RAB6B_HUMAN
ID RAB6B_HUMAN Reviewed; 208 AA.
AC Q9NRW1; B2R5Z9; B7Z337; D3DND3; Q92929;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Ras-related protein Rab-6B;
DE EC=3.6.5.2 {ECO:0000305|PubMed:16790928};
GN Name=RAB6B {ECO:0000312|HGNC:HGNC:14902};
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=10893188; DOI=10.1242/jcs.113.15.2725;
RA Opdam F.J.M., Echard A., Croes H.J.E., van den Hurk J.A.J.M.,
RA van de Vorstenbosch R.A., Ginsel L.A., Goud B., Fransen J.A.M.;
RT "The small GTPase Rab6B, a novel Rab6 subfamily member, is cell-type
RT specifically expressed and localised to the Golgi apparatus.";
RL J. Cell Sci. 113:2725-2735(2000).
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] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Amygdala, and Hippocampus;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=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 NUCLEOTIDE SEQUENCE [MRNA] OF 72-124 (ISOFORM 1/2).
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 [9]
RP FUNCTION, INTERACTION WITH BICD1, AND SUBCELLULAR LOCATION.
RX PubMed=17707369; DOI=10.1016/j.yexcr.2007.05.032;
RA Wanschers B.F.J.F., van de Vorstenbosch R., Schlager M.A., Splinter D.,
RA Akhmanova A., Hoogenraad C.C., Wieringa B., Fransen J.A.;
RT "A role for the Rab6B Bicaudal-D1 interaction in retrograde transport in
RT neuronal cells.";
RL Exp. Cell Res. 313:3408-3420(2007).
RN [10]
RP INTERACTION WITH DYNLRB1, AND SUBCELLULAR LOCATION.
RX PubMed=18044744; DOI=10.1002/cm.20254;
RA Wanschers B.F.J., van de Vorstenbosch R., Wijers M., Wieringa B.,
RA King S.M., Fransen J.;
RT "Rab6 family proteins interact with the dynein light chain protein
RT DYNLRB1.";
RL Cell Motil. Cytoskeleton 65:183-196(2008).
RN [11]
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 [12]
RP AMPYLATION AT TYR-82.
RX PubMed=21822290; DOI=10.1038/nature10335;
RA Mukherjee S., Liu X., Arasaki K., McDonough J., Galan J.E., Roy C.R.;
RT "Modulation of Rab GTPase function by a protein phosphocholine
RT transferase.";
RL Nature 477:103-106(2011).
RN [13]
RP INTERACTION WITH APBA1, AND MUTAGENESIS OF THR-27 AND GLN-72.
RX PubMed=23737971; DOI=10.1371/journal.pone.0064149;
RA Thyrock A., Ossendorf E., Stehling M., Kail M., Kurtz T., Pohlentz G.,
RA Waschbusch D., Eggert S., Formstecher E., Muthing J., Dreisewerd K.,
RA Kins S., Goud B., Barnekow A.;
RT "A new Mint1 isoform, but not the conventional Mint1, interacts with the
RT small GTPase Rab6.";
RL PLoS ONE 8:E64149-E64149(2013).
RN [14]
RP FUNCTION.
RX PubMed=26209634; DOI=10.1074/jbc.m115.669242;
RA Aizawa M., Fukuda M.;
RT "Small GTPase Rab2B and Its Specific Binding Protein Golgi-associated Rab2B
RT Interactor-like 4 (GARI-L4) Regulate Golgi Morphology.";
RL J. Biol. Chem. 290:22250-22261(2015).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) OF 13-174, AND CATALYTIC ACTIVITY.
RX PubMed=16790928; DOI=10.1107/s0907444906015319;
RA Garcia-Saez I., Tcherniuk S., Kozielski F.;
RT "The structure of human neuronal Rab6B in the active and inactive form.";
RL Acta Crystallogr. D 62:725-733(2006).
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 active GTP-bound and inactive
CC GDP-bound states. In their active state, drive transport of vesicular
CC carriers from donor organelles to acceptor organelles to regulate the
CC membrane traffic that maintains organelle identity and morphology
CC (Probable). Regulates the compacted morphology of the Golgi
CC (PubMed:26209634). Seems to have a role in retrograde membrane traffic
CC at the level of the Golgi complex. May function in retrograde transport
CC in neuronal cells (PubMed:17707369). {ECO:0000269|PubMed:17707369,
CC ECO:0000269|PubMed:26209634, ECO:0000305}.
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:0000305|PubMed:16790928};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000305|PubMed:16790928};
CC -!- ACTIVITY REGULATION: Regulated by guanine nucleotide exchange factors
CC (GEFs) which promote the exchange of bound GDP for free GTP, GTPase
CC activating proteins (GAPs) which increase the GTP hydrolysis activity,
CC and GDP dissociation inhibitors which inhibit the dissociation of the
CC nucleotide from the GTPase. {ECO:0000305}.
