CPLM-000752

Genbank Nucleotide ID

Protein Synonyms/Alias

Arsenical pump-driving ATPase; Arsenite-stimulated ATPase; Transmembrane domain recognition complex 40 kDa ATPase subunit; hARSA-I; hASNA-I

Homo sapiens (Human)

Position	Peptide	Type	References
38	IIEQRSLKWIFVGGK	ubiquitination	[1]
45	KWIFVGGKGGVGKTT	ubiquitination	[1]
50	GGKGGVGKTTCSCSL	ubiquitination	[1, 2]
63	SLAVQLSKGRESVLI	ubiquitination	[1, 3]
86	ISDAFDQKFSKVPTK	ubiquitination	[2, 3]
156	AEVMRLVKGMNFSVV	ubiquitination	[2]
269	IQELAKCKIDTHNII	ubiquitination	[1]
297	KMCEARHKIQAKYLD	ubiquitination	[1]
301	ARHKIQAKYLDQMED	ubiquitination	[1, 3]
317	YEDFHIVKLPLLPHE	ubiquitination	[1, 2, 3, 4]
330	HEVRGADKVNTFSAL	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] 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]
[3] 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]
[4] 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

ATPase required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to the endoplasmic reticulum by membrane-bound receptors, where the tail- anchored protein is released for insertion. This process is regulated by ATP binding and hydrolysis. ATP binding drives the homodimer towards the closed dimer state, facilitating recognition of newly synthesized TA membrane proteins. ATP hydrolysis is required for insertion. Subsequently, the homodimer reverts towards the open dimer state, lowering its affinity for the membrane-bound receptor, and returning it to the cytosol to initiate a new round of targeting (By similarity). May be involved in insulin signaling.

NP_BIND 45 52 ATP (By similarity).
ACT_SITE 74 74 By similarity.
METAL 289 289 Zinc; shared with dimeric partner (By
METAL 292 292 Zinc; shared with dimeric partner (By
BINDING 251 251 ATP (By similarity).
BINDING 278 278 ATP (By similarity).
MOD_RES 2 2 N-acetylalanine.

Acetylation; ATP-binding; Complete proteome; Cytoplasm; Endoplasmic reticulum; Hydrolase; Metal-binding; Nucleotide-binding; Nucleus; Polymorphism; Reference proteome; Transport; Zinc.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005737; C:cytoplasm; TAS:ProtInc.
GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO:0005730; C:nucleolus; TAS:ProtInc.
GO:0015105; F:arsenite transmembrane transporter activity; TAS:ProtInc.
GO:0005524; F:ATP binding; IEA:HAMAP.
GO:0016887; F:ATPase activity; IEA:InterPro.
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO:0006200; P:ATP catabolic process; IEA:GOC.
GO:0045048; P:protein insertion into ER membrane; IEA:HAMAP.

IPR025723; Anion-transp_ATPase-like_dom.
IPR016300; ATPase_ArsA/GET3.
IPR027542; ATPase_ArsA/GET3_euk.
IPR027417; P-loop_NTPase.

PF02374; ArsA_ATPase