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Search results 101 to 146 out of 146 for Znrf3

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0.025s

Type

Details

Score

Publication

- | J:63103

First Author:	Mouse Genome Database and National Center for Biotechnology Information
Year:	2000
Journal:	Database Release
Title:	Entrez Gene Load

•

Publication

- | J:85324

First Author:	Mouse Genome Informatics Group
Year:	2003
Journal:	Database Procedure
Title:	Automatic Encodes (AutoE) Reference

•

Publication

- | J:53168

First Author:	Bairoch A
Year:	1999
Journal:	Database Release
Title:	SWISS-PROT Annotated protein sequence database

•

Publication

- | J:91388

First Author:	Mouse Genome Informatics Scientific Curators
Year:	2005

Title:	Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations

•

Publication

- | J:155721

First Author:	Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI)
Year:	2010
Journal:	Database Download
Title:	Consensus CDS project

•

Publication

- | J:155221

First Author:	Mouse Genome Informatics
Year:	2010
Journal:	Database Release
Title:	Protein Ontology Association Load.

•

Publication

- | J:90438

First Author:	Mouse Genome Informatics Scientific Curators
Year:	2005

Title:	Obtaining and loading genome assembly coordinates from NCBI annotations

•

Publication

- | J:144086

First Author:	Mouse Genome Informatics Scientific Curators
Year:	2009
Journal:	Database Download
Title:	Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Gene 1.0 ST Array Platform

•

Publication

- | J:262123

First Author:	Allen Institute for Brain Science
Year:	2004
Journal:	Allen Institute
Title:	Allen Brain Atlas: mouse riboprobes

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UniProt Feature

Begin:	53
Description:	E3 ubiquitin-protein ligase ZNRF3
Type:	chain
End:	913

•

HT Experiment

GSE202940 | Kinetic comparative analysis of gene expression in whole adrenal glands from Znrf3 cKO and control mice


Experiment Type:	RNA-Seq
Study Type:	WT vs. Mutant
Source:	GEO

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Interaction Experiment

Peng WC (2013)

Description:

Structures of Wnt-antagonist ZNRF3 and its complex with R-spondin 1 and implications for signaling.

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Allele

Gt(ROSA)26Sor<tm10(tetO-Znrf3,CAG-rtTA)Npa> | MGI:6724075

Name:	gene trap ROSA 26, Philippe Soriano; targeted mutation 10, Novartis Pharma AG
Allele Type:	Targeted
Attribute String:	Inducible, Inserted expressed sequence

•

Protein Domain

IPR045903 | ZNRF3_Znf_RING

Type:

Domain

Description:

This entry represents the RING-type zinc finger domain of E3 ubiquitin-protein ligase ZNRF3 (Zinc/RING finger protein 3), a transmembrane enzyme () homologue of Ring finger protein 43 (RNF43). It is predominantly found in vertebrates.In humans, ZNRF3 acts as a negative regulator of the Wnt signaling pathway by mediating the ubiquitination and subsequent degradation of Wnt receptor complex components Frizzled and LRP6 [, , ]. ZNRF3 also functions as a tumour suppressor in the intestinal stem cell zone by restricting the size of the intestinal stem cell zone []. In frogs (Xenopus), ZNRF3 and RNF43 were seen to play a key role in limb specification, constituting a master switch along with RSPO2, which may have implications for regenerative medicine []. Zinc finger (Znf) domains are relatively small protein motifs which contain multiple finger-like protrusions that make tandem contacts with their target molecule. Some of these domains bind zinc, but many do not; instead binding other metals such as iron, or no metal at all. For example, some family members form salt bridges to stabilise the finger-like folds. They were first identified as a DNA-binding motif in transcription factor TFIIIA from Xenopus laevis (African clawed frog), however they are now recognised to bind DNA, RNA, protein and/or lipid substrates [, , , , ]. Their binding properties depend on the amino acid sequence of the finger domains and of the linker between fingers, as well as on the higher-order structures and the number of fingers. Znf domains are often found in clusters, where fingers can have different binding specificities. There are many superfamilies of Znf motifs, varying in both sequence and structure. They display considerable versatility in binding modes, even between members of the same class (e.g. some bind DNA, others protein), suggesting that Znf motifs are stable scaffolds that have evolved specialised functions. For example, Znf-containing proteins function in gene transcription, translation, mRNA trafficking, cytoskeleton organisation, epithelial development, cell adhesion, protein folding, chromatin remodelling and zinc sensing, to name but a few []. Zinc-binding motifs are stable structures, and they rarely undergo conformational changes upon binding their target.

