CPLM-017594

Genbank Nucleotide ID

ATPase family AAA domain-containing protein 1

Protein Synonyms/Alias

Homo sapiens (Human)

Position	Peptide	Type	References
46	DAIDPTRKQKVEAQK	ubiquitination	[1]
112	DTVILPIKKKHLFEN	ubiquitination	[1, 2, 3]
114	VILPIKKKHLFENSR	acetylation	[4]
114	VILPIKKKHLFENSR	ubiquitination	[5]
127	SRLLQPPKGVLLYGP	ubiquitination	[5]
139	YGPPGCGKTLIAKAT	ubiquitination	[5]
144	CGKTLIAKATAKEAG	ubiquitination	[5]
165	QPSTLTDKWYGESQK	ubiquitination	[3, 5]
263	HINQPALKQREAILK	ubiquitination	[1, 2, 3, 5, 6, 7]
270	KQREAILKLILKNEN	ubiquitination	[1, 2]
274	AILKLILKNENVDRH	ubiquitination	[3, 5]
300	GFSGSDLKEMCRDAA	ubiquitination	[5]
347	IEKMKKSKDAAFQNV	ubiquitination	[5]

[1] 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]
[2] 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]
[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] 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]
[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]
[7] 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]

Functional Description

ATPase that plays a critical role in regulating the surface expression of AMPA receptors (AMPAR), thereby regulating synaptic plasticity and learning and memory. Required for NMDA- stimulated AMPAR internalization and inhibition of GRIA1 and GRIA2 recycling back to the plasma membrane; these activities are ATPase-dependent (By similarity).

NP_BIND 133 140 ATP (Potential).
MOD_RES 322 322 Phosphoserine (By similarity).
CROSSLNK 46 46 Glycyl lysine isopeptide (Lys-Gly)

Alternative splicing; ATP-binding; Cell junction; Cell membrane; Complete proteome; Hydrolase; Isopeptide bond; Membrane; Nucleotide-binding; Peroxisome; Phosphoprotein; Polymorphism; Postsynaptic cell membrane; Reference proteome; Synapse; Ubl conjugation.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO:0005739; C:mitochondrion; IEA:Compara.
GO:0005778; C:peroxisomal membrane; IDA:UniProtKB.
GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
GO:0045211; C:postsynaptic membrane; ISS:UniProtKB.
GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO:0016887; F:ATPase activity; ISS:UniProtKB.
GO:0007612; P:learning; ISS:UniProtKB.
GO:0007613; P:memory; ISS:UniProtKB.
GO:0051967; P:negative regulation of synaptic transmission, glutamatergic; ISS:UniProtKB.
GO:0002092; P:positive regulation of receptor internalization; ISS:UniProtKB.

IPR003593; AAA+_ATPase.
IPR003959; ATPase_AAA_core.
IPR003960; ATPase_AAA_CS.
IPR027417; P-loop_NTPase.