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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

RanBP-type and C3HC4-type zinc finger containing 1

RBCK1, HOIL-1, RBCC protein interacting with PKC 1, RBCK2, HOIL-1L, XAP3
The protein encoded by this gene is similar to mouse UIP28/UbcM4 interacting protein. Alternative splicing has been observed at this locus, resulting in distinct isoforms. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Ubiquitin, Incontinentia Pigmenti, V1a, CAN, IRP2
Papers using RBCK1 antibodies
In TNF-stimulated cells, RIPK1 promotes cell survival by stabilizing TRAF2 and cIAP1, which limits induction of non-canonical NF-{kappa}B and activation of caspase-8
Vanden Berghe T et al., In Cell Death & Disease, 2010
... The following antibodies were used for western blot analysis: anti-HOIL-1 antibody (gift from H Walczak); anti-β-tubulin (HRP) (Ab21058, Abcam, Cambridge, UK); anti- ...
Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases
Sixma Titia K et al., In The EMBO Journal, 1999
... expression of HOIP and HOIL-1L was obtained from Genscript.
Papers on RBCK1
The paracaspase MALT1 dampens NF-κB signaling by cleaving the LUBAC subunit HOIL-1.
Schulze-Osthoff et al., Tübingen, Germany. In Febs J, Jan 2016
Two studies now report that MALT1 restrains NF-κB signaling and lymphocyte activation by cleaving heme-oxidized iron-responsive element-binding protein 2 ubiquitin ligase-1 (HOIL-1).
Polyglucosan storage myopathies.
Oldfors et al., Göteborg, Sweden. In Mol Aspects Med, Dec 2015
Mutations in eight human genes are known to be associated with polyglucosan storage involving muscle, namely GYG1, GBE1, RBCK1 (HOIL-1), PFKM, EPM2A, EPM2B (NHLRC1), PRDM8, and PRKAG2.
MALT1 cleaves the E3 ubiquitin ligase HOIL-1 in activated T cells, generating a dominant negative inhibitor of LUBAC-induced NF-κB signaling.
Beyaert et al., Gent, Belgium. In Febs J, Dec 2015
Here we show that T cell activation, as well as overexpression of the oncogenic fusion protein API2-MALT1, induces the MALT1-mediated cleavage of HOIL-1.
The multifaceted role of the E3 ubiquitin ligase HOIL-1: beyond linear ubiquitination.
Beyaert et al., Gent, Belgium. In Immunol Rev, Jul 2015
The E3 ubiquitin ligase HOIL-1 (heme-oxidized IRP2 ubiquitin ligase-1) is increasingly implicated in different signaling pathways and plays a vital role in immune regulation.
Roles of linear ubiquitinylation, a crucial regulator of NF-κB and cell death, in the immune system.
Iwai et al., Kyoto, Japan. In Immunol Rev, Jul 2015
Linear ubiquitinylation, a newly identified post-translational modification, is catalyzed by the linear ubiquitin assembly complex (LUBAC), which is composed of three different subunits, HOIL-1L (heme-oxidized IRP2 ligase 1L), HOIP (HOIL-1 interacting protein), and SHARPIN (SHANK-associated RH domain-interacting protein).
Human HOIP and LUBAC deficiency underlies autoinflammation, immunodeficiency, amylopectinosis, and lymphangiectasia.
Notarangelo et al., Paris, France. In J Exp Med, Jul 2015
Inherited, complete deficiency of human HOIL-1, a component of the linear ubiquitination chain assembly complex (LUBAC), underlies autoinflammation, infections, and amylopectinosis.
Effect of UBE2L3 genotype on regulation of the linear ubiquitin chain assembly complex in systemic lupus erythematosus.
Vyse et al., London, United Kingdom. In Lancet, Mar 2015
UBE2L3 is an E2 ubiquitin-conjugating enzyme with specificity for RING-in-between-RING E3 ligases, including HOIL-1 and HOIP, components of the linear ubiquitin chain assembly complex (LUBAC), which has a pivotal role in inflammation, through crucial regulation of NF-κB.
LUBAC Formation Is Impaired in the Livers of Mice with MCD-Dependent Nonalcoholic Steatohepatitis.
Asano et al., Hiroshima, Japan. In Mediators Inflamm, 2014
Recently, it was reported that the new ubiquitin ligase complex termed linear ubiquitin chain assembly complex (LUBAC), composed of SHARPIN (SHANK-associated RH domain-interacting protein), HOIL-1L (longer isoform of heme-oxidized iron-regulatory protein 2 ubiquitin ligase-1), and HOIP (HOIL-1L interacting protein), forms linear ubiquitin on NF-κB essential modulator (NEMO) and thereby induces NF-κB pathway activation.
Posttranslational Modification of HOIP Blocks Toll-Like Receptor 4-Mediated Linear-Ubiquitin-Chain Formation.
Jung et al., Los Angeles, United States. In Mbio, 2014
UNLABELLED: Linear ubiquitination is an atypical posttranslational modification catalyzed by the linear-ubiquitin-chain assembly complex (LUBAC), containing HOIP, HOIL-1L, and Sharpin.
RBR E3 ubiquitin ligases: new structures, new insights, new questions.
Shaw et al., London, Canada. In Biochem J, 2014
This unique family of E3 ligases includes parkin, whose dysfunction is linked to the pathogenesis of early-onset Parkinson's disease, and HOIP (HOIL-1-interacting protein) and HOIL-1 (haem-oxidized IRP2 ubiquitin ligase 1), members of the LUBAC (linear ubiquitin chain assembly complex).
New insights in the field of muscle glycogenoses.
DiMauro et al., Göteborg, Sweden. In Curr Opin Neurol, 2013
Polyglucosan body myopathy with cardiomyopathy has been associated with mutations in RBCK1, a ubiquitin ligase, which have also been reported in children with early-onset immune disorder.
Immunodeficiency, autoinflammation and amylopectinosis in humans with inherited HOIL-1 and LUBAC deficiency.
Picard et al., New York City, United States. In Nat Immunol, 2012
Patients from two kindreds carried biallelic loss-of-expression and loss-of-function mutations in HOIL1 (RBCK1), a component of the linear ubiquitination chain assembly complex (LUBAC).
Solution structure of the E3 ligase HOIL-1 Ubl domain.
Shaw et al., London, Canada. In Protein Sci, 2012
The solution structure of the HOIL1 Ubl domain was solved using NMR spectroscopy to compare it with that of parkin to determine the structural elements responsible for S5a subunit of the 26S proteasome intermolecular interactions.
Specific recognition of linear ubiquitin chains by the Npl4 zinc finger (NZF) domain of the HOIL-1L subunit of the linear ubiquitin chain assembly complex.
Fukai et al., Tokyo, Japan. In Proc Natl Acad Sci U S A, 2012
analysis of recognition of linear ubiquitin chains by the Npl4 zinc finger (NZF) domain of the HOIL-1L subunit of the linear ubiquitin chain assembly complex
SHARPIN forms a linear ubiquitin ligase complex regulating NF-κB activity and apoptosis.
Dikic et al., Frankfurt am Main, Germany. In Nature, 2011
This effect is further enhanced upon concurrent downregulation of HOIL-1L (also known as RBCK1), another HOIP-binding component of LUBAC.
Linear ubiquitination prevents inflammation and regulates immune signalling.
Walczak et al., London, United Kingdom. In Nature, 2011
Recently linear ubiquitin chains assembled by a complex containing HOIL-1 and HOIP (also known as RBCK1 and RNF31, respectively) were implicated in TNF signalling, yet their relevance in vivo remained uncertain.
SHARPIN is a component of the NF-κB-activating linear ubiquitin chain assembly complex.
Iwai et al., Suita, Japan. In Nature, 2011
SHARPIN shows significant similarity to HOIL-1L (also known as RBCK1), a component of linear ubiquitin chain assembly complex (LUBAC), which induces NF-κB activation through conjugation of linear polyubiquitin chains to NEMO.
Sipl1 and Rbck1 are novel Eya1-binding proteins with a role in craniofacial development.
Englert et al., Jena, Germany. In Mol Cell Biol, 2010
Data report the identification of the related proteins Sipl1 (Shank-interacting protein-like 1) and Rbck1 (RBCC protein interacting with PKC1) as novel interaction partners of Eya1.
RBCK1 drives breast cancer cell proliferation by promoting transcription of estrogen receptor alpha and cyclin B1.
Dahlman-Wright et al., Huddinge, Sweden. In Cancer Res, 2010
Findings suggest that RBCK1 regulates cell cycle progression and proliferation of ERalpha-positive breast cancer cells by supporting transcription of ERalpha and cyclin B1.
HOIL-1L interacting protein (HOIP) as an NF-kappaB regulating component of the CD40 signaling complex.
Colgan et al., Iowa City, United States. In Plos One, 2009
results demonstrate a powerful approach for the identification of signaling molecules associated with cell surface receptors and indicate an important role for the ubiquitin ligase activity of HOIP in proximal CD40 signaling
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