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P20340 (RAB6A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 169. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ras-related protein Rab-6A

Short name=Rab-6
Gene names
Name:RAB6A
Synonyms:RAB6
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length208 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Protein transport. Regulator of membrane traffic from the Golgi apparatus towards the endoplasmic reticulum (ER). Has a low GTPase activity.

Subunit structure

Interacts with CCDC64; leads to its accumulation in the pericentrosomal region By similarity. Interacts with SCYL1BP1. Interacts with VSP52 and RABGAP1. Interacts with GCC2 (via its GRIP domain). Interacts with RAB6IP1 (via its RUN 1 domain). Isoform 1 interacts with RAB6KIFL. Isoform 2 does not interact with RAB6KIFL. Isoform 1 interacts with BICD1. Isoform 2 interacts with BICD1. Isoform 1 interacts with BICD2. Isoform 2 interacts with BICD2. Interacts with TMF1. Isoform 1 (GTP-bound) interacts with DYNLRB1; the interaction is direct. Isoform 2 (GDP-bound) interacts with DYNLRB1; the interaction is direct. Interacts with PIFO. Interacts (GTP-bound) with APBA1/MINT1 isoform 2, also called Mint1_826, but not with isoform 1. Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.20 Ref.26 Ref.27 Ref.30

Subcellular location

Golgi apparatus membrane; Lipid-anchor.

Tissue specificity

Ubiquitous. Ref.4

Sequence similarities

Belongs to the small GTPase superfamily. Rab family.

Ontologies

Keywords
   Biological processER-Golgi transport
Protein transport
Transport
   Cellular componentGolgi apparatus
Membrane
   Coding sequence diversityAlternative splicing
   LigandGTP-binding
Nucleotide-binding
   PTMAcetylation
Lipoprotein
Methylation
Prenylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processGTP catabolic process

Inferred from direct assay Ref.28Ref.30. Source: GOC

antigen processing and presentation

Inferred from mutant phenotype PubMed 19717423. Source: UniProt

minus-end-directed organelle transport along microtubule

Traceable author statement Ref.14. Source: BHF-UCL

peptidyl-cysteine methylation

Inferred from direct assay PubMed 11121396. Source: MGI

protein localization to Golgi apparatus

Inferred from direct assay Ref.14. Source: BHF-UCL

protein targeting to Golgi

Inferred from direct assay Ref.30. Source: UniProtKB

retrograde vesicle-mediated transport, Golgi to ER

Traceable author statement Ref.14. Source: BHF-UCL

small GTPase mediated signal transduction

Inferred from electronic annotation. Source: InterPro

   Cellular_componentGolgi apparatus

Inferred from direct assay Ref.30Ref.31. Source: UniProtKB

Golgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasmic vesicle

Inferred from direct assay Ref.14. Source: BHF-UCL

cytosol

Inferred from direct assay Ref.14. Source: BHF-UCL

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337PubMed 23376485. Source: UniProt

membrane

Inferred from direct assay Ref.14. Source: BHF-UCL

trans-Golgi network

Inferred from direct assay Ref.14. Source: BHF-UCL

   Molecular_functionGTP binding

Inferred from direct assay Ref.28Ref.30Ref.31. Source: UniProtKB

GTPase activity

Inferred from direct assay Ref.28Ref.30. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.27. Source: IntAct

protein domain specific binding

Inferred from physical interaction Ref.14. Source: BHF-UCL

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P20340-1)

Also known as: Rab-6a;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P20340-2)

Also known as: Rab-6a'; Rab-6C; Rab6C;

The sequence of this isoform differs from the canonical sequence as follows:
     62-88: VRLQLWDTAGQERFRSLIPSYIRDSTV → IRLQLWDTAGQERFRSLIPSYIRDSAA
Isoform 3 (identifier: P20340-3)

The sequence of this isoform differs from the canonical sequence as follows:
     62-165: Missing.
Isoform 4 (identifier: P20340-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-33: Missing.
     62-88: VRLQLWDTAGQERFRSLIPSYIRDSTV → IRLQLWDTAGQERFRSLIPSYIRDSAA

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.12
Chain2 – 208207Ras-related protein Rab-6A
PRO_0000121112

Regions

Nucleotide binding20 – 289GTP
Nucleotide binding68 – 725GTP
Nucleotide binding126 – 1294GTP
Nucleotide binding156 – 1583GTP
Motif42 – 509Effector region By similarity

Amino acid modifications

Modified residue21N-acetylserine Ref.12 Ref.19 Ref.21 Ref.24 Ref.25
Modified residue821O-AMP-tyrosine; by Legionella DrrA
Modified residue2081Cysteine methyl ester By similarity
Lipidation2061S-geranylgeranyl cysteine By similarity
Lipidation2081S-geranylgeranyl cysteine By similarity

Natural variations

Alternative sequence1 – 3333Missing in isoform 4.
VSP_046967
Alternative sequence62 – 165104Missing in isoform 3.
VSP_045302
Alternative sequence62 – 8827VRLQL…RDSTV → IRLQLWDTAGQERFRSLIPS YIRDSAA in isoform 2 and isoform 4.
VSP_005527

Experimental info

Mutagenesis271T → N: Loss of APBA1-binding. Ref.27
Mutagenesis461I → E: Loss of RAB6IP1-binding. Ref.31
Mutagenesis721Q → L: Loss of GTPase activity. Interacts with APBA1. Ref.27 Ref.28 Ref.30 Ref.31
Sequence conflict1891I → T in BAH13508. Ref.7

Secondary structure

............................... 208
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Rab-6a) [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: C9A3C2DDBF6C3E9E

FASTA20823,593
        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 

« Hide

Isoform 2 (Rab-6a') (Rab-6C) (Rab6C) [UniParc].

Checksum: DF4B42559600F98B
Show »

FASTA20823,549
Isoform 3 [UniParc].

Checksum: 47907D182528BE16
Show »

FASTA10411,715
Isoform 4 [UniParc].

Checksum: 1667A3BFAE94F873
Show »

