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Q15907

- RB11B_HUMAN

UniProt

Q15907 - RB11B_HUMAN

Protein

Ras-related protein Rab-11B

Gene

RAB11B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 4 (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 plays a role in endocytic recycling, regulating apical recycling of several transmembrane proteins including cystic fibrosis transmembrane conductance regulator/CFTR, epithelial sodium channel/ENaC, potassium voltage-gated channel, and voltage-dependent L-type calcium channel. May also regulate constitutive and regulated secretion, like insulin granule exocytosis. Required for melanosome transport and release from melanocytes. Also regulates V-ATPase intracellular transport in response to extracellular acidosis.6 Publications

    Regions

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

    GO - Molecular functioni

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

    GO - Biological processi

    1. cellular response to acidic pH Source: UniProtKB
    2. constitutive secretory pathway Source: UniProtKB
    3. GTP catabolic process Source: GOC
    4. insulin secretion involved in cellular response to glucose stimulus Source: UniProtKB
    5. melanosome transport Source: UniProtKB
    6. protein transport Source: InterPro
    7. receptor recycling Source: UniProtKB
    8. regulated secretory pathway Source: UniProtKB
    9. regulation of anion transport Source: UniProtKB
    10. regulation of endocytic recycling Source: UniProtKB
    11. regulation of protein localization to cell surface Source: UniProtKB
    12. retrograde transport, endosome to plasma membrane Source: UniProtKB
    13. small GTPase mediated signal transduction Source: InterPro
    14. transferrin transport Source: UniProtKB

    Keywords - Biological processi

    Protein transport, Transport

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ras-related protein Rab-11B
    Alternative name(s):
    GTP-binding protein YPT3
    Gene namesi
    Name:RAB11B
    Synonyms:YPT3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:9761. RAB11B.

    Subcellular locationi

    Recycling endosome membrane By similarity; Lipid-anchor By similarity; Cytoplasmic side By similarity. Cytoplasmic vesiclesecretory vesiclesynaptic vesicle membrane By similarity; Lipid-anchor By similarity; Cytoplasmic side By similarity. Cytoplasmic vesiclephagosome membrane 1 Publication; Lipid-anchor 1 Publication; Cytoplasmic side 1 Publication
    Note: Recruited to phagosomes containing S.aureus.

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-KW
    2. extracellular vesicular exosome Source: UniProt
    3. mitochondrion Source: Ensembl
    4. phagocytic vesicle Source: UniProtKB
    5. phagocytic vesicle membrane Source: UniProtKB-SubCell
    6. recycling endosome Source: UniProtKB
    7. recycling endosome membrane Source: UniProtKB-SubCell
    8. synaptic vesicle Source: UniProtKB
    9. synaptic vesicle membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cytoplasmic vesicle, Endosome, Membrane, Synapse

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi25 – 251S → N: Dominant negative mutant locked in the inactive GDP-bound form; alters apical recycling. 1 Publication
    Mutagenesisi70 – 701Q → L: Constitutively active mutant locked in the active GTP-bound form; alters apical recycling. 1 Publication

    Organism-specific databases

    PharmGKBiPA34102.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 215214Ras-related protein Rab-11BPRO_0000121158Add
    BLAST
    Propeptidei216 – 2183Removed in mature formSequence AnalysisPRO_0000370815

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylglycine1 Publication
    Modified residuei4 – 41CitrullineBy similarity
    Lipidationi214 – 2141S-geranylgeranyl cysteine1 Publication
    Modified residuei215 – 2151Cysteine methyl esterSequence Analysis
    Lipidationi215 – 2151S-geranylgeranyl cysteine1 Publication

    Post-translational modificationi

    Citrullinated by PADI4.By similarity

    Keywords - PTMi

    Acetylation, Citrullination, Lipoprotein, Methylation, Prenylation

    Proteomic databases

    MaxQBiQ15907.
    PaxDbiQ15907.
    PeptideAtlasiQ15907.
    PRIDEiQ15907.

    PTM databases

    PhosphoSiteiQ15907.

    Expressioni

    Inductioni

    Up-regulated by extracellular acidosis and down-regulated by alkalosis (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiQ15907.
    BgeeiQ15907.
    CleanExiHS_RAB11B.
    GenevestigatoriQ15907.

    Interactioni

    Subunit structurei

    Interacts with KCNMA1 By similarity. Interacts with RAB11FIP1, RAB11FIP2, RAB11FIP3 and RAB11FIP4. May interact with TBC1D14. Interacts with ATP6V1E1.By similarity4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    TBC1D14Q9P2M42EBI-722234,EBI-2797718

    Protein-protein interaction databases

    BioGridi114661. 29 interactions.
    DIPiDIP-50898N.
    IntActiQ15907. 6 interactions.
    STRINGi9606.ENSP00000333547.

