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Search results 101 to 200 out of 221 for Sec13

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Type Details Score
Publication      
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)
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: FANTOM2 Data Curation in Mouse Genome Informatics
Publication        
First Author: Cyagen Biosciences Inc.
Year: 2022
Title: Cyagen Biosciences Website.
Publication
First Author: Stryke D
Year: 2003
Journal: Nucleic Acids Res
Title: BayGenomics: a resource of insertional mutations in mouse embryonic stem cells.
Volume: 31
Issue: 1
Pages: 278-81
Publication      
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
Publication
First Author: Adams DJ
Year: 2024
Journal: Nature
Title: Genetic determinants of micronucleus formation in vivo.
Volume: 627
Issue: 8002
Pages: 130-136
Publication        
First Author: UniProt-GOA
Year: 2012
Title: Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Publication        
First Author: The Gene Ontology Consortium
Year: 2014
Title: Automated transfer of experimentally-verified manual GO annotation data to mouse-rat orthologs
Publication
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
Publication        
First Author: GOA curators
Year: 2016
Title: Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2003
Title: MGI Sequence Curation Reference
Publication        
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
Publication        
First Author: UniProt-GOA
Year: 2012
Title: Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Publication        
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
Publication      
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
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: 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: The Gene Ontology Consortium
Year: 2010
Title: Automated transfer of experimentally-verified manual GO annotation data to mouse-human orthologs
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: 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: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
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 Genome 430 2.0 Array Platform
Publication      
First Author: Allen Institute for Brain Science
Year: 2004
Journal: Allen Institute
Title: Allen Brain Atlas: mouse riboprobes
Publication      
First Author: Mouse Genome Database and National Center for Biotechnology Information
Year: 2000
Journal: Database Release
Title: Entrez Gene Load
Publication      
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
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 (MGI) and The National Center for Biotechnology Information (NCBI)
Year: 2010
Journal: Database Download
Title: Consensus CDS project
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 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
Gene
Type: gene
Organism: dog, domestic
Gene
Type: gene
Organism: macaque, rhesus
Gene
Type: gene
Organism: chimpanzee
UniProt Feature
Begin: 2
Description: Protein SEC13 homolog
Type: chain
End: 322
Allele
Name: SEC13 homolog, nuclear pore and COPII coat complex component; targeted mutation 1, Beatriz Fontoura
Allele Type: Targeted
Attribute String: Conditional ready, Hypomorph
Gene
Type: gene
Organism: rat
Gene
Type: gene
Organism: rat
Gene
Type: gene
Organism: rat
Gene
Type: gene
Organism: frog, African clawed
Gene
Type: gene
Organism: frog, African clawed
Allele  
Name: SEC13 homolog, nuclear pore and COPII coat complex component; gene trap OST127487, Lexicon Genetics
Allele Type: Gene trapped
Allele  
Name: SEC13 homolog, nuclear pore and COPII coat complex component; gene trap OST214239, Lexicon Genetics
Allele Type: Gene trapped
Allele
Name: SEC13 homolog, nuclear pore and COPII coat complex component; endonuclease-mediated mutation 2, Cyagen Biosciences
Allele Type: Endonuclease-mediated
Attribute String: Conditional ready, No functional change
Allele
Name: SEC13 homolog, nuclear pore and COPII coat complex component; endonuclease-mediated mutation 1, Cyagen Biosciences
Allele Type: Endonuclease-mediated
Attribute String: Null/knockout
Allele  
Name: SEC13 homolog, nuclear pore and COPII coat complex component; gene trap XK440, BayGenomics
Allele Type: Gene trapped
Allele  
Name: SEC13 homolog, nuclear pore and COPII coat complex component; gene trap OST109385, Lexicon Genetics
Allele Type: Gene trapped
Allele
Name: SEC13 homolog, nuclear pore and COPII coat complex component; targeted mutation 1.2, Beatriz Fontoura
Allele Type: Targeted
Attribute String: Conditional ready, No functional change
Allele    
Name: SEC13 homolog, nuclear pore and COPII coat complex component; wild type
Allele
Name: SEC13 homolog, nuclear pore and COPII coat complex component; targeted mutation 1.1, Beatriz Fontoura
Allele Type: Targeted
Attribute String: Null/knockout
Strain
Attribute String: coisogenic, endonuclease-mediated mutation, mutant strain
Strain
Attribute String: coisogenic, endonuclease-mediated mutation, mutant strain
Strain
Attribute String: mutant stock, gene trap
Allele  
Name: SEC13 homolog, nuclear pore and COPII coat complex component; gene trap EUCE00147b03, Helmholtz Zentrum Muenchen GmbH
Allele Type: Gene trapped
Allele
Name: SEC13 homolog, nuclear pore and COPII coat complex component; endonuclease-mediated mutation 1, Helmholtz Zentrum Muenchen GmbH
Allele Type: Endonuclease-mediated
Attribute String: Null/knockout
Strain
Attribute String: coisogenic, targeted mutation
Strain
Attribute String: coisogenic, endonuclease-mediated mutation, mutant strain
Genotype
Symbol: Sec13/Sec13
Background: C57BL/6N-Sec13/Ieg
Zygosity: hm
Has Mutant Allele: true
Protein
Organism: Mus musculus/domesticus
Length: 326  
Fragment?: false
Genotype
Symbol: Sec13/Sec13<+>
Background: C57BL/6N-Sec13/Ieg
Zygosity: ht
Has Mutant Allele: true
Protein
Organism: Mus musculus/domesticus
Length: 67  
Fragment?: true
Publication
First Author: Zuccolo M
Year: 2007
Journal: EMBO J
Title: The human Nup107-160 nuclear pore subcomplex contributes to proper kinetochore functions.
Volume: 26
Issue: 7
Pages: 1853-64
Publication
First Author: Loïodice I
Year: 2004
Journal: Mol Biol Cell
Title: The entire Nup107-160 complex, including three new members, is targeted as one entity to kinetochores in mitosis.
Volume: 15
Issue: 7
Pages: 3333-44
Protein Domain
Type: Family
Description: This entry includes nucleoporin Nup37, a component of the Nup107-160 subcomplex of the nuclear pore complex (NPC). Nup107-160 is required for assembly of a functional NPC, as well as normal kinetochore microtubule attachment, mitotic progression and chromosome segregation []. The vertebrate Nup107-160 complex includes NUP160, NUP133, NUP107, NUP98, NUP85, NUP43, NUP37, SEH1 and SEC13 []. This entry also includes some uncharacterised fungal proteins.
Protein Domain
Type: Family
Description: Seh1 and Sec13 are WD40 repeat containing proteins. They are subunits of the Nup84 (Nup107-160 complex in higher eukaryotes) nuclear pore subcomplex []and the the SEA complex (GATOR1 complex in higher eukaryotes) [, , ]. The Nup107-160 complex, which is the major structural subcomplex of the nuclear pore complex (NPC), functions in the regulation of mRNA export as well as in the assembly and distribution of NPCs within the nuclear envelope, and may also have functions independent of nucleocytoplasmic transport [].In budding yeasts, the SEA complex associates with the vacuole and is involved in intracellular trafficking, amino acid biogenesis, and response to nitrogen starvation []. In Drosophila, GATOR1 complex inhibits TORC1 activity in response to amino acid limitation and contributes to multiple aspects of the development []. Besides Nup84 and SEA complexes, Sec13 is also part of the COPII vesicle coat required for ER-to-Golgi transport [, ].
Protein
Organism: Mus musculus/domesticus
Length: 926  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 924  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 336  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 322  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 926  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 924  
Fragment?: false
Publication
First Author: Siniossoglou S
Year: 1996
Journal: Cell
Title: A novel complex of nucleoporins, which includes Sec13p and a Sec13p homolog, is essential for normal nuclear pores.
Volume: 84
Issue: 2
Pages: 265-75
Publication
First Author: Bui KH
Year: 2013
Journal: Cell
Title: Integrated structural analysis of the human nuclear pore complex scaffold.
Volume: 155
Issue: 6
Pages: 1233-43
Protein Domain
Type: Family
Description: Nup84 forms a complex with five proteins, including Nup120, Nup85, Sec13, and a Sec13 homologue. This Nup84 complex in conjunction with Sec13-type proteins is required for correct nuclear pore biogenesis []. Nup107 is the vertebrate homologue of Nup84. The Nup107-160 complex (Nup84 complex in yeast) forms the cytoplasmic and nucleoplasmic rings of the nuclear pore complex (NPC) scaffold, which consists of three stacked rings [].
Publication
First Author: Whittle JR
Year: 2010
Journal: J Cell Biol
Title: Structure of the Sec13-Sec16 edge element, a template for assembly of the COPII vesicle coat.
Volume: 190
Issue: 3
Pages: 347-61
Protein Domain
Type: Domain
Description: Sec31 is a component of the COPII coat complex that mediates formation of transport vesicles from the ER. The central α-helical unit of Sec31 is structurally similar to four large architectural nucleoporins. This α-helical unit, common to COPII and nuclear pore complex proteins, has been termed the ancestral coatomer element 1 (ACE1) []. This entry represents the ACE1 element found in Sec31 and Sec16, which also contains an ACE1 []. The ACE1 element of Sec31 can functionally replace that of Sec16. Both Sec31 and Sec16 bind to Sec13 [].
