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Protein

Dimethyladenosine transferase 2, mitochondrial

Gene

TFB2M

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

S-adenosyl-L-methionine-dependent methyltransferase which specifically dimethylates mitochondrial 12S rRNA at the conserved stem loop. Also required for basal transcription of mitochondrial DNA, probably via its interaction with POLRMT and TFAM. Stimulates transcription independently of the methyltransferase activity. Compared to TFB1M, it activates transcription of mitochondrial DNA more efficiently, while it has less methyltransferase activity.4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei75 – 751S-adenosyl-L-methionine; via amide nitrogenPROSITE-ProRule annotation
Binding sitei124 – 1241S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei150 – 1501S-adenosyl-L-methioninePROSITE-ProRule annotation

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. rRNA (adenine-N6,N6-)-dimethyltransferase activity Source: InterPro
  3. transcription cofactor activity Source: UniProtKB

GO - Biological processi

  1. gene expression Source: Reactome
  2. mitochondrion organization Source: Reactome
  3. organelle organization Source: Reactome
  4. positive regulation of transcription, DNA-templated Source: UniProtKB
  5. transcription from mitochondrial promoter Source: UniProtKB
  6. transcription initiation from mitochondrial promoter Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

rRNA processing, Transcription, Transcription regulation

Keywords - Ligandi

RNA-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

ReactomeiREACT_200608. Transcriptional activation of mitochondrial biogenesis.
REACT_367. Mitochondrial transcription initiation.

Names & Taxonomyi

Protein namesi
Recommended name:
Dimethyladenosine transferase 2, mitochondrial (EC:2.1.1.-)
Alternative name(s):
Hepatitis C virus NS5A-transactivated protein 5
Short name:
HCV NS5A-transactivated protein 5
Mitochondrial 12S rRNA dimethylase 2
Mitochondrial transcription factor B2
Short name:
h-mtTFB
Short name:
h-mtTFB2
Short name:
hTFB2M
Short name:
mtTFB2
S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase 2
Gene namesi
Name:TFB2M
Synonyms:NS5ATP5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:18559. TFB2M.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial matrix Source: UniProtKB
  2. mitochondrial nucleoid Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi105 – 1051G → A: Abolishes methyltransferase activity. 1 Publication

Organism-specific databases

PharmGKBiPA38348.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 1919MitochondrionSequence AnalysisAdd
BLAST
Chaini20 – 396377Dimethyladenosine transferase 2, mitochondrialPRO_0000273179Add
BLAST

Proteomic databases

MaxQBiQ9H5Q4.
PaxDbiQ9H5Q4.
PeptideAtlasiQ9H5Q4.
PRIDEiQ9H5Q4.

PTM databases

PhosphoSiteiQ9H5Q4.

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Inductioni

By the nuclear respiratory factors NRF1 and NRF2/GABPB2 and PGC-1 coactivators.1 Publication

Gene expression databases

BgeeiQ9H5Q4.
CleanExiHS_TFB2M.
ExpressionAtlasiQ9H5Q4. baseline and differential.
GenevestigatoriQ9H5Q4.

Organism-specific databases

HPAiHPA030265.

Interactioni

Subunit structurei

Interacts with mitochondrial RNA polymerase POLRMT. Interacts with TFAM.2 Publications

Protein-protein interaction databases

BioGridi122106. 7 interactions.
DIPiDIP-50540N.
IntActiQ9H5Q4. 2 interactions.
STRINGi9606.ENSP00000355471.

Structurei

3D structure databases

ProteinModelPortaliQ9H5Q4.
SMRiQ9H5Q4. Positions 94-136.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. rRNA adenine N(6)-methyltransferase family. KsgA subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0030.
GeneTreeiENSGT00510000048533.
HOGENOMiHOG000060174.
HOVERGENiHBG094037.
InParanoidiQ9H5Q4.
KOiK17653.
OMAiVIHCDFF.
OrthoDBiEOG7RNK0M.
PhylomeDBiQ9H5Q4.
TreeFamiTF325100.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR001737. KsgA/Erm.
IPR029063. SAM-dependent_MTases.
IPR016861. TFB2M.
[Graphical view]
PANTHERiPTHR11727. PTHR11727. 1 hit.
PfamiPF00398. RrnaAD. 1 hit.
[Graphical view]
PIRSFiPIRSF027833. MtTFB2. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51689. SAM_RNA_A_N6_MT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9H5Q4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWIPVVGLPR RLRLSALAGA GRFCILGSEA ATRKHLPARN HCGLSDSSPQ
60 70 80 90 100
LWPEPDFRNP PRKASKASLD FKRYVTDRRL AETLAQIYLG KPSRPPHLLL
110 120 130 140 150
ECNPGPGILT QALLEAGAKV VALESDKTFI PHLESLGKNL DGKLRVIHCD
160 170 180 190 200
FFKLDPRSGG VIKPPAMSSR GLFKNLGIEA VPWTADIPLK VVGMFPSRGE
210 220 230 240 250
KRALWKLAYD LYSCTSIYKF GRIEVNMFIG EKEFQKLMAD PGNPDLYHVL
260 270 280 290 300
SVIWQLACEI KVLHMEPWSS FDIYTRKGPL ENPKRRELLD QLQQKLYLIQ
310 320 330 340 350
MIPRQNLFTK NLTPMNYNIF FHLLKHCFGR RSATVIDHLR SLTPLDARDI
360 370 380 390
LMQIGKQEDE KVVNMHPQDF KTLFETIERS KDCAYKWLYD ETLEDR
Length:396
Mass (Da):45,349
Last modified:March 1, 2001 - v1
Checksum:iC13DC398974BB88F
GO

Sequence cautioni

The sequence BAB15441.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti200 – 2012EK → GR in BAB15441 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti48 – 481S → F.1 Publication
Corresponds to variant rs148620105 [ dbSNP | Ensembl ].
VAR_071249
Natural varianti64 – 641A → T.2 Publications
Corresponds to variant rs143880306 [ dbSNP | Ensembl ].
VAR_071250
Natural varianti156 – 1561P → L.
Corresponds to variant rs11585481 [ dbSNP | Ensembl ].
VAR_030097
Natural varianti264 – 2641H → Y.1 Publication
Corresponds to variant rs12037377 [ dbSNP | Ensembl ].
VAR_030098

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF529366 mRNA. Translation: AAQ09600.1.
AK026314 mRNA. Translation: BAB15441.1. Different initiation.
AK026835 mRNA. Translation: BAB15566.1.
AL356583 Genomic DNA. Translation: CAI16399.1.
BC003383 mRNA. Translation: AAH03383.1.
CCDSiCCDS1627.1.
RefSeqiNP_071761.1. NM_022366.2.
UniGeneiHs.7395.

Genome annotation databases

EnsembliENST00000366514; ENSP00000355471; ENSG00000162851.
GeneIDi64216.
KEGGihsa:64216.
UCSCiuc001ibn.3. human.

Polymorphism databases

DMDMi74752681.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF529366 mRNA. Translation: AAQ09600.1.
AK026314 mRNA. Translation: BAB15441.1. Different initiation.
AK026835 mRNA. Translation: BAB15566.1.
AL356583 Genomic DNA. Translation: CAI16399.1.
BC003383 mRNA. Translation: AAH03383.1.
CCDSiCCDS1627.1.
RefSeqiNP_071761.1. NM_022366.2.
UniGeneiHs.7395.

3D structure databases

ProteinModelPortaliQ9H5Q4.
SMRiQ9H5Q4. Positions 94-136.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122106. 7 interactions.
DIPiDIP-50540N.
IntActiQ9H5Q4. 2 interactions.
STRINGi9606.ENSP00000355471.

PTM databases

PhosphoSiteiQ9H5Q4.

Polymorphism databases

DMDMi74752681.

Proteomic databases

MaxQBiQ9H5Q4.
PaxDbiQ9H5Q4.
PeptideAtlasiQ9H5Q4.
PRIDEiQ9H5Q4.

Protocols and materials databases

DNASUi64216.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000366514; ENSP00000355471; ENSG00000162851.
GeneIDi64216.
KEGGihsa:64216.
UCSCiuc001ibn.3. human.

Organism-specific databases

CTDi64216.
GeneCardsiGC01M246703.
HGNCiHGNC:18559. TFB2M.
HPAiHPA030265.
MIMi607055. gene.
neXtProtiNX_Q9H5Q4.
PharmGKBiPA38348.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0030.
GeneTreeiENSGT00510000048533.
HOGENOMiHOG000060174.
HOVERGENiHBG094037.
InParanoidiQ9H5Q4.
KOiK17653.
OMAiVIHCDFF.
OrthoDBiEOG7RNK0M.
PhylomeDBiQ9H5Q4.
TreeFamiTF325100.

Enzyme and pathway databases

ReactomeiREACT_200608. Transcriptional activation of mitochondrial biogenesis.
REACT_367. Mitochondrial transcription initiation.

Miscellaneous databases

GeneWikiiTFB2M.
GenomeRNAii64216.
NextBioi66127.
PROiQ9H5Q4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H5Q4.
CleanExiHS_TFB2M.
ExpressionAtlasiQ9H5Q4. baseline and differential.
GenevestigatoriQ9H5Q4.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR001737. KsgA/Erm.
IPR029063. SAM-dependent_MTases.
IPR016861. TFB2M.
[Graphical view]
PANTHERiPTHR11727. PTHR11727. 1 hit.
PfamiPF00398. RrnaAD. 1 hit.
[Graphical view]
PIRSFiPIRSF027833. MtTFB2. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51689. SAM_RNA_A_N6_MT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and identification of human gene 5 transactivated by hepatitis C virus NS5A protein."
    Liu Y., Cheng J., Wang G., Wang J., Zhang L., Chen J., Li L.
    Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung and Small intestine.
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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: Placenta.
  5. "Mitochondrial transcription factors B1 and B2 activate transcription of human mtDNA."
    Falkenberg M., Gaspari M., Rantanen A., Trifunovic A., Larsson N.-G., Gustafsson C.M.
    Nat. Genet. 31:289-294(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH POLRMT.
  6. "Human mitochondrial transcription factor B1 interacts with the C-terminal activation region of h-mtTFA and stimulates transcription independently of its RNA methyltransferase activity."
    McCulloch V., Shadel G.S.
    Mol. Cell. Biol. 23:5816-5824(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TFAM.
  7. "The mitochondrial RNA polymerase contributes critically to promoter specificity in mammalian cells."
    Gaspari M., Falkenberg M., Larsson N.-G., Gustafsson C.M.
    EMBO J. 23:4606-4614(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Control of mitochondrial transcription specificity factors (TFB1M and TFB2M) by nuclear respiratory factors (NRF-1 and NRF-2) and PGC-1 family coactivators."
    Gleyzer N., Vercauteren K., Scarpulla R.C.
    Mol. Cell. Biol. 25:1354-1366(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  9. "Evidence for an early gene duplication event in the evolution of the mitochondrial transcription factor B family and maintenance of rRNA methyltransferase activity in human mtTFB1 and mtTFB2."
    Cotney J., Shadel G.S.
    J. Mol. Evol. 63:707-717(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME ACTIVITY, MUTAGENESIS OF GLY-105.
  10. "Human mitochondrial transcription revisited: only TFAM and TFB2M are required for transcription of the mitochondrial genes in vitro."
    Litonin D., Sologub M., Shi Y., Savkina M., Anikin M., Falkenberg M., Gustafsson C.M., Temiakov D.
    J. Biol. Chem. 285:18129-18133(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Mitochondrial transcription factors TFA, TFB1 and TFB2: a search for DNA variants/haplotypes and the risk of cardiac hypertrophy."
    Alonso-Montes C., Castro M.G., Reguero J.R., Perrot A., Ozcelik C., Geier C., Posch M.G., Moris C., Alvarez V., Ruiz-Ortega M., Coto E.
    Dis. Markers 25:131-139(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS THR-64 AND TYR-264.
  13. "Mutational screening of the mitochondrial transcription factors B1 and B2 (TFB1M and TFB2M) in Parkinson's disease."
    Sanchez-Ferrero E., Coto E., Blazquez M., Ribacoba R., Guisasola L.M., Salvador C., Alvarez V.
    Parkinsonism Relat. Disord. 15:468-470(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS PHE-48 AND THR-64.

Entry informationi

Entry nameiTFB2M_HUMAN
AccessioniPrimary (citable) accession number: Q9H5Q4
Secondary accession number(s): Q9H626
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: March 1, 2001
Last modified: March 4, 2015
This is version 122 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.