RAB5A
entrez
5868
canonical
uniprot
P20339
canonical
ensembl
ENSG00000144566
resolver
ensp
ENSP00000273047
resolver
ensp
ENSP00000411941
resolver
genesymbol
RAB5A
resolver
genesymbol_syn
RAB5
resolver
hgnc
HGNC:9783
resolver
uniprot
B4DJA5
resolver
uniprot
Q6FI44
resolver
uniprot_entry
RAB5A_HUMAN
resolver
uniprot_sec
B4DJA5
resolver
uniprot_sec
Q6FI44
resolver
activity_regulation
ACTIVITY REGULATION: Regulated by guanine nucleotide exchange factors (GEFs) including RINL and RABGEF1, which promote the exchange of bound GDP for free GTP (By similarity). Regulated by GTPase activating proteins (GAPs) including SGSM3, which increase the GTP hydrolysis activity (PubMed:16086013, PubMed:17562788). Inhibited by GDP dissociation inhibitors (GDIs) (PubMed:23815289). {ECO:0000250|UniProtKB:P18066, ECO:0000269|PubMed:16086013, ECO:0000269|PubMed:17562788, ECO:0000269|PubMed:23815289}.
uniprot
proteins
amino_acid_sequence
MASRGATRPNGPNTGNKICQFKLVLLGESAVGKSSLVLRFVKGQFHEFQESTIGAAFLTQTVCLDDTTVKFEIWDTAGQERYHSLAPMYYRGAQAAIVVYDITNEESFARAKNWVKELQRQASPNIVIALSGNKADLANKRAVDFQEAQSYADDNSLLFMETSAKTSMNVNEIFMAIAKKLPKNEPQNPGANSARGRGVDLTEPTQPTRNQCCSN
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 sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. RAB5A is required for the fusion of plasma membranes and early endosomes and involved in early endocytic trafficking (PubMed:10818110, PubMed:14617813, PubMed:15378032, PubMed:16086013, PubMed:16410077, PubMed:17562788). Required for EEA1 recruitment to early endosomes (PubMed:16086013, PubMed:17562788). Recruits FERRY complex to early endosomes, where FERRY links early endosomes with a subgroup of mRNAs to enable mRNA intracellular distribution (PubMed:37267906). Recruits RABEP1/Rabaptin-5 effector to early endosomes, thereby promoting endocytic membrane fusion (By similarity). Required for EGF and transferrin endocytosis and trafficking through early endosomes (PubMed:16086013, PubMed:17562788). Contributes to the regulation of filopodia extension (PubMed:14978216). Required for the exosomal release of SDCBP, CD63, PDCD6IP and syndecan (PubMed:22660413). Regulates maturation of apoptotic cell-containing phagosomes, probably downstream of DYN2 and PIK3C3 (By similarity). {ECO:0000250|UniProtKB:P18066, ECO:0000250|UniProtKB:Q9CQD1, ECO:0000269|PubMed:10818110, ECO:0000269|PubMed:14617813, ECO:0000269|PubMed:14978216, ECO:0000269|PubMed:15378032, ECO:0000269|PubMed:16086013, ECO:0000269|PubMed:16410077, ECO:0000269|PubMed:17562788, ECO:0000269|PubMed:22660413, ECO:0000269|PubMed:37267906}.
