RBBP4_BOVIN
ID RBBP4_BOVIN Reviewed; 425 AA.
AC Q3MHL3; A5D9B1;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Histone-binding protein RBBP4;
DE AltName: Full=Nucleosome-remodeling factor subunit RBAP48;
DE AltName: Full=Retinoblastoma-binding protein 4;
DE Short=RBBP-4;
GN Name=RBBP4;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH HDAC1, AND
RP SUBCELLULAR LOCATION.
RX PubMed=8602529; DOI=10.1126/science.272.5260.408;
RA Taunton J., Hassig C.A., Schreiber S.L.;
RT "A mammalian histone deacetylase related to the yeast transcriptional
RT regulator Rpd3p.";
RL Science 272:408-411(1996).
CC -!- FUNCTION: Core histone-binding subunit that may target chromatin
CC assembly factors, chromatin remodeling factors and histone deacetylases
CC to their histone substrates in a manner that is regulated by
CC nucleosomal DNA. Component of several complexes which regulate
CC chromatin metabolism. These include the chromatin assembly factor 1
CC (CAF-1) complex, which is required for chromatin assembly following DNA
CC replication and DNA repair; the core histone deacetylase (HDAC)
CC complex, which promotes histone deacetylation and consequent
CC transcriptional repression; the nucleosome remodeling and histone
CC deacetylase complex (the NuRD complex), which promotes transcriptional
CC repression by histone deacetylation and nucleosome remodeling; the
CC PRC2/EED-EZH2 complex, which promotes repression of homeotic genes
CC during development; and the NURF (nucleosome remodeling factor)
CC complex. {ECO:0000250|UniProtKB:Q09028}.
CC -!- SUBUNIT: Interacts with SUV39H1 and HDAC7 (By similarity). Binds
CC directly to helix 1 of the histone fold of histone H4, a region that is
CC not accessible when H4 is in chromatin. Subunit of the chromatin
CC assembly factor 1 (CAF-1) complex, which is composed of RBBP4, CHAF1B
CC and CHAF1A. Subunit of the core histone deacetylase (HDAC) complex,
CC which is composed of HDAC1, HDAC2, RBBP4 and RBBP7. The core HDAC
CC complex associates with SIN3A, ARID4B/SAP180, SAP18, SAP30, SAP130,
CC SUDS3/SAP45 and possibly ARID4A/RBP1 and ING1 to form the SIN3 HDAC
CC complex. The core HDAC complex may also associate with MTA2, MBD3, CHD3
CC and CHD4 to form the nucleosome remodeling and histone deacetylase
CC complex (the NuRD complex). The NuRD complex may also interact with
CC MBD3L1 and MBD3L2. Interacts with MTA1. Component of the PRC2 complex,
CC which consists of the core subunits EED, EZH1 or EZH2, SUZ12, and
CC RBBP4, and various combinations of accessory subunits including AEBP2,
CC JARID2, PHF19, MTF2 and EPOP. Forms a monomeric PRC2.2 (class 2)
CC complex consisting of at least SUZ12, RBBP4, AEBP2 and JARID2. Forms a
CC dimeric PRC2.1 (class 1, PRC-PCL) complex consisting of at least SUZ12,
CC RBBP4, and PHF19; PHF19 stabilizes the dimeric structure which enhances
CC PRC2 interaction with chromatin. Component of the NURF-1 ISWI chromatin
CC remodeling complex (also called the nucleosome-remodeling factor (NURF)
CC complex) at least composed of SMARCA1; BPTF; RBBP4 and RBBP7 (By
CC similarity). Within the complex interacts with SMARCA1 (By similarity).
CC Interacts with the ISWI chromatin remodeling complex component SMARCA5;
CC the interaction is direct (By similarity). Interacts with the viral
CC protein-binding domain of the retinoblastoma protein (RB1). Interacts
CC with SPEN/MINT. Interacts with BRCA1. Interacts with CREBBP, and this
CC interaction may be enhanced by the binding of phosphorylated CREB1 to
CC CREBBP. Component of the DREAM complex (also named LINC complex) at
CC least composed of E2F4, E2F5, LIN9, LIN37, LIN52, LIN54, MYBL1, MYBL2,
CC RBL1, RBL2, RBBP4, TFDP1 and TFDP2. The complex exists in quiescent
CC cells where it represses cell cycle-dependent genes. It dissociates in
CC S phase when LIN9, LIN37, LIN52 and LIN54 form a subcomplex that binds
CC to MYBL2. Interacts with PHF6 (By similarity). Found in a complex
CC composed of at least SINHCAF, SIN3A, HDAC1, SAP30, RBBP4, OGT and TET1
CC (By similarity). Interacts with ERCC6 (By similarity). Interacts with
CC ZNF827; the interaction is direct and recruits RBBP4 to telomeres (By
CC similarity). Interacts with PWWP2B (By similarity).
