NLGNX_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: NLGNX_HUMAN
• UniProt AC: Q8N0W4
• Protein Name: Neuroligin-4, X-linked
• Gene Name: NLGN4X
• Organism: Homo sapiens (Human).
• Sequence Length: 816
• Subcellular Localization: Cell membrane; Single-pass type I membrane protein. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density.
• Protein Description: Putative neuronal cell surface protein involved in cell-cell-interactions..
• Protein Sequence: MSRPQGLLWLPLLFTPVCVMLNSNVLLWLTALAIKFTLIDSQAQYPVVNTNYGKIRGLRTPLPNEILGPVEQYLGVPYASPPTGERRFQPPEPPSSWTGIRNTTQFAAVCPQHLDERSLLHDMLPIWFTANLDTLMTYVQDQNEDCLYLNIYVPTEDDIHDQNSKKPVMVYIHGGSYMEGTGNMIDGSILASYGNVIVITINYRLGILGFLSTGDQAAKGNYGLLDQIQALRWIEENVGAFGGDPKRVTIFGSGAGASCVSLLTLSHYSEGLFQKAIIQSGTALSSWAVNYQPAKYTRILADKVGCNMLDTTDMVECLRNKNYKELIQQTITPATYHIAFGPVIDGDVIPDDPQILMEQGEFLNYDIMLGVNQGEGLKFVDGIVDNEDGVTPNDFDFSVSNFVDNLYGYPEGKDTLRETIKFMYTDWADKENPETRRKTLVALFTDHQWVAPAVATADLHAQYGSPTYFYAFYHHCQSEMKPSWADSAHGDEVPYVFGIPMIGPTELFSCNFSKNDVMLSAVVMTYWTNFAKTGDPNQPVPQDTKFIHTKPNRFEEVAWSKYNPKDQLYLHIGLKPRVRDHYRATKVAFWLELVPHLHNLNEIFQYVSTTTKVPPPDMTSFPYGTRRSPAKIWPTTKRPAITPANNPKHSKDPHKTGPEDTTVLIETKRDYSTELSVTIAVGASLLFLNILAFAALYYKKDKRRHETHRRPSPQRNTTNDIAHIQNEEIMSLQMKQLEHDHECESLQAHDTLRLTCPPDYTLTLRRSPDDIPLMTPNTITMIPNTLTGMQPLHTFNTFSGGQNSTNLPHGHSTTRV

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
78	Phosphorylation	EQYLGVPYASPPTGE HHHHCCCCCCCCCCC	19.80	18083107
102	N-linked_Glycosylation	SSWTGIRNTTQFAAV CCCCCCCCCHHHHHC	45.62	18093521
249	Phosphorylation	GGDPKRVTIFGSGAG CCCCCEEEEECCCCC	18.02	29116813
264	Phosphorylation	ASCVSLLTLSHYSEG HHHHHHHHHHHCCCC	31.35	29116813
311	Phosphorylation	VGCNMLDTTDMVECL CCCCCCCCCCHHHHH	22.27	29083192
312	Phosphorylation	GCNMLDTTDMVECLR CCCCCCCCCHHHHHH	23.05	29083192
407	Phosphorylation	SNFVDNLYGYPEGKD HHHHHHHHCCCCCHH	22.37	-
409	Phosphorylation	FVDNLYGYPEGKDTL HHHHHHCCCCCHHHH	5.64	-
511	N-linked_Glycosylation	PTELFSCNFSKNDVM CCCCEECCCCCCHHH	42.92	18093521
550	Ubiquitination	DTKFIHTKPNRFEEV CCCCCCCCCCCHHHC	26.57	-
620	Phosphorylation	VPPPDMTSFPYGTRR CCCCCCCCCCCCCCC	20.00	29507054
635	Phosphorylation	SPAKIWPTTKRPAIT CCCCCCCCCCCCCCC	29.92	29083192
636	Phosphorylation	PAKIWPTTKRPAITP CCCCCCCCCCCCCCC	22.45	29083192
671	Phosphorylation	LIETKRDYSTELSVT EEEECCCCCCCHHHH	22.86	25072903
672	Phosphorylation	IETKRDYSTELSVTI EEECCCCCCCHHHHH	21.50	25072903
673	Phosphorylation	ETKRDYSTELSVTIA EECCCCCCCHHHHHH	34.41	25072903
676	Phosphorylation	RDYSTELSVTIAVGA CCCCCCHHHHHHHHH	15.81	25072903
678	Phosphorylation	YSTELSVTIAVGASL CCCCHHHHHHHHHHH	10.39	25072903
684	Phosphorylation	VTIAVGASLLFLNIL HHHHHHHHHHHHHHH	21.48	25072903
697	Phosphorylation	ILAFAALYYKKDKRR HHHHHHHHHHHHHHC	14.44	25072903
698	Phosphorylation	LAFAALYYKKDKRRH HHHHHHHHHHHHHCC	16.65	25072903
707	Phosphorylation	KDKRRHETHRRPSPQ HHHHCCCCCCCCCCC	17.98	-
712	Phosphorylation	HETHRRPSPQRNTTN CCCCCCCCCCCCCCC	31.67	22912867
745	Phosphorylation	EHDHECESLQAHDTL CCCCHHCHHCCCCEE	37.12	28348404
760	Phosphorylation	RLTCPPDYTLTLRRS EEECCCCCEEEECCC	14.93	25884760

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
707	T	Phosphorylation	Kinase	PRKCA	P17252	GPS

Functions of PTM Sites

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

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DLG4_HUMAN	DLG4	physical	11368788

Drug and Disease Associations

• Kegg Disease
• H00480: Non-syndromic X-linked mental retardation
• OMIM Disease
• 300495: Autism, X-linked 2 (AUTSX2)
• 300497: Asperger syndrome, X-linked, 2 (ASPGX2)
• 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

N-linked Glycosylation

"Structural analysis of the synaptic protein neuroligin and its beta-neurexin complex: determinants for folding and cell adhesion.";
Fabrichny I.P., Leone P., Sulzenbacher G., Comoletti D., Miller M.T.,Taylor P., Bourne Y., Marchot P.;
Neuron 56:979-991(2007).
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 44-619 ALONE AND IN COMPLEXWITH RAT NRXN1, GLYCOSYLATION AT ASN-102 AND ASN-511, SUBUNIT, ANDDISULFIDE BONDS.
PubMed: 18093521