CC -!- SUBUNIT: Interacts with BICDL1/BICDR1; leads to its accumulation in the
CC pericentrosomal region (By similarity). Interacts with RAB6KIFL.
CC Interacts (GTP-bound) with BICD1 (via C-terminus); the interaction is
CC direct. Interacts (GDP-bound) with DYNLRB1. Interacts (GTP-bound) with
CC APBA1/MINT1 isoform 2, also called Mint1_826, but not with isoform 1.
CC {ECO:0000250, ECO:0000269|PubMed:17707369, ECO:0000269|PubMed:18044744,
CC ECO:0000269|PubMed:23737971}.
CC -!- INTERACTION:
CC Q9NRW1; Q02410-2: APBA1; NbExp=4; IntAct=EBI-1760079, EBI-9247455;
CC Q9NRW1; Q8TD16-2: BICD2; NbExp=3; IntAct=EBI-1760079, EBI-11975051;
CC Q9NRW1; Q9Y2V7: COG6; NbExp=5; IntAct=EBI-1760079, EBI-3866319;
CC Q9NRW1; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-1760079, EBI-16439278;
CC Q9NRW1; Q92871: PMM1; NbExp=5; IntAct=EBI-1760079, EBI-746784;
CC Q9NRW1; P52306-5: RAP1GDS1; NbExp=5; IntAct=EBI-1760079, EBI-12832744;
CC Q9NRW1; O14492-2: SH2B2; NbExp=3; IntAct=EBI-1760079, EBI-19952306;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:17707369, ECO:0000269|PubMed:18044744}; Lipid-
CC anchor {ECO:0000305}. Endoplasmic reticulum-Golgi intermediate
CC compartment {ECO:0000269|PubMed:17707369}. Cytoplasmic vesicle
CC {ECO:0000269|PubMed:17707369}. Note=Colocalizes with BICD1 at vesicular
CC structures that align along microtubules.
CC {ECO:0000269|PubMed:17707369}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NRW1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NRW1-2; Sequence=VSP_055831;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in brain.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AF166492; AAF61637.1; -; mRNA.
DR EMBL; AF498940; AAM21088.1; -; mRNA.
DR EMBL; BT007263; AAP35927.1; -; mRNA.
DR EMBL; AK295451; BAH12073.1; -; mRNA.
DR EMBL; AK312378; BAG35296.1; -; mRNA.
DR EMBL; AC080128; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW79158.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79159.1; -; Genomic_DNA.
DR EMBL; BC002510; AAH02510.1; -; mRNA.
DR EMBL; U66623; AAC51198.1; -; mRNA.
DR CCDS; CCDS3082.1; -. [Q9NRW1-1]
DR CCDS; CCDS87137.1; -. [Q9NRW1-2]
DR RefSeq; NP_057661.3; NM_016577.3. [Q9NRW1-1]
DR RefSeq; XP_011511195.1; XM_011512893.2.
DR PDB; 2E9S; X-ray; 1.78 A; A/B/C=13-174.
DR PDB; 2FE4; X-ray; 2.30 A; A=13-174.
DR PDB; 2FFQ; X-ray; 1.78 A; A=13-174.
DR PDBsum; 2E9S; -.
DR PDBsum; 2FE4; -.
DR PDBsum; 2FFQ; -.
DR AlphaFoldDB; Q9NRW1; -.
DR SMR; Q9NRW1; -.
DR BioGRID; 119610; 90.
DR IntAct; Q9NRW1; 45.
DR MINT; Q9NRW1; -.
DR STRING; 9606.ENSP00000285208; -.
DR iPTMnet; Q9NRW1; -.
DR PhosphoSitePlus; Q9NRW1; -.
DR SwissPalm; Q9NRW1; -.
DR BioMuta; RAB6B; -.
DR DMDM; 13633595; -.
DR EPD; Q9NRW1; -.
DR jPOST; Q9NRW1; -.
DR MassIVE; Q9NRW1; -.
DR MaxQB; Q9NRW1; -.
DR PaxDb; Q9NRW1; -.
DR PeptideAtlas; Q9NRW1; -.
DR PRIDE; Q9NRW1; -.
DR Antibodypedia; 46687; 187 antibodies from 24 providers.
DR DNASU; 51560; -.
DR Ensembl; ENST00000285208.9; ENSP00000285208.4; ENSG00000154917.11. [Q9NRW1-1]
DR Ensembl; ENST00000486858.5; ENSP00000419381.1; ENSG00000154917.11. [Q9NRW1-2]
DR Ensembl; ENST00000543906.5; ENSP00000437797.1; ENSG00000154917.11. [Q9NRW1-1]
DR GeneID; 51560; -.
DR KEGG; hsa:51560; -.
DR MANE-Select; ENST00000285208.9; ENSP00000285208.4; NM_016577.4; NP_057661.3.
DR UCSC; uc003epy.4; human. [Q9NRW1-1]
DR CTD; 51560; -.
DR DisGeNET; 51560; -.
