RAB5B_HUMAN
ID RAB5B_HUMAN Reviewed; 215 AA.
AC P61020; A8K982; B4DKD7; P35239; P35277; Q6PIK9; Q86TH0; Q8IXL2;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2004, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Ras-related protein Rab-5B;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P20339};
GN Name=RAB5B;
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] (ISOFORM 1).
RX PubMed=1541686; DOI=10.1172/jci115683;
RA Wilson D.B., Wilson M.P.;
RT "Identification and subcellular localization of human rab5b, a new member
RT of the ras-related superfamily of GTPases.";
RL J. Clin. Invest. 89:996-1005(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Testis, and Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Endometrium;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye, PNS, and Skin;
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 [8]
RP INTERACTION WITH EEA1.
RX PubMed=10491193; DOI=10.1046/j.1432-1327.1999.00743.x;
RA Callaghan J.M., Nixon S., Bucci C., Toh B.-H., Stenmark H.;
RT "Direct interaction of EEA1 with Rab5b.";
RL Eur. J. Biochem. 265:361-366(1999).
RN [9]
RP INTERACTION WITH RIN2 AND RIN3, AND MUTAGENESIS OF SER-34 AND GLN-79.
RX PubMed=11733506; DOI=10.1074/jbc.m106276200;
RA Saito K., Murai J., Kajiho H., Kontani K., Kurosu H., Katada T.;
RT "A novel binding protein composed of homophilic tetramer exhibits unique
RT properties for the small GTPase Rab5.";
RL J. Biol. Chem. 277:3412-3418(2002).
RN [10]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J.,
RA Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S.,
RA Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.;
RT "Proteomic and bioinformatic characterization of the biogenesis and
RT function of melanosomes.";
RL J. Proteome Res. 5:3135-3144(2006).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
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).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [14]
RP INTERACTION WITH GDI1; GDI2; CHML AND CHM, PHOSPHORYLATION AT SER-84, AND
RP MUTAGENESIS OF SER-84.
RX PubMed=29125462; DOI=10.7554/elife.31012;
RA Steger M., Diez F., Dhekne H.S., Lis P., Nirujogi R.S., Karayel O.,
RA Tonelli F., Martinez T.N., Lorentzen E., Pfeffer S.R., Alessi D.R.,
RA Mann M.;
RT "Systematic proteomic analysis of LRRK2-mediated Rab GTPase phosphorylation
RT establishes a connection to ciliogenesis.";
RL Elife 6:0-0(2017).
RN [15]
RP GLYCOSYLATION (MICROBIAL INFECTION).
RX PubMed=32974215; DOI=10.3389/fcimb.2020.00419;
RA Gan J., Scott N.E., Newson J.P.M., Wibawa R.R., Wong Fok Lung T.,
RA Pollock G.L., Ng G.Z., van Driel I., Pearson J.S., Hartland E.L.,
RA Giogha C.;
RT "The Salmonella effector SseK3 targets small Rab GTPases.";
RL Front. Cell. Infect. Microbiol. 10:419-419(2020).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 15-191 IN COMPLEX WITH GDP.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human RAB5B in complex with GDP.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Protein transport. Probably involved in vesicular traffic.
CC {ECO:0000250|UniProtKB:P20339}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; 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:P20339};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000250|UniProtKB:P20339};
CC -!- ACTIVITY REGULATION: Regulated by guanine nucleotide exchange factors
CC (GEFs) which promote the exchange of bound GDP for free GTP.
CC {ECO:0000250|UniProtKB:P18066}.
CC -!- SUBUNIT: Binds EEA1 (PubMed:10491193). Interacts with RIN2 and RIN3,
CC which probably regulate its pathway, possibly by acting as GEFs
CC (PubMed:11733506). Interacts with GDI1, GDI2, CHML and CHM;
CC phosphorylation at Ser-84 disrupts this interaction (PubMed:29125462).
CC {ECO:0000269|PubMed:10491193, ECO:0000269|PubMed:11733506,
CC ECO:0000269|PubMed:29125462}.
CC -!- INTERACTION:
CC P61020; Q15075: EEA1; NbExp=3; IntAct=EBI-399401, EBI-298113;
CC P61020; P42858: HTT; NbExp=3; IntAct=EBI-399401, EBI-466029;
CC P61020; Q5S007: LRRK2; NbExp=9; IntAct=EBI-399401, EBI-5323863;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17081065};
CC Lipid-anchor {ECO:0000269|PubMed:17081065}; Cytoplasmic side
CC {ECO:0000269|PubMed:17081065}. Early endosome membrane
CC {ECO:0000269|PubMed:17081065}; Lipid-anchor
CC {ECO:0000269|PubMed:17081065}. Melanosome
CC {ECO:0000269|PubMed:17081065}. Note=Enriched in stage I melanosomes.
