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Search results 601 to 700 out of 702 for Ring1

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Type Details Score
Protein Domain
IPR044675 | RING1-like
Type: Family
Description: This entry represents a group of RING-H2 finger proteins mostly from plants, including RING1 (also known as ATL55, At5g10380) and related proteins from Arabidopsis. RING1 is an E3 ubiquitin-protein ligase that may be involved in positive regulation of programmed cell death (PCD) by facilitating degradation of negative regulators ofPCD [].
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HT Experiment
GSE118263 | Polycomb group proteins regulate chromatin architecture in mouse oocytes and early embryos
 
Experiment Type: RNA-Seq
Study Type: WT vs. Mutant
Source: GEO
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HT Experiment
GSE175503 | PRC1 Sustains the Memory of Neuronal Fate Independent of PRC2 Function
 
Experiment Type: RNA-Seq
Study Type: WT vs. Mutant
Source: GEO
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Publication
28111200 | J:251488
First Author: Li H
Year: 2017
Journal: Cell Stem Cell
Title: RNA Helicase DDX5 Inhibits Reprogramming to Pluripotency by miRNA-Based Repression of RYBP and its PRC1-Dependent and -Independent Functions.
Volume: 20
Issue: 4
Pages: 462-477.e6
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Publication
22226355 | -
First Author: Morey L
Year: 2012
Journal: Cell Stem Cell
Title: Nonoverlapping functions of the Polycomb group Cbx family of proteins in embryonic stem cells.
Volume: 10
Issue: 1
Pages: 47-62
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Publication
32653576 | J:331734
 
First Author: Edmunds LR
Year: 2020
Journal: Mol Metab
Title: Liver-specific Prkn knockout mice are more susceptible to diet-induced hepatic steatosis and insulin resistance.
Volume: 41
Pages: 101051
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Protein Domain
IPR043540 | RING1/RING2
Type: Family
Description: E3 ubiquitin-protein ligase RING1 () is one of the three E3 ubiquitin-protein ligases that mediate monoubiquitination of 'Lys-119' of histone H2A, which is a specific tag for repression of epigenetic transcription and particularly for inactivation of chromosome X of female mammals [, ]. RING1 is a component of the Polycomb group (PcG) multiprotein PRC1-like complex, the repressive BCOR complex [], and the the E2F6.com-1 complex in G0 phase []. RING1 has a RING-type zinc finger.E3 ubiquitin-protein ligase RING2 () mediates monoubiquitination of 'Lys-119' of histone H2A (H2AK119Ub) [], which is a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals []. RING2 is a component of the PRC1 complex [], and other chromatin-associated Polycomb (PcG) complexes such as BCOR []. It is also a component of the MLL1/MLL complex [].This entry includes E3 ubiquitin-protein ligase RING1/RING2.
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HT Experiment
E-GEOD-23033 | Polycomb function during oogenesis is required for mouse early embryonic development (germinal vesicle oocytes)
Series Id: GSE23033
Experiment Type: transcription profiling by array
Study Type: WT vs. Mutant
Source: ArrayExpress
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Publication
16714294 | -
First Author: Li Z
Year: 2006
Journal: J Biol Chem
Title: Structure of a Bmi-1-Ring1B polycomb group ubiquitin ligase complex.
Volume: 281
Issue: 29
Pages: 20643-9
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Publication
15386022 | -
First Author: Wang H
Year: 2004
Journal: Nature
Title: Role of histone H2A ubiquitination in Polycomb silencing.
Volume: 431
Issue: 7010
Pages: 873-8
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Publication
16943429 | -
First Author: Gearhart MD
Year: 2006
Journal: Mol Cell Biol
Title: Polycomb group and SCF ubiquitin ligases are found in a novel BCOR complex that is recruited to BCL6 targets.
Volume: 26
Issue: 18
Pages: 6880-9
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Publication
23661642 | -
First Author: Trempe JF
Year: 2013
Journal: Science
Title: Structure of parkin reveals mechanisms for ubiquitin ligase activation.
Volume: 340
Issue: 6139
Pages: 1451-5
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Protein
A0A087WP87
Organism: Mus musculus/domesticus
Length: 211  
Fragment?: true
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Protein
Q7TPF8
Organism: Mus musculus/domesticus
Length: 120  
Fragment?: true
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Protein Domain
IPR041565 | Parkin_Znf-RING
Type: Domain
Description: This is a RING zinc finger domain found in parkin proteins. Parkin consists of a ubiquitin-like (Ubl) domain and a 60-amino acid linker followed by this domain RING0 and three additional zinc finger domains characteristic of the RBR family. RING0 binds two coordinated zinc atoms at each extremity of the domain with a hairpin. Deletion of RING0 massively derepressed parkin activity supporting the role of RING0 in autoinhibition, point mutations in RING0 (Phe146 to Ala) or RING2 (Phe463 to Ala) both increased parkin activity. The REP (repressor element of parkin) and RING0 domains play a preeminent role in repressing parkin ligase activity through their interactions with RING1 and RING2, respectively [].
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Publication
37165006 | J:344426
First Author: Undamatla R
Year: 2023
Journal: Sci Rep
Title: Reduced mitophagy is an early feature of NAFLD and liver-specific PARKIN knockout hastens the onset of steatosis, inflammation and fibrosis.
Volume: 13
Issue: 1
Pages: 7575
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Publication
22770845 | J:227373
First Author: Qin J
Year: 2012
Journal: Cell Stem Cell
Title: The polycomb group protein L3mbtl2 assembles an atypical PRC1-family complex that is essential in pluripotent stem cells and early development.
Volume: 11
Issue: 3
Pages: 319-32
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Publication
14647293 | J:90489
First Author: Gil J
Year: 2004
Journal: Nat Cell Biol
Title: Polycomb CBX7 has a unifying role in cellular lifespan.
Volume: 6
Issue: 1
Pages: 67-72
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Publication
32395866 | J:313429
First Author: Liu Z
Year: 2020
Journal: EMBO J
Title: SUMOylated PRC1 controls histone H3.3 deposition and genome integrity of embryonic heterochromatin.
Volume: 39
Issue: 13
Pages: e103697
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Publication
9205114 | J:41597
First Author: Kikuti YY
Year: 1997
Journal: Genomics
Title: Physical mapping 220 kb centromeric of the human MHC and DNA sequence analysis of the 43-kb segment including the RING1, HKE6, and HKE4 genes.
Volume: 42
Issue: 3
Pages: 422-35
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Protein
A0A1W2P7W2
Organism: Mus musculus/domesticus
Length: 288  
Fragment?: false
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Publication
25703348 | J:225041
First Author: Hasegawa K
Year: 2015
Journal: Dev Cell
Title: SCML2 establishes the male germline epigenome through regulation of histone H2A ubiquitination.
Volume: 32
Issue: 5
Pages: 574-88
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Protein
J3QMF8
Organism: Mus musculus/domesticus
Length: 71  
Fragment?: false
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Protein
A0A087WQQ3
Organism: Mus musculus/domesticus
Length: 73  
Fragment?: true
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Protein
Q9WVS6
Organism: Mus musculus/domesticus
Length: 464  
Fragment?: false
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Protein
A0A3B2W489
Organism: Mus musculus/domesticus
Length: 274  
Fragment?: false
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Publication
26618355 | J:231697
First Author: Logunova N
Year: 2015
Journal: PLoS Genet
Title: The QTL within the H2 Complex Involved in the Control of Tuberculosis Infection in Mice Is the Classical Class II H2-Ab1 Gene.
Volume: 11
Issue: 11
Pages: e1005672
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Publication
15236971 | -
First Author: Capili AD
Year: 2004
Journal: J Mol Biol
Title: Structure of the C-terminal RING finger from a RING-IBR-RING/TRIAD motif reveals a novel zinc-binding domain distinct from a RING.
Volume: 340
Issue: 5
Pages: 1117-29
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Publication
24489889 | -
First Author: Chen P
Year: 2014
Journal: PLoS One
Title: Genome-wide identification and characterization of RBR ubiquitin ligase genes in soybean.
Volume: 9
Issue: 1
Pages: e87282
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Publication
20644651 | -
First Author: Marín I
Year: 2010
Journal: PLoS One
Title: Diversification and Specialization of Plant RBR Ubiquitin Ligases.
Volume: 5
Issue: 7
Pages: e11579
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Publication
28827147 | -
First Author: Dove KK
Year: 2017
Journal: J Mol Biol
Title: RING-Between-RING E3 Ligases: Emerging Themes amid the Variations.
Volume: 429
Issue: 22
Pages: 3363-3375
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Protein Domain
IPR044066 | TRIAD_supradom
Type: Domain
