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Protein

Intron-binding protein aquarius

Gene

AQR

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

Functioni

Intron-binding spliceosomal protein required to link pre-mRNA splicing and snoRNP (small nucleolar ribonucleoprotein) biogenesis. Plays a key role in position-dependent assembly of intron-encoded box C/D small snoRNP, splicing being required for snoRNP assembly. May act by helping the folding of the snoRNA sequence. Binds to intron of pre-mRNAs in a sequence-independent manner, contacting the region between snoRNA and the branchpoint of introns (40 nucleotides upstream of the branchpoint) during the late stages of splicing.1 Publication

GO - Molecular functioni

  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-6781823. Formation of TC-NER Pre-Incision Complex.
R-HSA-6781827. Transcription-Coupled Nucleotide Excision Repair (TC-NER).
R-HSA-6782135. Dual incision in TC-NER.
R-HSA-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.

Names & Taxonomyi

Protein namesi
Recommended name:
Intron-binding protein aquarius
Alternative name(s):
Intron-binding protein of 160 kDa
Short name:
IBP160
Gene namesi
Name:AQR
Synonyms:KIAA0560
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:29513. AQR.

Subcellular locationi

  • Nucleus 1 Publication

  • Note: Localizes to speckle-like regions of the nucleoplasm.1 Publication

GO - Cellular componenti

  • catalytic step 2 spliceosome Source: UniProtKB
  • membrane Source: UniProtKB
  • nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134869224.

Polymorphism and mutation databases

BioMutaiAQR.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14851485Intron-binding protein aquariusPRO_0000252389Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1051 – 10511N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiO60306.
MaxQBiO60306.
PaxDbiO60306.
PRIDEiO60306.

PTM databases

iPTMnetiO60306.
PhosphoSiteiO60306.

Expressioni

Gene expression databases

BgeeiO60306.
CleanExiHS_AQR.
ExpressionAtlasiO60306. baseline and differential.
GenevisibleiO60306. HS.

Interactioni

Subunit structurei

Identified in the spliceosome C complex. Component of the XAB2 complex, a multimeric protein complex composed of XAB2, PRPF19, AQR, ZNF830, ISY1, and PPIE.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ZNF830Q96NB32EBI-2512328,EBI-3920997

Protein-protein interaction databases

BioGridi115065. 55 interactions.
DIPiDIP-53576N.
IntActiO60306. 23 interactions.
MINTiMINT-5005864.
STRINGi9606.ENSP00000156471.

Structurei

Secondary structure

1
1485
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi20 – 3011Combined sources
Helixi43 – 5210Combined sources
Turni53 – 586Combined sources
Helixi61 – 699Combined sources
Helixi72 – 754Combined sources
Helixi78 – 803Combined sources
Turni83 – 853Combined sources
Helixi88 – 10316Combined sources
Helixi110 – 1145Combined sources
Helixi119 – 13113Combined sources
Beta strandi136 – 1383Combined sources
Helixi140 – 15415Combined sources
Turni155 – 1584Combined sources
Helixi160 – 17011Combined sources
Helixi172 – 1776Combined sources
Helixi180 – 18910Combined sources
Helixi193 – 20513Combined sources
Helixi209 – 21911Combined sources
Helixi221 – 23414Combined sources
Beta strandi238 – 2403Combined sources
Helixi244 – 26118Combined sources
Helixi264 – 27613Combined sources
Helixi279 – 2846Combined sources
Helixi287 – 2904Combined sources
Turni292 – 2954Combined sources
Helixi296 – 30914Combined sources
Turni315 – 3173Combined sources
Helixi323 – 34422Combined sources
Helixi346 – 3483Combined sources
Helixi349 – 3535Combined sources
Helixi356 – 3594Combined sources
Helixi362 – 3698Combined sources
Helixi374 – 38310Combined sources
Helixi400 – 41112Combined sources
Helixi417 – 4226Combined sources
Helixi430 – 4334Combined sources
Turni436 – 4383Combined sources
Beta strandi446 – 4483Combined sources
Helixi462 – 49130Combined sources
Beta strandi494 – 4963Combined sources
Beta strandi502 – 5065Combined sources
Beta strandi509 – 52214Combined sources
Beta strandi535 – 5428Combined sources
Helixi547 – 5537Combined sources
Beta strandi561 – 5677Combined sources
Helixi583 – 5875Combined sources
Beta strandi589 – 60113Combined sources
Beta strandi620 – 62910Combined sources
Helixi631 – 64414Combined sources
Helixi649 – 6513Combined sources
Beta strandi655 – 6573Combined sources
Helixi661 – 6633Combined sources
Helixi666 – 67813Combined sources
Helixi685 – 6917Combined sources
Turni697 – 7004Combined sources
Helixi702 – 7043Combined sources
Beta strandi710 – 7156Combined sources
Helixi721 – 7277Combined sources
Beta strandi731 – 7366Combined sources
Turni740 – 7423Combined sources
Beta strandi745 – 7506Combined sources
Beta strandi775 – 7817Combined sources
Helixi791 – 7933Combined sources
Helixi804 – 81411Combined sources
Beta strandi815 – 8228Combined sources
Helixi829 – 84315Combined sources
Beta strandi849 – 8546Combined sources
Helixi856 – 86611Combined sources
Helixi873 – 8753Combined sources
Beta strandi876 – 8783Combined sources
Beta strandi888 – 8903Combined sources
Helixi894 – 91825Combined sources
Helixi929 – 93810Combined sources
Helixi940 – 95112Combined sources
Helixi961 – 9666Combined sources
Turni969 – 9768Combined sources
Beta strandi977 – 9793Combined sources
Helixi987 – 101125Combined sources
Helixi1013 – 10164Combined sources
Helixi1020 – 102910Combined sources
Beta strandi1033 – 10386Combined sources
Helixi1039 – 105214Combined sources
Beta strandi1057 – 10637Combined sources
Helixi1064 – 10663Combined sources
Helixi1069 – 10735Combined sources
Helixi1074 – 10774Combined sources
Beta strandi1090 – 10956Combined sources
Helixi1108 – 11136Combined sources
Helixi1119 – 11268Combined sources
Helixi1141 – 11488Combined sources
Beta strandi1151 – 11533Combined sources
Helixi1158 – 11625Combined sources
Helixi1164 – 11663Combined sources
Beta strandi1173 – 11819Combined sources
Beta strandi1188 – 11914Combined sources
Helixi1201 – 121717Combined sources
Helixi1221 – 12233Combined sources
Beta strandi1224 – 12296Combined sources
Helixi1231 – 124414Combined sources
Beta strandi1257 – 12593Combined sources
Helixi1260 – 12634Combined sources
Beta strandi1268 – 12747Combined sources
Helixi1282 – 12854Combined sources
Helixi1287 – 12937Combined sources
Beta strandi1296 – 130510Combined sources
Helixi1307 – 13115Combined sources
Helixi1314 – 13163Combined sources
Helixi1317 – 13237Combined sources
Beta strandi1328 – 13325Combined sources
Beta strandi1343 – 13464Combined sources
Beta strandi1353 – 13553Combined sources
Helixi1358 – 137518Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4PJ3X-ray2.30A19-1485[»]
ProteinModelPortaliO60306.
SMRiO60306. Positions 1007-1303.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the CWF11 family.Curated

Phylogenomic databases

eggNOGiKOG1806. Eukaryota.
ENOG410XPV8. LUCA.
GeneTreeiENSGT00810000125415.
HOGENOMiHOG000170551.
HOVERGENiHBG080430.
InParanoidiO60306.
KOiK12874.
OMAiINRRCGS.
OrthoDBiEOG78M012.
PhylomeDBiO60306.
TreeFamiTF105711.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR032464. Aquarius.
IPR032174. Aquarius_N.
IPR026300. CWF11_fam.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR10887:SF5. PTHR10887:SF5. 1 hit.
PfamiPF16399. Aquarius_N. 1 hit.
[Graphical view]
PIRSFiPIRSF038901. AQR_cwf11. 1 hit.
SUPFAMiSSF52540. SSF52540. 3 hits.

Sequencei

Sequence statusi: Complete.

