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UniProtKB/Swiss-Prot entry P20340


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name RAB6A_HUMAN
Primary accession number P20340
Secondary accession numbers A8K133 Q5U0A8 Q9UBE4
Integrated into Swiss-Prot on February 1, 1991
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    June 16, 2009 (Entry version 112)
Name and origin of the protein
Protein name Ras-related protein Rab-6A
Synonym Rab-6
Gene name
Name: RAB6A
Synonyms: RAB6
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=2501306 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Pancreatic tumor;
DOI=10.1002/1097-4644(20001215)79:4<628::AID-JCB120>3.0.CO;2-T; PubMed=10996854 [NCBI, ExPASy, EBI, Israel, Japan]
Caillol N., Pasqualini E., Lloubes R., Lombardo D.;
"Impairment of bile salt-dependent lipase secretion in human pancreatic tumoral SOJ-6 cells.";
J. Cell. Biochem. 79:628-647(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
DOI=10.1016/S0378-1119(00)00395-4; PubMed=11054569 [NCBI, ExPASy, EBI, Israel, Japan]
Shan J., Mason J.M., Yuan L., Barcia M., Porti D., Calabro A., Budman D., Vinciguerra V., Xu H.-P.;
"Rab6c, a new member of the Rab gene family, is involved in drug resistance in MCF7/AdrR cells.";
Gene 257:67-75(2000).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Barr F.A.;
"A second form of RAB6 in humans.";
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND CHARACTERIZATION.
PubMed=11071909 [NCBI, ExPASy, EBI, Israel, Japan]
Echard A., Opdam F.J.M., de Leeuw H.J.P.C., Jollivet F., Savelkoul P., Hendriks W., Voorberg J., Goud B., Fransen J.A.M.;
"Alternative splicing of the human Rab6A gene generates two close but functionally different isoforms.";
Mol. Biol. Cell 11:3819-3833(2000).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain, Spleen, and Thalamus;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain;
Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org).";
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Kidney, Placenta, and Testis;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
PROTEIN SEQUENCE OF 2-13; 64-74; 77-84 AND 116-143, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, AND MASS SPECTROMETRY.
TISSUE=Platelet;
Bienvenut W.V., Claeys D.;
Submitted (NOV-2005) to UniProtKB.
[11]
INTERACTION WITH RABGAP1.
DOI=10.1093/emboj/18.7.1772; PubMed=10202141 [NCBI, ExPASy, EBI, Israel, Japan]
Cuif M.-H., Possmayer F., Zander H., Bordes N., Jollivet F., Couedel-Courteille A., Janoueix-Lerosey I., Langsley G., Bornens M., Goud B.;
"Characterization of GAPCenA, a GTPase activating protein for Rab6, part of which associates with the centrosome.";
EMBO J. 18:1772-1782(1999).
[12]
INTERACTION WITH BICD1 AND BICD2.
DOI=10.1038/ncb891; PubMed=12447383 [NCBI, ExPASy, EBI, Israel, Japan]
Matanis T., Akhmanova A., Wulf P., Del Nery E., Weide T., Stepanova T., Galjart N., Grosveld F., Goud B., De Zeeuw C.I., Barnekow A., Hoogenraad C.C.;
"Bicaudal-D regulates COPI-independent Golgi-ER transport by recruiting the dynein-dynactin motor complex.";
Nat. Cell Biol. 4:986-992(2002).
[13]
INTERACTION WITH VSP52.
DOI=10.1016/j.yexcr.2005.01.022; PubMed=15878329 [NCBI, ExPASy, EBI, Israel, Japan]
Liewen H., Meinhold-Heerlein I., Oliveira V., Schwarzenbacher R., Luo G., Wadle A., Jung M., Pfreundschuh M., Stenner-Liewen F.;
"Characterization of the human GARP (Golgi associated retrograde protein) complex.";
Exp. Cell Res. 306:24-34(2005).
[14]
INTERACTION WITH TMF1.
DOI=10.1016/j.yexcr.2007.07.010; PubMed=17698061 [NCBI, ExPASy, EBI, Israel, Japan]
Yamane J., Kubo A., Nakayama K., Yuba-Kubo A., Katsuno T., Tsukita S., Tsukita S.;
"Functional involvement of TMF/ARA160 in Rab6-dependent retrograde membrane traffic.";
Exp. Cell Res. 313:3472-3485(2007).
[15]
INTERACTION WITH SCYL1BP1.
DOI=10.1038/ng.252; PubMed=18997784 [NCBI, ExPASy, EBI, Israel, Japan]
Hennies H.C., Kornak U., Zhang H., Egerer J., Zhang X., Seifert W., Kuhnisch J., Budde B., Naetebus M., Brancati F., Wilcox W.R., Mueller D., Kaplan P.B., Rajab A., Zampino G., Fodale V., Dallapiccola B., Newman W., Metcalfe K., Clayton-Smith J., Tassabehji M., Steinmann B., Barr F.A., Nuernberg P., Wieacker P., Mundlos S.;
"Gerodermia osteodysplastica is caused by mutations in SCYL1BP1, a Rab-6 interacting golgin.";
Nat. Genet. 40:1410-1412(2008).
[16]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M28212; AAA60246.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF130986; AAD25535.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF119836; AAF23593.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF130122; AAD27707.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF198616; AAF73841.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK057157; BAB71371.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK289748; BAF82437.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK290132; BAF82821.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF498939; AAM21087.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF498941; AAM21089.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT019698; AAV38504.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC003617; AAH03617.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC068486; AAH68486.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC096818; AAH96818.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00023526; -.
IPI00217943; -.
PIR G34323; G34323.
RefSeq NP_002860.2; -.
NP_942599.1; -.
UniGene Hs.503222
3D structure databases
PDB
1YZQ; X-ray; 1.78 A; A=10-177.[ExPASy / RCSB / EBI]
2GIL; X-ray; 1.82 A; A/B/C/D=13-173.[ExPASy / RCSB / EBI]
3BBP; X-ray; 3.00 A; A/B/C=1-206.[ExPASy / RCSB / EBI]
3CWZ; X-ray; 3.20 A; A=8-195.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1YZQ; -.
2GIL; -.
3BBP; -.
3CWZ; -.
ModBase P20340.
Protein-protein interaction databases
IntAct P20340; 5.
PTM databases
PhosphoSite P20340; -.
2D gel databases
Aarhus/Ghent-2DPAGE 3135; IEF.
3136; IEF.
Organism-specific databases
GeneCards GC11M073064; -.
H-InvDB HIX0009921; -.
HGNC HGNC:9786; RAB6A.
GenAtlas RAB6A.
HPA CAB009936; -.
MIM 179513; gene. [NCBI / EBI]
PharmGKB PA34146; -.
Gene expression databases
ArrayExpress P20340; -.
Bgee P20340; -.
CleanEx HS_RAB6A; -.
GermOnline ENSG00000175582; Homo sapiens.
Ontologies
GO
GO:0000139; Cellular component: Golgi membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005525; Molecular function: GTP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0003924; Molecular function: GTPase activity (traceable author statement from ProtInc).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0018125; Biological process: peptidyl-cysteine methylation (inferred from direct assay from MGI).
GO:0015031; Biological process: protein transport (inferred from electronic annotation from UniProtKB-KW).
GO:0007264; Biological process: small GTPase mediated signal transduction (inferred from electronic annotation from InterPro).
GO:0016192; Biological process: vesicle-mediated transport (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR003579; GTPase_Rab.
IPR015600; Rab6-like.
IPR013753; Ras.
IPR001806; Ras_GTPase.
IPR005225; Small_GTP_bd.
Graphical view of domain structure.
PANTHER PTHR11708:SF256; Rab6_like; 1.
Pfam PF00071; Ras; 1.
Pfam graphical view of domain structure.
PRINTS PR00449; RASTRNSFRMNG.
SMART SM00175; RAB; 1.
SMART graphical view of domain structure.
TIGRFAMs TIGR00231; small_GTP; 1.
PROSITE PS51419; RAB; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE P20340; -.
Genome annotation databases
Ensembl ENSG00000175582; Homo sapiens. [Contig view]
GeneID 5870; -.
KEGG hsa:5870; -.
Phylogenomic databases
HOGENOM P20340; -.
HOVERGEN P20340; -.
OMA P20340; FKWIDEV.
Other
NextBio 22798; -.
SOURCE RAB6A; Homo sapiens.
ProtoNet P20340.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Alternative splicing; Direct protein sequencing; ER-Golgi transport; Golgi apparatus; GTP-binding; Lipoprotein; Membrane; Methylation; Nucleotide-binding; Phosphoprotein; Prenylation; Protein transport; Transport.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   208  207     Ras-related protein Rab-6A. PRO_0000121112
NP_BIND   20    27  8     GTP (By similarity). 
NP_BIND   68    72  5     GTP (By similarity). 
NP_BIND   126   129  4     GTP (By similarity). 
MOTIF   42    50  9     Effector region (By similarity). 
MOD_RES   2     2        N-acetylserine. 
MOD_RES   180   180        Phosphothreonine (By similarity). 
MOD_RES   208   208        Cysteine methyl ester (By similarity). 
LIPID   206   206        S-geranylgeranyl cysteine (By similarity). 
LIPID   208   208        S-geranylgeranyl cysteine (By similarity). 
VAR_SEQ   62    88        VRLQLWDTAGQERFRSLIPSYIRDSTV -> IRLQLWDTAGQERFRSLIPSYIRDSAA (in isoform 2). VSP_005527
STRAND   15    21  7      
HELIX   26    35  10      
STRAND   47    56  10      
STRAND   61    69  9      
HELIX   73    78  6      
HELIX   79    83  5      
STRAND   87    94  8      
HELIX   98   102  5      
HELIX   104   115  12      
STRAND   118   126  9      
HELIX   131   133  3      
HELIX   138   147  10      
STRAND   151   154  4      
TURN   157   159  3      
HELIX   163   173  11      
Sequence information
Length: 208 AA [This is the length of the unprocessed precursor] Molecular weight: 23593 Da [This is the MW of the unprocessed precursor] CRC64: C9A3C2DDBF6C3E9E [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSTGGDFGNP LRKFKLVFLG EQSVGKTSLI TRFMYDSFDN TYQATIGIDF LSKTMYLEDR 

        70         80         90        100        110        120 
TVRLQLWDTA GQERFRSLIP SYIRDSTVAV VVYDITNVNS FQQTTKWIDD VRTERGSDVI 

       130        140        150        160        170        180 
IMLVGNKTDL ADKRQVSIEE GERKAKELNV MFIETSAKAG YNVKQLFRRV AAALPGMEST 

       190        200 
QDRSREDMID IKLEKPQEQP VSEGGCSC 

P20340 in FASTA format

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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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