RAB6A_HUMAN
ID RAB6A_HUMAN Reviewed; 208 AA.
AC P20340; A8K133; B7Z772; F5H668; Q1W5D8; Q5U0A8; Q9UBE4;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 237.
DE RecName: Full=Ras-related protein Rab-6A;
DE Short=Rab-6;
GN Name=RAB6A; Synonyms=RAB6;
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=2501306; DOI=10.1016/s0021-9258(18)63872-4;
RA Zahraoui A., Touchot N., Chardin P., Tavitian A.;
RT "The human Rab genes encode a family of GTP-binding proteins related to
RT yeast YPT1 and SEC4 products involved in secretion.";
RL J. Biol. Chem. 264:12394-12401(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Pancreatic tumor;
RX PubMed=10996854;
RX DOI=10.1002/1097-4644(20001215)79:4<628::aid-jcb120>3.0.co;2-t;
RA Caillol N., Pasqualini E., Lloubes R., Lombardo D.;
RT "Impairment of bile salt-dependent lipase secretion in human pancreatic
RT tumoral SOJ-6 cells.";
RL J. Cell. Biochem. 79:628-647(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=11054569; DOI=10.1016/s0378-1119(00)00395-4;
RA Shan J., Mason J.M., Yuan L., Barcia M., Porti D., Calabro A., Budman D.,
RA Vinciguerra V., Xu H.-P.;
RT "Rab6c, a new member of the Rab gene family, is involved in drug resistance
RT in MCF7/AdrR cells.";
RL Gene 257:67-75(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY,
RP CHARACTERIZATION, AND SUBCELLULAR LOCATION (ISOFORMS 1 AND 2).
RX PubMed=11071909; DOI=10.1091/mbc.11.11.3819;
RA Echard A., Opdam F.J.M., de Leeuw H.J.P.C., Jollivet F., Savelkoul P.,
RA Hendriks W., Voorberg J., Goud B., Fransen J.A.M.;
RT "Alternative splicing of the human Rab6A gene generates two close but
RT functionally different isoforms.";
RL Mol. Biol. Cell 11:3819-3833(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Barr F.A.;
RT "A second form of RAB6 in humans.";
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC TISSUE=Heart;
RA Delisle B.P., Foell J.D., Slind J.K., Kilby J.A., Balijepalli R.C.,
RA Kamp T.J., January C.T.;
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).
RC TISSUE=Brain, Spleen, 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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 [9]
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 (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Kidney, Placenta, and Testis;
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 [12]
RP PROTEIN SEQUENCE OF 2-13; 64-74; 77-84 AND 116-143, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Platelet;
RA Bienvenut W.V., Claeys D.;
RL Submitted (NOV-2005) to UniProtKB.
RN [13]
RP INTERACTION WITH RABGAP1.
RX PubMed=10202141; DOI=10.1093/emboj/18.7.1772;
RA Cuif M.-H., Possmayer F., Zander H., Bordes N., Jollivet F.,
RA Couedel-Courteille A., Janoueix-Lerosey I., Langsley G., Bornens M.,
RA Goud B.;
RT "Characterization of GAPCenA, a GTPase activating protein for Rab6, part of
RT which associates with the centrosome.";
RL EMBO J. 18:1772-1782(1999).
RN [14]
RP INTERACTION WITH BICD1 AND BICD2.
RX PubMed=12447383; DOI=10.1038/ncb891;
RA Matanis T., Akhmanova A., Wulf P., Del Nery E., Weide T., Stepanova T.,
RA Galjart N., Grosveld F., Goud B., De Zeeuw C.I., Barnekow A.,
RA Hoogenraad C.C.;
RT "Bicaudal-D regulates COPI-independent Golgi-ER transport by recruiting the
RT dynein-dynactin motor complex.";
RL Nat. Cell Biol. 4:986-992(2002).
RN [15]
RP INTERACTION WITH VSP52.
