UniProt Accession

 ARF6_HUMAN; P62330; P26438; Q6FGZ2 

Genbank Protein ID

 M57763; AY296206; AF047432; AF493885; AK313790; CR541964; CH471078; BC002952; BC008918 

Genbank Nucleotide ID

 AAA90928.1; AAP50257.1; AAC39877.1; AAM12599.1; BAG36527.1; CAG46762.1; EAW65740.1; AAH08918.1 

Protein Name

 ADP-ribosylation factor 6 

Protein Synonyms/Alias

  

Gene Name

 ARF6 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
7	*MGKVLSKIFGNKEM	ubiquitination	[1]
55	NVETVTYKNVKFNVW	ubiquitination	[2, 3]
58	TVTYKNVKFNVWDVG	ubiquitination	[1, 4]
69	WDVGGQDKIRPLWRH	ubiquitination	[1, 2, 3, 4, 5]
138	KPHEIQEKLGLTRIR	ubiquitination	[1]
174	TWLTSNYKS******	ubiquitination	[6]

Reference

 [1] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [5] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [6] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094] 

Functional Description

 GTP-binding protein involved in protein trafficking; regulates endocytic recycling and cytoskeleton remodeling. May modulate vesicle budding and uncoating within the Golgi apparatus. Functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. Involved in the regulation of dendritic spine development (By similarity). Contributes to the regulation of dendritic branching and filopodia extension. 

Sequence Annotation

 NP_BIND 20 27 GTP (By similarity).
 NP_BIND 63 67 GTP (By similarity).
 NP_BIND 122 125 GTP (By similarity).
 LIPID 2 2 N-myristoyl glycine.  

Keyword

 3D-structure; Cell membrane; Cell projection; Complete proteome; Differentiation; Endosome; ER-Golgi transport; Golgi apparatus; GTP-binding; Lipoprotein; Membrane; Myristate; Neurogenesis; Nucleotide-binding; Protein transport; Reference proteome; Transport. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 175 AA 

Protein Sequence

Gene Ontology

 GO:0005938; C:cell cortex; IDA:UniProtKB.
 GO:0005769; C:early endosome; IEA:Compara.
 GO:0030139; C:endocytic vesicle; IDA:UniProtKB.
 GO:0005768; C:endosome; IDA:UniProtKB.
 GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
 GO:0031527; C:filopodium membrane; IDA:UniProtKB.
 GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
 GO:0055037; C:recycling endosome; IEA:Compara.
 GO:0001726; C:ruffle; IDA:UniProtKB.
 GO:0005525; F:GTP binding; TAS:UniProtKB.
 GO:0003924; F:GTPase activity; TAS:ProtInc.
 GO:0006915; P:apoptotic process; IEA:Compara.
 GO:0007155; P:cell adhesion; TAS:UniProtKB.
 GO:0006928; P:cellular component movement; TAS:UniProtKB.
 GO:0030866; P:cortical actin cytoskeleton organization; IMP:UniProtKB.
 GO:0090162; P:establishment of epithelial cell polarity; IEA:Compara.
 GO:0001889; P:liver development; IEA:Compara.
 GO:0048261; P:negative regulation of receptor-mediated endocytosis; TAS:UniProtKB.
 GO:0030838; P:positive regulation of actin filament polymerization; IMP:UniProtKB.
 GO:0090004; P:positive regulation of establishment of protein localization to plasma membrane; ISS:BHF-UCL.
 GO:0034394; P:protein localization to cell surface; ISS:BHF-UCL.
 GO:0015031; P:protein transport; IEA:UniProtKB-KW.
 GO:0060998; P:regulation of dendritic spine development; ISS:UniProtKB.
 GO:0051489; P:regulation of filopodium assembly; IDA:UniProtKB.
 GO:0035020; P:regulation of Rac protein signal transduction; IDA:UniProtKB.
 GO:0031529; P:ruffle organization; IDA:UniProtKB.
 GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
 GO:0016192; P:vesicle-mediated transport; TAS:UniProtKB. 

Interpro

 IPR027417; P-loop_NTPase.
 IPR005225; Small_GTP-bd_dom.
 IPR024156; Small_GTPase_ARF.
 IPR006689; Small_GTPase_ARF/SAR. 

Pfam

 PF00025; Arf 

SMART

 SM00177; ARF 

PROSITE

 PS51417; ARF 

PRINTS

 PR00328; SAR1GTPBP.