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P62330 (ARF6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ADP-ribosylation factor 6
Gene names
Name:ARF6
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length175 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.9 Ref.13 Ref.17 Ref.22 Ref.29 Ref.30 Ref.34

Enzyme regulation

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. Ref.10 Ref.22

Subunit structure

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. Ref.11 Ref.12 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.20 Ref.21 Ref.23 Ref.25 Ref.27 Ref.30 Ref.32 Ref.33 Ref.34 Ref.35 Ref.36

Subcellular location

Golgi apparatus. Cell membrane; Lipid-anchor. Endosome membrane; Lipid-anchor. Recycling endosome membrane; Lipid-anchor Probable. 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. Ref.9 Ref.13 Ref.17 Ref.19 Ref.21 Ref.24 Ref.25 Ref.27

Tissue specificity

Ubiquitous, with higher levels in heart, substantia nigra, and kidney. Ref.2

Sequence similarities

Belongs to the small GTPase superfamily. Arf family.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Differentiation
ER-Golgi transport
Neurogenesis
Protein transport
Transport
   Cellular componentCell membrane
Cell projection
Cytoplasm
Endosome
Golgi apparatus
Membrane
   LigandGTP-binding
Nucleotide-binding
   PTMLipoprotein
Myristate
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGTP catabolic process

Traceable author statement Ref.1. Source: GOC

cell adhesion

Traceable author statement PubMed 10036235. Source: UniProtKB

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cell division

Inferred from electronic annotation. Source: UniProtKB-KW

cellular component movement

Traceable author statement PubMed 10036235. Source: UniProtKB

cortical actin cytoskeleton organization

Inferred from mutant phenotype PubMed 10913182. Source: UniProtKB

establishment of epithelial cell polarity

Inferred from electronic annotation. Source: Ensembl

hepatocyte apoptotic process

Inferred from electronic annotation. Source: Ensembl

liver development

Inferred from electronic annotation. Source: Ensembl

myeloid cell apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of receptor-mediated endocytosis

Traceable author statement PubMed 9312003. Source: UniProtKB

positive regulation of actin filament polymerization

Inferred from mutant phenotype PubMed 10036235. Source: UniProtKB

positive regulation of establishment of protein localization to plasma membrane

Inferred from sequence or structural similarity. Source: BHF-UCL

protein localization to cell surface

Inferred from sequence or structural similarity. Source: BHF-UCL

protein localization to endosome

Inferred from mutant phenotype Ref.27. Source: UniProtKB

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of Rac protein signal transduction

Inferred from direct assay PubMed 10036235. Source: UniProtKB

regulation of dendritic spine development

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of filopodium assembly

Inferred from direct assay Ref.13. Source: UniProtKB

ruffle organization

Inferred from direct assay PubMed 10036235. Source: UniProtKB

small GTPase mediated signal transduction

Inferred from electronic annotation. Source: InterPro

vesicle-mediated transport

Traceable author statement PubMed 10913182. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: UniProtKB-SubCell

cell cortex

Inferred from direct assay PubMed 10913182. Source: UniProtKB

cleavage furrow

Inferred from electronic annotation. Source: UniProtKB-SubCell

early endosome

Inferred from electronic annotation. Source: Ensembl

endocytic vesicle

Inferred from direct assay Ref.24. Source: UniProtKB

endosome

Inferred from direct assay Ref.25. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

filopodium membrane

Inferred from direct assay Ref.13. Source: UniProtKB

membrane

Traceable author statement PubMed 8702973. Source: ProtInc

midbody

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay PubMed 10036235Ref.19Ref.24. Source: UniProtKB

recycling endosome membrane

Inferred from direct assay Ref.27. Source: UniProtKB

ruffle

Inferred from direct assay PubMed 9312003. Source: UniProtKB

   Molecular_functionGTP binding

Traceable author statement PubMed 10913182. Source: UniProtKB

GTPase activity

Traceable author statement Ref.1. Source: ProtInc

thioesterase binding

Inferred from physical interaction Ref.12. Source: UniProtKB

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 175174ADP-ribosylation factor 6
PRO_0000207400

Regions

Nucleotide binding23 – 286GTP
Nucleotide binding41 – 444GTP
Nucleotide binding63 – 675GTP
Nucleotide binding122 – 1254GTP
Nucleotide binding155 – 1562GTP

Amino acid modifications

Lipidation21N-myristoyl glycine Ref.9

Experimental info

Mutagenesis21G → A: Fails to associate with membranes. Ref.9
Mutagenesis271T → N: Fails to associate with membranes. Does not inhibit filopodia formation. Ref.13 Ref.17 Ref.19
Mutagenesis671Q → L: Inhibits filopodia formation and dendritic branching. Ref.13 Ref.17

Secondary structure

.................................... 175
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P62330 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 49E38E59AEA52B98

FASTA17520,082
        10         20         30         40         50         60 
MGKVLSKIFG NKEMRILMLG LDAAGKTTIL YKLKLGQSVT TIPTVGFNVE TVTYKNVKFN 

        70         80         90        100        110        120 
VWDVGGQDKI RPLWRHYYTG TQGLIFVVDC ADRDRIDEAR QELHRIINDR EMRDAIILIF 

       130        140        150        160        170 
ANKQDLPDAM KPHEIQEKLG LTRIRDRNWY VQPSCATSGD GLYEGLTWLT SNYKS 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Molecular characterization of Rab11-FIP3 binding to ARF GTPases."
Schonteich E., Pilli M., Simon G.C., Matern H.T., Junutula J.R., Sentz D., Holmes R.K., Prekeris R.
Eur. J. Cell Biol. 86:417-431(2007) [PubMed] [Europe PMC] [Abstract]
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]"TBC1D24, an ARF6-interacting protein, is mutated in familial infantile myoclonic epilepsy."
Falace A., Filipello F., La Padula V., Vanni N., Madia F., De Pietri Tonelli D., de Falco F.A., Striano P., Dagna Bricarelli F., Minetti C., Benfenati F., Fassio A., Zara F.
Am. J. Hum. Genet. 87:365-370(2010) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"The structural GDP/GTP cycle of human Arf6."
Pasqualato S., Menetrey J., Franco M., Cherfils J.
EMBO Rep. 2:234-238(2001) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRB23741.
RefSeqNP_001654.1. NM_001663.3.
UniGeneHs.525330.
Hs.719973.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1E0SX-ray2.28A2-175[»]
2A5DX-ray1.80A2-174[»]
2A5FX-ray2.02A2-174[»]
2A5GX-ray2.66A2-174[»]
2BAONMR-A2-11[»]
2BAUNMR-A2-11[»]
2J5XX-ray2.80A/B1-175[»]
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[»]
ProteinModelPortalP62330.
SMRP62330. Positions 12-174.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106877. 41 interactions.
DIPDIP-33352N.
IntActP62330. 16 interactions.
MINTMINT-4824639.
STRING9606.ENSP00000298316.

Chemistry

ChEMBLCHEMBL5987.

PTM databases

PhosphoSiteP62330.

Polymorphism databases

DMDM51316984.

Proteomic databases

PaxDbP62330.
PeptideAtlasP62330.
PRIDEP62330.

Protocols and materials databases

DNASU382.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000298316; ENSP00000298316; ENSG00000165527.
GeneID382.
KEGGhsa:382.
UCSCuc001wxg.4. human.

Organism-specific databases

CTD382.
GeneCardsGC14P050359.
HGNCHGNC:659. ARF6.
HPACAB002778.
MIM600464. gene.
neXtProtNX_P62330.
PharmGKBPA24942.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1100.
HOGENOMHOG000163691.
HOVERGENHBG002073.
InParanoidP62330.
KOK07941.
OMATELHRII.
OrthoDBEOG7F5133.
PhylomeDBP62330.
TreeFamTF300808.

Enzyme and pathway databases

SignaLinkP62330.

Gene expression databases

BgeeP62330.
CleanExHS_ARF6.
GenevestigatorP62330.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR024156. Small_GTPase_ARF.
IPR006689. Small_GTPase_ARF/SAR.
[Graphical view]
PfamPF00025. Arf. 1 hit.
[Graphical view]
PRINTSPR00328. SAR1GTPBP.
SMARTSM00177. ARF. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51417. ARF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP62330.
GeneWikiARF6.
GenomeRNAi382.
NextBio1599.
PROP62330.
SOURCESearch...

Entry information

Entry nameARF6_HUMAN
AccessionPrimary (citable) accession number: P62330
Secondary accession number(s): P26438, Q6FGZ2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM