CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007208
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Adenosylhomocysteinase 
Protein Synonyms/Alias
 AdoHcyase; S-adenosyl-L-homocysteine hydrolase 
Gene Name
 SAH1 
Gene Synonyms/Alias
 YER043C 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
21SLAAFGRKEIELAEHubiquitination[1, 2]
38PGLMAIRKAYGDVQPacetylation[3]
38PGLMAIRKAYGDVQPubiquitination[2]
47YGDVQPLKGARIAGCacetylation[3]
47YGDVQPLKGARIAGCubiquitination[2]
127FAFKDNKKLNLILDDacetylation[4]
177MVKEGKLKVPAINVNubiquitination[2]
189NVNDSVTKSKFDNLYubiquitination[2]
191NDSVTKSKFDNLYGCacetylation[3]
191NDSVTKSKFDNLYGCubiquitination[2]
207ESLVDGIKRATDVMLacetylation[3]
207ESLVDGIKRATDVMLubiquitination[2]
229AGYGDVGKGCAAALRubiquitination[2]
319AWLKANAKECINIKPubiquitination[2]
325AKECINIKPQVDRYLubiquitination[2]
386NDKSFREKHIEFQKTacetylation[3]
413ILDEAVAKFHLGNLGacetylation[3]
413ILDEAVAKFHLGNLGubiquitination[1, 2]
428VRLTKLSKVQSEYLGacetylation[3]
428VRLTKLSKVQSEYLGubiquitination[2]
443IPEEGPFKADHYRY*acetylation[3]
Reference
 [1] Sites of ubiquitin attachment in Saccharomyces cerevisiae.
 Starita LM, Lo RS, Eng JK, von Haller PD, Fields S.
 Proteomics. 2012 Jan;12(2):236-40. [PMID: 22106047]
 [2] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, VillĂ©n J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301]
 [3] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [4] Preparative peptide isoelectric focusing as a tool for improving the identification of lysine-acetylated peptides from complex mixtures.
 Xie H, Bandhakavi S, Roe MR, Griffin TJ.
 J Proteome Res. 2007 May;6(5):2019-26. [PMID: 17397211
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 (By similarity). 
Sequence Annotation
 NP_BIND 160 162 NAD (By similarity).
 NP_BIND 223 228 NAD (By similarity).
 NP_BIND 302 304 NAD (By similarity).
 BINDING 58 58 Substrate (By similarity).
 BINDING 134 134 Substrate (By similarity).
 BINDING 159 159 Substrate (By similarity).
 BINDING 189 189 Substrate (By similarity).
 BINDING 193 193 Substrate (By similarity).
 BINDING 194 194 NAD (By similarity).
 BINDING 246 246 NAD (By similarity).
 BINDING 349 349 NAD (By similarity).
 MOD_RES 393 393 Phosphothreonine.  
Keyword
 Complete proteome; Hydrolase; NAD; One-carbon metabolism; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 449 AA 
Protein Sequence
MSAPAQNYKI ADISLAAFGR KEIELAEHEM PGLMAIRKAY GDVQPLKGAR IAGCLHMTIQ 60
TAVLIETLVA LGAEVTWSSC NIYSTQDHAA AAIAASGVPV FAWKGETEEE YLWCIEQQLF 120
AFKDNKKLNL ILDDGGDLTT LVHEKHPEML EDCFGLSEET TTGVHHLYRM VKEGKLKVPA 180
INVNDSVTKS KFDNLYGCRE SLVDGIKRAT DVMLAGKVAV VAGYGDVGKG CAAALRGMGA 240
RVLVTEIDPI NALQAAMEGY QVVTMEDASH IGQVFVTTTG CRDIINGEHF INMPEDAIVC 300
NIGHFDIEID VAWLKANAKE CINIKPQVDR YLLSSGRHVI LLANGRLVNL GCATGHSSFV 360
MSCSFSNQVL AQIALFKSND KSFREKHIEF QKTGPFEVGV HVLPKILDEA VAKFHLGNLG 420
VRLTKLSKVQ SEYLGIPEEG PFKADHYRY 449 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:SGD.
 GO:0004013; F:adenosylhomocysteinase activity; ISS:SGD.
 GO:0006555; P:methionine metabolic process; NAS:SGD.
 GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
 GO:0016259; P:selenocysteine metabolic process; NAS:SGD. 
Interpro
 IPR000043; Adenosylhomocysteinase.
 IPR015878; Ado_hCys_hydrolase_NAD-bd.
 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