dbPTM

DUT_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DUT_HUMAN
UniProt AC	P33316
Protein Name	Deoxyuridine 5'-triphosphate nucleotidohydrolase, mitochondrial
Gene Name	DUT
Organism	Homo sapiens (Human).
Sequence Length	252
Subcellular Localization	Isoform 2: Nucleus . Isoform 3: Mitochondrion .
Protein Description	This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA..
Protein Sequence	MTPLCPRPALCYHFLTSLLRSAMQNARGARQRAEAAVLSGPGPPLGRAAQHGIPRPLSSAGRLSQGCRGASTVGAAGWKGELPKAGGSPAPGPETPAISPSKRARPAEVGGMQLRFARLSEHATAPTRGSARAAGYDLYSAYDYTIPPMEKAVVKTDIQIALPSGCYGRVAPRSGLAAKHFIDVGAGVIDEDYRGNVGVVLFNFGKEKFEVKKGDRIAQLICERIFYPEIEEVQALDDTERGSGGFGSTGKN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4 (in isoform 2)	Phosphorylation	-	4.64	22167270
7 (in isoform 2)	Phosphorylation	-	28.29	22167270
11 (in isoform 2)	Phosphorylation	-	2.42	22167270
13 (in isoform 2)	Phosphorylation	-	15.39	30266825
14 (in isoform 2)	Ubiquitination	-	3.00	-
17	Phosphorylation	LCYHFLTSLLRSAMQ HHHHHHHHHHHHHHH	27.79	24719451
21	Phosphorylation	FLTSLLRSAMQNARG HHHHHHHHHHHHHHH	28.23	-
47	Methylation	GPGPPLGRAAQHGIP CCCCCCHHHHHHCCC	34.14	-
58	Phosphorylation	HGIPRPLSSAGRLSQ HCCCCCCCCCCCCCC	22.33	22210691
59	Phosphorylation	GIPRPLSSAGRLSQG CCCCCCCCCCCCCCC	42.28	22210691
63 (in isoform 2)	Ubiquitination	-	4.36	21890473
64	Phosphorylation	LSSAGRLSQGCRGAS CCCCCCCCCCCCCCC	24.14	-
67 (in isoform 2)	Ubiquitination	-	2.55	-
68	Methylation	GRLSQGCRGASTVGA CCCCCCCCCCCCCCC	51.00	-
71	Phosphorylation	SQGCRGASTVGAAGW CCCCCCCCCCCCCCC	26.84	28387310
72	Phosphorylation	QGCRGASTVGAAGWK CCCCCCCCCCCCCCC	23.56	30576142
84	Ubiquitination	GWKGELPKAGGSPAP CCCCCCCCCCCCCCC	72.75	-
88	Phosphorylation	ELPKAGGSPAPGPET CCCCCCCCCCCCCCC	19.57	29255136
91	Ubiquitination	KAGGSPAPGPETPAI CCCCCCCCCCCCCCC	63.36	19608861
91	Acetylation	KAGGSPAPGPETPAI CCCCCCCCCCCCCCC	63.36	19608861
91 (in isoform 2)	Ubiquitination	-	63.36	21890473
95	Phosphorylation	SPAPGPETPAISPSK CCCCCCCCCCCCCCC	22.58	30266825
99	Phosphorylation	GPETPAISPSKRARP CCCCCCCCCCCCCCC	25.81	29255136
101	Phosphorylation	ETPAISPSKRARPAE CCCCCCCCCCCCCCH	28.16	30266825
112	Sulfoxidation	RPAEVGGMQLRFARL CCCHHCCEEEEEEHH	2.52	21406390
115	Methylation	EVGGMQLRFARLSEH HHCCEEEEEEHHHCC	13.29	-
120	Phosphorylation	QLRFARLSEHATAPT EEEEEHHHCCCCCCC	23.06	25278378
120 (in isoform 2)	Ubiquitination	-	23.06	-
124	Phosphorylation	ARLSEHATAPTRGSA EHHHCCCCCCCCCCH	34.77	25278378
124	O-linked_Glycosylation	ARLSEHATAPTRGSA EHHHCCCCCCCCCCH	34.77	55821499
127	Phosphorylation	SEHATAPTRGSARAA HCCCCCCCCCCHHHC	45.24	25278378
127	O-linked_Glycosylation	SEHATAPTRGSARAA HCCCCCCCCCCHHHC	45.24	55821505
128	Methylation	EHATAPTRGSARAAG CCCCCCCCCCHHHCC	35.69	-
130	Phosphorylation	ATAPTRGSARAAGYD CCCCCCCCHHHCCCC	15.99	25278378
151	Ubiquitination	YTIPPMEKAVVKTDI CCCCCHHHCEEECEE	39.98	21906983
151 (in isoform 3)	Ubiquitination	-	39.98	21890473
155	Ubiquitination	PMEKAVVKTDIQIAL CHHHCEEECEEEEEC	33.60	-
155	Acetylation	PMEKAVVKTDIQIAL CHHHCEEECEEEEEC	33.60	25953088
155	Malonylation	PMEKAVVKTDIQIAL CHHHCEEECEEEEEC	33.60	26320211
156	Phosphorylation	MEKAVVKTDIQIALP HHHCEEECEEEEECC	27.07	26552605
163 (in isoform 2)	Ubiquitination	-	21.47	21890473
164	Phosphorylation	DIQIALPSGCYGRVA EEEEECCCCCCCCCC	42.20	28152594
166	Glutathionylation	QIALPSGCYGRVAPR EEECCCCCCCCCCCC	3.70	22555962
166	S-palmitoylation	QIALPSGCYGRVAPR EEECCCCCCCCCCCC	3.70	26865113
167	Phosphorylation	IALPSGCYGRVAPRS EECCCCCCCCCCCCC	16.11	28152594
174	Phosphorylation	YGRVAPRSGLAAKHF CCCCCCCCCCCHHHE	36.78	23898821
179 (in isoform 3)	Ubiquitination	-	33.18	21890473
179	Acetylation	PRSGLAAKHFIDVGA CCCCCCHHHEEEECC	33.18	23954790
179	Ubiquitination	PRSGLAAKHFIDVGA CCCCCCHHHEEEECC	33.18	21890473
193	Phosphorylation	AGVIDEDYRGNVGVV CCEECCCCCCCEEEE	20.55	-
206	Ubiquitination	VVLFNFGKEKFEVKK EEEEECCCCCEEEEC	54.30	-
208	Ubiquitination	LFNFGKEKFEVKKGD EEECCCCCEEEECCH	50.76	-
212	Acetylation	GKEKFEVKKGDRIAQ CCCCEEEECCHHHHH	43.79	25953088
216	Methylation	FEVKKGDRIAQLICE EEEECCHHHHHHHHH	34.51	-
222	Glutathionylation	DRIAQLICERIFYPE HHHHHHHHHHHHCCC	3.80	22555962
224	Methylation	IAQLICERIFYPEIE HHHHHHHHHHCCCHH	21.65	-
227	Phosphorylation	LICERIFYPEIEEVQ HHHHHHHCCCHHEEE	9.51	23186163
239	Phosphorylation	EVQALDDTERGSGGF EEEECCCCCCCCCCC	27.52	30266825
241	Methylation	QALDDTERGSGGFGS EECCCCCCCCCCCCC	46.82	-
243	Phosphorylation	LDDTERGSGGFGSTG CCCCCCCCCCCCCCC	41.80	30266825
248	Phosphorylation	RGSGGFGSTGKN--- CCCCCCCCCCCC---	31.55	30266825
249	Phosphorylation	GSGGFGSTGKN---- CCCCCCCCCCC----	53.18	23401153
251	Acetylation	GGFGSTGKN------ CCCCCCCCC------	60.62	23954790
251 (in isoform 3)	Ubiquitination	-	60.62	21890473
251	Ubiquitination	GGFGSTGKN------ CCCCCCCCC------	60.62	-