FASTA17519,935

References

« Hide 'large scale' references
[1]"The human Rab genes encode a family of GTP-binding proteins related to yeast YPT1 and SEC4 products involved in secretion."
Zahraoui A., Touchot N., Chardin P., Tavitian A.
J. Biol. Chem. 264:12394-12401(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Impairment of bile salt-dependent lipase secretion in human pancreatic tumoral SOJ-6 cells."
Caillol N., Pasqualini E., Lloubes R., Lombardo D.
J. Cell. Biochem. 79:628-647(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Pancreatic tumor.
[3]"Rab6c, a new member of the Rab gene family, is involved in drug resistance in MCF7/AdrR cells."
Shan J., Mason J.M., Yuan L., Barcia M., Porti D., Calabro A., Budman D., Vinciguerra V., Xu H.-P.
Gene 257:67-75(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[4]"Alternative splicing of the human Rab6A gene generates two close but functionally different isoforms."
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.
Mol. Biol. Cell 11:3819-3833(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, CHARACTERIZATION.
[5]"A second form of RAB6 in humans."
Barr F.A.
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[6]Delisle B.P., Foell J.D., Slind J.K., Kilby J.A., Balijepalli R.C., Kamp T.J., January C.T.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Tissue: Heart.
[7]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).
Tissue: Brain, Spleen and Thalamus.
[8]"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
Puhl H.L. III, Ikeda S.R., Aronstam R.S.
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Brain.
[9]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
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.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[10]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Kidney, Placenta and Testis.
[12]Bienvenut W.V., Claeys D.
Submitted (NOV-2005) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-13; 64-74; 77-84 AND 116-143, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Platelet.
[13]"Characterization of GAPCenA, a GTPase activating protein for Rab6, part of which associates with the centrosome."
Cuif M.-H., Possmayer F., Zander H., Bordes N., Jollivet F., Couedel-Courteille A., Janoueix-Lerosey I., Langsley G., Bornens M., Goud B.
EMBO J. 18:1772-1782(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RABGAP1.
[14]"Bicaudal-D regulates COPI-independent Golgi-ER transport by recruiting the dynein-dynactin motor complex."
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.
Nat. Cell Biol. 4:986-992(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BICD1 AND BICD2.
[15]"Characterization of the human GARP (Golgi associated retrograde protein) complex."
Liewen H., Meinhold-Heerlein I., Oliveira V., Schwarzenbacher R., Luo G., Wadle A., Jung M., Pfreundschuh M., Stenner-Liewen F.
Exp. Cell Res. 306:24-34(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH VSP52.
[16]"Functional involvement of TMF/ARA160 in Rab6-dependent retrograde membrane traffic."
Yamane J., Kubo A., Nakayama K., Yuba-Kubo A., Katsuno T., Tsukita S., Tsukita S.
Exp. Cell Res. 313:3472-3485(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TMF1.
[17]"Rab6 family proteins interact with the dynein light chain protein DYNLRB1."
Wanschers B.F.J., van de Vorstenbosch R., Wijers M., Wieringa B., King S.M., Fransen J.
Cell Motil. Cytoskeleton 65:183-196(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DYNLRB1.
[18]"Gerodermia osteodysplastica is caused by mutations in SCYL1BP1, a Rab-6 interacting golgin."
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. expand/collapse author list , Metcalfe K., Clayton-Smith J., Tassabehji M., Steinmann B., Barr F.A., Nuernberg P., Wieacker P., Mundlos S.
Nat. Genet. 40:1410-1412(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SCYL1BP1.
[19]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"Pitchfork regulates primary cilia disassembly and left-right asymmetry."
Kinzel D., Boldt K., Davis E.E., Burtscher I., Trumbach D., Diplas B., Attie-Bitach T., Wurst W., Katsanis N., Ueffing M., Lickert H.
Dev. Cell 19:66-77(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PIFO.
[21]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[22]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"Modulation of Rab GTPase function by a protein phosphocholine transferase."
Mukherjee S., Liu X., Arasaki K., McDonough J., Galan J.E., Roy C.R.
Nature 477:103-106(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: AMPYLATION AT TYR-82.
[24]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[26]"Molecular defects in the motor adaptor BICD2 cause proximal spinal muscular atrophy with autosomal-dominant inheritance."
Peeters K., Litvinenko I., Asselbergh B., Almeida-Souza L., Chamova T., Geuens T., Ydens E., Zimon M., Irobi J., De Vriendt E., De Winter V., Ooms T., Timmerman V., Tournev I., Jordanova A.
Am. J. Hum. Genet. 92:955-964(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BICD2.
[27]"A new Mint1 isoform, but not the conventional Mint1, interacts with the small GTPase Rab6."
Thyrock A., Ossendorf E., Stehling M., Kail M., Kurtz T., Pohlentz G., Waschbusch D., Eggert S., Formstecher E., Muthing J., Dreisewerd K., Kins S., Goud B., Barnekow A.
PLoS ONE 8:E64149-E64149(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH APBA1, MUTAGENESIS OF THR-27 AND GLN-72.
[28]"Structure of the extremely slow GTPase Rab6A in the GTP bound form at 1.8A resolution."
Bergbrede T., Pylypenko O., Rak A., Alexandrov K.
J. Struct. Biol. 152:235-238(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 13-174 IN COMPLEX WITH GTP, MUTAGENESIS OF GLN-72.
[29]"Structural basis of family-wide Rab GTPase recognition by rabenosyn-5."
Eathiraj S., Pan X., Ritacco C., Lambright D.G.
Nature 436:415-419(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) OF 10-177 IN COMPLEX WITH GTP ANALOG.
[30]"Rab and Arl GTPase family members cooperate in the localization of the golgin GCC185."
Burguete A.S., Fenn T.D., Brunger A.T., Pfeffer S.R.
Cell 132:286-298(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-206 IN COMPLEX WITH GTP, INTERACTION WITH GCC2, MUTAGENESIS OF GLN-72.
[31]"Structural basis for recruitment of Rab6-interacting protein 1 to Golgi via a RUN domain."
Recacha R., Boulet A., Jollivet F., Monier S., Houdusse A., Goud B., Khan A.R.
Structure 17:21-30(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 8-195 IN COMPLEX WITH GTP AND RAB6IP1, MUTAGENESIS OF ILE-46 AND GLN-72.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M28212 mRNA. Translation: AAA60246.1.
AF130986 mRNA. Translation: AAD25535.1.
AF119836 mRNA. Translation: AAF23593.1.
AF198616 mRNA. Translation: AAF73841.1.
AF130122 mRNA. Translation: AAD27707.1.
DQ437503 mRNA. Translation: ABD93919.1.
AK057157 mRNA. Translation: BAB71371.1.
AK289748 mRNA. Translation: BAF82437.1.
AK290132 mRNA. Translation: BAF82821.1.
AK301534 mRNA. Translation: BAH13508.1.
AF498939 mRNA. Translation: AAM21087.1.
AF498941 mRNA. Translation: AAM21089.1.
BT019698 mRNA. Translation: AAV38504.1.
AP002770 Genomic DNA. No translation available.
AP002993 Genomic DNA. No translation available.
BC003617 mRNA. Translation: AAH03617.1.
BC068486 mRNA. Translation: AAH68486.1.
BC096818 mRNA. Translation: AAH96818.1.
CCDSCCDS58155.1. [P20340-4]
CCDS58156.1. [P20340-3]
CCDS8223.1. [P20340-2]
CCDS8224.1. [P20340-1]
PIRG34323.
RefSeqNP_001230647.1. NM_001243718.1. [P20340-3]
NP_001230648.1. NM_001243719.1. [P20340-4]
NP_002860.2. NM_002869.4. [P20340-2]
NP_942599.1. NM_198896.1. [P20340-1]
UniGeneHs.503222.
Hs.591552.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1YZQX-ray1.78A10-177[»]
2GILX-ray1.82A/B/C/D13-174[»]
3BBPX-ray3.00A/B/C1-206[»]
3CWZX-ray3.20A8-195[»]
4DKXX-ray1.90A/B1-208[»]
ProteinModelPortalP20340.
SMRP20340. Positions 13-174.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111808. 22 interactions.
DIPDIP-39668N.
IntActP20340. 11 interactions.
MINTMINT-1482056.
STRING9606.ENSP00000311449.

