ID RAB24_HUMAN Reviewed; 203 AA. AC Q969Q5; A0A024R7N9; Q7Z4Z7; DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 28-JAN-2026, entry version 193. DE RecName: Full=Ras-related protein Rab-24; DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P35290}; GN Name=RAB24 {ECO:0000312|HGNC:HGNC:9765}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Zhang H.L., Yu L., Ding J.B., Zhao Y., Li M.Z., Zhao S.Y.; RT "Cloning and characterization of a new human cDNA homology to murine Rab24 RT protein mRNA."; RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Pancreas, Skin, and Uterus; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-203. RC TISSUE=Amygdala; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [6] RP SUBCELLULAR LOCATION, INDUCTION, ISOPRENYLATION, AND LACK OF INTERACTION RP WITH ARHGDIA AND ARHGDIB. RX PubMed=10660536; DOI=10.1074/jbc.275.6.3848; RA Erdman R.A., Shellenberger K.E., Overmeyer J.H., Maltese W.A.; RT "Rab24 is an atypical member of the Rab GTPase family. Deficient GTPase RT activity, GDP dissociation inhibitor interaction, and prenylation of Rab24 RT expressed in cultured cells."; RL J. Biol. Chem. 275:3848-3856(2000). RN [7] RP INTERACTION WITH ZFYVE20. RX PubMed=16034420; DOI=10.1038/nature03798; RA Eathiraj S., Pan X., Ritacco C., Lambright D.G.; RT "Structural basis of family-wide Rab GTPase recognition by rabenosyn-5."; RL Nature 436:415-419(2005). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). CC -!- FUNCTION: The small GTPases Rab are key regulators of intracellular CC membrane trafficking, from the formation of transport vesicles to their CC fusion with membranes. Rabs cycle between an inactive GDP-bound form CC and an active GTP-bound form that is able to recruit to membranes CC different sets of downstream effectors directly responsible for vesicle CC formation, movement, tethering and fusion. RAB24 is an atypical RAB CC protein that presents low GTPase activity and thereby exists CC predominantly in the GTP-bound active state. RAB24 is required for the CC clearance of late autophagic vacuoles under basal conditions. It is not CC needed for starvation-induced autophagy. Involved in the modulation of CC meiotic apparatus assembly and meiotic progression during oocyte CC maturation, possibly through regulation of kinetochore-microtubule CC interaction. {ECO:0000250|UniProtKB:P35290}. CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + H2O = GDP + phosphate + H(+); Xref=Rhea:RHEA:19669, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; CC Evidence={ECO:0000250|UniProtKB:P35290}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; CC Evidence={ECO:0000250|UniProtKB:P35290}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P62820}; CC -!- ACTIVITY REGULATION: Regulated by guanine nucleotide exchange factors CC (GEFs) which promote the exchange of bound GDP for free GTP (Probable). CC Regulated by GTPase activating proteins (GAPs) which increase the GTP CC hydrolysis activity (Probable). Inhibited by GDP dissociation CC inhibitors (GDIs) (Probable). {ECO:0000305}. CC -!- SUBUNIT: Interacts with ZFYVE20 (PubMed:16034420). Does not interact CC with the GDP dissociation inhibitors ARHGDIA and ARHGDIB CC (PubMed:10660536). {ECO:0000269|PubMed:10660536, CC ECO:0000269|PubMed:16034420}. CC -!- INTERACTION: CC Q969Q5; Q14353: GAMT; NbExp=3; IntAct=EBI-3060998, EBI-3909086; CC Q969Q5; P50395: GDI2; NbExp=5; IntAct=EBI-3060998, EBI-1049143; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:10660536}. CC Membrane {ECO:0000269|PubMed:10660536}; Lipid-anchor {ECO:0000305}. CC Cytoplasmic vesicle, autophagosome membrane CC {ECO:0000250|UniProtKB:P35290}. Cytoplasm, perinuclear region CC {ECO:0000250|UniProtKB:P35290}. Cytoplasm, cytoskeleton, spindle CC {ECO:0000250|UniProtKB:P35290}. Note=Only about 20% is recovered in the CC particulate fraction (PubMed:10660536). RAB24 localizes in perinuclear CC region and in the limiting membranes of autophagic compartments under CC basal conditions. RAB24 is localized in the cytoplasm with an CC accumulated distribution in nuclear region at germinal vesicle (GV) CC stage of oocyte meiotic progression. At pre-metaphase I stage, CC localized in the cytoplasm with a particular concentration around CC chromosomes. As the oocytes enter metaphase I, located to the spindle CC region. Similar distribution pattern is observed in MII oocytes (By CC similarity). {ECO:0000250|UniProtKB:P35290, CC ECO:0000269|PubMed:10660536}. CC -!