DTD1_HUMAN - dbPTM
DTD1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DTD1_HUMAN
UniProt AC Q8TEA8
Protein Name D-aminoacyl-tRNA deacylase 1 {ECO:0000250|UniProtKB:Q8IIS0}
Gene Name DTD1
Organism Homo sapiens (Human).
Sequence Length 209
Subcellular Localization Nucleus . Cytoplasm . Associated with chromatin at some replication origins containing functional DNA-unwinding elements (PubMed:20065034).
Protein Description Possible ATPase. [PubMed: 15653697) involved in DNA replication, may facilitate loading of CDC45 onto pre-replication complexes]
Protein Sequence MKAVVQRVTRASVTVGGEQISAIGRGICVLLGISLEDTQKELEHMVRKILNLRVFEDESGKHWSKSVMDKQYEILCVSQFTLQCVLKGNKPDFHLAMPTEQAEGFYNSFLEQLRKTYRPELIKDGKFGAYMQVHIQNDGPVTIELESPAPGTATSDPKQLSKLEKQQQRKEKTRAKGPSESSKERNTPRKEDRSASSGAEGDVSSEREP
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
12PhosphorylationVQRVTRASVTVGGEQ
HHHHHEEEEEECHHH		18.2829255136
53MethylationVRKILNLRVFEDESG
HHHHHCCCCEECCCC		29.97-
59PhosphorylationLRVFEDESGKHWSKS
CCCEECCCCCCCCHH		66.5222210691
61AcetylationVFEDESGKHWSKSVM
CEECCCCCCCCHHHH		51.7023236377
61MalonylationVFEDESGKHWSKSVM
CEECCCCCCCCHHHH		51.7026320211
61UbiquitinationVFEDESGKHWSKSVM
CEECCCCCCCCHHHH		51.70-
64PhosphorylationDESGKHWSKSVMDKQ
CCCCCCCCHHHHHHC		18.1222210691
65AcetylationESGKHWSKSVMDKQY
CCCCCCCHHHHHHCE		41.7119608861
66PhosphorylationSGKHWSKSVMDKQYE
CCCCCCHHHHHHCEE		19.7022210691
123UbiquitinationTYRPELIKDGKFGAY
HHCHHHHHCCCCEEE		73.40-
1232-HydroxyisobutyrylationTYRPELIKDGKFGAY
HHCHHHHHCCCCEEE		73.40-
179PhosphorylationKTRAKGPSESSKERN
HHHCCCCCCCHHHCC		59.8024275748
181PhosphorylationRAKGPSESSKERNTP
HCCCCCCCHHHCCCC		51.5626699800
182PhosphorylationAKGPSESSKERNTPR
CCCCCCCHHHCCCCC		34.1926699800
187PhosphorylationESSKERNTPRKEDRS
CCHHHCCCCCHHHHC		30.5930576142
194PhosphorylationTPRKEDRSASSGAEG
CCCHHHHCHHCCCCC		44.8422167270
196PhosphorylationRKEDRSASSGAEGDV
CHHHHCHHCCCCCCC		30.4729255136
197PhosphorylationKEDRSASSGAEGDVS
HHHHCHHCCCCCCCC		41.5629255136
204PhosphorylationSGAEGDVSSEREP--
CCCCCCCCCCCCC--		31.0829255136
205PhosphorylationGAEGDVSSEREP---
CCCCCCCCCCCC---		40.2919664994
207MethylationEGDVSSEREP-----
CCCCCCCCCC-----		64.53-
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
179SPhosphorylationKinaseCK2A1P68400
PSP
179SPhosphorylationKinaseCDC7O00311
PSP
181SPhosphorylationKinaseCDC7O00311
PSP
181SPhosphorylationKinaseCK2A1P68400
PSP
182SPhosphorylationKinaseCK2A1P68400
PSP
182SPhosphorylationKinaseCDC7O00311
PSP
187TPhosphorylationKinaseCDC7O00311
PSP
187TPhosphorylationKinaseCK2A1P68400
PSP
194SPhosphorylationKinaseCK2A1P68400
PSP
194SPhosphorylationKinaseCDC7O00311
PSP
196SPhosphorylationKinaseCK2A1P68400
PSP
196SPhosphorylationKinaseCDC7O00311
PSP
197SPhosphorylationKinaseCK2A1P68400
PSP
197SPhosphorylationKinaseCDC7O00311
PSP
204SPhosphorylationKinaseCK2A1P68400
PSP
204SPhosphorylationKinaseCDC7O00311
PSP
205SPhosphorylationKinaseCDC7O00311
PSP
205SPhosphorylationKinaseCK2A1P68400
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DTD1_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 DTD1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CDC45_HUMANCDC45physical
20065034
TOPB1_HUMANTOPBP1physical
20065034
ANKY2_HUMANANKMY2physical
22863883
HSF1_HUMANHSF1physical
22863883
KC1E_HUMANCSNK1Ephysical
26344197
POLK_HUMANPOLKphysical
28514442
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 DTD1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-65, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197 AND SER-205, ANDMASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194; SER-196; SER-197;SER-204 AND SER-205, AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197 AND SER-205, ANDMASS SPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-196; SER-197 ANDSER-205, AND MASS SPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-196 AND SER-204, ANDMASS SPECTROMETRY.

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