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Protein

Histone-binding protein RBBP7

Gene

RBBP7

Organism
Homo sapiens (Human)
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.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Chromatin regulator, Repressor

Keywords - Biological processi

DNA replication, Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciZFISH:ENSG00000102054-MONOMER.
ReactomeiR-HSA-212300. PRC2 methylates histones and DNA.
R-HSA-2559580. Oxidative Stress Induced Senescence.
R-HSA-3214815. HDACs deacetylate histones.
R-HSA-3214841. PKMTs methylate histone lysines.
R-HSA-3214847. HATs acetylate histones.
R-HSA-3214858. RMTs methylate histone arginines.
R-HSA-427389. ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression.
R-HSA-5617472. Activation of anterior HOX genes in hindbrain development during early embryogenesis.
R-HSA-606279. Deposition of new CENPA-containing nucleosomes at the centromere.
R-HSA-6804758. Regulation of TP53 Activity through Acetylation.
R-HSA-73762. RNA Polymerase I Transcription Initiation.
SignaLinkiQ16576.

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:9890. RBBP7.

Subcellular locationi

GO - Cellular componenti

  • ESC/E(Z) complex Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • NuRD complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi5931.
OpenTargetsiENSG00000102054.
PharmGKBiPA34254.

Chemistry databases

ChEMBLiCHEMBL3301388.

Polymorphism and mutation databases

BioMutaiRBBP7.
DMDMi2494891.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00000511952 – 425Histone-binding protein RBBP7Add BLAST424
Isoform 2 (identifier: Q16576-2)
Initiator methionineiRemovedCombined sources

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Modified residuei3PhosphoserineCombined sources1
Modified residuei4N6-acetyllysine; alternateCombined sources1
Cross-linki4Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate
Modified residuei10PhosphothreonineCombined sources1
Modified residuei95PhosphoserineCombined sources1
Modified residuei119N6-acetyllysineBy similarity1
Modified residuei159N6-acetyllysine; alternateBy similarity1
Cross-linki159Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei354PhosphoserineCombined sources1
Isoform 2 (identifier: Q16576-2)
Modified residuei2N-acetylalanineCombined sources1
Modified residuei13PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ16576.
PaxDbiQ16576.
PeptideAtlasiQ16576.
PRIDEiQ16576.

PTM databases

iPTMnetiQ16576.
PhosphoSitePlusiQ16576.
SwissPalmiQ16576.

Miscellaneous databases

PMAP-CutDBQ16576.

Expressioni

Gene expression databases

BgeeiENSG00000102054.
CleanExiHS_RBBP7.
ExpressionAtlasiQ16576. baseline and differential.
GenevisibleiQ16576. HS.

Organism-specific databases

HPAiCAB037084.
HPA060724.

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 (PubMed:12435631). 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) (PubMed:7503932, PubMed:10220405). Interacts with CREBBP, and this interaction may be enhanced by the binding of phosphorylated CREB1 to CREBBP. Interacts with BRCA1, HDAC7 and SUV39H1. Interacts with CENPA (PubMed:25556658).17 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DHX30Q7L2E34EBI-352227,EBI-1211456
HDAC1Q135477EBI-352227,EBI-301834
HIST2H4BP628054EBI-352227,EBI-302023
NR2E3Q9Y5X42EBI-352227,EBI-7216962
RBBP4Q090283EBI-352227,EBI-620823
SIN3AQ96ST32EBI-352227,EBI-347218
TBL3Q127882EBI-352227,EBI-715766

Protein-protein interaction databases

BioGridi111866. 163 interactors.
DIPiDIP-436N.
IntActiQ16576. 95 interactors.
MINTiMINT-90512.
STRINGi9606.ENSP00000369424.

Structurei

Secondary structure

1425
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi10 – 30Combined sources21
Beta strandi31 – 38Combined sources8
Beta strandi46 – 53Combined sources8
Beta strandi59 – 67Combined sources9
Beta strandi72 – 74Combined sources3
Beta strandi76 – 86Combined sources11
Beta strandi113 – 124Combined sources12
Beta strandi127 – 131Combined sources5
Beta strandi138 – 142Combined sources5
Beta strandi144 – 146Combined sources3
Beta strandi148 – 152Combined sources5
Helixi153 – 155Combined sources3
Beta strandi169 – 173Combined sources5
Beta strandi182 – 184Combined sources3
Beta strandi186 – 188Combined sources3
Beta strandi191 – 195Combined sources5
Beta strandi201 – 205Combined sources5
Beta strandi214 – 217Combined sources4
Beta strandi219 – 222Combined sources4
Beta strandi229 – 234Combined sources6
Beta strandi241 – 246Combined sources6
Beta strandi249 – 259Combined sources11
Beta strandi261 – 263Combined sources3
Beta strandi265 – 269Combined sources5
Beta strandi275 – 280Combined sources6
Beta strandi287 – 292Combined sources6
Beta strandi295 – 301Combined sources7
Beta strandi305 – 307Combined sources3
Beta strandi310 – 313Combined sources4
Beta strandi319 – 324Combined sources6
Beta strandi331 – 336Combined sources6
Beta strandi341 – 345Combined sources5
Helixi346 – 348Combined sources3
Helixi355 – 358Combined sources4
Beta strandi365 – 369Combined sources5
Beta strandi376 – 381Combined sources6
Beta strandi383 – 385Combined sources3
Beta strandi388 – 393Combined sources6
Beta strandi396 – 403Combined sources8
Helixi405 – 408Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3CFSX-ray2.40B1-411[»]
3CFVX-ray2.60A/B1-411[»]
ProteinModelPortaliQ16576.
SMRiQ16576.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ16576.

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

Contains 7 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiKOG0264. Eukaryota.
ENOG410XNU9. LUCA.
GeneTreeiENSGT00570000079069.
HOGENOMiHOG000160330.
HOVERGENiHBG053236.
InParanoidiQ16576.
KOiK11659.
OMAiPDIRINH.
OrthoDBiEOG091G0A20.
PhylomeDBiQ16576.
TreeFamiTF106485.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR020472. G-protein_beta_WD-40_rep.
IPR022052. Histone-bd_RBBP4_N.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF12265. CAF1C_H4-bd. 1 hit.
PF00400. WD40. 5 hits.
[Graphical view]
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM00320. WD40. 6 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 3 hits.
PS50082. WD_REPEATS_2. 5 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q16576-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« 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 EESDVTTSEL EGQGS
Length:425
Mass (Da):47,820
Last modified:November 1, 1997 - v1
Checksum:i1A4B4CD1A8E96815
GO
Isoform 2 (identifier: Q16576-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-6: MASKEM → MAAEAGVVGAGASPDGDWRDQACGLLLHVHLSSRLGRAAPVRTGRHLRTV

Note: No experimental confirmation available.Combined sources
Show »
Length:469
Mass (Da):52,314
Checksum:iD668D0B6D5715261
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0430161 – 6MASKEM → MAAEAGVVGAGASPDGDWRD QACGLLLHVHLSSRLGRAAP VRTGRHLRTV in isoform 2. 1 Publication6

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U35143 mRNA. Translation: AAC50231.1.
X72841 mRNA. Translation: CAA51360.1.
AK091911 mRNA. Translation: BAG52439.1.
AL929302 Genomic DNA. Translation: CAI41283.1.
CCDSiCCDS14179.1. [Q16576-1]
CCDS56598.1. [Q16576-2]
PIRiI39181.
RefSeqiNP_001185648.1. NM_001198719.1. [Q16576-2]
NP_002884.1. NM_002893.3. [Q16576-1]
UniGeneiHs.495755.

