NLGN2_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: NLGN2_RAT
• UniProt AC: Q62888
• Protein Name: Neuroligin-2
• Gene Name: Nlgn2
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 836
• Subcellular Localization: Cell membrane; Single-pass type I membrane protein. Cell junction, synapse, postsynaptic cell membrane. Cell junction, synapse, presynaptic cell membrane. Detected at presynaptic membranes in retina, and at postsynaptic membranes in brain. Detected a
• Protein Description: Transmembrane scaffolding protein involved in cell-cell interactions via its interactions with neurexin family members. Mediates cell-cell interactions both in neurons and in other types of cells, such as Langerhans beta cells. Plays a role in synapse function and synaptic signal transmission, especially via gamma-aminobutyric acid receptors (GABA(A) receptors). Functions by recruiting and clustering synaptic proteins. Promotes clustering of postsynaptic GABRG2 and GPHN. Modulates signaling by inhibitory synapses, and thereby plays a role in controlling the ratio of signaling by excitatory and inhibitory synapses and information processing. Required for normal signal amplitude from inhibitory synapses, but is not essential for normal signal frequency. May promote the initial formation of synapses, but is not essential for this. In vitro, triggers the de novo formation of presynaptic structures. Mediates cell-cell interactions between Langerhans beta cells and modulates insulin secretion..
• Protein Sequence: MWLLALCLVGLAGAQRGGGGPGGGAPGGPGLGLGSLGEERFPVVNTAYGRVRGVRRELNNEILGPVVQFLGVPYATPPLGARRFQPPEAPASWPGVRNATTLPPACPQNLHGALPAIMLPVWFTDNLEAAATYVQNQSEDCLYLNLYVPTEDGPLTKKRDEATLNPPDTDIRDSGKKPVMLFLHGGSYMEGTGNMFDGSVLAAYGNVIVATLNYRLGVLGFLSTGDQAAKGNYGLLDQIQALRWLSENIAHFGGDPERITIFGSGAGASCVNLLILSHHSEGLFQKAIAQSGTAISSWSVNYQPLKYTRLLAAKVGCDREDSTEAVECLRRKSSRELVDQDVQPARYHIAFGPVVDGDVVPDDPEILMQQGEFLNYDMLIGVNQGEGLKFVEDSAESEDGVSASAFDFTVSNFVDNLYGYPEGKDVLRETIKFMYTDWADRDNGEMRRKTLLALFTDHQWVAPAVATAKLHADYQSPVYFYTFYHHCQAEGRPEWADAAHGDELPYVFGVPMVGATDLFPCNFSKNDVMLSAVVMTYWTNFAKTGDPNQPVPQDTKFIHTKPNRFEEVVWSKFNSKEKQYLHIGLKPRVRDNYRANKVAFWLELVPHLHNLHTELFTTTTRLPPYATRWPPRTPGPGTSGTRRPPPPATLPPESDIDLGPRAYDRFPGDSRDYSTELSVTVAVGASLLFLNILAFAALYYKRDRRQELRCRRLSPPGGSGSGVPGGGPLLPTAGRELPPEEELVSLQLKRGGGVGADPAEALRPACPPDYTLALRRAPDDVPLLAPGALTLLPSGLGPPPPPPPPSLHPFGPFPPPPPTATSHNNTLPHPHSTTRV

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
98	N-linked_Glycosylation	ASWPGVRNATTLPPA CCCCCCCCCCCCCCC	38.95	-
136	N-linked_Glycosylation	AAATYVQNQSEDCLY HHHHHHHCCCCCCEE	36.98	-
522	N-linked_Glycosylation	ATDLFPCNFSKNDVM CCCCCCCCCCCCHHH	44.45	-
714	Phosphorylation	ELRCRRLSPPGGSGS HHEEEECCCCCCCCC	27.51	27097102
719	Phosphorylation	RLSPPGGSGSGVPGG ECCCCCCCCCCCCCC	35.38	27097102
721	Phosphorylation	SPPGGSGSGVPGGGP CCCCCCCCCCCCCCC	38.01	27097102
749	Ubiquitination	ELVSLQLKRGGGVGA HHEEEEECCCCCCCC	35.72	-
770	Phosphorylation	RPACPPDYTLALRRA CCCCCCCCEEEECCC	14.93	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of NLGN2_RAT !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of NLGN2_RAT !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of NLGN2_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DLG4_RAT	Dlg4	physical	15458844
DLG3_RAT	Dlg3	physical	15458844
DLG2_RAT	Dlg2	physical	15458844
MAGI1_RAT	Magi1	physical	15458844
MAGI2_RAT	Magi2	physical	15458844
MAGI3_RAT	Magi3	physical	15458844
SHAN1_RAT	Shank1	physical	15458844
SHAN3_RAT	Shank3	physical	15458844
PICK1_RAT	Pick1	physical	15458844
SI1L1_RAT	Sipa1l1	physical	15458844

Drug and Disease Associations

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