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Search results 101 to 157 out of 157 for Gp9

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Type Details Score
Publication
- | J:73796
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Function or Process or Component Unknown following Literature Review
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Publication
24194600 | J:228563
First Author: Koscielny G
Year: 2014
Journal: Nucleic Acids Res
Title: The International Mouse Phenotyping Consortium Web Portal, a unified point of access for knockout mice and related phenotyping data.
Volume: 42
Issue: Database issue
Pages: D802-9
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Publication
- | J:204739
     
First Author: International Knockout Mouse Consortium
Year: 2014
Journal: Database Download
Title: MGI download of modified allele data from IKMC and creation of new knockout alleles
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Publication
- | J:136110
     
First Author: Velocigene
Year: 2008
Journal: MGI Direct Data Submission
Title: Alleles produced for the KOMP project by Velocigene (Regeneron Pharmaceuticals)
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Publication
- | J:204812
     
First Author: International Mouse Strain Resource
Year: 2014
Journal: Database Download
Title: MGI download of germline transmission data for alleles from IMSR strain data
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Publication
- | J:211773
     
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
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Publication
38355793 | J:345621
First Author: Adams DJ
Year: 2024
Journal: Nature
Title: Genetic determinants of micronucleus formation in vivo.
Volume: 627
Issue: 8002
Pages: 130-136
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Publication
- | J:23000
       
First Author: MGD Nomenclature Committee
Year: 1995
Title: Nomenclature Committee Use
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Publication
- | J:293217
       
First Author: GemPharmatech
Year: 2020
Title: GemPharmatech Website.
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Publication
- | J:326541
       
First Author: Cyagen Biosciences Inc.
Year: 2022
Title: Cyagen Biosciences Website.
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Publication
- | J:60000
       
First Author: UniProt-GOA
Year: 2012
Title: Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
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Publication
- | J:68900
     
First Author: The Jackson Laboratory Mouse Radiation Hybrid Database
Year: 2004
Journal: Database Release
Title: Mouse T31 Radiation Hybrid Data Load
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Publication
- | J:164563
       
First Author: The Gene Ontology Consortium
Year: 2010
Title: Automated transfer of experimentally-verified manual GO annotation data to mouse-human orthologs
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Publication
21267068 | J:153498
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
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Publication
- | J:157972
     
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).
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Publication
- | J:57747
     
First Author: MGI Genome Annotation Group and UniGene Staff
Year: 2015
Journal: Database Download
Title: MGI-UniGene Interconnection Effort
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Publication
- | J:63103
     
First Author: Mouse Genome Database and National Center for Biotechnology Information
Year: 2000
Journal: Database Release
Title: Entrez Gene Load
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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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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
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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
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Publication
- | J:85324
     
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
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Publication
- | J:53168
     
First Author: Bairoch A
Year: 1999
Journal: Database Release
Title: SWISS-PROT Annotated protein sequence database
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Publication
- | J:91388
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations
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Publication
- | J:155221
     
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
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Publication
- | J:90438
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
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Publication
- | J:144087
     
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
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Protein Domain
IPR027412 | Gp9_C_dom_sf
Type: Homologous_superfamily
Description: The Bacteriophage T4 is a double-stranded, structurally complex virus that infects Escherichia coli. Gene product 9 (Gp9) connects the long tail fibres to the baseplate, and triggers baseplate reorganisation and tail contraction after virus attachment to the host cell. The Gp9 protein forms a homotrimer, with each monomer having three domains: the N-terminal α-helical domain forms a triple coiled coil, the middle domain is a mixed, seven-stranded beta sandwich with a unique fold, and the C-terminal domain is a eight-stranded β-sandwich with similarity to jellyroll viral capsid protein structures []. The flexible loops that occur between domains may enable the conformational changes necessary during infection. This superfamily represents the Gp9 C-terminal domain.
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Publication
10545330 | -
First Author: Kostyuchenko VA
Year: 1999
Journal: Structure
Title: The structure of bacteriophage T4 gene product 9: the trigger for tail contraction.
Volume: 7
Issue: 10
Pages: 1213-22
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Gene
2812 | GP1BB
Type: gene
Organism: human
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Publication
13677051 | -
 
