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Protein

ADP-ribosylation factor 6

Gene

ARF6

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

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

  • GTPase activity Source: ProtInc
  • GTP binding Source: UniProtKB
  • thioesterase binding Source: UniProtKB

GO - Biological processi

  • cell adhesion Source: UniProtKB
  • cell cycle Source: UniProtKB-KW
  • cell division Source: UniProtKB-KW
  • cortical actin cytoskeleton organization Source: UniProtKB
  • establishment of epithelial cell polarity Source: Ensembl
  • hepatocyte apoptotic process Source: Ensembl
  • liver development Source: Ensembl
  • metabolic process Source: GOC
  • movement of cell or subcellular component Source: UniProtKB
  • myeloid cell apoptotic process Source: Ensembl
  • negative regulation of receptor-mediated endocytosis Source: UniProtKB
  • positive regulation of actin filament polymerization Source: UniProtKB
  • positive regulation of establishment of protein localization to plasma membrane Source: BHF-UCL
  • protein localization to cell surface Source: BHF-UCL
  • protein localization to endosome Source: UniProtKB
  • protein transport Source: UniProtKB-KW
  • regulation of dendritic spine development Source: UniProtKB
  • regulation of filopodium assembly Source: UniProtKB
  • regulation of Rac protein signal transduction Source: UniProtKB
  • ruffle organization Source: UniProtKB
  • small GTPase mediated signal transduction Source: InterPro
  • vesicle-mediated transport Source: UniProtKB
Complete GO annotation...

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 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:659. ARF6.

Subcellular locationi

GO - Cellular componenti

  • cell cortex Source: UniProtKB
  • cleavage furrow Source: UniProtKB-SubCell
  • early endosome Source: Ensembl
  • endocytic vesicle Source: UniProtKB
  • endosome Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • filopodium membrane Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • Golgi apparatus Source: UniProtKB-SubCell
  • membrane Source: UniProtKB
  • midbody Source: UniProtKB-SubCell
  • plasma membrane Source: UniProtKB
  • recycling endosome membrane Source: UniProtKB
  • ruffle Source: UniProtKB
Complete GO annotation...

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.

Polymorphism and mutation databases

BioMutaiARF6.
DMDMi51316984.

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.
GenevisibleiP62330. HS.

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. 47 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 – 97Combined sources
Beta strandi13 – 197Combined sources
Helixi26 – 3510Combined sources
Beta strandi39 – 446Combined sources
Beta strandi45 – 5410Combined sources
Beta strandi57 – 648Combined sources
Helixi65 – 673Combined sources
Helixi68 – 7710Combined sources
Turni78 – 803Combined sources
Beta strandi83 – 897Combined sources
Helixi93 – 953Combined sources
Helixi96 – 10712Combined sources
Helixi110 – 1123Combined sources
Beta strandi116 – 1227Combined sources
Beta strandi125 – 1284Combined sources
Helixi132 – 1387Combined sources
Helixi141 – 1433Combined sources
Beta strandi149 – 1535Combined sources
Turni156 – 1594Combined sources
Helixi162 – 17211Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00780000121855.
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

        10         20         30         40         50
MGKVLSKIFG NKEMRILMLG LDAAGKTTIL YKLKLGQSVT TIPTVGFNVE
60 70 80 90 100
TVTYKNVKFN VWDVGGQDKI RPLWRHYYTG TQGLIFVVDC ADRDRIDEAR
110 120 130 140 150
QELHRIINDR EMRDAIILIF ANKQDLPDAM KPHEIQEKLG LTRIRDRNWY
160 170
VQPSCATSGD GLYEGLTWLT SNYKS
Length:175
Mass (Da):20,082
Last modified:January 23, 2007 - v2
Checksum:i49E38E59AEA52B98
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi106877. 47 interactions.
DIPiDIP-33352N.
IntActiP62330. 16 interactions.
MINTiMINT-4824639.
STRINGi9606.ENSP00000298316.

Chemistry

ChEMBLiCHEMBL5987.

PTM databases

PhosphoSiteiP62330.

Polymorphism and mutation databases

BioMutaiARF6.
DMDMi51316984.

Proteomic databases

MaxQBiP62330.
PaxDbiP62330.
PeptideAtlasiP62330.
PRIDEiP62330.

Protocols and materials databases

DNASUi382.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi382.
GeneCardsiGC14P050359.
HGNCiHGNC:659. ARF6.
HPAiCAB002778.
MIMi600464. gene.
neXtProtiNX_P62330.
PharmGKBiPA24942.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00780000121855.
HOGENOMiHOG000163691.
HOVERGENiHBG002073.
InParanoidiP62330.
KOiK07941.
OMAiRFNVWDV.
OrthoDBiEOG7F5133.
PhylomeDBiP62330.
TreeFamiTF300808.

Enzyme and pathway databases

SignaLinkiP62330.

Miscellaneous databases

EvolutionaryTraceiP62330.
GeneWikiiARF6.
GenomeRNAii382.
NextBioi1599.
PROiP62330.
SOURCEiSearch...

Gene expression databases

BgeeiP62330.
CleanExiHS_ARF6.
GenevisibleiP62330. HS.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  29. "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.
  30. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH GTP ANALOG, FUNCTION.
  31. "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.
  32. "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.
  33. "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.
  34. "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.
  35. "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.
  36. "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.
  37. "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: June 24, 2015
This is version 131 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.