CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005956
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 S-adenosylmethionine synthase isoform type-2 
Protein Synonyms/Alias
 AdoMet synthase 2; Methionine adenosyltransferase 2; MAT 2; Methionine adenosyltransferase II; MAT-II 
Gene Name
 MAT2A 
Gene Synonyms/Alias
 AMS2; MATA2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
61VACETVAKTGMILLAubiquitination[1, 2]
81RAAVDYQKVVREAVKacetylation[3]
81RAAVDYQKVVREAVKubiquitination[1, 4, 5, 6, 7, 8]
88KVVREAVKHIGYDDSubiquitination[1, 4, 8]
97IGYDDSSKGFDYKTCubiquitination[1, 4, 6, 9, 10]
102SSKGFDYKTCNVLVAubiquitination[1]
163LAHKLNAKLAELRRNubiquitination[1]
228ALKEKVIKAVVPAKYubiquitination[1, 4]
234IKAVVPAKYLDEDTIubiquitination[1, 4, 6, 7, 8, 9, 10]
285GGGAFSGKDYTKVDRubiquitination[1]
289FSGKDYTKVDRSAAYubiquitination[1, 4]
303YAARWVAKSLVKGGLubiquitination[1]
307WVAKSLVKGGLCRRVubiquitination[1, 9, 10]
350RELLEIVKKNFDLRPubiquitination[1, 4, 9, 10]
351ELLEIVKKNFDLRPGubiquitination[1, 7, 9, 10]
367IVRDLDLKKPIYQRTubiquitination[1, 2, 6, 8, 9, 10, 11]
368VRDLDLKKPIYQRTAubiquitination[1, 6]
392FPWEVPKKLKY****ubiquitination[1]
Reference
 [1] 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]
 [2] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [3] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [4] 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]
 [5] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [6] 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]
 [7] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [8] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [9] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [10] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [11] 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] 
Functional Description
 Catalyzes the formation of S-adenosylmethionine from methionine and ATP. 
Sequence Annotation
 NP_BIND 131 136 ATP (Potential).
 METAL 31 31 Magnesium (By similarity).
 METAL 57 57 Potassium (By similarity).
 METAL 283 283 Potassium (By similarity).
 METAL 291 291 Magnesium (By similarity).
 BINDING 159 159 ATP (Potential).
 MOD_RES 81 81 N6-acetyllysine.
 MOD_RES 114 114 Phosphoserine.  
Keyword
 3D-structure; Acetylation; ATP-binding; Cobalt; Complete proteome; Magnesium; Metal-binding; Nucleotide-binding; One-carbon metabolism; Phosphoprotein; Potassium; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 395 AA 
Protein Sequence
MNGQLNGFHE AFIEEGTFLF TSESVGEGHP DKICDQISDA VLDAHLQQDP DAKVACETVA 60
KTGMILLAGE ITSRAAVDYQ KVVREAVKHI GYDDSSKGFD YKTCNVLVAL EQQSPDIAQG 120
VHLDRNEEDI GAGDQGLMFG YATDETEECM PLTIVLAHKL NAKLAELRRN GTLPWLRPDS 180
KTQVTVQYMQ DRGAVLPIRV HTIVISVQHD EEVCLDEMRD ALKEKVIKAV VPAKYLDEDT 240
IYHLQPSGRF VIGGPQGDAG LTGRKIIVDT YGGWGAHGGG AFSGKDYTKV DRSAAYAARW 300
VAKSLVKGGL CRRVLVQVSY AIGVSHPLSI SIFHYGTSQK SERELLEIVK KNFDLRPGVI 360
VRDLDLKKPI YQRTAAYGHF GRDSFPWEVP KKLKY 395 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0004478; F:methionine adenosyltransferase activity; TAS:ProtInc.
 GO:0034641; P:cellular nitrogen compound metabolic process; TAS:Reactome.
 GO:0032259; P:methylation; TAS:Reactome.
 GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
 GO:0006556; P:S-adenosylmethionine biosynthetic process; IEA:UniProtKB-UniPathway.
 GO:0000096; P:sulfur amino acid metabolic process; TAS:Reactome.
 GO:0006805; P:xenobiotic metabolic process; TAS:Reactome. 
Interpro
 IPR022631; ADOMET_SYNTHASE_CS.
 IPR022630; S-AdoMet_synt_C.
 IPR022629; S-AdoMet_synt_central.
 IPR022628; S-AdoMet_synt_N.
 IPR002133; S-AdoMet_synthetase.
 IPR022636; S-AdoMet_synthetase_sfam. 
Pfam
 PF02773; S-AdoMet_synt_C
 PF02772; S-AdoMet_synt_M
 PF00438; S-AdoMet_synt_N 
SMART
  
PROSITE
 PS00376; ADOMET_SYNTHASE_1
 PS00377; ADOMET_SYNTHASE_2 
PRINTS