Genome annotation databases

EnsembliENST00000380084; ENSP00000369424; ENSG00000102054. [Q16576-2]
ENST00000380087; ENSP00000369427; ENSG00000102054. [Q16576-1]
GeneIDi5931.
KEGGihsa:5931.
UCSCiuc004cxs.3. human. [Q16576-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U35143 mRNA. Translation: AAC50231.1.
X72841 mRNA. Translation: CAA51360.1.
AK091911 mRNA. Translation: BAG52439.1.
AL929302 Genomic DNA. Translation: CAI41283.1.
CCDSiCCDS14179.1. [Q16576-1]
CCDS56598.1. [Q16576-2]
PIRiI39181.
RefSeqiNP_001185648.1. NM_001198719.1. [Q16576-2]
NP_002884.1. NM_002893.3. [Q16576-1]
UniGeneiHs.495755.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3CFSX-ray2.40B1-411[»]
3CFVX-ray2.60A/B1-411[»]
ProteinModelPortaliQ16576.
SMRiQ16576.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111866. 163 interactors.
DIPiDIP-436N.
IntActiQ16576. 95 interactors.
MINTiMINT-90512.
STRINGi9606.ENSP00000369424.

Chemistry databases

ChEMBLiCHEMBL3301388.

PTM databases

iPTMnetiQ16576.
PhosphoSitePlusiQ16576.
SwissPalmiQ16576.

Polymorphism and mutation databases

BioMutaiRBBP7.
DMDMi2494891.

Proteomic databases

EPDiQ16576.
PaxDbiQ16576.
PeptideAtlasiQ16576.
PRIDEiQ16576.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000380084; ENSP00000369424; ENSG00000102054. [Q16576-2]
ENST00000380087; ENSP00000369427; ENSG00000102054. [Q16576-1]
GeneIDi5931.
KEGGihsa:5931.
UCSCiuc004cxs.3. human. [Q16576-1]

Organism-specific databases

CTDi5931.
DisGeNETi5931.
GeneCardsiRBBP7.
HGNCiHGNC:9890. RBBP7.
HPAiCAB037084.
HPA060724.
MIMi300825. gene.
neXtProtiNX_Q16576.
OpenTargetsiENSG00000102054.
PharmGKBiPA34254.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0264. Eukaryota.
ENOG410XNU9. LUCA.
GeneTreeiENSGT00570000079069.
HOGENOMiHOG000160330.
HOVERGENiHBG053236.
InParanoidiQ16576.
KOiK11659.
OMAiPDIRINH.
OrthoDBiEOG091G0A20.
PhylomeDBiQ16576.
TreeFamiTF106485.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000102054-MONOMER.
ReactomeiR-HSA-212300. PRC2 methylates histones and DNA.
R-HSA-2559580. Oxidative Stress Induced Senescence.
R-HSA-3214815. HDACs deacetylate histones.
R-HSA-3214841. PKMTs methylate histone lysines.
R-HSA-3214847. HATs acetylate histones.
R-HSA-3214858. RMTs methylate histone arginines.
R-HSA-427389. ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression.
R-HSA-5617472. Activation of anterior HOX genes in hindbrain development during early embryogenesis.
R-HSA-606279. Deposition of new CENPA-containing nucleosomes at the centromere.
R-HSA-6804758. Regulation of TP53 Activity through Acetylation.
R-HSA-73762. RNA Polymerase I Transcription Initiation.
SignaLinkiQ16576.

Miscellaneous databases

ChiTaRSiRBBP7. human.
EvolutionaryTraceiQ16576.
GeneWikiiRBBP7.
GenomeRNAii5931.
PMAP-CutDBQ16576.
PROiQ16576.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000102054.
CleanExiHS_RBBP7.
ExpressionAtlasiQ16576. baseline and differential.
GenevisibleiQ16576. HS.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR020472. G-protein_beta_WD-40_rep.
IPR022052. Histone-bd_RBBP4_N.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF12265. CAF1C_H4-bd. 1 hit.
PF00400. WD40. 5 hits.
[Graphical view]
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM00320. WD40. 6 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 3 hits.
PS50082. WD_REPEATS_2. 5 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRBBP7_HUMAN
AccessioniPrimary (citable) accession number: Q16576
Secondary accession number(s): Q5JP00
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: November 30, 2016
This is version 170 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.