CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000839
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 ATPase Asna1 
Protein Synonyms/Alias
 Arsenical pump-driving ATPase; Arsenite-stimulated ATPase 
Gene Name
 Asna1 
Gene Synonyms/Alias
 Arsa 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
38IIEQRSLKWIFVGGKacetylation[1]
86ISDAFDQKFSKVPTKubiquitination[2]
Reference
 [1] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [2] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023
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). 
Sequence Annotation
 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 (By similarity).  
Keyword
 Acetylation; ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Endoplasmic reticulum; Hydrolase; Metal-binding; Nucleotide-binding; Nucleus; Reference proteome; Transport; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 348 AA 
Protein Sequence
MAAGVAGWGV EAEEFEDAPD VEPLEPTLSN IIEQRSLKWI FVGGKGGVGK TTCSCSLAVQ 60
LSKGRESVLI ISTDPAHNIS DAFDQKFSKV PTKVKGYDNL FAMEIDPSLG VAELPDEFFE 120
EDNMLSMGKK MMQEAMSAFP GIDEAMSYAE VMRLVKGMNF SVVVFDTAPT GHTLRLLNFP 180
TIVERGLGRL MQIKNQISPF ISQMCNMLGL GDMNADQLAS KLEETLPVIR SVSEQFKDPE 240
QTTFICVCIA EFLSLYETER LIQELAKCKI DTHNIIVNQL VFPDPEKPCK MCEARHKIQA 300
KYLDQMEDLY EDFHIVKLPL LPHEVRGADK VNTFSALLLE PYKPPSTQ 348 
Gene Ontology
 GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
 GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
 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.
 GO:0006810; P:transport; IEA:UniProtKB-KW. 
Interpro
 IPR025723; Anion-transp_ATPase-like_dom.
 IPR016300; ATPase_ArsA/GET3.
 IPR027542; ATPase_ArsA/GET3_euk.
 IPR027417; P-loop_NTPase. 
Pfam
 PF02374; ArsA_ATPase 
SMART
  
PROSITE
  
PRINTS