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Ring finger protein 1

RING finger protein, RING1, Ring1A
This gene belongs to the RING finger family, members of which encode proteins characterized by a RING domain, a zinc-binding motif related to the zinc finger domain. The gene product can bind DNA and can act as a transcriptional repressor. It is associated with the multimeric polycomb group protein complex. The gene product interacts with the polycomb group proteins BMI1, EDR1, and CBX4, and colocalizes with these proteins in large nuclear domains. It interacts with the CBX4 protein via its glycine-rich C-terminal domain. The gene maps to the HLA class II region, where it is contiguous with the RING finger genes FABGL and HKE4. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Ubiquitin, Polycomb, CAN, Bmi-1, ACID
Papers on RING finger protein
RING1 proteins contribute to early proximal-distal specification of the forelimb bud by restricting Meis2 expression.
Koseki et al., Kawasaki, Japan. In Development, Feb 2016
Depletion of the RING1 proteins RING1A (RING1) and RING1B (RNF2), which are essential components of Polycomb repressive complex 1 (PRC1), led to severe defects in forelimb formation along the PD axis.
The evolutionary landscape of PRC1 core components in green lineage.
Shen et al., Changsha, China. In Planta, Feb 2016
We evaluated the origin of plant PRC1 RING-finger proteins (RING1 and BMI1) through comparing with the homologs in some representative unikonts and using BMI1- and RING1-like proteins as reciprocal outgroup, finding both PRC1 RING-finger proteins have the earliest origin in mosses, similar to LHP1.
Role of Polycomb RYBP in Maintaining the B-1 to B-2 B-Cell Lineage Switch in Adult Hematopoiesis.
Vidal et al., Madrid, Spain. In Mol Cell Biol, Jan 2016
We have studied the hematopoietic activity of RYBP, a direct interactor and proposed modulator of RING1A/RING1B-dependent histone H2A monoubiquitylation (H2AUb).
Negative Regulation of CARD11 Signaling and Lymphoma Cell Survival by the E3 Ubiquitin Ligase RNF181.
Pomerantz et al., Baltimore, United States. In Mol Cell Biol, Jan 2016
Using this strategy we identified the RING finger protein RNF181 as an interactor of CARD11, a key signaling scaffold in the antigen receptor pathway.
Interaction between RING1 (R1) and Ubiquitin-Like (UBL) Domain Is Critical for the Regulation of Parkin Activity.
Chung et al., Seoul, South Korea. In J Biol Chem, Jan 2016
UNASSIGNED: Parkin is an E3 ligase that contains an UBL domain in the N-terminus and an R1-in-between-ring (IBR)-RING2 (R2) motif in the C-terminus.
The Ku70/80 ring in Non-Homologous End-Joining: easy to slip on, hard to remove.
Keijzers et al., Copenhagen, Denmark. In Front Biosci, Dec 2015
Recent studies suggest that Ku80 is conjugated to lysine48-linked ubiquitin chains by the Skp1-Cullin-F-box (SCF) complex and/or the RING finger protein 8 (RNF8) ubiquitin-protein ligases, followed by rapid proteasomal degradation.
Absence of Rybp Compromises Neural Differentiation of Embryonic Stem Cells.
Pirity et al., Szeged, Hungary. In Stem Cells Int, Dec 2015
Rybp (Ring1 and Yy1 Binding Protein) is a transcriptional regulator and member of the noncanonical polycomb repressive complex 1 with essential role in early embryonic development.
Arenavirus Quasispecies and Their Biological Implications.
de la Torre et al., Los Angeles, United States. In Curr Top Microbiol Immunol, Nov 2015
The L genome RNA encodes the viral RNA-dependent RNA polymerase (RdRp, or L polymerase) and the small (ca 11 kDa) RING finger protein Z that has functions of a bona fide matrix protein including directing virus budding.
Mechanism of phospho-ubiquitin-induced PARKIN activation.
Komander et al., Cambridge, United Kingdom. In Nature, Sep 2015
PhosphoUb binding leads to straightening of a helix in the RING1 domain, and the resulting conformational changes release the Ubl domain from the PARKIN core; this activates PARKIN.
RBR E3 ubiquitin ligases: new structures, new insights, new questions.
Shaw et al., London, Canada. In Biochem J, 2014
The RBR (RING-BetweenRING-RING) or TRIAD [two RING fingers and a DRIL (double RING finger linked)] E3 ubiquitin ligases comprise a group of 12 complex multidomain enzymes.
RBR E3-ligases at work.
Sixma et al., Amsterdam, Netherlands. In Embo Rep, 2014
They catalyse ubiquitin conjugation by a concerted RING/HECT-like mechanism in which the RING1 domain facilitates E2-discharge to directly form a thioester intermediate with a cysteine in RING2.
Structural basis for ligase-specific conjugation of linear ubiquitin chains by HOIP.
Rittinger et al., London, United Kingdom. In Nature, 2013
RBR family members act as RING/HECT hybrids, employing RING1 to recognize ubiquitin-loaded E2 while a conserved cysteine in RING2 subsequently forms a thioester intermediate with the transferred or 'donor' ubiquitin.
Structure of parkin reveals mechanisms for ubiquitin ligase activation.
Gehring et al., Montréal, Canada. In Science, 2013
The parkin protein is a RING-in-between-RING E3 ubiquitin ligase that exhibits low basal activity.
PRC1 coordinates timing of sexual differentiation of female primordial germ cells.
Peters et al., Basel, Switzerland. In Nature, 2013
Here we identify gene-dosage-dependent roles in PGC development for Ring1 and Rnf2, two central components of the Polycomb repressive complex 1 (PRC1).
Ring1a/b polycomb proteins regulate the mesenchymal stem cell niche in continuously growing incisors.
Sharpe et al., London, United Kingdom. In Dev Biol, 2012
loss of Ring1a/b postnatally results in defective cervical loops and disturbances of enamel and dentin formation in continuously growing incisors
The role of the histone H2A ubiquitinase Sce in Polycomb repression.
Müller et al., Heidelberg, Germany. In Development, 2012
Sce synergizes with the Polycomb repressive deubiquitinase complex to repress transcription at class I genes, suggesting that H2A monoubiquitylation must be appropriately balanced for their transcriptional repression.
Overexpression of the EZH2, RING1 and BMI1 genes is common in myelodysplastic syndromes: relation to adverse epigenetic alteration and poor prognostic scoring.
Chang et al., Shanghai, China. In Ann Hematol, 2011
Overexpression of the EZH2, RING1, and BMI1 genes is common in MDS and indicate poor prognosis. The products of these genes might participate in epigenetic regulation of Myelodysplastic syndromes.
Regulation of the Polycomb protein RING1B ubiquitination by USP7.
Ciechanover et al., Haifa, Israel. In Biochem Biophys Res Commun, 2010
USP7 was identified as a deubiquitinating enzyme that regulates the ubiquitination state of RING1B.
Transcriptional repression of p53 by parkin and impairment by mutations associated with autosomal recessive juvenile Parkinson's disease.
Checler et al., France. In Nat Cell Biol, 2009
Parkin lowered p53 mRNA levels and repressed p53 promoter transactivation through its Ring1 domain.
Role of polycomb proteins Ring1A and Ring1B in the epigenetic regulation of gene expression.
Vidal, Madrid, Spain. In Int J Dev Biol, 2008
Studies in mammalian cells have found a multiplicity of protein complexes containing Ring1A and Ring1B, suggesting an expanded regulatory role for Ring1A, Ring1B proteins in the epigenetic regulation of gene expression.
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