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Q9VB08

- RING1_DROME

UniProt

Q9VB08 - RING1_DROME

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Protein

E3 ubiquitin-protein ligase RING1

Gene

Sce

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

Functioni

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.4 Publications

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri46 – 8641RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. ligase activity Source: UniProtKB-KW
  2. zinc ion binding Source: FlyBase

GO - Biological processi

  1. chromatin silencing Source: UniProtKB
  2. germarium-derived female germ-line cyst encapsulation Source: FlyBase
  3. histone H2A monoubiquitination Source: FlyBase
  4. meiotic nuclear division Source: UniProtKB-KW
  5. multicellular organismal development Source: UniProtKB
  6. neurogenesis Source: FlyBase
  7. ovarian follicle cell stalk formation Source: FlyBase
  8. sex comb development Source: UniProtKB
  9. sister chromatid cohesion Source: UniProtKB
  10. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Ligase, Repressor

Keywords - Biological processi

Cell cycle, Meiosis, Transcription, Transcription regulation, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase RING1 (EC:6.3.2.-)
Alternative name(s):
Sex comb extra protein
dRING protein
dRING1
Gene namesi
Name:Sce
ORF Names:CG5595
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0003330. Sce.

Subcellular locationi

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.

GO - Cellular componenti

  1. cohesin complex Source: UniProtKB
  2. nucleolus Source: FlyBase
  3. nucleus Source: FlyBase
  4. PRC1 complex Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi65 – 651R → C in Sce33M2; induces extra sex combs due to derepression of Ubx homeotic gene and abolishes ability to ubiquitinate histone H2A. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 435435E3 ubiquitin-protein ligase RING1PRO_0000056113Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei202 – 2021Phosphoserine1 Publication
Modified residuei266 – 2661Phosphoserine1 Publication
Modified residuei267 – 2671Phosphothreonine1 Publication
Modified residuei269 – 2691Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9VB08.
PRIDEiQ9VB08.

Expressioni

Tissue specificityi

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.2 Publications

Developmental stagei

Expressed both maternally and zygotically.1 Publication

Gene expression databases

BgeeiQ9VB08.

Interactioni

Subunit structurei

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.4 Publications

Protein-protein interaction databases

BioGridi68209. 16 interactions.
DIPiDIP-21764N.
IntActiQ9VB08. 3 interactions.
MINTiMINT-860974.

Structurei

3D structure databases

ProteinModelPortaliQ9VB08.
SMRiQ9VB08. Positions 10-109, 326-434.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi158 – 17114Gly-richAdd
BLAST
Compositional biasi222 – 29978Ser-richAdd
BLAST

Sequence similaritiesi

Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri46 – 8641RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG324386.
GeneTreeiENSGT00390000016977.
InParanoidiQ9VB08.
KOiK10695.
OMAiSDCIITA.
OrthoDBiEOG7NGQC3.
PhylomeDBiQ9VB08.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF00097. zf-C3HC4. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9VB08-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTSLDPAPNK TWELSLYELQ RKPQEVITDS TEIAVSPRSL HSELMCPICL
60 70 80 90 100
DMLKKTMTTK ECLHRFCSDC IVTALRSGNK ECPTCRKKLV SKRSLRADPN
110 120 130 140 150
FDLLISKIYP SREEYEAIQE KVMAKFNQTQ SQQALVNSIN EGIKLQSQNR
160 170 180 190 200
PQRFRTKGGG GGGGGGGNGN GAANVAAPPA PGAPTAVGRN ASNQMHVHDT
210 220 230 240 250
ASNDSNSNTN SIDRENRDPG HSGTSAASAI TSASNAAPSS SANSGASTSA
260 270 280 290 300
TRMQVDDASN PPSVRSTPSP VPSNSSSSKP KRAMSVLTSE RSEESESDSQ
310 320 330 340 350
MDCRTEGDSN IDTEGEGNGE LGINDEIELV FKPHPTEMSA DNQLIRALKE
360 370 380 390 400
NCVRYIKTTA NATVDHLSKY LAMRLTLDLG ADLPEACRVL NFCIYVAPQP
410 420 430
QQLVILNGNQ TLHQVNDKFW KVNKPMEMYY SWKKT
Length:435
Mass (Da):47,256
Last modified:May 1, 2000 - v1
Checksum:i5DC5834BD3CC516C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti176 – 1761A → P in CAA04797. 1 PublicationCurated
Sequence conflicti201 – 2011A → P in CAA04797. 1 PublicationCurated
Sequence conflicti279 – 2791K → N in CAA04797. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ001514 mRNA. Translation: CAA04797.1.
AE014297 Genomic DNA. Translation: AAF56737.1.
AY058535 mRNA. Translation: AAL13764.1.
RefSeqiNP_477509.1. NM_058161.4.
UniGeneiDm.4170.

Genome annotation databases

EnsemblMetazoaiFBtr0085245; FBpp0084614; FBgn0003330.
GeneIDi43327.
KEGGidme:Dmel_CG5595.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ001514 mRNA. Translation: CAA04797.1 .
AE014297 Genomic DNA. Translation: AAF56737.1 .
AY058535 mRNA. Translation: AAL13764.1 .
RefSeqi NP_477509.1. NM_058161.4.
UniGenei Dm.4170.

3D structure databases

ProteinModelPortali Q9VB08.
SMRi Q9VB08. Positions 10-109, 326-434.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 68209. 16 interactions.
DIPi DIP-21764N.
IntActi Q9VB08. 3 interactions.
MINTi MINT-860974.

Proteomic databases

PaxDbi Q9VB08.
PRIDEi Q9VB08.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0085245 ; FBpp0084614 ; FBgn0003330 .
GeneIDi 43327.
KEGGi dme:Dmel_CG5595.

Organism-specific databases

CTDi 43327.
FlyBasei FBgn0003330. Sce.

Phylogenomic databases

eggNOGi NOG324386.
GeneTreei ENSGT00390000016977.
InParanoidi Q9VB08.
KOi K10695.
OMAi SDCIITA.
OrthoDBi EOG7NGQC3.
PhylomeDBi Q9VB08.

Enzyme and pathway databases

UniPathwayi UPA00143 .

Miscellaneous databases

GenomeRNAii 43327.
NextBioi 833362.
PROi Q9VB08.

Gene expression databases

Bgeei Q9VB08.

Family and domain databases

Gene3Di 3.30.40.10. 1 hit.
InterProi IPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view ]
Pfami PF00097. zf-C3HC4. 1 hit.
[Graphical view ]
SMARTi SM00184. RING. 1 hit.
[Graphical view ]
PROSITEi PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  5. 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.

Entry informationi

Entry nameiRING1_DROME
AccessioniPrimary (citable) accession number: Q9VB08
Secondary accession number(s): O18380
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: May 1, 2000
Last modified: October 29, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3