NRX1A_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: NRX1A_MOUSE
• UniProt AC: Q9CS84
• Protein Name: Neurexin-1
• Gene Name: Nrxn1
• Organism: Mus musculus (Mouse).
• Sequence Length: 1514
• Subcellular Localization: Cell membrane ; Single-pass type I membrane protein . Cell junction, synapse . Localized on the pre-synaptic membrane..
• Protein Description: Cell surface protein involved in cell-cell-interactions, exocytosis of secretory granules and regulation of signal transmission. Function is isoform-specific. Alpha-type isoforms have a long N-terminus with six laminin G-like domains and play an important role in synaptic signal transmission. Alpha-type isoforms play a role in the regulation of calcium channel activity and Ca(2+)-triggered neurotransmitter release at synapses and at neuromuscular junctions. They play an important role in Ca(2+)-triggered exocytosis of secretory granules in pituitary gland. They may effect their functions at synapses and in endocrine cells via their interactions with proteins from the exocytotic machinery. Likewise, alpha-type isoforms play a role in regulating the activity of postsynaptic NMDA receptors, a subtype of glutamate-gated ion channels. Both alpha-type and beta-type isoforms may play a role in the formation or maintenance of synaptic junctions via their interactions (via the extracellular domains) with neuroligin family members, CBLN1 or CBLN2. In vitro, triggers the de novo formation of presynaptic structures. May be involved in specification of excitatory synapses. Alpha-type isoforms were first identified as receptors for alpha-latrotoxin from spider venom..
• Protein Sequence: MGTALVQRGGCCLLCLSLLLLGCWAELGSGLEFPGAEGQWTRFPKWNACCESEMSFQLKTRSARGLVLYFDDEGFCDFLELILTRGGRLQLSFSIFCAEPATLLADTPVNDGAWHSVRIRRQFRNTTLYIDRAEAKWVEVKSKRRDMTVFSGLFVGGLPPELRAAALKLTLASVREREPFKGWIRDVRVNSSQALPVDGGEVKLDDEPPNSGGGSPCEAGEEGEGGVCLNGGVCSVVDDQAVCDCSRTGFRGKDCSQEDNNVEGLAHLMMGDQGKSKGKEEYIATFKGSEYFCYDLSQNPIQSSSDEITLSFKTLQRNGLMLHTGKSADYVNLALKNGAVSLVINLGSGAFEALVEPVNGKFNDNAWHDVKVTRNLRQHSGIGHAMVNKLHCSVTISVDGILTTTGYTQEDYTMLGSDDFFYVGGSPSTADLPGSPVSNNFMGCLKEVVYKNNDVRLELSRLAKQGDPKMKIHGVVAFKCENVATLDPITFETPESFISLPKWNAKKTGSISFDFRTTEPNGLILFSHGKPRHQKDAKHPQMIKVDFFAIEMLDGHLYLLLDMGSGTIKIKALQKKVNDGEWYHVDFQRDGRSGTISVNTLRTPYTAPGESEILDLDDELYLGGLPENKAGLVFPTEVWTALLNYGYVGCIRDLFIDGQSKDIRQMAEIQSTAGVKPSCSKETAKPCLSNPCKNNGMCRDGWNRYVCDCSGTGYLGRSCEREATVLSYDGSMFMKIQLPVVMHTEAEDVSLRFRSQRAYGILMATTSRDSADTLRLELDAGRVKLTVNLDCIRINCNSSKGPETLFAGYNLNDNEWHTVRVVRRGKSLKLTVDDQQAMTGQMAGDHTRLEFHNIETGIITERRYLSSVPSNFIGHLQSLTFNGMAYIDLCKNGDIDYCELNARFGFRNIIADPVTFKTKSSYVALATLQAYTSMHLFFQFKTTSLDGLILYNSGDGNDFIVVELVKGYLHYVFDLGNGANLIKGSSNKPLNDNQWHNVMISRDTSNLHTVKIDTKITTQITAGARNLDLKSDLYIGGVAKETYKSLPKLVHAKEGFQGCLASVDLNGRLPDLISDALFCNGQIERGCEGPSTTCQEDSCSNQGVCLQQWDGFSCDCSMTSFSGPLCNDPGTTYIFSKGGGQITYKWPPNDRPSTRADRLAIGFSTVQKEAVLVRVDSSSGLGDYLELHIHQGKIGVKFNVGTDDIAIEESNAIINDGKYHVVRFTRSGGNATLQVDSWPVIERYPAGNNDNERLAIARQRIPYRLGRVVDEWLLDKGRQLTIFNSQATIIIGGKEQGQPFQGQLSGLYYNGLKVLNMAAENDANIAIVGNVRLVGEVPSSMTTESTATAMQSEMSTSIMETTTTLATSTARRGKPPTKEPISQTTDDILVASAECPSDDEDIDPCEPSSGGLANPTRVGGREPYPGSAEVIRESSSTTGMVVGIVAAAALCILILLYAMYKYRNRDEGSYHVDESRNYISNSAQSNGAVVKEKQPSSAKSANKNKKNKDKEYYV

