|  Help  |  About  |  Contact Us

Search our database by keyword

Examples

  • Search this entire website. Enter identifiers, names or keywords for genes, diseases, strains, ontology terms, etc. (e.g. Pax6, Parkinson, ataxia)
  • Use OR to search for either of two terms (e.g. OR mus) or quotation marks to search for phrases (e.g. "dna binding").
  • Boolean search syntax is supported: e.g. Balb* for partial matches or mus AND NOT embryo to exclude a term

Search results 101 to 172 out of 172 for Rab32

<< First    < Previous  |  Next >    Last >>
0.02s
Type Details Score
Protein
Organism: Mus musculus/domesticus
Length: 215  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 217  
Fragment?: true
Publication
First Author: Oh J
Year: 1996
Journal: Nat Genet
Title: Positional cloning of a gene for Hermansky-Pudlak syndrome, a disorder of cytoplasmic organelles.
Volume: 14
Issue: 3
Pages: 300-6
Protein Domain
Type: Domain
Description: Small G-protein signalling modulator 1/2 (also known as RUTBC2/1) bind to Rab9A via their Pleckstrin homology (PH) domain [, ]. RUTBC1 stimulates GTP hydrolysis by Rab32 and Rab33B [], while RUTBC2 appears to be a GAP for Rab36, Rab9A and associated proteins controling the recycling of mannose-6-phosphate receptors from late endosomes to the trans-Golgi [, , ]. This entry represents the PH domain of RUTBC1/2.
Protein Domain
Type: Domain
Description: This domain adopts a PH-like fold. It has been called the Rab-binding domain (RBD) []. Small G-protein signalling modulator 1/2 (also known as RUTBC2/1) bind to Rab9A via their Pleckstrin homology (PH) domain [, ]. RUTBC1 stimulates GTP hydrolysis by Rab32 and Rab33B [], while RUTBC2 appears to be a GAP for Rab36, Rab9A and associated proteins controling the recycling of mannose-6-phosphate receptors from late endosomes to the trans-Golgi [, , ].
Publication      
First Author: Lian H
Year: 2023
Journal: Nat Microbiol
Title: Parkinson's disease kinase LRRK2 coordinates a cell-intrinsic itaconate-dependent defence pathway against intracellular Salmonella.
Publication
First Author: Yang H
Year: 2007
Journal: Genomics
Title: Identification of three novel proteins (SGSM1, 2, 3) which modulate small G protein (RAP and RAB)-mediated signaling pathway.
Volume: 90
Issue: 2
Pages: 249-60
Protein
Organism: Mus musculus/domesticus
Length: 704  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 712  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 634  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 635  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 635  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 627  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 634  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 703  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 704  
Fragment?: false
Publication
First Author: Gerondopoulos A
Year: 2012
Journal: Curr Biol
Title: BLOC-3 mutated in Hermansky-Pudlak syndrome is a Rab32/38 guanine nucleotide exchange factor.
Volume: 22
Issue: 22
Pages: 2135-9
Publication
First Author: Beaumont KA
Year: 2011
Journal: Traffic
Title: The recycling endosome protein Rab17 regulates melanocytic filopodia formation and melanosome trafficking.
Volume: 12
Issue: 5
Pages: 627-43
Publication
First Author: Lopes VS
Year: 2007
Journal: Mol Biol Cell
Title: Melanosome maturation defect in Rab38-deficient retinal pigment epithelium results in instability of immature melanosomes during transient melanogenesis.
Volume: 18
Issue: 10
Pages: 3914-27
Protein
Organism: Mus musculus/domesticus
Length: 671  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 671  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 671  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 671  
Fragment?: false
Protein Domain
Type: Domain
Description: Longin domains are evolutionarily conserved regions widely distributed among eukaryotes, involved in membrane dynamic regulation and exhibit similarities in primary sequence and secondary structure. Longin-like domains are found in FUZ and related proteins, such as the MON1 and HPS1 proteins [, , ]. The MON1/CCZ1 complex (MC1) is the GDP/GTP exchange factor (GEF) for the Rab GTPase Ypt7/Rab7 during vesicular trafficking []. The HPS1/HPS4 complex (BLOC-3) is a Rab32 and Rab38 GEF and is required for biogenesis of melanosomes and platelet dense granules []. Inturned (INTU) and Fuzzy (FUZ) proteins interact as members of the ciliogenesis and planar polarity effector (CPLANE) complex that controls recruitment of intraflagellar transport machinery to the basal body of primary cilia [, ]. Structurally, these domains are composed of an alpha/beta fold which contains five anti-parallel β-strands organised as a central β-sheet and around it, two α-helices [].This entry represents the third Longin domain found in CCZ1, INTU and HPS4 proteins.