Protein Domain
Type: Domain
Description: This entry represents the Nuclear pore complex protein Nup96 from animals its homologues from yeast and plants.Nuclear pore complexes (NPCs) facilitate all nucleocytoplasmic transport in eukaryotic cells, playing essential roles in cellular homeostasis. The NPC is a modular structure composed of multiple copies of ~30 proteins (nucleoporins, Nups) arranged into distinct subcomplexes [, ]. A number of these peptides are synthesised as precursors and undergo self-catalyzed cleavage. The largest NPC sub-complex is the heptameric Y-shaped mammalian Nup107-Nup160 complex (called Nup84 complex in budding yeast), an essential scaffolding component of the NPC [, , ]. Nup98 and Nup96 are encoded by the same gene that produces a 190 kDa polyprotein with autoproteolytic activity which generates the N-terminal NUP98 and C-terminal NUP96 proteins, part of the Nup107-Nup160 subcomplex [, ]. The yeast homologue Nup145 undergoes the similar proteolytic event to produce Nup145N and Nup145C, which are part of the Nup84 complex. The function of the heptamer is to coat the curvature of the nuclear pore complex between the inner and outer nuclear membranes. Nup96, which is predicted to be an alpha helical solenoid, complexes with Sec13 in the middle of the heptamer. The interaction between Nup96 and Sec13 is the point of curvature in the heptameric complex [, ].
Publication
First Author: Tang BL
Year: 2001
Journal: J Biol Chem
Title: A membrane protein enriched in endoplasmic reticulum exit sites interacts with COPII.
Volume: 276
Issue: 43
Pages: 40008-17
Publication
First Author: Long L
Year: 2021
Journal: Nature
Title: CRISPR screens unveil signal hubs for nutrient licensing of T cell immunity.
Volume: 600
Issue: 7888
Pages: 308-313
Publication
First Author: Pearce LR
Year: 2011
Journal: Biochem J
Title: Protor-1 is required for efficient mTORC2-mediated activation of SGK1 in the kidney.
Volume: 436
Issue: 1
Pages: 169-79
Protein
Organism: Mus musculus/domesticus
Length: 800  
Fragment?: true
Protein Domain
Type: Family
Description: Seh1 is a subunit of the Nup84 (Nup107-160 complex in higher eukaryotes) nuclear pore subcomplex []and the the SEA complex (GATOR1 complex in higher eukaryotes) [, , ]. The Nup107-160 complex, which is the major structural subcomplex of the nuclear pore complex (NPC), functions in the regulation of mRNA export as well as in the assembly and distribution of NPCs within the nuclear envelope, and may also have functions independent of nucleocytoplasmic transport [].In budding yeasts, the SEA complex associates with the vacuole and is involved in intracellular trafficking, amino acid biogenesis, and response to nitrogen starvation []. In Drosophila, GATOR1 complex inhibits TORC1 activity in response to amino acid limitation and contributes to multiple aspects of the development []. Both Sec13 and Seh1 are positive regulators of TORC1 signalling [].
Publication
First Author: Vasu S
Year: 2001
Journal: J Cell Biol
Title: Novel vertebrate nucleoporins Nup133 and Nup160 play a role in mRNA export.
Volume: 155
Issue: 3
Pages: 339-54
Publication
First Author: Dokudovskaya S
Year: 2002
Journal: Mol Cell
Title: Cleave to leave: structural insights into the dynamic organization of the nuclear pore complex.
Volume: 10
Issue: 2
Pages: 221-3
Publication
First Author: Robinson MA
Year: 2005
Journal: J Biol Chem
Title: Multiple conformations in the ligand-binding site of the yeast nuclear pore-targeting domain of Nup116p.
Volume: 280
Issue: 42
Pages: 35723-32
Publication
First Author: Hsia KC
Year: 2007
Journal: Cell
Title: Architecture of a coat for the nuclear pore membrane.
Volume: 131
Issue: 7
Pages: 1313-26
Publication  
First Author: Hampoelz B
Year: 2019
Journal: Annu Rev Biophys
Title: Structure and Assembly of the Nuclear Pore Complex.
Volume: 48
Pages: 515-536
Publication
First Author: Kramarz K
Year: 2020
Journal: Nat Commun
Title: The nuclear pore primes recombination-dependent DNA synthesis at arrested forks by promoting SUMO removal.
Volume: 11
Issue: 1
Pages: 5643
Publication
First Author: Nordeen SA
Year: 2020
Journal: Nat Commun
Title: Yeast Nup84-Nup133 complex structure details flexibility and reveals conservation of the membrane anchoring ALPS motif.
Volume: 11
Issue: 1
Pages: 6060
Publication
First Author: Debler EW
Year: 2010
Journal: Nucleus
Title: Characterization of the membrane-coating Nup84 complex: paradigm for the nuclear pore complex structure.
