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Histone-binding protein RBBP7 (Histone acetyltransferase type B subunit 2) (Nucleosome-remodeling factor subunit RBAP46) (Retinoblastoma-binding protein 7) (RBBP-7) (Retinoblastoma-binding protein p46)

 RBBP7_MOUSE             Reviewed;         425 AA.
Q60973; A2AFJ0; Q3UX20;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 1.
12-SEP-2018, entry version 185.
RecName: Full=Histone-binding protein RBBP7;
AltName: Full=Histone acetyltransferase type B subunit 2;
AltName: Full=Nucleosome-remodeling factor subunit RBAP46;
AltName: Full=Retinoblastoma-binding protein 7;
Short=RBBP-7;
AltName: Full=Retinoblastoma-binding protein p46;
Name=Rbbp7; Synonyms=Rbap46;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 7-32 AND 133-155, AND
TISSUE SPECIFICITY.
TISSUE=Embryo;
PubMed=7503932; DOI=10.1074/jbc.270.43.25507;
Qian Y.-W., Lee E.Y.-H.P.;
"Dual retinoblastoma-binding proteins with properties related to a
negative regulator of ras in yeast.";
J. Biol. Chem. 270:25507-25513(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD;
TISSUE=Egg, Heart, Kidney, Liver, Placenta, Sympathetic ganglion, and
Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
INTERACTION WITH SUV39H1.
PubMed=11788710; DOI=10.1093/nar/30.2.475;
Vaute O., Nicolas E., Vandel L., Trouche D.;
"Functional and physical interaction between the histone methyl
transferase Suv39H1 and histone deacetylases.";
Nucleic Acids Res. 30:475-481(2002).
[6]
INTERACTION WITH HDAC7.
PubMed=10984530; DOI=10.1073/pnas.97.19.10330;
Downes M., Ordentlich P., Kao H.-Y., Alvarez J.G.A., Evans R.M.;
"Identification of a nuclear domain with deacetylase activity.";
Proc. Natl. Acad. Sci. U.S.A. 97:10330-10335(2000).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and
Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[8]
IDENTIFICATION IN THE PRC2 COMPLEX.
PubMed=20144788; DOI=10.1016/j.stem.2009.12.014;
Walker E., Chang W.Y., Hunkapiller J., Cagney G., Garcha K.,
Torchia J., Krogan N.J., Reiter J.F., Stanford W.L.;
"Polycomb-like 2 associates with PRC2 and regulates transcriptional
networks during mouse embryonic stem cell self-renewal and
differentiation.";
Cell Stem Cell 6:153-166(2010).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2; LYS-4; LYS-119 AND
LYS-159, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
-!- 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}.
-!- 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 (By
similarity). Interacts with BRCA1, HDAC7 and SUV39H1.
{ECO:0000250|UniProtKB:Q16576, ECO:0000269|PubMed:10984530,
ECO:0000269|PubMed:11788710, ECO:0000269|PubMed:20144788}.
-!- SUBCELLULAR LOCATION: Nucleus.
-!- TISSUE SPECIFICITY: Higher levels in brain, thymus, lung, spleen,
kidney, testis, and ovary/uterus; lower levels in heart, liver,
and muscle. {ECO:0000269|PubMed:7503932}.
-!- SIMILARITY: Belongs to the WD repeat RBAP46/RBAP48/MSI1 family.
{ECO:0000305}.
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EMBL; U35142; AAC52276.1; -; mRNA.
EMBL; AK076016; BAC36122.1; -; mRNA.
EMBL; AK135779; BAE22658.1; -; mRNA.
EMBL; AK135956; BAE22743.1; -; mRNA.
EMBL; AK136110; BAE22826.1; -; mRNA.
EMBL; AK145531; BAE26487.1; -; mRNA.
EMBL; AK145651; BAE26567.1; -; mRNA.
EMBL; AK146014; BAE26833.1; -; mRNA.
EMBL; AK146904; BAE27517.1; -; mRNA.
EMBL; AK146967; BAE27573.1; -; mRNA.
EMBL; AK147062; BAE27646.1; -; mRNA.
EMBL; AK148852; BAE28678.1; -; mRNA.
EMBL; AK153913; BAE32251.1; -; mRNA.
EMBL; AK160023; BAE35566.1; -; mRNA.
EMBL; AL672123; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC003785; AAH03785.1; -; mRNA.
CCDS; CCDS30509.1; -.
PIR; I49367; I49367.
RefSeq; NP_033057.3; NM_009031.3.
UniGene; Mm.270186; -.
ProteinModelPortal; Q60973; -.
SMR; Q60973; -.
BioGrid; 232827; 22.
ComplexPortal; CPX-3441; SIN3A histone deacetylase complex, ES cell-specific variant.
ComplexPortal; CPX-3443; SIN3A histone deacetylase complex.
ComplexPortal; CPX-3444; SIN3B histone deacetylase complex.
ComplexPortal; CPX-694; NuRF chromatin remodelling complex.
