GenomeNet

Database: UniProt
Entry: Q8ST83
LinkDB: Q8ST83
Original site: Q8ST83 
ID   PHO_DROME               Reviewed;         520 AA.
AC   Q8ST83; A4V138; O76247; Q6W466; Q6W467; Q6W470; Q6W480; Q6W485; Q9V4A3;
DT   28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   28-MAR-2003, sequence version 2.
DT   27-MAR-2024, entry version 173.
DE   RecName: Full=Polycomb protein PHO;
DE   AltName: Full=Protein pleiohomeotic;
DE   AltName: Full=Transcription factor YY1 homolog;
GN   Name=pho; ORFNames=CG17743;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DNA-BINDING ACTIVITY.
RC   TISSUE=Embryo;
RX   PubMed=9651589; DOI=10.1016/s1097-2765(00)80106-9;
RA   Brown J.L., Mucci D., Whiteley M., Dirksen M.-L., Kassis J.A.;
RT   "The Drosophila Polycomb group gene pleiohomeotic encodes a DNA binding
RT   protein with homology to the transcription factor YY1.";
RL   Mol. Cell 1:1057-1064(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 48-373.
RC   STRAIN=253.27, 253.30, Closs10, Closs19, North7.13, Rio, South1.10, Y10,
RC   ZH56, and ZW30;
RX   PubMed=11778050; DOI=10.1126/science.1064521;
RA   Wang W., Thornton K., Berry A., Long M.;
RT   "Nucleotide variation along the Drosophila melanogaster fourth
RT   chromosome.";
RL   Science 295:134-137(2002).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 79-334.
RC   STRAIN=Crete24, Crete26, Crete30, Crete31, Crete35, Crete40, Crete42,
RC   Crete43, Crete44, Crete8, FTF1, FTF105, FTF14, FTF2, FTF20, FTF23, FTF26,
RC   FTF28, FTF5, FTF6, Zim11, Zim2, Zim30, and Zim53;
RX   PubMed=14668375; DOI=10.1093/genetics/165.3.1195;
RA   Sheldahl L.A., Weinreich D.M., Rand D.M.;
RT   "Recombination, dominance and selection on amino acid polymorphism in the
RT   Drosophila genome: contrasting patterns on the X and fourth chromosomes.";
RL   Genetics 165:1195-1208(2003).
RN   [7]
RP   FUNCTION.
RX   PubMed=10433918; DOI=10.1242/dev.126.17.3905;
RA   Fritsch C., Brown J.L., Kassis J.A., Mueller J.;
RT   "The DNA-binding Polycomb group protein pleiohomeotic mediates silencing of
RT   a Drosophila homeotic gene.";
RL   Development 126:3905-3913(1999).
RN   [8]
RP   LACK OF INTERACTION WITH THE PRC1 POLYCOMB COMPLEX.
RX   PubMed=11092813; DOI=10.1242/dev.128.1.75;
RA   Poux S., McCabe D., Pirrotta V.;
RT   "Recruitment of components of Polycomb group chromatin complexes in
RT   Drosophila.";
RL   Development 128:75-85(2001).
RN   [9]
RP   IDENTIFICATION IN A COMPLEX WITH HDAC1; ESC AND E(Z), AND TRANSIENT
RP   INTERACTION WITH THE PRC1 COMPLEX.
RX   PubMed=11581156; DOI=10.1101/gad.208901;
RA   Poux S., Melfi R., Pirrotta V.;
RT   "Establishment of Polycomb silencing requires a transient interaction
RT   between PC and ESC.";
RL   Genes Dev. 15:2509-2514(2001).
RN   [10]
RP   DNA-BINDING ACTIVITY, SUBCELLULAR LOCATION, IDENTIFICATION IN THE INO80
RP   COMPLEX, AND INTERACTION WITH SFMBT.
RC   TISSUE=Embryo;
RX   PubMed=16618800; DOI=10.1101/gad.377406;
RA   Klymenko T., Papp B., Fischle W., Koecher T., Schelder M., Fritsch C.,
RA   Wild B., Wilm M., Mueller J.;
RT   "A Polycomb group protein complex with sequence-specific DNA-binding and
RT   selective methyl-lysine-binding activities.";
RL   Genes Dev. 20:1110-1122(2006).
CC   -!- FUNCTION: Polycomb group (PcG) protein that binds to the 5'-
CC       CNGCCATNNNNG-3' sequence found in the regulatory regions of many genes.
CC       PcG proteins act by forming multiprotein complexes, which are required
CC       to maintain the transcriptionally repressive state of homeotic genes
CC       throughout development. PcG proteins are not required to initiate
CC       repression, but to maintain it during later stages of development. They
CC       probably act via the methylation of histones, rendering chromatin
CC       heritably changed in its expressibility. Probably targets the Esc/E(z)
CC       complex to DNA. Necessary but not sufficient to recruit a functional
CC       PcG repressive complex that represses target genes, suggesting that the
CC       recruitment of the distinct PRC1 complex is also required to allow a
CC       subsequent repression. {ECO:0000269|PubMed:10433918,
CC       ECO:0000269|PubMed:9651589}.
CC   -!- FUNCTION: Proposed core component of the chromatin remodeling Ino80
CC       complex which is involved in transcriptional regulation, DNA
CC       replication and probably DNA repair. {ECO:0000250}.
CC   -!- SUBUNIT: Component of the Esc/E(z) complex, composed of Esc, E(z),
CC       Su(z)12, HDAC1/Rpd3 and Caf1-55. This complex is distinct from the PRC1
CC       complex, which contains many other PcG proteins like Pc, Ph, Psc,
CC       Su(z)2. The two complexes however cooperate and interact together
CC       during the first 3 hours of development to establish PcG silencing.
CC       Component of the chromatin remodeling Ino80 complex. Interacts with
CC       Sfmbt to form a pho-repressive complex (PhoRC).
CC       {ECO:0000269|PubMed:11581156, ECO:0000269|PubMed:16618800}.
CC   -!- INTERACTION:
CC       Q8ST83; Q9VDY1: Ino80; NbExp=4; IntAct=EBI-125201, EBI-3414232;
CC       Q8ST83; Q9VK33: Sfmbt; NbExp=8; IntAct=EBI-125201, EBI-117801;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16618800}.
CC   -!- DEVELOPMENTAL STAGE: Maternally and zygotically expressed.
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DR   EMBL; AF034212; AAC39123.1; -; mRNA.
DR   EMBL; AE014135; AAF59378.2; -; Genomic_DNA.
DR   EMBL; AE014135; AAN06584.1; -; Genomic_DNA.
DR   EMBL; AY071143; AAL48765.1; -; mRNA.
DR   EMBL; AF433865; AAM18016.1; -; Genomic_DNA.
DR   EMBL; AF433866; AAM18017.1; -; Genomic_DNA.
DR   EMBL; AF433867; AAM18018.1; -; Genomic_DNA.
DR   EMBL; AF433868; AAM18019.1; -; Genomic_DNA.
DR   EMBL; AF433869; AAM18020.1; -; Genomic_DNA.
DR   EMBL; AF433870; AAM18021.1; -; Genomic_DNA.
DR   EMBL; AF433871; AAM18022.1; -; Genomic_DNA.
DR   EMBL; AF433872; AAM18023.1; -; Genomic_DNA.
DR   EMBL; AF433873; AAM18024.1; -; Genomic_DNA.
DR   EMBL; AF433874; AAM18025.1; -; Genomic_DNA.
DR   EMBL; AY312758; AAQ67572.1; -; Genomic_DNA.
DR   EMBL; AY312759; AAQ67573.1; -; Genomic_DNA.
DR   EMBL; AY312760; AAQ67574.1; -; Genomic_DNA.
DR   EMBL; AY312761; AAQ67575.1; -; Genomic_DNA.