•

Publication

35039505 | J:319631

First Author:	Belenguer G
Year:	2022
Journal:	Nat Commun
Title:	RNF43/ZNRF3 loss predisposes to hepatocellular-carcinoma by impairing liver regeneration and altering the liver lipid metabolic ground-state.
Volume:	13
Issue:	1
Pages:	334

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Publication

18313049 | -

First Author:	Sugiura T
Year:	2008
Journal:	Exp Cell Res
Title:	A cancer-associated RING finger protein, RNF43, is a ubiquitin ligase that interacts with a nuclear protein, HAP95.
Volume:	314
Issue:	7
Pages:	1519-28

•

Publication

29752411 | J:265323

First Author:	Park S
Year:	2018
Journal:	J Biol Chem
Title:	Differential activities and mechanisms of the four R-spondins in potentiating Wnt/β-catenin signaling.
Volume:	293
Issue:	25
Pages:	9759-9769

•

Publication

28368424 | J:248119

First Author:	Batisse-Lignier M
Year:	2017
Journal:	Oncogene
Title:	P53/Rb inhibition induces metastatic adrenocortical carcinomas in a preclinical transgenic model.
Volume:	36
Issue:	31
Pages:	4445-4456

•

Publication

30146491 | J:308689

First Author:	Gyllborg D
Year:	2018
Journal:	Stem Cell Reports
Title:	The Matricellular Protein R-Spondin 2 Promotes Midbrain Dopaminergic Neurogenesis and Differentiation.
Volume:	11
Issue:	3
Pages:	651-664

•

Publication

26123262 | -

First Author:	Zebisch M
Year:	2015
Journal:	J Struct Biol
Title:	Crystal structure of R-spondin 2 in complex with the ectodomains of its receptors LGR5 and ZNRF3.
Volume:	191
Issue:	2
Pages:	149-55

•

Publication

19238248 | -

First Author:	Ayadi L
Year:	2008
Journal:	Bioinformation
Title:	Molecular modelling of the TSR domain of R-spondin 4.
Volume:	3
Issue:	3
Pages:	119-23

•

Publication

17041604 | J:116076

First Author:	Blaydon DC
Year:	2006
Journal:	Nat Genet
Title:	The gene encoding R-spondin 4 (RSPO4), a secreted protein implicated in Wnt signaling, is mutated in inherited anonychia.
Volume:	38
Issue:	11
Pages:	1245-7

•

Publication

21108931 | -

First Author:	Shinada K
Year:	2011
Journal:	Biochem Biophys Res Commun
Title:	RNF43 interacts with NEDL1 and regulates p53-mediated transcription.
Volume:	404
Issue:	1
Pages:	143-7

•

Publication

23096461 | -

First Author:	Ryland GL
Year:	2013
Journal:	J Pathol
Title:	RNF43 is a tumour suppressor gene mutated in mucinous tumours of the ovary.
Volume:	229
Issue:	3
Pages:	469-76

•

Publication

29018044 | -

First Author:	Serra S
Year:	2018
Journal:	J Clin Pathol
Title:	Rnf43.
Volume:	71
Issue:	1
Pages:	1-6

•

Publication

25344691 | -

First Author:	Giannakis M
Year:	2014
Journal:	Nat Genet
Title:	RNF43 is frequently mutated in colorectal and endometrial cancers.
Volume:	46
Issue:	12
Pages:	1264-6

•

Protein Domain

IPR042993 | RSPO2/4

Type:

Family

Description:

The R-spondin (RSPO) family is a small group of four secreted proteins (RSPO1-RSPO4) that have pleiotropic functions in development and stem cell growth by strongly enhancing Wnt pathway activation. They contain an N-terminal secretory signal peptide sequence, two tandem furin-like cysteine-rich (Fu-CRD) domains, a thrombospondin type I repeat (TSP) domain, and a C-terminal basic amino acid-rich (BR) domain. Leucine-rich repeat-containing G-protein-coupled receptor 4 (LGR4), LGR5, and LGR6 have been identified as receptors for RSPOs [].RSPO2 is a secreted protein that belongs to the R-spondin (RSPO) family. Interestingly, it is one of the two members (RSPO2 and RSPO3) of the family capable of potentiating WNT signaling in cells lacking all three LGRs (Leucine-rich repeat-containing G-protein-coupled receptor 4/5/6) []. It plays a crucial role in limb specification, amplifying the Wnt signaling pathway independently of LGR4-6 receptors, possibly by acting as a direct antagonistic ligand to RNF43 and ZNRF3, hence governing the number of limbs an embryo should form []. It has been shown to promote midbrain dopaminergic neurogenesis and differentiation in human stem cells []. Its structures in complex with the ectodomains of its receptors LGR5 and ZNRF3 have been revealed []. RSPO4 is a secreted protein that belongs to the R-spondin (RSPO) family. It has been associated with embryonic nail development [, ].

•

Protein Domain

IPR045907 | RNF43_Znf_RING

Type:

Domain

Description:

This entry represents the RING-type zinc finger domain of E3 ubiquitin-protein ligase RNF43. Proteins containing this domain are found in vertebrates. RNF43 acts as a negative regulator of the Wnt signaling pathway by mediating the ubiquitination and subsequent degradation of Wnt receptor complex components Frizzled and LRP6 [, , ]. RNF43 also interacts with NEDD-4-like ubiquitin-protein ligase-1 (NEDL1) and regulates p53-mediated transcription []. It may also be involved in cell growth control potentially through the interaction with, a chromatin-associated protein interfacing the nuclear envelope []. Mutations of RNF43 have been identified in various tumours, including colorectal cancer (CRC), endometrial cancer, mucinous ovarian tumours, gastric adenocarcinoma, pancreatic ductal adenocarcinoma, liver fluke-associated cholangiocarcinoma, hepatocellular carcinoma, and glioma [, , ]. RNF43 contains an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane (TM) domain and a C3H2C3-type RING-H2 finger domain followed by a long C-terminal region [].In frogs (Xenopus), ZNRF3 and RNF43 were seen to play a key role in limb specification, constituting a master switch along with RSPO2, which may have implications for regenerative medicine [].

•

Publication

28467820 | J:252529

First Author:	Yan KS
Year:	2017
Journal:	Nature
Title:	Non-equivalence of Wnt and R-spondin ligands during Lgr5⁺ intestinal stem-cell self-renewal.
Volume:	545
Issue:	7653
Pages:	238-242

•

Publication

29405118 | J:259879

First Author:	Lebensohn AM
Year:	2018
Journal:	Elife
Title:	R-spondins can potentiate WNT signaling without LGRs.
Volume:	7

•

Publication

23756652 | -

First Author:	Wang D
Year:	2013
Journal:	Genes Dev
Title:	Structural basis for R-spondin recognition by LGR4/5/6 receptors.
Volume:	27
Issue:	12
Pages:	1339-44

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Protein

Q5NCP0

Organism:	Mus musculus/domesticus
Length:	784
Fragment?:	false

•

Protein

Q8BJ73

Organism:	Mus musculus/domesticus
Length:	228
Fragment?:	false

•

Protein

A3KMI3

Organism:	Mus musculus/domesticus
Length:	657
Fragment?:	false

•

Protein

E9PWJ5

Organism:	Mus musculus/domesticus
Length:	743
Fragment?:	false

•

Protein

A0AUN1

Organism:	Mus musculus/domesticus
Length:	221
Fragment?:	true

•

Protein

Q0P5Y9

Organism:	Mus musculus/domesticus
Length:	228
Fragment?:	false

•

Protein

Q8BFU0

Organism:	Mus musculus/domesticus
Length:	243
Fragment?:	false

•

Publication

12665246 | -

First Author:	Matthews JM
Year:	2002
Journal:	IUBMB Life
Title:	Zinc fingers--folds for many occasions.
Volume:	54
Issue:	6
Pages:	351-5

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Publication

17210253 | -

First Author:	Gamsjaeger R
Year:	2007
Journal:	Trends Biochem Sci
Title:	Sticky fingers: zinc-fingers as protein-recognition motifs.
Volume:	32
Issue:	2
Pages:	63-70

•

Publication

15963892 | -

First Author:	Hall TM
Year:	2005
Journal:	Curr Opin Struct Biol
Title:	Multiple modes of RNA recognition by zinc finger proteins.
Volume:	15
Issue:	3
Pages:	367-73

•

Publication

15718139 | -

First Author:	Brown RS
Year:	2005
Journal:	Curr Opin Struct Biol
Title:	Zinc finger proteins: getting a grip on RNA.
Volume:	15
Issue:	1
Pages:	94-8

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Publication

10529348 | -

First Author:	Klug A
Year:	1999
Journal:	J Mol Biol
Title:	Zinc finger peptides for the regulation of gene expression.
Volume:	293
Issue:	2
Pages:	215-8

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Publication

11179890 | -

First Author:	Laity JH
Year:	2001
Journal:	Curr Opin Struct Biol
Title:	Zinc finger proteins: new insights into structural and functional diversity.
Volume:	11
Issue:	1
Pages:	39-46

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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

19468303 | -

First Author:	Church DM
Year:	2009
Journal:	PLoS Biol
Title:	Lineage-specific biology revealed by a finished genome assembly of the mouse.
Volume:	7
Issue:	5
Pages:	e1000112

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