RAB8B_HUMAN
ID RAB8B_HUMAN Reviewed; 207 AA.
AC Q92930; Q5JPC4; Q9P293;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Ras-related protein Rab-8B;
DE Flags: Precursor;
GN Name=RAB8B;
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].
RC TISSUE=Fetal brain;
RA Seki N., Saito T.;
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph node;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 67-119.
RC TISSUE=Melanoma;
RX PubMed=9030196; DOI=10.1016/s0167-4889(96)00169-3;
RA Chen D., Guo J., Gahl W.A.;
RT "RAB GTPases expressed in human melanoma cells.";
RL Biochim. Biophys. Acta 1355:1-6(1997).
RN [7]
RP INTERACTION WITH RAB3IP.
RC TISSUE=Brain;
RX PubMed=12221131; DOI=10.1091/mbc.e02-03-0143;
RA Hattula K., Furuhjelm J., Arffman A., Peranen J.;
RT "A Rab8-specific GDP/GTP exchange factor is involved in actin remodeling
RT and polarized membrane transport.";
RL Mol. Biol. Cell 13:3268-3280(2002).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
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 [10]
RP SUBCELLULAR LOCATION.
RX PubMed=21255211; DOI=10.1111/j.1600-0854.2011.01165.x;
RA Seto S., Tsujimura K., Koide Y.;
RT "Rab GTPases regulating phagosome maturation are differentially recruited
RT to mycobacterial phagosomes.";
RL Traffic 12:407-420(2011).
RN [11]
RP INTERACTION WITH GDI1; GDI2; CHM AND CHML, PHOSPHORYLATION AT THR-72, AND
RP MUTAGENESIS OF THR-72.
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).
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. That Rab may be involved in
CC polarized vesicular trafficking and neurotransmitter release. May
CC participate in cell junction dynamics in Sertoli cells (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Associated with actin, delta-catenin and alpha and beta
CC tubulins (By similarity). Interacts with OTOF (By similarity).
CC Interacts with PEX5R (By similarity). Interacts with RAB3IP
CC (PubMed:12221131). Interacts with VIM (By similarity). Interacts with
CC CDH1 (By similarity). Interacts with MICALL2 (By similarity). Interacts
CC with GDI1, GDI2, CHML and CHM; phosphorylation at Thr-72 disrupts these
CC interactions (PubMed:29125462). {ECO:0000250|UniProtKB:P61028,
CC ECO:0000250|UniProtKB:P70550, ECO:0000269|PubMed:12221131,
CC ECO:0000269|PubMed:29125462}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle,
CC phagosome {ECO:0000269|PubMed:21255211}. Cytoplasmic vesicle, phagosome
CC membrane {ECO:0000269|PubMed:21255211}; Lipid-anchor
CC {ECO:0000269|PubMed:21255211}; Cytoplasmic side
CC {ECO:0000269|PubMed:21255211}. Note=Recruited to phagosomes containing
CC S.aureus or M.tuberculosis.
CC -!- PTM: Phosphorylation of Thr-72 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 -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AB038995; BAA92249.1; -; mRNA.
DR EMBL; AK001111; BAG50856.1; -; mRNA.
DR EMBL; AL833365; CAI46143.1; -; mRNA.
DR EMBL; AC016207; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC020654; AAH20654.1; -; mRNA.
DR EMBL; U66624; AAC51199.1; -; mRNA.
DR CCDS; CCDS10183.1; -.
DR RefSeq; NP_057614.1; NM_016530.2.
DR AlphaFoldDB; Q92930; -.
DR SMR; Q92930; -.
DR BioGRID; 119719; 76.
DR IntAct; Q92930; 27.
DR MINT; Q92930; -.
DR STRING; 9606.ENSP00000312734; -.
DR DrugBank; DB04315; Guanosine-5'-Diphosphate.
DR DrugBank; DB02082; Phosphoaminophosphonic acid guanylate ester.
DR GlyGen; Q92930; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q92930; -.
DR PhosphoSitePlus; Q92930; -.
DR SwissPalm; Q92930; -.
DR BioMuta; RAB8B; -.
DR DMDM; 13638434; -.
DR EPD; Q92930; -.
DR jPOST; Q92930; -.
DR MassIVE; Q92930; -.
DR MaxQB; Q92930; -.
DR PaxDb; Q92930; -.
DR PeptideAtlas; Q92930; -.
DR PRIDE; Q92930; -.
DR ProteomicsDB; 75610; -.
DR Antibodypedia; 25649; 262 antibodies from 31 providers.
DR DNASU; 51762; -.
DR Ensembl; ENST00000321437.9; ENSP00000312734.4; ENSG00000166128.13.
DR GeneID; 51762; -.
DR KEGG; hsa:51762; -.
