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Search results 101 to 149 out of 149 for Xirp2

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0.02s
Type Details Score
Publication
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
Publication        
First Author: MGD Nomenclature Committee
Year: 1995
Title: Nomenclature Committee Use
Publication
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
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2000
Title: Gene Ontology Annotation by electronic association of SwissProt Keywords with GO terms
Publication      
First Author: The Jackson Laboratory Mouse Radiation Hybrid Database
Year: 2004
Journal: Database Release
Title: Mouse T31 Radiation Hybrid Data Load
Publication
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
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Title: Human to Mouse ISO GO annotation transfer
Publication
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
Publication      
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome U74 Array Platform (A, B, C v2).
Publication      
First Author: MGI Genome Annotation Group and UniGene Staff
Year: 2015
Journal: Database Download
Title: MGI-UniGene Interconnection Effort
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Mouse Genome Informatics Computational Sequence to Gene Associations
Publication        
First Author: Marc Feuermann, Huaiyu Mi, Pascale Gaudet, Dustin Ebert, Anushya Muruganujan, Paul Thomas
Year: 2010
Title: Annotation inferences using phylogenetic trees
Publication      
First Author: Bairoch A
Year: 1999
Journal: Database Release
Title: SWISS-PROT Annotated protein sequence database
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
Publication      
First Author: Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI)
Year: 2010
Journal: Database Download
Title: Consensus CDS project
Publication      
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
Publication      
First Author: Mouse Genome Database and National Center for Biotechnology Information
Year: 2000
Journal: Database Release
Title: Entrez Gene Load
Publication      
First Author: Allen Institute for Brain Science
Year: 2004
Journal: Allen Institute
Title: Allen Brain Atlas: mouse riboprobes
Publication      
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      
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
Allele
Name: xin actin-binding repeat containing 2; targeted mutation 1, inGenious Targeting Laboratory
Allele Type: Targeted
Attribute String: Conditional ready, Hypomorph
Allele
Name: xin actin-binding repeat containing 2; targeted mutation 1.1, inGenious Targeting Laboratory
Allele Type: Targeted
Attribute String: Hypomorph
Publication
First Author: Ottenheijm CA
Year: 2010
Journal: Physiology (Bethesda)
Title: Lifting the nebula: novel insights into skeletal muscle contractility.
Volume: 25
Issue: 5
Pages: 304-10
Publication
First Author: Chu M
Year: 2016
Journal: J Exp Biol
Title: Nebulin, a multi-functional giant.
Volume: 219
Issue: Pt 2
Pages: 146-52
Publication  
First Author: Chen Y
Year: 2020
Journal: J Mol Cell Cardiol
Title: Identifying modifier genes for hypertrophic cardiomyopathy.
Volume: 144
Pages: 119-126
Publication
First Author: Carroll S
Year: 2004
Journal: J Cell Sci
Title: N-RAP scaffolds I-Z-I assembly during myofibrillogenesis in cultured chick cardiomyocytes.
Volume: 117
Issue: Pt 1
Pages: 105-14
Publication
First Author: Carroll SL
Year: 2001
Journal: J Cell Sci
Title: Targeting and functional role of N-RAP, a nebulin-related LIM protein, during myofibril assembly in cultured chick cardiomyocytes.
Volume: 114
Issue: Pt 23
Pages: 4229-38
Protein Domain
Type: Domain
Description: Nebulin is a giant filamentous protein (600-900 kD) that plays a role in numerous cellular processes including regulation of muscle contraction, Z-disc formation, and myofibril organization and assembly in skeletal muscle. It contains an N-terminal LIM domain, many nebulin repeats/super repeats, and a C-terminal SH3 domain. The N terminus of nebulin is located near the pointed end of the thin filament and contains a binding site for the actin filament capping protein tropomodulin (Tmod). The super repeat region of nebulin has been shown to interact with kelch-like family member 40 (KLHL40). The C terminus of nebulin is located within the highly specialized boundary of the sarcomere (Z-disc), and plays an important role in myofibril assembly, mechanosensing, signaling, force generation and transmission, and sarcolemmal resilience. The SH3 domain of nebulin interacts with multiple proteins, such as alpha-actinin, XIRP2 and titin []. Mutations in nebulin can cause nemaline myopathy, characterised by muscle weakness which can be severe and can lead to neonatal lethality []. This entry represents the SH3 domain of Nebulin.
Protein Domain
Type: Family
Description: This entry include nebulin and nebulin-related-anchoring protein (N-RAP). Nebulin is a giant filamentous protein (600-900 kD) that plays a role in numerous cellular processes including regulation of muscle contraction, Z-disc formation, and myofibril organization and assembly in skeletal muscle. It contains an N-terminal LIM domain, many nebulin repeats/super repeats, and a C-terminal SH3 domain. The N terminus of nebulin is located near the pointed end of the thin filament and contains a binding site for the actin filament capping protein tropomodulin (Tmod). The super repeat region of nebulin has been shown to interact with kelch-like family member 40 (KLHL40). The C terminus of nebulin is located within the highly specialized boundary of the sarcomere (Z-disc), and plays an important role in myofibril assembly, mechanosensing, signaling, force generation and transmission, and sarcolemmal resilience. The SH3 domain of nebulin interacts with multiple proteins, such as alpha-actinin, XIRP2 and titin []. Mutations in nebulin can cause nemaline myopathy, characterised by muscle weakness which can be severe and can lead to neonatal lethality []. Nebulin-related-anchoring protein (N-RAP) is a muscle-specific protein that may serve as a scaffold for premyofibril assembly [, ]. N-RAP contains a N-terminal LIM domain (LIM), the C-terminal actin-binding nebulin super repeats and the nebulin-related simple repeats (IB) in between the two []. The N-terminal IB region is essential for alpha-actinin organisation, while the N-RAP super repeats are essential for sarcomeric actin organisation [].
Publication
First Author: Lu S
Year: 2003
Journal: J Cell Sci
Title: New N-RAP-binding partners alpha-actinin, filamin and Krp1 detected by yeast two-hybrid screening: implications for myofibril assembly.
Volume: 116
Issue: Pt 11
Pages: 2169-78
Protein
Organism: Mus musculus/domesticus
Length: 354  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 269  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 1190  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 1190  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 342  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 424  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 387  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 1358  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 7488  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 7523  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 6909  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 3044  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 7152  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1728  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1692  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 768  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 768  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 1485  
Fragment?: false