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Q9CQJ4 (RING2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
E3 ubiquitin-protein ligase RING2

EC=6.3.2.-
Alternative name(s):
RING finger protein 1B
Short name=RING1b
RING finger protein 2
Gene names
Name:Rnf2
Synonyms:DinG, Ring1b
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length336 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

E3 ubiquitin-protein ligase that mediates monoubiquitination of 'Lys-119' of histone H2A (H2AK119Ub), thereby playing a central role in histone code and gene regulation. H2AK119Ub gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. May be involved in the initiation of both imprinted and random X inactivation. Essential component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones, rendering chromatin heritably changed in its expressibility. E3 ubiquitin-protein ligase activity is enhanced by BMI1/PCGF4. Acts as the main E3 ubiquitin ligase on histone H2A of the PRC1 complex, while RING1 may rather act as a modulator of RNF2/RING2 activity. Association to the chromosomal DNA is cell-cycle dependent. In resting B- and T-lymphocytes, interaction with AURKB leads to block its activity, thereby maintaining transcription in resting lymphocytes. Ref.6 Ref.7 Ref.12 Ref.13

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Part of the E2F6.com-1 complex in G0 phase composed of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EUHMTASE1, RNF1/RING1, RNF2/RING2, MBLR, L3MBTL2 and YAF2. Component of a PRC1-like complex. Component of some MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Interacts with RYBP, HIP2 and TFCP2. Association to the chromosomal DNA is cell-cycle dependent. Interacts with CBX4, CBX6, CBX7 and CBX8. Component of repressive BCOR complex containing Polycomb group subcomplex at least composed of RYBP, PCGF1, BCOR and RING1 By similarity. Component of chromatin-associated Polycomb (PcG) complexes. Interacts with RYBP, PCGF2, CBX2, RNF1/RING1, BMI1, PHC1 and PHC2. Interacts with CHTOP. Interacts with AURKB. Ref.1 Ref.5 Ref.6 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13

Subcellular location

Nucleus. Chromosome. Note: Enriched on inactive X chromosome (Xi) in female trophoblast stem (TS) cells as well as differentiating embryonic stem (ES) cells. The enrichment on Xi is transient during TS and ES cell differentiation. The association with Xi is mitotically stable in non-differentiated TS cells. Ref.6 Ref.8

Post-translational modification

Polyubiquitinated in the presence of UBE2D3 (in vitro).

Monoubiquitinated, by auto-ubiquitination.

Sequence similarities

Contains 1 RING-type zinc finger.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
Ubl conjugation pathway
   Cellular componentChromosome
Nucleus
   DomainZinc-finger
   LigandMetal-binding
Zinc
   Molecular functionLigase
Repressor
   PTMAcetylation
Isopeptide bond
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processanterior/posterior axis specification

Inferred from mutant phenotype Ref.6. Source: MGI

gastrulation with mouth forming second

Inferred from mutant phenotype PubMed 12589020. Source: MGI

histone H2A-K119 monoubiquitination

Inferred from mutant phenotype Ref.12. Source: UniProtKB

histone ubiquitination

Inferred from direct assay PubMed 16359901. Source: MGI

mitotic cell cycle

Inferred from mutant phenotype PubMed 12589020. Source: MGI

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype Ref.12. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentMLL1 complex

Inferred from sequence or structural similarity. Source: UniProtKB

PRC1 complex

Inferred from electronic annotation. Source: Ensembl

PcG protein complex

Inferred from direct assay PubMed 16359901PubMed 16624538. Source: MGI

euchromatin

Inferred from direct assay PubMed 18311137. Source: MGI

heterochromatin

Inferred from direct assay PubMed 18311137. Source: MGI

nuclear body

Inferred from direct assay Ref.6. Source: MGI

nucleus

Inferred from direct assay PubMed 14557078. Source: MGI

sex chromatin

Inferred from direct assay Ref.7. Source: MGI

ubiquitin ligase complex

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionchromatin binding

Inferred from direct assay Ref.6PubMed 15741318PubMed 16687444. Source: MGI

ubiquitin-protein ligase activity

Inferred from direct assay PubMed 16359901. Source: MGI

zinc ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 336335E3 ubiquitin-protein ligase RING2
PRO_0000056039

