TDIF1_HUMAN - dbPTM
TDIF1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TDIF1_HUMAN
UniProt AC Q9H147
Protein Name Deoxynucleotidyltransferase terminal-interacting protein 1
Gene Name DNTTIP1
Organism Homo sapiens (Human).
Sequence Length 329
Subcellular Localization Nucleus .
Protein Description Increases DNTT terminal deoxynucleotidyltransferase activity (in vitro). [PubMed: 11473582 Also acts as a transcriptional regulator, binding to the consensus sequence 5'-GNTGCATG-3' following an AT-tract. Associates with RAB20 promoter and positively regulates its transcription. Binds DNA and nucleosomes; may recruit HDAC1 complexes to nucleosomes or naked DNA.]
Protein Sequence MGATGDAEQPRGPSGAERGGLELGDAGAAGQLVLTNPWNIMIKHRQVQRRGRRSQMTTSFTDPAISMDLLRAVLQPSINEEIQTVFNKYMKFFQKAALNVRDNVGEEVDAEQLIQEACRSCLEQAKLLFSDGEKVIPRLTHELPGIKRGRQAEEECAHRGSPLPKKRKGRPPGHILSSDRAAAGMVWKPKSCEPIRREGPKWDPARLNESTTFVLGSRANKALGMGGTRGRIYIKHPHLFKYAADPQDKHWLAEQHHMRATGGKMAYLLIEEDIRDLAASDDYRGCLDLKLEELKSFVLPSWMVEKMRKYMETLRTENEHRAVEAPPQT
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
43UbiquitinationNPWNIMIKHRQVQRR
CCHHHEEEEHHHHHC		18.5023503661
54PhosphorylationVQRRGRRSQMTTSFT
HHHCCCCCCCCCCCC		23.9626055452
57PhosphorylationRGRRSQMTTSFTDPA
CCCCCCCCCCCCCHH		16.2028122231
58PhosphorylationGRRSQMTTSFTDPAI
CCCCCCCCCCCCHHH		19.2521712546
61PhosphorylationSQMTTSFTDPAISMD
CCCCCCCCCHHHCHH		40.62-
88UbiquitinationEIQTVFNKYMKFFQK
HHHHHHHHHHHHHHH		34.95-
91UbiquitinationTVFNKYMKFFQKAAL
HHHHHHHHHHHHHHH		39.6822817900
95UbiquitinationKYMKFFQKAALNVRD
HHHHHHHHHHHCCCC		30.3922817900
126UbiquitinationRSCLEQAKLLFSDGE
HHHHHHHHHHCCCCC		45.4729967540
130PhosphorylationEQAKLLFSDGEKVIP
HHHHHHCCCCCCHHH		44.68-
134SumoylationLLFSDGEKVIPRLTH
HHCCCCCCHHHHHHH		51.50-
134UbiquitinationLLFSDGEKVIPRLTH
HHCCCCCCHHHHHHH		51.5021906983
134SumoylationLLFSDGEKVIPRLTH
HHCCCCCCHHHHHHH		51.50-
147SumoylationTHELPGIKRGRQAEE
HHCCCCCHHCHHHHH		55.50-
147UbiquitinationTHELPGIKRGRQAEE
HHCCCCCHHCHHHHH		55.5033845483
147SumoylationTHELPGIKRGRQAEE
HHCCCCCHHCHHHHH		55.50-
147AcetylationTHELPGIKRGRQAEE
HHCCCCCHHCHHHHH		55.5025953088
161PhosphorylationEECAHRGSPLPKKRK
HHHHHCCCCCCCCCC		24.1823401153
177PhosphorylationRPPGHILSSDRAAAG
CCCCCCCCCCCCCCC		29.5925159151
178PhosphorylationPPGHILSSDRAAAGM
CCCCCCCCCCCCCCC		27.8928348404
188UbiquitinationAAAGMVWKPKSCEPI
CCCCCCCCCCCCCCC		31.02-
188AcetylationAAAGMVWKPKSCEPI
CCCCCCCCCCCCCCC		31.0225953088
190SumoylationAGMVWKPKSCEPIRR
CCCCCCCCCCCCCCC		65.10-
190SumoylationAGMVWKPKSCEPIRR
CCCCCCCCCCCCCCC		65.10-
201SumoylationPIRREGPKWDPARLN
CCCCCCCCCCHHHCC		75.08-
201SumoylationPIRREGPKWDPARLN
CCCCCCCCCCHHHCC		75.08-
221SumoylationVLGSRANKALGMGGT
EECCHHHHHCCCCCC		43.96-
221SumoylationVLGSRANKALGMGGT
EECCHHHHHCCCCCC		43.96-
229MethylationALGMGGTRGRIYIKH
HCCCCCCCCEEEECC		35.35-
241SumoylationIKHPHLFKYAADPQD
ECCHHHHHHCCCCCC		40.10-
241SumoylationIKHPHLFKYAADPQD
ECCHHHHHHCCCCCC		40.10-
241UbiquitinationIKHPHLFKYAADPQD
ECCHHHHHHCCCCCC		40.1029967540
249UbiquitinationYAADPQDKHWLAEQH
HCCCCCCHHHHHHHH		31.2829967540
290UbiquitinationYRGCLDLKLEELKSF
CCCHHHHCHHHHHHC		54.22-
295UbiquitinationDLKLEELKSFVLPSW
HHCHHHHHHCCCHHH		45.1629967540
306UbiquitinationLPSWMVEKMRKYMET
CHHHHHHHHHHHHHH		32.37-
310PhosphorylationMVEKMRKYMETLRTE
HHHHHHHHHHHHHCC		6.9928509920
313PhosphorylationKMRKYMETLRTENEH
HHHHHHHHHHCCCCH		12.6628509920
316PhosphorylationKYMETLRTENEHRAV
HHHHHHHCCCCHHCC		46.4028509920
329PhosphorylationAVEAPPQT-------
CCCCCCCC-------		46.4824719451
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 TDIF1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TDIF1_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 TDIF1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ABTB1_HUMANABTB1physical
19930467
TDIF1_HUMANDNTTIP1physical
11473582
EMSA1_HUMANELMSAN1physical
21258344
HDAC2_HUMANHDAC2physical
21258344
HDAC1_HUMANHDAC1physical
21258344
KDM1A_HUMANKDM1Aphysical
23455924
IF2A_HUMANEIF2S1physical
26344197
EMSA1_HUMANELMSAN1physical
26344197
PYM1_HUMANWIBGphysical
26344197
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 TDIF1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161, AND MASSSPECTROMETRY.

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