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Q9VB08 (RING1_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
E3 ubiquitin-protein ligase RING1

EC=6.3.2.-
Alternative name(s):
Sex comb extra protein
dRING protein
dRING1
Gene names
Name:Sce
ORF Names:CG5595
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length435 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.9 Ref.10 Ref.11 Ref.12

Pathway

Protein modification; protein ubiquitination.

Subunit structure

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. Ref.3 Ref.6 Ref.8 Ref.12

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. Ref.8 Ref.11

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. Ref.8 Ref.12

Developmental stage

Expressed both maternally and zygotically. Ref.8

Sequence similarities

Contains 1 RING-type zinc finger.

Ontologies

Keywords
   Biological processCell cycle
Meiosis
Transcription
Transcription regulation
Ubl conjugation pathway
   Cellular componentChromosome
Nucleus
   DomainZinc-finger
   LigandMetal-binding
Zinc
   Molecular functionLigase
Repressor
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processchromatin silencing

Inferred from direct assay Ref.7. Source: UniProtKB

germarium-derived female germ-line cyst encapsulation

Inferred from mutant phenotype PubMed 14993188. Source: FlyBase

histone H2A monoubiquitination

Inferred from mutant phenotype PubMed 22096074. Source: FlyBase

meiotic nuclear division

Inferred from electronic annotation. Source: UniProtKB-KW

multicellular organismal development

Inferred from direct assay PubMed 1350533. Source: UniProtKB

neurogenesis

Inferred from mutant phenotype PubMed 17287254. Source: FlyBase

ovarian follicle cell stalk formation

Inferred from mutant phenotype PubMed 14993188. Source: FlyBase

sex comb development

Inferred from direct assay PubMed 1350533. Source: UniProtKB

sister chromatid cohesion

Inferred from mutant phenotype Ref.12. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentPRC1 complex

Traceable author statement PubMed 15337121. Source: FlyBase

cohesin complex

Inferred from direct assay Ref.12. Source: UniProtKB

nucleolus

Inferred from direct assay PubMed 16272126. Source: FlyBase

nucleus

Inferred from direct assay PubMed 14630938Ref.12. Source: FlyBase

   Molecular_functionligase activity

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.12. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 435435E3 ubiquitin-protein ligase RING1
PRO_0000056113

Regions

Zinc finger46 – 8641RING-type
Compositional bias158 – 17114Gly-rich
Compositional bias222 – 29978Ser-rich

Amino acid modifications

Modified residue2021Phosphoserine Ref.13
Modified residue2661Phosphoserine Ref.13
Modified residue2671Phosphothreonine Ref.13
Modified residue2691Phosphoserine Ref.13

Experimental info

Mutagenesis651R → C in Sce33M2; induces extra sex combs due to derepression of Ubx homeotic gene and abolishes ability to ubiquitinate histone H2A. Ref.11
Sequence conflict1761A → P in CAA04797. Ref.1
Sequence conflict2011A → P in CAA04797. Ref.1
Sequence conflict2791K → N in CAA04797. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9VB08 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 5DC5834BD3CC516C

FASTA43547,256
        10         20         30         40         50         60 
MTSLDPAPNK TWELSLYELQ RKPQEVITDS TEIAVSPRSL HSELMCPICL DMLKKTMTTK 

        70         80         90        100        110        120 
ECLHRFCSDC IVTALRSGNK ECPTCRKKLV SKRSLRADPN FDLLISKIYP SREEYEAIQE 

       130        140        150        160        170        180 
KVMAKFNQTQ SQQALVNSIN EGIKLQSQNR PQRFRTKGGG GGGGGGGNGN GAANVAAPPA 

       190        200        210        220        230        240 
PGAPTAVGRN ASNQMHVHDT ASNDSNSNTN SIDRENRDPG HSGTSAASAI TSASNAAPSS 

