ID:RING2_HUMAN DESCRIPTION: RecName: Full=E3 ubiquitin-protein ligase RING2; EC=6.3.2.-; AltName: Full=Huntingtin-interacting protein 2-interacting protein 3; Short=HIP2-interacting protein 3; AltName: Full=Protein DinG; AltName: Full=RING finger protein 1B; Short=RING1b; AltName: Full=RING finger protein 2; AltName: Full=RING finger protein BAP-1; FUNCTION: E3 ubiquitin-protein ligase that mediates monoubiquitination of 'Lys-119' of histone H2A, thereby playing a central role in histone code and gene regulation. H2A 'Lys-119' ubiquitination 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. PATHWAY: Protein modification; protein ubiquitination. SUBUNIT: Component of chromatin-associated Polycomb (PcG) complexes. Part of the E2F6.com-1 complex in G0 phase composed of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EUHMTASE1, 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 MLL, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components C17orf49, 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. Component of repressive BCOR complex containing Polycomb group subcomplex at least composed of RYBP, PCGF1, BCOR and RING1. Interacts with Interacts with PCGF2, CBX4, CBX6, CBX7 and CBX8. Interacts with CBX2, BMI and PHC2. Interacts with RYBP, HIP2 and TFCP2 (By similarity). INTERACTION: P08183:ABCB1; NbExp=2; IntAct=EBI-722416, EBI-1057359; P35226:BMI1; NbExp=5; IntAct=EBI-722416, EBI-2341576; O00257-3:CBX4; NbExp=2; IntAct=EBI-722416, EBI-4392727; O95503:CBX6; NbExp=3; IntAct=EBI-722416, EBI-3951758; O95931:CBX7; NbExp=3; IntAct=EBI-722416, EBI-3923843; Q9HC52:CBX8; NbExp=4; IntAct=EBI-722416, EBI-712912; Q9H7Z6:KAT8; NbExp=2; IntAct=EBI-722416, EBI-896414; Q9BSM1:PCGF1; NbExp=4; IntAct=EBI-722416, EBI-749901; P35227:PCGF2; NbExp=6; IntAct=EBI-722416, EBI-2129767; Q3KNV8:PCGF3; NbExp=2; IntAct=EBI-722416, EBI-2339807; Q86SE9:PCGF5; NbExp=2; IntAct=EBI-722416, EBI-2827999; Q06587:RING1; NbExp=4; IntAct=EBI-722416, EBI-752313; SUBCELLULAR LOCATION: Nucleus. Chromosome (By similarity). 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 (By similarity). PTM: Polyubiquitinated in the presence of UBE2D3 (in vitro) (By similarity). PTM: Monoubiquitinated, by auto-ubiquitination (By similarity). MISCELLANEOUS: The hPRC-H complex purification reported by PubMed:12167701 probably presents a mixture of different PRC1-like complexes. SIMILARITY: Contains 1 RING-type zinc finger. SEQUENCE CAUTION: Sequence=CAI17849.1; Type=Erroneous gene model prediction; Sequence=CAI17850.1; Type=Erroneous gene model prediction;
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on Q99496
Front
Top
Side
The pictures above may be empty if there is no ModBase structure for the protein. The ModBase structure frequently covers just a fragment of the protein. You may be asked to log onto ModBase the first time you click on the pictures. It is simplest after logging in to just click on the picture again to get to the specific info on that model.
Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
US Server
Sequence and Links to Tools and Databases 
Common Gene Haplotype Alleles 
