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P62491

- RB11A_HUMAN

UniProt

P62491 - RB11A_HUMAN

Protein

Ras-related protein Rab-11A

Gene

RAB11A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      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. That Rab regulates endocytic recycling. Acts as a major regulator of membrane delivery during cytokinesis. Together with MYO5B and RAB8A participates in epithelial cell polarization. Together with RAB3IP, RAB8A, the exocyst complex, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of PODXL to the apical membrane initiation sites (AMIS), apical surface formation and lumenogenesis. Together with MYO5B participates in CFTR trafficking to the plasma membrane and TF (Transferrin) recycling in nonpolarized cells. Required in a complex with MYO5B and RAB11FIP2 for the transport of NPC1L1 to the plasma membrane. Participates in the sorting and basolateral transport of CDH1 from the Golgi apparatus to the plasma membrane. Regulates the recycling of FCGRT (receptor of Fc region of monomeric Ig G) to basolateral membranes. May also play a role in melanosome transport and release from melanocytes.6 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi18 – 269GTP3 Publications
    Nucleotide bindingi66 – 705GTP3 Publications
    Nucleotide bindingi124 – 1274GTP3 Publications
    Nucleotide bindingi154 – 1563GTP3 Publications

    GO - Molecular functioni

    1. GTPase activity Source: UniProtKB
    2. GTP binding Source: UniProtKB-KW
    3. protein binding Source: UniProtKB
    4. syntaxin binding Source: UniProtKB

    GO - Biological processi

    1. cytokinesis Source: UniProtKB
    2. melanosome transport Source: UniProtKB
    3. neuron projection development Source: UniProtKB
    4. plasma membrane to endosome transport Source: UniProtKB
    5. positive regulation of axon extension Source: Ensembl
    6. protein localization to plasma membrane Source: UniProtKB
    7. protein transport Source: UniProtKB-KW
    8. regulation of long-term neuronal synaptic plasticity Source: Ensembl
    9. regulation of protein transport Source: Ensembl
    10. small GTPase mediated signal transduction Source: InterPro
    11. transmembrane transport Source: Reactome
    12. vesicle-mediated transport Source: UniProtKB
    13. water transport Source: Reactome

    Keywords - Biological processi

    Cell cycle, Protein transport, Transport

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_147867. Translocation of GLUT4 to the plasma membrane.
    REACT_24023. Regulation of water balance by renal Aquaporins.
    SignaLinkiP62491.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ras-related protein Rab-11A
    Short name:
    Rab-11
    Alternative name(s):
    YL8
    Gene namesi
    Name:RAB11A
    Synonyms:RAB11
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:9760. RAB11A.

    Subcellular locationi

    Cell membrane; Peripheral membrane protein. Recycling endosome membrane; Peripheral membrane protein. Cleavage furrow. Cytoplasmic vesiclephagosome. Cytoplasmic vesiclephagosome membrane By similarity; Lipid-anchor By similarity; Cytoplasmic side By similarity
    Note: Translocates with RAB11FIP2 from the vesicles of the endocytic recycling compartment (ERC) to the plasma membrane. Localizes to the cleavage furrow. Colocalizes with PARD3, PRKCI, EXOC5, OCLN, PODXL and RAB8A in apical membrane initiation sites (AMIS) during the generation of apical surface and lumenogenesis. Recruited to phagosomes containing S.aureus or M.tuberculosis.

    GO - Cellular componenti

    1. axon Source: Ensembl
    2. cleavage furrow Source: UniProtKB
    3. cytoplasmic vesicle membrane Source: Reactome
    4. extracellular vesicular exosome Source: UniProt
    5. mitochondrion Source: Ensembl
    6. perinuclear region of cytoplasm Source: Ensembl
    7. phagocytic vesicle Source: UniProtKB
    8. phagocytic vesicle membrane Source: UniProtKB-SubCell
    9. plasma membrane Source: UniProtKB-SubCell
    10. protein complex Source: UniProtKB
    11. recycling endosome Source: UniProtKB
    12. recycling endosome membrane Source: UniProtKB-SubCell
    13. trans-Golgi network Source: MGI
    14. transport vesicle Source: Ensembl

