CPLM-010791

Genbank Nucleotide ID

Sorbitol dehydrogenase

Protein Synonyms/Alias

L-iditol 2-dehydrogenase

Homo sapiens (Human)

Position	Peptide	Type	References
6	**MAAAAKPNNLSLV	acetylation	[1]
6	**MAAAAKPNNLSLV	ubiquitination	[2]
64	IGNFIVKKPMVLGHE	ubiquitination	[2, 3]
78	EASGTVEKVGSSVKH	ubiquitination	[2]
84	EKVGSSVKHLKPGDR	ubiquitination	[2]
107	RENDEFCKMGRYNLS	ubiquitination	[2, 4]
134	GNLCRFYKHNAAFCY	ubiquitination	[2]
226	DLVLQISKESPQEIA	ubiquitination	[3]
295	AIREVDIKGVFRYCN	ubiquitination	[2]
319	ASKSVNVKPLVTHRF	ubiquitination	[3]
339	LEAFETFKKGLGLKI	ubiquitination	[3]
340	EAFETFKKGLGLKIM	ubiquitination	[2]
349	LGLKIMLKCDPSDQN	ubiquitination	[2, 4]

[1] Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome.
Morselli E, Mariño G, Bennetzen MV, Eisenberg T, Megalou E, Schroeder S, Cabrera S, Bénit P, Rustin P, Criollo A, Kepp O, Galluzzi L, Shen S, Malik SA, Maiuri MC, Horio Y, López-Otín C, Andersen JS, Tavernarakis N, Madeo F, Kroemer G.
J Cell Biol. 2011 Feb 21;192(4):615-29. [PMID: 21339330]
[2] 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]
[3] 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]
[4] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]

Functional Description

Converts sorbitol to fructose. Part of the polyol pathway that plays an important role in sperm physiology. May play a role in the sperm motility by providing an energetic source for sperm (By similarity).

METAL 45 45 Zinc; catalytic.
METAL 70 70 Zinc; catalytic.
METAL 71 71 Zinc; catalytic.
BINDING 51 51 Substrate (By similarity).
BINDING 156 156 Substrate (By similarity).
BINDING 299 299 Substrate (By similarity).
BINDING 300 300 Substrate (By similarity).
MOD_RES 2 2 N-acetylalanine.

3D-structure; Acetylation; Cell projection; Cilium; Complete proteome; Direct protein sequencing; Flagellum; Membrane; Metal-binding; Mitochondrion; NAD; Oxidoreductase; Polymorphism; Reference proteome; Zinc.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005615; C:extracellular space; TAS:UniProtKB.
GO:0016020; C:membrane; IDA:UniProtKB.
GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
GO:0031514; C:motile cilium; ISS:UniProtKB.
GO:0030246; F:carbohydrate binding; NAS:UniProtKB.
GO:0003939; F:L-iditol 2-dehydrogenase activity; IDA:UniProtKB.
GO:0051287; F:NAD binding; IDA:UniProtKB.
GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO:0046370; P:fructose biosynthetic process; IDA:UniProtKB.
GO:0006006; P:glucose metabolic process; TAS:UniProtKB.
GO:0051160; P:L-xylitol catabolic process; IDA:UniProtKB.
GO:0006062; P:sorbitol catabolic process; IDA:UniProtKB.
GO:0030317; P:sperm motility; ISS:UniProtKB.

IPR013149; ADH_C.
IPR013154; ADH_GroES-like.
IPR002085; ADH_SF_Zn-type.
IPR002328; ADH_Zn_CS.
IPR011032; GroES-like.
IPR016040; NAD(P)-bd_dom.

PF08240; ADH_N
PF00107; ADH_zinc_N