CC {ECO:0000269|PubMed:17081065}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P61020-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P61020-2; Sequence=VSP_045301;
CC -!- PTM: Phosphorylation of Ser-84 in the switch II region by LRRK2
CC prevents the association of RAB regulatory proteins, including CHM,
CC CHML and RAB GDP dissociation inhibitors GDI1 and GDI2.
CC {ECO:0000269|PubMed:29125462}.
CC -!- PTM: (Microbial infection) Glycosylated on arginine residues by
CC S.typhimurium protein Ssek3. {ECO:0000269|PubMed:32974215}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH40143.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X54871; CAA38653.1; -; mRNA.
DR EMBL; AF498937; AAM21085.1; -; mRNA.
DR EMBL; AK292597; BAF85286.1; -; mRNA.
DR EMBL; AK296517; BAG59149.1; -; mRNA.
DR EMBL; BX537408; CAD97650.1; -; mRNA.
DR EMBL; AC034102; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW96862.1; -; Genomic_DNA.
DR EMBL; CH471054; EAW96864.1; -; Genomic_DNA.
DR EMBL; BC032740; AAH32740.1; -; mRNA.
DR EMBL; BC040143; AAH40143.1; ALT_INIT; mRNA.
DR EMBL; BC050558; AAH50558.2; -; mRNA.
DR EMBL; BC056422; AAH56422.2; -; mRNA.
DR EMBL; BC065298; AAH65298.2; -; mRNA.
DR CCDS; CCDS58244.1; -. [P61020-2]
DR CCDS; CCDS8900.1; -. [P61020-1]
DR PIR; A43925; A43925.
DR RefSeq; NP_001238965.1; NM_001252036.1. [P61020-1]
DR RefSeq; NP_001238966.1; NM_001252037.1. [P61020-2]
DR RefSeq; NP_002859.1; NM_002868.3. [P61020-1]
DR RefSeq; XP_005269108.1; XM_005269051.2. [P61020-1]
DR RefSeq; XP_005269109.1; XM_005269052.2. [P61020-1]
DR PDB; 2HEI; X-ray; 1.55 A; A/B=15-191.
DR PDBsum; 2HEI; -.
DR AlphaFoldDB; P61020; -.
DR SMR; P61020; -.
DR BioGRID; 111807; 130.
DR IntAct; P61020; 23.
DR MINT; P61020; -.
DR STRING; 9606.ENSP00000353444; -.
DR GlyGen; P61020; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P61020; -.
DR MetOSite; P61020; -.
DR PhosphoSitePlus; P61020; -.
DR SwissPalm; P61020; -.
DR BioMuta; RAB5B; -.
DR DMDM; 46577637; -.
DR EPD; P61020; -.
DR jPOST; P61020; -.
DR MassIVE; P61020; -.
DR MaxQB; P61020; -.
DR PaxDb; P61020; -.
DR PeptideAtlas; P61020; -.
DR PRIDE; P61020; -.
DR ProteomicsDB; 4453; -.
DR ProteomicsDB; 57253; -. [P61020-1]
DR Antibodypedia; 4131; 180 antibodies from 33 providers.
DR DNASU; 5869; -.
DR Ensembl; ENST00000360299.10; ENSP00000353444.5; ENSG00000111540.16. [P61020-1]
DR Ensembl; ENST00000448789.2; ENSP00000391319.2; ENSG00000111540.16. [P61020-2]
DR Ensembl; ENST00000553116.5; ENSP00000450168.1; ENSG00000111540.16. [P61020-1]
DR GeneID; 5869; -.
DR KEGG; hsa:5869; -.
DR MANE-Select; ENST00000360299.10; ENSP00000353444.5; NM_002868.4; NP_002859.1.
DR UCSC; uc001siv.4; human. [P61020-1]
DR CTD; 5869; -.
DR DisGeNET; 5869; -.
DR GeneCards; RAB5B; -.
DR HGNC; HGNC:9784; RAB5B.
DR HPA; ENSG00000111540; Low tissue specificity.
DR MIM; 179514; gene.
DR neXtProt; NX_P61020; -.
DR OpenTargets; ENSG00000111540; -.
DR PharmGKB; PA34144; -.
DR VEuPathDB; HostDB:ENSG00000111540; -.
DR eggNOG; KOG0092; Eukaryota.
DR GeneTree; ENSGT00940000160756; -.
DR HOGENOM; CLU_041217_10_2_1; -.
DR InParanoid; P61020; -.
DR OMA; AVHFDIW; -.
DR PhylomeDB; P61020; -.
DR TreeFam; TF300199; -.
DR PathwayCommons; P61020; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-8854214; TBC/RABGAPs.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-HSA-8873719; RAB geranylgeranylation.
