gopubmed logo
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Makorin ring finger protein 1

MKRN1, Makorin Ring Finger Protein 1
The Makorin ring finger protein-1 gene (MKRN1) is a highly transcribed, intron-containing source for a family of intronless mammalian genes encoding a novel class of zinc finger proteins. Phylogenetic analyses indicate that the MKRN1 gene is the ancestral founder of this gene family (Gray et al., 2000 [PubMed 10843807]).[supplied by OMIM, Mar 2008] (from NCBI)
Top mentioned proteins: Ubiquitin, V1a, CAN, p53, p16
Papers on MKRN1
Integrative genomics positions MKRN1 as a novel ribonucleoprotein within the embryonic stem cell gene regulatory network.
Stanford et al., Toronto, Canada. In Embo Rep, Oct 2015
Our previous temporal microarray analysis of ESC commitment identified the E3 ubiquitin ligase protein Makorin-1 (MKRN1) as a potential novel component of the ESC GRN.
Binding of the sphingolipid S1P to hTERT stabilizes telomerase at the nuclear periphery by allosterically mimicking protein phosphorylation.
Ogretmen et al., Charleston, United States. In Sci Signal, Jul 2015
S1P binding inhibited the interaction of hTERT with makorin ring finger protein 1 (MKRN1), an E3 ubiquitin ligase that tags hTERT for degradation.
The genomic and transcriptomic landscape of anaplastic thyroid cancer: implications for therapy.
Jones et al., Vancouver, Canada. In Bmc Cancer, 2014
We found novel anaplastic gene fusions including MKRN1-BRAF, FGFR2-OGDH and SS18-SLC5A11, all expressed in-frame fusions involving a known proto-oncogene.
PI3K/AKT activation induces PTEN ubiquitination and destabilization accelerating tumourigenesis.
Song et al., Seoul, South Korea. In Nat Commun, 2014
EGFR/PI3K/AKT-mediated ubiquitination and degradation of PTEN are dependent on the MKRN1 E3 ligase.
Suppression of PPARγ through MKRN1-mediated ubiquitination and degradation prevents adipocyte differentiation.
Song et al., Seoul, South Korea. In Cell Death Differ, 2014
Here we report that MKRN1 is an E3 ligase of PPARγ that induces its ubiquitination, followed by proteasome-dependent degradation.
[Research advances in the Cap gene of circovirus and its encoding capsid protein].
Jia et al., Chengdu, China. In Bing Du Xue Bao, 2013
This review summarizes the research advance of Cap gene of circovirus in the sequence characteristics, its encoding capsid protein, basic functions of the capsid protein and its interaction with MKRN1 protein, Hsp40 protein, receptor protein gClqR and complement factor C1qB protein.
Acceleration of gastric tumorigenesis through MKRN1-mediated posttranslational regulation of p14ARF.
Song et al., Seoul, South Korea. In J Natl Cancer Inst, 2012
BACKGROUND: We investigated whether Makorin ring finger protein 1 (MKRN1), an E3 ligase, affects p14ARF-associated cellular senescence and tumorigenesis by posttranslational modification in gastric tumorigenesis.
A molecular insight into Darwin's "plant brain hypothesis" through expression pattern study of the MKRN gene in plant embryo compared with mouse embryo.
Abe et al., Japan. In Plant Signal Behav, 2012
Images of MKRN1 expression in e10.5 whole mount mouse embryo, hybridized with DIG labeled probes, were obtained from the Mouse Genome Database (MGD).
Makorin ring zinc finger protein 1 (MKRN1), a novel poly(A)-binding protein-interacting protein, stimulates translation in nerve cells.
Mohr et al., Hamburg, Germany. In J Biol Chem, 2012
In this study we identify RING zinc finger protein Makorin 1 (MKRN1), a bona fide RNA-binding protein, as a binding partner of PABP that interacts with PABP in an RNA-independent manner.
Ubiquitination and degradation of the FADD adaptor protein regulate death receptor-mediated apoptosis and necroptosis.
Song et al., Seoul, South Korea. In Nat Commun, 2011
Here we show that FADD is regulated by Makorin Ring Finger Protein 1 (MKRN1) E3 ligase-mediated ubiquitination and proteasomal degradation.
Differentiation linked regulation of telomerase activity by Makorin-1.
Muller et al., Orlando, United States. In Mol Cell Biochem, 2010
Makorin-1 (MKRN1) was previously shown to be an E3 ubiquitin ligase that targets the telomerase catalytic subunit (hTERT) for proteasome processing (Kim et al., Genes Dev 19:776-781, 2005).
MKRN1 induces degradation of West Nile virus capsid protein by functioning as an E3 ligase.
Song et al., Suwŏn, South Korea. In J Virol, 2010
MKRN1 could induce WNV capsid protein ubiquitination and degradation in a proteasome-dependent manner
Differential regulation of p53 and p21 by MKRN1 E3 ligase controls cell cycle arrest and apoptosis.
Song et al., Suwŏn, South Korea. In Embo J, 2009
Data indicate that MKRN1 is a novel modulator of p53 and p21, preferentially leading cells to p53-dependent apoptosis by suppressing p21.
Interaction of the replication proteins and the capsid protein of porcine circovirus type 1 and 2 with host proteins.
Mankertz et al., Berlin, Germany. In Virology, 2009
Six cellular proteins were found to interact with Cap (MKRN1, gC1qR, Par-4, NAP1, NPM1 and Hsp40) and three with Rep (ZNF265, TDG and VG5Q).
Identification of Makorin 1 as a novel SEREX antigen of esophageal squamous cell carcinoma.
Hiwasa et al., Chiba, Japan. In Bmc Cancer, 2008
Makorin 1 is a novel SEREX antigen of esophageal squamous cell carcinoma
Makorin RING finger protein 1 (MKRN1) has negative and positive effects on RNA polymerase II-dependent transcription.
Shemshedini et al., Toledo, United States. In Endocrine, 2006
MKRN1 may represent a nuclear protein with multiple nuclear functions, including regulating RNA polymerase II-catalyzed transcription.
share on facebooktweetadd +1mail to friends