CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000794
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Putative adenosylhomocysteinase 2 
Protein Synonyms/Alias
 AdoHcyase 2; DC-expressed AHCY-like molecule; S-adenosyl-L-homocysteine hydrolase 2; S-adenosylhomocysteine hydrolase-like protein 1 
Gene Name
 AHCYL1 
Gene Synonyms/Alias
 DCAL; XPVKONA 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
53DDMQEFTKFPTKTGRubiquitination[1]
100EKQQTNSKGSSNFCVubiquitination[2]
267HRLYQLSKAGKLCVPubiquitination[2]
270YQLSKAGKLCVPAMNubiquitination[2]
284NVNDSVTKQKFDNLYubiquitination[2]
286NDSVTKQKFDNLYCCubiquitination[2]
359MDGFRVVKLNEVIRQubiquitination[2]
389REHLDRMKNSCIVCNubiquitination[1, 2]
432HVIWPDGKRVVLLAEubiquitination[2]
478NAPEGRYKQDVYLLPubiquitination[2]
487DVYLLPKKMDEYVASubiquitination[2, 3]
Reference
 [1] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [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
Functional Description
  
Sequence Annotation
 NP_BIND 318 322 NAD.
 NP_BIND 397 399 NAD.
 REGION 65 92 PEST (By similarity).
 REGION 281 448 NAD binding (By similarity).
 REGION 520 530 PDZ-binding (By similarity).
 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.
 BINDING 376 376 NAD.
 MOD_RES 2 2 N-acetylserine.
 MOD_RES 2 2 Phosphoserine.
 MOD_RES 82 82 Phosphothreonine (By similarity).
 MOD_RES 84 84 Phosphoserine (By similarity).
 MOD_RES 85 85 Phosphoserine (By similarity).
 MOD_RES 391 391 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Complete proteome; 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; IEA:Compara.
 GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
 GO:0010765; P:positive regulation of sodium ion transport; IEA:Compara.
 GO:0006611; P:protein export from nucleus; IEA:Compara.
 GO:0044070; P:regulation of anion transport; IEA:Compara.
 GO:0032412; P:regulation of ion transmembrane transporter activity; IEA:Compara.
 GO:0031440; P:regulation of mRNA 3'-end processing; IEA:Compara. 
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