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Protein

Ras-related protein Rab-10

Gene

RAB10

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 PubMed:23263280, may play a role in endoplasmic reticulum dynamics and morphology controlling tubulation along microtubules and tubules fusion.By similarity3 Publications

Enzyme regulationi

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).By similarity1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi16 – 238GTPBy similarity
Nucleotide bindingi64 – 685GTPBy similarity
Nucleotide bindingi122 – 1254GTPBy similarity

GO - Molecular functioni

  1. GDP binding Source: UniProtKB
  2. GTPase activity Source: Reactome
  3. GTP binding Source: UniProtKB
  4. myosin V binding Source: UniProtKB

GO - Biological processi

  1. antigen processing and presentation Source: UniProtKB
  2. axonogenesis Source: UniProtKB
  3. basolateral protein localization Source: UniProtKB
  4. cellular response to insulin stimulus Source: UniProtKB
  5. endoplasmic reticulum tubular network organization Source: UniProtKB
  6. endosomal transport Source: UniProtKB
  7. establishment of neuroblast polarity Source: UniProtKB
  8. establishment of protein localization to endoplasmic reticulum membrane Source: UniProtKB
  9. establishment of protein localization to membrane Source: UniProtKB
  10. Golgi to plasma membrane protein transport Source: UniProtKB
  11. Golgi to plasma membrane transport Source: UniProtKB
  12. GTP catabolic process Source: GO_Central
  13. intracellular protein transport Source: GO_Central
  14. membrane organization Source: Reactome
  15. polarized epithelial cell differentiation Source: UniProtKB
  16. protein localization to plasma membrane Source: UniProtKB
  17. protein secretion Source: GO_Central
  18. Rab protein signal transduction Source: GO_Central
  19. regulation of exocytosis Source: GO_Central
  20. vesicle docking involved in exocytosis Source: GO_Central
  21. vesicle-mediated transport Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_147867. Translocation of GLUT4 to the plasma membrane.

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related protein Rab-10
Gene namesi
Name:RAB10
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:9759. RAB10.

Subcellular locationi

Cytoplasmic vesicle membrane Curated; Lipid-anchor Curated; Cytoplasmic side Curated. 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 PubMed:23263280 localizes to the endoplasmic reticulum at domains of new tubule growth.By similarity

GO - Cellular componenti

  1. cytoplasmic vesicle membrane Source: Reactome
  2. endoplasmic reticulum membrane Source: UniProtKB
  3. endoplasmic reticulum tubular network Source: UniProtKB
  4. endosome Source: UniProtKB
  5. endosome membrane Source: GO_Central
  6. extracellular vesicular exosome Source: UniProtKB
  7. focal adhesion Source: UniProtKB
  8. Golgi apparatus Source: UniProtKB
  9. insulin-responsive compartment Source: UniProtKB
  10. phagocytic vesicle membrane Source: UniProtKB-SubCell
  11. primary cilium Source: UniProtKB
  12. recycling endosome Source: UniProtKB
  13. recycling endosome membrane Source: UniProtKB-SubCell
  14. trans-Golgi network Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasmic vesicle, Endoplasmic reticulum, Endosome, Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi23 – 231T → 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. 2 Publications
Mutagenesisi68 – 681Q → 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. 1 Publication

Organism-specific databases

PharmGKBiPA34100.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 200200Ras-related protein Rab-10PRO_0000121146Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei102 – 1021N6-acetyllysine1 Publication
Lipidationi199 – 1991S-geranylgeranyl cysteineBy similarity
Lipidationi200 – 2001S-geranylgeranyl cysteineBy similarity

Keywords - PTMi

Acetylation, Lipoprotein, Prenylation

Proteomic databases

MaxQBiP61026.
PaxDbiP61026.
PeptideAtlasiP61026.
PRIDEiP61026.

PTM databases

PhosphoSiteiP61026.

