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E3 ubiquitin-protein ligase RING1 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase RING1) (Sex comb extra protein) (dRING protein) (dRING1)

 RING1_DROME             Reviewed;         435 AA.
Q9VB08; O18380;
19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
22-NOV-2017, entry version 136.
RecName: Full=E3 ubiquitin-protein ligase RING1;
EC=2.3.2.27;
AltName: Full=RING-type E3 ubiquitin transferase RING1 {ECO:0000305};
AltName: Full=Sex comb extra protein;
AltName: Full=dRING protein;
AltName: Full=dRING1;
Name=Sce; ORFNames=CG5595;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Dyer M.J., Abdul-Rauf M., White R.A.H.;
Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
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.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
IDENTIFICATION IN A PCG COMPLEX WITH PC; PH AND PSC.
PubMed=11583617; DOI=10.1016/S1097-2765(01)00316-1;
Francis N.J., Saurin A.J., Shao Z., Kingston R.E.;
"Reconstitution of a functional core polycomb repressive complex.";
Mol. Cell 8:545-556(2001).
[4]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
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., 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.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Embryo;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
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.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[6]
IDENTIFICATION IN THE PRC1 COMPLEX WITH PC; PSC AND PH.
PubMed=11493925; DOI=10.1038/35088096;
Saurin A.J., Shao Z., Erdjument-Bromage H., Tempst P., Kingston R.E.;
"A Drosophila Polycomb group complex includes Zeste and dTAFII
proteins.";
Nature 412:655-660(2001).
[7]
CHARACTERIZATION, AND MUTANT SCE33M2.
PubMed=12963114; DOI=10.1016/S0925-4773(03)00083-2;
Fritsch C., Beuchle D., Mueller J.;
"Molecular and genetic analysis of the Polycomb group gene Sex combs
extra/Ring in Drosophila.";
Mech. Dev. 120:949-954(2003).
[8]
CHARACTERIZATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
DEVELOPMENTAL STAGE, AND INTERACTION WITH PSC.
PubMed=15147763; DOI=10.1016/j.mod.2004.03.019;
Gorfinkiel N., Fanti L., Melgar T., Garcia E., Pimpinelli S.,
Guerrero I., Vidal M.;
"The Drosophila Polycomb group gene Sex combs extra encodes the
ortholog of mammalian Ring1 proteins.";
Mech. Dev. 121:449-462(2004).
[9]
FUNCTION OF THE PCG COMPLEX.
PubMed=15567868; DOI=10.1126/science.1100576;
Francis N.J., Kingston R.E., Woodcock C.L.;
"Chromatin compaction by a polycomb group protein complex.";
Science 306:1574-1577(2004).
[10]
FUNCTION OF THE PCG COMPLEX.
PubMed=14967148; DOI=10.1016/S1097-2765(04)00006-1;
Lavigne M., Francis N.J., King I.F., Kingston R.E.;
"Propagation of silencing; recruitment and repression of naive
chromatin in trans by polycomb repressed chromatin.";
Mol. Cell 13:415-425(2004).
[11]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-65.
PubMed=15386022; DOI=10.1038/nature02985;
Wang H., Wang L., Erdjument-Bromage H., Vidal M., Tempst P.,
Jones R.S., Zhang Y.;
"Role of histone H2A ubiquitination in Polycomb silencing.";
Nature 431:873-878(2004).
[12]
FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH ORD.
PubMed=14669021; DOI=10.1007/s00412-003-0266-0;
Balicky E.M., Young L., Orr-Weaver T.L., Bickel S.E.;
"A proposed role for the Polycomb group protein dRING in meiotic
sister-chromatid cohesion.";
Chromosoma 112:231-239(2004).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202; SER-266; THR-267
AND SER-269, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Embryo;
PubMed=18327897; DOI=10.1021/pr700696a;
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
J. Proteome Res. 7:1675-1682(2008).
-!- FUNCTION: E3 ubiquitin-protein ligase that mediates
monoubiquitination of 'Lys-118' of histone H2A, thereby playing a
central role in histone code and gene regulation. H2A 'Lys-118'
ubiquitination gives a specific tag for epigenetic transcriptional
repression. 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. PcG
complexes act via modification of histones, such as methylation,
deacetylation, ubiquitination rendering chromatin heritably
changed in its expressibility. May play a role in meiotic sister
chromatid cohesion. {ECO:0000269|PubMed:14669021,
ECO:0000269|PubMed:14967148, ECO:0000269|PubMed:15386022,
ECO:0000269|PubMed:15567868}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Interacts with ORD. 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 two complexes however
cooperate and interact together during the first 3 hours of
development to establish PcG silencing.
{ECO:0000269|PubMed:11493925, ECO:0000269|PubMed:11583617,
ECO:0000269|PubMed:14669021, ECO:0000269|PubMed:15147763}.
-!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Colocalizes with
ubiquitinated histone H2A. Colocalizes with Pc, Pcl, Psc, ph at
many sites on polytene chromosomes. Colocalizes with ORD on the
chromatin of primary spermatocytes during G2 of meiosis.
-!- TISSUE SPECIFICITY: Ubiquitously expressed in syncytial blastoderm
embryos. Ubiquitously expressed until stage 11. Then, it is only
expressed in the neuroectoderm. Later in embryonic development, it
is only expressed in the CNS. In larvae, it is expressed in all
imaginal disks. Expressed in the male and female gonads.
{ECO:0000269|PubMed:14669021, ECO:0000269|PubMed:15147763}.
-!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
{ECO:0000269|PubMed:15147763}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AJ001514; CAA04797.1; -; mRNA.
EMBL; AE014297; AAF56737.1; -; Genomic_DNA.
EMBL; AY058535; AAL13764.1; -; mRNA.
RefSeq; NP_477509.1; NM_058161.4.
UniGene; Dm.4170; -.
ProteinModelPortal; Q9VB08; -.
SMR; Q9VB08; -.
BioGrid; 68209; 31.
DIP; DIP-21764N; -.
IntAct; Q9VB08; 3.
MINT; MINT-860974; -.
STRING; 7227.FBpp0084614; -.
iPTMnet; Q9VB08; -.
PaxDb; Q9VB08; -.
PRIDE; Q9VB08; -.
EnsemblMetazoa; FBtr0085245; FBpp0084614; FBgn0003330.
GeneID; 43327; -.
KEGG; dme:Dmel_CG5595; -.
CTD; 43327; -.
FlyBase; FBgn0003330; Sce.
eggNOG; KOG0311; Eukaryota.
eggNOG; ENOG410XQ5G; LUCA.
GeneTree; ENSGT00390000016977; -.
InParanoid; Q9VB08; -.
KO; K10695; -.
OMA; FNQTQSQ; -.
OrthoDB; EOG091G06VO; -.
PhylomeDB; Q9VB08; -.
Reactome; R-DME-2559580; Oxidative Stress Induced Senescence.
Reactome; R-DME-3108214; SUMOylation of DNA damage response and repair proteins.
Reactome; R-DME-4570464; SUMOylation of RNA binding proteins.
Reactome; R-DME-8943724; Regulation of PTEN gene transcription.
Reactome; R-DME-8953750; Transcriptional Regulation by E2F6.
UniPathway; UPA00143; -.
GenomeRNAi; 43327; -.
PRO; PR:Q9VB08; -.
Proteomes; UP000000803; Chromosome 3R.
Bgee; FBgn0003330; -.
Genevisible; Q9VB08; DM.
GO; GO:0000790; C:nuclear chromatin; IDA:UniProtKB.
GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:FlyBase.
GO; GO:0005634; C:nucleus; IDA:FlyBase.
GO; GO:0031519; C:PcG protein complex; IDA:FlyBase.
GO; GO:0035102; C:PRC1 complex; IDA:FlyBase.
GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
GO; GO:0008270; F:zinc ion binding; ISM:FlyBase.
GO; GO:0006342; P:chromatin silencing; IDA:UniProtKB.
GO; GO:0030708; P:germarium-derived female germ-line cyst encapsulation; IMP:FlyBase.
GO; GO:0035518; P:histone H2A monoubiquitination; IMP:FlyBase.
GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
GO; GO:0007275; P:multicellular organism development; IDA:UniProtKB.
GO; GO:0022008; P:neurogenesis; IMP:FlyBase.
GO; GO:0030713; P:ovarian follicle cell stalk formation; IMP:FlyBase.
GO; GO:0045498; P:sex comb development; IDA:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0007419; P:ventral cord development; IMP:FlyBase.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR032443; RAWUL.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR017907; Znf_RING_CS.
Pfam; PF16207; RAWUL; 1.
SMART; SM00184; RING; 1.
PROSITE; PS00518; ZF_RING_1; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
Cell cycle; Chromosome; Complete proteome; Meiosis; Metal-binding;
Nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription;
Transcription regulation; Transferase; Ubl conjugation pathway; Zinc;
Zinc-finger.
CHAIN 1 435 E3 ubiquitin-protein ligase RING1.
/FTId=PRO_0000056113.
ZN_FING 46 86 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
COMPBIAS 158 171 Gly-rich.
COMPBIAS 222 299 Ser-rich.
MOD_RES 202 202 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 266 266 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 267 267 Phosphothreonine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 269 269 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MUTAGEN 65 65 R->C: In Sce33M2; induces extra sex combs
due to derepression of Ubx homeotic gene
and abolishes ability to ubiquitinate
histone H2A.
{ECO:0000269|PubMed:15386022}.
CONFLICT 176 176 A -> P (in Ref. 1; CAA04797).
{ECO:0000305}.
CONFLICT 201 201 A -> P (in Ref. 1; CAA04797).
{ECO:0000305}.
CONFLICT 279 279 K -> N (in Ref. 1; CAA04797).
{ECO:0000305}.
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


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