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Q24459 (PCL_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Polycomb protein Pcl
Alternative name(s):
Polycomblike protein
Gene names
Name:Pcl
ORF Names:CG5109
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length1043 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Polycomb group (PcG) protein. While PcG proteins are generally required to maintain the transcriptionally repressive state of homeotic genes throughout development, this protein is specifically required during the first 6 hours of embryogenesis to establish the repressed state. Component of the Esc/E(z) complex, which methylates 'Lys-9' and 'Lys-27' residues of histone H3, leading to transcriptional repression of the affected target gene. The Esc/E(z) complex is necessary but not sufficient for the repression of homeotic target genes, suggesting that the recruitment of the distinct PRC1 complex is also required. Required for the correct spatial expression of the homeotic genes of the Antennapedia and Bithorax complexes. Ref.1

Subunit structure

Component of a form of the Esc/E(z) complex present specifically during early embryogenesis which is composed of Caf1, esc, E(z), Su(z)12, Pcl and Rpd3. This complex is distinct from the PRC1 complex, which contains many other PcG proteins like Pc, Ph, Psc, Su(z)2. The two complexes however cooperate and interact together during the first 3 hours of development to establish PcG silencing. Interacts with corto in vitro. Ref.5 Ref.6

Subcellular location

Nucleus. Chromosome. Note: Associated with chromatin. Colocalizes with many PcG sites on polytene chromosomes. It also associates with many unique sites on polytene chromosomes. Ref.1

Developmental stage

Ubiquitous expression in embryos. Ref.1

Domain

The PHD-type zinc fingers mediate the interaction with E(z). Ref.8 Ref.9

In contrast to vertebrate homologs (PHF1, PHF19 and MTF2), the Tudor domain does not bind H3K36me3 (Ref.8 and Ref.9). Ref.8 Ref.9

Sequence similarities

Belongs to the Polycomblike family.

Contains 2 PHD-type zinc fingers.

Contains 1 Tudor domain.

Sequence caution

The sequence AAA64457.1 differs from that shown. Reason: Frameshift at position 807.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

E(z)P4212414EBI-430086,EBI-112315
Rpd3Q945175EBI-430086,EBI-302197

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10431043Polycomb protein Pcl
PRO_0000059339

Regions

Domain349 – 40456Tudor
Zinc finger424 – 47249PHD-type 1
Zinc finger512 – 56049PHD-type 2
Compositional bias237 – 25620Ser-rich
Compositional bias278 – 34770Pro-rich

Amino acid modifications

Modified residue8051Phosphoserine Ref.7
Modified residue8061Phosphoserine Ref.7

Experimental info

Mutagenesis5171C → S or A: Abolishes interaction with E(z). Ref.5
Mutagenesis527 – 5304MLQC → QQQA: Abolishes interaction with E(z). Ref.5
Sequence conflict931S → N in AAA64457. Ref.1

Secondary structure

............. 1043
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q24459 [UniParc].

Last modified May 10, 2004. Version 2.
Checksum: BD3325D7835EEAC3

FASTA1,043114,638
        10         20         30         40         50         60 
MMNNHFHLQH DHPPQNVAHP FMQQPSTAVP SAPPATYGYL AQPAGQQPQW MTTTYQILPP 

        70         80         90        100        110        120 
SVGPATVAKR YYATTGPQTT HPTHPSTIQI TNSFAQQSTP PKQQAATSCS PFKANNIRII 

       130        140        150        160        170        180 
STAPSVYSLN KPPQEAHSTY APVQSYYLPS GGGQTAGQIN LLAASGTGKQ LQPPPLVPVT 

       190        200        210        220        230        240 
NSTSPPSTVV LDRINICINN HYTETPTSLS SSLTTAQQPS PIIPAIQHKA ILPLIDSSTA 

       250        260        270        280        290        300 
DSSSCSSSSV SSSSYSGTAT TSAAVVIVDE PDSTTTTPQT PPTTPEAMSS PGKSSPSPPL 

       310        320        330        340        350        360 
LATQSLLKGV NSMKPSFKTV EAAPPTPPTP PSPPPPPPAP PVAAPSPAVT YALQEDVFIK 

       370        380        390        400        410        420 
CNDGRFYLGT IIDQTSDQYL IRFDDQSEQW CEPDKLRKLG GGSSITAGGG GASTTESTNT 

       430        440        450        460        470        480 
SPSGPMCVAC KRSDIEDVVE ICERCGRGYH RGCTVEIVTG SGIWSCKRCA KPMKMQQPVS 

       490        500        510        520        530        540 
HKITKPAGIC RQLPYHADKL SWDEKHRVNE EQIYCYCGKP GKFDHNMLQC CKCRNWFHTQ 

       550        560        570        580        590        600 
CMQNFKKKLL RGDMFFVFCC TVCNNGIEFV RRMQIEWVDV LHIALYNLRK HQHQKYHHLL 

       610        620        630        640        650        660 
NDIWPFILEQ RHQLPICEKW RTLPETALME RLKQTLKDYS DRFVCGREFK RAPAFYALRH 

       670        680        690        700        710        720 
SGPPHIPKVF LEPHEELSDE LLEKRFKLML MPEEPDEGAN ELPKRVPKDV YEFNTDEDDP 

       730        740        750        760        770        780 
VETSEDEIPI KQIIEKAKKQ AAQKADKHDE LPLKPDLADD NANDGDPGKL PAPIPPLLDA 

       790        800        810        820        830        840 
NSSRKRKAFR LSKRYDNSRN HCDLSSDENS SSSRGTSSLD LIIPPPVNFL GRNNPFLMAT 

       850        860        870        880        890        900 
PKKASQGRSI SVGTGVGVNG IINSIFKLKG TSKEQPRMVR TIKRRLSAKD ITIGPNQEVR 

       910        920        930        940        950        960 
RRRTRRLTTA IEVISTTTIN PIPSHYLPIY AKDLQPPAPP MGKPTHGRLL RQRPQKQSPS 

       970        980        990       1000       1010       1020 
QSRRNSTSST ATSSSSNGIG APGHSMLDLK QSVNKYFGGA MNRIDAGEPF AIRAKRRMGN 

      1030       1040 
GQVQYLVEWG GDTATTAIGL LGN 

« Hide

References

« Hide 'large scale' references
[1]"Molecular characterisation of the Polycomblike gene of Drosophila melanogaster, a trans-acting negative regulator of homeotic gene expression."
Lonie A., D'andrea R., Paro R., Saint R.
Development 120:2629-2636(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
Tissue: Embryo.
[2]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[3]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[4]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Embryo.
[5]"Polycomblike PHD fingers mediate conserved interaction with enhancer of zeste protein."
O'Connell S., Wang L., Robert S., Jones C.A., Saint R., Jones R.S.
J. Biol. Chem. 276:43065-43073(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH E(Z), MUTAGENESIS OF CYS-517 AND 527-MET--CYS-530.
[6]"A 1-megadalton ESC/E(Z) complex from Drosophila that contains polycomblike and RPD3."
Tie F., Prasad-Sinha J., Birve A., Rasmuson-Lestander A., Harte P.J.
Mol. Cell. Biol. 23:3352-3362(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN AN ESC/E(Z) COMPLEX WITH CAF1; ESC; E(Z); SU(Z)12 AND RPD3.
[7]"Phosphoproteome analysis of Drosophila melanogaster embryos."
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-805 AND SER-806, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Embryo.
[8]"Phf19 links methylated Lys36 of histone H3 to regulation of Polycomb activity."
Ballare C., Lange M., Lapinaite A., Martin G.M., Morey L., Pascual G., Liefke R., Simon B., Shi Y., Gozani O., Carlomagno T., Benitah S.A., Di Croce L.
Nat. Struct. Mol. Biol. 19:1257-1265(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAIN.
[9]"Molecular basis for H3K36me3 recognition by the Tudor domain of PHF1."
Musselman C.A., Avvakumov N., Watanabe R., Abraham C.G., Lalonde M.E., Hong Z., Allen C., Roy S., Nunez J.K., Nickoloff J., Kulesza C.A., Yasui A., Cote J., Kutateladze T.G.
Nat. Struct. Mol. Biol. 19:1266-1272(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAIN.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L35153 mRNA. Translation: AAA64457.1. Frameshift.
AE013599 Genomic DNA. Translation: AAF57748.2.
AY075585 mRNA. Translation: AAL68389.1.
RefSeqNP_001261067.1. NM_001274138.1.
NP_476672.1. NM_057324.5.
UniGeneDm.4284.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2XK0NMR-A339-404[»]
ProteinModelPortalQ24459.
SMRQ24459. Positions 350-404, 424-473, 512-567.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid62752. 19 interactions.
IntActQ24459. 24 interactions.
MINTMINT-5227221.

Proteomic databases

PaxDbQ24459.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0086735; FBpp0085914; FBgn0003044.
FBtr0329998; FBpp0303033; FBgn0003044.
GeneID37069.
KEGGdme:Dmel_CG5109.
UCSCCG5109-RA. d. melanogaster.

Organism-specific databases

FlyBaseFBgn0003044. Pcl.

Phylogenomic databases

eggNOGNOG244542.
GeneTreeENSGT00390000009222.
InParanoidQ24459.
KOK11485.
OMADEIPIKQ.
OrthoDBEOG73V6JJ.
PhylomeDBQ24459.

Gene expression databases

BgeeQ24459.

Family and domain databases

Gene3D3.30.40.10. 2 hits.
InterProIPR025894. 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]
PfamPF14061. Mtf2_C. 1 hit.
[Graphical view]
SMARTSM00249. PHD. 2 hits.
SM00333. TUDOR. 1 hit.
[Graphical view]
SUPFAMSSF57903. SSF57903. 2 hits.
PROSITEPS01359. ZF_PHD_1. 2 hits.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ24459.
GenomeRNAi37069.
NextBio801791.

Entry information

Entry namePCL_DROME
AccessionPrimary (citable) accession number: Q24459
Secondary accession number(s): Q8T8P9, Q9V8C2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: May 10, 2004
Last modified: July 9, 2014
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase