CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-031035
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 S-adenosylmethionine synthase 
Protein Synonyms/Alias
  
Gene Name
 MAT2A 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
18RAAVDYQKVVREAVKubiquitination[1, 2, 3, 4, 5]
25KVVREAVKHIGYDDSacetylation[5, 6]
25KVVREAVKHIGYDDSubiquitination[1, 3, 4, 5]
34IGYDDSSKGFDYKTCubiquitination[1, 2, 3, 5, 7, 8]
39SSKGFDYKTCNVLVAubiquitination[3]
96LTIVLAHKLNAKLAEubiquitination[8]
100LAHKLNAKLAELRRNubiquitination[3, 5, 8]
165ALKEKVIKAVVPAKYubiquitination[1, 3, 5]
171IKAVVPAKYLDEDTIacetylation[5]
171IKAVVPAKYLDEDTIubiquitination[1, 2, 3, 4, 5, 7]
222GGGAFSGKDYTKVDRubiquitination[3]
226FSGKDYTKVDRSAAYubiquitination[1, 3, 5]
240YAARWVAKSLVKGGLubiquitination[3]
244WVAKSLVKGGLCRRVubiquitination[3, 5, 7]
287RELLEIVKKNFDLRPubiquitination[1, 3, 5, 7]
288ELLEIVKKNFDLRPGubiquitination[3, 5, 7]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] 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 (By similarity). 
Sequence Annotation
  
Keyword
 ATP-binding; Complete proteome; Magnesium; Metal-binding; Nucleotide-binding; One-carbon metabolism; Potassium; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 299 AA 
Protein Sequence
MILLAGEITS RAAVDYQKVV REAVKHIGYD DSSKGFDYKT CNVLVALEQQ SPDIAQGVHL 60
DRNEEDIGAG DQGLMFGYAT DETEECMPLT IVLAHKLNAK LAELRRNGTL PWLRPDSKTQ 120
VTVQYMQDRG AVLPIRVHTI VISVQHDEEV CLDEMRDALK EKVIKAVVPA KYLDEDTIYH 180
LQPSGRFVIG GPQGDAGLTG RKIIVDTYGG WGAHGGGAFS GKDYTKVDRS AAYAARWVAK 240
SLVKGGLCRR VLVQVSYAIG VSHPLSISIF HYGTSQKSER ELLEIVKKNF DLRPGVIVR 299 
Gene Ontology
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0004478; F:methionine adenosyltransferase activity; IEA:EC.
 GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
 GO:0006556; P:S-adenosylmethionine biosynthetic process; IEA:UniProtKB-UniPathway. 
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