Protein Domain
Type: Domain
Description: Longin domains are evolutionarily conserved regions widely distributed among eukaryotes, involved in membrane dynamic regulation and exhibit similarities in primary sequence and secondary structure. Longin-like domains are found in FUZ and related proteins, such as the MON1 and HPS1 proteins [, , ]. The MON1/CCZ1 complex (MC1) is the GDP/GTP exchange factor (GEF) for the Rab GTPase Ypt7/Rab7 during vesicular trafficking []. The HPS1/HPS4 complex (BLOC-3) is a Rab32 and Rab38 GEF and is required for biogenesis of melanosomes and platelet dense granules []. Inturned (INTU) and Fuzzy (FUZ) proteins interact as members of the ciliogenesis and planar polarity effector (CPLANE) complex that controls recruitment of intraflagellar transport machinery to the basal body of primary cilia [, ]. Structurally, these domains are composed of an alpha/beta fold which contains five anti-parallel β-strands organised as a central β-sheet and around it, two α-helices [].This entry represents the first Longin domain found in INTU, CCZ1 and HPS4.
Protein Domain
Type: Domain
Description: Longin domains are evolutionarily conserved regions widely distributed among eukaryotes, involved in membrane dynamic regulation and exhibit similarities in primary sequence and secondary structure. Longin-like domains are found in FUZ and related proteins, such as the MON1 and HPS1 proteins [, , ]. The MON1/CCZ1 complex (MC1) is the GDP/GTP exchange factor (GEF) for the Rab GTPase Ypt7/Rab7 during vesicular trafficking []. The HPS1/HPS4 complex (BLOC-3) is a Rab32 and Rab38 GEF and is required for biogenesis of melanosomes and platelet dense granules []. Inturned (INTU) and Fuzzy (FUZ) proteins interact as members of the ciliogenesis and planar polarity effector (CPLANE) complex that controls recruitment of intraflagellar transport machinery to the basal body of primary cilia [, ]. Structurally, these domains are composed of an alpha/beta fold which contains five anti-parallel β-strands organised as a central β-sheet and around it, two α-helices [].This entry represents the second Longin domain found in INTU and CCZ1 proteins.
Protein Domain
Type: Domain
Description: Longin domains are evolutionarily conserved regions widely distributed among eukaryotes, involved in membrane dynamic regulation and exhibit similarities in primary sequence and secondary structure. Longin-like domains are found in FUZ and related proteins, such as the MON1 and HPS1 proteins [, , ]. The MON1/CCZ1 complex (MC1) is the GDP/GTP exchange factor (GEF) for the Rab GTPase Ypt7/Rab7 during vesicular trafficking []. The HPS1/HPS4 complex (BLOC-3) is a Rab32 and Rab38 GEF and is required for biogenesis of melanosomes and platelet dense granules []. Inturned (INTU) and Fuzzy (FUZ) proteins interact as members of the ciliogenesis and planar polarity effector (CPLANE) complex that controls recruitment of intraflagellar transport machinery to the basal body of primary cilia [, ]. Structurally, these domains are composed of an alpha/beta fold which contains five anti-parallel β-strands organised as a central β-sheet and around it, two α-helices [].This entry represents the first Longin domain found in FUZ, MON1 and HPS1 proteins.
Protein Domain
Type: Domain
Description: Longin domains are evolutionarily conserved regions widely distributed among eukaryotes, involved in membrane dynamic regulation and exhibit similarities in primary sequence and secondary structure. Longin-like domains are found in FUZ and related proteins, such as the MON1 and HPS1 proteins [, , ]. The MON1/CCZ1 complex (MC1) is the GDP/GTP exchange factor (GEF) for the Rab GTPase Ypt7/Rab7 during vesicular trafficking []. The HPS1/HPS4 complex (BLOC-3) is a Rab32 and Rab38 GEF and is required for biogenesis of melanosomes and platelet dense granules []. Inturned (INTU) and Fuzzy (FUZ) proteins interact as members of the ciliogenesis and planar polarity effector (CPLANE) complex that controls recruitment of intraflagellar transport machinery to the basal body of primary cilia [, ]. Structurally, these domains are composed of an alpha/beta fold which contains five anti-parallel β-strands organised as a central β-sheet and around it, two α-helices [].This entry represents the third Longin domain of FUZ, MON1 and HPS1 proteins.
Protein Domain
Type: Domain
Description: Longin domains are evolutionarily conserved regions widely distributed among eukaryotes, involved in membrane dynamic regulation and exhibit similarities in primary sequence and secondary structure. Longin-like domains are found in FUZ and related proteins, such as the MON1 and HPS1 proteins [, , ]. The MON1/CCZ1 complex (MC1) is the GDP/GTP exchange factor (GEF) for the Rab GTPase Ypt7/Rab7 during vesicular trafficking []. The HPS1/HPS4 complex (BLOC-3) is a Rab32 and Rab38 GEF and is required for biogenesis of melanosomes and platelet dense granules []. Inturned (INTU) and Fuzzy (FUZ) proteins interact as members of the ciliogenesis and planar polarity effector (CPLANE) complex that controls recruitment of intraflagellar transport machinery to the basal body of primary cilia [, ]. Structurally, these domains are composed of an alpha/beta fold which contains five anti-parallel β-strands organised as a central β-sheet and around it, two α-helices [].This entry represents the second Longin domain found in FUZ, MON1 and HPS1 proteins.
Publication
First Author: Toriyama M
Year: 2016
Journal: Nat Genet
Title: The ciliopathy-associated CPLANE proteins direct basal body recruitment of intraflagellar transport machinery.
Volume: 48
Issue: 6
Pages: 648-56
Publication
First Author: Gray RS
Year: 2009
Journal: Nat Cell Biol
Title: The planar cell polarity effector Fuz is essential for targeted membrane trafficking, ciliogenesis and mouse embryonic development.
Volume: 11
Issue: 10
Pages: 1225-32
Publication
First Author: Kinch LN
Year: 2006
Journal: Protein Sci
Title: Longin-like folds identified in CHiPS and DUF254 proteins: vesicle trafficking complexes conserved in eukaryotic evolution.
Volume: 15
Issue: 11
Pages: 2669-74
Publication  
First Author: Kiontke S
Year: 2017
Journal: Nat Commun
Title: Architecture and mechanism of the late endosomal Rab7-like Ypt7 guanine nucleotide exchange factor complex Mon1-Ccz1.
Volume: 8
Pages: 14034
Publication
First Author: Sanchez-Pulido L
Year: 2020
Journal: Bioinformatics
Title: Hexa-Longin domain scaffolds for inter-Rab signalling.
Volume: 36
Issue: 4
Pages: 990-993
Protein
Organism: Mus musculus/domesticus
Length: 480  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 556  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 415  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 553  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 556  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 387  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 379  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 415  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 349  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 191  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 461  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 223  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 211  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 204  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 211  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 121  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 77  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 223  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 192  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 204  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 94  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 223  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 258  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 204  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 942  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1093  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1005  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 677  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1031  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 706  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 1093  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 645  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 671  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 645  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 652  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 671  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 671  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 546  
Fragment?: false