| UniProt ID | NLGN2_MOUSE | |
|---|---|---|
| UniProt AC | Q69ZK9 | |
| Protein Name | Neuroligin-2 | |
| Gene Name | Nlgn2 | |
| Organism | Mus musculus (Mouse). | |
| 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 postsynaptic membranes in brain. Detected at dendritic spines in cultured neurons. |
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| 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. Mediates cell-cell interactions between Langerhans beta cells and modulates insulin secretion (By similarity). 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.. | |
| Protein Sequence | MWLLALCLVGLAGAQRGGGGPGGGAPGGPGLGLGSLGEERFPVVNTAYGRVRGVRRELNNEILGPVVQFLGVPYATPPLGARRFQPPEAPASWPGVRNATTLPPACPQNLHGALPAIMLPVWFTDNLEAAATYVQNQSEDCLYLNLYVPTEDGPLTKKRDEATLNPPDTDIRDSGKKPVMLFLHGGSYMEGTGNMFDGSVLAAYGNVIVVTLNYRLGVLGFLSTGDQAAKGNYGLLDQIQALRWLSENIAHFGGDPERITIFGSGAGASCVNLLILSHHSEGLFQKAIAQSGTAISSWSVNYQPLKYTRLLAAKVGCDREDSTEAVECLRRKSSRELVDQDVQPARYHIAFGPVVDGDVVPDDPEILMQQGEFLNYDMLIGVNQGEGLKFVEDSAESEDGVSASAFDFTVSNFVDNLYGYPEGKDVLRETIKFMYTDWADRDNGEMRRKTLLALFTDHQWVAPAVATAKLHADYQSPVYFYTFYHHCQAEGRPEWADAAHGDELPYVFGVPMVGATDLFPCNFSKNDVMLSAVVMTYWTNFAKTGDPNQPVPQDTKFIHTKPNRFEEVVWSKFNSKEKQYLHIGLKPRVRDNYRANKVAFWLELVPHLHNLHTELFTTTTRLPPYATRWPPRTPGPGTSGTRRPPPPATLPPESDIDLGPRAYDRFPGDSRDYSTELSVTVAVGASLLFLNILAFAALYYKRDRRQELRCRRLSPPGGSGSGVPGGGPLLPTAGRELPPEEELVSLQLKRGGGVGADPAEALRPACPPDYTLALRRAPDDVPLLAPGALTLLPSGLGPPPPPPPPSLHPFGPFPPPPPTATSHNNTLPHPHSTTRV | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 98 | N-linked_Glycosylation | ASWPGVRNATTLPPA CCCCCCCCCCCCCCC | 38.95 | 18250328 | |
| 136 | N-linked_Glycosylation | AAATYVQNQSEDCLY HHHHHHHCCCCCCEE | 36.98 | - | |
| 163 | Phosphorylation | TKKRDEATLNPPDTD CCCCCCCCCCCCCCC | 25.64 | 19367708 | |
| 522 | N-linked_Glycosylation | ATDLFPCNFSKNDVM CCCCCCCCCCCCHHH | 44.45 | - | |
| 714 | Phosphorylation | ELRCRRLSPPGGSGS HHEEEECCCCCCCCC | 27.51 | 25521595 | |
| 719 | Phosphorylation | RLSPPGGSGSGVPGG ECCCCCCCCCCCCCC | 35.38 | 25521595 | |
| 721 | Phosphorylation | SPPGGSGSGVPGGGP CCCCCCCCCCCCCCC | 38.01 | 22324799 | |
| 749 | Ubiquitination | ELVSLQLKRGGGVGA HHEEEEECCCCCCCC | 35.72 | 22790023 | |
| 750 | Methylation | LVSLQLKRGGGVGAD HEEEEECCCCCCCCC | 58.54 | 58858691 | |
| 770 | Phosphorylation | RPACPPDYTLALRRA CCCCCCCCEEEECCC | 14.93 | 29514104 |
| 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 NLGN2_MOUSE !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of NLGN2_MOUSE !! | ||||||
* 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 NLGN2_MOUSE !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of NLGN2_MOUSE !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| N-linked Glycosylation | |
| Reference | PubMed |
| "Crystal structure of the extracellular cholinesterase-like domainfrom neuroligin-2."; Koehnke J., Jin X., Budreck E.C., Posy S., Scheiffele P., Honig B.,Shapiro L.; Proc. Natl. Acad. Sci. U.S.A. 105:1873-1878(2008). Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 42-612, DISULFIDE BONDS, ANDGLYCOSYLATION AT ASN-98. | |
| Phosphorylation | |
| Reference | PubMed |
| "Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations."; Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.; Mol. Cell. Proteomics 6:283-293(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-714, AND MASSSPECTROMETRY. | |