O60306-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAPAQPKKI VAPTVSQINA EFVTQLACKY WAPHIKKKSP FDIKVIEDIY
60 70 80 90 100
EKEIVKSRFA IRKIMLLEFS QYLENYLWMN YSPEVSSKAY LMSICCMVNE
110 120 130 140 150
KFRENVPAWE IFKKKPDHFP FFFKHILKAA LAETDGEFSL HEQTVLLLFL
160 170 180 190 200
DHCFNSLEVD LIRSQVQQLI SLPMWMGLQL ARLELELKKT PKLRKFWNLI
210 220 230 240 250
KKNDEKMDPE AREQAYQERR FLSQLIQKFI SVLKSVPLSE PVTMDKVHYC
260 270 280 290 300
ERFIELMIDL EALLPTRRWF NTILDDSHLL VHCYLSNLVR REEDGHLFSQ
310 320 330 340 350
LLDMLKFYTG FEINDQTGNA LTENEMTTIH YDRITSLQRA AFAHFPELYD
360 370 380 390 400
FALSNVAEVD TRESLVKFFG PLSSNTLHQV ASYLCLLPTL PKNEDTTFDK
410 420 430 440 450
EFLLELLVSR HERRISQIQQ LNQMPLYPTE KIIWDENIVP TEYYSGEGCL
460 470 480 490 500
ALPKLNLQFL TLHDYLLRNF NLFRLESTYE IRQDIEDSVS RMKPWQSEYG
510 520 530 540 550
GVVFGGWARM AQPIVAFTVV EVAKPNIGEN WPTRVRADVT INLNVRDHIK
560 570 580 590 600
DEWEGLRKHD VCFLITVRPT KPYGTKFDRR RPFIEQVGLV YVRGCEIQGM
610 620 630 640 650
LDDKGRVIED GPEPRPNLRG ESRTFRVFLD PNQYQQDMTN TIQNGAEDVY
660 670 680 690 700
ETFNIIMRRK PKENNFKAVL ETIRNLMNTD CVVPDWLHDI ILGYGDPSSA
710 720 730 740 750
HYSKMPNQIA TLDFNDTFLS IEHLKASFPG HNVKVTVEDP ALQIPPFRIT
760 770 780 790 800
FPVRSGKGKK RKDADVEDED TEEAKTLIVE PHVIPNRGPY PYNQPKRNTI
810 820 830 840 850
QFTHTQIEAI RAGMQPGLTM VVGPPGTGKT DVAVQIISNI YHNFPEQRTL
860 870 880 890 900
IVTHSNQALN QLFEKIMALD IDERHLLRLG HGEEELETEK DFSRYGRVNY
910 920 930 940 950
VLARRIELLE EVKRLQKSLG VPGDASYTCE TAGYFFLYQV MSRWEEYISK
960 970 980 990 1000
VKNKGSTLPD VTEVSTFFPF HEYFANAPQP IFKGRSYEED MEIAEGCFRH
1010 1020 1030 1040 1050
IKKIFTQLEE FRASELLRSG LDRSKYLLVK EAKIIAMTCT HAALKRHDLV
1060 1070 1080 1090 1100
KLGFKYDNIL MEEAAQILEI ETFIPLLLQN PQDGFSRLKR WIMIGDHHQL
1110 1120 1130 1140 1150
PPVIKNMAFQ KYSNMEQSLF TRFVRVGVPT VDLDAQGRAR ASLCNLYNWR
1160 1170 1180 1190 1200
YKNLGNLPHV QLLPEFSTAN AGLLYDFQLI NVEDFQGVGE SEPNPYFYQN
1210 1220 1230 1240 1250
LGEAEYVVAL FMYMCLLGYP ADKISILTTY NGQKHLIRDI INRRCGNNPL
1260 1270 1280 1290 1300
IGRPNKVTTV DRFQGQQNDY ILLSLVRTRA VGHLRDVRRL VVAMSRARLG
1310 1320 1330 1340 1350
LYIFARVSLF QNCFELTPAF SQLTARPLHL HIIPTEPFPT TRKNGERPSH
1360 1370 1380 1390 1400
EVQIIKNMPQ MANFVYNMYM HLIQTTHHYH QTLLQLPPAM VEEGEEVQNQ
1410 1420 1430 1440 1450
ETELETEEEA MTVQADIIPS PTDTSCRQET PAFQTDTTPS ETGATSTPEA
1460 1470 1480
IPALSETTPT VVGAVSAPAE ANTPQDATSA PEETK
Length:1,485
Mass (Da):171,295
Last modified:October 17, 2006 - v4
Checksum:iD0ADDA621A9418FD
GO

Sequence cautioni

The sequence BAA25486.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti242 – 2421V → A in ABQ66265 (PubMed:17974005).Curated
Sequence conflicti1026 – 10261Y → F in ABQ66265 (PubMed:17974005).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB011132 mRNA. Translation: BAA25486.3. Different initiation.
EF553519 mRNA. Translation: ABQ66265.1.
BC036913 mRNA. Translation: AAH36913.1.
BC070379 mRNA. Translation: AAH70379.1.
BC108262 mRNA. Translation: AAI08263.1.
BC127111 mRNA. Translation: AAI27112.1.
BC127112 mRNA. Translation: AAI27113.1.
CCDSiCCDS42013.1.
PIRiT00333.
RefSeqiNP_055506.1. NM_014691.2.
UniGeneiHs.510958.

