TDT_HUMAN - dbPTM
TDT_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TDT_HUMAN
UniProt AC P04053
Protein Name DNA nucleotidylexotransferase
Gene Name DNTT
Organism Homo sapiens (Human).
Sequence Length 509
Subcellular Localization Nucleus .
Protein 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..
Protein Sequence MDPPRASHLSPRKKRPRQTGALMASSPQDIKFQDLVVFILEKKMGTTRRAFLMELARRKGFRVENELSDSVTHIVAENNSGSDVLEWLQAQKVQVSSQPELLDVSWLIECIRAGKPVEMTGKHQLVVRRDYSDSTNPGPPKTPPIAVQKISQYACQRRTTLNNCNQIFTDAFDILAENCEFRENEDSCVTFMRAASVLKSLPFTIISMKDTEGIPCLGSKVKGIIEEIIEDGESSEVKAVLNDERYQSFKLFTSVFGVGLKTSEKWFRMGFRTLSKVRSDKSLKFTRMQKAGFLYYEDLVSCVTRAEAEAVSVLVKEAVWAFLPDAFVTMTGGFRRGKKMGHDVDFLITSPGSTEDEEQLLQKVMNLWEKKGLLLYYDLVESTFEKLRLPSRKVDALDHFQKCFLIFKLPRQRVDSDQSSWQEGKTWKAIRVDLVLCPYERRAFALLGWTGSRQFERDLRRYATHERKMILDNHALYDKTKRIFLKAESEEEIFAHLGLDYIEPWERNA
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
7Phosphorylation-MDPPRASHLSPRKK
-CCCCCHHCCCCCCC		26.6626552605
10PhosphorylationPPRASHLSPRKKRPR
CCCHHCCCCCCCCCC		19.7530576142
25PhosphorylationQTGALMASSPQDIKF
CCCCCCCCCCCCCCH		28.6928634298
26PhosphorylationTGALMASSPQDIKFQ
CCCCCCCCCCCCCHH		19.6228634298
42UbiquitinationLVVFILEKKMGTTRR
EEEHHHHHCCCHHHH		44.61-
122UbiquitinationKPVEMTGKHQLVVRR
CCEEECCCCEEEEEE		21.0029967540
131PhosphorylationQLVVRRDYSDSTNPG
EEEEEECCCCCCCCC		16.7417929957
132PhosphorylationLVVRRDYSDSTNPGP
EEEEECCCCCCCCCC		29.4023684312
134PhosphorylationVRRDYSDSTNPGPPK
EEECCCCCCCCCCCC		24.9223684312
135PhosphorylationRRDYSDSTNPGPPKT
EECCCCCCCCCCCCC		50.8823684312
142PhosphorylationTNPGPPKTPPIAVQK
CCCCCCCCCCCHHHH		39.8223684312
149UbiquitinationTPPIAVQKISQYACQ
CCCCHHHHHHHHHHH		37.41-
199UbiquitinationMRAASVLKSLPFTII
HHHHHHHHHCCEEEE		48.0322505724
209UbiquitinationPFTIISMKDTEGIPC
CEEEEEEECCCCCCC		55.5022505724
220AcetylationGIPCLGSKVKGIIEE
CCCCCCHHHHHHHHH		46.2825953088
220UbiquitinationGIPCLGSKVKGIIEE
CCCCCCHHHHHHHHH		46.2829967540
222UbiquitinationPCLGSKVKGIIEEII
CCCCHHHHHHHHHHH		48.4022505724
238UbiquitinationDGESSEVKAVLNDER
CCCCHHHEEHHCCHH		28.8229967540
250UbiquitinationDERYQSFKLFTSVFG
CHHHHHHHHHHHHHC		48.1929967540
261UbiquitinationSVFGVGLKTSEKWFR
HHHCCCCCCCHHHHH		44.04-
265UbiquitinationVGLKTSEKWFRMGFR
CCCCCCHHHHHHHHH		51.9429967540
290UbiquitinationLKFTRMQKAGFLYYE
CCCEECEECCEEEHH		40.9329967540
296PhosphorylationQKAGFLYYEDLVSCV
EECCEEEHHHHHHHH		12.7127642862
316AcetylationEAVSVLVKEAVWAFL
HHHHHHHHHHHHHHC		35.487695111
339UbiquitinationGGFRRGKKMGHDVDF
CCCCCCCCCCCCCEE		53.6022505724
363UbiquitinationDEEQLLQKVMNLWEK
CHHHHHHHHHHHHHH		43.3429967540
370UbiquitinationKVMNLWEKKGLLLYY
HHHHHHHHCCCHHHH		40.3322505724
371UbiquitinationVMNLWEKKGLLLYYD
HHHHHHHCCCHHHHH		43.19-
382PhosphorylationLYYDLVESTFEKLRL
HHHHHHHHHHHHHCC		30.80-
383PhosphorylationYYDLVESTFEKLRLP
HHHHHHHHHHHHCCC		23.47-
393UbiquitinationKLRLPSRKVDALDHF
HHCCCCCHHCHHHHH		49.1322505724
402UbiquitinationDALDHFQKCFLIFKL
CHHHHHHHHEEEEEC		26.4729967540
408UbiquitinationQKCFLIFKLPRQRVD
HHHEEEEECCHHHCC		51.0629967540
425UbiquitinationQSSWQEGKTWKAIRV
CCHHHCCCCEEEEEE		50.9222505724
467UbiquitinationRRYATHERKMILDNH
HHHHHHHHHHHHCCH		26.6622505724
468UbiquitinationRYATHERKMILDNHA
HHHHHHHHHHHCCHH		27.5822505724
477PhosphorylationILDNHALYDKTKRIF
HHCCHHHHHHHCEEE		19.0425884760
478UbiquitinationLDNHALYDKTKRIFL
HCCHHHHHHHCEEEE		53.6622817900
479UbiquitinationDNHALYDKTKRIFLK
CCHHHHHHHCEEEEE		42.2522817900
480UbiquitinationNHALYDKTKRIFLKA
CHHHHHHHCEEEEEC		23.7422817900
481UbiquitinationHALYDKTKRIFLKAE
HHHHHHHCEEEEECC		49.6022817900
501PhosphorylationFAHLGLDYIEPWERN
HHHCCCCCCCCCCCC		16.5427642862
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of TDT_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TDT_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of TDT_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PRP19_HUMANPRPF19physical
12960389
TDIF2_HUMANDNTTIP2physical
12786946
PCNA_HUMANPCNAphysical
11554927
ABTB2_HUMANABTB2physical
18429817
CUL3_HUMANCUL3physical
18429817
TDIF1_HUMANDNTTIP1physical
11473582
REL_HUMANRELphysical
25416956
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TDT_HUMAN

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Related Literatures of Post-Translational Modification

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