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Q24459

- PCL_DROME

UniProt

Q24459 - PCL_DROME

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Protein

Polycomb protein Pcl

Gene

Pcl

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri424 – 47249PHD-type 1CuratedPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri512 – 56049PHD-type 2CuratedPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. chromatin binding Source: FlyBase
  2. DNA binding Source: UniProtKB
  3. sequence-specific DNA binding transcription factor activity Source: UniProtKB
  4. zinc ion binding Source: InterPro

GO - Biological processi

  1. chromatin modification Source: UniProtKB
  2. defense response to fungus Source: FlyBase
  3. negative regulation of transcription, DNA-templated Source: UniProtKB
  4. neurogenesis Source: FlyBase
  5. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Developmental protein, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Polycomb protein Pcl
Alternative name(s):
Polycomblike protein
Gene namesi
Name:Pcl
ORF Names:CG5109
OrganismiDrosophila melanogaster (Fruit fly)Imported
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0003044. Pcl.

Subcellular locationi

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

GO - Cellular componenti

  1. chromosome Source: UniProtKB-KW
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi517 – 5171C → S or A: Abolishes interaction with E(z). 1 Publication
Mutagenesisi527 – 5304MLQC → QQQA: Abolishes interaction with E(z). 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10431043Polycomb protein PclPRO_0000059339Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei805 – 8051Phosphoserine1 Publication
Modified residuei806 – 8061Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ24459.

Expressioni

Developmental stagei

Ubiquitous expression in embryos.1 Publication

Gene expression databases

BgeeiQ24459.

Interactioni

Subunit structurei

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.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
E(z)P4212414EBI-430086,EBI-112315
Rpd3Q945175EBI-430086,EBI-302197

Protein-protein interaction databases

BioGridi62752. 19 interactions.
IntActiQ24459. 24 interactions.
MINTiMINT-5227221.

Structurei

Secondary structure

1
1043
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi341 – 3455
Beta strandi356 – 3605
Beta strandi366 – 3749
Beta strandi379 – 3835
Beta strandi388 – 3914
Turni393 – 3953

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XK0NMR-A339-404[»]
ProteinModelPortaliQ24459.
SMRiQ24459. Positions 350-404, 425-471, 512-565.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ24459.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini349 – 40456TudorAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi237 – 25620Ser-richAdd
BLAST
Compositional biasi278 – 34770Pro-richAdd
BLAST

Domaini

The PHD-type zinc fingers mediate the interaction with E(z).
In contrast to vertebrate homologs (PHF1, PHF19 and MTF2), the Tudor domain does not bind H3K36me3 (PubMed:23104054 and PubMed:23142980).

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri424 – 47249PHD-type 1CuratedPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri512 – 56049PHD-type 2CuratedPROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG244542.
GeneTreeiENSGT00390000009222.
InParanoidiQ24459.
KOiK11485.
OMAiDEIPIKQ.
OrthoDBiEOG73V6JJ.
PhylomeDBiQ24459.

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.
[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]

Sequencei

Sequence statusi: Complete.

Q24459-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MMNNHFHLQH DHPPQNVAHP FMQQPSTAVP SAPPATYGYL AQPAGQQPQW
60 70 80 90 100
MTTTYQILPP SVGPATVAKR YYATTGPQTT HPTHPSTIQI TNSFAQQSTP
110 120 130 140 150
PKQQAATSCS PFKANNIRII STAPSVYSLN KPPQEAHSTY APVQSYYLPS
160 170 180 190 200
GGGQTAGQIN LLAASGTGKQ LQPPPLVPVT NSTSPPSTVV LDRINICINN
210 220 230 240 250
HYTETPTSLS SSLTTAQQPS PIIPAIQHKA ILPLIDSSTA DSSSCSSSSV
260 270 280 290 300
SSSSYSGTAT TSAAVVIVDE PDSTTTTPQT PPTTPEAMSS PGKSSPSPPL
310 320 330 340 350
LATQSLLKGV NSMKPSFKTV EAAPPTPPTP PSPPPPPPAP PVAAPSPAVT
360 370 380 390 400
YALQEDVFIK CNDGRFYLGT IIDQTSDQYL IRFDDQSEQW CEPDKLRKLG
410 420 430 440 450
GGSSITAGGG GASTTESTNT SPSGPMCVAC KRSDIEDVVE ICERCGRGYH
460 470 480 490 500
RGCTVEIVTG SGIWSCKRCA KPMKMQQPVS HKITKPAGIC RQLPYHADKL
510 520 530 540 550
SWDEKHRVNE EQIYCYCGKP GKFDHNMLQC CKCRNWFHTQ CMQNFKKKLL
560 570 580 590 600
RGDMFFVFCC TVCNNGIEFV RRMQIEWVDV LHIALYNLRK HQHQKYHHLL
610 620 630 640 650
NDIWPFILEQ RHQLPICEKW RTLPETALME RLKQTLKDYS DRFVCGREFK
660 670 680 690 700
RAPAFYALRH SGPPHIPKVF LEPHEELSDE LLEKRFKLML MPEEPDEGAN
710 720 730 740 750
ELPKRVPKDV YEFNTDEDDP VETSEDEIPI KQIIEKAKKQ AAQKADKHDE
760 770 780 790 800
LPLKPDLADD NANDGDPGKL PAPIPPLLDA NSSRKRKAFR LSKRYDNSRN
810 820 830 840 850
HCDLSSDENS SSSRGTSSLD LIIPPPVNFL GRNNPFLMAT PKKASQGRSI
860 870 880 890 900
SVGTGVGVNG IINSIFKLKG TSKEQPRMVR TIKRRLSAKD ITIGPNQEVR
910 920 930 940 950
RRRTRRLTTA IEVISTTTIN PIPSHYLPIY AKDLQPPAPP MGKPTHGRLL
960 970 980 990 1000
RQRPQKQSPS QSRRNSTSST ATSSSSNGIG APGHSMLDLK QSVNKYFGGA
1010 1020 1030 1040
MNRIDAGEPF AIRAKRRMGN GQVQYLVEWG GDTATTAIGL LGN
Length:1,043
Mass (Da):114,638
Last modified:May 10, 2004 - v2
Checksum:iBD3325D7835EEAC3
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti93 – 931S → N in AAA64457. (PubMed:7956837)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L35153 mRNA. Translation: AAA64457.1. Frameshift.
AE013599 Genomic DNA. Translation: AAF57748.2.
AY075585 mRNA. Translation: AAL68389.1.
RefSeqiNP_001261067.1. NM_001274138.2.
NP_476672.1. NM_057324.6.
UniGeneiDm.4284.

Genome annotation databases

EnsemblMetazoaiFBtr0086735; FBpp0085914; FBgn0003044.
FBtr0329998; FBpp0303033; FBgn0003044.
GeneIDi37069.
KEGGidme:Dmel_CG5109.
UCSCiCG5109-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L35153 mRNA. Translation: AAA64457.1 . Frameshift.
AE013599 Genomic DNA. Translation: AAF57748.2 .
AY075585 mRNA. Translation: AAL68389.1 .
RefSeqi NP_001261067.1. NM_001274138.2.
NP_476672.1. NM_057324.6.
UniGenei Dm.4284.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2XK0 NMR - A 339-404 [» ]
ProteinModelPortali Q24459.
SMRi Q24459. Positions 350-404, 425-471, 512-565.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 62752. 19 interactions.
IntActi Q24459. 24 interactions.
MINTi MINT-5227221.

Proteomic databases

PaxDbi Q24459.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0086735 ; FBpp0085914 ; FBgn0003044 .
FBtr0329998 ; FBpp0303033 ; FBgn0003044 .
GeneIDi 37069.
KEGGi dme:Dmel_CG5109.
UCSCi CG5109-RA. d. melanogaster.

Organism-specific databases

FlyBasei FBgn0003044. Pcl.

Phylogenomic databases

eggNOGi NOG244542.
GeneTreei ENSGT00390000009222.
InParanoidi Q24459.
KOi K11485.
OMAi DEIPIKQ.
OrthoDBi EOG73V6JJ.
PhylomeDBi Q24459.

Miscellaneous databases

EvolutionaryTracei Q24459.
GenomeRNAii 37069.
NextBioi 801791.

Gene expression databases

Bgeei Q24459.

Family and domain databases

Gene3Di 3.30.40.10. 2 hits.
InterProi IPR025894. 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 ]
Pfami PF14061. Mtf2_C. 1 hit.
[Graphical view ]
SMARTi SM00249. PHD. 2 hits.
SM00333. TUDOR. 1 hit.
[Graphical view ]
SUPFAMi SSF57903. SSF57903. 2 hits.
PROSITEi PS01359. ZF_PHD_1. 2 hits.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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: Embryo1 Publication.
  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.
    , 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: Berkeley1 Publication.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley1 Publication.
    Tissue: Embryo1 Publication.
  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. Cited for: DOMAIN.
  9. Cited for: DOMAIN.

Entry informationi

Entry nameiPCL_DROME
AccessioniPrimary (citable) accession number: Q24459
Secondary accession number(s): Q8T8P9, Q9V8C2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: May 10, 2004
Last modified: October 29, 2014
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3