    Keywords - Cellular componenti

    Cell membrane, Cytoplasmic vesicle, Endosome, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi25 – 251S → N: Dominant-negative mutant. Induces increased number of binucleated cells, indicating defects in cytokinesis. Inhibits the transport of NPC1L1 to the plama membrane. Disrupts the trafficking of CDH1 to the plasma membrane and promotes accumulation of CDH1 in RAB11A endosomes in nonpolarized cells. Promotes mistargeting of CDH1 to the apical membrane in polarized cells. 3 Publications
    Mutagenesisi70 – 701Q → L: Constitutively active mutant. Decreases GTPase activity. Disrupts the trafficking of CDH1 to the plasma membrane and promotes accumulation of CDH1 in RAB11A endosomes in nonpolarized cells. Promotes mistargeting of CDH1 to the apical membrane in polarized cells. 5 Publications

    Organism-specific databases

    PharmGKBiPA34101.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 213212Ras-related protein Rab-11APRO_0000121151Add
    BLAST
    Propeptidei214 – 2163Removed in mature formSequence AnalysisPRO_0000370807

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylglycine1 Publication
    Lipidationi212 – 2121S-geranylgeranyl cysteine1 Publication
    Modified residuei213 – 2131Cysteine methyl esterSequence Analysis
    Lipidationi213 – 2131S-geranylgeranyl cysteine1 Publication

    Keywords - PTMi

    Acetylation, Lipoprotein, Methylation, Prenylation

    Proteomic databases

    MaxQBiP62491.
    PaxDbiP62491.
    PRIDEiP62491.

    2D gel databases

    OGPiP62491.

    PTM databases

    PhosphoSiteiP62491.

    Expressioni

    Gene expression databases

    ArrayExpressiP62491.
    BgeeiP62491.
    CleanExiHS_RAB11A.
    GenevestigatoriP62491.

    Organism-specific databases

    HPAiCAB013097.

    Interactioni

    Subunit structurei

    Interacts with RIP11 and STXBP6. Interacts with SGSM1, SGSM2 and SGSM3 By similarity. Interacts with EXOC6 in a GTP-dependent manner By similarity. Interacts with RAB11FIP1, RAB11FIP2, RAB11FIP3 (via its C-terminus) and RAB11FIP4. Interacts with EVI5; EVI5 and RAB11FIP3 may be mutually exclusive and compete for binding RAB11A. Interacts with VIPAS39. Interacts with MYO5B. Found in a complex with MYO5B and CFTR. Interacts with NPC1L1. Interacts (GDP-bound form) with ZFYVE27. Interacts with BIRC6/bruce. May interact with TBC1D14. Interacts with UNC119; in a cell cycle-dependent manner.By similarity22 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RAB11FIP2Q7L8042EBI-745098,EBI-1049676
    ZFYVE27Q5T4F44EBI-745098,EBI-3892947

    Protein-protein interaction databases

    BioGridi114299. 49 interactions.
    DIPiDIP-29138N.
    IntActiP62491. 20 interactions.
    MINTiMINT-1434585.
    STRINGi9606.ENSP00000261890.

    Structurei

    Secondary structure

    1
    216
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi9 – 1810
    Helixi24 – 3310
    Beta strandi45 – 5511
    Beta strandi58 – 6710
    Beta strandi72 – 743
    Helixi78 – 814
    Beta strandi86 – 927
    Helixi96 – 1005
    Helixi102 – 11211
    Beta strandi118 – 1247
    Helixi126 – 1316
    Helixi136 – 14510
    Beta strandi149 – 1524
    Turni155 – 1573
    Helixi161 – 17212

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1OIVX-ray1.98A/B1-173[»]
    1OIWX-ray2.05A1-173[»]
    1OIXX-ray1.70A1-173[»]
    1YZKX-ray2.00A8-175[»]
    2D7CX-ray1.75A/B7-173[»]
    2GZDX-ray2.44A/B2-173[»]
    2GZHX-ray2.47A2-173[»]
    2HV8X-ray1.86A/B/C6-175[»]
    4C4PX-ray2.00A1-173[»]
    4D0LX-ray2.94B/D/F1-216[»]
    4D0MX-ray6.00B/D/H/J/N/P/R/T/X/Z/d/h1-216[»]
    4LWZX-ray2.55A/C1-177[»]
    4LX0X-ray2.19A/C1-177[»]
    ProteinModelPortaliP62491.
    SMRiP62491. Positions 6-173.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP62491.

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi40 – 489Effector regionBy similarity

    Sequence similaritiesi

    Belongs to the small GTPase superfamily. Rab family.Curated

    Phylogenomic databases

    eggNOGiCOG1100.
    HOGENOMiHOG000233968.
    HOVERGENiHBG009351.
    InParanoidiP62491.
    KOiK07904.
    OMAiAMGTRDD.
    PhylomeDBiP62491.
    TreeFamiTF300099.

    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]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P62491-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MGTRDDEYDY LFKVVLIGDS GVGKSNLLSR FTRNEFNLES KSTIGVEFAT    50
    RSIQVDGKTI KAQIWDTAGQ ERYRAITSAY YRGAVGALLV YDIAKHLTYE 100
    NVERWLKELR DHADSNIVIM LVGNKSDLRH LRAVPTDEAR AFAEKNGLSF 150
    IETSALDSTN VEAAFQTILT EIYRIVSQKQ MSDRRENDMS PSNNVVPIHV 200
    PPTTENKPKV QCCQNI 216
    Length:216
    Mass (Da):24,394
    Last modified:January 23, 2007 - v3
    Checksum:i76FC1E113A29B269
    GO
    Isoform 2 (identifier: P62491-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         147-216: GLSFIETSAL...KPKVQCCQNI → EANVRQTRK

    Note: No experimental confirmation available.

    Show »
    Length:155
    Mass (Da):17,659
    Checksum:i70C3A0F378C9893A
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei147 – 21670GLSFI…CCQNI → EANVRQTRK in isoform 2. 1 PublicationVSP_046755Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X53143 mRNA. Translation: CAA37300.1.
    X56740 mRNA. Translation: CAA40064.1.
    AF000231 mRNA. Translation: AAC32887.1.
    AF498946 mRNA. Translation: AAM21094.1.
    CR407669 mRNA. Translation: CAG28597.1.
    CR536493 mRNA. Translation: CAG38732.1.
    BT020151 mRNA. Translation: AAV38953.1.
    BT020154 mRNA. Translation: AAV38956.1.
    AK300008 mRNA. Translation: BAG61825.1.
    AK311770 mRNA. Translation: BAG34713.1.
    AC011939 Genomic DNA. No translation available.
    AC084854 Genomic DNA. No translation available.
    CH471082 Genomic DNA. Translation: EAW77752.1.
    BC013348 mRNA. Translation: AAH13348.1.
    CCDSiCCDS10212.1. [P62491-1]
    CCDS58373.1. [P62491-2]
    PIRiS47169.
    RefSeqiNP_001193765.1. NM_001206836.1. [P62491-2]
    NP_004654.1. NM_004663.4. [P62491-1]
    UniGeneiHs.321541.

    Genome annotation databases

    EnsembliENST00000261890; ENSP00000261890; ENSG00000103769. [P62491-1]
    ENST00000569896; ENSP00000456420; ENSG00000103769. [P62491-2]
    GeneIDi8766.
    KEGGihsa:8766.
    UCSCiuc002apk.3. human. [P62491-1]