PTM databases

PhosphoSiteP20340.

Polymorphism databases

DMDM131796.

Proteomic databases

MaxQBP20340.
PaxDbP20340.
PRIDEP20340.

Protocols and materials databases

DNASU5870.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000310653; ENSP00000311449; ENSG00000175582. [P20340-2]
ENST00000336083; ENSP00000336850; ENSG00000175582. [P20340-1]
ENST00000536566; ENSP00000437863; ENSG00000175582. [P20340-4]
ENST00000541588; ENSP00000445350; ENSG00000175582. [P20340-3]
GeneID5870.
KEGGhsa:5870.
UCSCuc001oue.3. human. [P20340-2]
uc001ouf.3. human. [P20340-1]
uc009yts.3. human.

Organism-specific databases

CTD5870.
GeneCardsGC11M073386.
HGNCHGNC:9786. RAB6A.
HPACAB009936.
HPA059131.
MIM179513. gene.
neXtProtNX_P20340.
PharmGKBPA34146.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1100.
HOGENOMHOG000233968.
HOVERGENHBG009351.
InParanoidP20340.
KOK07893.
OMASACAANC.
OrthoDBEOG77DJ7M.
PhylomeDBP20340.
TreeFamTF300803.

Gene expression databases

ArrayExpressP20340.
BgeeP20340.
CleanExHS_RAB6A.
GenevestigatorP20340.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
PfamPF00071. Ras. 1 hit.
[Graphical view]
PRINTSPR00449. RASTRNSFRMNG.
SMARTSM00175. RAB. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51419. RAB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRAB6A. human.
EvolutionaryTraceP20340.
GeneWikiRAB6A.
GenomeRNAi5870.
NextBio22798.
PROP20340.
SOURCESearch...

Entry information

Entry nameRAB6A_HUMAN
AccessionPrimary (citable) accession number: P20340
Secondary accession number(s): A8K133 expand/collapse secondary AC list , B7Z772, F5H668, Q1W5D8, Q5U0A8, Q9UBE4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 169 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM