dbPTM

MGMT_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MGMT_HUMAN
UniProt AC	P16455
Protein Name	Methylated-DNA--protein-cysteine methyltransferase
Gene Name	MGMT
Organism	Homo sapiens (Human).
Sequence Length	207
Subcellular Localization	Nucleus.
Protein Description	Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated..
Protein Sequence	MDKDCEMKRTTLDSPLGKLELSGCEQGLHEIKLLGKGTSAADAVEVPAPAAVLGGPEPLMQCTAWLNAYFHQPEAIEEFPVPALHHPVFQQESFTRQVLWKLLKVVKFGEVISYQQLAALAGNPKAARAVGGAMRGNPVPILIPCHRVVCSSGAVGNYSGGLAVKEWLLAHEGHRLGKPGLGGSSGLAGAWLKGAGATSGSPPAGRN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
8	Ubiquitination	MDKDCEMKRTTLDSP CCCCCCCCCCCCCCC	25.05	-
10	Phosphorylation	KDCEMKRTTLDSPLG CCCCCCCCCCCCCCC	26.62	22817900
11	Phosphorylation	DCEMKRTTLDSPLGK CCCCCCCCCCCCCCE	32.38	22817900
14	Phosphorylation	MKRTTLDSPLGKLEL CCCCCCCCCCCEEEC	25.74	21815630
22	Phosphorylation	PLGKLELSGCEQGLH CCCEEECCCCCCCHH	31.83	28555341
32	Ubiquitination	EQGLHEIKLLGKGTS CCCHHEEEECCCCCC	34.37	-
39	Ubiquitination	KLLGKGTSAADAVEV EECCCCCCHHHCEEC	30.08	-
41	Phosphorylation	LGKGTSAADAVEVPA CCCCCCHHHCEECCC	12.69	-
42	Phosphorylation	GKGTSAADAVEVPAP CCCCCHHHCEECCCC	51.36	-
45	Phosphorylation	TSAADAVEVPAPAAV CCHHHCEECCCCCHH	44.50	-
49	Ubiquitination	DAVEVPAPAAVLGGP HCEECCCCCHHHCCC	18.06	-
53	Phosphorylation	VPAPAAVLGGPEPLM CCCCCHHHCCCHHHH	5.87	-
63	Ubiquitination	PEPLMQCTAWLNAYF CHHHHHHHHHHHHHH	12.18	-
101	Acetylation	FTRQVLWKLLKVVKF HHHHHHHHHHHHHHH	39.52	25953088
101	Ubiquitination	FTRQVLWKLLKVVKF HHHHHHHHHHHHHHH	39.52	-
104	Ubiquitination	QVLWKLLKVVKFGEV HHHHHHHHHHHHHCE	56.25	-
125	Ubiquitination	AALAGNPKAARAVGG HHHHCCHHHHHHHCH	59.69	-
132	Ubiquitination	KAARAVGGAMRGNPV HHHHHHCHHHCCCCC	15.03	-
135	Ubiquitination	RAVGGAMRGNPVPIL HHHCHHHCCCCCCEE	41.00	-
156	Ubiquitination	VCSSGAVGNYSGGLA EECCCCCCCCCCCHH	27.16	-
158	Phosphorylation	SSGAVGNYSGGLAVK CCCCCCCCCCCHHHH	11.63	21945579
159	Phosphorylation	SGAVGNYSGGLAVKE CCCCCCCCCCHHHHH	30.31	21945579
165	Ubiquitination	YSGGLAVKEWLLAHE CCCCHHHHHHHHHCC	37.25	-
165	Acetylation	YSGGLAVKEWLLAHE CCCCHHHHHHHHHCC	37.25	23749302
178	Ubiquitination	HEGHRLGKPGLGGSS CCCCCCCCCCCCCCC	40.27	21890473
184	O-linked_Glycosylation	GKPGLGGSSGLAGAW CCCCCCCCCCCHHHH	21.31	29351928
184	Phosphorylation	GKPGLGGSSGLAGAW CCCCCCCCCCCHHHH	21.31	28450419
185	Phosphorylation	KPGLGGSSGLAGAWL CCCCCCCCCCHHHHH	40.89	28450419
196	Acetylation	GAWLKGAGATSGSPP HHHHCCCCCCCCCCC	37.75	-
196	Ubiquitination	GAWLKGAGATSGSPP HHHHCCCCCCCCCCC	37.75	-
198	Phosphorylation	WLKGAGATSGSPPAG HHCCCCCCCCCCCCC	32.47	24972180
199	Phosphorylation	LKGAGATSGSPPAGR HCCCCCCCCCCCCCC	36.42	25159151
201	Phosphorylation	GAGATSGSPPAGRN- CCCCCCCCCCCCCC-	27.72	25159151
209	Ubiquitination	PPAGRN--------- CCCCCC---------		-
224	Ubiquitination	------------------------ ------------------------		-
232	Phosphorylation	-------------------------------- --------------------------------		15302935

