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P51153

- RAB13_HUMAN

UniProt

P51153 - RAB13_HUMAN

Protein

Ras-related protein Rab-13

Gene

RAB13

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      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 sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab is involved in endocytic recycling and regulates the transport to the plasma membrane of transmembrane proteins like the tight junction protein OCLN/occludin. Thereby, it regulates the assembly and the activity of tight junctions. Moreover, it may also regulate tight junction assembly by activating the PKA signaling pathway and by reorganizing the actin cytoskeleton through the activation of the downstream effectors PRKACA and MICALL2 respectively. Through its role in tight junction assembly, may play a role in the establishment of Sertoli cell barrier. Plays also a role in angiogenesis through regulation of endothelial cells chemotaxis. Also involved in neurite outgrowth. Has also been proposed to play a role in post-Golgi membrane trafficking from the TGN to the recycling endosome. Finally, it has been involved in insulin-induced transport to the plasma membrane of the glucose transporter GLUT4 and therefore may play a role in glucose homeostasis.6 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). That Rab may be activated by DENND1C, a guanine exchange factor. Activated in response to insulin.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi15 – 228GTPBy similarity
    Nucleotide bindingi63 – 675GTPBy similarity
    Nucleotide bindingi121 – 1244GTPBy similarity

    GO - Molecular functioni

    1. GTPase activity Source: Reactome
    2. GTP binding Source: UniProtKB
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. cellular response to insulin stimulus Source: UniProtKB
    2. cortical actin cytoskeleton organization Source: UniProtKB
    3. endocytic recycling Source: UniProtKB
    4. endosomal transport Source: UniProtKB
    5. endothelial cell chemotaxis Source: UniProtKB
    6. establishment of protein localization to plasma membrane Source: UniProtKB
    7. establishment of Sertoli cell barrier Source: UniProtKB
    8. GTP catabolic process Source: GOC
    9. membrane organization Source: Reactome
    10. neuron projection development Source: UniProtKB
    11. protein kinase A signaling Source: UniProtKB
    12. protein transport Source: UniProtKB-KW
    13. small GTPase mediated signal transduction Source: InterPro
    14. tight junction assembly Source: UniProtKB
    15. trans-Golgi network to recycling endosome 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-13
    Alternative name(s):
    Cell growth-inhibiting gene 4 protein
    Gene namesi
    Name:RAB13
    ORF Names:GIG4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:9762. RAB13.

    Subcellular locationi

    Cell membrane; Lipid-anchor; Cytoplasmic side. Cytoplasmic vesicle membrane; Lipid-anchor; Cytoplasmic side. Cell junctiontight junction. Golgi apparatustrans-Golgi network membrane. Recycling endosome membrane. Cell projectionlamellipodium By similarity. Cytoplasmic vesiclesecretory vesicle membrane By similarity
    Note: Tight junctions or associated with vesicles scattered throughout the cytoplasm in cells lacking tight junctions. Relocalizes to the leading edge of lamellipodia in migrating endothelial cells.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytoplasmic vesicle Source: UniProtKB
    3. cytoplasmic vesicle membrane Source: Reactome
    4. endocytic vesicle Source: UniProtKB
    5. extracellular vesicular exosome Source: UniProt
    6. insulin-responsive compartment Source: UniProtKB
    7. lamellipodium Source: UniProtKB
    8. lateral plasma membrane Source: UniProtKB
    9. neuron projection Source: UniProtKB
    10. plasma membrane Source: UniProtKB
    11. recycling endosome Source: UniProtKB
    12. recycling endosome membrane Source: UniProtKB-SubCell
    13. tight junction Source: UniProtKB
    14. trans-Golgi network Source: UniProtKB
    15. transport vesicle membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cell projection, Cytoplasmic vesicle, Endosome, Golgi apparatus, Membrane, Tight junction

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi22 – 221T → N: Dominant negative. 1 Publication
    Mutagenesisi67 – 671Q → L: Constitutively active mutant locked in the active GTP-bound form. Impairs transports of cargo from the trans-Golgi network to the recycling endosomes and alters the assembly of functional tight junctions. 1 Publication

    Organism-specific databases

    PharmGKBiPA34103.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 200200Ras-related protein Rab-13PRO_0000121182Add
    BLAST
    Propeptidei201 – 2033Removed in mature formSequence AnalysisPRO_0000370756

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei178 – 1781Phosphoserine3 Publications
    Modified residuei200 – 2001Cysteine methyl esterSequence Analysis
    Lipidationi200 – 2001S-geranylgeranyl cysteine1 Publication

    Keywords - PTMi

    Lipoprotein, Methylation, Phosphoprotein, Prenylation

    Proteomic databases

    MaxQBiP51153.
    PaxDbiP51153.
    PRIDEiP51153.

    PTM databases

    PhosphoSiteiP51153.

    Expressioni

    Tissue specificityi

    Detected in several types of epithelia, including intestine, kidney, liver and in endothelial cells.