Description: The TRIAD (Two RING fingers and a DRIL, double RING finger linked) or RBR (RING-BetweenRING-RING) family of zinc finger proteins contains a tripartite motif of three double zinc fingers, the first of which, RING1, is a typical RING finger with a C3HC4 signature of conserved cysteine and histidine residues. The second (In-Between-Ring, IBR, BetweenRING or DRIL) and third (RING2) are dissimilar to RINGs but share notable similarity, as they have similar spacing of cysteines and some conserved residues. The cysteine and histidine rich TRIAD domain architecture is highly conserved and found mostly in eukaryotes. TRIAD E3 ligases (E3s) are complicated multi-domain enzymes that contain a variety of domains in addition to their TRIAD supradomain. The three fingers that define the TRIAD supradomain always appear in the same order RING1-IBR-RING2, but the position of the supradomain itself relative to other domains varies. All characterised proteins containing the TRIAD supradomain have been found to possess E3 ligase activity. TRIAD E3s differ fundamentally from their eponymous RING E3 cousins by virtue of their possessing an active site, a feature lacking in all RING-type E3s. Similar to canonical RINGs, the RING1 finger of the TRIAD supradomain binds E2s loaded with Ub (E2-Ubs). However, RING2s contain an essential active-site Cys that receives Ub from E2-Ub to generate a covalent E3-Ub intermediate [, , , ].The three fingers coordinates two Zn ions. RING1 is the only domain with a classical C3HC4 cross-brace zinc-coordination topology. IBR and RING2 fingers do not only share structural similarity but also have a completely distinct topology from classical RINGs. The IBR finger adopts a bilobal fold about the two zinc-binding sites. This arrangement brings the N-terminal of the domain within close proximity to its C-terminal. The RING2 has the same domain topology as the IBR finger and coordinates its two zinc atoms in a sequential fashion. The RING2 finger contains a conserved Cys residue that is not involved in Zn coordination but serves as the active site to which Ub is attached. While they resemble RING2s in topology, IBR fingers do not contain an active-site Cys. IBRs and their linkers on either side have been implicated in binding Ub during Ub transfer reactions, but the exact function of IBRs remains unknown [, , , ].This entry represents the TRIAD supradomain found in a number of proteins with different functions, such as Ariadne (ARI) proteins, implicated in the regulation of translation, cellular proliferation, and developmental processes; TRIAD proteins, associated with the regulation of myeloid progenitors proliferation, NF-kappaB signaling, and membrane trafficking or Parkin, implicated in a range of biological processes, including autophagy of damaged mitochondria (mitophagy), cell survival pathways, and vesicle trafficking. This supradomain is also present in heme-oxidized IRP2 ubiquitin ligase 1L (HOIL-1L) and HOIL-1L interacting protein (HOIP) which form the two linear ubiquitin chain assembly complex (LUBAC), associated with B-cell function, regulation of apoptosis, oncogenesis, and diverse autoimmune diseases.
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Protein
A0A087WQJ2
Organism: Mus musculus/domesticus
Length: 104  
Fragment?: true
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Publication
12004135 | -
First Author: Ogawa H
Year: 2002
Journal: Science
Title: A complex with chromatin modifiers that occupies E2F- and Myc-responsive genes in G0 cells.
Volume: 296
Issue: 5570
Pages: 1132-6
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Publication
29799838 | J:262823
First Author: Kasowitz SD
Year: 2018
Journal: PLoS Genet
Title: Nuclear m6A reader YTHDC1 regulates alternative polyadenylation and splicing during mouse oocyte development.
Volume: 14
Issue: 5
Pages: e1007412
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Protein
P58283
Organism: Mus musculus/domesticus
Length: 853  
Fragment?: false
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Protein
A2A7Q8
Organism: Mus musculus/domesticus
Length: 352  
Fragment?: true
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Protein
A4VCJ1
Organism: Mus musculus/domesticus
Length: 513  
Fragment?: true
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Protein
Q8K1N5
Organism: Mus musculus/domesticus
Length: 78  
Fragment?: true
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Protein
A0A0A6YXA7
Organism: Mus musculus/domesticus
Length: 79  
Fragment?: true
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Protein
B2KG08
Organism: Mus musculus/domesticus
Length: 551  
Fragment?: false
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Publication
10422847 | J:66295
First Author: van der Reijden BA
Year: 1999
Journal: Protein Sci
Title: TRIADs: a new class of proteins with a novel cysteine-rich signature.
Volume: 8
Issue: 7
Pages: 1557-61
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Publication
24576094 | -
First Author: Spratt DE
Year: 2014
Journal: Biochem J
Title: RBR E3 ubiquitin ligases: new structures, new insights, new questions.
Volume: 458
Issue: 3
Pages: 421-37
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Protein
Q9CQJ4
Organism: Mus musculus/domesticus
Length: 336  
Fragment?: false
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Protein
A0A087WRE9
Organism: Mus musculus/domesticus
Length: 264  
Fragment?: false
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Protein
F6TNF2
Organism: Mus musculus/domesticus
Length: 245  
Fragment?: false
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Protein
B8YP90
Organism: Mus musculus/domesticus
Length: 214  
Fragment?: false
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Protein
D3YYI7
Organism: Mus musculus/domesticus
Length: 515  
Fragment?: false
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Publication
15960975 | J:156231
First Author: Dou Y
Year: 2005
Journal: Cell
Title: Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF.
Volume: 121
Issue: 6
Pages: 873-85
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Protein
Q9Z1K5
Organism: Mus musculus/domesticus
Length: 555  
Fragment?: false
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Protein
P50636
Organism: Mus musculus/domesticus
Length: 840  
Fragment?: false
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Protein
A2A7Q9
Organism: Mus musculus/domesticus
Length: 732  
Fragment?: false
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Protein
Q6KAP7
Organism: Mus musculus/domesticus
Length: 590  
Fragment?: true
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Protein
A0A1Y7VMM6
Organism: Mus musculus/domesticus
Length: 132  
Fragment?: true
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Protein
H9KV21
Organism: Mus musculus/domesticus
Length: 476  
Fragment?: false
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Protein
A0A2I3BRK4
Organism: Mus musculus/domesticus
Length: 558  
Fragment?: false
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Protein
E9Q2L7
Organism: Mus musculus/domesticus
Length: 731  
Fragment?: false
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Protein
H7BWY7
Organism: Mus musculus/domesticus
Length: 381  
Fragment?: false
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Protein
F6VII1
Organism: Mus musculus/domesticus
Length: 233  
Fragment?: true
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Protein
Q3TM18
Organism: Mus musculus/domesticus
Length: 225  
Fragment?: false
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Protein
A0A0A6YXB0
Organism: Mus musculus/domesticus
Length: 318  
Fragment?: false
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Protein
Q9Z1K6
Organism: Mus musculus/domesticus
Length: 492  
Fragment?: false
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Protein
Q6ZPS6
Organism: Mus musculus/domesticus
Length: 1085  
Fragment?: false
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Protein
Q8BKD6
Organism: Mus musculus/domesticus
Length: 301  
Fragment?: false
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Protein
Q925F3
Organism: Mus musculus/domesticus
Length: 292  
Fragment?: false
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Protein
Q9JI90
Organism: Mus musculus/domesticus
Length: 485  
Fragment?: false
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Protein
Q924T7
Organism: Mus musculus/domesticus
Length: 1066  
Fragment?: false
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Protein
Q3TK92
Organism: Mus musculus/domesticus
Length: 492  
Fragment?: false
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Protein
A0A0G2JEA0
Organism: Mus musculus/domesticus
Length: 809  
Fragment?: true
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Protein
Q6WIZ9
Organism: Mus musculus/domesticus
Length: 1067  
Fragment?: false
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Protein
F6XVP7
Organism: Mus musculus/domesticus
Length: 912  
Fragment?: true
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Protein
G3XA54
Organism: Mus musculus/domesticus
Length: 359  
Fragment?: false
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Protein
B2RX15
Organism: Mus musculus/domesticus
Length: 1091  
Fragment?: false
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Publication
30186101 | J:266522
 
First Author: Elsen GE
Year: 2018
Journal: Front Neurosci
Title: The Epigenetic Factor Landscape of Developing Neocortex Is Regulated by Transcription Factors Pax6→ Tbr2→ Tbr1.
Volume: 12
Pages: 571
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Publication
16107646 | J:100324
First Author: Bulfone A
Year: 2005
Journal: J Neurosci
Title: Telencephalic embryonic subtractive sequences: a unique collection of neurodevelopmental genes.
Volume: 25
Issue: 33
Pages: 7586-600
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Protein
Q80TT8
Organism: Mus musculus/domesticus
Length: 1865  
Fragment?: false
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Protein
Q9WUB0
Organism: Mus musculus/domesticus
Length: 508  
Fragment?: false
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Protein
E9QP09
Organism: Mus musculus/domesticus
Length: 2520  
Fragment?: false
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Protein
S4R1Y1
Organism: Mus musculus/domesticus
Length: 2530  
Fragment?: false
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Publication
17967808 | J:152068
First Author: Friedel RH
Year: 2007
Journal: Brief Funct Genomic Proteomic
Title: EUCOMM--the European conditional mouse mutagenesis program.
Volume: 6
Issue: 3
Pages: 180-5
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Publication
- | J:265051
     
First Author: MGI and IMPC
Year: 2018
Journal: Database Release
Title: MGI Load of Endonuclease-Mediated Alleles (CRISPR) from the International Mouse Phenotyping Consortium (IMPC)
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Publication
- | J:77000
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: MGC Data curation in Mouse Genome Informatics
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Publication
12904583 | J:85162
First Author: Hansen J
Year: 2003
Journal: Proc Natl Acad Sci U S A
Title: A large-scale, gene-driven mutagenesis approach for the functional analysis of the mouse genome.
Volume: 100
Issue: 17
Pages: 9918-22
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Publication
- | J:148605
     