First Author: Cerritelli ME
Year: 2003
Journal: Adv Protein Chem
Title: Molecular mechanisms in bacteriophage T7 procapsid assembly, maturation, and DNA containment.
Volume: 64
Pages: 301-23
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Publication
16211007 | -
First Author: Agirrezabala X
Year: 2005
Journal: EMBO J
Title: Maturation of phage T7 involves structural modification of both shell and inner core components.
Volume: 24
Issue: 21
Pages: 3820-9
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Protein Domain
IPR008768 | Gp9-like
Type: Family
Description: This family includes the capsid assembly protein Gp9 (scaffolding protein) of bacteriophage T7, similar viral proteins and prophages from Proteobacteria. Gp9 facilitates assembly by binding to Gp10 hexamers but not the pentamers and locking them into a morphogenically correct conformation [, ].
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Protein Coding Gene
MGI:1333744 | Gp1ba
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:107852 | Gp1bb
Type: protein_coding_gene
Organism: mouse, laboratory
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Allele
Gp1ba<tm1Ware> | MGI:2181691
Name: glycoprotein 1b, alpha polypeptide; targeted mutation 1, Jerry Ware
Allele Type: Targeted
Attribute String: Null/knockout
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Allele
Gp1bb<tm1Ware> | MGI:3510459
Name: glycoprotein Ib, beta polypeptide; targeted mutation 1, Jerry Ware
Allele Type: Targeted
Attribute String: Null/knockout
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Allele
Gp1bb<tm1Frla> | MGI:3793296
Name: glycoprotein Ib, beta polypeptide; targeted mutation 1, Francois Lanza
Allele Type: Targeted
Attribute String: Null/knockout
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Allele
Gp1bb<tm2Frla> | MGI:3793297
Name: glycoprotein Ib, beta polypeptide; targeted mutation 2, Francois Lanza
Allele Type: Targeted
Attribute String: Humanized sequence, Hypomorph, Inserted expressed sequence
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Genotype
Genotype
Symbol: Gp1bb/Gp1bb
Background: Not Specified
Zygosity: hm
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Gp1bb/Gp1bb<+>
Background: Not Specified
Zygosity: ht
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Gp1ba/Gp1ba
Background: involves: 129S1/Sv * 129X1/SvJ
Zygosity: hm
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Gp1bb/Gp1bb
Background: involves: 129S2/SvPas * C57BL/6
Zygosity: hm
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Gp1bb/Gp1bb
Background: involves: 129S2/SvPas * C57BL/6
Zygosity: hm
Has Mutant Allele: true
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DO Term
DOID:2217 | Bernard-Soulier syndrome
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Publication
12626685 | -
First Author: Miller ES
Year: 2003
Journal: Microbiol Mol Biol Rev
Title: Bacteriophage T4 genome.
Volume: 67
Issue: 1
Pages: 86-156, table of contents
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Protein Domain
IPR027411 | Gp9/Gp10_mid_dom_sf
Type: Homologous_superfamily
Description: This superfamily represents the middle domain found in baseplate structural protein Gp9 and Gp10 of bacteriophage T4.The Bacteriophage T4 is a double-stranded, structurally complex virus that infects Escherichia coli. Gene product 9 (Gp9) connects the long tail fibres to the baseplate, and triggers baseplate reorganisation and tail contraction after virus attachment to the host cell. The Gp9 protein forms a homotrimer, with each monomer having three domains: the N-terminal α-helical domain forms a triple coiled coil, the middle domain is a mixed, seven-stranded beta sandwich with a unique fold, and the C-terminal domain is a eight-stranded β-sandwich with similarity to jellyroll viral capsid protein structures []. The flexible loops that occur between domains may enable the conformational changes necessary during infection. Together with gp11, gp10 initiates the assembly of wedges that then go on to associate with a hub to form the viral baseplate [].
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Gene
2811 | GP1BA
Type: gene
Organism: human
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Protein Domain
IPR036240 | Gp9-like_sf
Type: Homologous_superfamily
