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 |
|
•
•
•
•
•
|