P20340 (RAB6A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ras-related protein Rab-6A
Short name=Rab-6

Gene names

Name:	RAB6A
Synonyms:	RAB6

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	208 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.25
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 process	ER-Golgi transport Protein transport Transport
Cellular component	Golgi apparatus Membrane
Coding sequence diversity	Alternative splicing
Ligand	GTP-binding Nucleotide-binding
PTM	Acetylation Lipoprotein Methylation Phosphoprotein Prenylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	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 targeting to Golgi Inferred from direct assay Ref.25. 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_component	Golgi apparatus Inferred from direct assay Ref.25Ref.26. 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 membrane Inferred from direct assay Ref.14. Source: BHF-UCL trans-Golgi network Inferred from direct assay Ref.14. Source: BHF-UCL
Molecular_function	GTP binding Inferred from direct assay Ref.23Ref.25Ref.26. Source: UniProtKB GTPase activity Inferred from direct assay Ref.23Ref.25. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GCC2	Q8IWJ2	4	EBI-1052826,EBI-1645320

Alternative products

This entry describes 3 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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.12

Chain

2 – 208

207

Ras-related protein Rab-6A

PRO_0000121112

Regions

Nucleotide binding

20 – 28

9

GTP

Nucleotide binding

68 – 72

5

GTP

Nucleotide binding

126 – 129

4

GTP

Nucleotide binding

156 – 158

3

GTP

Motif

42 – 50

9

Effector region By similarity

Amino acid modifications

Modified residue

2

1

N-acetylserine Ref.12 Ref.20

Modified residue

82

1

O-AMP-tyrosine; by Legionella DrrA

Modified residue

180

1

Phosphothreonine By similarity

Modified residue

208

1

Cysteine methyl ester By similarity

Lipidation

206

1

S-geranylgeranyl cysteine By similarity

Lipidation

208

1

S-geranylgeranyl cysteine By similarity

Natural variations

Alternative sequence

62 – 165

104

Missing in isoform 3.

VSP_045302

Alternative sequence

62 – 88

27

VRLQL…RDSTV → IRLQLWDTAGQERFRSLIPS YIRDSAA in isoform 2.

VSP_005527

Experimental info

Mutagenesis

46

1

I → E: Abolishes the interaction with RAB6IP1. Ref.26

Mutagenesis

72

1

Q → L: Loss of GTPase activity. Ref.23 Ref.25 Ref.26

Secondary structure

1

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208

Helix Strand Turn

Details...

Beta strand

15 – 21

7

Helix

26 – 35

10

Beta strand

47 – 56

10

Beta strand

61 – 69

9

Helix

73 – 78

6

Helix

79 – 83

5

Beta strand

87 – 94

8

Helix

98 – 102

5

Helix

104 – 115

12

Beta strand

118 – 126

9

Helix

128 – 130

3

Helix

131 – 133

3

Helix

138 – 147

10

Beta strand

151 – 154

4

Turn

157 – 159

3

Helix

163 – 173

11

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Rab-6a) [UniParc]. Last modified January 23, 2007. Version 3. Checksum: C9A3C2DDBF6C3E9E	FASTA	208	23,593
	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
	Isoform 2 (Rab-6a') (Rab-6C) (Rab6C) [UniParc]. Checksum: DF4B42559600F98B	FASTA	208	23,549
	10 20 30 40 50 60 MSTGGDFGNP LRKFKLVFLG EQSVGKTSLI TRFMYDSFDN TYQATIGIDF LSKTMYLEDR 70 80 90 100 110 120 TIRLQLWDTA GQERFRSLIP SYIRDSAAAV VVYDITNVNS FQQTTKWIDD VRTERGSDVI 130 140 150 160 170 180 IMLVGNKTDL ADKRQVSIEE GERKAKELNV MFIETSAKAG YNVKQLFRRV AAALPGMEST 190 200 QDRSREDMID IKLEKPQEQP VSEGGCSC
	Isoform 3 [UniParc]. Checksum: 47907D182528BE16	FASTA	104	11,715
	10 20 30 40 50 60 MSTGGDFGNP LRKFKLVFLG EQSVGKTSLI TRFMYDSFDN TYQATIGIDF LSKTMYLEDR 70 80 90 100 TLFRRVAAAL PGMESTQDRS REDMIDIKLE KPQEQPVSEG GCSC

References

	« Hide 'large scale' referencesShow '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. , 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 AND 2). 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. , 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, 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. , 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]	"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.
[20]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[21]	"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].
[22]	"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.
[23]	"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.
[24]	"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.
[25]	"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.
[26]	"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.
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.

IPI

IPI00023526.
IPI00217943.

PIR

G34323.

RefSeq

NP_001230647.1. NM_001243718.1.
NP_002860.2. NM_002869.4.
NP_942599.1. NM_198896.1.

UniGene

Hs.503222.
Hs.535586.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1YZQ	X-ray	1.78	A	10-177	[»]
2GIL	X-ray	1.82	A/B/C/D	13-173	[»]
3BBP	X-ray	3.00	A/B/C	1-206	[»]
3CWZ	X-ray	3.20	A	8-195	[»]
4DKX	X-ray	1.90	A/B	1-208	[»]

ProteinModelPortal

P20340.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-39668N.

IntAct

P20340. 4 interactions.

MINT

MINT-1482056.

STRING

9606.ENSP00000311449.

PTM databases

PhosphoSite

P20340.

Polymorphism databases

DMDM

131796.

Proteomic databases

PaxDb

P20340.

PRIDE

P20340.

Protocols and materials databases

DNASU

5870.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000310653; ENSP00000311449; ENSG00000175582.
ENST00000336083; ENSP00000336850; ENSG00000175582.
ENST00000393571; ENSP00000377201; ENSG00000175582.
ENST00000541588; ENSP00000445350; ENSG00000175582.

GeneID

5870.

KEGG

hsa:5870.

UCSC

uc001oue.3. human.
uc001ouf.3. human.
uc009yts.3. human.

Organism-specific databases

CTD

5870.

GeneCards

GC11M073386.

HGNC

HGNC:9786. RAB6A.

HPA

CAB009936.

MIM

179513. gene.

neXtProt

NX_P20340.

PharmGKB

PA34146.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1100.

HOGENOM

HOG000233968.

HOVERGEN

HBG009351.

InParanoid

P20340.

KO

K07893.

OMA

FKWIDEV.

PhylomeDB

P20340.

Gene expression databases

ArrayExpress

P20340.

Bgee

P20340.

CleanEx

HS_RAB6A.

Genevestigator

P20340.

GermOnline

ENSG00000175582. Homo sapiens.

Family and domain databases

InterPro

IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]

Pfam

PF00071. Ras. 1 hit.
[Graphical view]

PRINTS

PR00449. RASTRNSFRMNG.

SMART

SM00175. RAB. 1 hit.
[Graphical view]

SUPFAM

SSF52540. SSF52540. 1 hit.

TIGRFAMs

TIGR00231. small_GTP. 1 hit.

PROSITE

PS51419. RAB. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

RAB6A. human.

EvolutionaryTrace

P20340.

GenomeRNAi

5870.

NextBio

22798.

SOURCE

Search...

Entry information

Entry name

RAB6A_HUMAN

Accession

Primary (citable) accession number: P20340
Secondary accession number(s): A8K133 , Q1W5D8, Q5U0A8, Q9UBE4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 157 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.