RING1_DROME
ID RING1_DROME Reviewed; 435 AA.
AC Q9VB08; O18380;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=E3 ubiquitin-protein ligase RING1;
DE EC=2.3.2.27;
DE AltName: Full=RING-type E3 ubiquitin transferase RING1 {ECO:0000305};
DE AltName: Full=Sex comb extra protein;
DE AltName: Full=dRING protein;
DE AltName: Full=dRING1;
GN Name=Sce; ORFNames=CG5595;
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].
RA Dyer M.J., Abdul-Rauf M., White R.A.H.;
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
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 IDENTIFICATION IN A PCG COMPLEX WITH PC; PH AND PSC.
RX PubMed=11583617; DOI=10.1016/s1097-2765(01)00316-1;
RA Francis N.J., Saurin A.J., Shao Z., Kingston R.E.;
RT "Reconstitution of a functional core polycomb repressive complex.";
RL Mol. Cell 8:545-556(2001).
RN [4]
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 [5]
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 [6]
RP IDENTIFICATION IN THE PRC1 COMPLEX WITH PC; PSC AND PH.
RX PubMed=11493925; DOI=10.1038/35088096;
RA Saurin A.J., Shao Z., Erdjument-Bromage H., Tempst P., Kingston R.E.;
RT "A Drosophila Polycomb group complex includes Zeste and dTAFII proteins.";
RL Nature 412:655-660(2001).
RN [7]
RP CHARACTERIZATION, AND MUTANT SCE33M2.
RX PubMed=12963114; DOI=10.1016/s0925-4773(03)00083-2;
RA Fritsch C., Beuchle D., Mueller J.;
RT "Molecular and genetic analysis of the Polycomb group gene Sex combs
RT extra/Ring in Drosophila.";
RL Mech. Dev. 120:949-954(2003).
RN [8]
RP CHARACTERIZATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND INTERACTION WITH PSC.
RX PubMed=15147763; DOI=10.1016/j.mod.2004.03.019;
RA Gorfinkiel N., Fanti L., Melgar T., Garcia E., Pimpinelli S., Guerrero I.,
RA Vidal M.;
RT "The Drosophila Polycomb group gene Sex combs extra encodes the ortholog of
RT mammalian Ring1 proteins.";
RL Mech. Dev. 121:449-462(2004).
RN [9]
RP FUNCTION OF THE PCG COMPLEX.
RX PubMed=15567868; DOI=10.1126/science.1100576;
RA Francis N.J., Kingston R.E., Woodcock C.L.;
RT "Chromatin compaction by a polycomb group protein complex.";
RL Science 306:1574-1577(2004).
RN [10]
RP FUNCTION OF THE PCG COMPLEX.
RX PubMed=14967148; DOI=10.1016/s1097-2765(04)00006-1;
RA Lavigne M., Francis N.J., King I.F., Kingston R.E.;
RT "Propagation of silencing; recruitment and repression of naive chromatin in
RT trans by polycomb repressed chromatin.";
RL Mol. Cell 13:415-425(2004).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-65.
RX PubMed=15386022; DOI=10.1038/nature02985;
RA Wang H., Wang L., Erdjument-Bromage H., Vidal M., Tempst P., Jones R.S.,
RA Zhang Y.;
RT "Role of histone H2A ubiquitination in Polycomb silencing.";
RL Nature 431:873-878(2004).
RN [12]
RP FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH ORD.
RX PubMed=14669021; DOI=10.1007/s00412-003-0266-0;
RA Balicky E.M., Young L., Orr-Weaver T.L., Bickel S.E.;
RT "A proposed role for the Polycomb group protein dRING in meiotic sister-
RT chromatid cohesion.";
RL Chromosoma 112:231-239(2004).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202; SER-266; THR-267 AND
RP SER-269, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that mediates monoubiquitination
CC of 'Lys-118' of histone H2A, thereby playing a central role in histone
CC code and gene regulation. H2A 'Lys-118' ubiquitination gives a specific
CC tag for epigenetic transcriptional repression. Polycomb group (PcG)
CC protein. PcG proteins act by forming multiprotein complexes, which are
CC required to maintain the transcriptionally repressive state of homeotic
CC genes throughout development. PcG proteins are not required to initiate
CC repression, but to maintain it during later stages of development. PcG
CC complexes act via modification of histones, such as methylation,
CC deacetylation, ubiquitination rendering chromatin heritably changed in
CC its expressibility. May play a role in meiotic sister chromatid
CC cohesion. {ECO:0000269|PubMed:14669021, ECO:0000269|PubMed:14967148,
CC ECO:0000269|PubMed:15386022, ECO:0000269|PubMed:15567868}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with ORD. Component of PRC1 complex, which contains
CC many PcG proteins like Pc, ph, Scm, Psc, Sce and also chromatin
CC remodeling proteins such as histone deacetylases. This complex is
CC distinct from the Esc/E(z) complex, at least composed of esc, E(z),
CC Su(z)12, HDAC1/Rpd3 and Caf1-55. The two complexes however cooperate
CC and interact together during the first 3 hours of development to
CC establish PcG silencing. {ECO:0000269|PubMed:11493925,
CC ECO:0000269|PubMed:11583617, ECO:0000269|PubMed:14669021,
CC ECO:0000269|PubMed:15147763}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Colocalizes with
CC ubiquitinated histone H2A. Colocalizes with Pc, Pcl, Psc, ph at many
CC sites on polytene chromosomes. Colocalizes with ORD on the chromatin of
CC primary spermatocytes during G2 of meiosis.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in syncytial blastoderm
CC embryos. Ubiquitously expressed until stage 11. Then, it is only
CC expressed in the neuroectoderm. Later in embryonic development, it is
CC only expressed in the CNS. In larvae, it is expressed in all imaginal
CC disks. Expressed in the male and female gonads.
