dbPTM

NLGN1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NLGN1_MOUSE
UniProt AC	Q99K10
Protein Name	Neuroligin-1
Gene Name	Nlgn1
Organism	Mus musculus (Mouse).
Sequence Length	843
Subcellular Localization	Cell membrane Single-pass type I membrane protein. Cell junction, synapse. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density. Enriched in synaptic plasma membranes and clustered in synaptic clefts and postsynaptic densities. D
Protein Description	Cell surface protein involved in cell-cell-interactions via its interactions with neurexin family members. Plays a role in synapse function and synaptic signal transmission, and probably mediates its effects by recruiting and clustering other synaptic proteins. May promote the initial formation of synapses, but is not essential for this. In vitro, triggers the de novo formation of presynaptic structures. May be involved in specification of excitatory synapses. Required to maintain wakefulness quality and normal synchrony of cerebral cortex activity during wakefulness and sleep. [PubMed: 23716671]
Protein Sequence	MALPRCMWPNYVWRAMMACVVHRGSGAPLTLCLLGCLLQTFHVLSQKLDDVDPLVTTNFGKIRGIKKELNNEILGPVIQFLGVPYAAPPTGEHRFQPPEPPSPWSDIRNATQFAPVCPQNIIDGRLPEVMLPVWFTNNLDVVSSYVQDQSEDCLYLNIYVPTEDGPLTKKHTDDLGDNDGAEDEDIRDSGGPKPVMVYIHGGSYMEGTGNLYDGSVLASYGNVIVITVNYRLGVLGFLSTGDQAAKGNYGLLDLIQALRWTSENIGFFGGDPLRITVFGSGAGGSCVNLLTLSHYSEGNRWSNSTKGLFQRAIAQSGTALSSWAVSFQPAKYARILATKVGCNVSDTVELVECLQKKPYKELVDQDVQPARYHIAFGPVIDGDVIPDDPQILMEQGEFLNYDIMLGVNQGEGLKFVENIVDSDDGVSASDFDFAVSNFVDNLYGYPEGKDVLRETIKFMYTDWADRHNPETRRKTLLALFTDHQWVAPAVATADLHSNFGSPTYFYAFYHHCQTDQVPAWADAAHGDEVPYVLGIPMIGPTELFPCNFSKNDVMLSAVVMTYWTNFAKTGDPNQPVPQDTKFIHTKPNRFEEVAWTRYSQKDQLYLHIGLKPRVKEHYRANKVNLWLELVPHLHNLNDISQYTSTTTKVPSTDITLRPTRKNSTPVTSAFPTAKQDDPKQQPSPFSVDQRDYSTELSVTIAVGASLLFLNILAFAALYYKKDKRRHDVHRRCSPQRTTTNDLTHAPEEEIMSLQMKHTDLDHECESIHPHEVVLRTACPPDYTLAMRRSPDDIPLMTPNTITMIPNTIPGIQPLHTFNTFTGGQNNTLPHPHPHPHSHSTTRV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
109	N-linked_Glycosylation	SPWSDIRNATQFAPV CCHHHHCCCCCCCCC	47.90	18084303
303	N-linked_Glycosylation	SEGNRWSNSTKGLFQ CCCCCCCCCHHHHHH	46.90	-
343	N-linked_Glycosylation	LATKVGCNVSDTVEL HHCCCCCCHHHHHHH	30.33	-
547	N-linked_Glycosylation	PTELFPCNFSKNDVM CCCCCCCCCCCCHHH	44.45	18084303
683	O-linked_Glycosylation	DDPKQQPSPFSVDQR CCCCCCCCCCCCCCC	33.95	-
686	O-linked_Glycosylation	KQQPSPFSVDQRDYS CCCCCCCCCCCCCCC	28.33	-
733	Phosphorylation	HDVHRRCSPQRTTTN HCCHHHCCCCCCCCC	23.43	-
739	Phosphorylation	CSPQRTTTNDLTHAP CCCCCCCCCCCCCCC	26.56	-
752	Phosphorylation	APEEEIMSLQMKHTD CCHHHHHHHHCCCCC	22.55	29899451
766	Phosphorylation	DLDHECESIHPHEVV CCCCCCCCCCCCCEE	37.54	29899451
782	Phosphorylation	RTACPPDYTLAMRRS EECCCCCCEEEECCC	14.93	-

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
739	T	Phosphorylation	Kinase	CAMK2A	Q9UQM7	PSP
782	Y	Phosphorylation	Kinase	FGFR1	P11362	PSP
782	Y	Phosphorylation	Kinase	FGFR1	P16092	PSP
782	Y	Phosphorylation	Kinase	TRKB	Q16620	PSP
782	Y	Phosphorylation	Kinase	TRKC	Q16288	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of NLGN1_MOUSE !!

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 NLGN1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of NLGN1_MOUSE !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of NLGN1_MOUSE

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Structural basis for synaptic adhesion mediated by neuroligin-neurexin interactions."; Chen X., Liu H., Shim A.H., Focia P.J., He X.; Nat. Struct. Mol. Biol. 15:50-56(2008). Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 39-635 IN COMPLEX WITH HUMANNRX1B, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-109 AND ASN-547.	18084303 [Abstract]