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P62330

- ARF6_HUMAN

UniProt

P62330 - ARF6_HUMAN

Protein

ADP-ribosylation factor 6

Gene

ARF6

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    GTP-binding protein involved in protein trafficking that regulates endocytic recycling and cytoskeleton remodeling. Required for normal completion of mitotic cytokinesis. Plays a role in the reorganization of the actin cytoskeleton and the formation of stress fibers. May also modulate vesicle budding and uncoating within the Golgi apparatus. Involved in the regulation of dendritic spine development, contributing to the regulation of dendritic branching and filopodia extension. Functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase.7 Publications

    Enzyme regulationi

    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). Activated by ASAP3. Inactivated by ACAP1 and ACAP2.2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi23 – 286GTP5 Publications
    Nucleotide bindingi41 – 444GTP5 Publications
    Nucleotide bindingi63 – 675GTP5 Publications
    Nucleotide bindingi122 – 1254GTP5 Publications
    Nucleotide bindingi155 – 1562GTP5 Publications

    GO - Molecular functioni

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

    GO - Biological processi

    1. cell adhesion Source: UniProtKB
    2. cell cycle Source: UniProtKB-KW
    3. cell division Source: UniProtKB-KW
    4. cellular component movement Source: UniProtKB
    5. cortical actin cytoskeleton organization Source: UniProtKB
    6. establishment of epithelial cell polarity Source: Ensembl
    7. GTP catabolic process Source: GOC
    8. hepatocyte apoptotic process Source: Ensembl
    9. liver development Source: Ensembl
    10. myeloid cell apoptotic process Source: Ensembl
    11. negative regulation of receptor-mediated endocytosis Source: UniProtKB
    12. positive regulation of actin filament polymerization Source: UniProtKB
    13. positive regulation of establishment of protein localization to plasma membrane Source: BHF-UCL
    14. protein localization to cell surface Source: BHF-UCL
    15. protein localization to endosome Source: UniProtKB
    16. protein transport Source: UniProtKB-KW
    17. regulation of dendritic spine development Source: UniProtKB
    18. regulation of filopodium assembly Source: UniProtKB
    19. regulation of Rac protein signal transduction Source: UniProtKB
    20. ruffle organization Source: UniProtKB
    21. small GTPase mediated signal transduction Source: InterPro
    22. vesicle-mediated transport Source: UniProtKB

    Keywords - Biological processi

    Cell cycle, Cell division, Differentiation, ER-Golgi transport, Neurogenesis, Protein transport, Transport

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    SignaLinkiP62330.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ADP-ribosylation factor 6
    Gene namesi
    Name:ARF6
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:659. ARF6.

    Subcellular locationi

    Golgi apparatus. Cell membrane; Lipid-anchor. Endosome membrane; Lipid-anchor. Recycling endosome membrane Curated; Lipid-anchor Curated. Cell projectionfilopodium membrane; Lipid-anchor. Midbody By similarity. Cytoplasm By similarity. Cleavage furrow By similarity
    Note: Distributed throughout the cytoplasm during metaphase. Transiently detected at the ingressing cleavage furrow during mitotic cytokinesis. Recruited to the midbody at later stages of cytokinesis; this requires interaction with KIF23 By similarity. Recruited to the cell membrane in association with CYTH2 and ARL4C. Colocalizes with DAB2IP at the plasma membrane and endocytic vesicles.By similarity

    GO - Cellular componenti

    1. cell cortex Source: UniProtKB
    2. cleavage furrow Source: UniProtKB-SubCell
    3. early endosome Source: Ensembl
    4. endocytic vesicle Source: UniProtKB
    5. endosome Source: UniProtKB
    6. extracellular vesicular exosome Source: UniProt
    7. filopodium membrane Source: UniProtKB
    8. Golgi apparatus Source: UniProtKB-SubCell
    9. membrane Source: UniProtKB
    10. midbody Source: UniProtKB-SubCell
    11. plasma membrane Source: UniProtKB
    12. recycling endosome membrane Source: UniProtKB
    13. ruffle Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Cytoplasm, Endosome, Golgi apparatus, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi2 – 21G → A: Fails to associate with membranes. 1 Publication
    Mutagenesisi27 – 271T → N: Fails to associate with membranes. Does not inhibit filopodia formation. 3 Publications
    Mutagenesisi67 – 671Q → L: Inhibits filopodia formation and dendritic branching. 2 Publications

    Organism-specific databases

    PharmGKBiPA24942.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed
    Chaini2 – 175174ADP-ribosylation factor 6PRO_0000207400Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycine1 Publication

    Keywords - PTMi

    Lipoprotein, Myristate

    Proteomic databases

    MaxQBiP62330.
    PaxDbiP62330.
    PeptideAtlasiP62330.
    PRIDEiP62330.

    PTM databases

    PhosphoSiteiP62330.

    Expressioni

    Tissue specificityi

    Ubiquitous, with higher levels in heart, substantia nigra, and kidney.1 Publication

    Gene expression databases

    BgeeiP62330.
    CleanExiHS_ARF6.
    GenevestigatoriP62330.

    Organism-specific databases

    HPAiCAB002778.

    Interactioni

    Subunit structurei

    Interacts with ARHGAP21, ASAP2, ASAP3, HERC1, PIP5K1C and UACA. The interaction with ASAP3 is stabilized by calcium ions. Interacts with NCS1/FREQ at the plasma membrane. Interacts with RAB11FIP3 and RAB11FIP4. Interacts with USP6 (via Rab-GAP TBC domain). Interacts with ECM29. Interacts with TBC1D24. Interacts with MICALL1. Interacts with KIF23, forming heterodimers and heterotetramers. Interacts with GGA1 and RAB11FIP4. Interacts with SPAG9 homodimers, forming heterotetramers. Interacts with CYTH3. Interacts with EspG from enteropathogenic E.coli. Identified in a complex with RAB1A and EspG from enteropathogenic E.coli. Interacts with the V.cholerae enterotoxin subunit A1; this causes a conformation change so that the toxin can bind NAD and catalyze the ADP-ribosylation of Gs alpha.20 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ARFIP2P533654EBI-638181,EBI-638194
    ATP6V1C1P212834EBI-638181,EBI-988663
    KIF23Q0224123EBI-638181,EBI-306852
    SPAG9O602718EBI-638181,EBI-1023301

    Protein-protein interaction databases

    BioGridi106877. 41 interactions.
    DIPiDIP-33352N.
    IntActiP62330. 16 interactions.
    MINTiMINT-4824639.
    STRINGi9606.ENSP00000298316.

    Structurei

    Secondary structure

    1
    175
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 97
    Beta strandi13 – 197
    Helixi26 – 3510
    Beta strandi39 – 446
    Beta strandi45 – 5410
    Beta strandi57 – 648
    Helixi65 – 673
    Helixi68 – 7710
    Turni78 – 803
    Beta strandi83 – 897
    Helixi93 – 953
    Helixi96 – 10712
    Helixi110 – 1123
    Beta strandi116 – 1227
    Beta strandi125 – 1284
    Helixi132 – 1387
    Helixi141 – 1433
    Beta strandi149 – 1535
    Turni156 – 1594
    Helixi162 – 17211

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1E0SX-ray2.28A2-175[»]
    2A5DX-ray1.80A1-175[»]
    2A5FX-ray2.02A1-175[»]
    2A5GX-ray2.66A1-175[»]
    2BAONMR-A2-11[»]
    2BAUNMR-A2-11[»]
    2J5XX-ray2.80A/B2-175[»]
    2W83X-ray1.93A/B/E13-175[»]
    3LVQX-ray3.38E11-175[»]
    3LVRX-ray3.38E11-175[»]
    3N5CX-ray1.82A/B14-175[»]
    3PCRX-ray2.50B14-175[»]
    4FMEX-ray4.10C/F14-173[»]
    4KAXX-ray1.85A14-173[»]
    ProteinModelPortaliP62330.
    SMRiP62330. Positions 12-174.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP62330.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the small GTPase superfamily. Arf family.Curated

    Phylogenomic databases

    eggNOGiCOG1100.
    HOGENOMiHOG000163691.
    HOVERGENiHBG002073.
    InParanoidiP62330.
    KOiK07941.
    OMAiRFNVWDV.
    OrthoDBiEOG7F5133.
    PhylomeDBiP62330.
    TreeFamiTF300808.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR027417. P-loop_NTPase.
    IPR005225. Small_GTP-bd_dom.
    IPR024156. Small_GTPase_ARF.
    IPR006689. Small_GTPase_ARF/SAR.
    [Graphical view]
    PfamiPF00025. Arf. 1 hit.
    [Graphical view]
    PRINTSiPR00328. SAR1GTPBP.
    SMARTiSM00177. ARF. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR00231. small_GTP. 1 hit.
    PROSITEiPS51417. ARF. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P62330-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGKVLSKIFG NKEMRILMLG LDAAGKTTIL YKLKLGQSVT TIPTVGFNVE    50
    TVTYKNVKFN VWDVGGQDKI RPLWRHYYTG TQGLIFVVDC ADRDRIDEAR 100
    QELHRIINDR EMRDAIILIF ANKQDLPDAM KPHEIQEKLG LTRIRDRNWY 150
    VQPSCATSGD GLYEGLTWLT SNYKS 175
    Length:175
    Mass (Da):20,082
    Last modified:January 23, 2007 - v2
    Checksum:i49E38E59AEA52B98
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M57763 mRNA. Translation: AAA90928.1.
    AY296206 Genomic DNA. Translation: AAP50257.1.
    AF047432 mRNA. Translation: AAC39877.1.
    AF493885 mRNA. Translation: AAM12599.1.
    AK313790 mRNA. Translation: BAG36527.1.
    CR541964 mRNA. Translation: CAG46762.1.
    CH471078 Genomic DNA. Translation: EAW65740.1.
    BC002952 mRNA. No translation available.
    BC008918 mRNA. Translation: AAH08918.1.
    CCDSiCCDS9695.1.
    PIRiB23741.
    RefSeqiNP_001654.1. NM_001663.3.
    UniGeneiHs.525330.
    Hs.719973.

