ID   RBP4B_XENLA             Reviewed;         425 AA.
AC   Q6INH0;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Histone-binding protein RBBP4-B;
DE   AltName: Full=Retinoblastoma-binding protein 4-B;
DE            Short=RBBP-4-B;
DE   AltName: Full=Retinoblastoma-binding protein p48-B;
GN   Name=rbbp4-b; Synonyms=rbap48-b;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   SUBCELLULAR LOCATION.
RX   PubMed=10454532; DOI=10.1128/mcb.19.9.5847;
RA   Vermaak D., Wade P.A., Jones P.L., Shi Y.-B., Wolffe A.P.;
RT   "Functional analysis of the SIN3-histone deacetylase RPD3-RbAp48-histone H4
RT   connection in the Xenopus oocyte.";
RL   Mol. Cell. Biol. 19:5847-5860(1999).
RN   [3]
RP   INTERACTION WITH HDAC1; HDAC2; NCOR1 AND SIN3A.
RX   PubMed=11254656; DOI=10.1074/jbc.c000879200;
RA   Jones P.L., Sachs L.M., Rouse N., Wade P.A., Shi Y.-B.;
RT   "Multiple N-CoR complexes contain distinct histone deacetylases.";
RL   J. Biol. Chem. 276:8807-8811(2001).
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. {ECO:0000250|UniProtKB:O93377}.
CC   -!- SUBUNIT: Component of the DREAM complex (By similarity). Binds directly
CC       to histone H4, probably via helix 1 of the histone fold, a region that
CC       is not accessible when histone H4 is in chromatin (By similarity).
CC       Probably forms a large corepressor complex that contains ncor1, sin3a,
CC       hdac1-A and/or hdac1-B, hdac2, rbbp4-A and/or rbbp4-B and possibly
CC       rbbp7 (PubMed:11254656). {ECO:0000250|UniProtKB:O93377,
CC       ECO:0000250|UniProtKB:Q09028, ECO:0000269|PubMed:11254656}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10454532}.
CC       Chromosome, telomere {ECO:0000250|UniProtKB:Q09028}.
CC   -!- SIMILARITY: Belongs to the WD repeat RBAP46/RBAP48/MSI1 family.
CC       {ECO:0000305}.
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DR   EMBL; BC072311; AAH72311.1; -; mRNA.
DR   RefSeq; NP_001085185.1; NM_001091716.1.
DR   AlphaFoldDB; Q6INH0; -.
DR   SMR; Q6INH0; -.
DR   DNASU; 432269; -.
DR   GeneID; 432269; -.
DR   KEGG; xla:432269; -.
DR   CTD; 432269; -.
DR   Xenbase; XB-GENE-6255728; rbbp4.S.
DR   OrthoDB; 831322at2759; -.
DR   Proteomes; UP000186698; Chromosome 2S.
DR   Bgee; 432269; Expressed in blastula and 19 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:0035098; C:ESC/E(Z) complex; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:HGNC-UCL.
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; ISS:HGNC-UCL.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
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   Nucleus; Reference proteome; Repeat; Repressor; Telomere; Transcription;
KW   Transcription regulation; WD repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..425
FT                   /note="Histone-binding protein RBBP4-B"
FT                   /id="PRO_0000051191"
FT   REPEAT          122..162
FT                   /note="WD 1"
FT   REPEAT          175..215
FT                   /note="WD 2"
FT   REPEAT          225..265
FT                   /note="WD 3"
FT   REPEAT          271..311
FT                   /note="WD 4"
FT   REPEAT          315..355
FT                   /note="WD 5"
FT   REPEAT          372..412
FT                   /note="WD 6"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   425 AA;  47639 MW;  50A6B79E0CD0D497 CRC64;
     MADKEAAFDD AVEERVINEE YKIWKKNTPF LYDLVMTHAL EWPSLTAQWL PDVTRPDGKD
     FSIHRLVLGT HTSDEQNHLV IASVQLPNDD AQFDASHYDS EKGEFGGFGS VSGKIEIEIK
     INHEGEVNRA RYMPQNPCII ATKTPSCDVL VFDYTKHPSK PDPSGECNPD LRLRGHQKEG
     YGLSWNPNLS GNLLSASDDH TICLWDISAV PKEGKVVDAK TIFTGHTAVV EDVSWHLLHE
     SLFGSVADDQ KLMIWDTRSN NTSKPSHSVD AHTAEVNCLS FNPYSEFILA TGSADKTVAL
     WDLRNLKLKL HSFESHKDEI FQVQWSPHNE TILASSGTDR RLNVWDLSKI GEEQSPEDAE
     DGPPELLFIH GGHTAKISDF SWNPNEPWVI CSVSEDNIMQ VWQMAENIYN DEDTEGSVDP
     EGQGS