RBBP7_PONAB
ID RBBP7_PONAB Reviewed; 426 AA.
AC Q5R654;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Histone-binding protein RBBP7;
DE AltName: Full=Nucleosome-remodeling factor subunit RBAP46;
DE AltName: Full=Retinoblastoma-binding protein 7;
DE Short=RBBP-7;
GN Name=RBBP7;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Core histone-binding subunit that may target chromatin
CC remodeling factors, histone acetyltransferases 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 type B histone
CC acetyltransferase (HAT) complex, which is required for chromatin
CC assembly following DNA replication; 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; and the
CC PRC2/EED-EZH2 complex, which promotes repression of homeotic genes
CC during development; and the NURF (nucleosome remodeling factor) complex
CC (By similarity). {ECO:0000250|UniProtKB:Q16576,
CC ECO:0000250|UniProtKB:Q60973}.
CC -!- SUBUNIT: Binds directly to helix 1 of the histone fold of histone H4, a
CC region that is not accessible when H4 is in chromatin. Subunit of the
CC type B histone acetyltransferase (HAT) complex, composed of RBBP7 and
CC HAT1. Subunit of the core histone deacetylase (HDAC) complex, which is
CC composed of HDAC1, HDAC2, RBBP4 and RBBP7. The core HDAC complex
CC associates with SIN3A, ARID4B/SAP180, SAP18, SAP30, SAP130, SUDS3/SAP45
CC and possibly ARID4A/RBP1 and ING1 to form the SIN3 HDAC complex. The
CC core HDAC complex may also associate with MTA2, MBD3, CHD3 and CHD4 to
CC form the nucleosome remodeling and histone deacetylase complex (the
CC NuRD complex). The NuRD complex may also interact with MBD3L1 and
CC MBD3L2. Interacts with MTA1. Subunit of the PRC2/EED-EZH2 complex,
CC which is composed of at least EED, EZH2, RBBP4, RBBP7 and SUZ12. The
CC PRC2/EED-EZH2 complex may also associate with HDAC1. Component of the
CC NURF-1 ISWI chromatin remodeling complex (also called the nucleosome-
CC remodeling factor (NURF) complex) at least composed of SMARCA1; BPTF;
CC RBBP4 and RBBP7 (By similarity). Within the complex interacts with
CC SMARCA1 (By similarity). Interacts with the viral protein-binding
CC domain of the retinoblastoma protein (RB1). Interacts with CREBBP, and
CC this interaction may be enhanced by the binding of phosphorylated CREB1
CC to CREBBP. Interacts with CENPA. Interacts with BRCA1, HDAC7 and
CC SUV39H1 (By similarity). Interacts with PWWP2B (By similarity).
CC {ECO:0000250|UniProtKB:Q16576, ECO:0000250|UniProtKB:Q60973}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the WD repeat RBAP46/RBAP48/MSI1 family.
CC {ECO:0000305}.
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DR EMBL; CR860642; CAH92762.1; -; Transcribed_RNA.
DR AlphaFoldDB; Q5R654; -.
DR SMR; Q5R654; -.
DR STRING; 9601.ENSPPYP00000022548; -.
DR eggNOG; KOG0264; Eukaryota.
DR InParanoid; Q5R654; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0035098; C:ESC/E(Z) complex; ISS:UniProtKB.
DR GO; GO:0016581; C:NuRD complex; ISS:UniProtKB.
DR GO; GO:0070370; P:cellular heat acclimation; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
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; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 3: Inferred from homology;
KW Acetylation; Chaperone; Chromatin regulator; DNA replication;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation; Ubl conjugation;
KW WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q16576"
FT CHAIN 2..426
FT /note="Histone-binding protein RBBP7"
FT /id="PRO_0000223244"
FT REPEAT 47..122
FT /note="WD 1"
FT REPEAT 128..173
FT /note="WD 2"
FT REPEAT 181..217
FT /note="WD 3"
FT REPEAT 228..269
FT /note="WD 4"
FT REPEAT 275..312
FT /note="WD 5"
FT REPEAT 318..370
FT /note="WD 6"
FT REPEAT 377..404
FT /note="WD 7"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q16576"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16576"
FT MOD_RES 4
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q16576"
FT MOD_RES 10
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q16576"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16576"
FT MOD_RES 119
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q60973"
FT MOD_RES 159
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q60973"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16576"
FT CROSSLNK 4
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q16576"
FT CROSSLNK 4
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q16576"
FT CROSSLNK 101
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q16576"
FT CROSSLNK 155
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q16576"
FT CROSSLNK 159
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q16576"
SQ SEQUENCE 426 AA; 47865 MW; F5EED881F1460C69 CRC64;
MASKEMFEDT VEERVINEEY KIWKKNTPFL YDLVMTHALQ WPSLTVQWLP EVTKPEGKDY
ALHWLVLGTH TSDEQNHLVV ARVHIPNDDA QFDASHCDSD KGEFGGFGSV TGKIECEIKI
NHEGEVNRAR YMPQNPHIIA TKTPSSGVLV FDYTKHPAKP DPSGECNPDL RLRGHQKEGY
GLSWNSNLSG HLLSASDDHT VCLWDINAGP KEGKIVDAKA VFTGHSAVVE DVAWHLLHES
LFGSVADDQK LMMWDTRSNT TSKPSHLVDA HTAEVNCLSF NPYSEFILAT GSADKTVALW
DLRNLKLKLH TFESHKDEIF QVVHWSPHNE TILASSGTDR RLNVWDLSKI GEEQSAEDAE
DGPPELLFIH GGHTAKISDF SWNPNEPWVI CSVSEDNIMQ IWQMAENIYN DEESDVTTSE
LEGQGS
