CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021492
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 5' exonuclease Apollo 
Protein Synonyms/Alias
 DNA cross-link repair 1B protein; SNM1 homolog B; SNMIB; hSNM1B 
Gene Name
 DCLRE1B 
Gene Synonyms/Alias
 SNM1B 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
290RAFVAALKPCQVVPIubiquitination[1, 2]
333YMSSSSRKPSLLWLLubiquitination[1]
371SQADRDSKKAKKEKLubiquitination[3]
372QADRDSKKAKKEKLSubiquitination[1]
377SKKAKKEKLSPWPADubiquitination[1]
407LFPDLYSKEWNKAVPubiquitination[1]
446DEEFISQKTREEIGLubiquitination[1, 3]
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] 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] 
Functional Description
 5'-3' exonuclease that plays a central role in telomere maintenance and protection during S-phase. Participates in the protection of telomeres against non-homologous end-joining (NHEJ)- mediated repair, thereby ensuring that telomeres do not fuse. Plays a key role in telomeric loop (T loop) formation by being recruited by TERF2 at the leading end telomeres and by processing leading-end telomeres immediately after their replication via its exonuclease activity: generates 3' single-stranded overhang at the leading end telomeres avoiding blunt leading-end telomeres that are vulnerable to end-joining reactions and expose the telomere end in a manner that activates the DNA repair pathways. Together with TERF2, required to protect telomeres from replicative damage during replication by controlling the amount of DNA topoisomerase (TOP1, TOP2A and TOP2B) needed for telomere replication during fork passage and prevent aberrant telomere topology. Also involved in response to DNA damage: plays a role in response to DNA interstrand cross-links (ICLs) by facilitating double-strand break formation. In case of spindle stress, involved in prophase checkpoint. 
Sequence Annotation
 MOTIF 496 511 TBM.  
Keyword
 3D-structure; Chromosome; Complete proteome; Cytoplasm; Cytoskeleton; DNA damage; DNA repair; Exonuclease; Hydrolase; Nuclease; Nucleus; Polymorphism; Reference proteome; Telomere; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 532 AA 
Protein Sequence
MNGVLIPHTP IAVDFWSLRR AGTARLFFLS HMHSDHTVGL SSTWARPLYC SPITAHLLHR 60
HLQVSKQWIQ ALEVGESHVL PLDEIGQETM TVTLLDANHC PGSVMFLFEG YFGTILYTGD 120
FRYTPSMLKE PALTLGKQIH TLYLDNTNCN PALVLPSRQE AAHQIVQLIR KHPQHNIKIG 180
LYSLGKESLL EQLALEFQTW VVLSPRRLEL VQLLGLADVF TVEEKAGRIH AVDHMEICHS 240
NMLRWNQTHP TIAILPTSRK IHSSHPDIHV IPYSDHSSYS ELRAFVAALK PCQVVPIVSR 300
RPCGGFQDSL SPRISVPLIP DSVQQYMSSS SRKPSLLWLL ERRLKRPRTQ GVVFESPEES 360
ADQSQADRDS KKAKKEKLSP WPADLEKQPS HHPLRIKKQL FPDLYSKEWN KAVPFCESQK 420
RVTMLTAPLG FSVHLRSTDE EFISQKTREE IGLGSPLVPM GDDDGGPEAT GNQSAWMGHG 480
SPLSHSSKGT PLLATEFRGL ALKYLLTPVN FFQAGYSSRR FDQQVEKYHK PC 532 
Gene Ontology
 GO:0005813; C:centrosome; IDA:UniProtKB.
 GO:0000781; C:chromosome, telomeric region; IDA:UniProtKB.
 GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0008409; F:5'-3' exonuclease activity; IDA:UniProtKB.
 GO:0000075; P:cell cycle checkpoint; IMP:UniProtKB.
 GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
 GO:0031848; P:protection from non-homologous end joining at telomere; IMP:UniProtKB.
 GO:0031860; P:telomeric 3' overhang formation; ISS:UniProtKB.
 GO:0031627; P:telomeric loop formation; ISS:UniProtKB. 
Interpro
 IPR001279; Beta-lactamas-like.
 IPR011084; DRMBL. 
Pfam
 PF07522; DRMBL 
SMART
 SM00849; Lactamase_B 
PROSITE
  
PRINTS