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UniProtKB - Q60972 (RBBP4_MOUSE)

Entry version 195 (02 Jun 2021)
Sequence version 5 (27 Jul 2011)
Previous versions | rss
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Protein

Histone-binding protein RBBP4

Gene

Rbbp4

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Core histone-binding subunit that may target chromatin assembly factors, chromatin remodeling factors 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 chromatin assembly factor 1 (CAF-1) complex, which is required for chromatin assembly following DNA replication and DNA repair; 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; the PRC2 complex, which promotes repression of homeotic genes during development; and the NURF (nucleosome remodeling factor) complex.

By similarity

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionChromatin regulator, Repressor
Biological processCell cycle, DNA replication, Transcription, Transcription regulation

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-MMU-1538133, G0 and Early G1
R-MMU-212300, PRC2 methylates histones and DNA
R-MMU-2559580, Oxidative Stress Induced Senescence
R-MMU-3214815, HDACs deacetylate histones
R-MMU-3214841, PKMTs methylate histone lysines
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-8953750, Transcriptional Regulation by E2F6

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Histone-binding protein RBBP4
Alternative name(s):
Chromatin assembly factor 1 subunit C
Short name:
CAF-1 subunit C
Chromatin assembly factor I p48 subunit
Short name:
CAF-I 48 kDa subunit
Short name:
CAF-I p48
Nucleosome-remodeling factor subunit RBAP48
Retinoblastoma-binding protein 4
Short name:
RBBP-4
Retinoblastoma-binding protein p48
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Rbbp4
Synonyms:Rbap48
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 4

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...MGIi		MGI:1194912, Rbbp4

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Nucleus

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000511872 – 425Histone-binding protein RBBP4Add BLAST424

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylalanineCombined sources1
Modified residuei4N6-acetyllysine; alternateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>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 residuei110PhosphoserineBy similarity1
Modified residuei160N6-acetyllysine; alternateCombined sources1
Cross-linki160Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei355PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		Q60972

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q60972

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q60972

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		Q60972

PeptideAtlas

More...PeptideAtlasi		Q60972

PRoteomics IDEntifications database

More...PRIDEi		Q60972

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		253176

2D gel databases

REPRODUCTION-2DPAGE

More...REPRODUCTION-2DPAGEi		Q60972

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q60972

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		Q60972

SwissPalm database of S-palmitoylation events

More...SwissPalmi		Q60972

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>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

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSMUSG00000057236, Expressed in cumulus cell and 323 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q60972, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q60972, MM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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 chromatin assembly factor 1 (CAF-1) complex, which is composed of RBBP4, CHAF1B and CHAF1A (By similarity). Subunit of the core histone deacetylase (HDAC) complex, which is composed of HDAC1, HDAC2, RBBP4 and RBBP7 (By similarity). 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 (Probable). 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) (By similarity). The NuRD complex may also interact with MBD3L1 and MBD3L2 (By similarity).

Interacts with MTA1 (By similarity).

Component of the PRC2 complex, which consists of the core subunits EED, EZH1 or EZH2, SUZ12, and RBBP4, and various combinations of accessory subunits including AEBP2, JARID2, PHF19, MTF2 and EPOP (PubMed:19026780).

Forms a monomeric PRC2.2 (class 2) complex consisting of at least SUZ12, RBBP4, AEBP2 and JARID2 (By similarity).

Forms a dimeric PRC2.1 (class 1, PRC-PCL) complex consisting of at least SUZ12, RBBP4, and PHF19; PHF19 stabilizes the dimeric structure which enhances PRC2 interaction with chromatin (By similarity). Part of the nucleosome remodeling factor (NURF) complex which consists of SMARCA1; BPTF; RBBP4 and RBBP7 (PubMed:10866654).

Interacts with SUV39H1 and HDAC7 (PubMed:10984530, PubMed:11788710).

Interacts with the viral protein-binding domain of the retinoblastoma protein (RB1) (By similarity).

Interacts with SPEN/MINT (By similarity).

Interacts with BRCA1 (By similarity).

