Q9VB08 (RING1_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Drosophila melanogaster (Fruit fly)

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	435 AA.
Sequence status	Complete.
Protein existence	Evidence 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.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 process	Cell cycle Meiosis Transcription Transcription regulation Ubl conjugation pathway
Cellular component	Chromosome Nucleus
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Ligase Repressor
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	chromatin silencing Inferred from direct assay Ref.7. Source: UniProtKB germarium-derived female germ-line cyst encapsulation Inferred from mutant phenotype. Source: FlyBase meiosis Inferred from electronic annotation. Source: UniProtKB-KW neurogenesis Inferred from mutant phenotype. Source: FlyBase ovarian follicle cell stalk formation Inferred from mutant phenotype. Source: FlyBase sex comb development Inferred from direct assay. Source: UniProtKB sister chromatid cohesion Inferred from mutant phenotype Ref.12. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	PRC1 complex Traceable author statement. Source: FlyBase cohesin complex Inferred from direct assay Ref.12. Source: UniProtKB
Molecular function	ligase 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 435	435	E3 ubiquitin-protein ligase RING1		PRO_0000056113
Regions
	Zinc finger	46 – 86	41	RING-type
	Compositional bias	158 – 171	14	Gly-rich
	Compositional bias	222 – 299	78	Ser-rich
Amino acid modifications
	Modified residue	202	1	Phosphoserine Ref.13
	Modified residue	266	1	Phosphoserine Ref.13
	Modified residue	267	1	Phosphothreonine Ref.13
	Modified residue	269	1	Phosphoserine Ref.13
Experimental info
	Mutagenesis	65	1	R → C in Sce33M2; induces extra sex combs due to derepression of Ubx homeotic gene and abolishes ability to ubiquitinate histone H2A. Ref.11
	Sequence conflict	176	1	A → P in CAA04797. Ref.1
	Sequence conflict	201	1	A → P in CAA04797. Ref.1
	Sequence conflict	279	1	K → N in CAA04797. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9VB08 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 5DC5834BD3CC516C	FASTA	435	47,256
	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

References

	« Hide 'large scale' referencesShow '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. , 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: 10731132] [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: 11583617] [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. , 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: 12537572] [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: 12537569] [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: 11493925] [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: 12963114] [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: 15147763] [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: 15567868] [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: 14967148] [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: 15386022] [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: 14669021] [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: 18327897] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202; SER-266; THR-267 AND SER-269, 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.
RefSeq	NP_477509.1. NM_058161.3.
UniGene	Dm.4170.
3D structure databases
ProteinModelPortal	Q9VB08.
SMR	Q9VB08. Positions 10-109, 324-434.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-21764N.
IntAct	Q9VB08. 3 interactions.
MINT	MINT-860974.
STRING	Q9VB08.
Proteomic databases
PRIDE	Q9VB08.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0085245; FBpp0084614; FBgn0003330.
GeneID	43327.
KEGG	dme:Dmel_CG5595.
NMPDR	fig|7227.3.peg.15018.
Organism-specific databases
CTD	43327.
FlyBase	FBgn0003330. Sce.
Phylogenomic databases
eggNOG	inNOG06540.
GeneTree	EMGT00050000002115.
InParanoid	Q9VB08.
OMA	CSNASVH.
OrthoDB	EOG489332.
PhylomeDB	Q9VB08.
Gene expression databases
ArrayExpress	Q9VB08.
Bgee	Q9VB08.
GermOnline	CG5595. Drosophila melanogaster.
Family and domain databases
InterPro	IPR018957. Znf_C3HC4_RING-type. IPR001841. Znf_RING. IPR013083. Znf_RING/FYVE/PHD. IPR017907. Znf_RING_CS. [Graphical view]
Gene3D	G3DSA:3.30.40.10. Znf_RING/FYVE/PHD. 1 hit.
KO	K10695.
Pfam	PF00097. zf-C3HC4. 1 hit. [Graphical view]
SMART	SM00184. RING. 1 hit. [Graphical view]
PROSITE	PS00518. ZF_RING_1. 1 hit. PS50089. ZF_RING_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	833362.

Entry information

Entry name

RING1_DROME

Accession

Primary (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:	January 25, 2012
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project