Full text data of RAB6A
RAB6A
(RAB6)
[Confidence: low (only semi-automatic identification from reviews)]
Ras-related protein Rab-6A; Rab-6
Ras-related protein Rab-6A; Rab-6
UniProt
P20340
ID RAB6A_HUMAN Reviewed; 208 AA.
AC P20340; A8K133; B7Z772; F5H668; Q1W5D8; Q5U0A8; Q9UBE4;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 163.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2501306;
RA Zahraoui A., Touchot N., Chardin P., Tavitian A.;
RT "The human Rab genes encode a family of GTP-binding proteins related
RT to 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
RT pancreatic 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.,
RA Budman D., Vinciguerra V., Xu H.-P.;
RT "Rab6c, a new member of the Rab gene family, is involved in drug
RT resistance in MCF7/AdrR cells.";
RL Gene 257:67-75(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND
RP CHARACTERIZATION.
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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
RT sequenced by 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
RT 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.,
RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA 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
RT project: 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
RP INITIATOR METHIONINE, ACETYLATION AT SER-2, AND 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,
RT part of 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.,
RA Stepanova T., Galjart N., Grosveld F., Goud B., De Zeeuw C.I.,
RA Barnekow A., Hoogenraad C.C.;
RT "Bicaudal-D regulates COPI-independent Golgi-ER transport by
RT recruiting the 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.,
RA Luo G., Wadle A., Jung M., Pfreundschuh M., Stenner-Liewen F.;
RT "Characterization of the human GARP (Golgi associated retrograde
RT protein) 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
RT membrane 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.,
RA Mueller D., Kaplan P.B., Rajab A., Zampino G., Fodale V.,
RA Dallapiccola B., Newman W., Metcalfe K., Clayton-Smith J.,
RA Tassabehji M., Steinmann B., Barr F.A., Nuernberg P., Wieacker P.,
RA Mundlos S.;
RT "Gerodermia osteodysplastica is caused by mutations in SCYL1BP1, a
RT Rab-6 interacting golgin.";
RL Nat. Genet. 40:1410-1412(2008).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a 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
RT asymmetry.";
RL Dev. Cell 19:66-77(2010).
RN [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [22]
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.,
RA Buerckstuemmer T., 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 [23]
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 [24]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [25]
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.,
RA Chamova T., Geuens T., Ydens E., Zimon M., Irobi J., De Vriendt E.,
RA De Winter V., 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 [26]
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
RT the small GTPase Rab6.";
RL PLoS ONE 8:E64149-E64149(2013).
RN [27]
RP X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 13-174 IN COMPLEX WITH GTP,
RP AND 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
RT 1.8A resolution.";
RL J. Struct. Biol. 152:235-238(2005).
RN [28]
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-
RT 5.";
RL Nature 436:415-419(2005).
RN [29]
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
RT the golgin GCC185.";
RL Cell 132:286-298(2008).
RN [30]
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
RT Golgi via a RUN domain.";
RL Structure 17:21-30(2009).
CC -!- FUNCTION: Protein transport. Regulator of membrane traffic from
CC the Golgi apparatus towards the endoplasmic reticulum (ER). Has a
CC low GTPase activity.
CC -!- SUBUNIT: Interacts with CCDC64; 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
CC GRIP domain). Interacts with RAB6IP1 (via its RUN 1 domain).
CC Isoform 1 interacts with RAB6KIFL. Isoform 2 does not interact
CC with RAB6KIFL. Isoform 1 interacts with BICD1. Isoform 2 interacts
CC with BICD1. Isoform 1 interacts with BICD2. Isoform 2 interacts
CC with BICD2. Interacts with TMF1. Isoform 1 (GTP-bound) interacts
CC with DYNLRB1; the interaction is direct. Isoform 2 (GDP-bound)
CC interacts with DYNLRB1; the interaction is direct. Interacts with
CC PIFO. Interacts (GTP-bound) with APBA1/MINT1 isoform 2, also
CC called Mint1_826, but not with isoform 1.
