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Histone-binding protein RBBP7 (Nucleosome-remodeling factor subunit RBAP46) (Retinoblastoma-binding protein 7) (RBBP-7)

 RBBP7_MACFA             Reviewed;         425 AA.
Q4R304;
07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
19-JUL-2005, sequence version 1.
05-DEC-2018, entry version 78.
RecName: Full=Histone-binding protein RBBP7;
AltName: Full=Nucleosome-remodeling factor subunit RBAP46;
AltName: Full=Retinoblastoma-binding protein 7;
Short=RBBP-7;
Name=RBBP7; ORFNames=QtsA-20489;
Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
NCBI_TaxID=9541;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
International consortium for macaque cDNA sequencing and analysis;
"DNA sequences of macaque genes expressed in brain or testis and its
evolutionary implications.";
Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Core histone-binding subunit that may target chromatin
remodeling factors, histone acetyltransferases 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 type B histone
acetyltransferase (HAT) complex, which is required for chromatin
assembly following DNA replication; 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|UniProtKB:Q16576, ECO:0000250|UniProtKB:Q60973}.
-!- 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 type B histone acetyltransferase (HAT) complex,
composed of RBBP7 and HAT1. 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. 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. 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
CREBBP, and this interaction may be enhanced by the binding of
phosphorylated CREB1 to CREBBP. Interacts with CENPA. Interacts
with BRCA1, HDAC7 and SUV39H1. {ECO:0000250|UniProtKB:Q16576,
ECO:0000250|UniProtKB:Q60973}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
-!- SIMILARITY: Belongs to the WD repeat RBAP46/RBAP48/MSI1 family.
{ECO:0000305}.
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EMBL; AB179464; BAE02515.1; -; mRNA.
RefSeq; NP_001272165.1; NM_001285236.1.
UniGene; Mfa.1945; -.
ProteinModelPortal; Q4R304; -.
SMR; Q4R304; -.
PRIDE; Q4R304; -.
Ensembl; ENSMFAT00000010593; ENSMFAP00000036348; ENSMFAG00000034492.
GeneID; 101926122; -.
KEGG; mcf:101926122; -.
CTD; 5931; -.
GeneTree; ENSGT00940000154748; -.
HOVERGEN; HBG053236; -.
KO; K11659; -.
GO; GO:0035098; C:ESC/E(Z) complex; ISS:UniProtKB.
GO; GO:0016581; C:NuRD complex; ISS:UniProtKB.
GO; GO:0070370; P:cellular heat acclimation; ISS:UniProtKB.
GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
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.
2: Evidence at transcript level;
Acetylation; Chaperone; Chromatin regulator; DNA replication;
Isopeptide bond; Nucleus; Phosphoprotein; Repeat; Repressor;
Transcription; Transcription regulation; Ubl conjugation; WD repeat.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q16576}.
CHAIN 2 425 Histone-binding protein RBBP7.
/FTId=PRO_0000223243.
REPEAT 47 122 WD 1.
REPEAT 128 173 WD 2.
REPEAT 181 217 WD 3.
REPEAT 228 269 WD 4.
REPEAT 275 312 WD 5.
REPEAT 318 369 WD 6.
REPEAT 376 403 WD 7.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:Q16576}.
MOD_RES 3 3 Phosphoserine.
{ECO:0000250|UniProtKB:Q16576}.
MOD_RES 4 4 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q16576}.
MOD_RES 10 10 Phosphothreonine.
{ECO:0000250|UniProtKB:Q16576}.
MOD_RES 95 95 Phosphoserine.
{ECO:0000250|UniProtKB:Q16576}.
MOD_RES 119 119 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q60973}.
MOD_RES 159 159 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q60973}.
MOD_RES 354 354 Phosphoserine.
{ECO:0000250|UniProtKB:Q16576}.
CROSSLNK 4 4 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q16576}.
CROSSLNK 4 4 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate.
{ECO:0000250|UniProtKB:Q16576}.
CROSSLNK 101 101 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q16576}.
CROSSLNK 155 155 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q16576}.
CROSSLNK 159 159 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q16576}.
SEQUENCE 425 AA; 47820 MW; 1A4B4CD1A8E96815 CRC64;
MASKEMFEDT VEERVINEEY KIWKKNTPFL YDLVMTHALQ WPSLTVQWLP EVTKPEGKDY
ALHWLVLGTH TSDEQNHLVV ARVHIPNDDA QFDASHCDSD KGEFGGFGSV TGKIECEIKI
NHEGEVNRAR YMPQNPHIIA TKTPSSDVLV FDYTKHPAKP DPSGECNPDL RLRGHQKEGY
GLSWNSNLSG HLLSASDDHT VCLWDINAGP KEGKIVDAKA IFTGHSAVVE DVAWHLLHES
LFGSVADDQK LMIWDTRSNT TSKPSHLVDA HTAEVNCLSF NPYSEFILAT GSADKTVALW
DLRNLKLKLH TFESHKDEIF QVHWSPHNET ILASSGTDRR LNVWDLSKIG EEQSAEDAED
GPPELLFIHG GHTAKISDFS WNPNEPWVIC SVSEDNIMQI WQMAENIYND EESDVTTSEL
EGQGS


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