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Histone-binding protein RBBP4 (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)

 RBBP4_MOUSE             Reviewed;         425 AA.
Q60972; A2A875;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 5.
20-JUN-2018, entry version 174.
RecName: Full=Histone-binding protein RBBP4;
AltName: Full=Chromatin assembly factor 1 subunit C;
Short=CAF-1 subunit C;
AltName: Full=Chromatin assembly factor I p48 subunit;
Short=CAF-I 48 kDa subunit;
Short=CAF-I p48;
AltName: Full=Nucleosome-remodeling factor subunit RBAP48;
AltName: Full=Retinoblastoma-binding protein 4;
Short=RBBP-4;
AltName: Full=Retinoblastoma-binding protein p48;
Name=Rbbp4; Synonyms=Rbap48;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
PubMed=7503932; DOI=10.1074/jbc.270.43.25507;
Qian Y.-W., Lee E.Y.-H.P.;
"Dual retinoblastoma-binding proteins with properties related to a
negative regulator of ras in yeast.";
J. Biol. Chem. 270:25507-25513(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
INTERACTION WITH SAP30.
PubMed=9702189; DOI=10.1016/S1097-2765(00)80111-2;
Laherty C.D., Billin A.N., Lavinsky R.M., Yochum G.S., Bush A.C.,
Sun J.-M., Mullen T.-M., Davie J.R., Rose D.W., Glass C.K.,
Rosenfeld M.G., Ayer D.E., Eisenman R.N.;
"SAP30, a component of the mSin3 corepressor complex involved in N-
CoR-mediated repression by specific transcription factors.";
Mol. Cell 2:33-42(1998).
[6]
INTERACTION WITH CREBBP.
PubMed=10866654; DOI=10.1128/MCB.20.14.4970-4978.2000;
Zhang Q., Vo N., Goodman R.H.;
"Histone binding protein RbAp48 interacts with a complex of CREB
binding protein and phosphorylated CREB.";
Mol. Cell. Biol. 20:4970-4978(2000).
[7]
INTERACTION WITH HDAC7.
PubMed=10984530; DOI=10.1073/pnas.97.19.10330;
Downes M., Ordentlich P., Kao H.-Y., Alvarez J.G.A., Evans R.M.;
"Identification of a nuclear domain with deacetylase activity.";
Proc. Natl. Acad. Sci. U.S.A. 97:10330-10335(2000).
[8]
INTERACTION WITH SUV39H1.
PubMed=11788710; DOI=10.1093/nar/30.2.475;
Vaute O., Nicolas E., Vandel L., Trouche D.;
"Functional and physical interaction between the histone methyl
transferase Suv39H1 and histone deacetylases.";
Nucleic Acids Res. 30:475-481(2002).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
Burlingame A.L.;
"Comprehensive identification of phosphorylation sites in postsynaptic
density preparations.";
Mol. Cell. Proteomics 5:914-922(2006).
[10]
IDENTIFICATION IN THE PRC2/EED-EZH1 COMPLEX.
PubMed=19026780; DOI=10.1016/j.molcel.2008.10.016;
Shen X., Liu Y., Hsu Y.-J., Fujiwara Y., Kim J., Mao X., Yuan G.-C.,
Orkin S.H.;
"EZH1 mediates methylation on histone H3 lysine 27 and complements
EZH2 in maintaining stem cell identity and executing pluripotency.";
Mol. Cell 32:491-502(2008).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-160, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[13]
IDENTIFICATION IN A COMPLEX WITH SIN3A; SINHCAF; HDAC1; SAP30; OGT AND
TET1.
PubMed=28554894; DOI=10.15252/embj.201696307;
Streubel G., Fitzpatrick D.J., Oliviero G., Scelfo A., Moran B.,
Das S., Munawar N., Watson A., Wynne K., Negri G.L., Dillon E.T.,
Jammula S., Hokamp K., O'Connor D.P., Pasini D., Cagney G.,
Bracken A.P.;
"Fam60a defines a variant Sin3a-Hdac complex in embryonic stem cells
required for self-renewal.";
EMBO J. 36:2216-2232(2017).
-!- FUNCTION: 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; and the PRC2/EED-EZH2
complex, which promotes repression of homeotic genes during
development; and the NURF (nucleosome remodeling factor) complex
(By similarity). {ECO:0000250}.
-!- SUBUNIT: Binds directly to helix 1 of the histone fold of histone
H4, a region that is not accessible when H4 is in chromatin.
Subunit of the chromatin assembly factor 1 (CAF-1) complex, which
is composed of RBBP4, CHAF1B and CHAF1A. Subunit of the core
histone deacetylase (HDAC) complex, which is composed of HDAC1,
HDAC2, RBBP4 and RBBP7. The core HDAC complex associates with
SIN3A, ARID4B/SAP180, SAP18, SAP30, SAP130, SUDS3/SAP45 and
possibly ARID4A/RBP1 and ING1 to form the SIN3 HDAC complex. The
core HDAC complex may also associate with MTA2, MBD3, CHD3 and
CHD4 to form the nucleosome remodeling and histone deacetylase
complex (the NuRD complex). The NuRD complex may also interact
with MBD3L1 and MBD3L2. Component of the PRC2/EED-EZH1 complex,
which includes EED, EZH1, SUZ12, RBBP4 and AEBP2. Interacts with
MTA1. Subunit of the PRC2/EED-EZH2 complex, which is composed of
at least EED, EZH2, RBBP4, RBBP7 and SUZ12. The PRC2/EED-EZH2
complex may also associate with HDAC1. Component of the PRC2/EED-
EZH1 complex, which includes EED, EZH1, SUZ12, RBBP4 and AEBP2.
Part of the nucleosome remodeling factor (NURF) complex which
consists of SMARCA1; BPTF; RBBP4 and RBBP7. Interacts with the
viral protein-binding domain of the retinoblastoma protein (RB1).
Interacts with SPEN/MINT. Interacts with BRCA1 (By similarity).
Interacts with CREBBP, and this interaction may be enhanced by the
binding of phosphorylated CREB1 to CREBBP. Interacts with SAP30,
SUV39H1 and HDAC7. Component of the DREAM complex (also named LINC
complex) at least composed of E2F4, E2F5, LIN9, LIN37, LIN52,
LIN54, MYBL1, MYBL2, RBL1, RBL2, RBBP4, TFDP1 and TFDP2. The
complex exists in quiescent cells where it represses cell cycle-
dependent genes. It dissociates in S phase when LIN9, LIN37, LIN52
and LIN54 form a subcomplex that binds to MYBL2. Found in a
complex composed of at least SINHCAF, SIN3A, HDAC1, SAP30, RBBP4,
OGT and TET1 (PubMed:28554894). {ECO:0000250|UniProtKB:Q09028,
ECO:0000269|PubMed:10866654, ECO:0000269|PubMed:10984530,
ECO:0000269|PubMed:11788710, ECO:0000269|PubMed:19026780,
ECO:0000269|PubMed:28554894, ECO:0000269|PubMed:9702189}.
-!- SUBCELLULAR LOCATION: Nucleus.
-!- TISSUE SPECIFICITY: Higher levels in brain, thymus, lung, spleen,
kidney, testis, and ovary/uterus; lower levels in heart, liver,
and muscle. {ECO:0000269|PubMed:7503932}.
-!- SIMILARITY: Belongs to the WD repeat RBAP46/RBAP48/MSI1 family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC52275.1; Type=Frameshift; Positions=425; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; U35141; AAC52275.1; ALT_FRAME; mRNA.
EMBL; AL607123; CAM22958.1; -; Genomic_DNA.
EMBL; CU234133; CAQ52144.1; -; Genomic_DNA.
EMBL; CH466552; EDL30202.1; -; Genomic_DNA.
EMBL; BC138568; AAI38569.1; -; mRNA.
EMBL; BC138570; AAI38571.1; -; mRNA.
CCDS; CCDS18688.1; -.
PIR; I49366; I49366.
RefSeq; NP_033056.2; NM_009030.3.
UniGene; Mm.12145; -.
ProteinModelPortal; Q60972; -.
SMR; Q60972; -.
BioGrid; 202816; 23.
ComplexPortal; CPX-570; Chromatin assembly factor 1 complex.
ComplexPortal; CPX-694; NuRF chromatin remodelling complex.
ComplexPortal; CPX-953; MBD2/NuRD nucleosome remodeling and deacetylase complex.
ComplexPortal; CPX-954; MBD3/NuRD nucleosome remodeling and deacetylase complex.
CORUM; Q60972; -.
DIP; DIP-32855N; -.
IntAct; Q60972; 20.
MINT; Q60972; -.
STRING; 10090.ENSMUSP00000099658; -.
iPTMnet; Q60972; -.
PhosphoSitePlus; Q60972; -.
SwissPalm; Q60972; -.
REPRODUCTION-2DPAGE; Q60972; -.
EPD; Q60972; -.
MaxQB; Q60972; -.
PaxDb; Q60972; -.
PeptideAtlas; Q60972; -.
PRIDE; Q60972; -.
Ensembl; ENSMUST00000102598; ENSMUSP00000099658; ENSMUSG00000057236.
GeneID; 19646; -.
KEGG; mmu:19646; -.
UCSC; uc008uwt.1; mouse.
CTD; 5928; -.
MGI; MGI:1194912; Rbbp4.
eggNOG; KOG0264; Eukaryota.
eggNOG; ENOG410XNU9; LUCA.
GeneTree; ENSGT00570000079069; -.
HOGENOM; HOG000160330; -.
HOVERGEN; HBG053236; -.
InParanoid; Q60972; -.
KO; K10752; -.
OMA; TNHLADF; -.
OrthoDB; EOG091G0A20; -.
TreeFam; TF106485; -.
Reactome; R-MMU-1538133; G0 and Early G1.
Reactome; R-MMU-212300; PRC2 methylates histones and DNA.
Reactome; R-MMU-2559580; Oxidative Stress Induced Senescence.
Reactome; R-MMU-3214841; PKMTs methylate histone lysines.
Reactome; R-MMU-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
Reactome; R-MMU-6804758; Regulation of TP53 Activity through Acetylation.
Reactome; R-MMU-73762; RNA Polymerase I Transcription Initiation.
Reactome; R-MMU-8943724; Regulation of PTEN gene transcription.
Reactome; R-MMU-8953750; Transcriptional Regulation by E2F6.
ChiTaRS; Rbbp4; mouse.
PRO; PR:Q60972; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000057236; -.
CleanEx; MM_RBBP4; -.
ExpressionAtlas; Q60972; baseline and differential.
Genevisible; Q60972; MM.
GO; GO:0033186; C:CAF-1 complex; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0035098; C:ESC/E(Z) complex; IDA:UniProtKB.
GO; GO:0000790; C:nuclear chromatin; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0016581; C:NuRD complex; IDA:MGI.
GO; GO:0016589; C:NURF complex; ISO:MGI.
GO; GO:0032991; C:protein-containing complex; ISO:MGI.
GO; GO:0008094; F:DNA-dependent ATPase activity; IEA:Ensembl.
GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0031497; P:chromatin assembly; ISS:UniProtKB.
GO; GO:0006338; P:chromatin remodeling; ISS:HGNC.
GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
GO; GO:0006335; P:DNA replication-dependent nucleosome assembly; ISO:MGI.
GO; GO:0006336; P:DNA replication-independent nucleosome assembly; ISO:MGI.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 2.130.10.10; -; 1.
InterPro; IPR020472; G-protein_beta_WD-40_rep.
InterPro; IPR022052; Histone-bd_RBBP4_N.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR019775; WD40_repeat_CS.
InterPro; IPR017986; WD40_repeat_dom.
InterPro; IPR036322; WD40_repeat_dom_sf.
Pfam; PF12265; CAF1C_H4-bd; 1.
Pfam; PF00400; WD40; 5.
PRINTS; PR00320; GPROTEINBRPT.
SMART; SM00320; WD40; 6.
SUPFAM; SSF50978; SSF50978; 1.
PROSITE; PS00678; WD_REPEATS_1; 3.
PROSITE; PS50082; WD_REPEATS_2; 5.
PROSITE; PS50294; WD_REPEATS_REGION; 1.
1: Evidence at protein level;
Acetylation; Cell cycle; Chromatin regulator; Complete proteome;
DNA replication; Isopeptide bond; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Repressor; Transcription;
Transcription regulation; Ubl conjugation; WD repeat.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:16452087}.
CHAIN 2 425 Histone-binding protein RBBP4.
/FTId=PRO_0000051187.
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.
{ECO:0000244|PubMed:16452087}.
MOD_RES 4 4 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q09028}.
MOD_RES 110 110 Phosphoserine.
{ECO:0000250|UniProtKB:Q09028}.
MOD_RES 160 160 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 355 355 Phosphoserine.
{ECO:0000250|UniProtKB:Q09028}.
CROSSLNK 4 4 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q09028}.
CROSSLNK 4 4 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate.
{ECO:0000250|UniProtKB:Q09028}.
CROSSLNK 160 160 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q09028}.
CONFLICT 213 213 E -> K (in Ref. 1; AAC52275).
{ECO:0000305}.
SEQUENCE 425 AA; 47656 MW; B71E2D55A444C360 CRC64;
MADKEAAFDD AVEERVINEE YKIWKKNTPF LYDLVMTHAL EWPSLTAQWL PDVTRPEGKD
FSIHRLVLGT HTSDEQNHLV IASVQLPNDD AQFDASHYDS EKGEFGGFGS VSGKIEIEIK
INHEGEVNRA RYMPQNPCII ATKTPSSDVL VFDYTKHPSK PDPSGECNPD LRLRGHQKEG
YGLSWNPNLS GHLLSASDDH TICLWDISAV PKEGKVVDAK TIFTGHTAVV EDVSWHLLHE
SLFGSVADDQ KLMIWDTRSN NTSKPSHSVD AHTAEVNCLS FNPYSEFILA TGSADKTVAL
WDLRNLKLKL HSFESHKDEI FQVQWSPHNE TILASSGTDR RLNVWDLSKI GEEQSPEDAE
DGPPELLFIH GGHTAKISDF SWNPNEPWVI CSVSEDNIMQ VWQMAENIYN DEDPEGSVDP
EGQGS


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