DR MANE-Select; ENST00000321437.9; ENSP00000312734.4; NM_016530.3; NP_057614.1.
DR UCSC; uc002alz.4; human.
DR CTD; 51762; -.
DR DisGeNET; 51762; -.
DR GeneCards; RAB8B; -.
DR HGNC; HGNC:30273; RAB8B.
DR HPA; ENSG00000166128; Tissue enhanced (bone).
DR MIM; 613532; gene.
DR neXtProt; NX_Q92930; -.
DR OpenTargets; ENSG00000166128; -.
DR PharmGKB; PA134944620; -.
DR VEuPathDB; HostDB:ENSG00000166128; -.
DR eggNOG; KOG0078; Eukaryota.
DR GeneTree; ENSGT00940000155363; -.
DR InParanoid; Q92930; -.
DR OMA; IMENRSK; -.
DR OrthoDB; 1426655at2759; -.
DR PhylomeDB; Q92930; -.
DR TreeFam; TF314097; -.
DR PathwayCommons; Q92930; -.
DR Reactome; R-HSA-8854214; TBC/RABGAPs.
DR Reactome; R-HSA-8873719; RAB geranylgeranylation.
DR Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR SignaLink; Q92930; -.
DR BioGRID-ORCS; 51762; 8 hits in 1077 CRISPR screens.
DR ChiTaRS; RAB8B; human.
DR GeneWiki; RAB8B; -.
DR GenomeRNAi; 51762; -.
DR Pharos; Q92930; Tbio.
DR PRO; PR:Q92930; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q92930; protein.
DR Bgee; ENSG00000166128; Expressed in sperm and 192 other tissues.
DR ExpressionAtlas; Q92930; baseline and differential.
DR Genevisible; Q92930; HS.
DR GO; GO:0051286; C:cell tip; IEA:Ensembl.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0005778; C:peroxisomal membrane; IDA:UniProtKB.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:UniProtKB.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0055038; C:recycling endosome membrane; TAS:Reactome.
DR GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central.
DR GO; GO:0030140; C:trans-Golgi network transport vesicle; IBA:GO_Central.
DR GO; GO:0019003; F:GDP binding; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
DR GO; GO:0030911; F:TPR domain binding; IEA:Ensembl.
DR GO; GO:0019882; P:antigen processing and presentation; IMP:UniProtKB.
DR GO; GO:0150115; P:cell-substrate junction organization; ISS:UniProtKB.
DR GO; GO:0032456; P:endocytic recycling; IBA:GO_Central.
DR GO; GO:0048210; P:Golgi vesicle fusion to target membrane; IBA:GO_Central.
DR GO; GO:0031346; P:positive regulation of cell projection organization; IEA:Ensembl.
DR GO; GO:0051461; P:positive regulation of corticotropin secretion; IEA:Ensembl.
DR GO; GO:0045046; P:protein import into peroxisome membrane; IDA:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; IBA:GO_Central.
DR GO; GO:0009306; P:protein secretion; IBA:GO_Central.
DR GO; GO:0017157; P:regulation of exocytosis; IBA:GO_Central.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; 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 Cell membrane; Cytoplasmic vesicle; GTP-binding; Lipoprotein; Membrane;
KW Methylation; Nucleotide-binding; Phosphoprotein; Prenylation;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..204
FT /note="Ras-related protein Rab-8B"
FT /id="PRO_0000121134"
FT PROPEP 205..207
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000370800"
FT MOTIF 37..45
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 15..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 121..124
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 72
FT /note="Phosphothreonine; by LRRK2"
FT /evidence="ECO:0000269|PubMed:29125462"
FT MOD_RES 180
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61028"
FT MOD_RES 204
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000255"
FT LIPID 204
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT MUTAGEN 72
FT /note="T->A: Loss of phosphorylation. No effect on GDI1 and
FT GDI2 binding. Reduced binding to CHM and CHML."
FT /evidence="ECO:0000269|PubMed:29125462"
FT MUTAGEN 72
FT /note="T->E: Phosphomimetic mutant. Loss of binding to
FT GDI1, GDI2, CHM, and CHML."
FT /evidence="ECO:0000269|PubMed:29125462"
SQ SEQUENCE 207 AA; 23584 MW; 5960993C0F87F944 CRC64;
MAKTYDYLFK LLLIGDSGVG KTCLLFRFSE DAFNTTFIST IGIDFKIRTI ELDGKKIKLQ
IWDTAGQERF RTITTAYYRG AMGIMLVYDI TNEKSFDNIK NWIRNIEEHA SSDVERMILG
NKCDMNDKRQ VSKERGEKLA IDYGIKFLET SAKSSANVEE AFFTLARDIM TKLNRKMNDS
NSAGAGGPVK ITENRSKKTS FFRCSLL
