CPLM-020208

Genbank Nucleotide ID

3-hydroxybutyrate dehydrogenase type 2

Protein Synonyms/Alias

Dehydrogenase/reductase SDR family member 6; Oxidoreductase UCPA; R-beta-hydroxybutyrate dehydrogenase

DHRS6; UNQ6308/PRO20933

Homo sapiens (Human)

Position	Peptide	Type	References
32	AFAREGAKVIATDIN	ubiquitination	[1]
42	ATDINESKLQELEKY	ubiquitination	[1]
48	SKLQELEKYPGIQTR	acetylation	[2]
48	SKLQELEKYPGIQTR	ubiquitination	[1, 3, 4, 5, 6]
124	LPKMLAQKSGNIINM	ubiquitination	[1]
159	AAVIGLTKSVAADFI	ubiquitination	[1, 3, 6]

[1] 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]
[2] 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]
[3] 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]
[4] 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]
[5] 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]
[6] 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]

Functional Description

Dehydrogenase that mediates the formation of 2,5- dihydroxybenzoic acid (2,5-DHBA), a siderophore that shares structural similarities with bacterial enterobactin and associates with LCN2, thereby playing a key role in iron homeostasis and transport. Also acts as a 3-hydroxybutyrate dehydrogenase (By similarity).

NP_BIND 10 37 NAD.
NP_BIND 180 184 NAD.
ACT_SITE 147 147 Proton acceptor (By similarity).
BINDING 58 58 NAD.
BINDING 144 144 Substrate (Probable).
BINDING 151 151 NAD.
BINDING 188 188 Substrate (Probable).
BINDING 205 205 Substrate (Probable).

3D-structure; Alternative splicing; Complete proteome; Cytoplasm; NAD; Oxidoreductase; Polymorphism; Reference proteome.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005737; C:cytoplasm; IDA:HGNC.
GO:0003858; F:3-hydroxybutyrate dehydrogenase activity; IDA:HGNC.
GO:0051287; F:NAD binding; IDA:HGNC.
GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; ISS:UniProtKB.
GO:0006635; P:fatty acid beta-oxidation; IDA:HGNC.
GO:0042168; P:heme metabolic process; ISS:UniProtKB.
GO:0055072; P:iron ion homeostasis; ISS:UniProtKB.
GO:0019290; P:siderophore biosynthetic 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.