Volume: 1
Issue: 2
Pages: 150-7
Publication
First Author: Brohawn SG
Year: 2009
Journal: Nat Struct Mol Biol
Title: Molecular architecture of the Nup84-Nup145C-Sec13 edge element in the nuclear pore complex lattice.
Volume: 16
Issue: 11
Pages: 1173-7
Publication
First Author: Teixeira MT
Year: 1999
Journal: J Biol Chem
Title: Self-catalyzed cleavage of the yeast nucleoporin Nup145p precursor.
Volume: 274
Issue: 45
Pages: 32439-44
Publication
First Author: Sampathkumar P
Year: 2010
Journal: Proteins
Title: Structures of the autoproteolytic domain from the Saccharomyces cerevisiae nuclear pore complex component, Nup145.
Volume: 78
Issue: 8
Pages: 1992-8
Publication
First Author: García-Martínez JM
Year: 2008
Journal: Biochem J
Title: mTOR complex 2 (mTORC2) controls hydrophobic motif phosphorylation and activation of serum- and glucocorticoid-induced protein kinase 1 (SGK1).
Volume: 416
Issue: 3
Pages: 375-85
Protein
Organism: Mus musculus/domesticus
Length: 1816  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1816  
Fragment?: false
Publication
First Author: Hodel AE
Year: 2002
Journal: Mol Cell
Title: The three-dimensional structure of the autoproteolytic, nuclear pore-targeting domain of the human nucleoporin Nup98.
Volume: 10
Issue: 2
Pages: 347-58
Protein Domain
Type: Homologous_superfamily
Description: Nuclear pore complexes (NPCs) facilitate all nucleocytoplasmic transport in eukaryotic cells, playing essential roles in cellular homeostasis. The NPC is a modular structure composed of multiple copies of ~30 proteins (nucleoporins, Nups) arranged into distinct subcomplexes [, ]. A number of these peptides are synthesised as precursors and undergo self-catalyzed cleavage. The largest NPC sub-complex is the heptameric Y-shaped mammalian Nup107-Nup160 complex (called Nup84 complex in budding yeast), an essential scaffolding component of the NPC [, , ]. Nup98 and Nup96 are encoded by the same gene that produces a 190 kDa polyprotein with autoproteolytic activity which generates the N-terminal NUP98 and C-terminal NUP96 proteins, part of the Nup107-Nup160 subcomplex [, ]. The yeast homologue Nup145 undergoes the similar proteolytic event to produce Nup145N and Nup145C, which are part of the Nup84 complex. The function of the heptamer is to coat the curvature of the nuclear pore complex between the inner and outer nuclear membranes. Nup96, which is predicted to be an alpha helical solenoid, complexes with Sec13 in the middle of the heptamer. The interaction between Nup96 and Sec13 is the point of curvature in the heptameric complex [, ].The proteolytic cleavage site of yeast Nup145p has been mapped upstream of an evolutionary conserved serine residue. Then, Nup145C form the heptameric Y-complex together with six other proteins while Nup145N shuttle between the NPC and the nuclear interior. [, ].Nup98,a component of the nuclear pore that plays its primary role in the export of RNAs, is expressed in two forms, derived from alternate mRNA splicing. Both forms are processed into two peptides through autoproteolysis mediated by the C-terminal domain of hNup98. The three-dimensional structure of the C-terminal domain reveals a novel protein fold, and thus a new class of autocatalytic proteases. The structure further reveals that the suggested nucleoporin RNA binding motif is unlikely to bind to RNA [].The following nucleoporins share an ~150-residue C-terminal domain responsible for NPC targeting [, ]:Vertebrate Nup98, a component of the nuclear pore that plays its primary role in the export of RNAs.Yeast Nup100, plays an important role in several nuclear export and import pathways including poly(A)+ RNA and protein transport.Yeast Nup116, involved in mRNA export and protein transport.Yeast Nup145, involved in nuclear poly(A)+ RNA and tRNA export.The NUP C-terminal domains of Nup98 and Nup145 possess peptidase S59autoproteolytic activity. The autoproteolytic sites of Nup98 and Nup145each occur immediately C-terminal to the NUP C-terminal domain. Thus, althoughthis domain occurs in the middle of each precursor polypeptide, it winds up atthe C-terminal end of the N-terminal cleavage product. Cleavage of the peptidechains are necessary for the proper targeting to the nuclear pore [, ].The NUP C-terminal domain adopts a predominantly β-strand structure. The molecule consists of a six-stranded β-sheet sandwiched against a two-stranded β-sheet and flanked by α-helical regions. The N-terminalhelical region consists of two short helices, whereas the stretch on the opposite side of molecule consists of a single, longer helix [, ].