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Protein

E3 ubiquitin-protein ligase RBX1

Gene

Rbx1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins, including proteins involved in cell cycle progression, signal transduction, transcription and transcription-coupled nucleotide excision repair (PubMed:22118460). The functional specificity of the E3 ubiquitin-protein ligase complexes depends on the variable substrate recognition components. As a component of the CSA complex promotes the ubiquitination of ERCC6 resulting in proteasomal degradation (By similarity). Through the RING-type zinc finger, seems to recruit the E2 ubiquitination enzyme, like CDC34, to the complex and brings it into close proximity to the substrate. Probably also stimulates CDC34 autoubiquitination. May be required for histone H3 and histone H4 ubiquitination in response to ultraviolet and for subsequent DNA repair. Promotes the neddylation of CUL1, CUL2, CUL4 and CUL4 via its interaction with UBE2M (By similarity). Involved in the ubiquitination of KEAP1, ENC1 and KLHL41 (By similarity). In concert with ATF2 and CUL3, promotes degradation of KAT5 attenuating its ability to acetylate and activate ATM (By similarity).By similarity1 Publication

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi42 – 421Zinc 11 Publication
Metal bindingi45 – 451Zinc 11 Publication
Metal bindingi53 – 531Zinc 21 Publication
Metal bindingi56 – 561Zinc 21 Publication
Metal bindingi68 – 681Zinc 21 Publication
Metal bindingi75 – 751Zinc 31 Publication
Metal bindingi77 – 771Zinc 3; via pros nitrogen1 Publication
Metal bindingi80 – 801Zinc 1; via pros nitrogen1 Publication
Metal bindingi82 – 821Zinc 21 Publication
Metal bindingi94 – 941Zinc 31 Publication
Metal bindingi97 – 971Zinc 31 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri53 – 9846RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • DNA repair Source: UniProtKB-KW
  • proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
  • protein catabolic process Source: MGI
  • protein monoubiquitination Source: UniProtKB
  • protein neddylation Source: UniProtKB
  • protein ubiquitination Source: UniProtKB
  • SCF-dependent proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
  • ubiquitin-dependent protein catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

DNA damage, DNA repair, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-110314. Recognition of DNA damage by PCNA-containing replication complex.
R-MMU-1170546. Prolactin receptor signaling.
R-MMU-1234176. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
R-MMU-195253. Degradation of beta-catenin by the destruction complex.
R-MMU-4641258. Degradation of DVL.
R-MMU-5610780. Degradation of GLI1 by the proteasome.
R-MMU-5610785. GLI3 is processed to GLI3R by the proteasome.
R-MMU-5632684. Hedgehog 'on' state.
R-MMU-5658442. Regulation of RAS by GAPs.
R-MMU-5696394. DNA Damage Recognition in GG-NER.
R-MMU-5696395. Formation of Incision Complex in GG-NER.
R-MMU-5696400. Dual Incision in GG-NER.
R-MMU-6781823. Formation of TC-NER Pre-Incision Complex.
R-MMU-6782135. Dual incision in TC-NER.
R-MMU-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-MMU-983168. Antigen processing: Ubiquitination & Proteasome degradation.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase RBX1 (EC:6.3.2.-)
Alternative name(s):
RING finger protein 75
RING-box protein 1
Short name:
Rbx1
Cleaved into the following chain:
Gene namesi
Name:Rbx1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:1891829. Rbx1.

Subcellular locationi

GO - Cellular componenti

  • anaphase-promoting complex Source: UniProtKB
  • Cul2-RING ubiquitin ligase complex Source: Ensembl
  • Cul3-RING ubiquitin ligase complex Source: UniProtKB
  • Cul4A-RING E3 ubiquitin ligase complex Source: UniProtKB
  • Cul4B-RING E3 ubiquitin ligase complex Source: UniProtKB
  • Cul5-RING ubiquitin ligase complex Source: Ensembl
  • Cul7-RING ubiquitin ligase complex Source: UniProtKB
  • cullin-RING ubiquitin ligase complex Source: MGI
  • cytosol Source: UniProtKB
  • SCF ubiquitin ligase complex Source: UniProtKB
  • ubiquitin ligase complex Source: UniProtKB
  • VCB complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 108108E3 ubiquitin-protein ligase RBX1PRO_0000056014Add
BLAST
Initiator methionineiRemoved; alternateBy similarity
Chaini2 – 108107E3 ubiquitin-protein ligase RBX1, N-terminally processedPRO_0000423265Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei2 – 21N-acetylalanine; in E3 ubiquitin-protein ligase RBX1, N-terminally processedBy similarity
Modified residuei9 – 91PhosphothreonineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP62878.
MaxQBiP62878.
PaxDbiP62878.
PRIDEiP62878.

