
 [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] 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]
 [4] Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome.
 Morselli E, Mariño G, Bennetzen MV, Eisenberg T, Megalou E, Schroeder S, Cabrera S, Bénit P, Rustin P, Criollo A, Kepp O, Galluzzi L, Shen S, Malik SA, Maiuri MC, Horio Y, López-Otín C, Andersen JS, Tavernarakis N, Madeo F, Kroemer G.
 J Cell Biol. 2011 Feb 21;192(4):615-29. [PMID: 21339330]
 [5] 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]
 [6] 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
 Component of the ACF complex, an ATP-dependent chromatin remodeling complex, that regulates spacing of nucleosomes using ATP to generate evenly spaced nucleosomes along the chromatin. The ATPase activity of the complex is regulated by the length of flanking DNA. Also involved in facilitating the DNA replication process. BAZ1A is the accessory, non-catalytic subunit of the complex which can enhance and direct the process provided by the ATPase subunit, SMARCA5, probably through targeting pericentromeric heterochromatin in late S phase. Moves end- positioned nucleosomes to a predominantly central position. May have a role in nuclear receptor-mediated transcription repression. 
Sequence Annotation
 DOMAIN 22 128 WAC.
 DOMAIN 422 487 DDT.
 DOMAIN 1446 1516 Bromo.
 ZN_FING 1148 1198 PHD-type.
 REGION 1 133 Required for interaction with NCOR1.
 REGION 1 128 Required for association with the
 REGION 667 933 Interaction with SMARCA5.
 MOD_RES 270 270 Phosphoserine.
 MOD_RES 702 702 Phosphoserine.
 MOD_RES 731 731 Phosphothreonine.
 MOD_RES 1281 1281 Phosphoserine.
 MOD_RES 1371 1371 Phosphoserine.
 MOD_RES 1402 1402 Phosphoserine.
 MOD_RES 1413 1413 Phosphoserine.
 MOD_RES 1417 1417 Phosphoserine.  
Keyword
 Alternative splicing; Bromodomain; Coiled coil; Complete proteome; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Transcription; Transcription regulation; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1556 AA 
Protein Sequence
MPLLHRKPFV RQKPPADLRP DEEVFYCKVT NEIFRHYDDF FERTILCNSL VWSCAVTGRP 60
GLTYQEALES EKKARQNLQS FPEPLIIPVL YLTSLTHRSR LHEICDDIFA YVKDRYFVEE 120
TVEVIRNNGA RLQCRILEVL PPSHQNGFAN GHVNSVDGET IIISDSDDSE TQSCSFQNGK 180
KKDAIDPLLF KYKVQPTKKE LHESAIVKAT QISRRKHLFS RDKLKLFLKQ HCEPQDGVIK 240
IKASSLSTYK IAEQDFSYFF PDDPPTFIFS PANRRRGRPP KRIHISQEDN VANKQTLASY 300
RSKATKERDK LLKQEEMKSL AFEKAKLKRE KADALEAKKK EKEDKEKKRE ELKKIVEEER 360
LKKKEEKERL KVEREKEREK LREEKRKYVE YLKQWSKPRE DMECDDLKEL PEPTPVKTRL 420
PPEIFGDALM VLEFLNAFGE LFDLQDEFPD GVTLEVLEEA LVGNDSEGPL CELLFFFLTA 480
IFQAIAEEEE EVAKEQLTDA DTKDLTEALD EDADPTKSAL SAVASLAAAW PQLHQGCSLK 540
SLDLDSCTLS EILRLHILAS GADVTSANAK YRYQKRGGFD ATDDACMELR LSNPSLVKKL 600
SSTSVYDLTP GEKMKILHAL CGKLLTLVST RDFIEDYVDI LRQAKQEFRE LKAEQHRKER 660
EEAAARIRKR KEEKLKEQEQ KMKEKQEKLK EDEQRNSTAD ISIGEEERED FDTSIESKDT 720
EQKELDQDMV TEDEDDPGSH KRGRRGKRGQ NGFKEFTRQE QINCVTREPL TADEEEALKQ 780
EHQRKEKELL EKIQSAIACT NIFPLGRDRM YRRYWIFPSI PGLFIEEDYS GLTEDMLLPR 840
PSSFQNNVQS QDPQVSTKTG EPLMSESTSN IDQGPRDHSV QLPKPVHKPN RWCFYSSCEQ 900
LDQLIEALNS RGHRESALKE TLLQEKSRIC AQLARFSEEK FHFSDKPQPD SKPTYSRGRS 960
SNAYDPSQMC AEKQLELRLR DFLLDIEDRI YQGTLGAIKV TDRHIWRSAL ESGRYELLSE 1020
ENKENGIIKT VNEDVEEMEI DEQTKVIVKD RLLGIKTETP STVSTNASTP QSVSSVVHYL 1080
AMALFQIEQG IERRFLKAPL DASDSGRSYK TVLDRWRESL LSSASLSQVF LHLSTLDRSV 1140
IWSKSILNAR CKICRKKGDA ENMVLCDGCD RGHHTYCVRP KLKTVPEGDW FCPECRPKQR 1200
SRRLSSRQRP SLESDEDVED SMGGEDDEVD GDEEEGQSEE EEYEVEQDED DSQEEEEVSL 1260
PKRGRPQVRL PVKTRGKLSS SFSSRGQQQE PGRYPSRSQQ STPKTTVSSK TGRSLRKINS 1320
APPTETKSLR IASRSTRHSH GPLQADVFVE LLSPRRKRRG RKSANNTPEN SPNFPNFRVI 1380
ATKSSEQSRS VNIASKLSLQ ESESKRRCRK RQSPEPSPVT LGRRSSGRQG GVHELSAFEQ 1440
LVVELVRHDD SWPFLKLVSK IQVPDYYDII KKPIALNIIR EKVNKCEYKL ASEFIDDIEL 1500
MFSNCFEYNP RNTSEAKAGT RLQAFFHIQA QKLGLHVTPS NVDQVSTPPA AKKSRI 1556 
Gene Ontology
 GO:0016590; C:ACF complex; TAS:BHF-UCL.
 GO:0008623; C:CHRAC; IDA:UniProtKB.
 GO:0000228; C:nuclear chromosome; IEA:Compara.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006338; P:chromatin remodeling; TAS:BHF-UCL.
 GO:0006261; P:DNA-dependent DNA replication; IDA:UniProtKB.
 GO:0006355; P:regulation of transcription, DNA-dependent; NAS:BHF-UCL.
 GO:0006351; P:transcription, DNA-dependent; NAS:BHF-UCL. 
Interpro
 IPR001487; Bromodomain.
 IPR018359; Bromodomain_CS.
 IPR004022; DDT_dom.
 IPR018500; DDT_dom_subgr.
 IPR018501; DDT_dom_superfamily.
 IPR013136; WSTF_Acf1_Cbp146.
 IPR019786; Zinc_finger_PHD-type_CS.
 IPR011011; Znf_FYVE_PHD.
 IPR001965; Znf_PHD.
 IPR019787; Znf_PHD-finger.
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF00439; Bromodomain
 PF02791; DDT
 PF00628; PHD
 PF10537; WAC_Acf1_DNA_bd 
SMART
 SM00297; BROMO
 SM00571; DDT
 SM00249; PHD
 SM00184; RING 
PROSITE
 PS00633; BROMODOMAIN_1
 PS50014; BROMODOMAIN_2
 PS50827; DDT
 PS51136; WAC
 PS01359; ZF_PHD_1
 PS50016; ZF_PHD_2 
PRINTS
 PR00503; BROMODOMAIN.