First Author: Wellcome Trust Sanger Institute
Year: 2009
Journal: MGI Direct Data Submission
Title: Alleles produced for the KOMP project by the Wellcome Trust Sanger Institute
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Publication
- | J:157065
     
First Author: Helmholtz Zentrum Muenchen GmbH
Year: 2010
Journal: MGI Direct Data Submission
Title: Alleles produced for the EUCOMM and EUCOMMTools projects by the Helmholtz Zentrum Muenchen GmbH (Hmgu)
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Publication
- | J:211773
     
First Author: Mouse Genome Informatics and the International Mouse Phenotyping Consortium (IMPC)
Year: 2014
Journal: Database Release
Title: Obtaining and Loading Phenotype Annotations from the International Mouse Phenotyping Consortium (IMPC) Database
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Publication
- | J:23000
       
First Author: MGD Nomenclature Committee
Year: 1995
Title: Nomenclature Committee Use
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Publication
34321999 | J:313619
 
First Author: Bedogni F
Year: 2021
Journal: Front Mol Neurosci
Title: Cell-Type-Specific Gene Expression in Developing Mouse Neocortex: Intermediate Progenitors Implicated in Axon Development.
Volume: 14
Pages: 686034
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Publication
21677750 | J:173534
First Author: Skarnes WC
Year: 2011
Journal: Nature
Title: A conditional knockout resource for the genome-wide study of mouse gene function.
Volume: 474
Issue: 7351
Pages: 337-42
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Publication
18799693 | J:142754
First Author: Hansen GM
Year: 2008
Journal: Genome Res
Title: Large-scale gene trapping in C57BL/6N mouse embryonic stem cells.
Volume: 18
Issue: 10
Pages: 1670-9
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Publication
- | J:293217
       
First Author: GemPharmatech
Year: 2020
Title: GemPharmatech Website.
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Publication
14610273 | J:86696
First Author: Zambrowicz BP
Year: 2003
Journal: Proc Natl Acad Sci U S A
Title: Wnk1 kinase deficiency lowers blood pressure in mice: a gene-trap screen to identify potential targets for therapeutic intervention.
Volume: 100
Issue: 24
Pages: 14109-14
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Publication
- | J:342587
       
First Author: AgBase, BHF-UCL, Parkinson's UK-UCL, dictyBase, HGNC, Roslin Institute, FlyBase and UniProtKB curators
Year: 2011
Title: Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
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Publication
- | J:85000
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2003
Title: MGI Sequence Curation Reference
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Publication
- | J:78475
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Chromosome assignment of mouse genes using the Mouse Genome Sequencing Consortium (MGSC) assembly and the ENSEMBL Database
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Publication
- | J:141210
     
First Author: Mouse Genome Informatics (MGI) and National Center for Biotechnology Information (NCBI)
Year: 2008
Journal: Database Download
Title: Mouse Gene Trap Data Load from dbGSS
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Publication
15489334 | -
First Author: Gerhard DS
Year: 2004
Journal: Genome Res
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Volume: 14
Issue: 10B
Pages: 2121-7
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Publication
12466851 | J:80000
First Author: Okazaki Y
Year: 2002
Journal: Nature
Title: Analysis of the mouse transcriptome based on functional annotation of 60,770 full-length cDNAs.
Volume: 420
Issue: 6915
Pages: 563-73
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Publication
11217851 | J:65060
First Author: Kawai J
Year: 2001
Journal: Nature
Title: Functional annotation of a full-length mouse cDNA collection.
Volume: 409
Issue: 6821
Pages: 685-90
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Publication
21267068 | J:153498
First Author: Diez-Roux G
Year: 2011
Journal: PLoS Biol
Title: A high-resolution anatomical atlas of the transcriptome in the mouse embryo.
Volume: 9
Issue: 1
Pages: e1000582
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MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

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