Regions

Zinc finger51 – 9141RING-type
Region2 – 179178Interaction with HIP2 By similarity

Amino acid modifications

Modified residue21N-acetylserine By similarity
Cross-link112Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

Experimental info

Sequence conflict2531N → H in BAC41075. Ref.2
Sequence conflict2991S → T in BAC41075. Ref.2
Sequence conflict3041V → L in BAC41075. Ref.2
Sequence conflict332 – 3365TKEHK → FTASGNVR in CAA73380. Ref.1

Secondary structure

..................... 336
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9CQJ4 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 84BA5B3E044DB7EC

FASTA33637,623
        10         20         30         40         50         60 
MSQAVQTNGT QPLSKTWELS LYELQRTPQE AITDGLEIVV SPRSLHSELM CPICLDMLKN 

        70         80         90        100        110        120 
TMTTKECLHR FCADCIITAL RSGNKECPTC RKKLVSKRSL RPDPNFDALI SKIYPSRDEY 

       130        140        150        160        170        180 
EAHQERVLAR INKHNNQQAL SHSIEEGLKI QAMNRLQRGK KQQIENGSGA EDNGDSSHCS 

       190        200        210        220        230        240 
NASTHSNQEA GPSNKRTKTS DDSGLELDNN NAAVAIDPVM DGASEIELVF RPHPTLMEKD 

       250        260        270        280        290        300 
DSAQTRYIKT SGNATVDHLS KYLAVRLALE ELRSKGESNQ MNLDTASEKQ YTIYIATASG 