    Structurei

    Secondary structure

    1
    218
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi9 – 1911
    Helixi24 – 3310
    Beta strandi47 – 559
    Beta strandi58 – 669
    Helixi70 – 723
    Helixi78 – 814
    Beta strandi85 – 928
    Helixi96 – 1005
    Helixi102 – 11211
    Beta strandi118 – 1247
    Helixi129 – 1313
    Helixi136 – 14510
    Beta strandi149 – 1524
    Turni155 – 1573
    Helixi161 – 17717

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2F9LX-ray1.55A8-205[»]
    2F9MX-ray1.95A8-205[»]
    ProteinModelPortaliQ15907.
    SMRiQ15907. Positions 8-188.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ15907.

    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.
    InParanoidiQ15907.
    KOiK07905.
    OMAiIQVDAKT.
    PhylomeDBiQ15907.
    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: Q15907-1) [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 AFAEKNNLSF 150
    IETSALDSTN VEEAFKNILT EIYRIVSQKQ IADRAAHDES PGNNVVDISV 200
    PPTTDGQKPN KLQCCQNL 218
    Length:218
    Mass (Da):24,489
    Last modified:January 23, 2007 - v4
    Checksum:i8DF146BA39EBD9FF
    GO
    Isoform 2 (identifier: Q15907-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         171-218: EIYRIVSQKQIADRAAHDESPGNNVVDISVPPTTDGQKPNKLQCCQNL → GGRGPDGCG

    Note: No experimental confirmation available.

    Show »
    Length:179
    Mass (Da):19,971
    Checksum:i9D14388D83279277
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti75 – 751A → R in CAA56176. (PubMed:7811277)Curated
    Sequence conflicti116 – 1161N → D in AAV38342. 1 PublicationCurated
    Sequence conflicti154 – 1541S → A in CAG38733. 1 PublicationCurated
    Sequence conflicti184 – 1841R → C in CAG46492. 1 PublicationCurated
    Sequence conflicti216 – 2161Q → R in ABQ59034. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei171 – 21848EIYRI…CCQNL → GGRGPDGCG in isoform 2. 1 PublicationVSP_055832Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X79780 mRNA. Translation: CAA56176.1.
    EF560724 mRNA. Translation: ABQ59034.1.
    AF498947 mRNA. Translation: AAM21095.1.
    AK297498 mRNA. Translation: BAG59912.1.
    AK312994 mRNA. Translation: BAG35831.1.
    BT019535 mRNA. Translation: AAV38342.1.
    BT019536 mRNA. Translation: AAV38343.1.
    CR536494 mRNA. Translation: CAG38733.1.
    CR541691 mRNA. Translation: CAG46492.1.
    AC136469 Genomic DNA. No translation available.
    CH471139 Genomic DNA. Translation: EAW68927.1.
    BC110081 mRNA. Translation: AAI10082.1.
    CCDSiCCDS12201.1.
    PIRiJC2487.
    RefSeqiNP_004209.2. NM_004218.3.
    UniGeneiHs.626404.

    Genome annotation databases

    EnsembliENST00000328024; ENSP00000333547; ENSG00000185236. [Q15907-1]
    ENST00000594216; ENSP00000471148; ENSG00000185236. [Q15907-2]
    GeneIDi9230.
    KEGGihsa:9230.
    UCSCiuc002mju.4. human.

    Polymorphism databases

    DMDMi38258938.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X79780 mRNA. Translation: CAA56176.1 .
    EF560724 mRNA. Translation: ABQ59034.1 .
    AF498947 mRNA. Translation: AAM21095.1 .
    AK297498 mRNA. Translation: BAG59912.1 .
    AK312994 mRNA. Translation: BAG35831.1 .
    BT019535 mRNA. Translation: AAV38342.1 .
    BT019536 mRNA. Translation: AAV38343.1 .
    CR536494 mRNA. Translation: CAG38733.1 .
    CR541691 mRNA. Translation: CAG46492.1 .
    AC136469 Genomic DNA. No translation available.
    CH471139 Genomic DNA. Translation: EAW68927.1 .
    BC110081 mRNA. Translation: AAI10082.1 .
    CCDSi CCDS12201.1.
    PIRi JC2487.
    RefSeqi NP_004209.2. NM_004218.3.
    UniGenei Hs.626404.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2F9L X-ray 1.55 A 8-205 [» ]
    2F9M X-ray 1.95 A 8-205 [» ]
    ProteinModelPortali Q15907.
    SMRi Q15907. Positions 8-188.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114661. 29 interactions.
    DIPi DIP-50898N.
    IntActi Q15907. 6 interactions.
    STRINGi 9606.ENSP00000333547.

    PTM databases

    PhosphoSitei Q15907.

    Polymorphism databases

    DMDMi 38258938.

    Proteomic databases

    MaxQBi Q15907.
    PaxDbi Q15907.
    PeptideAtlasi Q15907.
    PRIDEi Q15907.

