CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-016003
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Putative adenosylhomocysteinase 2 
Protein Synonyms/Alias
 AdoHcyase 2; IP3R-binding protein released with inositol 1,4,5-trisphosphate; S-adenosyl-L-homocysteine hydrolase 2; S-adenosylhomocysteine hydrolase-like protein 1 
Gene Name
 Ahcyl1 
Gene Synonyms/Alias
 Irbit 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
36SFMATVTKAPKKQIQubiquitination[1]
40TVTKAPKKQIQFADDacetylation[2, 3, 4, 5]
40TVTKAPKKQIQFADDubiquitination[1]
100EKQQTNSKGSSNFCVubiquitination[1]
111NFCVKNIKQAEFGRRubiquitination[1]
246KKYPNVFKKIRGIVEacetylation[6]
267HRLYQLSKAGKLCVPubiquitination[1]
487DVYLLPKKMDEYVASubiquitination[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] 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] 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]
 [4] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [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]
 [6] 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] 
Functional Description
  
Sequence Annotation
 NP_BIND 318 322 NAD (By similarity).
 NP_BIND 397 399 NAD (By similarity).
 REGION 65 92 PEST.
 REGION 281 448 NAD binding (By similarity).
 REGION 520 530 PDZ-binding.
 BINDING 155 155 Substrate (By similarity).
 BINDING 229 229 Substrate (By similarity).
 BINDING 254 254 Substrate (By similarity).
 BINDING 284 284 Substrate (By similarity).
 BINDING 288 288 Substrate (By similarity).
 BINDING 341 341 NAD (By similarity).
 BINDING 376 376 NAD (By similarity).
 MOD_RES 2 2 N-acetylserine (By similarity).
 MOD_RES 2 2 Phosphoserine (By similarity).
 MOD_RES 82 82 Phosphothreonine.
 MOD_RES 84 84 Phosphoserine.
 MOD_RES 85 85 Phosphoserine.
 MOD_RES 391 391 Phosphoserine (By similarity).  
Keyword
 Acetylation; Complete proteome; Direct protein sequencing; Endoplasmic reticulum; Hydrolase; NAD; One-carbon metabolism; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 530 AA 
Protein Sequence
MSMPDAMPLP GVGEELKQAK EIEDAEKYSF MATVTKAPKK QIQFADDMQE FTKFPTKTGR 60
RSLSRSISQS STDSYSSAAS YTDSSDDEVS PREKQQTNSK GSSNFCVKNI KQAEFGRREI 120
EIAEQDMSAL ISLRKRAQGE KPLAGAKIVG CTHITAQTAV LIETLCALGA QCRWSACNIY 180
STQNEVAAAL AEAGVAVFAW KGESEDDFWW CIDRCVNMDG WQANMILDDG GDLTHWVYKK 240
YPNVFKKIRG IVEESVTGVH RLYQLSKAGK LCVPAMNVND SVTKQKFDNL YCCRESILDG 300
LKRTTDVMFG GKQVVVCGYG EVGKGCCAAL KALGAIVYIT EIDPICALQA CMDGFRVVKL 360
NEVIRQVDVV ITCTGNKNVV TREHLDRMKN SCIVCNMGHS NTEIDVTSLR TPELTWERVR 420
SQVDHVIWPD GKRVVLLAEG RLLNLSCSTV PTFVLSITAT TQALALIELY NAPEGRYKQD 480
VYLLPKKMDE YVASLHLPSF DAHLTELTDD QAKYLGLNKN GPFKPNYYRY 530 
Gene Ontology
 GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
 GO:0004013; F:adenosylhomocysteinase activity; IEA:EC.
 GO:0006378; P:mRNA polyadenylation; IDA:MGI.
 GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
 GO:0010765; P:positive regulation of sodium ion transport; IGI:MGI.
 GO:0006611; P:protein export from nucleus; IDA:MGI.
 GO:0044070; P:regulation of anion transport; IGI:MGI.
 GO:0032412; P:regulation of ion transmembrane transporter activity; IGI:MGI.
 GO:0031440; P:regulation of mRNA 3'-end processing; IDA:MGI. 
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