Expressioni

Gene expression databases

BgeeiP61026.
CleanExiHS_RAB10.
ExpressionAtlasiP61026. baseline and differential.
GenevestigatoriP61026.

Organism-specific databases

HPAiHPA045611.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

BioGridi116096. 29 interactions.
IntActiP61026. 11 interactions.
MINTiMINT-1404404.
STRINGi9606.ENSP00000264710.

Structurei

3D structure databases

ProteinModelPortaliP61026.
SMRiP61026. Positions 9-173.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi38 – 469Effector regionBy similarity

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rab family.Curated

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000118937.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiP61026.
KOiK07903.
OMAiDKAPGYN.
OrthoDBiEOG7VB2H4.
PhylomeDBiP61026.
TreeFamiTF314097.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00175. RAB. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51419. RAB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P61026-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAKKTYDLLF KLLLIGDSGV GKTCVLFRFS DDAFNTTFIS TIGIDFKIKT
60 70 80 90 100
VELQGKKIKL QIWDTAGQER FHTITTSYYR GAMGIMLVYD ITNGKSFENI
110 120 130 140 150
SKWLRNIDEH ANEDVERMLL GNKCDMDDKR VVPKGKGEQI AREHGIRFFE
160 170 180 190 200
TSAKANINIE KAFLTLAEDI LRKTPVKEPN SENVDISSGG GVTGWKSKCC
Length:200
Mass (Da):22,541
Last modified:April 26, 2004 - v1
Checksum:i7F02B8E8E46EE1E8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti138 – 1381E → G in CAB66585. (PubMed:11230166)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS1720.1.
RefSeqiNP_057215.3. NM_016131.4.
UniGeneiHs.467960.

Genome annotation databases

EnsembliENST00000264710; ENSP00000264710; ENSG00000084733.
GeneIDi10890.
KEGGihsa:10890.
UCSCiuc002rgv.3. human.

Polymorphism databases

DMDMi46577638.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS1720.1.
RefSeqiNP_057215.3. NM_016131.4.
UniGeneiHs.467960.

3D structure databases

ProteinModelPortaliP61026.
SMRiP61026. Positions 9-173.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116096. 29 interactions.
IntActiP61026. 11 interactions.
MINTiMINT-1404404.
STRINGi9606.ENSP00000264710.

PTM databases

PhosphoSiteiP61026.

Polymorphism databases

DMDMi46577638.

Proteomic databases

MaxQBiP61026.
PaxDbiP61026.
PeptideAtlasiP61026.
PRIDEiP61026.

Protocols and materials databases

DNASUi10890.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000264710; ENSP00000264710; ENSG00000084733.
GeneIDi10890.
KEGGihsa:10890.
UCSCiuc002rgv.3. human.

Organism-specific databases

CTDi10890.
GeneCardsiGC02P026256.
HGNCiHGNC:9759. RAB10.
HPAiHPA045611.
MIMi612672. gene.
neXtProtiNX_P61026.
PharmGKBiPA34100.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000118937.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiP61026.
KOiK07903.
OMAiDKAPGYN.
OrthoDBiEOG7VB2H4.
PhylomeDBiP61026.
TreeFamiTF314097.

Enzyme and pathway databases

ReactomeiREACT_147867. Translocation of GLUT4 to the plasma membrane.

Miscellaneous databases

ChiTaRSiRAB10. human.
GeneWikiiRAB10.
GenomeRNAii10890.
NextBioi41349.
PROiP61026.
SOURCEiSearch...

Gene expression databases

BgeeiP61026.
CleanExiHS_RAB10.
ExpressionAtlasiP61026. baseline and differential.
GenevestigatoriP61026.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00175. RAB. 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. "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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Pituitary.
  4. 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. 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. 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.

Entry informationi

Entry nameiRAB10_HUMAN
AccessioniPrimary (citable) accession number: P61026
Secondary accession number(s): D6W538
, O88386, Q6IA52, Q9D7X6, Q9H0T3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: April 26, 2004
Last modified: February 4, 2015
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.