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Search results 201 to 220 out of 220 for Map6

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0.019s
Type Details Score
Protein
Organism: Mus musculus/domesticus
Length: 260  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 93  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 185  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 156  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 171  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 116  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 121  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 165  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 166  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 70  
Fragment?: true
Publication
First Author: Wu C
Year: 2017
Journal: Kidney Blood Press Res
Title: TMEM106a is a Novel Tumor Suppressor in Human Renal Cancer.
Volume: 42
Issue: 5
Pages: 853-864
Publication      
First Author: Liu J
Year: 2018
Journal: J Cell Biochem
Title: TMEM106A inhibits cell proliferation, migration, and induces apoptosis of lung cancer cells.
Publication
First Author: Brady OA
Year: 2013
Journal: Hum Mol Genet
Title: The frontotemporal lobar degeneration risk factor, TMEM106B, regulates lysosomal morphology and function.
Volume: 22
Issue: 4
Pages: 685-95
Protein Domain
Type: Family
Description: This family includes Transmembrane protein 106A/B/C, type II transmembrane proteins which have homology to the late embryogenesis abundant-2 (LEA-2) domain []. TMEM106A has been identified as a key factor to regulate macrophage activation and a tumor suppressor in gastric, renal cancer and nonsmall-cell lung carcinoma (NSCLC), being an interesting therapeutic target for the management of NSCLC [, ]. TMEM106B localises to late endosomes and lysosomes, and it is involved in dendrite morphogenesis and maintenance by regulating lysosomal trafficking via its interaction with MAP6 []. Its overexpression is associated with familial frontotemporal lobar degeneration []. It has also been identified as a protein required for productive SARS-CoV-2 infection []. Structural analysis of LEA-2 domains revealed that they have a long, conserved lipid-binding groove, implying that TMEM106B and its homologues, Vac7 and Tag1 from yeast, may all be lipid transfer proteins in the lumen of late endocytic organelles.
Publication
First Author: Gory-Fauré S
Year: 2014
Journal: PLoS One
Title: Non-microtubular localizations of microtubule-associated protein 6 (MAP6).
Volume: 9
Issue: 12
Pages: e114905
Publication
First Author: Levine TP
Year: 2022
Journal: Proteins
Title: TMEM106B in humans and Vac7 and Tag1 in yeast are predicted to be lipid transfer proteins.
Volume: 90
Issue: 1
Pages: 164-175
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2003
Title: Data Curation Using Mouse Genome Assembly
Publication      
First Author: MGI Genome Annotation Group and UniGene Staff
Year: 2015
Journal: Database Download
Title: MGI-UniGene Interconnection Effort
Publication
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
Publication
First Author: Huttlin EL
Year: 2010
Journal: Cell
Title: A tissue-specific atlas of mouse protein phosphorylation and expression.
Volume: 143
Issue: 7
Pages: 1174-89