CC -!- INTERACTION:
CC Q8IWJ2:GCC2; NbExp=4; IntAct=EBI-1052826, EBI-1645320;
CC Q01968:OCRL; NbExp=11; IntAct=EBI-1052826, EBI-6148898;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Lipid-anchor.
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.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
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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 PIR; G34323; G34323.
DR RefSeq; NP_001230647.1; NM_001243718.1.
DR RefSeq; NP_001230648.1; NM_001243719.1.
DR RefSeq; NP_002860.2; NM_002869.4.
DR RefSeq; NP_942599.1; NM_198896.1.
DR UniGene; Hs.503222; -.
DR UniGene; Hs.591552; -.
DR PDB; 1YZQ; X-ray; 1.78 A; A=10-177.
DR PDB; 2GIL; X-ray; 1.82 A; A/B/C/D=13-173.
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 PDBsum; 1YZQ; -.
DR PDBsum; 2GIL; -.
DR PDBsum; 3BBP; -.
DR PDBsum; 3CWZ; -.
DR PDBsum; 4DKX; -.
DR ProteinModelPortal; P20340; -.
DR SMR; P20340; 13-174.
DR DIP; DIP-39668N; -.
DR IntAct; P20340; 9.
DR MINT; MINT-1482056; -.
DR STRING; 9606.ENSP00000311449; -.
DR PhosphoSite; P20340; -.
DR DMDM; 131796; -.
DR PaxDb; P20340; -.
DR PRIDE; P20340; -.
DR DNASU; 5870; -.
DR Ensembl; ENST00000310653; ENSP00000311449; ENSG00000175582.
DR Ensembl; ENST00000336083; ENSP00000336850; ENSG00000175582.
DR Ensembl; ENST00000536566; ENSP00000437863; ENSG00000175582.
DR Ensembl; ENST00000541588; ENSP00000445350; ENSG00000175582.
DR GeneID; 5870; -.
DR KEGG; hsa:5870; -.
DR UCSC; uc021qnd.1; human.
DR CTD; 5870; -.
DR GeneCards; GC11M073386; -.
DR HGNC; HGNC:9786; RAB6A.
DR HPA; CAB009936; -.
DR MIM; 179513; gene.
DR neXtProt; NX_P20340; -.
DR PharmGKB; PA34146; -.
DR eggNOG; COG1100; -.
DR HOGENOM; HOG000233968; -.
DR HOVERGEN; HBG009351; -.
DR InParanoid; P20340; -.
DR KO; K07893; -.
DR OMA; STSKWID; -.
DR OrthoDB; EOG77DJ7M; -.
DR PhylomeDB; P20340; -.
DR ChiTaRS; RAB6A; human.
DR EvolutionaryTrace; P20340; -.
DR GeneWiki; RAB6A; -.
DR GenomeRNAi; 5870; -.
DR NextBio; 22798; -.
DR PRO; PR:P20340; -.
DR ArrayExpress; P20340; -.
DR Bgee; P20340; -.
DR CleanEx; HS_RAB6A; -.
DR Genevestigator; P20340; -.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:BHF-UCL.
DR GO; GO:0005802; C:trans-Golgi network; IDA:BHF-UCL.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0072385; P:minus-end-directed organelle transport along microtubule; TAS:BHF-UCL.
DR GO; GO:0018125; P:peptidyl-cysteine methylation; IDA:MGI.
DR GO; GO:0000042; P:protein targeting to Golgi; IDA:UniProtKB.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; TAS:BHF-UCL.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR003579; Small_GTPase_Rab_type.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SMART; SM00175; RAB; 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; Complete proteome;
KW Direct protein sequencing; ER-Golgi transport; Golgi apparatus;
KW GTP-binding; Lipoprotein; Membrane; Methylation; Nucleotide-binding;
KW Prenylation; Protein transport; Reference proteome; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 208 Ras-related protein Rab-6A.
FT /FTId=PRO_0000121112.
FT NP_BIND 20 28 GTP.