    Protocols and materials databases

    DNASUi 9230.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000328024 ; ENSP00000333547 ; ENSG00000185236 . [Q15907-1 ]
    ENST00000594216 ; ENSP00000471148 ; ENSG00000185236 . [Q15907-2 ]
    GeneIDi 9230.
    KEGGi hsa:9230.
    UCSCi uc002mju.4. human.

    Organism-specific databases

    CTDi 9230.
    GeneCardsi GC19P008455.
    HGNCi HGNC:9761. RAB11B.
    MIMi 604198. gene.
    neXtProti NX_Q15907.
    PharmGKBi PA34102.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1100.
    HOGENOMi HOG000233968.
    HOVERGENi HBG009351.
    InParanoidi Q15907.
    KOi K07905.
    OMAi IQVDAKT.
    PhylomeDBi Q15907.
    TreeFami TF300099.

    Miscellaneous databases

    ChiTaRSi RAB11B. human.
    EvolutionaryTracei Q15907.
    GeneWikii RAB11B.
    GenomeRNAii 9230.
    NextBioi 34597.
    PROi Q15907.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15907.
    Bgeei Q15907.
    CleanExi HS_RAB11B.
    Genevestigatori Q15907.

    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. "Molecular cloning of two small GTP-binding proteins from human skeletal muscle."
      Zhu A.X., Zhao Y., Flier J.S.
      Biochem. Biophys. Res. Commun. 205:1875-1882(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Muscle.
    2. Schupp I.
      Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Brain.
    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] (ISOFORM 1).
      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] (ISOFORMS 1 AND 2).
      Tissue: Brain and Cerebellum.
    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 (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    6. "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).
    7. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] (ISOFORM 1).
    10. Bienvenut W.V.
      Submitted (MAR-2005) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-13; 34-51; 62-72; 83-95; 111-125 AND 167-174, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT GLY-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: B-cell lymphoma.
    11. Cited for: INTERACTION WITH RAB11FIP1; RAB11FIP2; RAB11FIP3 AND RAB11FIP4.
    12. "Divergent functions of neuronal Rab11b in Ca2+-regulated versus constitutive exocytosis."
      Khvotchev M.V., Ren M., Takamori S., Jahn R., Suedhof T.C.
      J. Neurosci. 23:10531-10539(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN EXOCYTOSIS.
    13. "Small GTPase determinants for the Golgi processing and plasmalemmal expression of human ether-a-go-go related (hERG) K+ channels."
      Delisle B.P., Underkofler H.A., Moungey B.M., Slind J.K., Kilby J.A., Best J.M., Foell J.D., Balijepalli R.C., Kamp T.J., January C.T.
      J. Biol. Chem. 284:2844-2853(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. "Rab11b regulates the apical recycling of the cystic fibrosis transmembrane conductance regulator in polarized intestinal epithelial cells."
      Silvis M.R., Bertrand C.A., Ameen N., Golin-Bisello F., Butterworth M.B., Frizzell R.A., Bradbury N.A.
      Mol. Biol. Cell 20:2337-2350(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN APICAL RECYCLING, MUTAGENESIS OF SER-25 AND GLN-70.
    15. "Small GTPase Rab11b regulates degradation of surface membrane L-type Cav1.2 channels."
      Best J.M., Foell J.D., Buss C.R., Delisle B.P., Balijepalli R.C., January C.T., Kamp T.J.
      Am. J. Physiol. 300:C1023-C1033(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Rab11b and its effector Rip11 regulate the acidosis-induced traffic of V-ATPase in salivary ducts."
      Oehlke O., Martin H.W., Osterberg N., Roussa E.
      J. Cell. Physiol. 226:638-651(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN V-ATPASE TRANSPORT, INTERACTION WITH ATP6V1E1, INDUCTION.
    18. "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.
    19. "Rab11b regulates the trafficking and recycling of the epithelial sodium channel (ENaC)."
      Butterworth M.B., Edinger R.S., Silvis M.R., Gallo L.I., Liang X., Apodaca G., Frizzell R.A., Fizzell R.A., Johnson J.P.
      Am. J. Physiol. 302:F581-F590(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    20. "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.
    21. "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-214 AND CYS-215, IDENTIFICATION BY MASS SPECTROMETRY.
    22. "The crystal structure of the small GTPase Rab11b reveals critical differences relative to the Rab11a isoform."
      Scapin S.M., Carneiro F.R., Alves A.C., Medrano F.J., Guimaraes B.G., Zanchin N.I.
      J. Struct. Biol. 154:260-268(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 8-205 IN COMPLEX WITH GTP ANALOG AND GDP.

    Entry informationi

    Entry nameiRB11B_HUMAN
    AccessioniPrimary (citable) accession number: Q15907
    Secondary accession number(s): A5YM50
    , B2R7I4, B4DMK0, D6W671, Q2YDT2, Q5U0I1, Q6FHR0, Q6FI42, Q8NI07
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 146 of the entry and version 4 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 19
      Human chromosome 19: 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