CPLM-005666

Genbank Nucleotide ID

ATP-binding cassette sub-family D member 3

Protein Synonyms/Alias

70 kDa peroxisomal membrane protein; PMP70

Homo sapiens (Human)

Position	Peptide	Type	References
39	ALGLHGKKSGKPPLQ	ubiquitination	[1]
61	KERAVVDKVFFSRLI	ubiquitination	[1, 2]
72	SRLIQILKIMVPRTF	ubiquitination	[3]
174	LQAFTYYKMGNLDNR	ubiquitination	[1]
253	RLRRPIGKMTITEQK	ubiquitination	[1]
260	KMTITEQKYEGEYRY	acetylation	[4]
260	KMTITEQKYEGEYRY	ubiquitination	[1, 2, 5]
286	IAFYNGNKREKQTVH	ubiquitination	[1, 3, 5]
347	LSHPRHLKSTHSELL	ubiquitination	[1, 2, 5]
399	TELMQVLKDLNHGKY	acetylation	[4]
399	TELMQVLKDLNHGKY	ubiquitination	[1]
405	LKDLNHGKYERTMVS	ubiquitination	[1]
535	GREDQKRKGISDLVL	ubiquitination	[1]
543	GISDLVLKEYLDNVQ	ubiquitination	[1]
576	DVLSGGEKQRMAMAR	ubiquitination	[1, 5]

[1] 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]
[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] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
[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] 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

Probable transporter. The nucleotide-binding fold acts as an ATP-binding subunit with ATPase activity.

DOMAIN 85 372 ABC transmembrane type-1.
DOMAIN 440 659 ABC transporter.
NP_BIND 473 480 ATP (Potential).
REGION 2 199 Interaction with PEX19.
REGION 2 124 Targeting to peroxisomes.
MOD_RES 260 260 N6-acetyllysine.
MOD_RES 399 399 N6-acetyllysine.
CARBOHYD 12 12 N-linked (GlcNAc...) (Potential).
CARBOHYD 106 106 N-linked (GlcNAc...) (Potential).
CARBOHYD 206 206 N-linked (GlcNAc...) (Potential).

Acetylation; Alternative splicing; ATP-binding; Complete proteome; Glycoprotein; Membrane; Nucleotide-binding; Peroxisome; Polymorphism; Reference proteome; Transmembrane; Transmembrane helix; Transport.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005829; C:cytosol; TAS:Reactome.
GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
GO:0005743; C:mitochondrial inner membrane; IEA:Compara.
GO:0005782; C:peroxisomal matrix; IDA:UniProtKB.
GO:0005778; C:peroxisomal membrane; IDA:UniProtKB.
GO:0005524; F:ATP binding; IDA:UniProtKB.
GO:0016887; F:ATPase activity; IDA:UniProtKB.
GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IEA:InterPro.
GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO:0006635; P:fatty acid beta-oxidation; IGI:UniProtKB.
GO:0007031; P:peroxisome organization; IDA:UniProtKB.
GO:0055085; P:transmembrane transport; TAS:Reactome.
GO:0042760; P:very long-chain fatty acid catabolic process; IGI:UniProtKB.

IPR003593; AAA+_ATPase.
IPR010509; ABC_Ald_N.
IPR003439; ABC_transporter-like.
IPR017871; ABC_transporter_CS.
IPR017940; ABC_transporter_type1.
IPR011527; ABC_transptrTM_dom_typ1.
IPR005283; FA_transporter.
IPR027417; P-loop_NTPase.

PF06472; ABC_membrane_2
PF00005; ABC_tran

PS50929; ABC_TM1F
PS00211; ABC_TRANSPORTER_1
PS50893; ABC_TRANSPORTER_2