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Protein

Histone-binding protein RBBP7

Gene

Rbbp7

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Molecular functioni

  • RNA binding Source: MGI

GO - Biological processi

  • cellular heat acclimation Source: UniProtKB
  • chromatin remodeling Source: MGI
  • chromatin silencing at rDNA Source: Reactome
  • covalent chromatin modification Source: UniProtKB-KW
  • DNA replication Source: UniProtKB-KW
  • negative regulation of cell growth Source: UniProtKB
  • negative regulation of transcription, DNA-templated Source: MGI
  • negative regulation of transcription from RNA polymerase II promoter Source: MGI
  • response to steroid hormone Source: Ensembl
  • transcription, DNA-templated Source: UniProtKB-KW

Keywordsi

Molecular functionChaperone, Chromatin regulator, Repressor
Biological processDNA replication, Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiR-MMU-212300. PRC2 methylates histones and DNA.
R-MMU-2559580. Oxidative Stress Induced Senescence.
R-MMU-3214841. PKMTs methylate histone lysines.
R-MMU-3214847. HATs acetylate histones.
R-MMU-3214858. RMTs methylate histone arginines.
R-MMU-573389. NoRC negatively regulates rRNA expression.
R-MMU-606279. Deposition of new CENPA-containing nucleosomes at the centromere.
R-MMU-6804758. Regulation of TP53 Activity through Acetylation.
R-MMU-73762. RNA Polymerase I Transcription Initiation.
R-MMU-8943724. Regulation of PTEN gene transcription.
R-MMU-8951664. Neddylation.
R-MMU-8953750. Transcriptional Regulation by E2F6.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone-binding protein RBBP7
Alternative name(s):
Histone acetyltransferase type B subunit 2
Nucleosome-remodeling factor subunit RBAP46
Retinoblastoma-binding protein 7
Short name:
RBBP-7
Retinoblastoma-binding protein p46
Gene namesi
Name:Rbbp7
Synonyms:Rbap46
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:1194910. Rbbp7.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00000511962 – 425Histone-binding protein RBBP7Add BLAST424

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Modified residuei3PhosphoserineBy similarity1
Modified residuei4N6-acetyllysine; alternateCombined sources1
Cross-linki4Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Cross-linki4Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei10PhosphothreonineBy similarity1
Modified residuei95PhosphoserineBy similarity1
Cross-linki101Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei119N6-acetyllysineCombined sources1
Cross-linki155Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei159N6-acetyllysine; alternateCombined sources1
Cross-linki159Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei354PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ60973.
MaxQBiQ60973.
PaxDbiQ60973.
PeptideAtlasiQ60973.
PRIDEiQ60973.

2D gel databases

REPRODUCTION-2DPAGEiQ60973.

PTM databases

iPTMnetiQ60973.
PhosphoSitePlusiQ60973.

Expressioni

Tissue specificityi

Higher levels in brain, thymus, lung, spleen, kidney, testis, and ovary/uterus; lower levels in heart, liver, and muscle.1 Publication

Gene expression databases

BgeeiENSMUSG00000031353.
CleanExiMM_RBBP7.
ExpressionAtlasiQ60973. baseline and differential.
GenevisibleiQ60973. MM.

Interactioni

Subunit structurei

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.By similarity3 Publications

Protein-protein interaction databases

BioGridi232827. 20 interactors.
CORUMiQ60973.
DIPiDIP-32856N.
IntActiQ60973. 12 interactors.
MINTiMINT-1867543.
STRINGi10090.ENSMUSP00000033720.

Structurei

3D structure databases

ProteinModelPortaliQ60973.
SMRiQ60973.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati47 – 122WD 1Add BLAST76
Repeati128 – 173WD 2Add BLAST46
Repeati181 – 217WD 3Add BLAST37
Repeati228 – 269WD 4Add BLAST42
Repeati275 – 312WD 5Add BLAST38
Repeati318 – 369WD 6Add BLAST52
Repeati376 – 403WD 7Add BLAST28

Sequence similaritiesi

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiKOG0264. Eukaryota.
ENOG410XNU9. LUCA.
GeneTreeiENSGT00570000079069.
HOGENOMiHOG000160330.
HOVERGENiHBG053236.
InParanoidiQ60973.
KOiK11659.
OMAiVAWHVLH.
OrthoDBiEOG091G0A20.
PhylomeDBiQ60973.
TreeFamiTF106485.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiView protein in InterPro
IPR020472. G-protein_beta_WD-40_rep.
IPR022052. Histone-bd_RBBP4_N.
IPR015943. WD40/YVTN_repeat-like_dom_sf.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
IPR036322. WD40_repeat_dom_sf.
PfamiView protein in Pfam
PF12265. CAF1C_H4-bd. 1 hit.
PF00400. WD40. 5 hits.
PRINTSiPR00320. GPROTEINBRPT.
SMARTiView protein in SMART
SM00320. WD40. 6 hits.
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiView protein in PROSITE
PS00678. WD_REPEATS_1. 3 hits.
PS50082. WD_REPEATS_2. 5 hits.
PS50294. WD_REPEATS_REGION. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q60973-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASKEMFEDT VEERVINEEY KIWKKNTPFL YDLVMTHALQ WPSLTVQWLP
60 70 80 90 100
EVTKPEGKDY ALHWLVLGTH TSDEQNHLVV ARVHIPNDDA QFDASHCDSD
110 120 130 140 150
KGEFGGFGSV TGKIECEIKI NHEGEVNRAR YMPQNPHIIA TKTPSSDVLV
160 170 180 190 200
FDYTKHPAKP DPSGECNPDL RLRGHQKEGY GLSWNSNLSG HLLSASDDHT
210 220 230 240 250
VCLWDINAGP KEGKIVDAKA IFTGHSAVVE DVAWHLLHES LFGSVADDQK
260 270 280 290 300
LMIWDTRSNT TSKPSHLVDA HTAEVNCLSF NPYSEFILAT GSADKTVALW
310 320 330 340 350
DLRNLKLKLH TFESHKDEIF QVHWSPHNET ILASSGTDRR LNVWDLSKIG
360 370 380 390 400
EEQSAEDAED GPPELLFIHG GHTAKISDFS WNPNEPWVIC SVSEDNIMQI
410 420
WQMAENIYND EESDVTASEL EGQGS
Length:425
Mass (Da):47,790
Last modified:November 1, 1997 - v1
Checksum:i0A4A4CD1A8E96815
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U35142 mRNA. Translation: AAC52276.1.
AK076016 mRNA. Translation: BAC36122.1.
AK135779 mRNA. Translation: BAE22658.1.
AK135956 mRNA. Translation: BAE22743.1.
AK136110 mRNA. Translation: BAE22826.1.
AK145531 mRNA. Translation: BAE26487.1.
AK145651 mRNA. Translation: BAE26567.1.
AK146014 mRNA. Translation: BAE26833.1.
AK146904 mRNA. Translation: BAE27517.1.
AK146967 mRNA. Translation: BAE27573.1.
AK147062 mRNA. Translation: BAE27646.1.
AK148852 mRNA. Translation: BAE28678.1.
AK153913 mRNA. Translation: BAE32251.1.
AK160023 mRNA. Translation: BAE35566.1.
AL672123 Genomic DNA. Translation: CAM24314.1.
BC003785 mRNA. Translation: AAH03785.1.
CCDSiCCDS30509.1.
PIRiI49367.
RefSeqiNP_033057.3. NM_009031.3.
UniGeneiMm.270186.

Genome annotation databases

EnsembliENSMUST00000033720; ENSMUSP00000033720; ENSMUSG00000031353.
GeneIDi245688.
KEGGimmu:245688.
UCSCiuc009uug.2. mouse.

Similar proteinsi

Entry informationi

Entry nameiRBBP7_MOUSE
AccessioniPrimary (citable) accession number: Q60973
Secondary accession number(s): A2AFJ0, Q3UX20
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: November 22, 2017
This is version 176 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families