CC {ECO:0000269|PubMed:14669021, ECO:0000269|PubMed:15147763}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:15147763}.
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DR EMBL; AJ001514; CAA04797.1; -; mRNA.
DR EMBL; AE014297; AAF56737.1; -; Genomic_DNA.
DR EMBL; AY058535; AAL13764.1; -; mRNA.
DR RefSeq; NP_477509.1; NM_058161.4.
DR AlphaFoldDB; Q9VB08; -.
DR SMR; Q9VB08; -.
DR BioGRID; 68209; 35.
DR DIP; DIP-21764N; -.
DR IntAct; Q9VB08; 3.
DR STRING; 7227.FBpp0084614; -.
DR iPTMnet; Q9VB08; -.
DR PaxDb; Q9VB08; -.
DR DNASU; 43327; -.
DR EnsemblMetazoa; FBtr0085245; FBpp0084614; FBgn0003330.
DR GeneID; 43327; -.
DR KEGG; dme:Dmel_CG5595; -.
DR CTD; 43327; -.
DR FlyBase; FBgn0003330; Sce.
DR VEuPathDB; VectorBase:FBgn0003330; -.
DR eggNOG; KOG0311; Eukaryota.
DR HOGENOM; CLU_056557_1_1_1; -.
DR InParanoid; Q9VB08; -.
DR OMA; XYIKTSG; -.
DR OrthoDB; 1319463at2759; -.
DR PhylomeDB; Q9VB08; -.
DR Reactome; R-DME-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-DME-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-DME-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-DME-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-DME-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR Reactome; R-DME-8943724; Regulation of PTEN gene transcription.
DR Reactome; R-DME-8953750; Transcriptional Regulation by E2F6.
DR SignaLink; Q9VB08; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 43327; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 43327; -.
DR PRO; PR:Q9VB08; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0003330; Expressed in adult abdomen and 41 other tissues.
DR Genevisible; Q9VB08; DM.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0031519; C:PcG protein complex; IDA:FlyBase.
DR GO; GO:0035102; C:PRC1 complex; IDA:FlyBase.
DR GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:FlyBase.
DR GO; GO:0008270; F:zinc ion binding; ISM:FlyBase.
DR GO; GO:0009948; P:anterior/posterior axis specification; IMP:UniProtKB.
DR GO; GO:0030708; P:germarium-derived female germ-line cyst encapsulation; IMP:FlyBase.
DR GO; GO:0031507; P:heterochromatin assembly; IDA:UniProtKB.
DR GO; GO:0035518; P:histone H2A monoubiquitination; IMP:FlyBase.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0022008; P:neurogenesis; IMP:FlyBase.
DR GO; GO:0030713; P:ovarian follicle cell stalk formation; IMP:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0007419; P:ventral cord development; HMP:FlyBase.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR032443; RAWUL.
DR InterPro; IPR043540; RING1/RING2.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR46076; PTHR46076; 3.
DR Pfam; PF16207; RAWUL; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Chromosome; Meiosis; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..435
FT /note="E3 ubiquitin-protein ligase RING1"
FT /id="PRO_0000056113"
FT ZN_FING 46..86
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 144..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..311
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 266
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 267
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MUTAGEN 65
FT /note="R->C: In Sce33M2; induces extra sex combs due to
FT derepression of Ubx homeotic gene and abolishes ability to
FT ubiquitinate histone H2A."
FT /evidence="ECO:0000269|PubMed:15386022"
FT CONFLICT 176
FT /note="A -> P (in Ref. 1; CAA04797)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="A -> P (in Ref. 1; CAA04797)"
FT /evidence="ECO:0000305"
FT CONFLICT 279
FT /note="K -> N (in Ref. 1; CAA04797)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 435 AA; 47256 MW; 5DC5834BD3CC516C CRC64;
MTSLDPAPNK TWELSLYELQ RKPQEVITDS TEIAVSPRSL HSELMCPICL DMLKKTMTTK
ECLHRFCSDC IVTALRSGNK ECPTCRKKLV SKRSLRADPN FDLLISKIYP SREEYEAIQE
KVMAKFNQTQ SQQALVNSIN EGIKLQSQNR PQRFRTKGGG GGGGGGGNGN GAANVAAPPA
PGAPTAVGRN ASNQMHVHDT ASNDSNSNTN SIDRENRDPG HSGTSAASAI TSASNAAPSS
SANSGASTSA TRMQVDDASN PPSVRSTPSP VPSNSSSSKP KRAMSVLTSE RSEESESDSQ
MDCRTEGDSN IDTEGEGNGE LGINDEIELV FKPHPTEMSA DNQLIRALKE NCVRYIKTTA
NATVDHLSKY LAMRLTLDLG ADLPEACRVL NFCIYVAPQP QQLVILNGNQ TLHQVNDKFW
KVNKPMEMYY SWKKT
