RAB24_HUMAN
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 03-AUG-2022, entry version 176.
DE RecName: Full=Ras-related protein Rab-24;
GN Name=RAB24;
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: May be involved in autophagy-related processes.
CC {ECO:0000250}.
CC -!- SUBUNIT: Unlike other Rab family members, does not interact with GDP
CC dissociation inhibitors (GDIs), including ARHGDIA and ARHGDIB.
CC Interacts with ZFYVE20. {ECO:0000269|PubMed:16034420}.
CC -!- INTERACTION:
CC Q969Q5; Q14353: GAMT; NbExp=3; IntAct=EBI-3060998, EBI-3909086;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:10660536}.
CC Membrane {ECO:0000269|PubMed:10660536}; Lipid-anchor {ECO:0000305}.
CC Note=Only about 20-25% is recovered in the particulate fraction.
CC {ECO:0000269|PubMed:10660536}.
CC -!- INDUCTION: By extensive retinoic acid treatment, in Ntera-2 teratoma
CC cell line induced to differentiate into post-mitotic neurons (NTN2) (at
CC protein level). {ECO:0000269|PubMed:10660536}.
CC -!- PTM: Isoprenylation is inefficient compared to other Rab family
CC members. {ECO:0000269|PubMed:10660536}.
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 (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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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_001031677.3.
DR RefSeq; NP_570137.2; NM_130781.3.
DR AlphaFoldDB; Q969Q5; -.
DR SMR; Q969Q5; -.
DR BioGRID; 119817; 29.
DR IntAct; Q969Q5; 14.
DR MINT; Q969Q5; -.
DR STRING; 9606.ENSP00000304376; -.
DR iPTMnet; Q969Q5; -.
DR PhosphoSitePlus; Q969Q5; -.
DR BioMuta; RAB24; -.
DR DMDM; 23396831; -.
DR EPD; Q969Q5; -.
DR jPOST; Q969Q5; -.
DR MassIVE; Q969Q5; -.
DR MaxQB; Q969Q5; -.
DR PaxDb; Q969Q5; -.
DR PeptideAtlas; Q969Q5; -.
DR PRIDE; Q969Q5; -.
DR ProteomicsDB; 75816; -.
DR Antibodypedia; 29222; 285 antibodies from 24 providers.
DR DNASU; 53917; -.
DR Ensembl; ENST00000303251.11; ENSP00000304376.6; ENSG00000169228.14.
DR Ensembl; ENST00000393611.6; ENSP00000377235.2; ENSG00000169228.14.
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 CTD; 53917; -.
DR DisGeNET; 53917; -.
DR GeneCards; RAB24; -.
DR HGNC; HGNC:9765; RAB24.
DR HPA; ENSG00000169228; Low tissue specificity.
DR MIM; 612415; gene.
DR neXtProt; NX_Q969Q5; -.
DR OpenTargets; ENSG00000169228; -.
DR PharmGKB; PA34114; -.
DR VEuPathDB; HostDB:ENSG00000169228; -.
DR eggNOG; KOG0092; Eukaryota.
DR GeneTree; ENSGT00910000144316; -.
DR HOGENOM; CLU_041217_10_2_1; -.
DR InParanoid; Q969Q5; -.
DR OMA; TAKYWIQ; -.
DR OrthoDB; 1340129at2759; -.
DR PhylomeDB; Q969Q5; -.
DR TreeFam; TF300199; -.
DR PathwayCommons; Q969Q5; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-8873719; RAB geranylgeranylation.
DR SignaLink; Q969Q5; -.
DR BioGRID-ORCS; 53917; 24 hits in 1077 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 95 other tissues.
DR ExpressionAtlas; Q969Q5; baseline and differential.
DR Genevisible; Q969Q5; HS.
DR GO; GO:0005776; C:autophagosome; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0030139; C:endocytic vesicle; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR CDD; cd04118; Rab24; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR041828; Rab24.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51419; RAB; 1.
PE 1: Evidence at protein level;
KW Autophagy; Cytoplasm; GTP-binding; Lipoprotein; Membrane;
KW Nucleotide-binding; Prenylation; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..203
FT /note="Ras-related protein Rab-24"
FT /id="PRO_0000121213"
FT MOTIF 37..45
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 14..22
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 63..67
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 120..123
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 154..156
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT LIPID 200
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 201
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
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
