CPLM-016837

Genbank Nucleotide ID

Aflatoxin B1 aldehyde reductase member 2

Protein Synonyms/Alias

Succinic semialdehyde reductase; SSA reductase

Mus musculus (Mouse)

Position	Peptide	Type	References
120	KANPWEGKSLKPDSI	acetylation	[1]
120	KANPWEGKSLKPDSI	ubiquitination	[2]
123	PWEGKSLKPDSIRSQ	acetylation	[1, 3]
136	SQLETSLKRLQCPRV	acetylation	[1, 4]
244	AGGLLTGKYKYEDKD	acetylation	[5]
244	AGGLLTGKYKYEDKD	succinylation	[5]
244	AGGLLTGKYKYEDKD	ubiquitination	[2]
246	GLLTGKYKYEDKDGK	acetylation	[1]
250	GKYKYEDKDGKQPVG	acetylation	[1, 4]
253	KYEDKDGKQPVGRFF	acetylation	[1]
286	EAIALVEKALQTTYG	acetylation	[1, 3]

[1] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
[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]
[3] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
[4] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
[5] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]

Functional Description

Catalyzes the NADPH-dependent reduction of succinic semialdehyde to gamma-hydroxybutyrate. May have an important role in producing the neuromodulator gamma-hydroxybutyrate (GHB). Has broad substrate specificity. Can reduce the dialdehyde protein- binding form of aflatoxin B1 (AFB1) to the non-binding AFB1 dialcohol. May be involved in protection of liver against the toxic and carcinogenic effects of AFB1, a potent hepatocarcinogen (By similarity).

NP_BIND 179 180 NADP.
NP_BIND 234 244 NADP.
NP_BIND 326 334 NADP.
ACT_SITE 85 85 Proton donor.
BINDING 80 80 NADP.
BINDING 149 149 Substrate.
BINDING 205 205 NADP.
BINDING 258 258 NADP.
BINDING 268 268 Substrate.
BINDING 271 271 Substrate.
BINDING 367 367 Substrate.
MOD_RES 40 40 Phosphoserine.
MOD_RES 48 48 Phosphothreonine.

3D-structure; Complete proteome; Cytoplasm; Golgi apparatus; NADP; Oxidoreductase; Phosphoprotein; Reference proteome.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
GO:0005739; C:mitochondrion; IDA:MGI.
GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; IEA:Compara.
GO:0019119; F:phenanthrene-9,10-epoxide hydrolase activity; IEA:Compara.
GO:0044597; P:daunorubicin metabolic process; IEA:Compara.
GO:0044598; P:doxorubicin metabolic process; IEA:Compara.

IPR001395; Aldo/ket_red.
IPR023210; NADP_OxRdtase_dom.

PF00248; Aldo_ket_red