DR GeneCards; RAB6B; -.
DR HGNC; HGNC:14902; RAB6B.
DR HPA; ENSG00000154917; Tissue enriched (brain).
DR MIM; 615852; gene.
DR neXtProt; NX_Q9NRW1; -.
DR OpenTargets; ENSG00000154917; -.
DR PharmGKB; PA34147; -.
DR VEuPathDB; HostDB:ENSG00000154917; -.
DR eggNOG; KOG0094; Eukaryota.
DR GeneTree; ENSGT00940000159656; -.
DR InParanoid; Q9NRW1; -.
DR OMA; TRFVYDH; -.
DR OrthoDB; 1277051at2759; -.
DR PhylomeDB; Q9NRW1; -.
DR TreeFam; TF300803; -.
DR BRENDA; 3.6.5.2; 2681.
DR PathwayCommons; Q9NRW1; -.
DR Reactome; R-HSA-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Reactome; R-HSA-6811440; Retrograde transport at the Trans-Golgi-Network.
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; Q9NRW1; -.
DR SIGNOR; Q9NRW1; -.
DR BioGRID-ORCS; 51560; 12 hits in 1072 CRISPR screens.
DR ChiTaRS; RAB6B; human.
DR EvolutionaryTrace; Q9NRW1; -.
DR GeneWiki; RAB6B; -.
DR GenomeRNAi; 51560; -.
DR Pharos; Q9NRW1; Tbio.
DR PRO; PR:Q9NRW1; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9NRW1; protein.
DR Bgee; ENSG00000154917; Expressed in lateral nuclear group of thalamus and 168 other tissues.
DR ExpressionAtlas; Q9NRW1; baseline and differential.
DR Genevisible; Q9NRW1; HS.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR GO; GO:0098793; C:presynapse; IEA:Ensembl.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0031489; F:myosin V binding; IPI:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; IMP:UniProtKB.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0031175; P:neuron projection development; TAS:UniProtKB.
DR GO; GO:1903292; P:protein localization to Golgi membrane; IDA:UniProtKB.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IBA:GO_Central.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; 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; Alternative splicing; Cytoplasmic vesicle;
KW ER-Golgi transport; Golgi apparatus; GTP-binding; Hydrolase; Lipoprotein;
KW Membrane; Methylation; Nucleotide-binding; Phosphoprotein; Prenylation;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..208
FT /note="Ras-related protein Rab-6B"
FT /id="PRO_0000121115"
FT MOTIF 42..50
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 20..27
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 45
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 68..72
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 126..129
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT MOD_RES 82
FT /note="O-AMP-tyrosine; by Legionella DrrA"
FT /evidence="ECO:0000269|PubMed:21822290"
FT MOD_RES 208
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 206
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 208
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..24
FT /note="MSAGGDFGNPLRKFKLVFLGEQSV -> MWHMTRNWPLV (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055831"
FT MUTAGEN 27
FT /note="T->N: Loss of APBA1-binding."
FT /evidence="ECO:0000269|PubMed:23737971"
FT MUTAGEN 72
FT /note="Q->L: Interacts with APBA1."
FT /evidence="ECO:0000269|PubMed:23737971"
FT STRAND 15..19
FT /evidence="ECO:0007829|PDB:2E9S"
FT HELIX 26..35
FT /evidence="ECO:0007829|PDB:2E9S"
FT STRAND 47..57
FT /evidence="ECO:0007829|PDB:2E9S"
FT STRAND 60..69
FT /evidence="ECO:0007829|PDB:2E9S"
FT HELIX 73..78
FT /evidence="ECO:0007829|PDB:2E9S"
FT HELIX 79..84
FT /evidence="ECO:0007829|PDB:2E9S"
FT STRAND 87..94
FT /evidence="ECO:0007829|PDB:2E9S"
FT HELIX 98..102
FT /evidence="ECO:0007829|PDB:2E9S"
FT HELIX 104..115
FT /evidence="ECO:0007829|PDB:2E9S"
FT STRAND 118..126
FT /evidence="ECO:0007829|PDB:2E9S"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:2E9S"
FT HELIX 138..147
FT /evidence="ECO:0007829|PDB:2E9S"
FT STRAND 151..154
FT /evidence="ECO:0007829|PDB:2E9S"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:2E9S"
FT HELIX 163..174
FT /evidence="ECO:0007829|PDB:2E9S"
SQ SEQUENCE 208 AA; 23462 MW; E81C831996E2446D CRC64;
MSAGGDFGNP LRKFKLVFLG EQSVGKTSLI TRFMYDSFDN TYQATIGIDF LSKTMYLEDR
TVRLQLWDTA GQERFRSLIP SYIRDSTVAV VVYDITNLNS FQQTSKWIDD VRTERGSDVI
IMLVGNKTDL ADKRQITIEE GEQRAKELSV MFIETSAKTG YNVKQLFRRV ASALPGMENV
QEKSKEGMID IKLDKPQEPP ASEGGCSC
