NEUG_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: NEUG_HUMAN
• UniProt AC: Q92686
• Protein Name: Neurogranin
• Gene Name: NRGN
• Organism: Homo sapiens (Human).
• Sequence Length: 78
• Protein Description: Acts as a "third messenger" substrate of protein kinase C-mediated molecular cascades during synaptic development and remodeling. Binds to calmodulin in the absence of calcium (By similarity)..
• Protein Sequence: MDCCTENACSKPDDDILDIPLDDPGANAAAAKIQASFRGHMARKKIKSGERGRKGPGPGGPGGAGVARGGAGGGPSGD

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
1	Acetylation	-------MDCCTENA -------CCCCCCCC	8.86	19413330
3	S-glutathionyl cysteine	-----MDCCTENACS -----CCCCCCCCCC	2.74	-
4	S-glutathionyl cysteine	----MDCCTENACSK ----CCCCCCCCCCC	4.69	-
5	Phosphorylation	---MDCCTENACSKP ---CCCCCCCCCCCC	38.31	28060719
9	S-glutathionyl cysteine	DCCTENACSKPDDDI CCCCCCCCCCCCCCC	8.95	-
10	Phosphorylation	CCTENACSKPDDDIL CCCCCCCCCCCCCCC	44.83	28060719
36	Phosphorylation	AAAKIQASFRGHMAR HHHHHHHHHHHHHHH	10.09	8424932
38	Methylation	AKIQASFRGHMARKK HHHHHHHHHHHHHHH	31.45	54557547
48	Phosphorylation	MARKKIKSGERGRKG HHHHHHHCCCCCCCC	49.73	29457462
68	Citrullination	PGGAGVARGGAGGGP CCCCCCCCCCCCCCC	41.49	-
68	Methylation	PGGAGVARGGAGGGP CCCCCCCCCCCCCCC	41.49	24129315
68	Citrullination	PGGAGVARGGAGGGP CCCCCCCCCCCCCCC	41.49	23828821

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
36	S	Phosphorylation	Kinase	PKCA	P17252	PSP
36	S	Phosphorylation	Kinase	PRKCA	P05696	GPS
36	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
36	S	Phosphorylation	Kinase	PHK	-	Uniprot
36	S	Phosphorylation	Kinase	PKC	-	Uniprot
36	S	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
36	S	Phosphorylation	Phosphorylated at Ser-36 by PHK and PKC, phosphorylation prevents interaction with Calmodulin and interrupts several learning- and memory-associated functions.	-

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of NEUG_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TRI62_HUMAN	TRIM62	physical	28514442
EFCB7_HUMAN	EFCAB7	physical	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.

Related Literatures of Post-Translational Modification

Acetylation

"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
PubMed: 19413330