CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012000
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Chromatin assembly factor 1 subunit A 
Protein Synonyms/Alias
 CAF-1 subunit A; Chromatin assembly factor I p150 subunit; CAF-I 150 kDa subunit; CAF-I p150; hp150 
Gene Name
 CHAF1A 
Gene Synonyms/Alias
 CAF; CAF1P150 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
22AATAMDCKDRPAFPVubiquitination[1]
467TLAGSCGKFAPFEIKacetylation[2]
674EWDEFLAKGKRFRVLacetylation[3]
870QGTPISLKRKSAGSMubiquitination[1]
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] 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]
 [3] 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] 
Functional Description
 Core component of the CAF-1 complex, a complex thought to mediate chromatin assembly in DNA replication and DNA repair. Assembles histone octamers onto replicating DNA in vitro. CAF-1 performs the first step of the nucleosome assembly process, bringing newly synthesized histones H3 and H4 to replicating DNA; histones H2A/H2B can bind to this chromatin precursor subsequent to DNA replication to complete the histone octamer. CHAF1A binds to histones H3 and H4. It may play a role in heterochromatin maintenance in proliferating cells by bringing newly synthesized cbx proteins to heterochromatic DNA replication foci (By similarity). 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. 
Sequence Annotation
 REGION 1 314 Binds to CBX1 chromo shadow domain.
 REGION 1 49 Binds to PCNA.
 REGION 642 678 Necessary for homodimerization and
 REGION 660 956 Binds to p60.
 MOTIF 233 246 PxVxL motif.
 MOD_RES 65 65 Phosphoserine.
 MOD_RES 123 123 Phosphoserine.
 MOD_RES 138 138 Phosphoserine.
 MOD_RES 141 141 Phosphoserine.
 MOD_RES 143 143 Phosphoserine.
 MOD_RES 206 206 Phosphoserine.
 MOD_RES 224 224 Phosphoserine.
 MOD_RES 310 310 Phosphoserine.
 MOD_RES 722 722 Phosphothreonine.
 MOD_RES 772 772 Phosphoserine.
 MOD_RES 775 775 Phosphoserine.
 MOD_RES 865 865 Phosphothreonine.
 MOD_RES 873 873 Phosphoserine.
 MOD_RES 951 951 Phosphoserine.  
Keyword
 Alternative splicing; Cell cycle; Chaperone; Complete proteome; DNA damage; DNA repair; DNA replication; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 956 AA 
Protein Sequence
MLEELECGAP GARGAATAMD CKDRPAFPVK KLIQARLPFK RLNLVPKGKA DDMSDDQGTS 60
VQSKSPDLEA SLDTLENNCH VGSDIDFRPK LVNGKGPLDN FLRNRIETSI GQSTVIIDLT 120
EDSNEQPDSL VDHNKLNSEA SPSREAINGQ REDTGDQQGL LKAIQNDKLA FPGETLSDIP 180
CKTEEEGVGC GGAGRRGDSQ ECSPRSCPEL TSGPRMCPRK EQDSWSEAGG ILFKGKVPMV 240
VLQDILAVRP PQIKSLPATP QGKNMTPESE VLESFPEEDS VLSHSSLSSP SSTSSPEGPP 300
APPKQHSSTS PFPTSTPLRR ITKKFVKGST EKNKLRLQRD QERLGKQLKL RAEREEKEKL 360
KEEAKRAKEE AKKKKEEEKE LKEKERREKR EKDEKEKAEK QRLKEERRKE RQEALEAKLE 420
EKRKKEEEKR LREEEKRIKA EKAEITRFFQ KPKTPQAPKT LAGSCGKFAP FEIKEHMVLA 480
PRRRTAFHPD LCSQLDQLLQ QQSGEFSFLK DLKGRQPLRS GPTHVSTRNA DIFNSDVVIV 540
ERGKGDGVPE RRKFGRMKLL QFCENHRPAY WGTWNKKTAL IRARDPWAQD TKLLDYEVDS 600
DEEWEEEEPG ESLSHSEGDD DDDMGEDEDE DDGFFVPHGY LSEDEGVTEE CADPENHKVR 660
QKLKAKEWDE FLAKGKRFRV LQPVKIGCVW AADRDCAGDD LKVLQQFAAC FLETLPAQEE 720
QTPKASKRER RDEQILAQLL PLLHGNVNGS KVIIREFQEH CRRGLLSNHT GSPRSPSTTY 780
LHTPTPSEDA AIPSKSRLKR LISENSVYEK RPDFRMCWYV HPQVLQSFQQ EHLPVPCQWS 840
YVTSVPSAPK EDSGSVPSTG PSQGTPISLK RKSAGSMCIT QFMKKRRHDG QIGAEDMDGF 900
QADTEEEEEE EGDCMIVDVP DAAEVQAPCG AASGAGGGVG VDTGKATLTS SPLGAS 956 
Gene Ontology
 GO:0033186; C:CAF-1 complex; IDA:UniProtKB.
 GO:0071778; C:WINAC complex; IDA:BHF-UCL.
 GO:0003682; F:chromatin binding; TAS:ProtInc.
 GO:0051082; F:unfolded protein binding; TAS:ProtInc.
 GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
 GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
 GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
 GO:0006335; P:DNA replication-dependent nucleosome assembly; TAS:ProtInc.
 GO:0006461; P:protein complex assembly; TAS:ProtInc.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR021644; CAF-1_p150.
 IPR022043; CAF1A. 
Pfam
 PF11600; CAF-1_p150
 PF12253; CAF1A 
SMART
  
PROSITE
  
PRINTS