FT NP_BIND 68 72 GTP.
FT NP_BIND 126 129 GTP.
FT NP_BIND 156 158 GTP.
FT MOTIF 42 50 Effector region (By similarity).
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 82 82 O-AMP-tyrosine; by Legionella DrrA.
FT MOD_RES 208 208 Cysteine methyl ester (By similarity).
FT LIPID 206 206 S-geranylgeranyl cysteine (By
FT similarity).
FT LIPID 208 208 S-geranylgeranyl cysteine (By
FT similarity).
FT VAR_SEQ 1 33 Missing (in isoform 4).
FT /FTId=VSP_046967.
FT VAR_SEQ 62 165 Missing (in isoform 3).
FT /FTId=VSP_045302.
FT VAR_SEQ 62 88 VRLQLWDTAGQERFRSLIPSYIRDSTV -> IRLQLWDTAG
FT QERFRSLIPSYIRDSAA (in isoform 2 and
FT isoform 4).
FT /FTId=VSP_005527.
FT MUTAGEN 27 27 T->N: Loss of APBA1-binding.
FT MUTAGEN 46 46 I->E: Loss of RAB6IP1-binding.
FT MUTAGEN 72 72 Q->L: Loss of GTPase activity. Interacts
FT with APBA1.
FT CONFLICT 189 189 I -> T (in Ref. 7; BAH13508).
FT STRAND 15 21
FT HELIX 26 35
FT STRAND 47 56
FT STRAND 61 69
FT HELIX 73 78
FT HELIX 79 83
FT STRAND 87 94
FT HELIX 98 102
FT HELIX 104 115
FT STRAND 118 126
FT HELIX 128 130
FT HELIX 131 133
FT HELIX 138 147
FT STRAND 151 154
FT TURN 157 159
FT HELIX 163 173
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
//
ID RAB6A_HUMAN Reviewed; 208 AA.
AC P20340; A8K133; B7Z772; F5H668; Q1W5D8; Q5U0A8; Q9UBE4;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 163.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2501306;
RA Zahraoui A., Touchot N., Chardin P., Tavitian A.;
RT "The human Rab genes encode a family of GTP-binding proteins related
RT to 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
RT pancreatic 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.,
RA Budman D., Vinciguerra V., Xu H.-P.;
RT "Rab6c, a new member of the Rab gene family, is involved in drug
RT resistance in MCF7/AdrR cells.";
RL Gene 257:67-75(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND
RP CHARACTERIZATION.
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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
RT sequenced by 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
RT 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.,
RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA 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
RT project: 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
RP INITIATOR METHIONINE, ACETYLATION AT SER-2, AND 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,
RT part of 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.,
RA Stepanova T., Galjart N., Grosveld F., Goud B., De Zeeuw C.I.,
RA Barnekow A., Hoogenraad C.C.;
RT "Bicaudal-D regulates COPI-independent Golgi-ER transport by
RT recruiting the 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.,
RA Luo G., Wadle A., Jung M., Pfreundschuh M., Stenner-Liewen F.;
RT "Characterization of the human GARP (Golgi associated retrograde
RT protein) 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
RT membrane 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.,
RA Mueller D., Kaplan P.B., Rajab A., Zampino G., Fodale V.,
RA Dallapiccola B., Newman W., Metcalfe K., Clayton-Smith J.,
RA Tassabehji M., Steinmann B., Barr F.A., Nuernberg P., Wieacker P.,
RA Mundlos S.;
RT "Gerodermia osteodysplastica is caused by mutations in SCYL1BP1, a
RT Rab-6 interacting golgin.";
RL Nat. Genet. 40:1410-1412(2008).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a 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
RT asymmetry.";
RL Dev. Cell 19:66-77(2010).
RN [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [22]
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.,
RA Buerckstuemmer T., 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 [23]
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 [24]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [25]
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.,
RA Chamova T., Geuens T., Ydens E., Zimon M., Irobi J., De Vriendt E.,
RA De Winter V., 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 [26]
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
RT the small GTPase Rab6.";
RL PLoS ONE 8:E64149-E64149(2013).
RN [27]
RP X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 13-174 IN COMPLEX WITH GTP,
RP AND 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
RT 1.8A resolution.";
RL J. Struct. Biol. 152:235-238(2005).
RN [28]
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-
RT 5.";
RL Nature 436:415-419(2005).
RN [29]
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
RT the golgin GCC185.";
RL Cell 132:286-298(2008).
RN [30]
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
RT Golgi via a RUN domain.";
RL Structure 17:21-30(2009).
CC -!- FUNCTION: Protein transport. Regulator of membrane traffic from
CC the Golgi apparatus towards the endoplasmic reticulum (ER). Has a
CC low GTPase activity.
CC -!- SUBUNIT: Interacts with CCDC64; 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
CC GRIP domain). Interacts with RAB6IP1 (via its RUN 1 domain).
CC Isoform 1 interacts with RAB6KIFL. Isoform 2 does not interact
CC with RAB6KIFL. Isoform 1 interacts with BICD1. Isoform 2 interacts
CC with BICD1. Isoform 1 interacts with BICD2. Isoform 2 interacts
CC with BICD2. Interacts with TMF1. Isoform 1 (GTP-bound) interacts
CC with DYNLRB1; the interaction is direct. Isoform 2 (GDP-bound)
CC interacts with DYNLRB1; the interaction is direct. Interacts with
CC PIFO. Interacts (GTP-bound) with APBA1/MINT1 isoform 2, also
CC called Mint1_826, but not with isoform 1.
CC -!- INTERACTION:
CC Q8IWJ2:GCC2; NbExp=4; IntAct=EBI-1052826, EBI-1645320;
CC Q01968:OCRL; NbExp=11; IntAct=EBI-1052826, EBI-6148898;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Lipid-anchor.
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.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
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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 PIR; G34323; G34323.
DR RefSeq; NP_001230647.1; NM_001243718.1.
DR RefSeq; NP_001230648.1; NM_001243719.1.
DR RefSeq; NP_002860.2; NM_002869.4.
DR RefSeq; NP_942599.1; NM_198896.1.
DR UniGene; Hs.503222; -.
DR UniGene; Hs.591552; -.
DR PDB; 1YZQ; X-ray; 1.78 A; A=10-177.
DR PDB; 2GIL; X-ray; 1.82 A; A/B/C/D=13-173.
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 PDBsum; 1YZQ; -.
DR PDBsum; 2GIL; -.
DR PDBsum; 3BBP; -.
DR PDBsum; 3CWZ; -.
DR PDBsum; 4DKX; -.
DR ProteinModelPortal; P20340; -.
DR SMR; P20340; 13-174.
DR DIP; DIP-39668N; -.
DR IntAct; P20340; 9.
DR MINT; MINT-1482056; -.
DR STRING; 9606.ENSP00000311449; -.
DR PhosphoSite; P20340; -.
DR DMDM; 131796; -.
DR PaxDb; P20340; -.
DR PRIDE; P20340; -.
DR DNASU; 5870; -.
DR Ensembl; ENST00000310653; ENSP00000311449; ENSG00000175582.
DR Ensembl; ENST00000336083; ENSP00000336850; ENSG00000175582.
DR Ensembl; ENST00000536566; ENSP00000437863; ENSG00000175582.
DR Ensembl; ENST00000541588; ENSP00000445350; ENSG00000175582.
DR GeneID; 5870; -.
DR KEGG; hsa:5870; -.
DR UCSC; uc021qnd.1; human.
DR CTD; 5870; -.
DR GeneCards; GC11M073386; -.
DR HGNC; HGNC:9786; RAB6A.
DR HPA; CAB009936; -.
DR MIM; 179513; gene.
DR neXtProt; NX_P20340; -.
DR PharmGKB; PA34146; -.
DR eggNOG; COG1100; -.
DR HOGENOM; HOG000233968; -.
DR HOVERGEN; HBG009351; -.
DR InParanoid; P20340; -.
DR KO; K07893; -.
DR OMA; STSKWID; -.
DR OrthoDB; EOG77DJ7M; -.
DR PhylomeDB; P20340; -.
DR ChiTaRS; RAB6A; human.
DR EvolutionaryTrace; P20340; -.
DR GeneWiki; RAB6A; -.
DR GenomeRNAi; 5870; -.
DR NextBio; 22798; -.
DR PRO; PR:P20340; -.
DR ArrayExpress; P20340; -.
DR Bgee; P20340; -.
DR CleanEx; HS_RAB6A; -.
DR Genevestigator; P20340; -.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:BHF-UCL.
DR GO; GO:0005802; C:trans-Golgi network; IDA:BHF-UCL.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0072385; P:minus-end-directed organelle transport along microtubule; TAS:BHF-UCL.
DR GO; GO:0018125; P:peptidyl-cysteine methylation; IDA:MGI.
DR GO; GO:0000042; P:protein targeting to Golgi; IDA:UniProtKB.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; TAS:BHF-UCL.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR003579; Small_GTPase_Rab_type.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SMART; SM00175; RAB; 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; Complete proteome;
KW Direct protein sequencing; ER-Golgi transport; Golgi apparatus;
KW GTP-binding; Lipoprotein; Membrane; Methylation; Nucleotide-binding;
KW Prenylation; Protein transport; Reference proteome; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 208 Ras-related protein Rab-6A.
FT /FTId=PRO_0000121112.
FT NP_BIND 20 28 GTP.
FT NP_BIND 68 72 GTP.
FT NP_BIND 126 129 GTP.
FT NP_BIND 156 158 GTP.
FT MOTIF 42 50 Effector region (By similarity).
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 82 82 O-AMP-tyrosine; by Legionella DrrA.
FT MOD_RES 208 208 Cysteine methyl ester (By similarity).
FT LIPID 206 206 S-geranylgeranyl cysteine (By
FT similarity).
FT LIPID 208 208 S-geranylgeranyl cysteine (By
FT similarity).
FT VAR_SEQ 1 33 Missing (in isoform 4).
FT /FTId=VSP_046967.
FT VAR_SEQ 62 165 Missing (in isoform 3).
FT /FTId=VSP_045302.
FT VAR_SEQ 62 88 VRLQLWDTAGQERFRSLIPSYIRDSTV -> IRLQLWDTAG
FT QERFRSLIPSYIRDSAA (in isoform 2 and
FT isoform 4).
FT /FTId=VSP_005527.
FT MUTAGEN 27 27 T->N: Loss of APBA1-binding.
FT MUTAGEN 46 46 I->E: Loss of RAB6IP1-binding.
FT MUTAGEN 72 72 Q->L: Loss of GTPase activity. Interacts
FT with APBA1.
FT CONFLICT 189 189 I -> T (in Ref. 7; BAH13508).
FT STRAND 15 21
FT HELIX 26 35
FT STRAND 47 56
FT STRAND 61 69
FT HELIX 73 78
FT HELIX 79 83
FT STRAND 87 94
FT HELIX 98 102
FT HELIX 104 115
FT STRAND 118 126
FT HELIX 128 130
FT HELIX 131 133
FT HELIX 138 147
FT STRAND 151 154
FT TURN 157 159
FT HELIX 163 173
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
//
MIM
179513
*RECORD*
*FIELD* NO
179513
*FIELD* TI
*179513 RAS-ASSOCIATED PROTEIN RAB6A; RAB6A
;;RAS-ASSOCIATED PROTEIN RAB6; RAB6
*FIELD* TX
read more
CLONING
The mammalian RAB proteins show striking similarities to the S.
cerevisiae YPT1 and SEC4 proteins, Ras-related GTP-binding proteins
involved in the regulation of secretion. Zahraoui et al. (1989) isolated
cDNAs encoding RAB6 and several other human RAB proteins. The predicted
human RAB6 protein contains 208 amino acids. Northern blot analysis
revealed that the RAB6 gene was expressed as a 3.6-kb mRNA in a human
fibroblast cell line.