DR Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR SignaLink; P61020; -.
DR SIGNOR; P61020; -.
DR BioGRID-ORCS; 5869; 11 hits in 1081 CRISPR screens.
DR ChiTaRS; RAB5B; human.
DR EvolutionaryTrace; P61020; -.
DR GeneWiki; RAB5B; -.
DR GenomeRNAi; 5869; -.
DR Pharos; P61020; Tbio.
DR PRO; PR:P61020; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P61020; protein.
DR Bgee; ENSG00000111540; Expressed in lower esophagus mucosa and 194 other tissues.
DR ExpressionAtlas; P61020; baseline and differential.
DR Genevisible; P61020; HS.
DR GO; GO:0098993; C:anchored component of synaptic vesicle membrane; IEA:Ensembl.
DR GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR GO; GO:0031901; C:early endosome membrane; TAS:Reactome.
DR GO; GO:0030139; C:endocytic vesicle; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0019003; F:GDP binding; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0030742; F:GTP-dependent protein binding; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0019882; P:antigen processing and presentation; IMP:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0007032; P:endosome organization; IEA:Ensembl.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0048227; P:plasma membrane to endosome transport; IMP:UniProtKB.
DR GO; GO:0030100; P:regulation of endocytosis; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
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 3D-structure; Acetylation; Alternative splicing; Cell membrane; Endosome;
KW Glycoprotein; GTP-binding; Hydrolase; Lipoprotein; Membrane;
KW Nucleotide-binding; Phosphoprotein; Prenylation; Protein transport;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..215
FT /note="Ras-related protein Rab-5B"
FT /id="PRO_0000121107"
FT REGION 186..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 49..57
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT COMPBIAS 200..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 27..35
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|Ref.16, ECO:0007744|PDB:2HEI"
FT BINDING 46..52
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|Ref.16, ECO:0007744|PDB:2HEI"
FT BINDING 75..79
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P20339"
FT BINDING 133..136
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|Ref.16, ECO:0007744|PDB:2HEI"
FT BINDING 163..165
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|Ref.16, ECO:0007744|PDB:2HEI"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 84
FT /note="Phosphoserine; by LRRK2"
FT /evidence="ECO:0000269|PubMed:29125462"
FT LIPID 212
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P20339"
FT LIPID 213
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P20339"
FT VAR_SEQ 106..146
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045301"
FT MUTAGEN 34
FT /note="S->N: Constitutively inactivated. Strongly reduces
FT interaction with RIN2."
FT /evidence="ECO:0000269|PubMed:11733506"
FT MUTAGEN 79
FT /note="Q->L: Constitutively active."
FT /evidence="ECO:0000269|PubMed:11733506"
FT MUTAGEN 84
FT /note="S->A: Loss of phosphorylation. No effect on GDI1,
FT GDI2, CHML and CHM binding."
FT /evidence="ECO:0000269|PubMed:29125462"
FT MUTAGEN 84
FT /note="S->E: Phosphomimetic mutant. Loss of GDI1, GDI2,
FT CHML and CHM binding."
FT /evidence="ECO:0000269|PubMed:29125462"
FT STRAND 19..26
FT /evidence="ECO:0007829|PDB:2HEI"
FT HELIX 33..42
FT /evidence="ECO:0007829|PDB:2HEI"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:2HEI"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:2HEI"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:2HEI"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:2HEI"
FT HELIX 86..90
FT /evidence="ECO:0007829|PDB:2HEI"
FT STRAND 95..101
FT /evidence="ECO:0007829|PDB:2HEI"
FT HELIX 105..121
FT /evidence="ECO:0007829|PDB:2HEI"
FT STRAND 127..133
FT /evidence="ECO:0007829|PDB:2HEI"
FT HELIX 135..140
FT /evidence="ECO:0007829|PDB:2HEI"
FT HELIX 145..154
FT /evidence="ECO:0007829|PDB:2HEI"
FT STRAND 158..161
FT /evidence="ECO:0007829|PDB:2HEI"
FT TURN 164..166
FT /evidence="ECO:0007829|PDB:2HEI"
FT HELIX 170..180
FT /evidence="ECO:0007829|PDB:2HEI"
SQ SEQUENCE 215 AA; 23707 MW; D47AD834BCF8B591 CRC64;
MTSRSTARPN GQPQASKICQ FKLVLLGESA VGKSSLVLRF VKGQFHEYQE STIGAAFLTQ
SVCLDDTTVK FEIWDTAGQE RYHSLAPMYY RGAQAAIVVY DITNQETFAR AKTWVKELQR
QASPSIVIAL AGNKADLANK RMVEYEEAQA YADDNSLLFM ETSAKTAMNV NDLFLAIAKK
LPKSEPQNLG GAAGRSRGVD LHEQSQQNKS QCCSN
