CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021947
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 DNA-directed DNA/RNA polymerase mu 
Protein Synonyms/Alias
 Pol Mu; Terminal transferase 
Gene Name
 POLM 
Gene Synonyms/Alias
 polmu 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
187CRAASVLKALPSPVTubiquitination[1]
238SERYQTMKLFTQIFGubiquitination[1]
249QIFGVGVKTADRWYRubiquitination[1]
271DLREQPQKLTQQQKAubiquitination[1]
277QKLTQQQKAGLQHHQubiquitination[1]
325TGGFRRGKLQGHDVDubiquitination[1, 2]
339DFLITHPKEGQEAGLubiquitination[1]
452RRFSRKEKGLWLNSHubiquitination[1]
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] 
Functional Description
 Gap-filling polymerase involved in repair of DNA double- strand breaks by non-homologous end joining (NHEJ). Participates in immunoglobulin (Ig) light chain gene rearrangement in V(D)J recombination. 
Sequence Annotation
 DOMAIN 22 122 BRCT.
 REGION 323 332 Involved in ssDNA binding (By
 METAL 330 330 Magnesium (By similarity).
 METAL 332 332 Magnesium (By similarity).
 METAL 418 418 Magnesium (By similarity).
 MOD_RES 12 12 Phosphoserine.  
Keyword
 3D-structure; Complete proteome; DNA damage; DNA recombination; DNA repair; DNA-directed DNA polymerase; Magnesium; Metal-binding; Nucleotidyltransferase; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 494 AA 
Protein Sequence
MLPKRRRARV GSPSGDAASS TPPSTRFPGV AIYLVEPRMG RSRRAFLTGL ARSKGFRVLD 60
ACSSEATHVV MEETSAEEAV SWQERRMAAA PPGCTPPALL DISWLTESLG AGQPVPVECR 120
HRLEVAGPRK GPLSPAWMPA YACQRPTPLT HHNTGLSEAL EILAEAAGFE GSEGRLLTFC 180
RAASVLKALP SPVTTLSQLQ GLPHFGEHSS RVVQELLEHG VCEEVERVRR SERYQTMKLF 240
TQIFGVGVKT ADRWYREGLR TLDDLREQPQ KLTQQQKAGL QHHQDLSTPV LRSDVDALQQ 300
VVEEAVGQAL PGATVTLTGG FRRGKLQGHD VDFLITHPKE GQEAGLLPRV MCRLQDQGLI 360
LYHQHQHSCC ESPTRLAQQS HMDAFERSFC IFRLPQPPGA AVGGSTRPCP SWKAVRVDLV 420
VAPVSQFPFA LLGWTGSKLF QRELRRFSRK EKGLWLNSHG LFDPEQKTFF QAASEEDIFR 480
HLGLEYLPPE QRNA 494 
Gene Ontology
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0003677; F:DNA binding; IEA:InterPro.
 GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0030183; P:B cell differentiation; IEA:Compara.
 GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
 GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
 GO:0016446; P:somatic hypermutation of immunoglobulin genes; IEA:Compara. 
Interpro
 IPR001357; BRCT_dom.
 IPR002054; DNA-dir_DNA_pol_X.
 IPR027249; DNA/RNApol_mu.
 IPR019843; DNA_pol-X_BS.
 IPR010996; DNA_pol_b-like_N.
 IPR018944; DNA_pol_lambd_fingers_domain.
 IPR022312; DNA_pol_X.
 IPR027421; DNA_pol_X_lyase_dom.
 IPR001726; TdT/Mu. 
Pfam
 PF10391; DNA_pol_lambd_f 
SMART
 SM00292; BRCT
 SM00483; POLXc 
PROSITE
 PS50172; BRCT
 PS00522; DNA_POLYMERASE_X 
PRINTS
 PR00869; DNAPOLX.
 PR00871; DNAPOLXTDT.