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Protein

Polycomb group protein Pc

Gene

Pc

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

Functioni

Polycomb group (PcG) protein. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development. PcG proteins are not required to initiate repression, but to maintain it during later stages of development. Component of the PcG multiprotein PRC1 complex, a complex that acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-118', rendering chromatin heritably changed in its expressibility. Promotes locus-specific chromatin compaction.

GO - Molecular functioni

  • chromatin binding Source: FlyBase
  • core promoter binding Source: FlyBase
  • methylated histone binding Source: FlyBase

GO - Biological processi

  • chromatin silencing Source: FlyBase
  • gene silencing Source: FlyBase
  • negative regulation of response to gamma radiation Source: FlyBase
  • negative regulation of transcription, DNA-templated Source: FlyBase
  • neurogenesis Source: FlyBase
  • neuron remodeling Source: FlyBase
  • regulation of transcription, DNA-templated Source: FlyBase
  • specification of segmental identity, abdomen Source: FlyBase
  • syncytial blastoderm mitotic cell cycle Source: FlyBase
  • ventral cord development Source: FlyBase
  • wound healing Source: FlyBase
Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-DME-3108214. SUMOylation of DNA damage response and repair proteins.
R-DME-4570464. SUMOylation of RNA binding proteins.
SignaLinkiP26017.

Names & Taxonomyi

Protein namesi
Recommended name:
Polycomb group protein Pc
Short name:
Protein polycomb
Gene namesi
Name:Pc
ORF Names:CG7618
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0003042. Pc.

Subcellular locationi

GO - Cellular componenti

  • chromatin Source: FlyBase
  • intercalary heterochromatin Source: FlyBase
  • nucleolus Source: FlyBase
  • nucleus Source: FlyBase
  • PRC1 complex Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 390390Polycomb group protein PcPRO_0000080218Add
BLAST

Proteomic databases

PaxDbiP26017.

Expressioni

Developmental stagei

Required during the entire larval period for normal adult development. It is found in almost all cells and tissues throughout gastrulation and organogenesis though at a much lower level than in early syncytial stages.

Gene expression databases

BgeeiP26017.
ExpressionAtlasiP26017. differential.
GenevisibleiP26017. DM.

Interactioni

Subunit structurei

Component of PRC1 complex, which contains many PcG proteins like Pc, ph, Scm, Psc, Sce and also chromatin-remodeling proteins such as histone deacetylases. This complex is distinct from the Esc/E(z) complex, at least composed of esc, E(z), Su(z)12, Rpd3 and Caf1. The 2 complexes however cooperate and interact together during the first 3 hours of development to establish PcG silencing.2 Publications

GO - Molecular functioni

  • methylated histone binding Source: FlyBase

Protein-protein interaction databases

BioGridi65606. 46 interactions.
IntActiP26017. 1 interaction.
MINTiMINT-271335.
STRINGi7227.FBpp0078059.

Structurei

Secondary structure

1
390
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi24 – 3714Combined sources
Beta strandi40 – 478Combined sources
Helixi52 – 543Combined sources
Beta strandi56 – 594Combined sources
Helixi60 – 623Combined sources
Helixi67 – 737Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PDQX-ray1.76A15-77[»]
1PFBX-ray1.40A23-77[»]
ProteinModelPortaliP26017.
SMRiP26017. Positions 23-77.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26017.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 8459ChromoPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi134 – 14310Poly-His
Compositional biasi160 – 1678Poly-His

Sequence similaritiesi

Contains 1 chromo domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2748. Eukaryota.
ENOG41122KC. LUCA.
InParanoidiP26017.
KOiK11455.
OMAiINQKQPL.
OrthoDBiEOG7XPZ5Z.
PhylomeDBiP26017.