    Genome annotation databases

    EnsembliENST00000298316; ENSP00000298316; ENSG00000165527.
    GeneIDi382.
    KEGGihsa:382.
    UCSCiuc001wxg.4. human.

    Polymorphism databases

    DMDMi51316984.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M57763 mRNA. Translation: AAA90928.1 .
    AY296206 Genomic DNA. Translation: AAP50257.1 .
    AF047432 mRNA. Translation: AAC39877.1 .
    AF493885 mRNA. Translation: AAM12599.1 .
    AK313790 mRNA. Translation: BAG36527.1 .
    CR541964 mRNA. Translation: CAG46762.1 .
    CH471078 Genomic DNA. Translation: EAW65740.1 .
    BC002952 mRNA. No translation available.
    BC008918 mRNA. Translation: AAH08918.1 .
    CCDSi CCDS9695.1.
    PIRi B23741.
    RefSeqi NP_001654.1. NM_001663.3.
    UniGenei Hs.525330.
    Hs.719973.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1E0S X-ray 2.28 A 2-175 [» ]
    2A5D X-ray 1.80 A 1-175 [» ]
    2A5F X-ray 2.02 A 1-175 [» ]
    2A5G X-ray 2.66 A 1-175 [» ]
    2BAO NMR - A 2-11 [» ]
    2BAU NMR - A 2-11 [» ]
    2J5X X-ray 2.80 A/B 2-175 [» ]
    2W83 X-ray 1.93 A/B/E 13-175 [» ]
    3LVQ X-ray 3.38 E 11-175 [» ]
    3LVR X-ray 3.38 E 11-175 [» ]
    3N5C X-ray 1.82 A/B 14-175 [» ]
    3PCR X-ray 2.50 B 14-175 [» ]
    4FME X-ray 4.10 C/F 14-173 [» ]
    4KAX X-ray 1.85 A 14-173 [» ]
    ProteinModelPortali P62330.
    SMRi P62330. Positions 12-174.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106877. 41 interactions.
    DIPi DIP-33352N.
    IntActi P62330. 16 interactions.
    MINTi MINT-4824639.
    STRINGi 9606.ENSP00000298316.

    Chemistry

    ChEMBLi CHEMBL5987.

    PTM databases

    PhosphoSitei P62330.

    Polymorphism databases

    DMDMi 51316984.

    Proteomic databases

    MaxQBi P62330.
    PaxDbi P62330.
    PeptideAtlasi P62330.
    PRIDEi P62330.

    Protocols and materials databases

    DNASUi 382.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000298316 ; ENSP00000298316 ; ENSG00000165527 .
    GeneIDi 382.
    KEGGi hsa:382.
    UCSCi uc001wxg.4. human.

    Organism-specific databases

    CTDi 382.
    GeneCardsi GC14P050359.
    HGNCi HGNC:659. ARF6.
    HPAi CAB002778.
    MIMi 600464. gene.
    neXtProti NX_P62330.
    PharmGKBi PA24942.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1100.
    HOGENOMi HOG000163691.
    HOVERGENi HBG002073.
    InParanoidi P62330.
    KOi K07941.
    OMAi RFNVWDV.
    OrthoDBi EOG7F5133.
    PhylomeDBi P62330.
    TreeFami TF300808.

    Enzyme and pathway databases

    SignaLinki P62330.

    Miscellaneous databases

    EvolutionaryTracei P62330.
    GeneWikii ARF6.
    GenomeRNAii 382.
    NextBioi 1599.
    PROi P62330.
    SOURCEi Search...

    Gene expression databases

    Bgeei P62330.
    CleanExi HS_ARF6.
    Genevestigatori P62330.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR027417. P-loop_NTPase.
    IPR005225. Small_GTP-bd_dom.
    IPR024156. Small_GTPase_ARF.
    IPR006689. Small_GTPase_ARF/SAR.
    [Graphical view ]
    Pfami PF00025. Arf. 1 hit.
    [Graphical view ]
    PRINTSi PR00328. SAR1GTPBP.
    SMARTi SM00177. ARF. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR00231. small_GTP. 1 hit.
    PROSITEi PS51417. ARF. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular identification of ADP-ribosylation factor mRNAs and their expression in mammalian cells."
      Tsuchiya M., Price S.R., Tsai S.-C., Moss J., Vaughan M.
      J. Biol. Chem. 266:2772-2777(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Sequence, genomic organization, and expression of the human ADP-ribosylation factor 6 (ARF6) gene: a class III ARF."
      Lebeda R.A., Johnson S.K., Stewart M.I., Haun R.S.
      DNA Cell Biol. 22:737-741(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
    3. "Identification of genes expressed in human CD34(+) hematopoietic stem/progenitor cells by expressed sequence tags and efficient full-length cDNA cloning."
      Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H., He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H., Wang Y.-X., Chen S.-J., Chen Z.
      Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Umbilical cord blood.
    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 (MAR-2002) to the EMBL/GenBank/DDBJ databases
      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].
      Tissue: Trachea.
    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].
    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: Skin and Uterus.
    9. "Myristoylation is required for the intracellular localization and endocytic function of ARF6."
      D'Souza-Schorey C., Stahl P.D.
      Exp. Cell Res. 221:153-159(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: MYRISTOYLATION AT GLY-2, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF GLY-2.
    10. "ACAPs are arf6 GTPase-activating proteins that function in the cell periphery."
      Jackson T.R., Brown F.D., Nie Z., Miura K., Foroni L., Sun J., Hsu V.W., Donaldson J.G., Randazzo P.A.
      J. Cell Biol. 151:627-638(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
      Tissue: Leukocyte.
    11. "ARF6 stimulates clathrin/AP-2 recruitment to synaptic membranes by activating phosphatidylinositol phosphate kinase type Igamma."
      Krauss M., Kinuta M., Wenk M.R., De Camilli P., Takei K., Haucke V.
      J. Cell Biol. 162:113-124(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PIP5K1C.
    12. "The TBC (Tre-2/Bub2/Cdc16) domain protein TRE17 regulates plasma membrane-endosomal trafficking through activation of Arf6."
      Martinu L., Masuda-Robens J.M., Robertson S.E., Santy L.C., Casanova J.E., Chou M.M.
      Mol. Cell. Biol. 24:9752-9762(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH USP6.
    13. "Regulation of dendritic branching and filopodia formation in hippocampal neurons by specific acylated protein motifs."
      Gauthier-Campbell C., Bredt D.S., Murphy T.H., El-Husseini A.
      Mol. Biol. Cell 15:2205-2217(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF THR-27 AND GLN-67.
    14. "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.
    15. "Requirement of phosphatidylinositol-4,5-bisphosphate for HERC1-mediated guanine nucleotide release from ARF proteins."
      Garcia-Gonzalo F.R., Bartrons R., Ventura F., Rosa J.L.
      FEBS Lett. 579:343-348(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HERC1.
    16. "Golgi-localized GAP for Cdc42 functions downstream of ARF1 to control Arp2/3 complex and F-actin dynamics."
      Dubois T., Paleotti O., Mironov A.A. Jr., Fraisier V., Stradal T.E.B., De Matteis M.A., Franco M., Chavrier P.
      Nat. Cell Biol. 7:353-364(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ARHGAP21.
    17. "Proteomic identification and functional characterization of a novel ARF6 GTPase-activating protein, ACAP4."
      Fang Z., Miao Y., Ding X., Deng H., Liu S., Wang F., Zhou R., Watson C., Fu C., Hu Q., Lillard J.W. Jr., Powell M., Chen Y., Forte J.G., Yao X.
      Mol. Cell. Proteomics 5:1437-1449(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF THR-27 AND GLN-67, INTERACTION WITH ASAP3.
    18. "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: INTERACTION WITH RAB11FIP3 AND RAB11FIP4.
    19. "The Arl4 family of small G proteins can recruit the cytohesin Arf6 exchange factors to the plasma membrane."
      Hofmann I., Thompson A., Sanderson C.M., Munro S.
      Curr. Biol. 17:711-716(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF THR-27, SUBCELLULAR LOCATION.
    20. Cited for: INTERACTION WITH RAB11FIP3.
    21. "Specificity, promiscuity and localization of ARF protein interactions with NCS-1 and phosphatidylinositol-4 kinase-III beta."
      Haynes L.P., Sherwood M.W., Dolman N.J., Burgoyne R.D.
      Traffic 8:1080-1092(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NCS1, SUBCELLULAR LOCATION.
    22. "ASAP3 is a focal adhesion-associated Arf GAP that functions in cell migration and invasion."
      Ha V.L., Bharti S., Inoue H., Vass W.C., Campa F., Nie Z., de Gramont A., Ward Y., Randazzo P.A.
      J. Biol. Chem. 283:14915-14926(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION.
    23. Cited for: INTERACTION WITH TBC1D24.
    24. "AIP1 functions as Arf6-GAP to negatively regulate TLR4 signaling."
      Wan T., Liu T., Zhang H., Tang S., Min W.
      J. Biol. Chem. 285:3750-3757(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    25. "A protein interaction network for Ecm29 links the 26 S proteasome to molecular motors and endosomal components."
      Gorbea C., Pratt G., Ustrell V., Bell R., Sahasrabudhe S., Hughes R.E., Rechsteiner M.
      J. Biol. Chem. 285:31616-31633(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH ECM29.
    26. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. "MICAL-L1 is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a."
      Rahajeng J., Giridharan S.S., Cai B., Naslavsky N., Caplan S.
      Traffic 13:82-93(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MICALL1, SUBCELLULAR LOCATION.
    28. "Structure of Arf6-GDP suggests a basis for guanine nucleotide exchange factors specificity."
      Menetrey J., Macia E., Pasqualato S., Franco M., Cherfils J.
      Nat. Struct. Biol. 7:466-469(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) IN COMPLEX WITH GDP.
    29. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH GTP ANALOG, FUNCTION.
    30. "Structural basis for the activation of cholera toxin by human ARF6-GTP."
      O'Neal C.J., Jobling M.G., Holmes R.K., Hol W.G.
      Science 309:1093-1096(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH GTP AND V.CHOLERAE ENTEROTOXIN SUBUNIT A1, SUBUNIT, FUNCTION.
    31. "NMR structural studies of the myristoylated N-terminus of ADP ribosylation factor 6 (Arf6)."
      Gizachew D., Oswald R.
      FEBS Lett. 580:4296-4301(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 2-11.
    32. "The structural basis of Arf effector specificity: the crystal structure of ARF6 in a complex with JIP4."
      Isabet T., Montagnac G., Regazzoni K., Raynal B., El Khadali F., England P., Franco M., Chavrier P., Houdusse A., Menetrey J.
      EMBO J. 28:2835-2845(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 13-175 IN COMPLEX WITH GTP AND SPAG9, INTERACTION WITH SPAG9.
    33. "The structure of an Arf-ArfGAP complex reveals a Ca2+ regulatory mechanism."
      Ismail S.A., Vetter I.R., Sot B., Wittinghofer A.
      Cell 141:812-821(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.38 ANGSTROMS) OF 11-175 IN COMPLEX WITH GDP ASAP3 AND CALCIUM IONS, INTERACTION WITH ASAP3.
    34. "The assembly of a GTPase-kinase signalling complex by a bacterial catalytic scaffold."
      Selyunin A.S., Sutton S.E., Weigele B.A., Reddick L.E., Orchard R.C., Bresson S.M., Tomchick D.R., Alto N.M.
      Nature 469:107-111(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 14-175 IN COMPLEX WITH GTP AND E.COLI ESPG, FUNCTION, SUBUNIT.
    35. "Structurally distinct bacterial TBC-like GAPs link Arf GTPase to Rab1 inactivation to counteract host defenses."
      Dong N., Zhu Y., Lu Q., Hu L., Zheng Y., Shao F.
      Cell 150:1029-1041(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (4.10 ANGSTROMS) OF 14-173 IN COMPLEX WITH GTP; RAB1A AND E.COLI ESPG, SUBUNIT.
    36. "Structural basis for membrane recruitment and allosteric activation of cytohesin family Arf GTPase exchange factors."
      Malaby A.W., van den Berg B., Lambright D.G.
      Proc. Natl. Acad. Sci. U.S.A. 110:14213-14218(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 14-173 IN COMPLEX WITH CYTH3 AND GTP, SUBUNIT.

    Entry informationi

    Entry nameiARF6_HUMAN
    AccessioniPrimary (citable) accession number: P62330
    Secondary accession number(s): P26438, Q6FGZ2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 5, 2004
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 124 of the entry and version 2 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, Reference proteome

    Documents

    1. Human chromosome 14
      Human chromosome 14: 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