Genome annotation databases

EnsembliENST00000156471; ENSP00000156471; ENSG00000021776.
GeneIDi9716.
KEGGihsa:9716.
UCSCiuc001ziv.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB011132 mRNA. Translation: BAA25486.3. Different initiation.
EF553519 mRNA. Translation: ABQ66265.1.
BC036913 mRNA. Translation: AAH36913.1.
BC070379 mRNA. Translation: AAH70379.1.
BC108262 mRNA. Translation: AAI08263.1.
BC127111 mRNA. Translation: AAI27112.1.
BC127112 mRNA. Translation: AAI27113.1.
CCDSiCCDS42013.1.
PIRiT00333.
RefSeqiNP_055506.1. NM_014691.2.
UniGeneiHs.510958.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4PJ3X-ray2.30A19-1485[»]
ProteinModelPortaliO60306.
SMRiO60306. Positions 1007-1303.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115065. 55 interactions.
DIPiDIP-53576N.
IntActiO60306. 23 interactions.
MINTiMINT-5005864.
STRINGi9606.ENSP00000156471.

PTM databases

iPTMnetiO60306.
PhosphoSiteiO60306.

Polymorphism and mutation databases

BioMutaiAQR.

Proteomic databases

EPDiO60306.
MaxQBiO60306.
PaxDbiO60306.
PRIDEiO60306.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000156471; ENSP00000156471; ENSG00000021776.
GeneIDi9716.
KEGGihsa:9716.
UCSCiuc001ziv.4. human.

Organism-specific databases

CTDi9716.
GeneCardsiAQR.
HGNCiHGNC:29513. AQR.
MIMi610548. gene.
neXtProtiNX_O60306.
PharmGKBiPA134869224.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1806. Eukaryota.
ENOG410XPV8. LUCA.
GeneTreeiENSGT00810000125415.
HOGENOMiHOG000170551.
HOVERGENiHBG080430.
InParanoidiO60306.
KOiK12874.
OMAiINRRCGS.
OrthoDBiEOG78M012.
PhylomeDBiO60306.
TreeFamiTF105711.

Enzyme and pathway databases

ReactomeiR-HSA-6781823. Formation of TC-NER Pre-Incision Complex.
R-HSA-6781827. Transcription-Coupled Nucleotide Excision Repair (TC-NER).
R-HSA-6782135. Dual incision in TC-NER.
R-HSA-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.

Miscellaneous databases

ChiTaRSiAQR. human.
GenomeRNAii9716.
NextBioi36525.
PROiO60306.
SOURCEiSearch...

Gene expression databases

BgeeiO60306.
CleanExiHS_AQR.
ExpressionAtlasiO60306. baseline and differential.
GenevisibleiO60306. HS.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR032464. Aquarius.
IPR032174. Aquarius_N.
IPR026300. CWF11_fam.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR10887:SF5. PTHR10887:SF5. 1 hit.
PfamiPF16399. Aquarius_N. 1 hit.
[Graphical view]
PIRSFiPIRSF038901. AQR_cwf11. 1 hit.
SUPFAMiSSF52540. SSF52540. 3 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
    Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:31-39(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Uterus.
  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].
    Tissue: Cervix and Mammary gland.
  4. "Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis."
    Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.
    RNA 8:426-439(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
  5. "A spliceosomal intron binding protein, IBP160, links Position-dependent assembly of intron-encoded box C/D snoRNP to pre-mRNA splicing."
    Hirose T., Ideue T., Nagai M., Hagiwara M., Shu M.-D., Steitz J.A.
    Mol. Cell 23:673-684(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION.
  6. "Isolation of XAB2 complex involved in pre-mRNA splicing, transcription, and transcription-coupled repair."
    Kuraoka I., Ito S., Wada T., Hayashida M., Lee L., Saijo M., Nakatsu Y., Matsumoto M., Matsunaga T., Handa H., Qin J., Nakatani Y., Tanaka K.
    J. Biol. Chem. 283:940-950(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION AS PART OF THE XAB2 COMPLEX.
  7. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1051, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiAQR_HUMAN
AccessioniPrimary (citable) accession number: O60306
Secondary accession number(s): A0JP17
, A5YKK3, Q2YDX9, Q6IRU8, Q6PIC8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: October 17, 2006
Last modified: April 13, 2016
This is version 116 of the entry and version 4 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  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.