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P61026

- RAB10_HUMAN

UniProt

P61026 - RAB10_HUMAN

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
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 1 (26 Apr 2004)
      Previous versions | rss
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    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: UniProt
    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. Golgi to plasma membrane protein transport Source: UniProtKB
    10. Golgi to plasma membrane transport Source: UniProtKB
    11. GTP catabolic process Source: GOC
    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

    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. extracellular vesicular exosome Source: UniProt
    6. Golgi apparatus Source: UniProtKB
    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

    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

    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.By similarity

    Protein-protein interaction databases

    BioGridi116096. 28 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.
    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

    Experimental Info

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

    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

    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: October 1, 2014
    This is version 113 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