dbPTM

UNG_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	UNG_HUMAN
UniProt AC	P13051
Protein Name	Uracil-DNA glycosylase {ECO:0000255\|HAMAP-Rule:MF_03166}
Gene Name	UNG {ECO:0000255\|HAMAP-Rule:MF_03166}
Organism	Homo sapiens (Human).
Sequence Length	313
Subcellular Localization	Isoform 1: Mitochondrion. Isoform 2: Nucleus.
Protein Description	Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine..
Protein Sequence	MIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEESGDAAAIPAKKAPAGQEEPGTPPSSPLSAEQLDRIQRNKAAALLRLAARNVPVGFGESWKKHLSGEFGKPYFIKLMGFVAEERKHYTVYPPPHQVFTWTQMCDIKDVKVVILGQDPYHGPNQAHGLCFSVQRPVPPPPSLENIYKELSTDIEDFVHPGHGDLSGWAKQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNSNGLVFLLWGSYAQKKGSAIDRKRHHVLQTAHPSPLSVYRGFFGCRHFSKTNELLQKSGKKPIDWKEL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MIGQKTLY -------CCCCCCHH	7.58	-
5	Acetylation	---MIGQKTLYSFFS ---CCCCCCHHCCCC	34.97	23954790
5 (in isoform 1)	Ubiquitination	-	34.97	21890473
5	Ubiquitination	---MIGQKTLYSFFS ---CCCCCCHHCCCC	34.97	21890473
6	Phosphorylation	--MIGQKTLYSFFSP --CCCCCCHHCCCCC	24.04	21945579
8	Phosphorylation	MIGQKTLYSFFSPSP CCCCCCHHCCCCCCH	14.52	21945579
9	Phosphorylation	IGQKTLYSFFSPSPA CCCCCHHCCCCCCHH	23.95	21945579
12	Phosphorylation	KTLYSFFSPSPARKR CCHHCCCCCCHHHHC	23.58	21945579
14	Phosphorylation	LYSFFSPSPARKRHA HHCCCCCCHHHHCCC	29.96	23401153
23	Phosphorylation	ARKRHAPSPEPAVQG HHHCCCCCCCCCCCC	42.55	29255136
27 (in isoform 2)	Phosphorylation	-	12.47	-
31	Phosphorylation	PEPAVQGTGVAGVPE CCCCCCCCCCCCCCC	16.05	29255136
40	Phosphorylation	VAGVPEESGDAAAIP CCCCCCCCCCCCCEE	40.07	29255136
49 (in isoform 1)	Ubiquitination	-	44.08	21890473
49	Acetylation	DAAAIPAKKAPAGQE CCCCEECCCCCCCCC	44.08	25953088
49	Ubiquitination	DAAAIPAKKAPAGQE CCCCEECCCCCCCCC	44.08	21906983
50	Ubiquitination	AAAIPAKKAPAGQEE CCCEECCCCCCCCCC	62.80	-
51 (in isoform 2)	Phosphorylation	-	9.85	-
54 (in isoform 2)	Phosphorylation	-	34.08	-
55 (in isoform 2)	Phosphorylation	-	54.72	-
58 (in isoform 2)	Phosphorylation	-	51.73	-
60	Phosphorylation	AGQEEPGTPPSSPLS CCCCCCCCCCCCCCC	42.62	29255136
63	Phosphorylation	EEPGTPPSSPLSAEQ CCCCCCCCCCCCHHH	45.88	29255136
64	Phosphorylation	EPGTPPSSPLSAEQL CCCCCCCCCCCHHHH	35.32	29255136
67	Phosphorylation	TPPSSPLSAEQLDRI CCCCCCCCHHHHHHH	32.89	29255136
69 (in isoform 2)	Ubiquitination	-	48.58	22053931
78	Ubiquitination	LDRIQRNKAAALLRL HHHHHHHHHHHHHHH	41.41	22053931
99	Malonylation	VGFGESWKKHLSGEF CCCCHHHHHHHCCCC	39.33	32601280
100	Ubiquitination	GFGESWKKHLSGEFG CCCHHHHHHHCCCCC	43.45	-
103	Phosphorylation	ESWKKHLSGEFGKPY HHHHHHHCCCCCCCH	35.68	27067055
108	Ubiquitination	HLSGEFGKPYFIKLM HHCCCCCCCHHHHHH	41.69	-
125	Phosphorylation	VAEERKHYTVYPPPH HHCCCCCEEECCCCH	10.84	29496907
126	Phosphorylation	AEERKHYTVYPPPHQ HCCCCCEEECCCCHH	17.18	22817900
128	Phosphorylation	ERKHYTVYPPPHQVF CCCCEEECCCCHHEE	11.39	-
188	Phosphorylation	NIYKELSTDIEDFVH HHHHHHCCCHHHHCC	54.33	-
261	Ubiquitination	WGSYAQKKGSAIDRK EHHHHHHCCCHHHHH	46.12	-
279	Phosphorylation	VLQTAHPSPLSVYRG HHCCCCCCCHHHHHC	28.71	29214152
282	Phosphorylation	TAHPSPLSVYRGFFG CCCCCCHHHHHCCCC	22.08	24719451
284	Phosphorylation	HPSPLSVYRGFFGCR CCCCHHHHHCCCCCC	11.14	-
286 (in isoform 2)	Acetylation	-	12.44	-
286 (in isoform 2)	Ubiquitination	-	12.44	22053931
293 (in isoform 2)	Ubiquitination	-	4.07	22053931
295 (in isoform 1)	Ubiquitination	-	55.19	21890473
295	Ubiquitination	FGCRHFSKTNELLQK CCCCCHHHHHHHHHH	55.19	21906983
295	Acetylation	FGCRHFSKTNELLQK CCCCCHHHHHHHHHH	55.19	19608861
302 (in isoform 1)	Ubiquitination	-	62.23	21890473
302	Ubiquitination	KTNELLQKSGKKPID HHHHHHHHCCCCCCC	62.23	2190698

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
12	S	Phosphorylation	Kinase	CDK2	P24941	PSP
23	S	Phosphorylation	Kinase	CDK2	P24941	PSP
60	T	Phosphorylation	Kinase	CDK2	P24941	PSP
60	T	Phosphorylation	Kinase	GSK3A	P49840	PSP
60	T	Phosphorylation	Kinase	GSK3B	P49841	PSP
64	S	Phosphorylation	Kinase	CDK1	P06493	PSP
64	S	Phosphorylation	Kinase	CDK2	P24941	PSP
64	S	Phosphorylation	Kinase	GSK3A	P49840	PSP
64	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	DCAF1	Q9Y4B6	PMID:20870715

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of UNG_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 UNG_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RFA2_HUMAN	RPA2	physical	9045683
DPOLB_HUMAN	POLB	physical	10629618
HSPB1_HUMAN	HSPB1	physical	10629618
A4_HUMAN	APP	physical	21832049
PCNA_HUMAN	PCNA	physical	10393198
RFA2_HUMAN	RPA2	physical	10393198
DCAF1_HUMAN	VPRBP	physical	22292079
DDB1_HUMAN	DDB1	physical	22292079

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
608106	Immunodeficiency with hyper-IgM 5 (HIGM5)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of UNG_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 MET-1; LYS-5 AND LYS-295, ANDMASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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-14; SER-23; THR-60 ANDSER-64, AND MASS SPECTROMETRY.	19690332 [Abstract]
"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-23; THR-60; SER-63;SER-64 AND SER-67, AND MASS SPECTROMETRY.	19413330 [Abstract]
"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-12; SER-14; SER-23;THR-60; SER-63 AND SER-64, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12 AND SER-14, AND MASSSPECTROMETRY.	18220336 [Abstract]
"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 THR-60 AND SER-63, AND MASSSPECTROMETRY.	17287340 [Abstract]
"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-23 AND THR-60, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-60, AND MASSSPECTROMETRY.	15302935 [Abstract]