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Protein

Metal-response element-binding transcription factor 2

Gene

MTF2

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

Functioni

Polycomb group (PcG) that specifically binds histone H3 trimethylated at 'Lys-36' (H3K36me3) and recruits the PRC2 complex. Acts by binding to H3K36me3, a mark for transcriptional activation, and recruiting the PRC2 complex, leading to enhance PRC2 H3K27me3 methylation activity. Regulates the transcriptional networks during embryonic stem cell self-renewal and differentiation. Promotes recruitment of the PRC2 complex to the inactive X chromosome in differentiating XX ES cells and PRC2 recruitment to target genes in undifferentiated ES cells. Required to repress Hox genes by enhancing H3K27me3 methylation of the PRC2 complex. In some conditions may act as an inhibitor of PRC2 activity: able to activate the CDKN2A gene and promote cellular senescence by suppressing the catalytic activity of the PRC2 complex locally. Binds to the metal-regulating-element (MRE) of MT1A gene promoter (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri102 – 15756PHD-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri201 – 25555PHD-type 2PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • methylated histone binding Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-212300. PRC2 methylates histones and DNA.

Names & Taxonomyi

Protein namesi
Recommended name:
Metal-response element-binding transcription factor 2
Alternative name(s):
Metal regulatory transcription factor 2
Metal-response element DNA-binding protein M96
Polycomb-like protein 2
Short name:
hPCl2
Gene namesi
Name:MTF2
Synonyms:PCL2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:29535. MTF2.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA128394586.

Polymorphism and mutation databases

BioMutaiMTF2.
DMDMi317373393.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 593593Metal-response element-binding transcription factor 2PRO_0000059317Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei24 – 241PhosphothreonineCombined sources
Modified residuei452 – 4521PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9Y483.
MaxQBiQ9Y483.
PaxDbiQ9Y483.
PeptideAtlasiQ9Y483.
PRIDEiQ9Y483.

PTM databases

iPTMnetiQ9Y483.
PhosphoSiteiQ9Y483.

Expressioni

Gene expression databases

BgeeiQ9Y483.
CleanExiHS_MTF2.
ExpressionAtlasiQ9Y483. baseline and differential.
GenevisibleiQ9Y483. HS.

Interactioni

Subunit structurei

Associated component of the PRC2 complex.By similarity

GO - Molecular functioni

  • methylated histone binding Source: UniProtKB

Protein-protein interaction databases

BioGridi116499. 21 interactions.
IntActiQ9Y483. 14 interactions.
MINTiMINT-1186792.
STRINGi9606.ENSP00000359321.

Structurei

3D structure databases

ProteinModelPortaliQ9Y483.
SMRiQ9Y483. Positions 36-162, 202-253.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini44 – 10158TudorAdd
BLAST

Domaini

The Tudor domain recognizes and binds H3K36me3 (PubMed:23142980, PubMed:23228662).2 Publications

Sequence similaritiesi

Belongs to the Polycomblike family.Curated
Contains 2 PHD-type zinc fingers.PROSITE-ProRule annotation
Contains 1 Tudor domain.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri102 – 15756PHD-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri201 – 25555PHD-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG4323. Eukaryota.
ENOG410XQ6E. LUCA.
HOGENOMiHOG000010307.
HOVERGENiHBG004755.
InParanoidiQ9Y483.
KOiK11485.
OrthoDBiEOG73V6JJ.
PhylomeDBiQ9Y483.
TreeFamiTF106420.