By screening a human kidney cDNA library with a DNA fragment of RAB6C
(612909), Shan et al. (2000) isolated a RAB6A variant that they called
RAB6C. The deduced 208-amino acid protein encoded by this variant
differs at only 3 amino acids compared with the previously reported
RAB6A isoform.
GENE FUNCTION
Using quantitative RT-PCR, Shan et al. (2000) showed that a RAB6A
variant that they called RAB6C was downregulated in a
multidrug-resistant clone of MCF7 breast cancer cells compared with the
parental MCF7 cell line. Reexpression of the RAB6A variant in the
resistant cell line restored sensitivity to several anticancer drugs.
Flow cytometry experiments showed that sensitivity to doxorubicin was
associated with increased drug accumulation in cells expressing the
RAB6A variant.
Using a large-scale small interfering RNA screen to identify host
factors required by human immunodeficiency virus (HIV)-1 (see 609423),
Brass et al. (2008) identified more than 250 HIV-dependency factors
(HDFs), 79 of which showed significantly higher expression in immune
tissues compared with other tissues. The HDFs RAB6 and VPS53, retrograde
Golgi transport proteins, were involved in viral entry. Brass et al.
(2008) proposed that targeting of HDFs essential for the viral cycle but
not critical for the host may avoid drug resistance due to viral
diversity and escape mutation.
MAPPING
By in situ hybridization, Rousseau-Merck et al. (1991) assigned the RAB6
gene to chromosome 2q14-q21.
*FIELD* RF
1. Brass, A. L.; Dykxhoorn, D. M.; Benita, Y.; Yan, N.; Engelman,
A.; Xavier, R. J.; Lieberman, J.; Elledge, S. J.: Identification
of host proteins required for HIV infection through a functional genomic
screen. Science 319: 921-926, 2008.
2. Rousseau-Merck, M.-F.; Zahraoui, A.; Touchot, N.; Tavitian, A.;
Berger, R.: Chromosome assignment of four RAS-related RAB genes. Hum.
Genet. 86: 350-354, 1991.
3. Shan, J.; Mason, J. M.; Yuan, L.; Barcia, M.; Porti, D.; Calabro,
A.; Budman, D.; Vinciguerra, V.; Xu, H.: Rab6c, a new member of the
Rab gene family, is involved in drug resistance in MCF7/AdrR cells. Gene 257:
67-75, 2000.
4. Shan, J.; Mason, J. M.; Yuan, L.; Barcia, M.; Porti, D.; Calabro,
A.; Budman, D.; Vinciguerra, V.; Xu, H.: Rab6c, a new member of the
Rab gene family, is involved in drug resistance in MCF7/AdrR cells. Gene 257:
67-75, 2000.
5. Zahraoui, A.; Touchot, N.; Chardin, P.; Tavitian, A.: The human
rab genes encode a family of GTP-binding proteins related to yeast
YPT1 and SEC4 products involved in secretion. J. Biol. Chem. 264:
12394-12401, 1989.
*FIELD* CN
Patricia A. Hartz - updated: 7/10/2009
Paul J. Converse - updated: 2/29/2008
Rebekah S. Rasooly - updated: 3/8/1999
*FIELD* CD
Victor A. McKusick: 7/9/1990
*FIELD* ED
mgross: 07/13/2009
terry: 7/10/2009
mgross: 2/29/2008
carol: 4/3/2001
mgross: 3/10/1999
mgross: 3/9/1999
mgross: 3/8/1999
supermim: 3/16/1992
carol: 3/22/1991
carol: 9/9/1990
carol: 7/9/1990
*RECORD*
*FIELD* NO
179513
*FIELD* TI
*179513 RAS-ASSOCIATED PROTEIN RAB6A; RAB6A
;;RAS-ASSOCIATED PROTEIN RAB6; RAB6
*FIELD* TX
read more
CLONING
The mammalian RAB proteins show striking similarities to the S.
cerevisiae YPT1 and SEC4 proteins, Ras-related GTP-binding proteins
involved in the regulation of secretion. Zahraoui et al. (1989) isolated
cDNAs encoding RAB6 and several other human RAB proteins. The predicted
human RAB6 protein contains 208 amino acids. Northern blot analysis
revealed that the RAB6 gene was expressed as a 3.6-kb mRNA in a human
fibroblast cell line.
By screening a human kidney cDNA library with a DNA fragment of RAB6C
(612909), Shan et al. (2000) isolated a RAB6A variant that they called
RAB6C. The deduced 208-amino acid protein encoded by this variant
differs at only 3 amino acids compared with the previously reported
RAB6A isoform.
GENE FUNCTION
Using quantitative RT-PCR, Shan et al. (2000) showed that a RAB6A
variant that they called RAB6C was downregulated in a
multidrug-resistant clone of MCF7 breast cancer cells compared with the
parental MCF7 cell line. Reexpression of the RAB6A variant in the
resistant cell line restored sensitivity to several anticancer drugs.
Flow cytometry experiments showed that sensitivity to doxorubicin was
associated with increased drug accumulation in cells expressing the
RAB6A variant.
Using a large-scale small interfering RNA screen to identify host
factors required by human immunodeficiency virus (HIV)-1 (see 609423),
Brass et al. (2008) identified more than 250 HIV-dependency factors
(HDFs), 79 of which showed significantly higher expression in immune
tissues compared with other tissues. The HDFs RAB6 and VPS53, retrograde
Golgi transport proteins, were involved in viral entry. Brass et al.
(2008) proposed that targeting of HDFs essential for the viral cycle but
not critical for the host may avoid drug resistance due to viral
diversity and escape mutation.
MAPPING
By in situ hybridization, Rousseau-Merck et al. (1991) assigned the RAB6
gene to chromosome 2q14-q21.
*FIELD* RF
1. Brass, A. L.; Dykxhoorn, D. M.; Benita, Y.; Yan, N.; Engelman,
A.; Xavier, R. J.; Lieberman, J.; Elledge, S. J.: Identification
of host proteins required for HIV infection through a functional genomic
screen. Science 319: 921-926, 2008.
2. Rousseau-Merck, M.-F.; Zahraoui, A.; Touchot, N.; Tavitian, A.;
Berger, R.: Chromosome assignment of four RAS-related RAB genes. Hum.
Genet. 86: 350-354, 1991.
3. Shan, J.; Mason, J. M.; Yuan, L.; Barcia, M.; Porti, D.; Calabro,
A.; Budman, D.; Vinciguerra, V.; Xu, H.: Rab6c, a new member of the
Rab gene family, is involved in drug resistance in MCF7/AdrR cells. Gene 257:
67-75, 2000.
4. Shan, J.; Mason, J. M.; Yuan, L.; Barcia, M.; Porti, D.; Calabro,
A.; Budman, D.; Vinciguerra, V.; Xu, H.: Rab6c, a new member of the
Rab gene family, is involved in drug resistance in MCF7/AdrR cells. Gene 257:
67-75, 2000.
5. Zahraoui, A.; Touchot, N.; Chardin, P.; Tavitian, A.: The human
rab genes encode a family of GTP-binding proteins related to yeast
YPT1 and SEC4 products involved in secretion. J. Biol. Chem. 264:
12394-12401, 1989.
*FIELD* CN
Patricia A. Hartz - updated: 7/10/2009
Paul J. Converse - updated: 2/29/2008
Rebekah S. Rasooly - updated: 3/8/1999
*FIELD* CD
Victor A. McKusick: 7/9/1990
*FIELD* ED
mgross: 07/13/2009
terry: 7/10/2009
mgross: 2/29/2008
carol: 4/3/2001
mgross: 3/10/1999
mgross: 3/9/1999
mgross: 3/8/1999
supermim: 3/16/1992
carol: 3/22/1991
carol: 9/9/1990
carol: 7/9/1990