Description: Members of this entry are similar to gene products 9 (gp9) and 10 (gp10) of bacteriophage T4. Both proteins are components of the viral baseplate []. Gp9 connects the long tail fibres of the virus to the baseplate and triggers tail contraction after viral attachment to a host cell. The protein is active as a trimer, with each monomer being composed of three domains. The N-terminal domain consists of an extended polypeptide chain and two alpha helices. The alpha1 helix from each of the three monomers in the trimer interacts with its counterparts to form a coiled-coil structure. The middle domain is a seven-stranded β-sandwich that is thought to be a novel protein fold. The C-terminal domain is thought to be essential for gp9 trimerisation and is organised into an eight- stranded antiparallel β-barrel, which was found to resemble the 'jelly roll' fold found in many viral capsid proteins. The long flexible region between the N-terminal and middle domains may be required for the function of gp9 to transmit signals from the long tail fibres []. Together with gp11, gp10 initiates the assembly of wedges that then go on to associate with a hub to form the viral baseplate [].
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Protein Domain
IPR008987 | Baseplate_struct_prot_Gp9/10
Type: Family
Description: The members of this family are similar to gene products 9 (gp9) and 10 (gp10) of bacteriophage T4. Both proteins are components of the viral baseplate []. Gp9 connects the long tail fibres of the virus to the baseplate and triggers tail contraction after viral attachment to a host cell. The protein is active as a trimer, with each monomer being composed of three domains. The N-terminal domain consists of an extended polypeptide chain and two alpha helices. The alpha1 helix from each of the three monomers in the trimer interacts with its counterparts to form a coiled-coil structure. The middle domain is a seven-stranded β-sandwich that is thought to be a novel protein fold. The C-terminal domain is thought to be essential for gp9 trimerisation and is organised into an eight- stranded antiparallel β-barrel, which was found to resemble the 'jelly roll' fold found in many viral capsid proteins. The long flexible region between the N-terminal and middle domains may be required for the function of gp9 to transmit signals from the long tail fibres []. Together with gp11, gp10 initiates the assembly of wedges that then go on to associate with a hub to form the viral baseplate [].
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Publication
12923574 | -
First Author: Kostyuchenko VA
Year: 2003
Journal: Nat Struct Biol
Title: Three-dimensional structure of bacteriophage T4 baseplate.
Volume: 10
Issue: 9
Pages: 688-93
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Publication
10966799 | -
First Author: Leiman PG
Year: 2000
Journal: J Mol Biol
Title: Structure of bacteriophage T4 gene product 11, the interface between the baseplate and short tail fibers.
Volume: 301
Issue: 4
Pages: 975-85
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Protein Domain
IPR014791 | Baseplate_struct_Gp11
Type: Family
Description: The bacteriophage baseplate controls host cell recognition, attachment, tail sheath contraction and viral DNA ejection. The baseplate is a multi-subunit assembly at the distal end of the tail, which is composed of long and short tail fibres []. The tail region is responsible for attachment to the host bacteria during infection: long tail fibres enable host receptor recognition, while irreversible attachment is via short tail fibres. Recognition and attachment induce a conformational transition of the baseplate from a hexagonal to a star-shaped structure. In viruses such as Bacteriophage T4, Gp11 acts as a structural protein to connect the short tail fibres to the baseplate, while Gp9 connects the baseplate with the long tail fibres. Both Gp9 and Gp11 are trimers. Each Gp11 monomer consists of three domains, which are entwined together in the trimer: the N-terminal domains of the three monomers form a central, trimeric, parallel coiled coilsurrounded by the entwined middle finger domains; the C-terminal domains appear to be responsible for trimerisation [].
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Protein Domain
IPR036214 | Gp11_sf
Type: Homologous_superfamily
Description: The bacteriophage baseplate controls host cell recognition, attachment, tail sheath contraction and viral DNA ejection. The baseplate is a multi-subunit assembly at the distal end of the tail, which is composed of long and short tail fibres []. The tail region is responsible for attachment to the host bacteria during infection: long tail fibres enable host receptor recognition, while irreversible attachment is via short tail fibres. Recognition and attachment induce a conformational transition of the baseplate from a hexagonal to a star-shaped structure. In viruses such as Bacteriophage T4, Gp11 acts as a structural protein to connect the short tail fibres to the baseplate, while Gp9 connects the baseplate with the long tail fibres. Both Gp9 and Gp11 are trimers. Each Gp11 monomer consists of three domains, which are entwined together in the trimer: the N-terminal domains of the three monomers form a central, trimeric, parallel coiled coil surrounded by the entwined middle finger domains; the C-terminal domains appear to be responsible for trimerisation [].
