CPLM-011669

Genbank Nucleotide ID

Histone-binding protein RBBP4

Protein Synonyms/Alias

Chromatin assembly factor 1 subunit C; CAF-1 subunit C; Chromatin assembly factor I p48 subunit; CAF-I 48 kDa subunit; CAF-I p48; Nucleosome-remodeling factor subunit RBAP48; Retinoblastoma-binding protein 4; RBBP-4; Retinoblastoma-binding protein p48

Homo sapiens (Human)

Position	Peptide	Type	References
4	****MADKEAAFDDA	acetylation	[1]
4	****MADKEAAFDDA	ubiquitination	[2, 3, 4, 5, 6]
22	RVINEEYKIWKKNTP	acetylation	[1]
22	RVINEEYKIWKKNTP	ubiquitination	[4, 5, 7, 8, 9]
25	NEEYKIWKKNTPFLY	ubiquitination	[5, 7]
143	NPCIIATKTPSSDVL	ubiquitination	[5, 10, 11]
156	VLVFDYTKHPSKPDP	ubiquitination	[5, 10, 11]
160	DYTKHPSKPDPSGEC	acetylation	[11]
160	DYTKHPSKPDPSGEC	ubiquitination	[4, 5, 10, 11]
215	SAVPKEGKVVDAKTI	acetylation	[11]
317	LHSFESHKDEIFQVQ	ubiquitination	[5]
349	LNVWDLSKIGEEQSP	ubiquitination	[5]

[1] 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]
[2] Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry.
Meierhofer D, Wang X, Huang L, Kaiser P.
J Proteome Res. 2008 Oct;7(10):4566-76. [PMID: 18781797]
[3] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
[4] 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]
[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] 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]
[7] 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]
[8] 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]
[9] 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]
[10] 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]
[11] 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

Core histone-binding subunit that may target chromatin assembly factors, chromatin remodeling factors and histone deacetylases to their histone substrates in a manner that is regulated by nucleosomal DNA. Component of several complexes which regulate chromatin metabolism. These include the chromatin assembly factor 1 (CAF-1) complex, which is required for chromatin assembly following DNA replication and DNA repair; the core histone deacetylase (HDAC) complex, which promotes histone deacetylation and consequent transcriptional repression; the nucleosome remodeling and histone deacetylase complex (the NuRD complex), which promotes transcriptional repression by histone deacetylation and nucleosome remodeling; the PRC2/EED-EZH2 complex, which promotes repression of homeotic genes during development; and the NURF (nucleosome remodeling factor) complex.

REPEAT 122 155 WD 1.
REPEAT 175 206 WD 2.
REPEAT 225 256 WD 3.
REPEAT 271 302 WD 4.
REPEAT 315 346 WD 5.
REPEAT 372 403 WD 6.
MOD_RES 2 2 N-acetylalanine.
MOD_RES 4 4 N6-acetyllysine; alternate.
MOD_RES 110 110 Phosphoserine.
CROSSLNK 4 4 Glycyl lysine isopeptide (Lys-Gly)

3D-structure; Acetylation; Alternative splicing; Cell cycle; Chromatin regulator; Complete proteome; Direct protein sequencing; DNA replication; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription; Transcription regulation; Ubl conjugation; WD repeat.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0033186; C:CAF-1 complex; IDA:UniProtKB.
GO:0035098; C:ESC/E(Z) complex; IDA:UniProtKB.
GO:0016581; C:NuRD complex; IDA:UniProtKB.
GO:0016589; C:NURF complex; IDA:UniProtKB.
GO:0016580; C:Sin3 complex; NAS:BHF-UCL.
GO:0042393; F:histone binding; NAS:BHF-UCL.
GO:0034080; P:CENP-A containing nucleosome assembly at centromere; TAS:Reactome.
GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
GO:0000278; P:mitotic cell cycle; TAS:Reactome.
GO:0008285; P:negative regulation of cell proliferation; TAS:ProtInc.
GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.

IPR020472; G-protein_beta_WD-40_rep.
IPR022052; Histone-bd_RBBP4.
IPR015943; WD40/YVTN_repeat-like_dom.
IPR001680; WD40_repeat.
IPR019775; WD40_repeat_CS.
IPR017986; WD40_repeat_dom.

PF12265; CAF1C_H4-bd
PF00400; WD40

PS00678; WD_REPEATS_1
PS50082; WD_REPEATS_2
PS50294; WD_REPEATS_REGION

PR00320; GPROTEINBRPT.