       250        260        270        280        290        300 
SANSGASTSA TRMQVDDASN PPSVRSTPSP VPSNSSSSKP KRAMSVLTSE RSEESESDSQ 

       310        320        330        340        350        360 
MDCRTEGDSN IDTEGEGNGE LGINDEIELV FKPHPTEMSA DNQLIRALKE NCVRYIKTTA 

       370        380        390        400        410        420 
NATVDHLSKY LAMRLTLDLG ADLPEACRVL NFCIYVAPQP QQLVILNGNQ TLHQVNDKFW 

       430 
KVNKPMEMYY SWKKT 

« Hide

References

« Hide 'large scale' references
[1]Dyer M.J., Abdul-Rauf M., White R.A.H.
Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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. expand/collapse author list , 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]"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 PC; PH AND PSC.
[4]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
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. expand/collapse author list , 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.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[5]"A Drosophila full-length cDNA resource."
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.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Embryo.
[6]"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 PC; PSC AND PH.
[7]"Molecular and genetic analysis of the Polycomb group gene Sex combs extra/Ring in Drosophila."
Fritsch C., Beuchle D., Mueller J.
Mech. Dev. 120:949-954(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, MUTANT SCE33M2.
[8]"The Drosophila Polycomb group gene Sex combs extra encodes the ortholog of mammalian Ring1 proteins."
Gorfinkiel N., Fanti L., Melgar T., Garcia E., Pimpinelli S., Guerrero I., Vidal M.
Mech. Dev. 121:449-462(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INTERACTION WITH PSC.
[9]"Chromatin compaction by a polycomb group protein complex."
Francis N.J., Kingston R.E., Woodcock C.L.
Science 306:1574-1577(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE PCG COMPLEX.
[10]"Propagation of silencing; recruitment and repression of naive chromatin in trans by polycomb repressed chromatin."
Lavigne M., Francis N.J., King I.F., Kingston R.E.
Mol. Cell 13:415-425(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE PCG COMPLEX.
[11]"Role of histone H2A ubiquitination in Polycomb silencing."
Wang H., Wang L., Erdjument-Bromage H., Vidal M., Tempst P., Jones R.S., Zhang Y.
Nature 431:873-878(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-65.
[12]"A proposed role for the Polycomb group protein dRING in meiotic sister-chromatid cohesion."
Balicky E.M., Young L., Orr-Weaver T.L., Bickel S.E.
Chromosoma 112:231-239(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH ORD.
[13]"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-202; SER-266; THR-267 AND SER-269, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ001514 mRNA. Translation: CAA04797.1.
AE014297 Genomic DNA. Translation: AAF56737.1.
AY058535 mRNA. Translation: AAL13764.1.
RefSeqNP_477509.1. NM_058161.4.
UniGeneDm.4170.

3D structure databases

ProteinModelPortalQ9VB08.
SMRQ9VB08. Positions 10-109, 326-434.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid68209. 16 interactions.
DIPDIP-21764N.
IntActQ9VB08. 3 interactions.
MINTMINT-860974.

Proteomic databases

PaxDbQ9VB08.
PRIDEQ9VB08.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0085245; FBpp0084614; FBgn0003330.
GeneID43327.
KEGGdme:Dmel_CG5595.

Organism-specific databases

CTD43327.
FlyBaseFBgn0003330. Sce.

Phylogenomic databases

eggNOGNOG324386.
GeneTreeENSGT00390000016977.
InParanoidQ9VB08.
KOK10695.
OMASDCIITA.
OrthoDBEOG7NGQC3.
PhylomeDBQ9VB08.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

BgeeQ9VB08.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamPF00097. zf-C3HC4. 1 hit.
[Graphical view]
SMARTSM00184. RING. 1 hit.
[Graphical view]
PROSITEPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi43327.
NextBio833362.
PROQ9VB08.

Entry information

Entry nameRING1_DROME
AccessionPrimary (citable) accession number: Q9VB08
Secondary accession number(s): O18380
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase