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P61026 (RAB10_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ras-related protein Rab-10
Gene names
Name:RAB10
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length200 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion By similarity. That Rab is mainly involved in the biosynthetic transport of proteins from the Golgi to the plasma membrane. Regulates, for instance, SLC2A4/GLUT4 glucose transporter-enriched vesicles delivery to the plasma membrane. In parallel, it regulates the transport of TLR4, a toll-like receptor to the plasma membrane and therefore may be important for innate immune response. Plays also a specific role in asymmetric protein transport to the plasma membrane within the polarized neuron and epithelial cells. In neurons, it is involved in axonogenesis through regulation of vesicular membrane trafficking toward the axonal plasma membrane while in epithelial cells, it regulates transport from the Golgi to the basolateral membrane. Moreover, may play a role in the basolateral recycling pathway and in phagosome maturation. According to Ref.18, may play a role in endoplasmic reticulum dynamics and morphology controlling tubulation along microtubules and tubules fusion. Ref.10 Ref.16 Ref.18

Enzyme regulation

Rab activation is generally mediated by a guanine exchange factor (GEF), while inactivation through hydrolysis of bound GTP is catalyzed by a GTPase activating protein (GAP) By similarity. That Rab is activated by the DENND4C guanine exchange factor (GEF). Ref.14

Subunit structure

Interacts with MYO5A; mediates the transport to the plasma membrane of SLC2A4/GLUT4 storage vesicles. Interacts with GDI1 and maybe with GDI2; negatively regulates RAB10 association with membranes and activation. Interacts (GDP-bound form) with LLGL1; the interaction is direct and promotes RAB10 association with membranes and activation through competition with the Rab inhibitor GDI1 By similarity. Interacts with EXOC4; probably associates with the exocyst By similarity. Ref.11 Ref.17

Subcellular location

Cytoplasmic vesicle membrane; Lipid-anchor Probable; Cytoplasmic side Probable. Golgi apparatustrans-Golgi network membrane By similarity. Endosome membrane. Recycling endosome membrane. Cytoplasmic vesiclephagosome membrane By similarity. Cell projectioncilium. Endoplasmic reticulum membrane. Note: Associates with SLC2A4/GLUT4 storage vesicles. Localizes to the base of the cilium. Transiently associates with phagosomes By similarity. According to Ref.18 localizes to the endoplasmic reticulum at domains of new tubule growth. Ref.10 Ref.13 Ref.17 Ref.18

Sequence similarities

Belongs to the small GTPase superfamily. Rab family.

Ontologies

Keywords
   Biological processProtein transport
Transport
   Cellular componentCell projection
Cytoplasmic vesicle
Endoplasmic reticulum
Endosome
Golgi apparatus
Membrane
   LigandGTP-binding
Nucleotide-binding
   PTMAcetylation
Lipoprotein
Prenylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGTP catabolic process

Inferred from experiment. Source: GOC

Golgi to plasma membrane protein transport

Inferred from sequence or structural similarity. Source: UniProtKB

Golgi to plasma membrane transport

Inferred from sequence or structural similarity. Source: UniProtKB

antigen processing and presentation

Inferred from mutant phenotype PubMed 19717423. Source: UniProt

axonogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

basolateral protein localization

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to insulin stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

endoplasmic reticulum tubular network organization

Inferred from mutant phenotype Ref.18. Source: UniProtKB

endosomal transport

Inferred from mutant phenotype Ref.10. Source: UniProtKB

establishment of neuroblast polarity

Inferred from sequence or structural similarity. Source: UniProtKB

establishment of protein localization to endoplasmic reticulum membrane

Inferred from mutant phenotype Ref.18. Source: UniProtKB

membrane organization

Traceable author statement. Source: Reactome

polarized epithelial cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

protein localization to plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

small GTPase mediated signal transduction

Inferred from electronic annotation. Source: InterPro

vesicle-mediated transport

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from direct assay Ref.18. Source: UniProtKB

cytoplasmic vesicle membrane

Traceable author statement. Source: Reactome

endoplasmic reticulum membrane

Inferred from direct assay Ref.18. Source: UniProtKB

endoplasmic reticulum tubular network

Inferred from direct assay Ref.18. Source: UniProtKB

endosome

Inferred from direct assay Ref.13. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 20458337. Source: UniProt

insulin-responsive compartment

Inferred from direct assay Ref.17. Source: UniProtKB

phagocytic vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

primary cilium

Inferred from direct assay Ref.13. Source: UniProtKB

recycling endosome

Inferred from direct assay Ref.10. Source: UniProtKB

recycling endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

trans-Golgi network

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionGDP binding

Inferred from direct assay Ref.14. Source: UniProtKB

GTP binding

Inferred from direct assay Ref.14. Source: UniProtKB

GTPase activity

Inferred from experiment. Source: Reactome

myosin V binding

Inferred from physical interaction Ref.17. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 200200Ras-related protein Rab-10
PRO_0000121146

Regions

Nucleotide binding16 – 238GTP By similarity
Nucleotide binding64 – 685GTP By similarity
Nucleotide binding122 – 1254GTP By similarity
Motif38 – 469Effector region By similarity

Amino acid modifications

Modified residue1021N6-acetyllysine Ref.12
Lipidation1991S-geranylgeranyl cysteine By similarity
Lipidation2001S-geranylgeranyl cysteine By similarity

Experimental info

Mutagenesis231T → N: Probable dominant negative mutant locked in the inactive GDP-bound form; alters the basolateral recycling pathway in epithelial cells and endoplasmic reticulum membrane morphology. Ref.13 Ref.18
Mutagenesis681Q → L: Probable constitutively active mutant unable to hydrolyze GTP; accumulates at the base of the primary cilium and alters the basolateral recycling pathway in epithelial cells. Ref.13
Sequence conflict1381E → G in CAB66585. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P61026 [UniParc].