Family and domain databases

Gene3Di3.30.40.10. 2 hits.
InterProiIPR025894. Mtf2_C_dom.
IPR002999. Tudor.
IPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF14061. Mtf2_C. 1 hit.
PF00628. PHD. 1 hit.
[Graphical view]
SMARTiSM00249. PHD. 2 hits.
SM00333. TUDOR. 1 hit.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 2 hits.
PROSITEiPS01359. ZF_PHD_1. 2 hits.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9Y483-1) [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
MRDSTGAGNS LVHKRSPLRR NQKTPTSLTK LSLQDGHKAK KPACKFEEGQ
60 70 80 90 100
DVLARWSDGL FYLGTIKKIN ILKQSCFIIF EDSSKSWVLW KDIQTGATGS
110 120 130 140 150
GEMVCTICQE EYSEAPNEMV ICDKCGQGYH QLCHTPHIDC SVIDSDEKWL
160 170 180 190 200
CRQCVFATTT KRGGALKKGP NAKALQVMKQ TLPYSVADLE WDAGHKTNVQ
210 220 230 240 250
QCYCYCGGPG DWYLKMLQCC KCKQWFHEAC VQCLQKPMLF GDRFYTFICS
260 270 280 290 300
VCSSGPEYLK RLPLQWVDIA HLCLYNLSVI HKKKYFDSEL ELMTYINENW
310 320 330 340 350
DRLHPGELAD TPKSERYEHV LEALNDYKTM FMSGKEIKKK KHLFGLRIRV
360 370 380 390 400
PPVPPNVAFK AEKEPEGTSH EFKIKGRKAS KPISDSREVS NGIEKKGKKK
410 420 430 440 450
SVGRPPGPYT RKMIQKTAEP LLDKESISEN PTLDLPCSIG RTEGTAHSSN
460 470 480 490 500
TSDVDFTGAS SAKETTSSSI SRHYGLSDSR KRTRTGRSWP AAIPHLRRRR
510 520 530 540 550
GRLPRRALQT QNSEIVKDDE GKEDYQFDEL NTEILNNLAD QELQLNHLKN
560 570 580 590
SITSYFGAAG RIACGEKYRV LARRVTLDGK VQYLVEWEGA TAS
Length:593
Mass (Da):67,106
Last modified:January 11, 2011 - v2
Checksum:iC91B04C5294AA2A7
GO
Isoform 2 (identifier: Q9Y483-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-331: Missing.

Show »
Length:262
Mass (Da):29,213
Checksum:iA631A09C112D2B1D
GO
Isoform 3 (identifier: Q9Y483-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-102: Missing.

Show »
Length:491
Mass (Da):55,741
Checksum:iEA2D24C0CDB0F999
GO
Isoform 4 (identifier: Q9Y483-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     331-387: Missing.

Note: No experimental confirmation available.
Show »
Length:536
Mass (Da):60,665
Checksum:iDFEBB14CEB33381E
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti140 – 1401C → S.3 Publications
Corresponds to variant rs2815427 [ dbSNP | Ensembl ].
VAR_054765

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 331331Missing in isoform 2. 1 PublicationVSP_004696Add
BLAST
Alternative sequencei1 – 102102Missing in isoform 3. 1 PublicationVSP_040329Add
BLAST
Alternative sequencei331 – 38757Missing in isoform 4. CuratedVSP_053348Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF072814 mRNA. Translation: AAC27618.1.
AF073293 mRNA. Translation: AAC27080.1.
AJ010014 mRNA. Translation: CAA08970.1.
AK290318 mRNA. Translation: BAF83007.1.
AL117354, AC093577 Genomic DNA. Translation: CAI23502.1.
CCDSiCCDS53340.1. [Q9Y483-4]
CCDS53341.1. [Q9Y483-3]
RefSeqiNP_001157863.1. NM_001164391.1.
NP_001157865.1. NM_001164393.1.
NP_031384.1. NM_007358.3.
XP_011539318.1. XM_011541016.1.
UniGeneiHs.31016.

Genome annotation databases

EnsembliENST00000370298; ENSP00000359321; ENSG00000143033.
GeneIDi22823.
KEGGihsa:22823.
UCSCiuc009wdj.4. human. [Q9Y483-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF072814 mRNA. Translation: AAC27618.1.
AF073293 mRNA. Translation: AAC27080.1.
AJ010014 mRNA. Translation: CAA08970.1.
AK290318 mRNA. Translation: BAF83007.1.
AL117354, AC093577 Genomic DNA. Translation: CAI23502.1.
CCDSiCCDS53340.1. [Q9Y483-4]
CCDS53341.1. [Q9Y483-3]
RefSeqiNP_001157863.1. NM_001164391.1.
NP_001157865.1. NM_001164393.1.
NP_031384.1. NM_007358.3.
XP_011539318.1. XM_011541016.1.
UniGeneiHs.31016.

3D structure databases

ProteinModelPortaliQ9Y483.
SMRiQ9Y483. Positions 36-162, 202-253.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116499. 21 interactions.
IntActiQ9Y483. 14 interactions.
MINTiMINT-1186792.
STRINGi9606.ENSP00000359321.

PTM databases

iPTMnetiQ9Y483.
PhosphoSiteiQ9Y483.

Polymorphism and mutation databases

BioMutaiMTF2.
DMDMi317373393.

Proteomic databases

EPDiQ9Y483.
MaxQBiQ9Y483.
PaxDbiQ9Y483.
PeptideAtlasiQ9Y483.
PRIDEiQ9Y483.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000370298; ENSP00000359321; ENSG00000143033.
GeneIDi22823.
KEGGihsa:22823.
UCSCiuc009wdj.4. human. [Q9Y483-1]

Organism-specific databases

CTDi22823.
GeneCardsiMTF2.
HGNCiHGNC:29535. MTF2.
MIMi609882. gene.
neXtProtiNX_Q9Y483.
PharmGKBiPA128394586.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4323. Eukaryota.
ENOG410XQ6E. LUCA.
HOGENOMiHOG000010307.
HOVERGENiHBG004755.
InParanoidiQ9Y483.
KOiK11485.
OrthoDBiEOG73V6JJ.
PhylomeDBiQ9Y483.
TreeFamiTF106420.

Enzyme and pathway databases

ReactomeiR-HSA-212300. PRC2 methylates histones and DNA.

Miscellaneous databases

ChiTaRSiMTF2. human.
GenomeRNAii22823.
PROiQ9Y483.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y483.
CleanExiHS_MTF2.
ExpressionAtlasiQ9Y483. baseline and differential.
GenevisibleiQ9Y483. HS.

Family and domain databases

Gene3Di3.30.40.10. 2 hits.
InterProiIPR025894. Mtf2_C_dom.
IPR002999. Tudor.
IPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF14061. Mtf2_C. 1 hit.
PF00628. PHD. 1 hit.
[Graphical view]
SMARTiSM00249. PHD. 2 hits.
SM00333. TUDOR. 1 hit.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 2 hits.
PROSITEiPS01359. ZF_PHD_1. 2 hits.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and cloning of a novel human M96 cDNA, spliced isoforms."
    Tao B., Wang J., Yuan J., Qiang B.
    Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), VARIANT SER-140.
  2. "The polycomblike protein family."
    Holen T., Aasland R.
    Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT SER-140.
  3. "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] (ISOFORM 1), VARIANT SER-140.
    Tissue: Tongue.
  4. "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].
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-24, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. Cited for: H3K36ME3-BINDING.
  7. "Tudor domains of the PRC2 components PHF1 and PHF19 selectively bind to histone H3K36me3."
    Qin S., Guo Y., Xu C., Bian C., Fu M., Gong S., Min J.
    Biochem. Biophys. Res. Commun. 430:547-553(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: H3K36ME3-BINDING.
  8. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-452, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Erythroleukemia.

Entry informationi

Entry nameiMTF2_HUMAN
AccessioniPrimary (citable) accession number: Q9Y483
Secondary accession number(s): A6NGQ9
, A8K2Q3, B1AKT5, B1AKT6, Q9UES9, Q9UP40
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: January 11, 2011
Last modified: July 6, 2016
This is version 132 of the entry and version 2 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

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.