CC {ECO:0000250|UniProtKB:Q09028, ECO:0000250|UniProtKB:Q60972}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8602529}. Chromosome,
CC telomere {ECO:0000250|UniProtKB:Q09028}. Note=Localizes to chromatin as
CC part of the PRC2 complex. {ECO:0000250|UniProtKB:Q09028}.
CC -!- SIMILARITY: Belongs to the WD repeat RBAP46/RBAP48/MSI1 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BT030530; ABQ12970.1; -; mRNA.
DR EMBL; BC105195; AAI05196.1; -; mRNA.
DR RefSeq; NP_001070481.1; NM_001077013.2.
DR AlphaFoldDB; Q3MHL3; -.
DR SMR; Q3MHL3; -.
DR IntAct; Q3MHL3; 1.
DR MINT; Q3MHL3; -.
DR STRING; 9913.ENSBTAP00000007758; -.
DR PaxDb; Q3MHL3; -.
DR PeptideAtlas; Q3MHL3; -.
DR PRIDE; Q3MHL3; -.
DR Ensembl; ENSBTAT00000007758; ENSBTAP00000007758; ENSBTAG00000005904.
DR GeneID; 767940; -.
DR KEGG; bta:767940; -.
DR CTD; 5928; -.
DR VEuPathDB; HostDB:ENSBTAG00000005904; -.
DR VGNC; VGNC:33770; RBBP4.
DR eggNOG; KOG0264; Eukaryota.
DR GeneTree; ENSGT00940000153375; -.
DR HOGENOM; CLU_020445_3_1_1; -.
DR InParanoid; Q3MHL3; -.
DR OMA; PHEEGCL; -.
DR OrthoDB; 831322at2759; -.
DR TreeFam; TF106485; -.
DR Reactome; R-BTA-212300; PRC2 methylates histones and DNA.
DR Reactome; R-BTA-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-BTA-3214815; HDACs deacetylate histones.
DR Reactome; R-BTA-3214841; PKMTs methylate histone lysines.
DR Reactome; R-BTA-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
DR Reactome; R-BTA-8943724; Regulation of PTEN gene transcription.
DR Proteomes; UP000009136; Chromosome 2.
DR Bgee; ENSBTAG00000005904; Expressed in spermatocyte and 105 other tissues.
DR GO; GO:0033186; C:CAF-1 complex; ISS:UniProtKB.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0035098; C:ESC/E(Z) complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016581; C:NuRD complex; IBA:GO_Central.
DR GO; GO:0016589; C:NURF complex; IEA:Ensembl.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IEA:Ensembl.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0031497; P:chromatin assembly; ISS:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0006335; P:DNA replication-dependent chromatin assembly; IEA:Ensembl.
DR GO; GO:0006336; P:DNA replication-independent chromatin assembly; IEA:Ensembl.
DR GO; GO:0016575; P:histone deacetylation; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR022052; Histone-bd_RBBP4_N.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF12265; CAF1C_H4-bd; 1.
DR Pfam; PF00400; WD40; 5.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 3.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell cycle; Chromatin regulator; Chromosome; DNA replication;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; Telomere; Transcription; Transcription regulation;
KW Ubl conjugation; WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q09028"
FT CHAIN 2..425
FT /note="Histone-binding protein RBBP4"
FT /id="PRO_0000051185"
FT REPEAT 122..155
FT /note="WD 1"
FT REPEAT 175..206
FT /note="WD 2"
FT REPEAT 225..256
FT /note="WD 3"
FT REPEAT 271..302
FT /note="WD 4"
FT REPEAT 315..346
FT /note="WD 5"
FT REPEAT 372..403
FT /note="WD 6"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q09028"
FT MOD_RES 4
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q09028"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q09028"
FT MOD_RES 160
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q60972"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q09028"
FT CROSSLNK 4
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q09028"
FT CROSSLNK 4
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q09028"
FT CROSSLNK 160
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q09028"
SQ 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
