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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
  • 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
Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Chromatin regulator, Repressor

Keywords - Biological processi

DNA 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-427413. NoRC negatively regulates rRNA expression.
R-MMU-5617472. Activation of anterior HOX genes in hindbrain development during early embryogenesis.
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.

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:1194910. Rbbp7.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 425424Histone-binding protein RBBP7PRO_0000051196Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei3 – 31PhosphoserineBy similarity
Modified residuei4 – 41N6-acetyllysine; alternateCombined sources
Cross-linki4 – 4Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei10 – 101PhosphothreonineBy similarity
Modified residuei95 – 951PhosphoserineBy similarity
Modified residuei119 – 1191N6-acetyllysineCombined sources
Modified residuei159 – 1591N6-acetyllysine; alternateCombined sources
Cross-linki159 – 159Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei354 – 3541PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ60973.
MaxQBiQ60973.
PaxDbiQ60973.
PeptideAtlasiQ60973.
PRIDEiQ60973.

2D gel databases

REPRODUCTION-2DPAGEQ60973.

PTM databases

iPTMnetiQ60973.
PhosphoSiteiQ60973.

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

BgeeiQ60973.
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 BRCA1, HDAC7 and SUV39H1.3 Publications

Protein-protein interaction databases

BioGridi232827. 20 interactions.
DIPiDIP-32856N.
IntActiQ60973. 11 interactions.
MINTiMINT-1867543.
STRINGi10090.ENSMUSP00000033720.

Structurei

3D structure databases

ProteinModelPortaliQ60973.
SMRiQ60973. Positions 1-410.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati47 – 12276WD 1Add
BLAST
Repeati128 – 17346WD 2Add
BLAST
Repeati181 – 21737WD 3Add
BLAST
Repeati228 – 26942WD 4Add
BLAST
Repeati275 – 31238WD 5Add
BLAST
Repeati318 – 36952WD 6Add
BLAST
Repeati376 – 40328WD 7Add
BLAST

Sequence similaritiesi

Contains 7 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiKOG0264. Eukaryota.
ENOG410XNU9. LUCA.
GeneTreeiENSGT00570000079069.
HOGENOMiHOG000160330.
HOVERGENiHBG053236.
InParanoidiQ60973.
KOiK11659.
OMAiPDIRINH.
OrthoDBiEOG70PBXB.
PhylomeDBiQ60973.
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]

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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliQ60973.
SMRiQ60973. Positions 1-410.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi232827. 20 interactions.
DIPiDIP-32856N.
IntActiQ60973. 11 interactions.
MINTiMINT-1867543.
STRINGi10090.ENSMUSP00000033720.

PTM databases

iPTMnetiQ60973.
PhosphoSiteiQ60973.

2D gel databases

REPRODUCTION-2DPAGEQ60973.

Proteomic databases

EPDiQ60973.
MaxQBiQ60973.
PaxDbiQ60973.
PeptideAtlasiQ60973.
PRIDEiQ60973.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi5931.
MGIiMGI:1194910. Rbbp7.

Phylogenomic databases

eggNOGiKOG0264. Eukaryota.
ENOG410XNU9. LUCA.
GeneTreeiENSGT00570000079069.
HOGENOMiHOG000160330.
HOVERGENiHBG053236.
InParanoidiQ60973.
KOiK11659.
OMAiPDIRINH.
OrthoDBiEOG70PBXB.
PhylomeDBiQ60973.
TreeFamiTF106485.

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-427413. NoRC negatively regulates rRNA expression.
R-MMU-5617472. Activation of anterior HOX genes in hindbrain development during early embryogenesis.
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.

Miscellaneous databases

ChiTaRSiRbbp7. mouse.
PROiQ60973.
SOURCEiSearch...

Gene expression databases

BgeeiQ60973.
CleanExiMM_RBBP7.
ExpressionAtlasiQ60973. baseline and differential.
GenevisibleiQ60973. MM.

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...

Publicationsi

« Hide 'large scale' publications
  1. "Dual retinoblastoma-binding proteins with properties related to a negative regulator of ras in yeast."
    Qian Y.-W., Lee E.Y.-H.P.
    J. Biol. Chem. 270:25507-25513(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 7-32 AND 133-155, TISSUE SPECIFICITY.
    Tissue: Embryo.
  2. "The transcriptional landscape of the mammalian genome."
    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.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Egg, Heart, Kidney, Liver, Placenta, Sympathetic ganglion and Thymus.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Mammary tumor.
  5. "Functional and physical interaction between the histone methyl transferase Suv39H1 and histone deacetylases."
    Vaute O., Nicolas E., Vandel L., Trouche D.
    Nucleic Acids Res. 30:475-481(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SUV39H1.
  6. Cited for: INTERACTION WITH HDAC7.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  8. "Polycomb-like 2 associates with PRC2 and regulates transcriptional networks during mouse embryonic stem cell self-renewal and differentiation."
    Walker E., Chang W.Y., Hunkapiller J., Cagney G., Garcha K., Torchia J., Krogan N.J., Reiter J.F., Stanford W.L.
    Cell Stem Cell 6:153-166(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE PRC2 COMPLEX.
  9. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    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.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2; LYS-4; LYS-119 AND LYS-159, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiRBBP7_MOUSE
AccessioniPrimary (citable) accession number: Q60973
Secondary accession number(s): A2AFJ0, Q3UX20
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: July 6, 2016
This is version 163 of the entry and version 1 of the sequence. [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

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.