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 MGMT_HUMAN !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ESR1_HUMAN	ESR1	physical	11564893
SMC1A_HUMAN	SMC1A	physical	16226712
H2BFM_HUMAN	H2BFM	physical	16226712
H31T_HUMAN	HIST3H3	physical	16226712
MCM3_HUMAN	MCM3	physical	16226712
MSH2_HUMAN	MSH2	physical	16226712
TOP1_HUMAN	TOP1	physical	16226712
PRKDC_HUMAN	PRKDC	physical	16226712
XRCC6_HUMAN	XRCC6	physical	16226712
DDX5_HUMAN	DDX5	physical	16226712
DDX24_HUMAN	DDX24	physical	16226712
UBP19_HUMAN	USP19	physical	16226712
RNF8_HUMAN	RNF8	physical	16226712
PSME2_HUMAN	PSME2	physical	16226712
UBB_HUMAN	UBB	physical	16226712
PSMD9_HUMAN	PSMD9	physical	16226712
FBX2_HUMAN	FBXO2	physical	16226712
FBX27_HUMAN	FBXO27	physical	16226712
HS90A_HUMAN	HSP90AA1	physical	16226712
HS90B_HUMAN	HSP90AB1	physical	16226712
CDK12_HUMAN	CDK12	physical	16226712
CDK10_HUMAN	CDK10	physical	16226712
KPCL_HUMAN	PRKCH	physical	16226712
PRP4_HUMAN	PRPF4	physical	16226712
CDKL5_HUMAN	CDKL5	physical	16226712
SET_HUMAN	SET	physical	16226712
PTN4_HUMAN	PTPN4	physical	16226712
1433Z_HUMAN	YWHAZ	physical	16226712
IMB1_HUMAN	KPNB1	physical	16226712
WNT9B_HUMAN	WNT9B	physical	16226712
PABP3_HUMAN	PABPC3	physical	16226712
AN32E_HUMAN	ANP32E	physical	16226712
NUCL_HUMAN	NCL	physical	16226712
ROA2_HUMAN	HNRNPA2B1	physical	16226712
HNRPC_HUMAN	HNRNPC	physical	16226712
RS15A_HUMAN	RPS15A	physical	16226712
RLA1_HUMAN	RPLP1	physical	16226712
EIF3H_HUMAN	EIF3H	physical	16226712
EF1A1_HUMAN	EEF1A1	physical	16226712
EF1A2_HUMAN	EEF1A2	physical	16226712
EF1B_HUMAN	EEF1B2	physical	16226712
ADT1_HUMAN	SLC25A4	physical	16226712
ADT3_HUMAN	SLC25A6	physical	16226712
KPYM_HUMAN	PKM	physical	16226712
TTPA_HUMAN	TTPA	physical	16226712
IL25_HUMAN	IL25	physical	16226712
FBRL_HUMAN	FBL	physical	16226712
TBB4B_HUMAN	TUBB4B	physical	16226712
TBA1C_HUMAN	TUBA1C	physical	16226712
ANXA1_HUMAN	ANXA1	physical	16226712
ANXA2_HUMAN	ANXA2	physical	16226712
ACTB_HUMAN	ACTB	physical	16226712
MYO7A_HUMAN	MYO7A	physical	16226712
VIME_HUMAN	VIM	physical	16226712
PHB_HUMAN	PHB	physical	16226712
SRP09_HUMAN	SRP9	physical	16226712
SSRP1_HUMAN	SSRP1	physical	16226712
PCNA_HUMAN	PCNA	physical	16226712
CDK2_HUMAN	CDK2	physical	16226712
CDK1_HUMAN	CDK1	physical	16226712
CCNB1_HUMAN	CCNB1	physical	16226712
CDN1A_HUMAN	CDKN1A	physical	16226712
MCM2_HUMAN	MCM2	physical	16226712
ORC1_HUMAN	ORC1	physical	16226712
DPOD1_HUMAN	POLD1	physical	16226712
BRCA2_HUMAN	BRCA2	physical	19047179
FANCA_HUMAN	FANCA	physical	28215707

Drug and Disease Associations

Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
DB00151	L-Cysteine

Regulatory Network of MGMT_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-201, AND MASSSPECTROMETRY.	15302935 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-10 AND THR-11, AND MASSSPECTROMETRY.	18187866 [Abstract]