CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-031246
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 DNA ligase 
Protein Synonyms/Alias
  
Gene Name
 LIG1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
188QEEEEQTKPPRRAPKubiquitination[1]
195KPPRRAPKTLSSFFTubiquitination[2]
255ACWKPGQKVPYLAVAubiquitination[3]
267AVARTFEKIEEVSARubiquitination[3]
345VRAEAAEKGDVGLVAubiquitination[1, 4]
376TASGVFSKFRDIARLubiquitination[1, 2, 3]
397AKKIDIIKGLFVACRubiquitination[3]
510LSPGIPLKPMLAHPTubiquitination[1, 3]
525RGISEVLKRFEEAAFubiquitination[3]
599VAWDREKKQIQPFQVubiquitination[3]
706DATYEIAKRSHNWLKubiquitination[3]
713KRSHNWLKLKKDYLDubiquitination[3]
764EELQAICKLGTGFSDmethylation[5]
764EELQAICKLGTGFSDubiquitination[6]
835RGLVDSDKGISLRFPubiquitination[1, 3]
Reference
 [1] 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]
 [2] 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]
 [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] 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] A general molecular affinity strategy for global detection and proteomic analysis of lysine methylation.
 Moore KE, Carlson SM, Camp ND, Cheung P, James RG, Chua KF, Wolf-Yadlin A, Gozani O.
 Mol Cell. 2013 May 9;50(3):444-56. [PMID: 23583077]
 [6] 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
 ATP-binding; Complete proteome; DNA damage; DNA recombination; DNA repair; DNA replication; Ligase; Nucleotide-binding; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 888 AA 
Protein Sequence
MQRSIMAALK EWNGVVSESD SPVKRPGRKA ARVLGSEGEE EDEALSPAKG QKPALDCSQV 60
SPPRPATSPE NNASLSDTSP MDSSPSGIPK RRTARKQLPK RTIQEVLEEQ SEDEDREAKR 120
KKEEEEETPK ESLTEAEVAT EKEGEDGDQP TTPPKPLKTS KAETPTESVS EPEVATKQEL 180
QEEEEQTKPP RRAPKTLSSF FTPRKPAVKK EVKEEEPGAP GKEGAAEGPL DPSGYNPAKN 240
NYHPVEDACW KPGQKVPYLA VARTFEKIEE VSARLRMVET LSNLLRSVVA LSPPDLLPVL 300
YLSLNHLGPP QQGLELGVGD GVLLKAVAQA TGRQLESVRA EAAEKGDVGL VAENSRSTQR 360
LMLPPPPLTA SGVFSKFRDI ARLTGSASTA KKIDIIKGLF VACRHSEARF IARSLSGRLR 420
LGLAEQSVLA ALSQAVSLTP PGQEFPPAMV DAGKGKTAEA RKTWLEEQGM ILKQTFCEVP 480
DLDRIIPVLL EHGLERLPEH CKLSPGIPLK PMLAHPTRGI SEVLKRFEEA AFTCEYKYDG 540
QRAQIHALEG GEVKIFSRNQ EDNTGKYPDI ISRIPKIKLP SVTSFILDTE AVAWDREKKQ 600
IQPFQVLTTR KRKEVDASEI QVQVCLYAFD LIYLNGESLV REPLSRRRQL LRENFVETEG 660
EFVFATSLDT KDIEQIAEFL EQSVKDSCEG LMVKTLDVDA TYEIAKRSHN WLKLKKDYLD 720
GVGDTLDLVV IGAYLGRGKR AGRYGGFLLA SYDEDSEELQ AICKLGTGFS DEELEEHHQS 780
LKALVLPSPR PYVRIDGAVI PDHWLDPSAV WEVKCADLSL SPIYPAARGL VDSDKGISLR 840
FPRFIRVRED KQPEQATTSA QVACLYRKQS QIQNQQGEDS GSDPEDTY 888 
Gene Ontology
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0003677; F:DNA binding; IEA:InterPro.
 GO:0003910; F:DNA ligase (ATP) activity; IEA:EC.
 GO:0051103; P:DNA ligation involved in DNA repair; IEA:InterPro.
 GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
 GO:0006260; P:DNA replication; IEA:UniProtKB-KW. 
Interpro
 IPR000977; DNA_ligase_ATP-dep.
 IPR012309; DNA_ligase_ATP-dep_C.
 IPR012310; DNA_ligase_ATP-dep_cent.
 IPR016059; DNA_ligase_ATP-dep_CS.
 IPR012308; DNA_ligase_ATP-dep_N.
 IPR012340; NA-bd_OB-fold. 
Pfam
 PF04679; DNA_ligase_A_C
 PF01068; DNA_ligase_A_M
 PF04675; DNA_ligase_A_N 
SMART
  
PROSITE
 PS00697; DNA_LIGASE_A1
 PS00333; DNA_LIGASE_A2
 PS50160; DNA_LIGASE_A3 
PRINTS