RX PubMed=15878329; DOI=10.1016/j.yexcr.2005.01.022;
RA Liewen H., Meinhold-Heerlein I., Oliveira V., Schwarzenbacher R., Luo G.,
RA Wadle A., Jung M., Pfreundschuh M., Stenner-Liewen F.;
RT "Characterization of the human GARP (Golgi associated retrograde protein)
RT complex.";
RL Exp. Cell Res. 306:24-34(2005).
RN [16]
RP INTERACTION WITH TMF1.
RX PubMed=17698061; DOI=10.1016/j.yexcr.2007.07.010;
RA Yamane J., Kubo A., Nakayama K., Yuba-Kubo A., Katsuno T., Tsukita S.,
RA Tsukita S.;
RT "Functional involvement of TMF/ARA160 in Rab6-dependent retrograde membrane
RT traffic.";
RL Exp. Cell Res. 313:3472-3485(2007).
RN [17]
RP INTERACTION WITH DYNLRB1.
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 [18]
RP INTERACTION WITH SCYL1BP1.
RX PubMed=18997784; DOI=10.1038/ng.252;
RA Hennies H.C., Kornak U., Zhang H., Egerer J., Zhang X., Seifert W.,
RA Kuhnisch J., Budde B., Naetebus M., Brancati F., Wilcox W.R., Mueller D.,
RA Kaplan P.B., Rajab A., Zampino G., Fodale V., Dallapiccola B., Newman W.,
RA Metcalfe K., Clayton-Smith J., Tassabehji M., Steinmann B., Barr F.A.,
RA Nuernberg P., Wieacker P., Mundlos S.;
RT "Gerodermia osteodysplastica is caused by mutations in SCYL1BP1, a Rab-6
RT interacting golgin.";
RL Nat. Genet. 40:1410-1412(2008).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-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 [20]
RP INTERACTION WITH PIFO.
RX PubMed=20643351; DOI=10.1016/j.devcel.2010.06.005;
RA Kinzel D., Boldt K., Davis E.E., Burtscher I., Trumbach D., Diplas B.,
RA Attie-Bitach T., Wurst W., Katsanis N., Ueffing M., Lickert H.;
RT "Pitchfork regulates primary cilia disassembly and left-right asymmetry.";
RL Dev. Cell 19:66-77(2010).
RN [21]
RP INTERACTION WITH BICD2.
RX PubMed=20386726; DOI=10.1371/journal.pbio.1000350;
RA Splinter D., Tanenbaum M.E., Lindqvist A., Jaarsma D., Flotho A., Yu K.L.,
RA Grigoriev I., Engelsma D., Haasdijk E.D., Keijzer N., Demmers J.,
RA Fornerod M., Melchior F., Hoogenraad C.C., Medema R.H., Akhmanova A.;
RT "Bicaudal D2, dynein, and kinesin-1 associate with nuclear pore complexes
RT and regulate centrosome and nuclear positioning during mitotic entry.";
RL PLoS Biol. 8:E1000350-E1000350(2010).
RN [22]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [23]
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 [24]
RP INTERACTION WITH HUMAN CYTOMEGALOVIRUS PROTEIN UL32 (MICROBIAL INFECTION).
RX PubMed=21411515; DOI=10.1128/jvi.02605-10;
RA Indran S.V., Britt W.J.;
RT "A role for the small GTPase Rab6 in assembly of human cytomegalovirus.";
RL J. Virol. 85:5213-5219(2011).
RN [25]
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 [26]
RP INTERACTION WITH RIC1 AND RGP1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP THR-27.
RX PubMed=23091056; DOI=10.1074/jbc.m112.414565;
RA Pusapati G.V., Luchetti G., Pfeffer S.R.;
RT "Ric1-Rgp1 complex is a guanine nucleotide exchange factor for the late
RT Golgi Rab6A GTPase and an effector of the medial Golgi Rab33B GTPase.";
RL J. Biol. Chem. 287:42129-42137(2012).
RN [27]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [28]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [29]
RP INTERACTION WITH BICD2.
RX PubMed=23664119; DOI=10.1016/j.ajhg.2013.04.013;
RA Peeters K., Litvinenko I., Asselbergh B., Almeida-Souza L., Chamova T.,
RA Geuens T., Ydens E., Zimon M., Irobi J., De Vriendt E., De Winter V.,
RA Ooms T., Timmerman V., Tournev I., Jordanova A.;
RT "Molecular defects in the motor adaptor BICD2 cause proximal spinal
RT muscular atrophy with autosomal-dominant inheritance.";
RL Am. J. Hum. Genet. 92:955-964(2013).
RN [30]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [31]
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 [32]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [33]
RP FUNCTION, INTERACTION WITH BICD2, SUBCELLULAR LOCATION, AND ISOPRENYLATION.
RX PubMed=25962623; DOI=10.1016/j.bbamcr.2015.05.005;
RA Matsuto M., Kano F., Murata M.;
RT "Reconstitution of the targeting of Rab6A to the Golgi apparatus in semi-
RT intact HeLa cells: A role of BICD2 in stabilizing Rab6A on Golgi membranes
RT and a concerted role of Rab6A/BICD2 interactions in Golgi-to-ER retrograde
RT transport.";
RL Biochim. Biophys. Acta 1853:2592-2609(2015).
RN [34]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [35]
RP X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 13-174 IN COMPLEX WITH GTP, AND
RP MUTAGENESIS OF GLN-72.
RX PubMed=16332443; DOI=10.1016/j.jsb.2005.10.001;
RA Bergbrede T., Pylypenko O., Rak A., Alexandrov K.;
RT "Structure of the extremely slow GTPase Rab6A in the GTP bound form at 1.8A
RT resolution.";
RL J. Struct. Biol. 152:235-238(2005).
RN [36]
RP X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) OF 10-177 IN COMPLEX WITH GTP
RP ANALOG.
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 [37]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-206 IN COMPLEX WITH GTP,
RP INTERACTION WITH GCC2, AND MUTAGENESIS OF GLN-72.
RX PubMed=18243103; DOI=10.1016/j.cell.2007.11.048;
RA Burguete A.S., Fenn T.D., Brunger A.T., Pfeffer S.R.;
RT "Rab and Arl GTPase family members cooperate in the localization of the
RT golgin GCC185.";
RL Cell 132:286-298(2008).
RN [38]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 8-195 IN COMPLEX WITH GTP AND
RP RAB6IP1, AND MUTAGENESIS OF ILE-46 AND GLN-72.
RX PubMed=19141279; DOI=10.1016/j.str.2008.10.014;
RA Recacha R., Boulet A., Jollivet F., Monier S., Houdusse A., Goud B.,
RA Khan A.R.;
RT "Structural basis for recruitment of Rab6-interacting protein 1 to Golgi
RT via a RUN domain.";
RL Structure 17:21-30(2009).
CC -!- FUNCTION: Protein transport. Regulator of membrane traffic from the
CC Golgi apparatus towards the endoplasmic reticulum (ER). Has a low
CC GTPase activity. Involved in COPI-independent retrograde transport from
CC the Golgi to the ER (PubMed:25962623). {ECO:0000269|PubMed:25962623}.
CC -!- SUBUNIT: Interacts with BICDL1; leads to its accumulation in the
CC pericentrosomal region (By similarity). Interacts with SCYL1BP1.
CC Interacts with VSP52 and RABGAP1. Interacts with GCC2 (via its GRIP
CC domain). Interacts with RAB6IP1 (via its RUN 1 domain). Isoform 1
CC interacts with RAB6KIFL. Isoform 2 does not interact with RAB6KIFL.
