CPLM-017483

Genbank Nucleotide ID

ADP-ribosylation factor GTPase-activating protein 1

Protein Synonyms/Alias

ARF GAP 1; ADP-ribosylation factor 1 GTPase-activating protein; ARF1 GAP; ARF1-directed GTPase-activating protein

Homo sapiens (Human)

Position	Peptide	Type	References
74	WKDIELEKMKAGGNA	ubiquitination	[1]
102	PCWSLQEKYNSRAAA	ubiquitination	[1]
114	AAALFRDKVVALAEG	ubiquitination	[1]
231	AAKEGATKFGSQASQ	acetylation	[2]
231	AAKEGATKFGSQASQ	ubiquitination	[1]
278	GVSQLASKVQGVGSK	ubiquitination	[1, 3, 4, 5]
285	KVQGVGSKGWRDVTT	ubiquitination	[1]

[1] 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]
[2] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
[3] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
[4] 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]
[5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
Chen Z, Zhou Y, Song J, Zhang Z.
Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]

Functional Description

GTPase-activating protein (GAP) for the ADP ribosylation factor 1 (ARF1). Involved in membrane trafficking and /or vesicle transport. Promotes hydrolysis of the ARF1-bound GTP and thus, is required for the dissociation of coat proteins from Golgi-derived membranes and vesicles, a prerequisite for vesicle's fusion with target compartment. Probably regulates ARF1-mediated transport via its interaction with the KDELR proteins and TMED2. Overexpression induces the redistribution of the entire Golgi complex to the endoplasmic reticulum, as when ARF1 is deactivated. Its activity is stimulated by phosphoinosides and inhibited by phosphatidylcholine (By similarity).

DOMAIN 7 124 Arf-GAP.
ZN_FING 22 45 C4-type.
MOD_RES 135 135 Phosphothreonine.
MOD_RES 189 189 Phosphothreonine.
MOD_RES 231 231 N6-acetyllysine.
MOD_RES 304 304 Phosphoserine.
MOD_RES 343 343 Phosphoserine (By similarity).
MOD_RES 345 345 Phosphoserine (By similarity).
MOD_RES 348 348 Phosphoserine (By similarity).
MOD_RES 361 361 Phosphoserine (By similarity).

3D-structure; Acetylation; Alternative splicing; Complete proteome; Cytoplasm; ER-Golgi transport; Golgi apparatus; GTPase activation; Metal-binding; Phosphoprotein; Polymorphism; Protein transport; Reference proteome; Transport; Zinc; Zinc-finger.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005829; C:cytosol; TAS:Reactome.
GO:0005783; C:endoplasmic reticulum; IDA:HPA.
GO:0030660; C:Golgi-associated vesicle membrane; TAS:Reactome.
GO:0031965; C:nuclear membrane; IDA:HPA.
GO:0005886; C:plasma membrane; IDA:HPA.
GO:0045202; C:synapse; IEA:Compara.
GO:0008060; F:ARF GTPase activator activity; IEA:InterPro.
GO:0005096; F:GTPase activator activity; IDA:MGI.
GO:0008270; F:zinc ion binding; IEA:InterPro.
GO:0006987; P:activation of signaling protein activity involved in unfolded protein response; TAS:Reactome.
GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO:0048205; P:COPI coating of Golgi vesicle; TAS:Reactome.
GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO:0032312; P:regulation of ARF GTPase activity; IEA:InterPro.
GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; TAS:Reactome.

PR00405; REVINTRACTNG.