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
11	S	Phosphorylation	Kinase	CDK1	P06493	PSP
99	S	Phosphorylation	Kinase	CDK1	P06493	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
11	S	Phosphorylation		8631817
Nuclear isoform 2 is phosphorylated in vivo on Ser-11, a reaction that can be catalyzed in vitro by CDC2.

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 DUT_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SPAT2_HUMAN	SPATA2	physical	16189514
NUD18_HUMAN	NUDT18	physical	16189514
MAN1_HUMAN	LEMD3	physical	22939629
RL38_HUMAN	RPL38	physical	22939629
UBL4A_HUMAN	UBL4A	physical	22939629
RM14_HUMAN	MRPL14	physical	22939629
GDIR1_HUMAN	ARHGDIA	physical	26344197
EF1A1_HUMAN	EEF1A1	physical	26344197
ROA1_HUMAN	HNRNPA1	physical	26344197
HS74L_HUMAN	HSPA4L	physical	26344197
MOES_HUMAN	MSN	physical	26344197
RAB1A_HUMAN	RAB1A	physical	26344197
RAB1B_HUMAN	RAB1B	physical	26344197
TIAR_HUMAN	TIAL1	physical	26344197
TYSY_HUMAN	TYMS	physical	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 DUT_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-179, AND MASS SPECTROMETRY.	19608861 [Abstract]

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