CPLM-012687

Genbank Nucleotide ID

Histone-binding protein RBBP7

Protein Synonyms/Alias

Histone acetyltransferase type B subunit 2; Nucleosome-remodeling factor subunit RBAP46; Retinoblastoma-binding protein 7; RBBP-7; Retinoblastoma-binding protein p46

Homo sapiens (Human)

Position	Peptide	Type	References
4	****MASKEMFEDTV	acetylation	[1]
4	****MASKEMFEDTV	ubiquitination	[2, 3, 4]
21	RVINEEYKIWKKNTP	ubiquitination	[5, 6]
101	ASHCDSDKGEFGGFG	acetylation	[7]
101	ASHCDSDKGEFGGFG	ubiquitination	[4, 7, 8]
119	GKIECEIKINHEGEV	acetylation	[9]
119	GKIECEIKINHEGEV	ubiquitination	[4]
142	NPHIIATKTPSSDVL	ubiquitination	[5, 10]
155	VLVFDYTKHPAKPDP	ubiquitination	[4]
159	DYTKHPAKPDPSGEC	ubiquitination	[4]
263	TRSNTTSKPSHLVDA	ubiquitination	[4]
316	LHTFESHKDEIFQVH	ubiquitination	[10]
348	LNVWDLSKIGEEQSA	ubiquitination	[4, 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] 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]
[4] 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]
[5] 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]
[6] 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]
[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]
[8] 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]
[9] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647]
[10] 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]

Functional Description

Core histone-binding subunit that may target chromatin remodeling factors, histone acetyltransferases 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 type B histone acetyltransferase (HAT) complex, which is required for chromatin assembly following DNA replication; 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; and the PRC2/EED-EZH2 complex, which promotes repression of homeotic genes during development; and the NURF (nucleosome remodeling factor) complex.

REPEAT 47 122 WD 1.
REPEAT 128 173 WD 2.
REPEAT 181 217 WD 3.
REPEAT 228 269 WD 4.
REPEAT 275 312 WD 5.
REPEAT 318 369 WD 6.
REPEAT 376 403 WD 7.
MOD_RES 2 2 N-acetylalanine.
MOD_RES 3 3 Phosphoserine.
MOD_RES 4 4 N6-acetyllysine; alternate.
MOD_RES 99 99 Phosphoserine (By similarity).
MOD_RES 354 354 Phosphoserine.
CROSSLNK 4 4 Glycyl lysine isopeptide (Lys-Gly)

3D-structure; Acetylation; Alternative splicing; Chaperone; 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:0035098; C:ESC/E(Z) complex; IDA:UniProtKB.
GO:0016581; C:NuRD complex; IDA:UniProtKB.
GO:0008283; P:cell proliferation; TAS:ProtInc.
GO:0070370; P:cellular heat acclimation; IDA:UniProtKB.
GO:0034080; P:CENP-A containing nucleosome assembly at centromere; TAS:Reactome.
GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
GO:0007275; P:multicellular organismal development; TAS:ProtInc.
GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB.
GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Compara.
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.