Interacts with CREBBP, and this interaction may be enhanced by the binding of phosphorylated CREB1 to CREBBP (By similarity).

Component of the DREAM complex (also named LINC complex) at least composed of E2F4, E2F5, LIN9, LIN37, LIN52, LIN54, MYBL1, MYBL2, RBL1, RBL2, RBBP4, TFDP1 and TFDP2 (By similarity). The complex exists in quiescent cells where it represses cell cycle-dependent genes (By similarity). It dissociates in S phase when LIN9, LIN37, LIN52 and LIN54 form a subcomplex that binds to MYBL2 (By similarity).

Interacts with PHF6 (By similarity).

Found in a complex composed of at least SINHCAF, SIN3A, HDAC1, SAP30, RBBP4, OGT and TET1 (PubMed:28554894).

Interacts with ERCC6 (By similarity).

By similarity1 Publication5 Publications

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		202816, 41 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-3441, SIN3A histone deacetylase complex, ES cell-specific variant
CPX-3443, SIN3A histone deacetylase complex
CPX-3444, SIN3B histone deacetylase complex
CPX-570, Chromatin assembly factor 1 complex
CPX-694, NuRF chromatin remodelling complex
CPX-953, MBD2/NuRD nucleosome remodeling and deacetylase complex
CPX-954, MBD3/NuRD nucleosome remodeling and deacetylase complex

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		Q60972

Database of interacting proteins

More...DIPi		DIP-32855N

Protein interaction database and analysis system

More...IntActi		Q60972, 20 interactors

Molecular INTeraction database

More...MINTi		Q60972

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000099658

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		Q60972, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		Q60972

Database of comparative protein structure models

More...ModBasei		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati122 – 155WD 1Add BLAST34
Repeati175 – 206WD 2Add BLAST32
Repeati225 – 256WD 3Add BLAST32
Repeati271 – 302WD 4Add BLAST32
Repeati315 – 346WD 5Add BLAST32
Repeati372 – 403WD 6Add BLAST32

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the WD repeat RBAP46/RBAP48/MSI1 family.Curated

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0264, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000153375

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_020445_3_1_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q60972

Identification of Orthologs from Complete Genome Data

More...OMAi		HLADFSW

Database of Orthologous Groups

More...OrthoDBi		831322at2759

TreeFam database of animal gene trees

More...TreeFami		TF106485

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.130.10.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View 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

Pfam protein domain database

More...Pfami		View protein in Pfam
PF12265, CAF1C_H4-bd, 1 hit
PF00400, WD40, 5 hits

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00320, GPROTEINBRPT

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00320, WD40, 6 hits

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF50978, SSF50978, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00678, WD_REPEATS_1, 3 hits
PS50082, WD_REPEATS_2, 5 hits
PS50294, WD_REPEATS_REGION, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

Q60972-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MADKEAAFDD AVEERVINEE YKIWKKNTPF LYDLVMTHAL EWPSLTAQWL 
        60         70         80         90        100
PDVTRPEGKD FSIHRLVLGT HTSDEQNHLV IASVQLPNDD AQFDASHYDS 
       110        120        130        140        150
EKGEFGGFGS VSGKIEIEIK INHEGEVNRA RYMPQNPCII ATKTPSSDVL 
       160        170        180        190        200
VFDYTKHPSK PDPSGECNPD LRLRGHQKEG YGLSWNPNLS GHLLSASDDH 
       210        220        230        240        250
TICLWDISAV PKEGKVVDAK TIFTGHTAVV EDVSWHLLHE SLFGSVADDQ 
       260        270        280        290        300
KLMIWDTRSN NTSKPSHSVD AHTAEVNCLS FNPYSEFILA TGSADKTVAL 
       310        320        330        340        350
WDLRNLKLKL HSFESHKDEI FQVQWSPHNE TILASSGTDR RLNVWDLSKI 
       360        370        380        390        400
GEEQSPEDAE DGPPELLFIH GGHTAKISDF SWNPNEPWVI CSVSEDNIMQ 
       410        420 
VWQMAENIYN DEDPEGSVDP EGQGS
Length:425
Mass (Da):47,656
Last modified:July 27, 2011 - v5
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iB71E2D55A444C360
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A8Y5E8A8Y5E8_MOUSE
Histone-binding protein RBBP4
Rbbp4
48Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAC52275 differs from that shown. Reason: Frameshift.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti213E → K in AAC52275 (PubMed:7503932).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
U35141 mRNA Translation: AAC52275.1 Frameshift.
AL607123 Genomic DNA No translation available.
CU234133 Genomic DNA No translation available.
CH466552 Genomic DNA Translation: EDL30202.1
BC138568 mRNA Translation: AAI38569.1
BC138570 mRNA Translation: AAI38571.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS18688.1