       310        320        330 
QFTVLNGSFS LELVSEKYWK VNKPMELYYA PTKEHK 

« Hide

References

« Hide 'large scale' references
[1]"Ring1A is a transcriptional repressor that interacts with the Polycomb-M33 protein and is expressed at rhombomere boundaries in the mouse hindbrain."
Schoorlemmer J., Marcos-Gutierrez C., Were F., Martinez R., Garcia E., Satijn D.P.E., Otte A.P., Vidal M.
EMBO J. 16:5930-5942(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH CBX2.
Strain: NIH Swiss.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: B-cell and Ovary.
[3]"Cloning of mouse full open reading frames in Gateway(R) system entry vector (pDONR201)."
Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J., Wiemann S., Schick M., Korn B.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Czech II.
Tissue: Mammary tumor.
[5]"RYBP, a new repressor protein that interacts with components of the mammalian Polycomb complex, and with the transcription factor YY1."
Garcia E., Marcos-Gutierrez C., del Mar Lorente M., Moreno J.C., Vidal M.
EMBO J. 18:3404-3418(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RYBP AND RING1.
[6]"Involvement of the Polycomb-group gene Ring1B in the specification of the anterior-posterior axis in mice."
Suzuki M., Mizutani-Koseki Y., Fujimura Y., Miyagishima H., Kaneko T., Takada Y., Akasaka T., Tanzawa H., Takihara Y., Nakano M., Masumoto H., Vidal M., Isono K., Koseki H.
Development 129:4171-4183(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CBX2; PCGF2; PHC1; PHC2; RNF1 AND BMI1, FUNCTION, SUBCELLULAR LOCATION.
[7]"Polycomb group proteins Ring1A/B link ubiquitylation of histone H2A to heritable gene silencing and X inactivation."
de Napoles M., Mermoud J.E., Wakao R., Tang Y.A., Endoh M., Appanah R., Nesterova T.B., Silva J., Otte A.P., Vidal M., Koseki H., Brockdorff N.
Dev. Cell 7:663-676(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME ACTIVITY, FUNCTION.
[8]"Ring1b-mediated H2A ubiquitination associates with inactive X chromosomes and is involved in initiation of X inactivation."
Fang J., Chen T., Chadwick B., Li E., Zhang Y.
J. Biol. Chem. 279:52812-52815(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[9]"Mammalian polyhomeotic homologues Phc2 and Phc1 act in synergy to mediate polycomb repression of Hox genes."
Isono K., Fujimura Y., Shinga J., Yamaki M., O-Wang J., Takihara Y., Murahashi Y., Takada Y., Mizutani-Koseki Y., Koseki H.
Mol. Cell. Biol. 25:6694-6706(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PHC2.
[10]"The transcriptional repressor RYBP is a natively unfolded protein which folds upon binding to DNA."
Neira J.L., Roman-Trufero M., Contreras L.M., Prieto J., Singh G., Barrera F.N., Renart M.L., Vidal M.
Biochemistry 48:1348-1360(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RYBP.
[11]"Five friends of methylated chromatin target of protein-arginine-methyltransferase[prmt]-1 (chtop), a complex linking arginine methylation to desumoylation."
Fanis P., Gillemans N., Aghajanirefah A., Pourfarzad F., Demmers J., Esteghamat F., Vadlamudi R.K., Grosveld F., Philipsen S., van Dijk T.B.
Mol. Cell. Proteomics 11:1263-1273(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CHTOP.
[12]"The Aurora B kinase and the Polycomb protein Ring1B combine to regulate active promoters in quiescent lymphocytes."
Frangini A., Sjoberg M., Roman-Trufero M., Dharmalingam G., Haberle V., Bartke T., Lenhard B., Malumbres M., Vidal M., Dillon N.
Mol. Cell 51:647-661(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH AURKB.
[13]"Structure and E3-ligase activity of the Ring-Ring complex of polycomb proteins Bmi1 and Ring1b."
Buchwald G., van der Stoop P., Weichenrieder O., Perrakis A., van Lohuizen M., Sixma T.K.
EMBO J. 25:2465-2474(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-159 IN COMPLEX WITH BMI1 AND ZINC IONS, FUNCTION, MONOUBIQUITINATION, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y12880 mRNA. Translation: CAA73380.1.
Y12783 mRNA. Translation: CAA73321.1.
AK145767 mRNA. Translation: BAE26638.1.
AK012358 mRNA. Translation: BAB28186.1.
AK013124 mRNA. Translation: BAB28663.1.
AK030319 mRNA. Translation: BAC26898.1.
AK090066 mRNA. Translation: BAC41075.1.
CT010297 mRNA. Translation: CAJ18505.1.
BC020122 mRNA. Translation: AAH20122.1.
RefSeqNP_035407.1. NM_011277.2.
UniGeneMm.474038.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CKLX-ray2.00B1-159[»]
ProteinModelPortalQ9CQJ4.
SMRQ9CQJ4. Positions 15-114, 223-333.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202919. 121 interactions.
IntActQ9CQJ4. 57 interactions.
MINTMINT-1341250.
STRING10090.ENSMUSP00000075476.

PTM databases

PhosphoSiteQ9CQJ4.

Proteomic databases

PaxDbQ9CQJ4.
PRIDEQ9CQJ4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000076110; ENSMUSP00000075476; ENSMUSG00000026484.
GeneID19821.
KEGGmmu:19821.
UCSCuc007cyx.1. mouse.

Organism-specific databases

CTD6045.
MGIMGI:1101759. Rnf2.

Phylogenomic databases

eggNOGNOG324386.
GeneTreeENSGT00390000016977.
HOGENOMHOG000273917.
HOVERGENHBG079942.
InParanoidQ9CQJ4.
KOK10695.
OMASDCIITA.
OrthoDBEOG7NGQC3.
PhylomeDBQ9CQJ4.
TreeFamTF105501.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

BgeeQ9CQJ4.
CleanExMM_RNF2.
GenevestigatorQ9CQJ4.

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

EvolutionaryTraceQ9CQJ4.
NextBio297285.
PROQ9CQJ4.
SOURCESearch...

Entry information

Entry nameRING2_MOUSE
AccessionPrimary (citable) accession number: Q9CQJ4
Secondary accession number(s): O35699 expand/collapse secondary AC list , O35729, Q4FJV5, Q8C1X8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot