CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019636
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein artemis 
Protein Synonyms/Alias
 DNA cross-link repair 1C protein; Protein A-SCID; SNM1 homolog C; hSNM1C; SNM1-like protein 
Gene Name
 DCLRE1C 
Gene Synonyms/Alias
 ARTEMIS; ASCID; SCIDA; SNM1C 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
157LHSGGRVKDIQSVYLubiquitination[1]
260IHACRHPKAEEYFQWubiquitination[1]
683TGESIAVKKRKCSLLacetylation[2]
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] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786
Functional Description
 Required for V(D)J recombination, the process by which exons encoding the antigen-binding domains of immunoglobulins and T-cell receptor proteins are assembled from individual V, (D), and J gene segments. V(D)J recombination is initiated by the lymphoid specific RAG endonuclease complex, which generates site specific DNA double strand breaks (DSBs). These DSBs present two types of DNA end structures: hairpin sealed coding ends and phosphorylated blunt signal ends. These ends are independently repaired by the non homologous end joining (NHEJ) pathway to form coding and signal joints respectively. This protein exhibits single-strand specific 5'-3' exonuclease activity in isolation and acquires endonucleolytic activity on 5' and 3' hairpins and overhangs when in a complex with PRKDC. The latter activity is required specifically for the resolution of closed hairpins prior to the formation of the coding joint. May also be required for the repair of complex DSBs induced by ionizing radiation, which require substantial end-processing prior to religation by NHEJ. 
Sequence Annotation
 MOD_RES 645 645 Phosphoserine; by ATM.  
Keyword
 3D-structure; Adaptive immunity; Alternative splicing; Complete proteome; Disease mutation; DNA damage; DNA recombination; DNA repair; Endonuclease; Exonuclease; Hydrolase; Immunity; Magnesium; Nuclease; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; SCID. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 692 AA 
Protein Sequence
MSSFEGQMAE YPTISIDRFD RENLRARAYF LSHCHKDHMK GLRAPTLKRR LECSLKVYLY 60
CSPVTKELLL TSPKYRFWKK RIISIEIETP TQISLVDEAS GEKEEIVVTL LPAGHCPGSV 120
MFLFQGNNGT VLYTGDFRLA QGEAARMELL HSGGRVKDIQ SVYLDTTFCD PRFYQIPSRE 180
ECLSGVLELV RSWITRSPYH VVWLNCKAAY GYEYLFTNLS EELGVQVHVN KLDMFRNMPE 240
ILHHLTTDRN TQIHACRHPK AEEYFQWSKL PCGITSRNRI PLHIISIKPS TMWFGERSRK 300
TNVIVRTGES SYRACFSFHS SYSEIKDFLS YLCPVNAYPN VIPVGTTMDK VVEILKPLCR 360
SSQSTEPKYK PLGKLKRART VHRDSEEEDD YLFDDPLPIP LRHKVPYPET FHPEVFSMTA 420
VSEKQPEKLR QTPGCCRAEC MQSSRFTNFV DCEESNSESE EEVGIPASLQ GDLGSVLHLQ 480
KADGDVPQWE VFFKRNDEIT DESLENFPSS TVAGGSQSPK LFSDSDGEST HISSQNSSQS 540
THITEQGSQG WDSQSDTVLL SSQERNSGDI TSLDKADYRP TIKENIPASL MEQNVICPKD 600
TYSDLKSRDK DVTIVPSTGE PTTLSSETHI PEEKSLLNLS TNADSQSSSD FEVPSTPEAE 660
LPKREHLQYL YEKLATGESI AVKKRKCSLL DT 692 
Gene Ontology
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0008409; F:5'-3' exonuclease activity; IDA:MGI.
 GO:0000014; F:single-stranded DNA specific endodeoxyribonuclease activity; IDA:MGI.
 GO:0030183; P:B cell differentiation; IEA:Compara.
 GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
 GO:0006302; P:double-strand break repair; IEA:Compara.
 GO:0010212; P:response to ionizing radiation; IEA:Compara.
 GO:0000723; P:telomere maintenance; IEA:Compara. 
Interpro
 IPR001279; Beta-lactamas-like.
 IPR011084; DRMBL. 
Pfam
 PF07522; DRMBL 
SMART
 SM00849; Lactamase_B 
PROSITE
  
PRINTS