RBBP4_DANRE
ID RBBP4_DANRE Reviewed; 424 AA.
AC Q6P3H7; Q6TLG5; Q7ZW28;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Histone-binding protein RBBP4;
DE AltName: Full=Retinoblastoma-binding protein 4;
DE Short=RBBP-4;
GN Name=rbbp4; Synonyms=rbb4;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney marrow;
RX PubMed=15520368; DOI=10.1073/pnas.0407241101;
RA Song H.-D., Sun X.-J., Deng M., Zhang G.-W., Zhou Y., Wu X.-Y., Sheng Y.,
RA Chen Y., Ruan Z., Jiang C.-L., Fan H.-Y., Zon L.I., Kanki J.P., Liu T.X.,
RA Look A.T., Chen Z.;
RT "Hematopoietic gene expression profile in zebrafish kidney marrow.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:16240-16245(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
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}.
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 {ECO:0000250|UniProtKB:O93377, ECO:0000250|UniProtKB:Q09028}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q09028}.
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; AY394940; AAQ94567.1; -; mRNA.
DR EMBL; BC045315; AAH45315.1; -; mRNA.
DR EMBL; BC063984; AAH63984.1; -; mRNA.
DR RefSeq; NP_997760.1; NM_212595.1.
DR AlphaFoldDB; Q6P3H7; -.
DR SMR; Q6P3H7; -.
DR STRING; 7955.ENSDARP00000112131; -.
DR PaxDb; Q6P3H7; -.
DR GeneID; 321726; -.
DR KEGG; dre:321726; -.
DR CTD; 5928; -.
DR ZFIN; ZDB-GENE-030131-445; rbbp4.
DR eggNOG; KOG0264; Eukaryota.
DR InParanoid; Q6P3H7; -.
DR OrthoDB; 831322at2759; -.
DR PhylomeDB; Q6P3H7; -.
DR Reactome; R-DRE-1538133; G0 and Early G1.
DR Reactome; R-DRE-212300; PRC2 methylates histones and DNA.
DR Reactome; R-DRE-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-DRE-3214815; HDACs deacetylate histones.
DR Reactome; R-DRE-3214841; PKMTs methylate histone lysines.
DR Reactome; R-DRE-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
DR Reactome; R-DRE-6804758; Regulation of TP53 Activity through Acetylation.
DR Reactome; R-DRE-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-DRE-8943724; Regulation of PTEN gene transcription.
DR Reactome; R-DRE-8953750; Transcriptional Regulation by E2F6.
DR PRO; PR:Q6P3H7; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
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:0016581; C:NuRD complex; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
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 GO; GO:0031101; P:fin regeneration; IGI:ZFIN.
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 2: Evidence at transcript 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..424
FT /note="Histone-binding protein RBBP4"
FT /id="PRO_0000051193"
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"
FT CONFLICT 191
FT /note="S -> R (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="H -> Q (in Ref. 2; AAH45315)"
FT /evidence="ECO:0000305"
FT CONFLICT 383
FT /note="N -> T (in Ref. 2; AAH45315)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 424 AA; 47651 MW; A7A5BBD6EC195820 CRC64;
MADKEAAFDD AVEERVINEE YKIWKKNTPF LYDLVMTHAL EWPSLTAQWL PDVTRPEGKD
FSVHRLVLGT HTSDEQNHLV IASVQLPNDD AQFDASHYDS EKGEFGGFGS VSGKIEIEIK
INHEGEVNRA RYMPQNPCII ATKTPTSDVL VFDYTKHPSK PDPSGECTPD LRLRGHQKEG
YGLSWNPNLR SCLLSASDDH TICLWDISTV PKEGKIVDAK TIFTGHTAVV EDVSWHLLHE
SLFGSVADDQ KLMIWDTRSN NTSKPSHAVD AHTAEVNCLS FNPYSEFILA TGSADKTVAL
WDLRNLKLKL HSFESHKDEI FQVQWSPHNE TILASSGTDR RLNVWDLSKI GEEQSPEDAE
DGPPELLFIH GGHTAKISDF SWNPNEPWVI CSVSEDNIMQ VWQMAENIYN DEDPEGAADT
EVQG