- INDUCTION: By extensive retinoic acid treatment, in Ntera-2 teratoma CC cell line induced to differentiate into postmitotic neurons (NTN2) (at CC protein level). {ECO:0000269|PubMed:10660536}. CC -!- DOMAIN: Switch I, switch II and the interswitch regions are CC characteristic of Rab GTPases and mediate the interactions with Rab CC downstream effectors. The switch regions undergo conformational changes CC upon nucleotide binding which drive interaction with specific sets of CC effector proteins, with most effectors only binding to GTP-bound Rab. CC {ECO:0000250|UniProtKB:P62820}. CC -!- PTM: Prenylated; prenylation is required for RAB24 localization to CC autophagosomes (By similarity). Isoprenylation is inefficient compared CC to other Rab family members (PubMed:10660536). CC {ECO:0000250|UniProtKB:P35290, ECO:0000269|PubMed:10660536}. CC -!- PTM: Phosphorylated at Tyr-17 and Tyr-172 (By similarity). Cytosolic CC pool of RAB24 is more phosphorylated than the membrane-associated pool CC (By similarity). {ECO:0000250|UniProtKB:P35290}. CC -!- MISCELLANEOUS: The unusual Ser-67, instead of a conserved Gln in other CC family members, is the cause of low GTPase activity. As a result, the CC predominant nucleotide associated with the protein is GTP. CC {ECO:0000250|UniProtKB:P35290}. CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF087904; AAP97202.1; -; mRNA. DR EMBL; BT007268; AAP35932.1; -; mRNA. DR EMBL; CH471195; EAW85025.1; -; Genomic_DNA. DR EMBL; CH471195; EAW85028.1; -; Genomic_DNA. DR EMBL; CH471195; EAW85029.1; -; Genomic_DNA. DR EMBL; BC010006; AAH10006.1; -; mRNA. DR EMBL; BC015534; AAH15534.1; -; mRNA. DR EMBL; BC021263; AAH21263.1; -; mRNA. DR EMBL; AL833898; CAD38754.1; -; mRNA. DR CCDS; CCDS34300.1; -. DR RefSeq; NP_001026847.1; NM_001031677.4. DR RefSeq; NP_570137.2; NM_130781.4. DR AlphaFoldDB; Q969Q5; -. DR SMR; Q969Q5; -. DR BioGRID; 119817; 38. DR CORUM; Q969Q5; -. DR FunCoup; Q969Q5; 1313. DR IntAct; Q969Q5; 33. DR MINT; Q969Q5; -. DR STRING; 9606.ENSP00000304376; -. DR iPTMnet; Q969Q5; -. DR PhosphoSitePlus; Q969Q5; -. DR SwissPalm; Q969Q5; -. DR BioMuta; RAB24; -. DR DMDM; 23396831; -. DR jPOST; Q969Q5; -. DR MassIVE; Q969Q5; -. DR PaxDb; 9606-ENSP00000304376; -. DR PeptideAtlas; Q969Q5; -. DR ProteomicsDB; 75816; -. DR Pumba; Q969Q5; -. DR Antibodypedia; 29222; 282 antibodies from 25 providers. DR DNASU; 53917; -. DR Ensembl; ENST00000303251.11; ENSP00000304376.6; ENSG00000169228.15. DR Ensembl; ENST00000393611.6; ENSP00000377235.2; ENSG00000169228.15. DR GeneID; 53917; -. DR KEGG; hsa:53917; -. DR MANE-Select; ENST00000303251.11; ENSP00000304376.6; NM_001031677.4; NP_001026847.1. DR UCSC; uc003mfv.5; human. DR AGR; HGNC:9765; -. DR ClinPGx; PA34114; -. DR CTD; 53917; -. DR DisGeNET; 53917; -. DR GeneCards; RAB24; -. DR HGNC; HGNC:9765; RAB24. DR HPA; ENSG00000169228; Low tissue specificity. DR MIM; 612415; gene. DR OpenTargets; ENSG00000169228; -. DR VEuPathDB; HostDB:ENSG00000169228; -. DR eggNOG; KOG0092; Eukaryota. DR GeneTree; ENSGT00910000144316; -. DR HOGENOM; CLU_041217_10_2_1; -. DR InParanoid; Q969Q5; -. DR OMA; RFRAGPY; -. DR OrthoDB; 25896at2759; -. DR PAN-GO; Q969Q5; 6 GO annotations based on evolutionary models. DR PhylomeDB; Q969Q5; -. DR PathwayCommons; Q969Q5; -. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR Reactome; R-HSA-8873719; RAB geranylgeranylation. DR SignaLink; Q969Q5; -. DR Agora; ENSG00000169228; -. DR BioGRID-ORCS; 53917; 24 hits in 1156 CRISPR screens. DR ChiTaRS; RAB24; human. DR GenomeRNAi; 53917; -. DR Pharos; Q969Q5; Tbio. DR PRO; PR:Q969Q5; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; Q969Q5; protein. DR Bgee; ENSG00000169228; Expressed in granulocyte and 97 other cell types or tissues. DR ExpressionAtlas; Q969Q5; baseline and differential. DR GO; GO:0005776; C:autophagosome; IBA:GO_Central. DR GO; GO:0000421; C:autophagosome membrane; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0030139; C:endocytic vesicle; IBA:GO_Central. DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central. DR GO; GO:0005768; C:endosome; IBA:GO_Central. DR GO; GO:0005739; C:mitochondrion; HTP:FlyBase. DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0030667; C:secretory granule membrane; TAS:Reactome. DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell. DR GO; GO:0003925; F:G protein activity; ISS:UniProtKB. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008608; P:attachment of spindle microtubules to kinetochore; ISS:UniProtKB. DR GO; GO:0006914; P:autophagy; ISS:UniProtKB. DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central. DR GO; GO:0140013; P:meiotic nuclear division; ISS:UniProtKB. DR GO; GO:0001556; P:oocyte maturation; ISS:UniProtKB. DR CDD; cd04118; Rab24; 1. DR FunFam; 3.40.50.300:FF:000799; ras-related protein Rab-24 isoform X1; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR041828; Rab24. DR InterPro; IPR005225; Small_GTP-bd. DR InterPro; IPR001806; Small_GTPase. DR NCBIfam; TIGR00231; small_GTP; 1. DR PANTHER; PTHR47978; -; 1. DR Pfam; PF00071; Ras; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR SMART; SM00175; RAB; 1. DR SMART; SM00176; RAN; 1. DR SMART; SM00173; RAS; 1. DR SMART; SM00174; RHO; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS51419; RAB; 1. PE 1: Evidence at protein level; KW Autophagy; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; GTP-binding; KW Hydrolase; Lipoprotein; Magnesium; Membrane; Metal-binding; KW Nucleotide-binding; Phosphoprotein; Prenylation; Protein transport; KW Proteomics identification; Reference proteome; Transport. FT CHAIN 1..203 FT /note="Ras-related protein Rab-24" FT /id="PRO_0000121213" FT REGION 30..45 FT /note="Switch I" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00753" FT REGION 63..80 FT /note="Switch II" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00753" FT BINDING 19 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P62820" FT BINDING 20 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P62820" FT BINDING 21 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P62820" FT BINDING 21 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P62820" FT BINDING 40 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P62820" FT BINDING 40 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P62820" FT BINDING 63 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P62820" FT BINDING 66 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P62820" FT BINDING 121 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P62820" FT BINDING 123 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P62820" FT BINDING 156 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P62820" FT MOD_RES 17 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P35290" FT MOD_RES 172 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P35290" FT LIPID 200 FT /note="S-geranylgeranyl cysteine" FT /evidence="ECO:0000250|UniProtKB:P62820" FT LIPID 201 FT /note="S-geranylgeranyl cysteine" FT /evidence="ECO:0000250|UniProtKB:P62820" FT CONFLICT 55..56 FT /note="RT -> AL (in Ref. 1; AAP97202)" FT /evidence="ECO:0000305" FT CONFLICT 108 FT /note="S -> T (in Ref. 1; AAP97202)" FT /evidence="ECO:0000305" FT CONFLICT 129..130 FT /note="RR -> QE (in Ref. 1; AAP97202)" FT /evidence="ECO:0000305" SQ SEQUENCE 203 AA; 23124 MW; 979E1AF6F7A4E5F1 CRC64; MSGQRVDVKV VMLGKEYVGK TSLVERYVHD RFLVGPYQNT IGAAFVAKVM SVGDRTVTLG IWDTAGSERY EAMSRIYYRG AKAAIVCYDL TDSSSFERAK FWVKELRSLE EGCQIYLCGT KSDLLEEDRR RRRVDFHDVQ DYADNIKAQL FETSSKTGQS VDELFQKVAE DYVSVAAFQV MTEDKGVDLG QKPNPYFYSC CHH //