CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002083
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 DNA nucleotidylexotransferase 
Protein Synonyms/Alias
 Terminal addition enzyme; Terminal deoxynucleotidyltransferase; Terminal transferase 
Gene Name
 DNTT 
Gene Synonyms/Alias
 TDT 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
42LVVFILEKKMGTTRRubiquitination[1]
199MRAASVLKSLPFTIIubiquitination[1, 2, 3]
209PFTIISMKDTEGIPCubiquitination[1, 2, 3]
220GIPCLGSKVKGIIEEubiquitination[1]
222PCLGSKVKGIIEEIIubiquitination[1, 2, 3]
250DERYQSFKLFTSVFGubiquitination[1]
261SVFGVGLKTSEKWFRubiquitination[1]
265VGLKTSEKWFRMGFRubiquitination[1, 3]
290LKFTRMQKAGFLYYEubiquitination[1]
339GGFRRGKKMGHDVDFubiquitination[1, 2]
370KVMNLWEKKGLLLYYubiquitination[1, 2]
371VMNLWEKKGLLLYYDubiquitination[1]
393KLRLPSRKVDALDHFubiquitination[1, 2, 3]
402DALDHFQKCFLIFKLubiquitination[1]
408QKCFLIFKLPRQRVDubiquitination[1]
425QSSWQEGKTWKAIRVubiquitination[1, 2, 3]
468RYATHERKMILDNHAubiquitination[1, 2, 3]
479DNHALYDKTKRIFLKubiquitination[1, 2, 3, 4]
481HALYDKTKRIFLKAEubiquitination[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] 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]
 [3] 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]
 [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
Functional Description
 Template-independent DNA polymerase which catalyzes the random addition of deoxynucleoside 5'-triphosphate to the 3'-end of a DNA initiator. One of the in vivo functions of this enzyme is the addition of nucleotides at the junction (N region) of rearranged Ig heavy chain and T-cell receptor gene segments during the maturation of B- and T-cells. 
Sequence Annotation
 DOMAIN 27 124 BRCT.
 REGION 151 509 Mediates interaction with DNTTIP2.
 REGION 336 345 Involved in ssDNA binding (By
 METAL 253 253 Sodium; via carbonyl oxygen (By
 METAL 255 255 Sodium; via carbonyl oxygen (By
 METAL 343 343 Magnesium (By similarity).
 METAL 345 345 Magnesium (By similarity).
 METAL 433 433 Magnesium (By similarity).  
Keyword
 3D-structure; Alternative splicing; Complete proteome; Magnesium; Metal-binding; Nucleotidyltransferase; Nucleus; Polymorphism; Reference proteome; Terminal addition; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 509 AA 
Protein Sequence
MDPPRASHLS PRKKRPRQTG ALMASSPQDI KFQDLVVFIL EKKMGTTRRA FLMELARRKG 60
FRVENELSDS VTHIVAENNS GSDVLEWLQA QKVQVSSQPE LLDVSWLIEC IRAGKPVEMT 120
GKHQLVVRRD YSDSTNPGPP KTPPIAVQKI SQYACQRRTT LNNCNQIFTD AFDILAENCE 180
FRENEDSCVT FMRAASVLKS LPFTIISMKD TEGIPCLGSK VKGIIEEIIE DGESSEVKAV 240
LNDERYQSFK LFTSVFGVGL KTSEKWFRMG FRTLSKVRSD KSLKFTRMQK AGFLYYEDLV 300
SCVTRAEAEA VSVLVKEAVW AFLPDAFVTM TGGFRRGKKM GHDVDFLITS PGSTEDEEQL 360
LQKVMNLWEK KGLLLYYDLV ESTFEKLRLP SRKVDALDHF QKCFLIFKLP RQRVDSDQSS 420
WQEGKTWKAI RVDLVLCPYE RRAFALLGWT GSRQFERDLR RYATHERKMI LDNHALYDKT 480
KRIFLKAESE EEIFAHLGLD YIEPWERNA 509 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0003677; F:DNA binding; IEA:InterPro.
 GO:0003912; F:DNA nucleotidylexotransferase activity; TAS:ProtInc.
 GO:0003887; F:DNA-directed DNA polymerase activity; IEA:InterPro.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0006304; P:DNA modification; IEA:UniProtKB-KW. 
Interpro
 IPR001357; BRCT_dom.
 IPR002054; DNA-dir_DNA_pol_X.
 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.
 IPR002934; Nucleotidyltransferase.
 IPR027292; TdT.
 IPR001726; TdT/Mu. 
Pfam
 PF00533; BRCT
 PF10391; DNA_pol_lambd_f
 PF01909; NTP_transf_2 
SMART
 SM00292; BRCT
 SM00483; POLXc 
PROSITE
 PS50172; BRCT
 PS00522; DNA_POLYMERASE_X 
PRINTS
 PR00869; DNAPOLX.
 PR00871; DNAPOLXTDT.