3MG_HUMAN - dbPTM
3MG_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID 3MG_HUMAN
UniProt AC P29372
Protein Name DNA-3-methyladenine glycosylase
Gene Name MPG
Organism Homo sapiens (Human).
Sequence Length 298
Subcellular Localization Cytoplasm . Mitochondrion matrix, mitochondrion nucleoid . Nucleus .
Protein Description Hydrolysis of the deoxyribose N-glycosidic bond to excise 3-methyladenine, and 7-methylguanine from the damaged DNA polymer formed by alkylation lesions..
Protein Sequence MVTPALQMKKPKQFCRRMGQKKQRPARAGQPHSSSDAAQAPAEQPHSSSDAAQAPCPRERCLGPPTTPGPYRSIYFSSPKGHLTRLGLEFFDQPAVPLARAFLGQVLVRRLPNGTELRGRIVETEAYLGPEDEAAHSRGGRQTPRNRGMFMKPGTLYVYIIYGMYFCMNISSQGDGACVLLRALEPLEGLETMRQLRSTLRKGTASRVLKDRELCSGPSKLCQALAINKSFDQRDLAQDEAVWLERGPLEPSEPAVVAAARVGVGHAGEWARKPLRFYVRGSPWVSVVDRVAEQDTQA
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
5 (in isoform 4)Phosphorylation-10.8926552605
5 (in isoform 2)Phosphorylation-10.8926552605
34PhosphorylationRAGQPHSSSDAAQAP
CCCCCCCCCCHHHCC
29.2428165663
35PhosphorylationAGQPHSSSDAAQAPA
CCCCCCCCCHHHCCC
33.9928555341
48PhosphorylationPAEQPHSSSDAAQAP
CCCCCCCCCCHHHCC
29.2428555341
66PhosphorylationERCLGPPTTPGPYRS
HHCCCCCCCCCCCEE
49.0828348404
67PhosphorylationRCLGPPTTPGPYRSI
HCCCCCCCCCCCEEE
31.8322617229
71PhosphorylationPPTTPGPYRSIYFSS
CCCCCCCCEEEEEEC
23.9423403867
73PhosphorylationTTPGPYRSIYFSSPK
CCCCCCEEEEEECCC
18.7920068231
75UbiquitinationPGPYRSIYFSSPKGH
CCCCEEEEEECCCCH
9.9221890473
75 (in isoform 2)Ubiquitination-9.9221890473
75PhosphorylationPGPYRSIYFSSPKGH
CCCCEEEEEECCCCH
9.9229396449
77PhosphorylationPYRSIYFSSPKGHLT
CCEEEEEECCCCHHH
28.8525159151
78PhosphorylationYRSIYFSSPKGHLTR
CEEEEEECCCCHHHH
22.2625159151
80UbiquitinationSIYFSSPKGHLTRLG
EEEEECCCCHHHHHC
61.9921890473
80 (in isoform 1)Ubiquitination-61.9921890473
115PhosphorylationVRRLPNGTELRGRIV
HHCCCCCCEEECEEE
38.19-
137PhosphorylationPEDEAAHSRGGRQTP
CCCHHHHHCCCCCCC
28.08-
162NitrationTLYVYIIYGMYFCMN
CEEEEEEEEHHHHHH
6.05-
210UbiquitinationGTASRVLKDRELCSG
CCHHHHHCCHHHCCC
52.46-
224 (in isoform 2)Ubiquitination-9.6621890473
224UbiquitinationGPSKLCQALAINKSF
CHHHHHHHHHHCCCC
9.6621890473
229 (in isoform 1)Ubiquitination-46.5221890473
229UbiquitinationCQALAINKSFDQRDL
HHHHHHCCCCCHHHH
46.522189047
230PhosphorylationQALAINKSFDQRDLA
HHHHHCCCCCHHHHH
29.5729214152
252PhosphorylationERGPLEPSEPAVVAA
HCCCCCCCCCHHHHE
47.0021082442
278PhosphorylationARKPLRFYVRGSPWV
HCCCEEEEECCCCCE
5.25-

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 3MG_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of 3MG_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 3MG_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LRC59_HUMANLRRC59physical
17353931
FBLN1_HUMANFBLN1physical
17353931
GSTM3_HUMANGSTM3physical
17353931
AATM_HUMANGOT2physical
17353931
RANG_HUMANRANBP1physical
17353931
APRIO_HUMANPRNPphysical
18482256
PRIO_HUMANPRNPphysical
18482256
A4_HUMANAPPphysical
21832049
SRSF1_HUMANSRSF1physical
23537643
SPA12_HUMANSERPINA12physical
23537643
UHRF1_HUMANUHRF1physical
23537643
RFC4_HUMANRFC4physical
23537643
KPYM_HUMANPKMphysical
23537643
PR38B_HUMANPRPF38Bphysical
23537643
PRDX1_HUMANPRDX1physical
23537643
NCBP1_HUMANNCBP1physical
23537643
FXR2_HUMANFXR2physical
23537643
FILA_HUMANFLGphysical
23537643
DHX33_HUMANDHX33physical
23537643
CDSN_HUMANCDSNphysical
23537643
FUBP2_HUMANKHSRPphysical
23537643
RGAP1_HUMANRACGAP1physical
23537643
GELS_HUMANGSNphysical
23537643
CAZA1_HUMANCAPZA1physical
23537643
LSHR_HUMANLHCGRphysical
23537643
TFP11_HUMANTFIP11physical
23537643
NOC2L_HUMANNOC2Lphysical
23537643
MO4L1_HUMANMORF4L1physical
23537643
CLAP2_HUMANCLASP2physical
23537643
SNUT1_HUMANSART1physical
23537643
PP1RA_HUMANPPP1R10physical
23537643
RPRD2_HUMANRPRD2physical
23537643
OBSCN_HUMANOBSCNphysical
23537643
GNL3_HUMANGNL3physical
23537643
RPA43_HUMANTWISTNBphysical
23537643
CSTF1_HUMANCSTF1physical
23537643
KDM2A_HUMANKDM2Aphysical
23537643
RRP1B_HUMANRRP1Bphysical
23537643
RRP7A_HUMANRRP7Aphysical
23537643
NOG2_HUMANGNL2physical
23537643
LARP4_HUMANLARP4physical
23537643
EXOS9_HUMANEXOSC9physical
23537643
CYTM_HUMANCST6physical
23537643
KPRP_HUMANKPRPphysical
23537643
UHRF2_HUMANUHRF2physical
23537643
DHB14_HUMANHSD17B14physical
25416956
ELP1_HUMANIKBKAPphysical
26186194
ELP3_HUMANELP3physical
26186194
ELP2_HUMANELP2physical
26186194
KBTB4_HUMANKBTBD4physical
26186194
EIF2A_HUMANEIF2Aphysical
26344197
KIFC1_HUMANKIFC1physical
26344197
KBTB4_HUMANKBTBD4physical
28514442
ELP3_HUMANELP3physical
28514442
ELP2_HUMANELP2physical
28514442
ELP1_HUMANIKBKAPphysical
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 3MG_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-78, AND MASSSPECTROMETRY.
"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 SER-252, AND MASSSPECTROMETRY.

TOP