dbPTM

NNMT_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NNMT_HUMAN
UniProt AC	P40261
Protein Name	Nicotinamide N-methyltransferase
Gene Name	NNMT
Organism	Homo sapiens (Human).
Sequence Length	264
Subcellular Localization	Cytoplasm.
Protein Description	Catalyzes the N-methylation of nicotinamide and other pyridines to form pyridinium ions. This activity is important for biotransformation of many drugs and xenobiotic compounds..
Protein Sequence	MESGFTSKDTYLSHFNPRDYLEKYYKFGSRHSAESQILKHLLKNLFKIFCLDGVKGDLLIDIGSGPTIYQLLSACESFKEIVVTDYSDQNLQELEKWLKKEPEAFDWSPVVTYVCDLEGNRVKGPEKEEKLRQAVKQVLKCDVTQSQPLGAVPLPPADCVLSTLCLDAACPDLPTYCRALRNLGSLLKPGGFLVIMDALKSSYYMIGEQKFSSLPLGREAVEAAVKEAGYTIEWFEVISQSYSSTMANNEGLFSLVARKLSRPL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----MESGFTSKDT -----CCCCCCCCCC	37.60	-
8	2-Hydroxyisobutyrylation	MESGFTSKDTYLSHF CCCCCCCCCCCHHHC	51.54	-
8	Ubiquitination	MESGFTSKDTYLSHF CCCCCCCCCCCHHHC	51.54	-
8	Succinylation	MESGFTSKDTYLSHF CCCCCCCCCCCHHHC	51.54	23954790
8	Acetylation	MESGFTSKDTYLSHF CCCCCCCCCCCHHHC	51.54	27452117
8	"N6,N6-dimethyllysine"	MESGFTSKDTYLSHF CCCCCCCCCCCHHHC	51.54	-
8	Methylation	MESGFTSKDTYLSHF CCCCCCCCCCCHHHC	51.54	23644510
11	Phosphorylation	GFTSKDTYLSHFNPR CCCCCCCCHHHCCHH	19.15	25159151
13	Phosphorylation	TSKDTYLSHFNPRDY CCCCCCHHHCCHHHH	18.67	28857561
23	Ubiquitination	NPRDYLEKYYKFGSR CHHHHHHHHHHHCCC	51.81	-
23	Succinylation	NPRDYLEKYYKFGSR CHHHHHHHHHHHCCC	51.81	23954790
23	2-Hydroxyisobutyrylation	NPRDYLEKYYKFGSR CHHHHHHHHHHHCCC	51.81	-
23	Acetylation	NPRDYLEKYYKFGSR CHHHHHHHHHHHCCC	51.81	27178108
23	Malonylation	NPRDYLEKYYKFGSR CHHHHHHHHHHHCCC	51.81	26320211
24	Phosphorylation	PRDYLEKYYKFGSRH HHHHHHHHHHHCCCC	11.51	-
25	Phosphorylation	RDYLEKYYKFGSRHS HHHHHHHHHHCCCCC	15.77	-
26	Malonylation	DYLEKYYKFGSRHSA HHHHHHHHHCCCCCH	39.91	26320211
26	2-Hydroxyisobutyrylation	DYLEKYYKFGSRHSA HHHHHHHHHCCCCCH	39.91	-
26	Acetylation	DYLEKYYKFGSRHSA HHHHHHHHHCCCCCH	39.91	26051181
26	Ubiquitination	DYLEKYYKFGSRHSA HHHHHHHHHCCCCCH	39.91	-
29	Phosphorylation	EKYYKFGSRHSAESQ HHHHHHCCCCCHHHH	29.92	27690223
32	Phosphorylation	YKFGSRHSAESQILK HHHCCCCCHHHHHHH	32.40	20068231
35	Phosphorylation	GSRHSAESQILKHLL CCCCCHHHHHHHHHH	23.41	20068231
39	Acetylation	SAESQILKHLLKNLF CHHHHHHHHHHHHHH	33.56	19608861
39	Ubiquitination	SAESQILKHLLKNLF CHHHHHHHHHHHHHH	33.56	19608861
39	Malonylation	SAESQILKHLLKNLF CHHHHHHHHHHHHHH	33.56	26320211
43	Acetylation	QILKHLLKNLFKIFC HHHHHHHHHHHHHHC	58.95	23954790
43	Ubiquitination	QILKHLLKNLFKIFC HHHHHHHHHHHHHHC	58.95	-
47	Ubiquitination	HLLKNLFKIFCLDGV HHHHHHHHHHCCCCC	37.73	-
47	2-Hydroxyisobutyrylation	HLLKNLFKIFCLDGV HHHHHHHHHHCCCCC	37.73	-
47	Acetylation	HLLKNLFKIFCLDGV HHHHHHHHHHCCCCC	37.73	26051181
96	Ubiquitination	QNLQELEKWLKKEPE HCHHHHHHHHHHCCC	71.14	-
100	Ubiquitination	ELEKWLKKEPEAFDW HHHHHHHHCCCCCCC	76.08	-
108	Phosphorylation	EPEAFDWSPVVTYVC CCCCCCCCCEEEEEE	15.06	25159151
113	Phosphorylation	DWSPVVTYVCDLEGN CCCCEEEEEEECCCC	6.35	24927040
123	Ubiquitination	DLEGNRVKGPEKEEK ECCCCCCCCHHHHHH	66.56	-
136	Ubiquitination	EKLRQAVKQVLKCDV HHHHHHHHHHHCCCC	37.39	-
185	Phosphorylation	RALRNLGSLLKPGGF HHHHHHHHHCCCCEE	33.42	24719451
201	Phosphorylation	VIMDALKSSYYMIGE EEEEHHHHCEEEECC	25.15	27642862
203	Phosphorylation	MDALKSSYYMIGEQK EEHHHHCEEEECCCC	12.25	27642862
204	Phosphorylation	DALKSSYYMIGEQKF EHHHHCEEEECCCCC	5.56	27642862
205	Sulfoxidation	ALKSSYYMIGEQKFS HHHHCEEEECCCCCC	2.11	30846556
210	Ubiquitination	YYMIGEQKFSSLPLG EEEECCCCCCCCCCC	42.80	-
261	Phosphorylation	SLVARKLSRPL---- HHHHHHHCCCC----	34.58	23927012

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 NNMT_HUMAN !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
A4_HUMAN	APP	physical	21832049
GLOD4_HUMAN	GLOD4	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
DB00627	Niacin

Regulatory Network of NNMT_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-39, AND MASS SPECTROMETRY.	19608861 [Abstract]