P35279 (RAB6A_MOUSE) 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
ORF Names:	MNCb-1660

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

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) By similarity.
Subunit structure	Interacts with VSP52 and RABGAP1 By similarity. Interacts with GCC2 (via its GRIP domain) By similarity. Interacts with RAB6IP1 (via its RUN 1 domain) By similarity. Interacts with RAB6KIFL By similarity. Interacts with BICD1 By similarity. Interacts with BICD2 By similarity. Interacts with TMF1 By similarity. Interacts (GTP-bound) with DYNLRB1; the interaction is direct By similarity. Interacts with SCYL1BP1. Interacts with CCDC64; leads to its accumulation in the pericentrosomal region. Interacts with PIFO. Ref.8 Ref.9 Ref.10
Subcellular location	Golgi apparatus membrane; Lipid-anchor.
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.7
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	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	protein targeting to Golgi Inferred from sequence or structural similarity. Source: UniProtKB small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro
Cellular component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	GTP binding Inferred from sequence or structural similarity. Source: UniProtKB GTPase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SYTL5	Q8TDW5	2	EBI-444674,EBI-2939487	From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P35279-1)

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: P35279-2)

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

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

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 208	207	Ras-related protein Rab-6A		PRO_0000121113
Regions
	Nucleotide binding	20 – 28	9	GTP By similarity
	Nucleotide binding	68 – 72	5	GTP By similarity
	Nucleotide binding	126 – 129	4	GTP By similarity
	Nucleotide binding	156 – 158	3	GTP By similarity
	Motif	42 – 50	9	Effector region By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylserine By similarity
	Modified residue	180	1	Phosphothreonine Ref.7
	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 – 88	27	VRLQL…RDSTV → IRLQLWDTAGQERFRSLIPS YIRDSAA in isoform 2.		VSP_005528
Experimental info
	Mutagenesis	22	1	Q → V: Loss of binding to rabkinesin-6.
	Mutagenesis	27	1	T → N: Loss of binding to rabkinesin-6; when associated with L-73.
	Mutagenesis	46	1	I → E: Loss of binding to rabkinesin-6.
	Mutagenesis	72	1	Q → L: Loss of binding to rabkinesin-6; when associated with N-28.

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Rab-6a) [UniParc]. Last modified January 23, 2007. Version 4. Checksum: DD08CC2914668FD4	FASTA	208	23,590
	10 20 30 40 50 60 MSAGGDFGNP 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 VNEGGCSC
	Isoform 2 (Rab-6a') (Rab6C) [UniParc]. Checksum: CBE04CA13D0A48C1	FASTA	208	23,546
	10 20 30 40 50 60 MSAGGDFGNP 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 VNEGGCSC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation of full-length cDNA clones from mouse brain cDNA library made by oligo-capping method." Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K. Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: C57BL/6. Tissue: Brain.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: C57BL/6J and NOD. Tissue: Hippocampus and Spinal ganglion.
[3]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
[4]	"The complexity of the Rab and Rho GTP-binding protein subfamilies revealed by a PCR cloning approach." Chavrier P., Simons K., Zerial M. Gene 112:261-264(1992) [PubMed: 1555775] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-73 (ISOFORM 2). Tissue: Kidney.
[5]	Lubec G., Kang S.U. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 64-74 AND 144-158, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain.
[6]	"Interaction of a Golgi-associated kinesin-like protein with Rab6." Echard A., Jollivet F., Martinez O., Lacapere J.-J., Rousselet A., Janoueix-Lerosey I., Goud B. Science 279:580-585(1998) [PubMed: 9438855] [Abstract] Cited for: MUTAGENESIS.
[7]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-180, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[8]	"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: 18997784] [Abstract] Cited for: INTERACTION WITH SCYL1BP1.
[9]	"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: 20643351] [Abstract] Cited for: INTERACTION WITH PIFO.
[10]	"Pericentrosomal targeting of Rab6 secretory vesicles by Bicaudal-D-related protein 1 (BICDR-1) regulates neuritogenesis." Schlager M.A., Kapitein L.C., Grigoriev I., Burzynski G.M., Wulf P.S., Keijzer N., de Graaff E., Fukuda M., Shepherd I.T., Akhmanova A., Hoogenraad C.C. EMBO J. 29:1637-1651(2010) [PubMed: 20360680] [Abstract] Cited for: INTERACTION WITH CCDC64.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB041575 mRNA. Translation: BAA95059.1. AK051246 mRNA. Translation: BAC34572.1. AK083262 mRNA. Translation: BAC38834.1. AK084131 mRNA. Translation: BAC39121.1. AK160134 mRNA. Translation: BAE35649.1. AK160866 mRNA. Translation: BAE36058.1. AK169842 mRNA. Translation: BAE41406.1. BC019118 mRNA. Translation: AAH19118.1. BC026915 mRNA. Translation: AAH26915.1. M79313 mRNA. Translation: AAK14837.1.
IPI	IPI00116697. IPI00230011.
PIR	A38883.
RefSeq	NP_001157135.1. NM_001163663.1. NP_077249.1. NM_024287.4.
UniGene	Mm.28650.
3D structure databases
ProteinModelPortal	P35279.
SMR	P35279. Positions 13-174.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-120N.
IntAct	P35279. 3 interactions.
STRING	P35279.
PTM databases
PhosphoSite	P35279.
Proteomic databases
PRIDE	P35279.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000032946; ENSMUSP00000032946; ENSMUSG00000030704. ENSMUST00000098252; ENSMUSP00000095852; ENSMUSG00000030704.
GeneID	19346.
KEGG	mmu:19346.
Organism-specific databases
CTD	5870.
MGI	MGI:894313. Rab6a.
Phylogenomic databases
eggNOG	roNOG11398.
HOVERGEN	HBG009351.
OMA	FKWIDEV.
OrthoDB	EOG4NP74D.
PhylomeDB	P35279.
Gene expression databases
ArrayExpress	P35279.
Bgee	P35279.
CleanEx	MM_RAB6.
Genevestigator	P35279.
GermOnline	ENSMUSG00000030704. Mus musculus.
Family and domain databases
InterPro	IPR005225. Small_GTP-bd_dom. IPR001806. Small_GTPase. IPR003579. Small_GTPase_Rab_type. [Graphical view]
KO	K07893.
Pfam	PF00071. Ras. 1 hit. [Graphical view]
PRINTS	PR00449. RASTRNSFRMNG.
SMART	SM00175. RAB. 1 hit. [Graphical view]
TIGRFAMs	TIGR00231. Small_GTP. 1 hit.
PROSITE	PS51419. RAB. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	296365.
SOURCE	Search...

Entry information

Entry name

RAB6A_MOUSE

Accession

Primary (citable) accession number: P35279
Secondary accession number(s): Q542M6 , Q8R2Z7, Q8VEE5, Q9JJD4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 120 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program