UniProt Accession

 SAHH_MOUSE; P50247; Q91WF1 

Genbank Protein ID

 L32836; BC015304 

Genbank Nucleotide ID

 AAA70378.1; AAH15304.1 

Protein Name

 Adenosylhomocysteinase 

Protein Synonyms/Alias

 AdoHcyase; CUBP; Liver copper-binding protein; S-adenosyl-L-homocysteine hydrolase 

Gene Name

 Ahcy 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
8	MSDKLPYKVADIGLA	ubiquitination	[1]
20	GLAAWGRKALDIAEN	ubiquitination	[1]
43	REMYSASKPLKGARI	ubiquitination	[1]
46	YSASKPLKGARIAGC	ubiquitination	[1]
166	TGVHNLYKMMSNGIL	ubiquitination	[1]
174	MMSNGILKVPAINVN	acetylation	[2]
174	MMSNGILKVPAINVN	ubiquitination	[1]
186	NVNDSVTKSKFDNLY	ubiquitination	[1]
188	NDSVTKSKFDNLYGC	acetylation	[3, 4]
188	NDSVTKSKFDNLYGC	ubiquitination	[1]
204	ESLIDGIKRATDVMI	ubiquitination	[1]
226	AGYGDVGKGCAQALR	ubiquitination	[1]
318	LNENAVEKVNIKPQV	acetylation	[3]
318	LNENAVEKVNIKPQV	ubiquitination	[1]
322	AVEKVNIKPQVDRYW	ubiquitination	[1]
331	QVDRYWLKNGRRIIL	acetylation	[4, 5]
331	QVDRYWLKNGRRIIL	ubiquitination	[1]
389	GVHFLPKKLDEAVAE	ubiquitination	[1]
401	VAEAHLGKLNVKLTK	ubiquitination	[1]
405	HLGKLNVKLTKLTEK	ubiquitination	[1]
408	KLNVKLTKLTEKQAQ	acetylation	[4]
412	KLTKLTEKQAQYLGM	ubiquitination	[1]
426	MPINGPFKPDHYRY*	ubiquitination	[1]

Reference

 [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] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405]
 [3] 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]
 [4] 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]
 [5] 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] 

Functional Description

 Adenosylhomocysteine is a competitive inhibitor of S- adenosyl-L-methionine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine. 

Sequence Annotation

 REGION 183 350 NAD binding (By similarity).
 BINDING 57 57 Substrate (By similarity).
 BINDING 131 131 Substrate (By similarity).
 BINDING 156 156 Substrate (By similarity).
 BINDING 186 186 Substrate (By similarity).
 BINDING 190 190 Substrate (By similarity).
 MOD_RES 2 2 N-acetylserine (By similarity).  

Keyword

 Acetylation; Complete proteome; Cytoplasm; Hydrolase; NAD; One-carbon metabolism; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 432 AA 

Protein Sequence

Gene Ontology

 GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
 GO:0004013; F:adenosylhomocysteinase activity; IEA:EC.
 GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW. 

Interpro

 IPR000043; Adenosylhomocysteinase.
 IPR015878; Ado_hCys_hydrolase_NAD-bd.
 IPR016040; NAD(P)-bd_dom.
 IPR020082; S-Ado-L-homoCys_hydrolase_CS. 

Pfam

 PF05221; AdoHcyase
 PF00670; AdoHcyase_NAD 

SMART

 SM00996; AdoHcyase
 SM00997; AdoHcyase_NAD 

PROSITE

 PS00738; ADOHCYASE_1
 PS00739; ADOHCYASE_2 

PRINTS