CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-036991
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Adenylosuccinate lyase 
Protein Synonyms/Alias
  
Gene Name
 ADSL 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
75NLENIDFKMAAEEEKacetylation[1]
75NLENIDFKMAAEEEKubiquitination[2, 3, 4]
82KMAAEEEKRLRHDVMacetylation[4, 5]
161SRLADFAKERASLPTubiquitination[3]
184AQLTTVGKRCCLWIQubiquitination[2, 3, 4, 6, 7]
213DLRFRGVKGTTGTQAubiquitination[3]
232LFEGDDHKVEQLDKMubiquitination[3, 4]
238HKVEQLDKMVTEKAGacetylation[1]
243LDKMVTEKAGFKRAFubiquitination[2, 3]
290IRLLANLKEMEEPFEubiquitination[2, 3, 4, 7]
298EMEEPFEKQQIGSSAacetylation[1]
298EMEEPFEKQQIGSSAubiquitination[2, 3]
309GSSAMPYKRNPMRSEacetylation[1, 4, 5]
309GSSAMPYKRNPMRSEubiquitination[3]
405NIIMAMVKAGGSRQDubiquitination[3]
429QQAASVVKQEGGDNDubiquitination[2, 3, 4, 8]
484EEVYPLLKPYESVMKubiquitination[2, 3]
493YESVMKVKAELCL**ubiquitination[3, 4]
Reference
 [1] 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]
 [2] 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]
 [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] 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]
 [5] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [6] 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]
 [7] 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]
 [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
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 498 AA 
Protein Sequence
MAAGGDHGSP DSYRSPLASR YASPEMCFVF SDRYKFRTWR QLWLWLAEAE QTLGLPITDE 60
QIQEMKSNLE NIDFKMAAEE EKRLRHDVMA HVHTFGHCCP KAAGIIHLGA TSCYVGDNTS 120
LILSRGVIKA YCNLRLPGSD SSPVSVSQLA RVISRLADFA KERASLPTLG FTHFQPAQLT 180
TVGKRCCLWI QDLCMDLQNL KRVRDDLRFR GVKGTTGTQA SFLQLFEGDD HKVEQLDKMV 240
TEKAGFKRAF IITGQTYTRK VDIEVLSVLA SLGASVHKIC TDIRLLANLK EMEEPFEKQQ 300
IGSSAMPYKR NPMRSERCCS LARHLMTLVM DPLQTASVQW FERTLDDSAN RRICLAEAFL 360
TADTILNTLQ NISEGLVVYP KVIERRIRQE LPFMATENII MAMVKAGGSR QDCHEKIRVL 420
SQQAASVVKQ EGGDNDLIER IQVDAYFSPI HSQLDHLLDP SSFTGRASQQ VQRFLEEEVY 480
PLLKPYESVM KVKAELCL 498 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0004018; F:N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity; IEA:InterPro.
 GO:0009152; P:purine ribonucleotide biosynthetic process; IEA:InterPro. 
Interpro
 IPR019468; AdenyloSucc_lyase_C.
 IPR003031; D_crystallin.
 IPR024083; Fumarase/histidase_N.
 IPR000362; Fumarate_lyase.
 IPR020557; Fumarate_lyase_CS.
 IPR022761; Fumarate_lyase_N.
 IPR008948; L-Aspartase-like.
 IPR004769; Pur_lyase. 
Pfam
 PF10397; ADSL_C
 PF00206; Lyase_1 
SMART
 SM00998; ADSL_C 
PROSITE
 PS00163; FUMARATE_LYASES 
PRINTS
 PR00145; ARGSUCLYASE.
 PR00149; FUMRATELYASE.