CPLM-007663

Genbank Nucleotide ID

Aldehyde dehydrogenase family 3 member B1

Protein Synonyms/Alias

Aldehyde dehydrogenase 7

Homo sapiens (Human)

Position	Peptide	Type	References
41	GRFLQENKQLLHDAL	ubiquitination	[1, 2, 3, 4, 5]
89	MKDERVPKNLATQLD	ubiquitination	[1, 2, 5, 6]
202	IVMTAAAKHLTPVTL	ubiquitination	[3]
214	VTLELGGKNPCYVDD	ubiquitination	[3]
289	LGRIINQKQFQRLRA	ubiquitination	[2, 3, 4, 6, 7]
360	EFINRREKPLALYAF	ubiquitination	[2]
375	SNSSQVVKRVLTQTS	ubiquitination	[1, 3, 4, 5]
437	LRSPGMEKLNALRYP	ubiquitination	[1, 2, 3, 4, 5, 7]

[1] 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]
[2] 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]
[3] 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]
[4] 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]
[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]
[6] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
[7] 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]

Functional Description

Oxidizes medium and long chain saturated and unsaturated aldehydes. Metabolizes also benzaldehyde. Low activity towards acetaldehyde and 3,4-dihydroxyphenylacetaldehyde. May not metabolize short chain aldehydes. May use both NADP(+) and NAD(+) as cofactors. May have a protective role against the cytotoxicity induced by lipid peroxidation.

NP_BIND 188 193 NAD (By similarity).
ACT_SITE 210 210 By similarity.
ACT_SITE 244 244 By similarity.

Alternative splicing; Complete proteome; NAD; Oxidoreductase; Reference proteome.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005737; C:cytoplasm; IDA:MGI.
GO:0004028; F:3-chloroallyl aldehyde dehydrogenase activity; TAS:ProtInc.
GO:0004030; F:aldehyde dehydrogenase [NAD(P)+] activity; IDA:MGI.
GO:0006066; P:alcohol metabolic process; TAS:ProtInc.
GO:0046185; P:aldehyde catabolic process; IDA:MGI.
GO:0034599; P:cellular response to oxidative stress; IDA:MGI.
GO:0006068; P:ethanol catabolic process; IEA:UniProtKB-UniPathway.
GO:0006629; P:lipid metabolic process; TAS:ProtInc.

IPR016161; Ald_DH/histidinol_DH.
IPR016163; Ald_DH_C.
IPR016160; Ald_DH_CS.
IPR016162; Ald_DH_N.
IPR015590; Aldehyde_DH_dom.
IPR012394; Aldehyde_DH_NAD(P).

PS00070; ALDEHYDE_DEHYDR_CYS
PS00687; ALDEHYDE_DEHYDR_GLU