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Protein

Protein phosphatase 1 regulatory subunit 3F

Gene

PPP1R3F

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

Functioni

Glycogen-targeting subunit for protein phosphatase 1 (PP1).1 Publication

GO - Molecular functioni

  • glycogen binding Source: MGI
  • protein phosphatase binding Source: MGI

GO - Biological processi

  • regulation of glycogen (starch) synthase activity Source: MGI
  • regulation of glycogen biosynthetic process Source: MGI
Complete GO annotation...

Protein family/group databases

CAZyiCBM21. Carbohydrate-Binding Module Family 21.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein phosphatase 1 regulatory subunit 3F
Short name:
R3F
Gene namesi
Name:PPP1R3F
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:14944. PPP1R3F.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 768768CytoplasmicSequence analysisAdd
BLAST
Transmembranei769 – 78921HelicalSequence analysisAdd
BLAST
Topological domaini790 – 79910ExtracellularSequence analysis

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33656.

Polymorphism and mutation databases

BioMutaiPPP1R3F.
DMDMi226694145.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 799799Protein phosphatase 1 regulatory subunit 3FPRO_0000257496Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei14 – 141Phosphoserine1 Publication
Modified residuei18 – 181Phosphoserine1 Publication
Modified residuei420 – 4201Phosphoserine1 Publication
Modified residuei421 – 4211Phosphoserine1 Publication
Modified residuei547 – 5471PhosphoserineCombined sources
Modified residuei589 – 5891PhosphoserineBy similarity
Modified residuei594 – 5941PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ6ZSY5.
MaxQBiQ6ZSY5.
PaxDbiQ6ZSY5.
PeptideAtlasiQ6ZSY5.
PRIDEiQ6ZSY5.

PTM databases

iPTMnetiQ6ZSY5.
PhosphoSiteiQ6ZSY5.

Expressioni

Tissue specificityi

Expressed in brain, skeletal muscle and heart.1 Publication

Gene expression databases

BgeeiQ6ZSY5.
CleanExiHS_PPP1R3F.
ExpressionAtlasiQ6ZSY5. baseline and differential.
GenevisibleiQ6ZSY5. HS.

Organism-specific databases

HPAiHPA000244.
HPA000918.

Interactioni

GO - Molecular functioni

  • protein phosphatase binding Source: MGI

Protein-protein interaction databases

BioGridi124607. 4 interactions.
IntActiQ6ZSY5. 2 interactions.
STRINGi9606.ENSP00000055335.

Structurei

3D structure databases

ProteinModelPortaliQ6ZSY5.
SMRiQ6ZSY5. Positions 113-284.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini128 – 284157CBM21PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi36 – 394PP1-binding motif

Sequence similaritiesi

Contains 1 CBM21 (carbohydrate binding type-21) domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3986. Eukaryota.
ENOG4111FT1. LUCA.
GeneTreeiENSGT00390000013859.
HOGENOMiHOG000090209.
HOVERGENiHBG104043.
InParanoidiQ6ZSY5.
KOiK17453.
OMAiHPARYVP.
PhylomeDBiQ6ZSY5.
TreeFamiTF352142.

Family and domain databases

InterProiIPR005036. CBM21_dom.
[Graphical view]
PfamiPF03370. CBM_21. 1 hit.
[Graphical view]
PROSITEiPS51159. CBM21. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q6ZSY5-1) [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
MARTAPVEPP LRHSAPPSPA AGEPRTSVEA AVAPRRVLFA DEALGLPLAQ
60 70 80 90 100
LRRYRPWGGP GAGKMAAAAG QDGGGGGGAD EDDDGEDGDE GEEEEEACPE
110 120 130 140 150
PSPLCPVPAG GGFYLVPTFS LPPAPGRLER LGRVMVELEA LLPPPGAVPG
160 170 180 190 200
GAGVWVPGGR PPVLRGLVRV LNRSFEKAVH VRASHDGWAS FCDHPARYVP
210 220 230 240 250
RSPPWAGAGG TGAGDPILDP GLGLGPGQAS ASSPDDGGRT DRFAFQLPFA
260 270 280 290 300
EGAGDGARLD FVVRYETPEG TFWANNHGRN YTVLLRIAPA PTPTDAEGLP
310 320 330 340 350
QQQQLPQLEP QPECQGPVEA EARQLKSCMK PVRRRPAEEE LKTKNMDDNT
360 370 380 390 400
FAMAEHPDVQ ESVGPLVAPT PLRPWPQMTL QVSDVPMTGN PAEEGDVPRS
410 420 430 440 450
SPPVAFTEVL QAPAIRIPPS SPLCGLGGSP RDQASGPDAS EGATGPFLEP
460 470 480 490 500
SQQQAEATWG VSSENGGGLE AVSGSEELLG EDTIDQELEQ LYLSHLSRLR
510 520 530 540 550
AAVAAGGAGG GGEGSTDGGM SPSHPLGILT DRDLILKWPG PERALNSALA
560 570 580 590 600
EEITLHYARL GRGVELIKDT EDPDDEGEGE EGLSVTPSSP EGDSPKESPP
610 620 630 640 650
EILSGARSVV ATMGDVWLPW AEGSGCDGPV VLGTEGQFIG DPEKGMGKDT
660 670 680 690 700
SSLHMNRVIA GVTESLGEAG TEAQIEVTSE WAGSLDPISG KEPASPVLLQ
710 720 730 740 750
GQNPTLLSPL GAEVCLSSVA RPHVSSQDEK DAGPSLEPPK KSPTLAVPAE
760 770 780 790
CVCALPPQLR GPLTQTLGVL AGLVVVPVAL NSGVSLLVLA LCLSLAWFS
Length:799
Mass (Da):82,798
Last modified:April 14, 2009 - v3
Checksum:i7E9EDD5515DE245D
GO
Isoform 2 (identifier: Q6ZSY5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-345: Missing.
     354-354: Missing.

Note: No experimental confirmation available.
Show »
Length:453
Mass (Da):46,609
Checksum:i16EAC69D6811DFCF
GO

Sequence cautioni

The sequence AAI31589.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAG51824.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti377 – 3771Q → H in BAG51824 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti351 – 3511F → S.
Corresponds to variant rs17148347 [ dbSNP | Ensembl ].
VAR_028918

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 345345Missing in isoform 2. 1 PublicationVSP_045003Add
BLAST
Alternative sequencei354 – 3541Missing in isoform 2. 1 PublicationVSP_045004

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF235097 Genomic DNA. No translation available.
BC131588 mRNA. Translation: AAI31589.1. Different initiation.
AK056909 mRNA. Translation: BAG51824.1. Different initiation.
CCDSiCCDS35254.1. [Q6ZSY5-1]
CCDS55415.1. [Q6ZSY5-2]
RefSeqiNP_001171674.1. NM_001184745.1. [Q6ZSY5-2]
NP_149992.3. NM_033215.4. [Q6ZSY5-1]
UniGeneiHs.433652.

Genome annotation databases

EnsembliENST00000055335; ENSP00000055335; ENSG00000049769. [Q6ZSY5-1]
ENST00000376188; ENSP00000365359; ENSG00000049769. [Q6ZSY5-2]
ENST00000466508; ENSP00000420687; ENSG00000049769. [Q6ZSY5-2]
ENST00000495799; ENSP00000417535; ENSG00000049769. [Q6ZSY5-2]
GeneIDi89801.
KEGGihsa:89801.
UCSCiuc004dnh.3. human. [Q6ZSY5-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF235097 Genomic DNA. No translation available.
BC131588 mRNA. Translation: AAI31589.1. Different initiation.
AK056909 mRNA. Translation: BAG51824.1. Different initiation.
CCDSiCCDS35254.1. [Q6ZSY5-1]
CCDS55415.1. [Q6ZSY5-2]
RefSeqiNP_001171674.1. NM_001184745.1. [Q6ZSY5-2]
NP_149992.3. NM_033215.4. [Q6ZSY5-1]
UniGeneiHs.433652.

3D structure databases

ProteinModelPortaliQ6ZSY5.
SMRiQ6ZSY5. Positions 113-284.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124607. 4 interactions.
IntActiQ6ZSY5. 2 interactions.
STRINGi9606.ENSP00000055335.

Protein family/group databases

CAZyiCBM21. Carbohydrate-Binding Module Family 21.

PTM databases

iPTMnetiQ6ZSY5.
PhosphoSiteiQ6ZSY5.

Polymorphism and mutation databases

BioMutaiPPP1R3F.
DMDMi226694145.

Proteomic databases

EPDiQ6ZSY5.
MaxQBiQ6ZSY5.
PaxDbiQ6ZSY5.
PeptideAtlasiQ6ZSY5.
PRIDEiQ6ZSY5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000055335; ENSP00000055335; ENSG00000049769. [Q6ZSY5-1]
ENST00000376188; ENSP00000365359; ENSG00000049769. [Q6ZSY5-2]
ENST00000466508; ENSP00000420687; ENSG00000049769. [Q6ZSY5-2]
ENST00000495799; ENSP00000417535; ENSG00000049769. [Q6ZSY5-2]
GeneIDi89801.
KEGGihsa:89801.
UCSCiuc004dnh.3. human. [Q6ZSY5-1]

Organism-specific databases

CTDi89801.
GeneCardsiPPP1R3F.
HGNCiHGNC:14944. PPP1R3F.
HPAiHPA000244.
HPA000918.
neXtProtiNX_Q6ZSY5.
PharmGKBiPA33656.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3986. Eukaryota.
ENOG4111FT1. LUCA.
GeneTreeiENSGT00390000013859.
HOGENOMiHOG000090209.
HOVERGENiHBG104043.
InParanoidiQ6ZSY5.
KOiK17453.
OMAiHPARYVP.
PhylomeDBiQ6ZSY5.
TreeFamiTF352142.

Miscellaneous databases

ChiTaRSiPPP1R3F. human.
GenomeRNAii89801.
PROiQ6ZSY5.

Gene expression databases

BgeeiQ6ZSY5.
CleanExiHS_PPP1R3F.
ExpressionAtlasiQ6ZSY5. baseline and differential.
GenevisibleiQ6ZSY5. HS.

Family and domain databases

InterProiIPR005036. CBM21_dom.
[Graphical view]
PfamiPF03370. CBM_21. 1 hit.
[Graphical view]
PROSITEiPS51159. CBM21. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "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] (ISOFORM 2).
  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] OF 51-799 (ISOFORM 1).
    Tissue: Brain and Prostate.
  4. "R3F, a novel membrane-associated glycogen targeting subunit of protein phosphatase 1 regulates glycogen synthase in astrocytoma cells in response to glucose and extracellular signals."
    Kelsall I.R., Voss M., Munro S., Cuthbertson D.J., Cohen P.T.
    J. Neurochem. 118:596-610(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION AT SER-14; SER-18; SER-420 AND SER-421.
  5. "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-547, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Erythroleukemia.

Entry informationi

Entry nameiPPR3F_HUMAN
AccessioniPrimary (citable) accession number: Q6ZSY5
Secondary accession number(s): A2VDJ8, B3KPW2, E9PCM3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: April 14, 2009
Last modified: July 6, 2016
This is version 93 of the entry and version 3 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 X
    Human chromosome X: 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. 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.