Last modified April 26, 2004. Version 1.
Checksum: 7F02B8E8E46EE1E8

FASTA20022,541
        10         20         30         40         50         60 
MAKKTYDLLF KLLLIGDSGV GKTCVLFRFS DDAFNTTFIS TIGIDFKIKT VELQGKKIKL 

        70         80         90        100        110        120 
QIWDTAGQER FHTITTSYYR GAMGIMLVYD ITNGKSFENI SKWLRNIDEH ANEDVERMLL 

       130        140        150        160        170        180 
GNKCDMDDKR VVPKGKGEQI AREHGIRFFE TSAKANINIE KAFLTLAEDI LRKTPVKEPN 

       190        200 
SENVDISSGG GVTGWKSKCC 

« Hide

References

« Hide 'large scale' references
[1]"Identification and characterization of nine novel human small GTPases showing variable expressions in liver cancer tissues."
He H., Dai F.Y., Yu L., She X., Zhao Y., Jiang J., Chen X., Zhao S.Y.
Gene Expr. 10:231-242(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]Wong K., Hong W., Tang B.
Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning."
Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M. expand/collapse author list , Zhou J., Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Pituitary.
[4]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[5]"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].
[6]"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].
Tissue: Brain.
[7]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[8]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"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].
Tissue: Cervix.
[10]"Rab10 regulates membrane transport through early endosomes of polarized Madin-Darby canine kidney cells."
Babbey C.M., Ahktar N., Wang E., Chen C.C., Grant B.D., Dunn K.W.
Mol. Biol. Cell 17:3156-3175(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[11]"GDI-1 preferably interacts with Rab10 in insulin-stimulated GLUT4 translocation."
Chen Y., Deng Y., Zhang J., Yang L., Xie X., Xu T.
Biochem. J. 422:229-235(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GDI1 AND GDI2.
[12]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-102, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Rab10 associates with primary cilia and the exocyst complex in renal epithelial cells."
Babbey C.M., Bacallao R.L., Dunn K.W.
Am. J. Physiol. 299:F495-506(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF THR-23 AND GLN-68.
[14]"Family-wide characterization of the DENN domain Rab GDP-GTP exchange factors."
Yoshimura S., Gerondopoulos A., Linford A., Rigden D.J., Barr F.A.
J. Cell Biol. 191:367-381(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION.
[15]"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].
[16]"Role of Rab GTPases in membrane traffic and cell physiology."
Hutagalung A.H., Novick P.J.
Physiol. Rev. 91:119-149(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[17]"Rab10 and myosin-Va mediate insulin-stimulated GLUT4 storage vesicle translocation in adipocytes."
Chen Y., Wang Y., Zhang J., Deng Y., Jiang L., Song E., Wu X.S., Hammer J.A., Xu T., Lippincott-Schwartz J.
J. Cell Biol. 198:545-560(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH MYO5A.
[18]"Rab10 GTPase regulates ER dynamics and morphology."
English A.R., Voeltz G.K.
Nat. Cell Biol. 15:169-178(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN ENDOPLASMIC RETICULUM MEMBRANE DYNAMICS, SUBCELLULAR LOCATION, MUTAGENESIS OF THR-23.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF086917 mRNA. Translation: AAP97147.1.
AF297660 mRNA. Translation: AAG13413.1.
AF106681 mRNA. Translation: AAD43034.1.
AL136650 mRNA. Translation: CAB66585.1.
AK023223 mRNA. Translation: BAB14474.1.
AF498945 mRNA. Translation: AAM21093.1.
CR457303 mRNA. Translation: CAG33584.1.
CH471053 Genomic DNA. Translation: EAX00710.1.
CH471053 Genomic DNA. Translation: EAX00711.1.
BC000896 mRNA. Translation: AAH00896.1.
RefSeqNP_057215.3. NM_016131.4.
UniGeneHs.467960.

3D structure databases

ProteinModelPortalP61026.
SMRP61026. Positions 9-173.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116096. 23 interactions.
IntActP61026. 11 interactions.
MINTMINT-1404404.
STRING9606.ENSP00000264710.

PTM databases

PhosphoSiteP61026.

Polymorphism databases

DMDM46577638.

Proteomic databases

PaxDbP61026.
PeptideAtlasP61026.
PRIDEP61026.

Protocols and materials databases

DNASU10890.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264710; ENSP00000264710; ENSG00000084733.
GeneID10890.
KEGGhsa:10890.
UCSCuc002rgv.3. human.

Organism-specific databases

CTD10890.
GeneCardsGC02P026256.
HGNCHGNC:9759. RAB10.
HPAHPA045611.
MIM612672. gene.
neXtProtNX_P61026.
PharmGKBPA34100.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1100.
HOGENOMHOG000233968.
HOVERGENHBG009351.
InParanoidP61026.
KOK07903.
OMASNINIER.
OrthoDBEOG7VB2H4.
PhylomeDBP61026.
TreeFamTF314097.

Enzyme and pathway databases

ReactomeREACT_11123. Membrane Trafficking.

Gene expression databases

ArrayExpressP61026.
BgeeP61026.
CleanExHS_RAB10.
GenevestigatorP61026.

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

ChiTaRSRAB10. human.
GeneWikiRAB10.
GenomeRNAi10890.
NextBio41349.
PROP61026.
SOURCESearch...

Entry information

Entry nameRAB10_HUMAN
AccessionPrimary (citable) accession number: P61026
Secondary accession number(s): D6W538 expand/collapse secondary AC list , O88386, Q6IA52, Q9D7X6, Q9H0T3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: April 26, 2004
Last modified: April 16, 2014
This is version 108 of the entry and version 1 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

MIM cross-references

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

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM