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Search results 201 to 217 out of 217 for Mia3

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0.024s
Type Details Score
Publication      
First Author: Bairoch A
Year: 1999
Journal: Database Release
Title: SWISS-PROT Annotated protein sequence database
Publication      
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
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: 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
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
Publication
First Author: Pitman JL
Year: 2011
Journal: J Lipid Res
Title: Reduced cholesterol and triglycerides in mice with a mutation in Mia2, a liver protein that localizes to ER exit sites.
Volume: 52
Issue: 10
Pages: 1775-86
Protein Domain
Type: Family
Description: Otoraplin, also known as MIAL (MIA-like), is specifically expressed in the cochlea and the vestibule of the inner ear and may contribute to inner ear dysfunction in humans []. It is a member of the MIA family. MIA (melanoma inhibitory activity) family members include MIA, MIAL, MIA2, and MIA3 (also called TANGO). MIA was found to be strongly expressed and secreted by malignant melanomas. It contains a domain that adopts a Src Homology 3 (SH3) domain-like fold; however, it contains an additional antiparallel beta sheet and two disulfide bonds compared to classical SH3 domains. Unlike classical SH3 domains, MIA does not bind proline-rich ligands [, ].
Protein Domain
Type: Domain
Description: Otoraplin, also known as MIAL (MIA-like), is specifically expressed in the cochlea and the vestibule of the inner ear and may contribute to inner ear dysfunction in humans []. It is a member of the MIA family. MIA (melanoma inhibitory activity) family members include MIA, MIAL, MIA2, and MIA3 (also called TANGO). MIA was found to be strongly expressed and secreted by malignant melanomas. It contains a domain that adopts a Src Homology 3 (SH3) domain-like fold; however, it contains an additional antiparallel beta sheet and two disulfide bonds compared to classical SH3 domains. Unlike classical SH3 domains, MIA does not bind proline-rich ligands [, ].
Publication
First Author: Rendtorff ND
Year: 2001
Journal: Genomics
Title: Identification and characterization of an inner ear-expressed human melanoma inhibitory activity (MIA)-like gene (MIAL) with a frequent polymorphism that abolishes translation.
Volume: 71
Issue: 1
Pages: 40-52
Publication
First Author: Stoll R
Year: 2008
Journal: Curr Protein Pept Sci
Title: Extracellular SH3 domain containing proteins--features of a new protein family.
Volume: 9
Issue: 3
Pages: 221-6
Publication
First Author: Stoll R
Year: 2003
Journal: Protein Sci
Title: Backbone dynamics of the human MIA protein studied by (15)N NMR relaxation: implications for extended interactions of SH3 domains.
Volume: 12
Issue: 3
Pages: 510-9
Publication
First Author: Bosserhoff AK
Year: 2003
Journal: J Biol Chem
Title: Specific expression and regulation of the new melanoma inhibitory activity-related gene MIA2 in hepatocytes.
Volume: 278
Issue: 17
Pages: 15225-31
Publication
First Author: Hellerbrand C
Year: 2008
Journal: Gut
Title: The novel gene MIA2 acts as a tumour suppressor in hepatocellular carcinoma.
Volume: 57
Issue: 2
Pages: 243-51
Publication
First Author: Hellerbrand C
Year: 2005
Journal: Liver Int
Title: In situ expression patterns of melanoma inhibitory activity 2 in healthy and diseased livers.
Volume: 25
Issue: 2
Pages: 357-66
Protein Domain
Type: Domain
Description: MIA2 is expressed specifically in hepatocytes and its expression is controlled by hepatocyte nuclear factor 1 binding sites in the MIA2 promoter [, ]. It inhibits the growth and invasion of hepatocellular carcinomas (HCC) and may act as a tumour suppressor []. A mutation in MIA2 in mice resulted in reduced cholesterol and triglycerides. Since MIA2 localizes to ER exit sites, it may function as an ER-to-Golgi trafficking protein that regulates lipid metabolism []. MIA2 contains an N-terminal SH3-like domain, similar to MIA.MIA (melanoma inhibitory activity) family members include MIA, MIAL, MIA2, and MIA3 (also called TANGO). MIA was found to be strongly expressed and secreted by malignant melanomas. It contains a domain that adopts a Src Homology 3 (SH3) domain-like fold; however, it contains an additional antiparallel beta sheet and two disulfide bonds compared to classical SH3 domains. Unlike classical SH3 domains, MIA does not bind proline-rich ligands [, ].
Protein
Organism: Mus musculus/domesticus
Length: 128  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 128  
Fragment?: false