CC Isoform 1 interacts with BICD1. Isoform 2 interacts with BICD1. Isoform
CC 1 interacts with BICD2. Isoform 2 interacts with BICD2. Interacts with
CC TMF1. Isoform 1 (GTP-bound) interacts with DYNLRB1; the interaction is
CC direct. Isoform 2 (GDP-bound) interacts with DYNLRB1; the interaction
CC is direct. Interacts with PIFO. Interacts (GTP-bound) with APBA1/MINT1
CC isoform 2, also called Mint1_826, but not with isoform 1. Interacts
CC with RIC1 and RGP1; the interactions are direct with a preference for
CC RAB6A-GDP. {ECO:0000250|UniProtKB:P35279, ECO:0000269|PubMed:10202141,
CC ECO:0000269|PubMed:12447383, ECO:0000269|PubMed:15878329,
CC ECO:0000269|PubMed:16034420, ECO:0000269|PubMed:16332443,
CC ECO:0000269|PubMed:17698061, ECO:0000269|PubMed:18044744,
CC ECO:0000269|PubMed:18243103, ECO:0000269|PubMed:18997784,
CC ECO:0000269|PubMed:19141279, ECO:0000269|PubMed:20386726,
CC ECO:0000269|PubMed:20643351, ECO:0000269|PubMed:23091056,
CC ECO:0000269|PubMed:23664119, ECO:0000269|PubMed:23737971,
CC ECO:0000269|PubMed:25962623}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human cytomegalovirus
CC protein UL32. {ECO:0000269|PubMed:21411515}.
CC -!- INTERACTION:
CC P20340; Q8TD16: BICD2; NbExp=3; IntAct=EBI-1052826, EBI-2372628;
CC P20340; Q8IWJ2: GCC2; NbExp=4; IntAct=EBI-1052826, EBI-1645320;
CC P20340; Q01968: OCRL; NbExp=12; IntAct=EBI-1052826, EBI-6148898;
CC P20340; Q92871: PMM1; NbExp=4; IntAct=EBI-1052826, EBI-746784;
CC P20340-1; Q02410-2: APBA1; NbExp=4; IntAct=EBI-8851226, EBI-9247455;
CC P20340-1; Q6PAL8: Dennd5a; Xeno; NbExp=4; IntAct=EBI-8851226, EBI-15750630;
CC P20340-1; Q5ZWZ3: lpg0940; Xeno; NbExp=2; IntAct=EBI-8851226, EBI-6417967;
CC P20340-2; P05067: APP; NbExp=3; IntAct=EBI-8840191, EBI-77613;
CC P20340-2; Q9NP61: ARFGAP3; NbExp=3; IntAct=EBI-8840191, EBI-2875816;
CC P20340-2; P20042: EIF2S2; NbExp=3; IntAct=EBI-8840191, EBI-711977;
CC P20340-2; Q92871: PMM1; NbExp=3; IntAct=EBI-8840191, EBI-746784;
CC P20340-2; Q16560-2: SNRNP35; NbExp=3; IntAct=EBI-8840191, EBI-12938570;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:23091056, ECO:0000269|PubMed:25962623}; Lipid-
CC anchor {ECO:0000269|PubMed:25962623}. Note=BICD2 facilitates its
CC targeting to Golgi apparatus membrane. {ECO:0000269|PubMed:25962623}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Golgi apparatus membrane
CC {ECO:0000269|PubMed:11071909}; Lipid-anchor {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Golgi apparatus membrane
CC {ECO:0000269|PubMed:11071909}; Lipid-anchor {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=Rab-6a;
CC IsoId=P20340-1; Sequence=Displayed;
CC Name=2; Synonyms=Rab-6a', Rab-6C, Rab6C;
CC IsoId=P20340-2; Sequence=VSP_005527;
CC Name=3;
CC IsoId=P20340-3; Sequence=VSP_045302;
CC Name=4;
CC IsoId=P20340-4; Sequence=VSP_046967, VSP_005527;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11071909}.