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Protein Domain
IPR015976 | Phage_T4_Gp11_C
Type: Homologous_superfamily
Description: The bacteriophage baseplate controls host cell recognition, attachment, tail sheath contraction and viral DNA ejection. The baseplate is a multi-subunit assembly at the distal end of the tail, which is composed of long and short tail fibres []. The tail region is responsible for attachment to the host bacteria during infection: long tail fibres enable host receptor recognition, while irreversible attachment is via short tail fibres. Recognition and attachment induce a conformational transition of the baseplate from a hexagonal to a star-shaped structure. In viruses such as Bacteriophage T4, Gp11 acts as a structural protein to connect the short tail fibres to the baseplate, while Gp9 connects the baseplate with the long tail fibres. Both Gp9 and Gp11 are trimers. Each Gp11 monomer consists of three domains, which are entwined together in the trimer: the N-terminal domains of the three monomers form a central, trimeric, parallel coiled coil surrounded by the entwined middle finger domains; the C-terminal domains appear to be responsible for trimerisation [].This superfamily includes the middle finger domain, which is a seven-stranded, antiparallel, skewed β-roll with one α-helix [].
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Protein Domain
IPR015982 | Baseplate_struct_Gp11_N_sf
Type: Homologous_superfamily
Description: The bacteriophage baseplate controls host cell recognition, attachment, tail sheath contraction and viral DNA ejection. The baseplate is a multi-subunit assembly at the distal end of the tail, which is composed of long and short tail fibres []. The tail region is responsible for attachment to the host bacteria during infection: long tail fibres enable host receptor recognition, while irreversible attachment is via short tail fibres. Recognition and attachment induce a conformational transition of the baseplate from a hexagonal to a star-shaped structure. In viruses such as Bacteriophage T4, Gp11 acts as a structural protein to connect the short tail fibres to the baseplate, while Gp9 connects the baseplate with the long tail fibres. Both Gp9 and Gp11 are trimers. Each Gp11 monomer consists of three domains, which are entwined together in the trimer: the N-terminal domains of the three monomers form a central, trimeric, parallel coiled coil surrounded by the entwined middle finger domains; the C-terminal domains appear to be responsible for trimerisation [].This superfamily represents the N-terminal domain of Gp11, which has an α-helical structure that assumes an orthogonal bundle topology.
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Protein Domain
IPR043180 | Baseplate_struct_Gp11_C
Type: Homologous_superfamily
Description: The bacteriophage baseplate controls host cell recognition, attachment, tail sheath contraction and viral DNA ejection. The baseplate is a multi-subunit assembly at the distal end of the tail, which is composed of long and short tail fibres []. The tail region is responsible for attachment to the host bacteria during infection: long tail fibres enable host receptor recognition, while irreversible attachment is via short tail fibres. Recognition and attachment induce a conformational transition of the baseplate from a hexagonal to a star-shaped structure. In viruses such as Bacteriophage T4, Gp11 acts as a structural protein to connect the short tail fibres to the baseplate, while Gp9 connects the baseplate with the long tail fibres. Both Gp9 and Gp11 are trimers. Each Gp11 monomer consists of three domains, which are entwined together in the trimer: the N-terminal domains of the three monomers form a central, trimeric, parallel coiled coil surrounded by the entwined middle finger domains; the C-terminal domains appear to be responsible for trimerisation [].This superfamily represents the C-terminal domain of Gp11.
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Gene
7450 | VWF
Type: gene
Organism: human
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