Rab24
entrez
19336
canonical
uniprot
P35290
canonical
ensembl
ENSMUSG00000034789
resolver
ensp
ENSMUSP00000046188
resolver
ensp
ENSMUSP00000299961
resolver
enst
ENSMUST00000035242
resolver
genesymbol
Rab24
resolver
uniprot
Q0PD31
resolver
uniprot_entry
Q0PD31_MOUSE
resolver
uniprot_entry
RAB24_MOUSE
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) which increase the GTP hydrolysis activity (Probable). Inhibited by GDP dissociation inhibitors (GDIs) (Probable). {ECO:0000305}.
uniprot
proteins
amino_acid_sequence
MSGQRVDVKVVMLGKEYVGKTSLVERYVHDRFLVGPYQNTIGAAFVAKVMCVGDRTVTLGIWDTAGSERYEAMSRIYYRGAKAAIVCYDLTDSSSFERAKFWVKELRSLEEGCQIYLCGTKSDLLEEDRRRRRVDFHDVQDYADNIKAQLFETSSKTGQSVDELFQKVAEDYVSVAAFQVMTEDKGVDLSQKANPYFYSCCHH
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:26325487, PubMed:31496367). 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 (PubMed:10660536, PubMed:26325487, PubMed:31496367). RAB24 is an atypical RAB protein that presents low GTPase activity and thereby exists predominantly in the GTP-bound active state (PubMed:10660536). RAB24 is required for the clearance of late autophagic vacuoles under basal conditions (PubMed:26325487). It is not needed for starvation-induced autophagy (PubMed:26325487). Involved in the modulation of meiotic apparatus assembly and meiotic progression during oocyte maturation, possibly through regulation of kinetochore-microtubule interaction (PubMed:31496367). {ECO:0000269|PubMed:10660536, ECO:0000269|PubMed:26325487, ECO:0000269|PubMed:31496367}.
uniprot
proteins
mass_dalton
23144
uniprot
proteins
mutagenesis
MUTAGEN 17; /note="Y->F: No change in autophagosome targeting under fed condition. Decreased autophagosome targeting under starved condition."; /evidence="ECO:0000269|PubMed:26325487"; MUTAGEN 22; /note="S->N: Predominantly in the GTP-bound state. No effect on subcellular location."; /evidence="ECO:0000269|PubMed:12323076"; MUTAGEN 67; /note="S->L: Increased GTPase activity. Decreased autophagosome targeting under fed and starved conditions."; /evidence="ECO:0000269|PubMed:26325487"; MUTAGEN 67; /note="S->Q: Increase in GTPase activity. No effect neither on prenylation, nor on subcellular location."; /evidence="ECO:0000269|PubMed:10660536"; MUTAGEN 120; /note="T->A,I: Accumulates in punctate structures in both cytoplasmic and nuclear compartments."; /evidence="ECO:0000269|PubMed:12323076"; MUTAGEN 123; /note="D->I: Accumulates in punctate structures in both cytoplasmic and nuclear compartments. Disrupts the integrity of the nuclear envelope."; /evidence="ECO:0000269|PubMed:12323076"; MUTAGEN 172; /note="Y->F: No change in autophagosome targeting under fed condition. Decreased autophagosome targeting under starved condition."; /evidence="ECO:0000269|PubMed:26325487"; MUTAGEN 200..201; /note="CC->SS: Loss of prenylation. Loss of autophagosome targeting under fed condition. Decreased autophagosome targeting under starved condition."; /evidence="ECO:0000269|PubMed:26325487"; MUTAGEN 200..201; /note="Missing: Loss of prenylation. Loss of autophagosome targeting under fed condition. Decreased autophagosome targeting under starved condition."; /evidence="ECO:0000269|PubMed:26325487"; MUTAGEN 202..203; /note="HH->SN: Slight increased prenylation. No effect on subcellular location."; /evidence="ECO:0000269|PubMed:26325487"; MUTAGEN 202..203; /note="Missing: Slight increased prenylation. No effect on subcellular location."; /evidence="ECO:0000269|PubMed:26325487
uniprot
proteins
post_translational_modification
PTM: Prenylated; prenylation is required for RAB24 localization to autophagosomes (PubMed:26325487). Isoprenylation is inefficient compared to other Rab family members (PubMed:10660536). {ECO:0000269|PubMed:10660536, ECO:0000269|PubMed:26325487}.; PTM: Phosphorylated at Tyr-17 and Tyr-172 (PubMed:14680817). Cytosolic pool of RAB24 is more phosphorylated than the membrane-associated pool (PubMed:14680817). {ECO:0000269|PubMed:14680817}.
uniprot
proteins
protein_family
Rab family
uniprot
proteins
protein_family
Small GTPase superfamily
uniprot
proteins
pubmed
10660536
uniprot
proteins
pubmed
12323076
uniprot
proteins
pubmed
14680817
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1555775
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
26325487
uniprot
proteins
pubmed
31496367
uniprot
proteins
pubmed
8126105
uniprot
proteins
sequence_length
203
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:10660536, ECO:0000269|PubMed:12323076, ECO:0000269|PubMed:31496367}. Membrane {ECO:0000269|PubMed:10660536, ECO:0000269|PubMed:12323076}; Lipid-anchor {ECO:0000305}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000269|PubMed:26325487}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:26325487, ECO:0000269|PubMed:31496367}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:31496367}. Note=Only about 20% is recovered in the particulate fraction (PubMed:10660536). RAB24 localizes in perinuclear region and in the limiting membranes of autophagic compartments under basal conditions (PubMed:26325487). RAB24 is localized in the cytoplasm with an accumulated distribution in nuclear region at germinal vesicle (GV) stage of oocyte meiotic progression. At pre-metaphase I stage, localized in the cytoplasm with a particular concentration around chromosomes. As the oocytes enter metaphase I, located to the spindle region. Similar distribution pattern is observed in MII oocytes (PubMed:31496367). {ECO:0000269|PubMed:10660536, ECO:0000269|PubMed:26325487, ECO:0000269|PubMed:31496367}.
uniprot
proteins