PTM databases

PhosphoSiteiP62878.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiP62878.
CleanExiMM_RBX1.
GenevisibleiP62878. MM.

Interactioni

Subunit structurei

Interacts with COPS6. Component of the DCX DET1-COP1 ubiquitin ligase complex at least composed of RBX1, DET1, DDB1, CUL4A and COP1. Part of an E3 ligase complex composed of RBX1, DDB1, DDB2 and CUL4A or CUL4B (PubMed:22118460). Interacts with CAND1 (PubMed:22118460). Interacts with UBE2M (By similarity). Part of a SCF complex consisting of CUL1, RBX1, SKP1 and SKP2. Part of a SCF-like complex consisting of CUL7, RBX1, SKP1 and FBXW8. Part of CBC(VHL) complexes with elongin BC complex (TCEB1 and TCEB2), CUL2 or CUL5 and VHL. Part of the CSA complex (DCX(ERCC8) complex), a DCX E3 ubiquitin-protein ligase complex containing ERCC8, RBX1, DDB1 and CUL4A; the CSA complex interacts with RNA polymerase II; upon UV irradiation it interacts with the COP9 signalosome and preferentially with the hyperphosphorylated form of RNA polymerase II (By similarity). Part of multisubunit E3 ubiquitin ligase complexes with elongin BC complex (TCEB1 and TCEB2), CUL2 and MED8; elongin BC complex (TCEB1 and TCEB2), CUL5 and MUF1. Part of multisubunit complexes with elongin BC complex (TCEB1 and TCEB2), elongin A/TCEB3 or SOCS1 or WSB1 and CUL5. Interacts directly with CUL1 and probably also with CUL2, CUL3, CUL4A, CUL4B, CUL5 and CUL7. Probably interacts with CDC34. Part of a SCF complex consisting of CUL1, RBX1, SKP1 and FBXO2. Part of a SCF complex consisting of CUL1, FBXO3, RBX1 and SKP1; this complex interacts with PML via FBXO3. Component of the SCF(Cyclin F) complex consisting of CUL1, RBX1, SKP1 and CCNF. Identified in a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex together with HINT1 and CDC34 (By similarity). Component of multiple BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes formed of CUL3, RBX1 and a variable BTB domain-containing protein. Part of the BCR(ENC1) complex containing ENC1. Part of the BCR(GAN) complex containing GAN. Part of the BCR(KLHL41) complex containing KLHL41. Part of the BCR(KEAP1) complex containing KEAP1 (By similarity). Interacts with DCUN1D3 (By similarity).By similarity1 Publication

GO - Molecular functioni

  • cullin family protein binding Source: MGI
  • eukaryotic initiation factor 4E binding Source: UniProtKB

Protein-protein interaction databases

BioGridi207980. 25 interactions.
IntActiP62878. 8 interactions.
STRINGi10090.ENSMUSP00000023036.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4A0CX-ray3.80D/F12-108[»]
4A0KX-ray5.93B12-108[»]
4A0LX-ray7.40F/I12-108[»]
ProteinModelPortaliP62878.
SMRiP62878. Positions 19-106.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

The RING-type zinc finger domain is essential for ubiquitin ligase activity. It coordinates an additional third zinc ion.

Sequence similaritiesi

Belongs to the RING-box family.Curated
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri53 – 9846RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG2930. Eukaryota.
COG5194. LUCA.
GeneTreeiENSGT00390000017058.
HOVERGENiHBG001507.
InParanoidiP62878.
KOiK03868.
OMAiARSVCPL.
OrthoDBiEOG7CG721.
PhylomeDBiP62878.
TreeFamiTF105503.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR024766. Znf_RING_H2.
[Graphical view]
PfamiPF12678. zf-rbx1. 1 hit.
[Graphical view]
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P62878-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAAMDVDTP SGTNSGAGKK RFEVKKWNAV ALWAWDIVVD NCAICRNHIM
60 70 80 90 100
DLCIECQANQ ASATSEECTV AWGVCNHAFH FHCISRWLKT RQVCPLDNRE

WEFQKYGH
Length:108
Mass (Da):12,274
Last modified:August 16, 2004 - v1
Checksum:i30FC5ADF66096C0E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti42 – 421C → F in BAB22612 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF140599 mRNA. Translation: AAD29716.1.
AK003159 mRNA. Translation: BAB22612.1.
BC027396 mRNA. Translation: AAH27396.1.
BC051473 mRNA. Translation: AAH51473.1.
BC056992 mRNA. Translation: AAH56992.1.
CCDSiCCDS49676.1.
RefSeqiNP_062686.1. NM_019712.3.
UniGeneiMm.29405.

Genome annotation databases

EnsembliENSMUST00000023036; ENSMUSP00000023036; ENSMUSG00000022400.
GeneIDi56438.
KEGGimmu:56438.
UCSCiuc007wwq.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF140599 mRNA. Translation: AAD29716.1.
AK003159 mRNA. Translation: BAB22612.1.
BC027396 mRNA. Translation: AAH27396.1.
BC051473 mRNA. Translation: AAH51473.1.
BC056992 mRNA. Translation: AAH56992.1.
CCDSiCCDS49676.1.
RefSeqiNP_062686.1. NM_019712.3.
UniGeneiMm.29405.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4A0CX-ray3.80D/F12-108[»]
4A0KX-ray5.93B12-108[»]
4A0LX-ray7.40F/I12-108[»]
ProteinModelPortaliP62878.
SMRiP62878. Positions 19-106.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi207980. 25 interactions.
IntActiP62878. 8 interactions.
STRINGi10090.ENSMUSP00000023036.

PTM databases

PhosphoSiteiP62878.

Proteomic databases

EPDiP62878.
MaxQBiP62878.
PaxDbiP62878.
PRIDEiP62878.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000023036; ENSMUSP00000023036; ENSMUSG00000022400.
GeneIDi56438.
KEGGimmu:56438.
UCSCiuc007wwq.1. mouse.

Organism-specific databases

CTDi9978.
MGIiMGI:1891829. Rbx1.

Phylogenomic databases

eggNOGiKOG2930. Eukaryota.
COG5194. LUCA.
GeneTreeiENSGT00390000017058.
HOVERGENiHBG001507.
InParanoidiP62878.
KOiK03868.
OMAiARSVCPL.
OrthoDBiEOG7CG721.
PhylomeDBiP62878.
TreeFamiTF105503.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-MMU-110314. Recognition of DNA damage by PCNA-containing replication complex.
R-MMU-1170546. Prolactin receptor signaling.
R-MMU-1234176. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
R-MMU-195253. Degradation of beta-catenin by the destruction complex.
R-MMU-4641258. Degradation of DVL.
R-MMU-5610780. Degradation of GLI1 by the proteasome.
R-MMU-5610785. GLI3 is processed to GLI3R by the proteasome.
R-MMU-5632684. Hedgehog 'on' state.
R-MMU-5658442. Regulation of RAS by GAPs.
R-MMU-5696394. DNA Damage Recognition in GG-NER.
R-MMU-5696395. Formation of Incision Complex in GG-NER.
R-MMU-5696400. Dual Incision in GG-NER.
R-MMU-6781823. Formation of TC-NER Pre-Incision Complex.
R-MMU-6782135. Dual incision in TC-NER.
R-MMU-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-MMU-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

ChiTaRSiRbx1. mouse.
PROiP62878.
SOURCEiSearch...

Gene expression databases

BgeeiP62878.
CleanExiMM_RBX1.
GenevisibleiP62878. MM.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR024766. Znf_RING_H2.
[Graphical view]
PfamiPF12678. zf-rbx1. 1 hit.
[Graphical view]
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION IN CBC(VHL) COMPLEX.
  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.
    Tissue: Embryo.
  3. "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].
    Strain: C57BL/6J.
    Tissue: Brain and Mammary tumor.
  4. "Genomic organization and expression of the ubiquitin-proteasome complex-associated protein Rbx1/ROC1/Hrt1."
    Perin J.-P., Seddiqi N., Charbonnier F., Goudou D., Belkadi L., Rieger F., Alliel P.M.
    Cell. Mol. Biol. 45:1131-1137(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  5. "Muf1, a novel elongin BC-interacting leucine-rich repeat protein that can assemble with Cul5 and Rbx1 to reconstitute a ubiquitin ligase."
    Kamura T., Burian D., Yan Q., Schmidt S.L., Lane W.S., Querido E., Branton P.E., Shilatifard A., Conaway R.C., Conaway J.W.
    J. Biol. Chem. 276:29748-29753(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN E3 UBIQUITIN LIGASE COMPLEX WITH MUF1, IDENTIFICATION IN COMPLEXES WITH CUL5.
  6. Cited for: FUNCTION, SUBUNIT.
  7. "The molecular basis of CRL4DDB2/CSA ubiquitin ligase architecture, targeting, and activation."
    Fischer E.S., Scrima A., Bohm K., Matsumoto S., Lingaraju G.M., Faty M., Yasuda T., Cavadini S., Wakasugi M., Hanaoka F., Iwai S., Gut H., Sugasawa K., Thoma N.H.
    Cell 147:1024-1039(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.80 ANGSTROMS) OF 12-108 IN COMPLEXES WITH ZINC; DDB1; CUL4B; CAND1 AND DAMAGED DNA, SUBUNIT, FUNCTION.

Entry informationi

Entry nameiRBX1_MOUSE
AccessioniPrimary (citable) accession number: P62878
Secondary accession number(s): Q8N6Z8
, Q9D1S2, Q9WUK9, Q9Y254
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: June 8, 2016
This is version 115 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.