    Polymorphism databases

    DMDMi50402542.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X53143 mRNA. Translation: CAA37300.1 .
    X56740 mRNA. Translation: CAA40064.1 .
    AF000231 mRNA. Translation: AAC32887.1 .
    AF498946 mRNA. Translation: AAM21094.1 .
    CR407669 mRNA. Translation: CAG28597.1 .
    CR536493 mRNA. Translation: CAG38732.1 .
    BT020151 mRNA. Translation: AAV38953.1 .
    BT020154 mRNA. Translation: AAV38956.1 .
    AK300008 mRNA. Translation: BAG61825.1 .
    AK311770 mRNA. Translation: BAG34713.1 .
    AC011939 Genomic DNA. No translation available.
    AC084854 Genomic DNA. No translation available.
    CH471082 Genomic DNA. Translation: EAW77752.1 .
    BC013348 mRNA. Translation: AAH13348.1 .
    CCDSi CCDS10212.1. [P62491-1 ]
    CCDS58373.1. [P62491-2 ]
    PIRi S47169.
    RefSeqi NP_001193765.1. NM_001206836.1. [P62491-2 ]
    NP_004654.1. NM_004663.4. [P62491-1 ]
    UniGenei Hs.321541.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1OIV X-ray 1.98 A/B 1-173 [» ]
    1OIW X-ray 2.05 A 1-173 [» ]
    1OIX X-ray 1.70 A 1-173 [» ]
    1YZK X-ray 2.00 A 8-175 [» ]
    2D7C X-ray 1.75 A/B 7-173 [» ]
    2GZD X-ray 2.44 A/B 2-173 [» ]
    2GZH X-ray 2.47 A 2-173 [» ]
    2HV8 X-ray 1.86 A/B/C 6-175 [» ]
    4C4P X-ray 2.00 A 1-173 [» ]
    4D0L X-ray 2.94 B/D/F 1-216 [» ]
    4D0M X-ray 6.00 B/D/H/J/N/P/R/T/X/Z/d/h 1-216 [» ]
    4LWZ X-ray 2.55 A/C 1-177 [» ]
    4LX0 X-ray 2.19 A/C 1-177 [» ]
    ProteinModelPortali P62491.
    SMRi P62491. Positions 6-173.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114299. 49 interactions.
    DIPi DIP-29138N.
    IntActi P62491. 20 interactions.
    MINTi MINT-1434585.
    STRINGi 9606.ENSP00000261890.

    PTM databases

    PhosphoSitei P62491.

    Polymorphism databases

    DMDMi 50402542.

    2D gel databases

    OGPi P62491.

    Proteomic databases

    MaxQBi P62491.
    PaxDbi P62491.
    PRIDEi P62491.

    Protocols and materials databases

    DNASUi 8766.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000261890 ; ENSP00000261890 ; ENSG00000103769 . [P62491-1 ]
    ENST00000569896 ; ENSP00000456420 ; ENSG00000103769 . [P62491-2 ]
    GeneIDi 8766.
    KEGGi hsa:8766.
    UCSCi uc002apk.3. human. [P62491-1 ]

    Organism-specific databases

    CTDi 8766.
    GeneCardsi GC15P066018.
    HGNCi HGNC:9760. RAB11A.
    HPAi CAB013097.
    MIMi 605570. gene.
    neXtProti NX_P62491.
    PharmGKBi PA34101.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1100.
    HOGENOMi HOG000233968.
    HOVERGENi HBG009351.
    InParanoidi P62491.
    KOi K07904.
    OMAi AMGTRDD.
    PhylomeDBi P62491.
    TreeFami TF300099.

    Enzyme and pathway databases

    Reactomei REACT_147867. Translocation of GLUT4 to the plasma membrane.
    REACT_24023. Regulation of water balance by renal Aquaporins.
    SignaLinki P62491.

    Miscellaneous databases

    EvolutionaryTracei P62491.
    GeneWikii RAB11A.
    GenomeRNAii 8766.
    NextBioi 32876.
    PROi P62491.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P62491.
    Bgeei P62491.
    CleanExi HS_RAB11A.
    Genevestigatori P62491.

    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 a human homolog of the Schizosaccharomyces pombe ras-like gene YPT-3."
      Drivas G.T., Shih A., Coutavas E.E., D'Eustachio P., Rush M.G.
      Oncogene 6:3-9(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. Zahraoui A., Joberty G., Tavitian A.
      Submitted (NOV-1990) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Human rab11a: transcription, chromosome mapping and effect on the expression levels of host GTP-binding proteins."
      Gromov P.S., Celis J.E., Hansen C., Tommerup N., Gromova I., Madsen P.
      FEBS Lett. 429:359-364(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. "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] (ISOFORM 1).
      Tissue: Brain.
    5. "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] (ISOFORM 1).
    6. "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] (ISOFORM 1).
    7. "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] (ISOFORMS 1 AND 2).
      Tissue: Brain.
    8. "Analysis of the DNA sequence and duplication history of human chromosome 15."
      Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
      , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
      Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. "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] (ISOFORM 1).
      Tissue: Brain.
    11. Bienvenut W.V.
      Submitted (OCT-2005) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-24; 34-58; 62-72; 75-95 AND 133-140, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT GLY-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: B-cell lymphoma and Platelet.
    12. Cited for: INTERACTION WITH RAB11FIP1; RAB11FIP2; RAB11FIP3 AND RAB11FIP4.
    13. "Rab11-FIP4 interacts with Rab11 in a GTP-dependent manner and its overexpression condenses the Rab11 positive compartment in HeLa cells."
      Wallace D.M., Lindsay A.J., Hendrick A.G., McCaffrey M.W.
      Biochem. Biophys. Res. Commun. 299:770-779(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RAB11FIP4.
    14. Cited for: INTERACTION WITH RAB11FIP4.
      Tissue: Cervix carcinoma.
    15. "Rab11-FIP2 functions in transferrin recycling and associates with endosomal membranes via its COOH-terminal domain."
      Lindsay A.J., McCaffrey M.W.
      J. Biol. Chem. 277:27193-27199(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    16. "Characterisation of the Rab binding properties of Rab coupling protein (RCP) by site-directed mutagenesis."
      Lindsay A.J., McCaffrey M.W.
      FEBS Lett. 571:86-92(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RAB11FIP1.
    17. "Molecular characterization of Rab11 interactions with members of the family of Rab11-interacting proteins."
      Junutula J.R., Schonteich E., Wilson G.M., Peden A.A., Scheller R.H., Prekeris R.
      J. Biol. Chem. 279:33430-33437(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RAB11FIP2.
    18. "The C2 domains of the class I Rab11 family of interacting proteins target recycling vesicles to the plasma membrane."
      Lindsay A.J., McCaffrey M.W.
      J. Cell Sci. 117:4365-4375(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    19. Cited for: INTERACTION WITH RAB11FIP1, SUBCELLULAR LOCATION.
    20. "Rab11-FIP3 and FIP4 interact with Arf6 and the exocyst to control membrane traffic in cytokinesis."
      Fielding A.B., Schonteich E., Matheson J., Wilson G., Yu X., Hickson G.R., Srivastava S., Baldwin S.A., Prekeris R., Gould G.W.
      EMBO J. 24:3389-3399(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RAB11FIP3 AND RAB11FIP4.
    21. "The FIP3-Rab11 protein complex regulates recycling endosome targeting to the cleavage furrow during late cytokinesis."
      Wilson G.M., Fielding A.B., Simon G.C., Yu X., Andrews P.D., Hames R.S., Frey A.M., Peden A.A., Gould G.W., Prekeris R.
      Mol. Biol. Cell 16:849-860(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RAB11FIP3 AND RAB11FIP4, MUTAGENESIS OF SER-25.
    22. "Rab11 in recycling endosomes regulates the sorting and basolateral transport of E-cadherin."
      Lock J.G., Stow J.L.
      Mol. Biol. Cell 16:1744-1755(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF SER-25 AND GLN-70.
    23. "Protrudin induces neurite formation by directional membrane trafficking."
      Shirane M., Nakayama K.I.
      Science 314:818-821(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ZFYVE27.
    24. "Myosin Vb is required for trafficking of the cystic fibrosis transmembrane conductance regulator in Rab11a-specific apical recycling endosomes in polarized human airway epithelial cells."
      Swiatecka-Urban A., Talebian L., Kanno E., Moreau-Marquis S., Coutermarsh B., Hansen K., Karlson K.H., Barnaby R., Cheney R.E., Langford G.M., Fukuda M., Stanton B.A.
      J. Biol. Chem. 282:23725-23736(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MYO5B, IDENTIFICATION IN A COMPLEX WITH MYO5B AND CFTR.
    25. Cited for: INTERACTION WITH RAB11FIP3 AND EVI5.
    26. "Final stages of cytokinesis and midbody ring formation are controlled by BRUCE."
      Pohl C., Jentsch S.
      Cell 132:832-845(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BIRC6/BRUCE.
    27. "Requirement of myosin Vb.Rab11a.Rab11-FIP2 complex in cholesterol-regulated translocation of NPC1L1 to the cell surface."
      Chu B.-B., Ge L., Xie C., Zhao Y., Miao H.-H., Wang J., Li B.-L., Song B.-L.
      J. Biol. Chem. 284:22481-22490(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH NPC1L1, MUTAGENESIS OF SER-25.
    28. "A molecular network for de novo generation of the apical surface and lumen."
      Bryant D.M., Datta A., Rodriguez-Fraticelli A.E., Peraenen J., Martin-Belmonte F., Mostov K.E.
      Nat. Cell Biol. 12:1035-1045(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    29. Cited for: INTERACTION WITH VIPAS39.
    30. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    31. "Rab GTPase-Myo5B complexes control membrane recycling and epithelial polarization."
      Roland J.T., Bryant D.M., Datta A., Itzen A., Mostov K.E., Goldenring J.R.
      Proc. Natl. Acad. Sci. U.S.A. 108:2789-2794(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MYO5B.
    32. "Rab GTPases regulating phagosome maturation are differentially recruited to mycobacterial phagosomes."
      Seto S., Tsujimura K., Koide Y.
      Traffic 12:407-420(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    33. "TBC1D14 regulates autophagosome formation via Rab11- and ULK1-positive recycling endosomes."
      Longatti A., Lamb C.A., Razi M., Yoshimura S., Barr F.A., Tooze S.A.
      J. Cell Biol. 197:659-675(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TBC1D14.
    34. "UNC119a bridges the transmission of Fyn signals to Rab11, leading to the completion of cytokinesis."
      Lee Y., Chung S., Baek I.K., Lee T.H., Paik S.Y., Lee J.
      Cell Cycle 12:1303-1315(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH UNC119.
    35. "Large-scale top down proteomics of the human proteome: membrane proteins, mitochondria, and senescence."
      Catherman A.D., Durbin K.R., Ahlf D.R., Early B.P., Fellers R.T., Tran J.C., Thomas P.M., Kelleher N.L.
      Mol. Cell. Proteomics 12:3465-3473(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ISOPRENYLATION AT CYS-212 AND CYS-213, IDENTIFICATION BY MASS SPECTROMETRY.
    36. "Structural basis of family-wide Rab GTPase recognition by rabenosyn-5."
      Eathiraj S., Pan X., Ritacco C., Lambright D.G.
      Nature 436:415-419(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 8-175 IN COMPLEX WITH GTP ANALOG.
    37. "Crystallographic evidence for substrate-assisted GTP hydrolysis by a small GTP binding protein."
      Pasqualato S., Cherfils J.
      Structure 13:533-540(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-173 IN COMPLEX WITH GTP ANALOG AND GDP, MUTAGENESIS OF GLN-70.
    38. "Structural basis for Rab11-mediated recruitment of FIP3 to recycling endosomes."
      Eathiraj S., Mishra A., Prekeris R., Lambright D.G.
      J. Mol. Biol. 364:121-135(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 6-175 IN COMPLEX WITH GTP AND RAB11FIP3, MUTAGENESIS OF GLN-70.
    39. "Structural basis for Rab11-dependent membrane recruitment of a family of Rab11-interacting protein 3 (FIP3)/Arfophilin-1."
      Shiba T., Koga H., Shin H.-W., Kawasaki M., Kato R., Nakayama K., Wakatsuki S.
      Proc. Natl. Acad. Sci. U.S.A. 103:15416-15421(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 7-173 IN COMPLEX WITH GTP, INTERACTION WITH RAB11FIP3 AND RAB11FIP4, MUTAGENESIS OF GLN-70.
    40. "Crystal structure of rab11 in complex with rab11 family interacting protein 2."
      Jagoe W.N., Lindsay A.J., Read R.J., McCoy A.J., McCaffrey M.W., Khan A.R.
      Structure 14:1273-1283(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.44 ANGSTROMS) OF 1-173 IN COMPLEX WITH GTP, INTERACTION WITH RAB11FIP2, MUTAGENESIS OF GLN-70.

    Entry informationi

    Entry nameiRB11A_HUMAN
    AccessioniPrimary (citable) accession number: P62491
    Secondary accession number(s): B2R4B6
    , B4DT13, P24410, Q5TZN9, Q9JLX1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2004
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 129 of the entry and version 3 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 15
      Human chromosome 15: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3