CPLM-008083

Genbank Nucleotide ID

Carbonyl reductase [NADPH] 1

Protein Synonyms/Alias

15-hydroxyprostaglandin dehydrogenase [NADP(+)]; NADPH-dependent carbonyl reductase 1; Prostaglandin 9-ketoreductase; Prostaglandin-E(2) 9-reductase

Mus musculus (Mouse)

Position	Peptide	Type	References
15	ALVTGANKGIGFAIT	ubiquitination	[1]
28	ITRDLCRKFSGDVVL	acetylation	[2]
28	ITRDLCRKFSGDVVL	ubiquitination	[1]
49	RGQTAVQKLQAEGLS	ubiquitination	[1]
123	FGTRDVCKELLPLIK	acetylation	[3, 4]
123	FGTRDVCKELLPLIK	ubiquitination	[1]
157	CRLELQQKFRSETIT	acetylation	[4, 5]
157	CRLELQQKFRSETIT	succinylation	[5]
157	CRLELQQKFRSETIT	ubiquitination	[1]
272	HGQFVQDKKVEPW**	ubiquitination	[1]

[1] 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]
[2] 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]
[3] 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]
[4] 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]
[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

NADPH-dependent reductase with broad substrate specificity. Catalyzes the reduction of a wide variety of carbonyl compounds including quinones, prostaglandins, menadione, plus various xenobiotics. Catalyzes the reduction of the antitumor anthracyclines doxorubicin and daunorubicin to the cardiotoxic compounds doxorubicinol and daunorubicinol. Can convert prostaglandin E2 to prostaglandin F2-alpha. Can bind glutathione, which explains its higher affinity for glutathione-conjugated substrates. Catalyzes the reduction of S-nitrosoglutathione (By similarity).

NP_BIND 10 34 NADP (By similarity).
NP_BIND 63 64 NADP (By similarity).
NP_BIND 194 198 NADP (By similarity).
NP_BIND 231 233 NADP (By similarity).
REGION 95 97 Glutathione binding (By similarity).
REGION 193 194 Glutathione binding (By similarity).
ACT_SITE 194 194 Proton acceptor (By similarity).
BINDING 90 90 NADP; via carbonyl oxygen (By
BINDING 106 106 Glutathione (By similarity).
BINDING 140 140 Substrate (By similarity).
MOD_RES 2 2 N-acetylserine (By similarity).

Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; NADP; Oxidoreductase; Reference proteome.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO:0047021; F:15-hydroxyprostaglandin dehydrogenase (NADP+) activity; IEA:EC.
GO:0004090; F:carbonyl reductase (NADPH) activity; ISS:UniProtKB.
GO:0050221; F:prostaglandin-E2 9-reductase activity; IEA:EC.
GO:0017144; P:drug metabolic process; ISS:UniProtKB.
GO:0042373; P:vitamin K metabolic process; ISS:UniProtKB.

IPR002198; DH_sc/Rdtase_SDR.
IPR002347; Glc/ribitol_DH.
IPR016040; NAD(P)-bd_dom.
IPR020904; Sc_DH/Rdtase_CS.

PR00081; GDHRDH.
PR00080; SDRFAMILY.