Q9CQJ4 · RING2_MOUSE

  • Protein
    E3 ubiquitin-protein ligase RING2
  • Gene
    Rnf2
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

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 (PubMed:15525528, PubMed:22325148, PubMed:28596365).
H2AK119Ub gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals (PubMed:15525528, PubMed:28596365).
May be involved in the initiation of both imprinted and random X inactivation (PubMed:15525528).
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 (PubMed:16710298, PubMed:22325148).
PcG PRC1 complex acts via chromatin remodeling and modification of histones, rendering chromatin heritably changed in its expressibility (PubMed:15525528, PubMed:16710298, PubMed:22325148).
E3 ubiquitin-protein ligase activity is enhanced by BMI1/PCGF4 (PubMed:16710298).
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 (PubMed:15525528, PubMed:16710298).
Plays a role in the transcriptional repression of genes that are required for pluripotency in embryonic stem cells, thereby contributing to differentiation of the ectodermal and endodermal germ layers (PubMed:22226355).
Association with 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 (PubMed:24034696).
Also acts as a negative regulator of autophagy by mediating ubiquitination of AMBRA1, leading to its subsequent degradation (PubMed:24980959).

Catalytic activity

  • S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine.
    EC:2.3.2.27 (UniProtKB | ENZYME | Rhea)

Pathway

Protein modification; protein ubiquitination.

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componenteuchromatin
Cellular Componentheterochromatin
Cellular ComponentMLL1 complex
Cellular Componentnuclear body
Cellular Componentnucleus
Cellular ComponentPcG protein complex
Cellular ComponentPRC1 complex
Cellular Componentsex chromatin
Cellular Componentubiquitin ligase complex
Molecular Functionchromatin binding
Molecular Functionhistone H2AK119 ubiquitin ligase activity
Molecular FunctionRING-like zinc finger domain binding
Molecular Functionubiquitin protein ligase activity
Molecular Functionzinc ion binding
Biological Processanterior/posterior axis specification
Biological Processchromatin organization
Biological Processepigenetic regulation of gene expression
Biological Processgastrulation with mouth forming second
Biological Processgene expression
Biological Processgerm cell development
Biological Processmitotic cell cycle
Biological Processnegative regulation of transcription by RNA polymerase II
Biological Processprotein ubiquitination

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    E3 ubiquitin-protein ligase RING2
  • EC number
  • Alternative names
    • RING finger protein 1B (RING1b)
    • RING finger protein 2
    • RING-type E3 ubiquitin transferase RING2

Gene names

    • Name
      Rnf2
    • Synonyms
      DinG, Ring1b

Organism names

  • Taxonomic identifier
  • Strains
    • NIH Swiss
    • C57BL/6J
    • Czech II
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q9CQJ4
  • Secondary accessions
    • O35699
    • O35729
    • Q4FJV5
    • Q8C1X8

Proteomes

Organism-specific databases

Subcellular Location

Nucleus
Cytoplasm
Chromosome
Note: Enriched on inactive X chromosome (Xi) in female trophoblast stem (TS) cells as well as differentiating embryonic stem (ES) cells (PubMed:12183370).
The enrichment on Xi is transient during TS and ES cell differentiation. The association with Xi is mitotically stable in non-differentiated TS cells (PubMed:12183370).
Co-localizes with SAMD7 in nuclear polycomb bodies (PubMed:28900001).

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis69Loss of ubiquitin ligase activity.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 23 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain, cross-link.

TypeIDPosition(s)Description
Initiator methionine1Removed
Modified residue2N-acetylserine
ChainPRO_00000560392-336E3 ubiquitin-protein ligase RING2
Modified residue41Phosphoserine
Cross-link112Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Modified residue143Phosphoserine
Modified residue168Phosphoserine
Cross-link249Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link323Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)

Post-translational modification

Monoubiquitinated, by auto-ubiquitination (PubMed:16710298).
Polyubiquitinated in the presence of UBE2D3 (in vitro) (By similarity).

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed in embryonic stem cells.

Gene expression databases

Interaction

Subunit

Component of chromatin-associated Polycomb (PcG) complexes (PubMed:22325148).
Component of a number of PRC1-like complexes; these complexes contain either the polycomb group ring finger protein PCGF1, or PCGF2, or PCGF3, or BMI1, or PCGF5, or PCGF6 (PubMed:16710298, PubMed:28596365).
Distinct PRC1-like complexes are composed of a RING1 subunit (RING1B or RING1A), one of the six PCGF proteins (PCGF1, PCGF2, PCGF3, BMI1, PCGF5 or PCGF6), one PHC protein (PHC1, PHC2 or PHC3) and one of the CBX proteins (CBX2, CBX4, CBX6, CBX7 or CBX8) (Probable). Part of a complex that contains RNF2, UB2D3 and BMI1; within that complex RNF2 and BMI1 form a tight heterodimer, where UB2D3 interacts only with RNF2. The complex composed of RNF2, UB2D3 and BMI1 binds nucleosomes, and has activity only with nucleosomal histone H2A (By similarity).
Part of a complex that contains PCGF5, RNF2 and UBE2D3. Part of a complex that contains AUTS2, PCGF5, RNF2, CSNK2B and RYBP (By similarity).
Interacts with CBX6 and CBX8 (By similarity).
Interacts with PHC1, PCGF2, RYBP, CBX7, CBX4, CBX2, RNF1/RING1, BMI1 and PHC2 (PubMed:10369680, PubMed:12183370, PubMed:16024804, PubMed:16710298, PubMed:19170609, PubMed:22226355, PubMed:22325148, PubMed:9312051).
Interaction with RYBP and CBX7 is mutually exclusive; both compete for the same binding site on RNF2 (PubMed:22325148).
Component of repressive BCOR complex containing a Polycomb group subcomplex at least composed of RYBP, PCGF1, BCOR and RING1 (By similarity).
Interacts with CBX2 and PHC1 (PubMed:22226355).
Interacts with CHTOP (PubMed:22872859).
Interacts with AURKB (PubMed:24034696).
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 (By similarity).
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 (By similarity).
Interacts with NUPR1 (By similarity).
Interacts with SAMD7 in a PHC2-dependent manner (PubMed:28900001).

Binary interactions

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for region, zinc finger, compositional bias.

TypeIDPosition(s)Description
Region2-179Interaction with HIP2
Zinc finger51-91RING-type
Region93-98Interaction with nucleosomes via an acidic patch on histone H2A and histone H2B
Compositional bias157-194Polar residues
Region157-206Disordered

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    336
  • Mass (Da)
    37,623
  • Last updated
    2001-06-01 v1
  • Checksum
    84BA5B3E044DB7EC
MSQAVQTNGTQPLSKTWELSLYELQRTPQEAITDGLEIVVSPRSLHSELMCPICLDMLKNTMTTKECLHRFCADCIITALRSGNKECPTCRKKLVSKRSLRPDPNFDALISKIYPSRDEYEAHQERVLARINKHNNQQALSHSIEEGLKIQAMNRLQRGKKQQIENGSGAEDNGDSSHCSNASTHSNQEAGPSNKRTKTSDDSGLELDNNNAAVAIDPVMDGASEIELVFRPHPTLMEKDDSAQTRYIKTSGNATVDHLSKYLAVRLALEELRSKGESNQMNLDTASEKQYTIYIATASGQFTVLNGSFSLELVSEKYWKVNKPMELYYAPTKEHK

Computationally mapped potential isoform sequences

There are 3 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A087WP87A0A087WP87_MOUSERnf2211
A0A087WQQ3A0A087WQQ3_MOUSERnf273
A0A087WRE9A0A087WRE9_MOUSERnf2264

Features

Showing features for compositional bias, sequence conflict.

TypeIDPosition(s)Description
Compositional bias157-194Polar residues
Sequence conflict253in Ref. 2; BAC41075
Sequence conflict299in Ref. 2; BAC41075
Sequence conflict304in Ref. 2; BAC41075
Sequence conflict332-336in Ref. 1; CAA73380

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
Y12880
EMBL· GenBank· DDBJ
CAA73380.1
EMBL· GenBank· DDBJ
mRNA
Y12783
EMBL· GenBank· DDBJ
CAA73321.1
EMBL· GenBank· DDBJ
mRNA
AK145767
EMBL· GenBank· DDBJ
BAE26638.1
EMBL· GenBank· DDBJ
mRNA
AK012358
EMBL· GenBank· DDBJ
BAB28186.1
EMBL· GenBank· DDBJ
mRNA
AK013124
EMBL· GenBank· DDBJ
BAB28663.1
EMBL· GenBank· DDBJ
mRNA
AK030319
EMBL· GenBank· DDBJ
BAC26898.1
EMBL· GenBank· DDBJ
mRNA
AK090066
EMBL· GenBank· DDBJ
BAC41075.1
EMBL· GenBank· DDBJ
mRNA
CT010297
EMBL· GenBank· DDBJ
CAJ18505.1
EMBL· GenBank· DDBJ
mRNA
BC020122
EMBL· GenBank· DDBJ
AAH20122.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp