RAB10
entrez
10890
canonical
uniprot
P61026
canonical
ensembl
ENSG00000084733
resolver
ensp
ENSP00000264710
resolver
ensp
ENSP00000576138
resolver
ensp
ENSP00000576139
resolver
ensp
ENSP00000576141
resolver
enst
ENST00000264710
resolver
enst
ENST00000906079
resolver
enst
ENST00000906080
resolver
enst
ENST00000906082
resolver
genesymbol
RAB10
resolver
hgnc
HGNC:9759
resolver
uniprot
D6W538
resolver
uniprot
O88386
resolver
uniprot
Q6IA52
resolver
uniprot
Q9D7X6
resolver
uniprot
Q9H0T3
resolver
uniprot_entry
RAB10_HUMAN
resolver
uniprot_sec
D6W538
resolver
uniprot_sec
O88386
resolver
uniprot_sec
Q6IA52
resolver
uniprot_sec
Q9D7X6
resolver
uniprot_sec
Q9H0T3
resolver
activity_regulation
ACTIVITY REGULATION: Regulated by guanine nucleotide exchange factors (GEFs) DENND4C and RABIF which promote the exchange of bound GDP for free GTP (PubMed:20937701, PubMed:31540829). Regulated by GTPase activating proteins (GAPs) including TBC1D21 which increase the GTP hydrolysis activity (Probable). Inhibited by GDP dissociation inhibitors GDI1 and GDI2 which prevent Rab-GDP dissociation (PubMed:19570034, PubMed:26824392, PubMed:29125462). {ECO:0000269|PubMed:19570034, ECO:0000269|PubMed:20937701, ECO:0000269|PubMed:26824392, ECO:0000269|PubMed:29125462, ECO:0000269|PubMed:31540829, ECO:0000305|PubMed:28067790}.
uniprot
proteins
amino_acid_sequence
MAKKTYDLLFKLLLIGDSGVGKTCVLFRFSDDAFNTTFISTIGIDFKIKTVELQGKKIKLQIWDTAGQERFHTITTSYYRGAMGIMLVYDITNGKSFENISKWLRNIDEHANEDVERMLLGNKCDMDDKRVVPKGKGEQIAREHGIRFFETSAKANINIEKAFLTLAEDILRKTPVKEPNSENVDISSGGGVTGWKSKCC
uniprot
proteins
ec_number
3.6.5.2
uniprot
proteins
function
FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes (PubMed:21248164). Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (PubMed:21248164). RAB10 is mainly involved in the biosynthetic transport of proteins from the Golgi to the plasma membrane (PubMed:21248164). Regulates, for instance, SLC2A4/GLUT4 glucose transporter-enriched vesicles delivery to the plasma membrane (By similarity). In parallel, RAB10 regulates the transport of TLR4, a toll-like receptor to the plasma membrane and therefore may be important for innate immune response (By similarity). Also plays a specific role in asymmetric protein transport to the plasma membrane (PubMed:16641372). In neurons, involved in axonogenesis through regulation of vesicular membrane trafficking toward the axonal plasma membrane (By similarity). In epithelial cells, regulates transport from the Golgi to the basolateral membrane (PubMed:16641372). May play a role in the basolateral recycling pathway and in phagosome maturation (By similarity). May play a role in endoplasmic reticulum dynamics and morphology controlling tubulation along microtubules and tubules fusion (PubMed:23263280). Together with LRRK2, RAB8A, and RILPL1, regulates ciliogenesis (PubMed:30398148). When phosphorylated by LRRK2 on Thr-73, binds RILPL1 and inhibits ciliogenesis (PubMed:30398148). Participates in the export of a subset of neosynthesized proteins through a Rab8-Rab10-Rab11-dependent endososomal export route (PubMed:32344433). Targeted to and stabilized on stressed lysosomes through LRRK2 phosphorylation where it promotes the extracellular release of lysosomal content through EHBP1 and EHNP1L1 effector proteins (PubMed:30209220). {ECO:0000250|UniProtKB:P24409, ECO:0000250|UniProtKB:P61027, ECO:0000269|PubMed:16641372, ECO:0000269|PubMed:21248164, ECO:0000269|PubMed:23263280, ECO:0000269|PubMed:30209220, ECO:0000269|PubMed:30398148, ECO:0000269|PubMed:32344433}.; FUNCTION: (Microbial infection) Upon Legionella pneumophila infection promotes endoplasmic reticulum recruitment and bacterial replication. Plays a role in remodeling the Legionella-containing vacuole (LCV) into an endoplasmic reticulum-like vacuole. {ECO:0000269|PubMed:31540829}.
uniprot
proteins
mass_dalton
22541
uniprot
proteins
mutagenesis
MUTAGEN 23; /note="T->N: Probable dominant negative mutant locked in the inactive GDP-bound form; alters the basolateral recycling pathway in epithelial cells and endoplasmic reticulum membrane morphology. Reduces endoplasmic reticulum recruitment to the Legionella-containing vacuole. Decreased WDR44-positive tubulation. Loss of E-cadherin and MMP14 export and decreased CFTR export."; /evidence="ECO:0000269|PubMed:20576682, ECO:0000269|PubMed:23263280, ECO:0000269|PubMed:31540829"; MUTAGEN 68; /note="Q->L: Probable constitutively active mutant unable to hydrolyze GTP; accumulates at the base of the primary cilium and alters the basolateral recycling pathway in epithelial cells. No effect on endoplasmic reticulum recruitment to the Legionella-containing vacuole. Increased WDR44-positive tubulation."; /evidence="ECO:0000269|PubMed:20576682, ECO:0000269|PubMed:31540829, ECO:0000269|PubMed:32344433"; MUTAGEN 73; /note="T->A: Loss of phosphorylation. No effect on GDI1 and GDI2 binding. Increases localization to the cytosol. Does not translocate to LRRK2-positive lysosomes and does not promote lysosomal content release."; /evidence="ECO:0000269|PubMed:26824392, ECO:0000269|PubMed:29125462, ECO:0000269|PubMed:30209220, ECO:0000269|PubMed:30398148"; MUTAGEN 73; /note="T->D: Phosphomimetic mutant. Reduces interaction with GDI1."; /evidence="ECO:0000269|PubMed:30209220"; MUTAGEN 73; /note="T->E: Phosphomimetic mutant. Loss of GDI1 and GDI2 binding. Increases localization to the Golgi complex."; /evidence="ECO:0000269|PubMed:26824392, ECO:0000269|PubMed:29125462, ECO:0000269|PubMed:30209220, ECO:0000269|PubMed:30398148
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated upon Legionella pneumophila infection. Ubiquitination does not lead to proteasomal degradation. {ECO:0000269|PubMed:31540829}.; PTM: Phosphorylation of Thr-73 in the switch II region by LRRK2 prevents the association of dRAB regulatory proteins, including CHM, CHML and RAB GDP dissociation inhibitors GDI1 and GDI2 (PubMed:26824392). Phosphorylation of Thr-73 by LRRK2 is stimulated by RAB29 and RAB32 (PubMed:38127736). Phosphorylation by LRRK2 is required for localization to stressed lysosomes (PubMed:30209220). {ECO:0000269|PubMed:26824392, ECO:0000269|PubMed:30209220, ECO:0000269|PubMed:38127736}.
uniprot
proteins
protein_family
Rab family
uniprot
proteins
protein_family
Small GTPase superfamily
uniprot
proteins
pubmed
10931946
uniprot
proteins
pubmed
11230166
uniprot
proteins
pubmed
12450215
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16641372
uniprot
proteins
pubmed
19570034
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
20576682
uniprot
proteins
pubmed
20937701
uniprot
proteins
pubmed
21248164
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22908308
uniprot
proteins
pubmed
23263280
uniprot
proteins
pubmed
24891604
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26824392
uniprot
proteins
pubmed
27552051
uniprot
proteins
pubmed
28067790
uniprot
proteins
pubmed
29125462
uniprot
proteins
pubmed
29127255
uniprot
proteins
pubmed
29212815
uniprot
proteins
pubmed
29562525
uniprot
proteins
pubmed
30209220
uniprot
proteins
pubmed
30398148
uniprot
proteins
pubmed
30635421
uniprot
proteins
pubmed
31540829
uniprot
proteins
pubmed
32344433
uniprot
proteins
pubmed
38127736
uniprot
proteins
sequence_length
200
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Golgi apparatus membrane {ECO:0000269|PubMed:23263280}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:P24409}. Endosome membrane {ECO:0000269|PubMed:16641372, ECO:0000269|PubMed:32344433}. Recycling endosome membrane {ECO:0000250|UniProtKB:P24409}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:P24409}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:20576682, ECO:0000269|PubMed:30398148}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:23263280, ECO:0000269|PubMed:24891604}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:29212815}. Lysosome {ECO:0000269|PubMed:30209220}. Note=Associates with SLC2A4/GLUT4 storage vesicles (PubMed:22908308). Localizes to the base of the cilium when phosphorylated by LRRK2 on Thr-73 (PubMed:20576682, PubMed:30398148). Transiently associates with phagosomes (By similarity). Localizes to the endoplasmic reticulum at domains of new tubule growth (PubMed:23263280). Colocalizes with MICAL1, GRAF1/ARHGAP26 and GRAF2/ARHGAP10 on endosomal tubules (PubMed:32344433). Localizes to enlarged lysosomes through LRRK2 phosphorylation (PubMed:30209220). {ECO:0000250|UniProtKB:P24409, ECO:0000269|PubMed:20576682, ECO:0000269|PubMed:22908308, ECO:0000269|PubMed:23263280, ECO:0000269|PubMed:30209220, ECO:0000269|PubMed:30398148, ECO:0000269|PubMed:32344433}.
uniprot
proteins