ComplexPortal; CPX-953; MBD2/NuRD nucleosome remodeling and deacetylase complex.
ComplexPortal; CPX-954; MBD3/NuRD nucleosome remodeling and deacetylase complex.
CORUM; Q60973; -.
DIP; DIP-32856N; -.
IntAct; Q60973; 14.
MINT; Q60973; -.
STRING; 10090.ENSMUSP00000033720; -.
iPTMnet; Q60973; -.
PhosphoSitePlus; Q60973; -.
REPRODUCTION-2DPAGE; Q60973; -.
EPD; Q60973; -.
MaxQB; Q60973; -.
PaxDb; Q60973; -.
PeptideAtlas; Q60973; -.
PRIDE; Q60973; -.
Ensembl; ENSMUST00000033720; ENSMUSP00000033720; ENSMUSG00000031353.
GeneID; 245688; -.
KEGG; mmu:245688; -.
UCSC; uc009uug.2; mouse.
CTD; 5931; -.
MGI; MGI:1194910; Rbbp7.
eggNOG; KOG0264; Eukaryota.
eggNOG; ENOG410XNU9; LUCA.
GeneTree; ENSGT00570000079069; -.
HOGENOM; HOG000160330; -.
HOVERGEN; HBG053236; -.
InParanoid; Q60973; -.
KO; K11659; -.
OMA; WQMADNI; -.
OrthoDB; EOG091G0A20; -.
PhylomeDB; Q60973; -.
TreeFam; TF106485; -.
Reactome; R-MMU-212300; PRC2 methylates histones and DNA.
Reactome; R-MMU-2559580; Oxidative Stress Induced Senescence.
Reactome; R-MMU-3214815; HDACs deacetylate histones.
Reactome; R-MMU-3214841; PKMTs methylate histone lysines.
Reactome; R-MMU-3214847; HATs acetylate histones.
Reactome; R-MMU-3214858; RMTs methylate histone arginines.
Reactome; R-MMU-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
Reactome; R-MMU-6804758; Regulation of TP53 Activity through Acetylation.
Reactome; R-MMU-73762; RNA Polymerase I Transcription Initiation.
Reactome; R-MMU-8943724; Regulation of PTEN gene transcription.
Reactome; R-MMU-8951664; Neddylation.
Reactome; R-MMU-8953750; Transcriptional Regulation by E2F6.
ChiTaRS; Rbbp7; mouse.
PRO; PR:Q60973; -.
Proteomes; UP000000589; Chromosome X.
Bgee; ENSMUSG00000031353; Expressed in 309 organ(s), highest expression level in secondary oocyte.
CleanEx; MM_RBBP7; -.
ExpressionAtlas; Q60973; baseline and differential.
Genevisible; Q60973; MM.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0035098; C:ESC/E(Z) complex; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0016581; C:NuRD complex; IDA:MGI.
GO; GO:0003723; F:RNA binding; IPI:MGI.
GO; GO:0070370; P:cellular heat acclimation; ISS:UniProtKB.
GO; GO:0006338; P:chromatin remodeling; TAS:MGI.
GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0048545; P:response to steroid hormone; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
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.
1: Evidence at protein level;
Acetylation; Chaperone; Chromatin regulator; Complete proteome;
Direct protein sequencing; DNA replication; Isopeptide bond; Nucleus;
Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
Transcription regulation; Ubl conjugation; WD repeat.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:23806337}.
CHAIN 2 425 Histone-binding protein RBBP7.
/FTId=PRO_0000051196.
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:0000244|PubMed:23806337}.
MOD_RES 3 3 Phosphoserine.
{ECO:0000250|UniProtKB:Q16576}.
MOD_RES 4 4 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
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:0000244|PubMed:23806337}.
MOD_RES 159 159 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
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; 47790 MW; 0A4A4CD1A8E96815 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 EESDVTASEL
EGQGS


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EIAAB46626 CBF-A,CCAAT-binding transcription factor I subunit A,DBPB,DNA-binding protein B,EFI-A,Enhancer factor I subunit A,Homo sapiens,Human,NSEP1,Nuclease-sensitive element-binding protein 1,YB1,YB-1,Y-box t
EIAAB46625 CBF-A,CCAAT-binding transcription factor I subunit A,DBPB,DNA-binding protein B,EFI-A,Enhancer factor I subunit A,Mouse,Msy1,Msy-1,Mus musculus,Nsep1,Nuclease-sensitive element-binding protein 1,Yb1,Y
EIAAB46624 CBF-A,CCAAT-binding transcription factor I subunit A,DBPB,DNA-binding protein B,EFI-A,Enhancer factor I subunit A,Msy-1,Nsep1,Nuclease-sensitive element-binding protein 1,Rat,Rattus norvegicus,Yb1,YB-


 

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