Protein sequence database of the Protein Information Resource

More...PIRi		I49366

NCBI Reference Sequences

More...RefSeqi		NP_033056.2, NM_009030.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSMUST00000102598; ENSMUSP00000099658; ENSMUSG00000057236

Database of genes from NCBI RefSeq genomes

More...GeneIDi		19646

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:19646

UCSC genome browser

More...UCSCi		uc008uwt.1, mouse

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U35141 mRNA Translation: AAC52275.1 Frameshift.
AL607123 Genomic DNA No translation available.
CU234133 Genomic DNA No translation available.
CH466552 Genomic DNA Translation: EDL30202.1
BC138568 mRNA Translation: AAI38569.1
BC138570 mRNA Translation: AAI38571.1
CCDSiCCDS18688.1
PIRiI49366
RefSeqiNP_033056.2, NM_009030.3

3D structure databases

SMRiQ60972
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi202816, 41 interactors
ComplexPortaliCPX-3441, SIN3A histone deacetylase complex, ES cell-specific variant
CPX-3443, SIN3A histone deacetylase complex
CPX-3444, SIN3B histone deacetylase complex
CPX-570, Chromatin assembly factor 1 complex
CPX-694, NuRF chromatin remodelling complex
CPX-953, MBD2/NuRD nucleosome remodeling and deacetylase complex
CPX-954, MBD3/NuRD nucleosome remodeling and deacetylase complex
CORUMiQ60972
DIPiDIP-32855N
IntActiQ60972, 20 interactors
MINTiQ60972
STRINGi10090.ENSMUSP00000099658

PTM databases

iPTMnetiQ60972
PhosphoSitePlusiQ60972
SwissPalmiQ60972

2D gel databases

REPRODUCTION-2DPAGEiQ60972

Proteomic databases

EPDiQ60972
jPOSTiQ60972
MaxQBiQ60972
PaxDbiQ60972
PeptideAtlasiQ60972
PRIDEiQ60972
ProteomicsDBi253176

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		19646

Genome annotation databases

EnsembliENSMUST00000102598; ENSMUSP00000099658; ENSMUSG00000057236
GeneIDi19646
KEGGimmu:19646
UCSCiuc008uwt.1, mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		5928
MGIiMGI:1194912, Rbbp4

Phylogenomic databases

eggNOGiKOG0264, Eukaryota
GeneTreeiENSGT00940000153375
HOGENOMiCLU_020445_3_1_1
InParanoidiQ60972
OMAiHLADFSW
OrthoDBi831322at2759
TreeFamiTF106485

Enzyme and pathway databases

ReactomeiR-MMU-1538133, G0 and Early G1
R-MMU-212300, PRC2 methylates histones and DNA
R-MMU-2559580, Oxidative Stress Induced Senescence
R-MMU-3214815, HDACs deacetylate histones
R-MMU-3214841, PKMTs methylate histone lysines
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-8953750, Transcriptional Regulation by E2F6

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		19646, 28 hits in 57 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		Rbbp4, mouse

Protein Ontology

More...PROi		PR:Q60972
RNActiQ60972, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSMUSG00000057236, Expressed in cumulus cell and 323 other tissues
ExpressionAtlasiQ60972, baseline and differential
GenevisibleiQ60972, MM

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

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiRBBP4_MOUSE
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q60972
Secondary accession number(s): A2A875
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: June 2, 2021
This is version 195 of the entry and version 5 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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
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