RAB1B
entrez
81876
canonical
uniprot
Q9H0U4
canonical
ensembl
ENSG00000174903
resolver
ensp
ENSP00000310226
resolver
enst
ENST00000311481
resolver
genesymbol
RAB1B
resolver
hgnc
HGNC:18370
resolver
uniprot
A8K7S1
resolver
uniprot_entry
RAB1B_HUMAN
resolver
uniprot_sec
A8K7S1
resolver
activity_regulation
ACTIVITY REGULATION: Regulated by guanine nucleotide exchange factors (GEFs) which promote the exchange of bound GDP for free GTP (Probable). Regulated by GTPase activating proteins (GAPs) including TBC1D20 which increases the GTP hydrolysis activity (PubMed:23236136). Inhibited by GDP dissociation inhibitors (GDIs) (PubMed:11389151, PubMed:8836150). {ECO:0000269|PubMed:11389151, ECO:0000269|PubMed:23236136, ECO:0000269|PubMed:8836150, ECO:0000305}.
uniprot
proteins
amino_acid_sequence
MNPEYDYLFKLLLIGDSGVGKSCLLLRFADDTYTESYISTIGVDFKIRTIELDGKTIKLQIWDTAGQERFRTITSSYYRGAHGIIVVYDVTDQESYANVKQWLQEIDRYASENVNKLLVGNKSDLTTKKVVDNTTAKEFADSLGIPFLETSAKNATNVEQAFMTMAAEIKKRMGPGAASGGERPNLKIDSTPVKPAGGGCC
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:20545908, PubMed:9437002, PubMed:23236136). 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:9437002). Plays a role in the initial events of the autophagic vacuole development which take place at specialized regions of the endoplasmic reticulum (PubMed:20545908). Regulates vesicular transport between the endoplasmic reticulum and successive Golgi compartments (By similarity). Required to modulate the compacted morphology of the Golgi (PubMed:26209634). Promotes the recruitment of lipid phosphatase MTMR6 to the endoplasmic reticulum-Golgi intermediate compartment (By similarity). {ECO:0000250|UniProtKB:P10536, ECO:0000269|PubMed:20545908, ECO:0000269|PubMed:23236136, ECO:0000269|PubMed:26209634, ECO:0000269|PubMed:9437002}.
uniprot
proteins
mass_dalton
22171
uniprot
proteins
mutagenesis
MUTAGEN 67; /note="Q->L: No effect on GDI1 binding. Reduces prenylation in vitro, but not in vivo. No effect on interaction with REP1/CHM; 100-fold refunction in intrinsic GTPase activity."; /evidence="ECO:0000269|PubMed:23236136, ECO:0000269|PubMed:8836150, ECO:0000269|PubMed:9437002"; MUTAGEN 73; /note="I->N: Abolishes interaction with REP1/CHM. No prenylation. Much lower GDP/GTP ratio."; /evidence="ECO:0000269|PubMed:9437002"; MUTAGEN 76; /note="S->A: Abolishes phosphocholination by Legionella AnkX."; /evidence="ECO:0000269|PubMed:21822290"; MUTAGEN 77; /note="Y->F: Abolishes AMPylation by Legionella DrrA."; /evidence="ECO:0000269|PubMed:20651120"; MUTAGEN 78; /note="Y->D: Abolishes interaction with REP1/CHM and GDI1. No prenylation. Much lower GDP/GTP ratio. No membrane association."; /evidence="ECO:0000269|PubMed:11389151, ECO:0000269|PubMed:9437002"; MUTAGEN 81; /note="A->D: Abolishes interaction with REP1/CHM. No prenylation. Lowers GDP/GTP ratio by half."; /evidence="ECO:0000269|PubMed:9437002"; MUTAGEN 103; /note="L->R: No effect on prenylation."; /evidence="ECO:0000269|PubMed:9437002"; MUTAGEN 110; /note="A->D: No effect on prenylation."; /evidence="ECO:0000269|PubMed:9437002"; MUTAGEN 121; /note="N->I: Prevent formation of autophagosomes."; /evidence="ECO:0000269|PubMed:20545908"; MUTAGEN 137; /note="K->E: No effect on prenylation."; /evidence="ECO:0000269|PubMed:9437002"; MUTAGEN 144; /note="G->N: No effect on prenylation."; /evidence="ECO:0000269|PubMed:9437002
uniprot
proteins
post_translational_modification
PTM: Prenylated; by GGTase II, only after interaction of the substrate with Rab escort protein 1 (REP1). {ECO:0000269|PubMed:11389151, ECO:0000269|PubMed:8836150}.; PTM: (Microbial infection) AMPylation at Tyr-77 by L.pneumophila DrrA occurs in the switch 2 region and leads to moderate inactivation of the GTPase activity. It appears to prolong the lifetime of the GTP state of RAB1B by restricting access of GTPase effectors to switch 2 and blocking effector-stimulated GTP hydrolysis, thereby rendering RAB1B constitutively active. It is later de-AMPylated by L.pneumophila SidD, releasing RAB1B from bacterial phagosomes. {ECO:0000269|PubMed:20651120}.; PTM: (Microbial infection) Phosphocholinated at Ser-76 by L.pneumophila AnkX, leading to displace GDP dissociation inhibitors (GDI) (PubMed:21822290, PubMed:22307087). Both GDP-bound and GTP-bound forms can be phosphocholinated. Dephosphocholinated by L.pneumophila Lem3, restoring accessibility to L.pneumophila GTPase effector LepB (PubMed:22158903, PubMed:22307087). {ECO:0000269|PubMed:21822290, ECO:0000269|PubMed:22158903, ECO:0000269|PubMed:22307087}.; PTM: (Microbial infection) Glycosylated by S.typhimurium protein Ssek3: arginine GlcNAcylation prevents GTPase activity, thereby disrupting vesicular protein transport from the endoplasmic reticulum (ER) to the Golgi compartment. {ECO:0000269|PubMed:32974215}.
uniprot
proteins
protein_family
Rab family
uniprot
proteins
protein_family
Small GTPase superfamily
uniprot
proteins
pubmed
11230166
uniprot
proteins
pubmed
11389151
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15694364
uniprot
proteins
pubmed
20064470
uniprot
proteins
pubmed
20545908
uniprot
proteins
pubmed
20651120
uniprot
proteins
pubmed
21680813
uniprot
proteins
pubmed
21734656
uniprot
proteins
pubmed
21822290
uniprot
proteins
pubmed
22158903
uniprot
proteins
pubmed
22307087
uniprot
proteins
pubmed
23188820
uniprot
proteins
pubmed
23236136
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26209634
uniprot
proteins
pubmed
27552051
uniprot
proteins
pubmed
32974215
uniprot
proteins
pubmed
8836150
uniprot
proteins
pubmed
9437002
uniprot
proteins
sequence_length
201
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11389151}. Membrane {ECO:0000269|PubMed:11389151}; Lipid-anchor {ECO:0000269|PubMed:11389151}; Cytoplasmic side {ECO:0000269|PubMed:11389151}. Preautophagosomal structure membrane {ECO:0000269|PubMed:20545908}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P10536}. Note=Targeted by REP1 to membranes of specific subcellular compartments including endoplasmic reticulum, Golgi apparatus, and intermediate vesicles between these two compartments (PubMed:11389151). In the GDP-form, colocalizes with GDI in the cytoplasm (PubMed:11389151). Co-localizes with MTMR6 to the endoplasmic reticulum-Golgi intermediate compartment and to the peri-Golgi region (By similarity). {ECO:0000250|UniProtKB:P10536, ECO:0000269|PubMed:11389151}.
uniprot
proteins