    Inductioni

    Up-regulated during osteoclast differentiation.1 Publication

    Gene expression databases

    ArrayExpressiP51153.
    BgeeiP51153.
    CleanExiHS_RAB13.
    GenevestigatoriP51153.

    Organism-specific databases

    HPAiHPA003996.

    Interactioni

    Subunit structurei

    Interacts (GTP-bound form) with MICALL2; competes with RAB8A and is involved in tight junctions assembly. Interacts (GTP-bound form) with MICALL1. Interacts with PRKACA; downstream effector of RAB13 involved in tight junction assembly. Interacts with GRB2; may recruit RAB13 to the leading edge of migrating endothelial cells where it can activate RHOA. Interacts (isoprenylated form) with PDE6D; dissociates RAB13 from membranes. Interacts with CCDC64B/BICDR2. Interacts with LEPROT and LEPROTL1.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Leprotl1Q6PDU44EBI-1780121,EBI-8702651From a different organism.
    Micall2Q3TN348EBI-1780121,EBI-1779852From a different organism.
    PDE6DO439242EBI-1780121,EBI-712685

    Protein-protein interaction databases

    BioGridi111810. 8 interactions.
    DIPiDIP-40268N.
    IntActiP51153. 9 interactions.
    MINTiMINT-3018790.
    STRINGi9606.ENSP00000357564.

    Structurei

    3D structure databases

    ProteinModelPortaliP51153.
    SMRiP51153. Positions 6-172.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi37 – 459Effector regionBy similarity

    Sequence similaritiesi

    Belongs to the small GTPase superfamily. Rab family.Curated

    Phylogenomic databases

    eggNOGiCOG1100.
    HOVERGENiHBG009351.
    InParanoidiP51153.
    KOiK06109.
    OMAiKVQREQA.
    OrthoDBiEOG7VB2H4.
    PhylomeDBiP51153.
    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P51153-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAKAYDHLFK LLLIGDSGVG KTCLIIRFAE DNFNNTYIST IGIDFKIRTV    50
    DIEGKKIKLQ VWDTAGQERF KTITTAYYRG AMGIILVYDI TDEKSFENIQ 100
    NWMKSIKENA SAGVERLLLG NKCDMEAKRK VQKEQADKLA REHGIRFFET 150
    SAKSSMNVDE AFSSLARDIL LKSGGRRSGN GNKPPSTDLK TCDKKNTNKC 200
    SLG 203
    Length:203
    Mass (Da):22,774
    Last modified:October 1, 1996 - v1
    Checksum:i141621CB998178DA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X75593 mRNA. Translation: CAA53266.1.
    AY423722 mRNA. Translation: AAS00485.1.
    AF498948 mRNA. Translation: AAM21096.1.
    AK291580 mRNA. Translation: BAF84269.1.
    BT019700 mRNA. Translation: AAV38506.1.
    BT019701 mRNA. Translation: AAV38507.1.
    AL358472 Genomic DNA. Translation: CAI14031.1.
    CH471121 Genomic DNA. Translation: EAW53249.1.
    CH471121 Genomic DNA. Translation: EAW53250.1.
    BC000799 mRNA. Translation: AAH00799.1.
    BC009227 mRNA. Translation: AAH09227.2.
    BC073168 mRNA. Translation: AAH73168.2.
    CCDSiCCDS1058.1.
    PIRiA49647.
    RefSeqiNP_001258967.1. NM_001272038.1.
    NP_002861.1. NM_002870.3.
    UniGeneiHs.151536.

    Genome annotation databases

    EnsembliENST00000368575; ENSP00000357564; ENSG00000143545.
    GeneIDi5872.
    KEGGihsa:5872.
    UCSCiuc001fdt.2. human.

    Polymorphism databases

    DMDMi1710016.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X75593 mRNA. Translation: CAA53266.1 .
    AY423722 mRNA. Translation: AAS00485.1 .
    AF498948 mRNA. Translation: AAM21096.1 .
    AK291580 mRNA. Translation: BAF84269.1 .
    BT019700 mRNA. Translation: AAV38506.1 .
    BT019701 mRNA. Translation: AAV38507.1 .
    AL358472 Genomic DNA. Translation: CAI14031.1 .
    CH471121 Genomic DNA. Translation: EAW53249.1 .
    CH471121 Genomic DNA. Translation: EAW53250.1 .
    BC000799 mRNA. Translation: AAH00799.1 .
    BC009227 mRNA. Translation: AAH09227.2 .
    BC073168 mRNA. Translation: AAH73168.2 .
    CCDSi CCDS1058.1.
    PIRi A49647.
    RefSeqi NP_001258967.1. NM_001272038.1.
    NP_002861.1. NM_002870.3.
    UniGenei Hs.151536.

    3D structure databases

    ProteinModelPortali P51153.
    SMRi P51153. Positions 6-172.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111810. 8 interactions.
    DIPi DIP-40268N.
    IntActi P51153. 9 interactions.
    MINTi MINT-3018790.
    STRINGi 9606.ENSP00000357564.

    PTM databases

    PhosphoSitei P51153.

    Polymorphism databases

    DMDMi 1710016.

    Proteomic databases

    MaxQBi P51153.
    PaxDbi P51153.
    PRIDEi P51153.

    Protocols and materials databases

    DNASUi 5872.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000368575 ; ENSP00000357564 ; ENSG00000143545 .
    GeneIDi 5872.
    KEGGi hsa:5872.
    UCSCi uc001fdt.2. human.

    Organism-specific databases

    CTDi 5872.
    GeneCardsi GC01M153954.
    HGNCi HGNC:9762. RAB13.
    HPAi HPA003996.
    MIMi 602672. gene.
    neXtProti NX_P51153.
    PharmGKBi PA34103.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1100.
    HOVERGENi HBG009351.
    InParanoidi P51153.
    KOi K06109.
    OMAi KVQREQA.
    OrthoDBi EOG7VB2H4.
    PhylomeDBi P51153.
    TreeFami TF314097.

    Enzyme and pathway databases

    Reactomei REACT_147867. Translocation of GLUT4 to the plasma membrane.

    Miscellaneous databases

    ChiTaRSi RAB13. human.
    GeneWikii RAB13.
    GenomeRNAii 5872.
    NextBioi 22808.
    PROi P51153.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P51153.
    Bgeei P51153.
    CleanExi HS_RAB13.
    Genevestigatori P51153.

    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. "A small rab GTPase is distributed in cytoplasmic vesicles in non polarized cells but colocalizes with the tight junction marker ZO-1 in polarized epithelial cells."
      Zahraoui A., Joberty G., Arpin M., Fontaine J.J., Hellio R., Tavitian A., Louvard D.
      J. Cell Biol. 124:101-115(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
    2. "Identification of a human growth inhibition gene 4 (GIG4)."
      Kim J.W.
      Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    3. "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.
    4. "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].
      Tissue: Placenta.
    5. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    6. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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: Ovary, Placenta and PNS.
    9. "Isoprenylation of Rab proteins possessing a C-terminal CaaX motif."
      Joberty G., Tavitian A., Zahraoui A.
      FEBS Lett. 330:323-328(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: ISOPRENYLATION AT CYS-200.
    10. "The rod cGMP phosphodiesterase delta subunit dissociates the small GTPase Rab13 from membranes."
      Marzesco A.M., Galli T., Louvard D., Zahraoui A.
      J. Biol. Chem. 273:22340-22345(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PDE6D.
    11. "The small GTPase Rab13 regulates assembly of functional tight junctions in epithelial cells."
      Marzesco A.M., Dunia I., Pandjaitan R., Recouvreur M., Dauzonne D., Benedetti E.L., Louvard D., Zahraoui A.
      Mol. Biol. Cell 13:1819-1831(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN TIGHT JUNCTION ASSEMBLY, SUBCELLULAR LOCATION.
    12. "Rab13 regulates PKA signaling during tight junction assembly."
      Koehler K., Louvard D., Zahraoui A.
      J. Cell Biol. 165:175-180(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN TIGHT JUNCTION ASSEMBLY, INTERACTION WITH PRKACA.
    13. "Rab13 mediates the continuous endocytic recycling of occludin to the cell surface."
      Morimoto S., Nishimura N., Terai T., Manabe S., Yamamoto Y., Shinahara W., Miyake H., Tashiro S., Shimada M., Sasaki T.
      J. Biol. Chem. 280:2220-2228(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN ENDOCYTIC RECYLING, SUBCELLULAR LOCATION.
    14. "JRAB/MICAL-L2 is a junctional Rab13-binding protein mediating the endocytic recycling of occludin."
      Terai T., Nishimura N., Kanda I., Yasui N., Sasaki T.
      Mol. Biol. Cell 17:2465-2475(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN TIGHT JUNCTION ASSEMBLY, INTERACTION WITH MICALL2.
    15. "Rab13 regulates membrane trafficking between TGN and recycling endosomes in polarized epithelial cells."
      Nokes R.L., Fields I.C., Collins R.N., Foelsch H.
      J. Cell Biol. 182:845-853(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF THR-22 AND GLN-67.
    16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. "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.
    18. "Rab13 regulates neurite outgrowth in PC12 cells through its effector protein, JRAB/MICAL-L2."
      Sakane A., Honda K., Sasaki T.
      Mol. Cell. Biol. 30:1077-1087(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN NEURITE OUTGROWTH, INTERACTION WITH MICALL2.
    19. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. Cited for: INTERACTION WITH MICALL1.
      Tissue: Uterine adenocarcinoma.
    22. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "Rab13 is upregulated during osteoclast differentiation and associates with small vesicles revealing polarized distribution in resorbing cells."
      Hirvonen M.J., Mulari M.T., Bueki K.G., Vihko P., Haerkoenen P.L., Vaeaenaenen H.K.
      J. Histochem. Cytochem. 60:537-549(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.

    Entry informationi

    Entry nameiRAB13_HUMAN
    AccessioniPrimary (citable) accession number: P51153
    Secondary accession number(s): A8K6B5
    , D3DV67, Q5U0A6, Q6GPG6, Q96GU4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 144 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 1
      Human chromosome 1: 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