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Protein

Ras-related protein Rab-6A

Gene

Rab6a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Protein transport. Regulator of membrane traffic from the Golgi apparatus towards the endoplasmic reticulum (ER) (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi20 – 289GTPBy similarity
Nucleotide bindingi68 – 725GTPBy similarity
Nucleotide bindingi126 – 1294GTPBy similarity
Nucleotide bindingi156 – 1583GTPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

ER-Golgi transport, Protein transport, Transport

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-6811436. COPI-independent Golgi-to-ER retrograde traffic.
R-MMU-6811440. Retrograde transport at the Trans-Golgi-Network.

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related protein Rab-6A
Short name:
Rab-6
Gene namesi
Name:Rab6a
Synonyms:Rab6
ORF Names:MNCb-1660
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:894313. Rab6a.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi22 – 221Q → V: Loss of binding to rabkinesin-6. 1 Publication
Mutagenesisi27 – 271T → N: Loss of binding to rabkinesin-6; when associated with L-73. 1 Publication
Mutagenesisi46 – 461I → E: Loss of binding to rabkinesin-6. 1 Publication
Mutagenesisi72 – 721Q → L: Loss of binding to rabkinesin-6; when associated with N-28. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 208207Ras-related protein Rab-6APRO_0000121113Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei184 – 1841PhosphoserineCombined sources
Lipidationi206 – 2061S-geranylgeranyl cysteineBy similarity
Modified residuei208 – 2081Cysteine methyl esterBy similarity
Lipidationi208 – 2081S-geranylgeranyl cysteineBy similarity

Keywords - PTMi

Acetylation, Lipoprotein, Methylation, Phosphoprotein, Prenylation

Proteomic databases

EPDiP35279.
PaxDbiP35279.
PeptideAtlasiP35279.
PRIDEiP35279.
TopDownProteomicsiP35279-1. [P35279-1]

PTM databases

iPTMnetiP35279.
PhosphoSiteiP35279.

Expressioni

Gene expression databases

BgeeiP35279.
CleanExiMM_RAB6.
ExpressionAtlasiP35279. baseline and differential.
GenevisibleiP35279. MM.

Interactioni

Subunit structurei

Interacts with RIC1 and RGP1; the interactions are direct with a preference for RAB6A-GDP. Interacts with VSP52 and RABGAP1. Interacts with GCC2 (via its GRIP domain). Interacts with RAB6IP1 (via its RUN 1 domain). Interacts with RAB6KIFL. Interacts with BICD1. Interacts with BICD2. Interacts with TMF1. 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. Interacts (GTP-bound) with APBA1/MINT1 isoform 3, also called Mint1_826.By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Bicd2Q921C53EBI-444674,EBI-642984
Ccdc64A0JNT96EBI-444674,EBI-7893170
SYTL5Q8TDW52EBI-444674,EBI-2939487From a different organism.

GO - Molecular functioni

Protein-protein interaction databases

BioGridi202550. 3 interactions.
DIPiDIP-120N.
IntActiP35279. 26 interactions.
MINTiMINT-1865398.
STRINGi10090.ENSMUSP00000032946.

Structurei

3D structure databases

ProteinModelPortaliP35279.
SMRiP35279. Positions 13-174.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi42 – 509Effector regionBy similarity

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rab family.Curated

Phylogenomic databases

eggNOGiKOG0094. Eukaryota.
ENOG410XPBI. LUCA.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiP35279.
KOiK07893.
OMAiMQESGCW.
PhylomeDBiP35279.
TreeFamiTF300803.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51419. RAB. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P35279-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MSAGGDFGNP LRKFKLVFLG EQSVGKTSLI TRFMYDSFDN TYQATIGIDF
60 70 80 90 100
LSKTMYLEDR TVRLQLWDTA GQERFRSLIP SYIRDSTVAV VVYDITNVNS
110 120 130 140 150
FQQTTKWIDD VRTERGSDVI IMLVGNKTDL ADKRQVSIEE GERKAKELNV
160 170 180 190 200
MFIETSAKAG YNVKQLFRRV AAALPGMEST QDRSREDMID IKLEKPQEQP

VNEGGCSC
Length:208
Mass (Da):23,590
Last modified:January 23, 2007 - v4
Checksum:iDD08CC2914668FD4
GO
Isoform 2 (identifier: P35279-2) [UniParc]FASTAAdd to basket

Also known as: Rab-6a', Rab6C

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

Show »
Length:208
Mass (Da):23,546
Checksum:iCBE04CA13D0A48C1
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei62 – 8827VRLQL…RDSTV → IRLQLWDTAGQERFRSLIPS YIRDSAA in isoform 2. 2 PublicationsVSP_005528Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS21503.1. [P35279-1]
CCDS52323.1. [P35279-2]
PIRiA38883.
RefSeqiNP_001157135.1. NM_001163663.1. [P35279-2]
NP_077249.1. NM_024287.4. [P35279-1]
UniGeneiMm.28650.

Genome annotation databases

EnsembliENSMUST00000032946; ENSMUSP00000032946; ENSMUSG00000030704. [P35279-1]
ENSMUST00000098252; ENSMUSP00000095852; ENSMUSG00000030704. [P35279-2]
GeneIDi19346.
KEGGimmu:19346.
UCSCiuc009ini.2. mouse. [P35279-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS21503.1. [P35279-1]
CCDS52323.1. [P35279-2]
PIRiA38883.
RefSeqiNP_001157135.1. NM_001163663.1. [P35279-2]
NP_077249.1. NM_024287.4. [P35279-1]
UniGeneiMm.28650.

3D structure databases

ProteinModelPortaliP35279.
SMRiP35279. Positions 13-174.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202550. 3 interactions.
DIPiDIP-120N.
IntActiP35279. 26 interactions.
MINTiMINT-1865398.
STRINGi10090.ENSMUSP00000032946.

PTM databases

iPTMnetiP35279.
PhosphoSiteiP35279.

Proteomic databases

EPDiP35279.
PaxDbiP35279.
PeptideAtlasiP35279.
PRIDEiP35279.
TopDownProteomicsiP35279-1. [P35279-1]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000032946; ENSMUSP00000032946; ENSMUSG00000030704. [P35279-1]
ENSMUST00000098252; ENSMUSP00000095852; ENSMUSG00000030704. [P35279-2]
GeneIDi19346.
KEGGimmu:19346.
UCSCiuc009ini.2. mouse. [P35279-1]

Organism-specific databases

CTDi5870.
MGIiMGI:894313. Rab6a.

Phylogenomic databases

eggNOGiKOG0094. Eukaryota.
ENOG410XPBI. LUCA.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiP35279.
KOiK07893.
OMAiMQESGCW.
PhylomeDBiP35279.
TreeFamiTF300803.

Enzyme and pathway databases

ReactomeiR-MMU-6811436. COPI-independent Golgi-to-ER retrograde traffic.
R-MMU-6811440. Retrograde transport at the Trans-Golgi-Network.

Miscellaneous databases

PROiP35279.
SOURCEiSearch...

Gene expression databases

BgeeiP35279.
CleanExiMM_RAB6.
ExpressionAtlasiP35279. baseline and differential.
GenevisibleiP35279. MM.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51419. RAB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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/6J.
    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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J.
    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] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.
  7. Cited for: INTERACTION WITH SCYL1BP1.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  9. 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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CCDC64.
  11. Cited for: INTERACTION WITH APBA1.

Entry informationi

Entry nameiRAB6A_MOUSE
AccessioniPrimary (citable) accession number: P35279
Secondary accession number(s): Q542M6
, Q8R2Z7, Q8VEE5, Q9JJD4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 159 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.