uniprot
proteins
mass_dalton
23659
uniprot
proteins
mutagenesis
MUTAGEN 34; /note="S->N: Constitutively inactive (GDP-bound) mutant. Increased interaction wih ATP9A. Loss of EEA1 targeting to early endosomes."; /evidence="ECO:0000269|PubMed:16086013, ECO:0000269|PubMed:36604604"; MUTAGEN 54; /note="G->Q: Strongly decreases ZFYVE20 binding affinity."; /evidence="ECO:0000269|PubMed:16034420"; MUTAGEN 56; /note="A->E: Strongly decreases ZFYVE20 binding affinity."; /evidence="ECO:0000269|PubMed:16034420"; MUTAGEN 57; /note="F->A: Strongly decreases RABEP1 and ZFYVE20 binding affinity."; /evidence="ECO:0000269|PubMed:15378032, ECO:0000269|PubMed:16034420"; MUTAGEN 74; /note="W->A: Strongly decreases RABEP1 binding affinity."; /evidence="ECO:0000269|PubMed:15378032"; MUTAGEN 79; /note="Q->L: Constitutively active (GTP-bound) mutant. Loss of GTPase activity. Does not inhibit filopodia formation. Increased EEA1 targeting to early endosomes."; /evidence="ECO:0000269|PubMed:14978216, ECO:0000269|PubMed:15378032, ECO:0000269|PubMed:16086013"; MUTAGEN 82; /note="Y->A: Strongly decreases RABEP1 binding affinity. Impairs endosome fusion."; /evidence="ECO:0000269|PubMed:15378032"; MUTAGEN 84; /note="S->A: Loss of phosphorylation. No effect on GDI1 and GDI2 binding."; /evidence="ECO:0000269|PubMed:29125462"; MUTAGEN 84; /note="S->E: Phosphomimetic mutant. Loss of GDI1 and GDI2 binding."; /evidence="ECO:0000269|PubMed:29125462"; MUTAGEN 89; /note="Y->A: Strongly decreases RABEP1 binding affinity."; /evidence="ECO:0000269|PubMed:15378032"; MUTAGEN 116; /note="K->E: No effect on RABEP1 binding affinity."; /evidence="ECO:0000269|PubMed:15378032"; MUTAGEN 120; /note="R->E: No effect on RABEP1 binding affinity."; /evidence="ECO:0000269|PubMed:15378032
uniprot
proteins
post_translational_modification
PTM: Phosphorylation of Ser-84 in the switch II region by LRRK2 prevents the association of RAB regulatory proteins, including RAB GDP dissociation inhibitors GDI1 and GDI2. {ECO:0000269|PubMed:29125462}.; PTM: (Microbial infection) Glycosylated on arginine residues by S.typhimurium protein Ssek3. {ECO:0000269|PubMed:32974215}.
uniprot
proteins
protein_family
Rab family
uniprot
proteins
protein_family
Small GTPase superfamily
uniprot
proteins
pubmed
10491193
uniprot
proteins
pubmed
10818110
uniprot
proteins
pubmed
11062261
uniprot
proteins
pubmed
11703925
uniprot
proteins
pubmed
12433916
uniprot
proteins
pubmed
14617813
uniprot
proteins
pubmed
14684892
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14978216
uniprot
proteins
pubmed
15378032
uniprot
proteins
pubmed
15388334
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16034420
uniprot
proteins
pubmed
16086013
uniprot
proteins
pubmed
16410077
uniprot
proteins
pubmed
16641997
uniprot
proteins
pubmed
17081065
uniprot
proteins
pubmed
17562788
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
20534488
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22431521
uniprot
proteins
pubmed
22660413
uniprot
proteins
pubmed
23382462
uniprot
proteins
pubmed
23815289
uniprot
proteins
pubmed
2501306
uniprot
proteins
pubmed
25869668
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
29125462
uniprot
proteins
pubmed
32974215
uniprot
proteins
pubmed
36604604
uniprot
proteins
pubmed
37267906
uniprot
proteins
pubmed
39319391
uniprot
proteins
pubmed
7991565
uniprot
proteins
sequence_length
215
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23815289}; Lipid-anchor {ECO:0000305|PubMed:7991565}; Cytoplasmic side {ECO:0000269|PubMed:23382462}. Early endosome membrane {ECO:0000269|PubMed:16086013, ECO:0000269|PubMed:23815289, ECO:0000269|PubMed:25869668}; Lipid-anchor {ECO:0000305|PubMed:7991565}. Melanosome {ECO:0000269|PubMed:17081065}. Cytoplasmic vesicle {ECO:0000269|PubMed:10818110}. Cell projection, ruffle {ECO:0000250|UniProtKB:P18066}. Membrane {ECO:0000269|PubMed:23815289}. Cytoplasm, cytosol {ECO:0000269|PubMed:23382462}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:Q9CQD1}. Endosome membrane {ECO:0000269|PubMed:22431521, ECO:0000269|PubMed:23382462}. Note=Enriched in stage I melanosomes (PubMed:17081065). Alternates between membrane-bound and cytosolic forms (Probable). {ECO:0000269|PubMed:17081065, ECO:0000305}.
uniprot
proteins