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
125	N-linked_Glycosylation	RIRRQFRNTTLYIDR EHHHHHCCEEEEEEH	38.41	-
127	Phosphorylation	RRQFRNTTLYIDRAE HHHHCCEEEEEEHHH	22.55	24719451
129	Phosphorylation	QFRNTTLYIDRAEAK HHCCEEEEEEHHHCE	9.93	24719451
190	N-linked_Glycosylation	WIRDVRVNSSQALPV CEEEEEECCCCCCCC	25.94	-
191	Phosphorylation	IRDVRVNSSQALPVD EEEEEECCCCCCCCC	22.44	21930439
544	Ubiquitination	AKHPQMIKVDFFAIE CCCCCCEEEEEEEEE	30.34	-
727	Phosphorylation	EREATVLSYDGSMFM CCEEEEEEECCCEEE	19.49	-
728	Phosphorylation	REATVLSYDGSMFMK CEEEEEEECCCEEEE	21.84	-
731	Phosphorylation	TVLSYDGSMFMKIQL EEEEECCCEEEEEEE	13.12	-
797	N-linked_Glycosylation	DCIRINCNSSKGPET EEEEEECCCCCCCCE	44.84	-
809	Phosphorylation	PETLFAGYNLNDNEW CCEEEEEEECCCCCC	17.04	-
1034	Phosphorylation	LDLKSDLYIGGVAKE CCCCCCEEECCHHHH	11.51	21454597
1119	Phosphorylation	FSCDCSMTSFSGPLC CCCEEEEECEECCCC	15.44	-
1131	Phosphorylation	PLCNDPGTTYIFSKG CCCCCCCCEEEEECC	23.09	-
1132	Phosphorylation	LCNDPGTTYIFSKGG CCCCCCCEEEEECCC	22.12	-
1133	Phosphorylation	CNDPGTTYIFSKGGG CCCCCCEEEEECCCC	10.37	-
1230	N-linked_Glycosylation	RFTRSGGNATLQVDS EEEECCCCEEEEEEC	33.02	-
1377	Phosphorylation	ARRGKPPTKEPISQT HCCCCCCCCCCCCCC	57.47	-
1469	Phosphorylation	YRNRDEGSYHVDESR HCCCCCCCCCCCCCC	15.26	25521595
1480	Phosphorylation	DESRNYISNSAQSNG CCCCCCCCCCHHHCC	17.86	29899451
1482	Phosphorylation	SRNYISNSAQSNGAV CCCCCCCCHHHCCCE	22.39	21183079
1485	Phosphorylation	YISNSAQSNGAVVKE CCCCCHHHCCCEEEC	36.63	21183079
1491	Ubiquitination	QSNGAVVKEKQPSSA HHCCCEEECCCCCCC	53.23	22790023
1493	Ubiquitination	NGAVVKEKQPSSAKS CCCEEECCCCCCCCC	62.89	-

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

Oops, there are no upstream regulatory protein records of NRX1A_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of NRX1A_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of NRX1A_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of NRX1A_MOUSE !!

Drug and Disease Associations

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