CC -!- PTM: Prenylated. {ECO:0000269|PubMed:25962623}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; M28212; AAA60246.1; -; mRNA.
DR EMBL; AF130986; AAD25535.1; -; mRNA.
DR EMBL; AF119836; AAF23593.1; -; mRNA.
DR EMBL; AF198616; AAF73841.1; -; mRNA.
DR EMBL; AF130122; AAD27707.1; -; mRNA.
DR EMBL; DQ437503; ABD93919.1; -; mRNA.
DR EMBL; AK057157; BAB71371.1; -; mRNA.
DR EMBL; AK289748; BAF82437.1; -; mRNA.
DR EMBL; AK290132; BAF82821.1; -; mRNA.
DR EMBL; AK301534; BAH13508.1; -; mRNA.
DR EMBL; AF498939; AAM21087.1; -; mRNA.
DR EMBL; AF498941; AAM21089.1; -; mRNA.
DR EMBL; BT019698; AAV38504.1; -; mRNA.
DR EMBL; AP002770; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP002993; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC003617; AAH03617.1; -; mRNA.
DR EMBL; BC068486; AAH68486.1; -; mRNA.
DR EMBL; BC096818; AAH96818.1; -; mRNA.
DR CCDS; CCDS58155.1; -. [P20340-4]
DR CCDS; CCDS58156.1; -. [P20340-3]
DR CCDS; CCDS8223.1; -. [P20340-2]
DR CCDS; CCDS8224.1; -. [P20340-1]
DR PIR; G34323; G34323.
DR RefSeq; NP_001230647.1; NM_001243718.1. [P20340-3]
DR RefSeq; NP_001230648.1; NM_001243719.1. [P20340-4]
DR RefSeq; NP_002860.2; NM_002869.4. [P20340-2]
DR RefSeq; NP_942599.1; NM_198896.1. [P20340-1]
DR PDB; 1YZQ; X-ray; 1.78 A; A=10-177.
DR PDB; 2GIL; X-ray; 1.82 A; A/B/C/D=13-174.
DR PDB; 3BBP; X-ray; 3.00 A; A/B/C=1-206.
DR PDB; 3CWZ; X-ray; 3.20 A; A=8-195.
DR PDB; 4DKX; X-ray; 1.90 A; A/B=1-208.
DR PDB; 5LEF; X-ray; 2.09 A; A/B=8-195.
DR PDBsum; 1YZQ; -.
DR PDBsum; 2GIL; -.
DR PDBsum; 3BBP; -.
DR PDBsum; 3CWZ; -.
DR PDBsum; 4DKX; -.
DR PDBsum; 5LEF; -.
DR AlphaFoldDB; P20340; -.
DR SMR; P20340; -.
DR BioGRID; 111808; 115.
DR DIP; DIP-39668N; -.
DR IntAct; P20340; 41.
DR MINT; P20340; -.
DR STRING; 9606.ENSP00000311449; -.
DR BindingDB; P20340; -.
DR ChEMBL; CHEMBL4105703; -.
DR iPTMnet; P20340; -.
DR MetOSite; P20340; -.
DR PhosphoSitePlus; P20340; -.
DR SwissPalm; P20340; -.
DR BioMuta; RAB6A; -.
DR DMDM; 131796; -.
DR EPD; P20340; -.
DR jPOST; P20340; -.
DR MassIVE; P20340; -.
DR MaxQB; P20340; -.
DR PaxDb; P20340; -.
DR PeptideAtlas; P20340; -.
DR PRIDE; P20340; -.
DR ProteomicsDB; 27097; -.
DR ProteomicsDB; 53752; -. [P20340-1]
DR ProteomicsDB; 53753; -. [P20340-2]
DR ProteomicsDB; 61249; -.
DR TopDownProteomics; P20340-2; -. [P20340-2]
DR ABCD; P20340; 1 sequenced antibody.
DR Antibodypedia; 4093; 301 antibodies from 33 providers.
DR DNASU; 5870; -.
DR Ensembl; ENST00000310653.10; ENSP00000311449.5; ENSG00000175582.20. [P20340-2]
DR Ensembl; ENST00000336083.8; ENSP00000336850.3; ENSG00000175582.20. [P20340-1]
DR Ensembl; ENST00000541588.5; ENSP00000445350.1; ENSG00000175582.20. [P20340-3]
DR Ensembl; ENST00000541973.5; ENSP00000443782.2; ENSG00000175582.20. [P20340-4]
DR GeneID; 5870; -.
DR KEGG; hsa:5870; -.
DR MANE-Select; ENST00000336083.8; ENSP00000336850.3; NM_198896.2; NP_942599.1.
DR UCSC; uc001oue.4; human. [P20340-1]
DR CTD; 5870; -.
DR DisGeNET; 5870; -.
DR GeneCards; RAB6A; -.
DR HGNC; HGNC:9786; RAB6A.
DR HPA; ENSG00000175582; Low tissue specificity.
DR MIM; 179513; gene.
DR neXtProt; NX_P20340; -.
DR OpenTargets; ENSG00000175582; -.
DR PharmGKB; PA34146; -.
DR VEuPathDB; HostDB:ENSG00000175582; -.
DR eggNOG; KOG0094; Eukaryota.
DR GeneTree; ENSGT00940000154769; -.
DR HOGENOM; CLU_041217_10_2_1; -.
DR InParanoid; P20340; -.
DR OMA; PVSNDGC; -.
DR PhylomeDB; P20340; -.
DR TreeFam; TF300803; -.
DR PathwayCommons; P20340; -.
DR Reactome; R-HSA-1912420; Pre-NOTCH Processing in Golgi.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
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; P20340; -.
DR SIGNOR; P20340; -.
DR BioGRID-ORCS; 5870; 325 hits in 1019 CRISPR screens.
DR ChiTaRS; RAB6A; human.
DR EvolutionaryTrace; P20340; -.
DR GeneWiki; RAB6A; -.
DR GenomeRNAi; 5870; -.
DR Pharos; P20340; Tchem.
DR PRO; PR:P20340; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P20340; protein.
DR Bgee; ENSG00000175582; Expressed in cortical plate and 167 other tissues.
DR ExpressionAtlas; P20340; baseline and differential.
DR Genevisible; P20340; HS.
DR GO; GO:0002080; C:acrosomal membrane; ISS:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0070381; C:endosome to plasma membrane transport vesicle; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
DR GO; GO:0005802; C:trans-Golgi network; IDA:BHF-UCL.
DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0031489; F:myosin V binding; IPI:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; IPI:BHF-UCL.
DR GO; GO:0019882; P:antigen processing and presentation; IMP:UniProtKB.
DR GO; GO:0034498; P:early endosome to Golgi transport; 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:0072385; P:minus-end-directed organelle transport along microtubule; TAS:BHF-UCL.
DR GO; GO:0031175; P:neuron projection development; TAS:UniProtKB.
DR GO; GO:0018125; P:peptidyl-cysteine methylation; IDA:MGI.
DR GO; GO:0034067; P:protein localization to Golgi apparatus; IDA:UniProtKB.
DR GO; GO:1903292; P:protein localization to Golgi membrane; IMP: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; IMP:UniProtKB.
DR DisProt; DP02733; -.
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; Direct protein sequencing;
KW ER-Golgi transport; Golgi apparatus; GTP-binding; Host-virus interaction;
KW Lipoprotein; Membrane; Methylation; Nucleotide-binding; Phosphoprotein;
KW Prenylation; Protein transport; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.12, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712"
FT CHAIN 2..208
FT /note="Ras-related protein Rab-6A"
FT /id="PRO_0000121112"
FT MOTIF 42..50
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 20..28
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:16332443,
FT ECO:0000269|PubMed:18243103, ECO:0000269|PubMed:19141279"
FT BINDING 68..72
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:16332443,
FT ECO:0000269|PubMed:18243103, ECO:0000269|PubMed:19141279"
FT BINDING 126..129
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:16332443,
FT ECO:0000269|PubMed:18243103, ECO:0000269|PubMed:19141279"
FT BINDING 156..158
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:16332443,
FT ECO:0000269|PubMed:18243103, ECO:0000269|PubMed:19141279"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|Ref.12, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712"
FT MOD_RES 82
FT /note="O-AMP-tyrosine; by Legionella DrrA"
FT /evidence="ECO:0000269|PubMed:21822290"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35279"
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..33
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046967"
FT VAR_SEQ 62..165
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_045302"
FT VAR_SEQ 62..88
FT /note="VRLQLWDTAGQERFRSLIPSYIRDSTV -> IRLQLWDTAGQERFRSLIPSY
FT IRDSAA (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:11054569,
FT ECO:0000303|PubMed:11071909, ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.5,
FT ECO:0000303|Ref.8"
FT /id="VSP_005527"
FT MUTAGEN 27
FT /note="T->N: Loss of APBA1-binding. No loss of RIC1- and
FT RGP1-binding."
FT /evidence="ECO:0000269|PubMed:23091056,
FT ECO:0000269|PubMed:23737971"
FT MUTAGEN 46
FT /note="I->E: Loss of RAB6IP1-binding."
FT /evidence="ECO:0000269|PubMed:19141279"
FT MUTAGEN 72
FT /note="Q->L: Loss of GTPase activity. Interacts with
FT APBA1."
FT /evidence="ECO:0000269|PubMed:16332443,
FT ECO:0000269|PubMed:18243103, ECO:0000269|PubMed:19141279,
FT ECO:0000269|PubMed:23737971"
FT CONFLICT 189
FT /note="I -> T (in Ref. 7; BAH13508)"
FT /evidence="ECO:0000305"
FT STRAND 15..21
FT /evidence="ECO:0007829|PDB:1YZQ"
FT HELIX 26..35
FT /evidence="ECO:0007829|PDB:1YZQ"
FT STRAND 47..56
FT /evidence="ECO:0007829|PDB:1YZQ"
FT STRAND 61..69
FT /evidence="ECO:0007829|PDB:1YZQ"
FT HELIX 73..78
FT /evidence="ECO:0007829|PDB:1YZQ"
FT HELIX 79..83
FT /evidence="ECO:0007829|PDB:1YZQ"
FT STRAND 87..94
FT /evidence="ECO:0007829|PDB:1YZQ"
FT HELIX 98..102
FT /evidence="ECO:0007829|PDB:1YZQ"
FT HELIX 104..115
FT /evidence="ECO:0007829|PDB:1YZQ"
FT STRAND 118..126
FT /evidence="ECO:0007829|PDB:1YZQ"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:3BBP"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:1YZQ"
FT HELIX 138..147
FT /evidence="ECO:0007829|PDB:1YZQ"
FT STRAND 151..154
FT /evidence="ECO:0007829|PDB:1YZQ"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:1YZQ"
FT HELIX 163..173
FT /evidence="ECO:0007829|PDB:1YZQ"
SQ SEQUENCE 208 AA; 23593 MW; C9A3C2DDBF6C3E9E CRC64;
MSTGGDFGNP LRKFKLVFLG EQSVGKTSLI TRFMYDSFDN TYQATIGIDF LSKTMYLEDR
TVRLQLWDTA GQERFRSLIP SYIRDSTVAV VVYDITNVNS FQQTTKWIDD VRTERGSDVI
IMLVGNKTDL ADKRQVSIEE GERKAKELNV MFIETSAKAG YNVKQLFRRV AAALPGMEST
QDRSREDMID IKLEKPQEQP VSEGGCSC