DR   EMBL; AY312762; AAQ67576.1; -; Genomic_DNA.
DR   EMBL; AY312763; AAQ67577.1; -; Genomic_DNA.
DR   EMBL; AY312764; AAQ67578.1; -; Genomic_DNA.
DR   EMBL; AY312765; AAQ67579.1; -; Genomic_DNA.
DR   EMBL; AY312766; AAQ67580.1; -; Genomic_DNA.
DR   EMBL; AY312767; AAQ67581.1; -; Genomic_DNA.
DR   EMBL; AY312768; AAQ67582.1; -; Genomic_DNA.
DR   EMBL; AY312769; AAQ67583.1; -; Genomic_DNA.
DR   EMBL; AY312770; AAQ67584.1; -; Genomic_DNA.
DR   EMBL; AY312771; AAQ67585.1; -; Genomic_DNA.
DR   EMBL; AY312772; AAQ67586.1; -; Genomic_DNA.
DR   EMBL; AY312773; AAQ67587.1; -; Genomic_DNA.
DR   EMBL; AY312774; AAQ67588.1; -; Genomic_DNA.
DR   EMBL; AY312775; AAQ67589.1; -; Genomic_DNA.
DR   EMBL; AY312776; AAQ67590.1; -; Genomic_DNA.
DR   EMBL; AY312777; AAQ67591.1; -; Genomic_DNA.
DR   EMBL; AY312778; AAQ67592.1; -; Genomic_DNA.
DR   EMBL; AY312779; AAQ67593.1; -; Genomic_DNA.
DR   EMBL; AY312780; AAQ67594.1; -; Genomic_DNA.
DR   EMBL; AY312781; AAQ67595.1; -; Genomic_DNA.
DR   RefSeq; NP_524630.1; NM_079891.3.
DR   RefSeq; NP_726651.1; NM_166827.2.
DR   PDB; 4C5E; X-ray; 1.95 A; E/F/G/H=145-172.
DR   PDB; 4C5G; X-ray; 2.10 A; B=145-172.
DR   PDB; 4C5H; X-ray; 3.20 A; B=116-246.
DR   PDBsum; 4C5E; -.
DR   PDBsum; 4C5G; -.
DR   PDBsum; 4C5H; -.
DR   AlphaFoldDB; Q8ST83; -.
DR   SMR; Q8ST83; -.
DR   BioGRID; 68646; 38.
DR   ComplexPortal; CPX-2693; INO80 chromatin remodeling complex.
DR   ComplexPortal; CPX-7941; PHO transcriptional repressor complex, PHO variant.
DR   DIP; DIP-20923N; -.
DR   IntAct; Q8ST83; 19.
DR   MINT; Q8ST83; -.
DR   STRING; 7227.FBpp0088268; -.
DR   GlyGen; Q8ST83; 1 site, 1 O-linked glycan (1 site).
DR   PaxDb; 7227-FBpp0088268; -.
DR   DNASU; 43819; -.
DR   EnsemblMetazoa; FBtr0089204; FBpp0088268; FBgn0002521.
DR   EnsemblMetazoa; FBtr0089205; FBpp0088269; FBgn0002521.
DR   GeneID; 43819; -.
DR   KEGG; dme:Dmel_CG17743; -.
DR   UCSC; CG17743-RA; d. melanogaster.
DR   AGR; FB:FBgn0002521; -.
DR   CTD; 334003; -.
DR   FlyBase; FBgn0002521; pho.
DR   VEuPathDB; VectorBase:FBgn0002521; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000154763; -.
DR   HOGENOM; CLU_039881_0_0_1; -.
DR   InParanoid; Q8ST83; -.
DR   OMA; GYEMNIN; -.
DR   OrthoDB; 47408at2759; -.
DR   PhylomeDB; Q8ST83; -.
DR   Reactome; R-DME-5689603; UCH proteinases.
DR   Reactome; R-DME-5696394; DNA Damage Recognition in GG-NER.
DR   SignaLink; Q8ST83; -.
DR   BioGRID-ORCS; 43819; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 43819; -.
DR   PRO; PR:Q8ST83; -.
DR   Proteomes; UP000000803; Chromosome 4.
DR   Bgee; FBgn0002521; Expressed in cleaving embryo and 25 other cell types or tissues.
DR   Genevisible; Q8ST83; DM.
DR   GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR   GO; GO:0031011; C:Ino80 complex; IDA:FlyBase.
DR   GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR   GO; GO:0031519; C:PcG protein complex; IDA:FlyBase.
DR   GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR   GO; GO:0005703; C:polytene chromosome puff; IDA:FlyBase.
DR   GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR   GO; GO:0003682; F:chromatin binding; IDA:FlyBase.
DR   GO; GO:0031490; F:chromatin DNA binding; IDA:FlyBase.
DR   GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:FlyBase.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:FlyBase.
DR   GO; GO:0009948; P:anterior/posterior axis specification; IMP:UniProtKB.
DR   GO; GO:0006338; P:chromatin remodeling; IC:FlyBase.
DR   GO; GO:0048813; P:dendrite morphogenesis; IMP:FlyBase.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006265; P:DNA topological change; IDA:FlyBase.
DR   GO; GO:0031507; P:heterochromatin formation; IDA:FlyBase.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:FlyBase.
DR   GO; GO:0010629; P:negative regulation of gene expression; IMP:FlyBase.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IMP:FlyBase.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR   GO; GO:0045815; P:transcription initiation-coupled chromatin remodeling; IDA:UniProtKB.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 4.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR14003:SF19; TRANSCRIPTION FACTOR YY1-RELATED; 1.
DR   PANTHER; PTHR14003; TRANSCRIPTIONAL REPRESSOR PROTEIN YY; 1.
DR   Pfam; PF00096; zf-C2H2; 3.
DR   SMART; SM00355; ZnF_C2H2; 4.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 3.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE   1: Evidence at protein level;
KW   3D-structure; Developmental protein; DNA damage; DNA recombination;
KW   DNA repair; DNA-binding; Metal-binding; Nucleus; Reference proteome;
KW   Repeat; Repressor; Transcription; Transcription regulation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..520
FT                   /note="Polycomb protein PHO"
FT                   /id="PRO_0000047017"
FT   ZN_FING         357..381
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         386..408
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         414..438
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         444..468
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          475..497
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   STRAND          147..157
FT                   /evidence="ECO:0007829|PDB:4C5E"
FT   STRAND          160..169
FT                   /evidence="ECO:0007829|PDB:4C5E"
SQ   SEQUENCE   520 AA;  58224 MW;  95E729571C5194E1 CRC64;
     MAYERFGIIL QSEQYDEDIG NTKVNQKMNE GNHYDLHRKN AFDRIIHSES KKGDNVINYN
     IHENDKIKAA DNIFSSKLKM NPNMSYEMNI NCFKNIGYGE NQETSKVLTN SLSNNDINTE
     ESGVVDKNSP FLTLGTTILN SNGKSRRWEQ KLVHIKTMEG EFSVTMWASG ISDDEYSGSD
     QIVGASDLLK GKEEFGIDGF TSQQNKEYQK MESKFTNAQT LEMPHPISSV QIMDHLIKER
     GNLSQENNIS ERILSKTTLS FEEPILLPDS SSIELVNETA AMTINNHRTL SNHTGNTGDL
     HALPSSVPFR IGLHEGQVND CLSTISQSTH QDNTDSTGCG EMNLSEVTVS YTNDKKIACP
     HKGCNKHFRD SSAMRKHLHT HGPRVHVCAE CGKAFVESSK LKRHQLVHTG EKPFQCTFEG
     CGKRFSLDFN LRTHVRIHTG DRPFVCPFDA CNKKFAQSTN LKSHILTHAK AKRNTSISGK
     SGCSNAESNS QSEDTSANYV KVELQDSVTE NHVPFVVYAD
//
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