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P61026

- RAB10_HUMAN

UniProt

P61026 - RAB10_HUMAN

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Protein
Ras-related protein Rab-10
Gene
RAB10
Organism
Homo sapiens (Human)
Status
Reviewed - 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 1 Publication, may play a role in endoplasmic reticulum dynamics and morphology controlling tubulation along microtubules and tubules fusion.3 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).1 Publication

Regions

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

GO - Molecular functioni

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

GO - Biological processi

  1. GTP catabolic process Source: GOC
  2. Golgi to plasma membrane protein transport Source: UniProtKB
  3. Golgi to plasma membrane transport Source: UniProtKB
  4. antigen processing and presentation Source: UniProt
  5. axonogenesis Source: UniProtKB
  6. basolateral protein localization Source: UniProtKB
  7. cellular response to insulin stimulus Source: UniProtKB
  8. endoplasmic reticulum tubular network organization Source: UniProtKB
  9. endosomal transport Source: UniProtKB
  10. establishment of neuroblast polarity Source: UniProtKB
  11. establishment of protein localization to endoplasmic reticulum membrane Source: UniProtKB
  12. membrane organization Source: Reactome
  13. polarized epithelial cell differentiation Source: UniProtKB
  14. protein localization to plasma membrane Source: UniProtKB
  15. small GTPase mediated signal transduction Source: InterPro
  16. 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; Lipid-anchor Inferred; Cytoplasmic side Inferred. 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 1 Publication localizes to the endoplasmic reticulum at domains of new tubule growth.4 Publications

GO - Cellular componenti

  1. Golgi apparatus Source: UniProtKB
  2. cytoplasmic vesicle membrane Source: Reactome
  3. endoplasmic reticulum membrane Source: UniProtKB
  4. endoplasmic reticulum tubular network Source: UniProtKB
  5. endosome Source: UniProtKB
  6. extracellular vesicular exosome Source: UniProt
  7. insulin-responsive compartment Source: UniProtKB
  8. phagocytic vesicle membrane Source: UniProtKB-SubCell
  9. primary cilium Source: UniProtKB
  10. recycling endosome Source: UniProtKB
  11. recycling endosome membrane Source: UniProtKB-SubCell
  12. 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-10
PRO_0000121146Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation, Lipoprotein, Prenylation

Proteomic databases

MaxQBiP61026.
PaxDbiP61026.
PeptideAtlasiP61026.
PRIDEiP61026.

PTM databases

PhosphoSiteiP61026.

Expressioni

Gene expression databases

ArrayExpressiP61026.
BgeeiP61026.
CleanExiHS_RAB10.
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.2 Publications

Protein-protein interaction databases

BioGridi116096. 28 interactions.
IntActiP61026. 11 interactions.
MINTiMINT-1404404.
STRINGi9606.ENSP00000264710.

Structurei

3D structure databases

ProteinModelPortaliP61026.
SMRiP61026. Positions 9-173.

Family & Domainsi

Motif

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1100.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiP61026.
KOiK07903.
OMAiERAFCEL.
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

MAKKTYDLLF KLLLIGDSGV GKTCVLFRFS DDAFNTTFIS TIGIDFKIKT    50
VELQGKKIKL QIWDTAGQER FHTITTSYYR GAMGIMLVYD ITNGKSFENI 100
SKWLRNIDEH ANEDVERMLL GNKCDMDDKR VVPKGKGEQI AREHGIRFFE 150
TSAKANINIE KAFLTLAEDI LRKTPVKEPN SENVDISSGG GVTGWKSKCC 200
Length:200
Mass (Da):22,541
Last modified:April 26, 2004 - v1
Checksum:i7F02B8E8E46EE1E8
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti138 – 1381E → G in CAB66585. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS1720.1.
RefSeqi NP_057215.3. NM_016131.4.
UniGenei Hs.467960.

3D structure databases

ProteinModelPortali P61026.
SMRi P61026. Positions 9-173.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116096. 28 interactions.
IntActi P61026. 11 interactions.
MINTi MINT-1404404.
STRINGi 9606.ENSP00000264710.

PTM databases

PhosphoSitei P61026.

Polymorphism databases

DMDMi 46577638.

Proteomic databases

MaxQBi P61026.
PaxDbi P61026.
PeptideAtlasi P61026.
PRIDEi P61026.

Protocols and materials databases

DNASUi 10890.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000264710 ; ENSP00000264710 ; ENSG00000084733 .
GeneIDi 10890.
KEGGi hsa:10890.
UCSCi uc002rgv.3. human.

Organism-specific databases

CTDi 10890.
GeneCardsi GC02P026256.
HGNCi HGNC:9759. RAB10.
HPAi HPA045611.
MIMi 612672. gene.
neXtProti NX_P61026.
PharmGKBi PA34100.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1100.
HOGENOMi HOG000233968.
HOVERGENi HBG009351.
InParanoidi P61026.
KOi K07903.
OMAi ERAFCEL.
OrthoDBi EOG7VB2H4.
PhylomeDBi P61026.
TreeFami TF314097.

Enzyme and pathway databases

Reactomei REACT_147867. Translocation of GLUT4 to the plasma membrane.

Miscellaneous databases

ChiTaRSi RAB10. human.
GeneWikii RAB10.
GenomeRNAii 10890.
NextBioi 41349.
PROi P61026.
SOURCEi Search...

Gene expression databases

ArrayExpressi P61026.
Bgeei P61026.
CleanExi HS_RAB10.
Genevestigatori P61026.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
InterProi IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view ]
Pfami PF00071. Ras. 1 hit.
[Graphical view ]
PRINTSi PR00449. RASTRNSFRMNG.
SMARTi SM00175. RAB. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR00231. small_GTP. 1 hit.
PROSITEi PS51419. RAB. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 112 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

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