Family and domain databases

InterProiIPR000953. Chromo/shadow_dom.
IPR017984. Chromo_dom_subgr.
IPR023780. Chromo_domain.
IPR016197. Chromodomain-like.
IPR023779. Chromodomain_CS.
[Graphical view]
PfamiPF00385. Chromo. 1 hit.
[Graphical view]
PRINTSiPR00504. CHROMODOMAIN.
SMARTiSM00298. CHROMO. 1 hit.
[Graphical view]
SUPFAMiSSF54160. SSF54160. 1 hit.
PROSITEiPS00598. CHROMO_1. 1 hit.
PS50013. CHROMO_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P26017-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTGRGKGSKG KLGRDNATDD PVDLVYAAEK IIQKRVKKGV VEYRVKWKGW
60 70 80 90 100
NQRYNTWEPE VNILDRRLID IYEQTNKSSG TPSKRGIKKK EKEPDPEPES
110 120 130 140 150
EEDEYTFTEN DVDTHQATTS SATHDKESKK EKKHHHHHHH HHHIKSERNS
160 170 180 190 200
GRRSESPLTH HHHHHHHESK RQRIDHSSSS NSSFTHNSFV PEPDSNSSSS
210 220 230 240 250
EDQPLIGTKR KAEVLKESGK IGVTIKTSPD GPTIKPQPTQ QVTPSQQQPF
260 270 280 290 300
QDQQQAEKIA SEAATQLKSE QQATPLATEA INTTPAESGA EEEEVANEEG
310 320 330 340 350
NQQAPQVPSE NNNIPKPCNN LAINQKQPLT PLSPRALPPR FWLPAKCNIS
360 370 380 390
NRVVITDVTV NLETVTIREC KTERGFFRER DMKGDSSPVA
Length:390
Mass (Da):43,976
Last modified:May 1, 1992 - v1
Checksum:i5DB24AE4B326C3B9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X55702 Genomic DNA. Translation: CAA39229.1.
AE014296 Genomic DNA. Translation: AAF51707.1.
PIRiA38565.
RefSeqiNP_524199.1. NM_079475.3.
UniGeneiDm.13644.

Genome annotation databases

EnsemblMetazoaiFBtr0078405; FBpp0078059; FBgn0003042.
GeneIDi40358.
KEGGidme:Dmel_CG32443.
UCSCiCG32443-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X55702 Genomic DNA. Translation: CAA39229.1.
AE014296 Genomic DNA. Translation: AAF51707.1.
PIRiA38565.
RefSeqiNP_524199.1. NM_079475.3.
UniGeneiDm.13644.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PDQX-ray1.76A15-77[»]
1PFBX-ray1.40A23-77[»]
ProteinModelPortaliP26017.
SMRiP26017. Positions 23-77.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi65606. 46 interactions.
IntActiP26017. 1 interaction.
MINTiMINT-271335.
STRINGi7227.FBpp0078059.

Proteomic databases

PaxDbiP26017.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0078405; FBpp0078059; FBgn0003042.
GeneIDi40358.
KEGGidme:Dmel_CG32443.
UCSCiCG32443-RA. d. melanogaster.

Organism-specific databases

CTDi5091.
FlyBaseiFBgn0003042. Pc.

Phylogenomic databases

eggNOGiKOG2748. Eukaryota.
ENOG41122KC. LUCA.
InParanoidiP26017.
KOiK11455.
OMAiINQKQPL.
OrthoDBiEOG7XPZ5Z.
PhylomeDBiP26017.

Enzyme and pathway databases

ReactomeiR-DME-3108214. SUMOylation of DNA damage response and repair proteins.
R-DME-4570464. SUMOylation of RNA binding proteins.
SignaLinkiP26017.

Miscellaneous databases

EvolutionaryTraceiP26017.
GenomeRNAii40358.
PROiP26017.

Gene expression databases

BgeeiP26017.
ExpressionAtlasiP26017. differential.
GenevisibleiP26017. DM.

Family and domain databases

InterProiIPR000953. Chromo/shadow_dom.
IPR017984. Chromo_dom_subgr.
IPR023780. Chromo_domain.
IPR016197. Chromodomain-like.
IPR023779. Chromodomain_CS.
[Graphical view]
PfamiPF00385. Chromo. 1 hit.
[Graphical view]
PRINTSiPR00504. CHROMODOMAIN.
SMARTiSM00298. CHROMO. 1 hit.
[Graphical view]
SUPFAMiSSF54160. SSF54160. 1 hit.
PROSITEiPS00598. CHROMO_1. 1 hit.
PS50013. CHROMO_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The Polycomb protein shares a homologous domain with a heterochromatin-associated protein of Drosophila."
    Paro R., Hogness D.S.
    Proc. Natl. Acad. Sci. U.S.A. 88:263-267(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Oregon-R.
  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: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. "A Drosophila Polycomb group complex includes Zeste and dTAFII proteins."
    Saurin A.J., Shao Z., Erdjument-Bromage H., Tempst P., Kingston R.E.
    Nature 412:655-660(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE PRC1 COMPLEX WITH SCE; PSC AND PH.
  5. "Reconstitution of a functional core polycomb repressive complex."
    Francis N.J., Saurin A.J., Shao Z., Kingston R.E.
    Mol. Cell 8:545-556(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A PCG COMPLEX WITH SCE; PH AND PSC.

Entry informationi

Entry nameiPC_DROME
AccessioniPrimary (citable) accession number: P26017
Secondary accession number(s): Q9VP49
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: June 8, 2016
This is version 143 of the entry and version 1 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

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.