RAB43
entrez
339122
canonical
uniprot
Q86YS6
canonical
ensembl
ENSG00000172780
resolver
ensp
ENSP00000319781
resolver
ensp
ENSP00000376981
resolver
ensp
ENSP00000376982
resolver
ensp
ENSP00000376984
resolver
ensp
ENSP00000376985
resolver
ensp
ENSP00000427632
resolver
genesymbol
RAB43
resolver
genesymbol_syn
RAB41
resolver
hgnc
HGNC:19983
resolver
uniprot
A8K4P9
resolver
uniprot
E9PBQ0
resolver
uniprot_entry
RAB43_HUMAN
resolver
uniprot_sec
A8K4P9
resolver
uniprot_sec
E9PBQ0
resolver
activity_regulation
ACTIVITY REGULATION: Regulated by guanine nucleotide exchange factors (GEFs) which promote the exchange of bound GDP for free GTP. Regulated by GTPase activating proteins (GAPs) including USP6NL, which increase the GTP hydrolysis activity (PubMed:16086013, PubMed:17562788, PubMed:17684057). Inhibited by GDP dissociation inhibitors (GDIs) (By similarity). {ECO:0000250|UniProtKB:P62820, ECO:0000269|PubMed:16086013, ECO:0000269|PubMed:17562788, ECO:0000269|PubMed:17684057}.
uniprot
proteins
amino_acid_sequence
MAGPGPGPGDPDEQYDFLFKLVLVGDASVGKTCVVQRFKTGAFSERQGSTIGVDFTMKTLEIQGKRVKLQIWDTAGQERFRTITQSYYRSANGAILAYDITKRSSFLSVPHWIEDVRKYAGSNIVQLLIGNKSDLSELREVSLAEAQSLAEHYDILCAIETSAKDSSNVEEAFLRVATELIMRHGGPLFSEKSPDHIQLNSKDIGEGWGCGC
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. 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:16086013, PubMed:17562788, PubMed:17684057, PubMed:18664496, PubMed:21255211, PubMed:29069590). Involved in retrograde transport from the endocytic pathway to the Golgi apparatus (PubMed:17684057). Required for the structural integrity of the Golgi complex (PubMed:17684057, PubMed:18664496). Also controls the anterograde ER-to-Golgi transport of nascent G protein-coupled receptors (including ADRA2A, ADRA2B, ADRA2C, ADRA1B, ADRB2 and AGTR1) and regulates the ER sorting of GPCR members by virtue of its ability to interact directly (PubMed:18664496, PubMed:29069590). Involved in the transport of Shiga toxin from early and recycling endosomes to the trans-Golgi network (PubMed:17562788). Plays a role in the maturation of phagosomes that engulf pathogens, such as S.aureus and M.tuberculosis (PubMed:21255211). {ECO:0000269|PubMed:16086013, ECO:0000269|PubMed:17562788, ECO:0000269|PubMed:17684057, ECO:0000269|PubMed:18664496, ECO:0000269|PubMed:21255211, ECO:0000269|PubMed:29069590}.
uniprot
proteins
mass_dalton
23339
uniprot
proteins
mutagenesis
MUTAGEN 32; /note="T->N: Constitutively inactive (GDP-bound) mutant. Disruption of Golgi structure. Localized to the cytoplasm. Loss of interaction with ADRA2B. Decreased cell-surface transport and signaling of adernergic receptor ADRA2B."; /evidence="ECO:0000269|PubMed:17684057, ECO:0000269|PubMed:18664496, ECO:0000269|PubMed:29069590"; MUTAGEN 77; /note="Q->L: Constitutively active (GTP-bound) mutant. Decreased cell-surface transport and signaling of adernergic receptor ADRA2B."; /evidence="ECO:0000269|PubMed:29069590"; MUTAGEN 82; /note="T->A: Loss of phosphorylation. No effect on binding of GDI1 and GDI2."; /evidence="ECO:0000269|PubMed:29125462"; MUTAGEN 82; /note="T->E: Phosphomimetic mutant. Loss of binding to GDI1, GDI2, CHM and CHML."; /evidence="ECO:0000269|PubMed:29125462"; MUTAGEN 131; /note="N->I: Disruption of Golgi structure. Localized to the cytoplasm. Loss of interaction with ADRA2B. Decreased cell-surface transport and signaling of G protein-coupled receptors ADRA2A, ADRA2B, ADRA2C, ADRA1B, ADRB2 and AGTR1."; /evidence="ECO:0000269|PubMed:29069590
uniprot
proteins
protein_family
Rab family
uniprot
proteins
protein_family
Small GTPase superfamily
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15018353
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16086013
uniprot
proteins
pubmed
16641997
uniprot
proteins
pubmed
17562788
uniprot
proteins
pubmed
17684057
uniprot
proteins
pubmed
18664496
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21255211
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
29069590
uniprot
proteins
pubmed
29125462
uniprot
proteins
sequence_length
212
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:16086013, ECO:0000269|PubMed:17562788, ECO:0000269|PubMed:18664496}. Golgi apparatus, cis-Golgi network membrane {ECO:0000269|PubMed:29069590}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Golgi apparatus, trans-Golgi network membrane {ECO:0000305|PubMed:17562788}; Lipid-anchor {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:29069590}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000269|PubMed:29069590}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle, phagosome membrane {ECO:0000305|PubMed:21255211}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Recruited to phagosomes containing S.aureus or M.tuberculosis (PubMed:21255211). {ECO:0000269|PubMed:21255211}.
uniprot
proteins