P61026 (RAB10_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ras-related protein Rab-10

Gene names

Name:

RAB10

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	200 AA.
Sequence status	Complete.
Protein existence	Evidence 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 apparatus › trans-Golgi network membrane By similarity. Endosome membrane. Recycling endosome membrane. Cytoplasmic vesicle › phagosome membrane By similarity. Cell projection › cilium. 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 process	Protein transport Transport
Cellular component	Cell projection Cytoplasmic vesicle Endoplasmic reticulum Endosome Golgi apparatus Membrane
Ligand	GTP-binding Nucleotide-binding
PTM	Acetylation Lipoprotein Prenylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Golgi to plasma membrane protein transport Inferred from sequence or structural similarity. Source: UniProtKB 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 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
Cellular_component	Golgi 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 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_function	GDP 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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 200	200	Ras-related protein Rab-10		PRO_0000121146
Regions
	Nucleotide binding	16 – 23	8	GTP By similarity
	Nucleotide binding	64 – 68	5	GTP By similarity
	Nucleotide binding	122 – 125	4	GTP By similarity
	Motif	38 – 46	9	Effector region By similarity
Amino acid modifications
	Modified residue	102	1	N6-acetyllysine Ref.12
	Lipidation	199	1	S-geranylgeranyl cysteine By similarity
	Lipidation	200	1	S-geranylgeranyl cysteine By similarity
Experimental info
	Mutagenesis	23	1	T → 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
	Mutagenesis	68	1	Q → 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 conflict	138	1	E → G in CAB66585. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P61026 [UniParc]. Last modified April 26, 2004. Version 1. Checksum: 7F02B8E8E46EE1E8	FASTA	200	22,541
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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. , 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, MASS SPECTROMETRY.
[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(2012) [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.
IPI	IPI00016513.
RefSeq	NP_057215.3. NM_016131.4.
UniGene	Hs.467960.
3D structure databases
ProteinModelPortal	P61026.
ModBase	Search...
Protein-protein interaction databases
IntAct	P61026. 8 interactions.
MINT	MINT-1404404.
STRING	9606.ENSP00000264710.
PTM databases
PhosphoSite	P61026.
Polymorphism databases
DMDM	46577638.
Proteomic databases
PaxDb	P61026.
PeptideAtlas	P61026.
PRIDE	P61026.
Protocols and materials databases
DNASU	10890.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000264710; ENSP00000264710; ENSG00000084733.
GeneID	10890.
KEGG	hsa:10890.
UCSC	uc002rgv.3. human.
Organism-specific databases
CTD	10890.
GeneCards	GC02P026256.
HGNC	HGNC:9759. RAB10.
HPA	HPA045611.
MIM	612672. gene.
neXtProt	NX_P61026.
PharmGKB	PA34100.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1100.
HOGENOM	HOG000233968.
HOVERGEN	HBG009351.
InParanoid	P61026.
KO	K07903.
OMA	WKSKCCS.
OrthoDB	EOG4K3KX6.
PhylomeDB	P61026.
Enzyme and pathway databases
Reactome	REACT_11123. Membrane Trafficking.
Gene expression databases
ArrayExpress	P61026.
Bgee	P61026.
CleanEx	HS_RAB10.
Genevestigator	P61026.
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	RAB10. human.
GenomeRNAi	10890.
NextBio	41349.
SOURCE	Search...

Entry information

Entry name

RAB10_HUMAN

Accession

Primary (citable) accession number: P61026
Secondary accession number(s): D6W538 , O88386, Q6IA52, Q9D7X6, Q9H0T3

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2004
Last sequence update:	April 26, 2004
Last modified:	May 29, 2013
This is version 100 of the entry and version 1 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.