NRX1A_HUMAN - dbPTM
NRX1A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NRX1A_HUMAN
UniProt AC Q9ULB1
Protein Name Neurexin-1
Gene Name NRXN1
Organism Homo sapiens (Human).
Sequence Length 1477
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 calcium-dependent 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 (By similarity)..
Protein Sequence MGTALLQRGGCFLLCLSLLLLGCWAELGSGLEFPGAEGQWTRFPKWNACCESEMSFQLKTRSARGLVLYFDDEGFCDFLELILTRGGRLQLSFSIFCAEPATLLADTPVNDGAWHSVRIRRQFRNTTLFIDQVEAKWVEVKSKRRDMTVFSGLFVGGLPPELRAAALKLTLASVREREPFKGWIRDVRVNSSQVLPVDSGEVKLDDEPPNSGGGSPCEAGEEGEGGVCLNGGVCSVVDDQAVCDCSRTGFRGKDCSQEDNNVEGLAHLMMGDQGKSKGKEEYIATFKGSEYFCYDLSQNPIQSSSDEITLSFKTLQRNGLMLHTGKSADYVNLALKNGAVSLVINLGSGAFEALVEPVNGKFNDNAWHDVKVTRNLRQHSGIGHAMVTISVDGILTTTGYTQEDYTMLGSDDFFYVGGSPSTADLPGSPVSNNFMGCLKEVVYKNNDVRLELSRLAKQGDPKMKIHGVVAFKCENVATLDPITFETPESFISLPKWNAKKTGSISFDFRTTEPNGLILFSHGKPRHQKDAKHPQMIKVDFFAIEMLDGHLYLLLDMGSGTIKIKALLKKVNDGEWYHVDFQRDGRSGTISVNTLRTPYTAPGESEILDLDDELYLGGLPENKAGLVFPTEVWTALLNYGYVGCIRDLFIDGQSKDIRQMAEVQSTAGVKPSCSKETAKPCLSNPCKNNGMCRDGWNRYVCDCSGTGYLGRSCEREATVLSYDGSMFMKIQLPVVMHTEAEDVSLRFRSQRAYGILMATTSRDSADTLRLELDAGRVKLTVNLDCIRINCNSSKGPETLFAGYNLNDNEWHTVRVVRRGKSLKLTVDDQQAMTGQMAGDHTRLEFHNIETGIITERRYLSSVPSNFIGHLQSLTFNGMAYIDLCKNGDIDYCELNARFGFRNIIADPVTFKTKSSYVALATLQAYTSMHLFFQFKTTSLDGLILYNSGDGNDFIVVELVKGYLHYVFDLGNGANLIKGSSNKPLNDNQWHNVMISRDTSNLHTVKIDTKITTQITAGARNLDLKSDLYIGGVAKETYKSLPKLVHAKEGFQGCLASVDLNGRLPDLISDALFCNGQIERGCEGPSTTCQEDSCSNQGVCLQQWDGFSCDCSMTSFSGPLCNDPGTTYIFSKGGGQITYKWPPNDRPSTRADRLAIGFSTVQKEAVLVRVDSSSGLGDYLELHIHQGKIGVKFNVGTDDIAIEESNAIINDGKYHVVRFTRSGGNATLQVDSWPVIERYPAGRQLTIFNSQATIIIGGKEQGQPFQGQLSGLYYNGLKVLNMAAENDANIAIVGNVRLVGEVPSSMTTESTATAMQSEMSTSIMETTTTLATSTARRGKPPTKEPISQTTDDILVASAECPSDDEDIDPCEPSSGGLANPTRAGGREPYPGSAEVIRESSSTTGMVVGIVAAAALCILILLYAMYKYRNRDEGSYHVDESRNYISNSAQSNGAVVKEKQPSSAKSSNKNKKNKDKEYYV
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 Orthologous
Protein Cluster
125N-linked_GlycosylationRIRRQFRNTTLFIDQ
EHHHHHCCEEEEEEE		38.41UniProtKB CARBOHYD
190N-linked_GlycosylationWIRDVRVNSSQVLPV
CEEEEEECCCCEEEC		25.94UniProtKB CARBOHYD
279 (in isoform 3)Phosphorylation-51.6225954137
284 (in isoform 3)Phosphorylation-13.1925954137
311PhosphorylationSSDEITLSFKTLQRN
CCCEEEEEEEEEECC		18.9524719451
324PhosphorylationRNGLMLHTGKSADYV
CCCEEEECCCCCHHH		42.2020860994
341PhosphorylationALKNGAVSLVINLGS
EECCCCEEEEEECCC		19.1819413330
380PhosphorylationTRNLRQHSGIGHAMV
CCCCHHHCCCCCEEE		24.6222817900
410PhosphorylationEDYTMLGSDDFFYVG
HHEEEECCCCCEEEC		30.0027542207
413 (in isoform 3)Phosphorylation-5.9720860994
415PhosphorylationLGSDDFFYVGGSPST
ECCCCCEEECCCCCC		9.7427542207
419PhosphorylationDFFYVGGSPSTADLP
CCEEECCCCCCCCCC		15.1127542207
421PhosphorylationFYVGGSPSTADLPGS
EEECCCCCCCCCCCC		37.6127542207
422PhosphorylationYVGGSPSTADLPGSP
EECCCCCCCCCCCCC		27.8127542207
428PhosphorylationSTADLPGSPVSNNFM
CCCCCCCCCCCCCHH		21.8627542207
431PhosphorylationDLPGSPVSNNFMGCL
CCCCCCCCCCHHHHH		29.4627542207
492PhosphorylationETPESFISLPKWNAK
CCCHHHCCCCCCCCC		36.2924719451
664PhosphorylationRQMAEVQSTAGVKPS
HHHHHHHCCCCCCCC		25.9630206219
665PhosphorylationQMAEVQSTAGVKPSC
HHHHHHCCCCCCCCC		15.4428450419
671PhosphorylationSTAGVKPSCSKETAK
CCCCCCCCCCCCCCC		25.8828450419
673PhosphorylationAGVKPSCSKETAKPC
CCCCCCCCCCCCCCC		37.5517929957
676PhosphorylationKPSCSKETAKPCLSN
CCCCCCCCCCCCCCC		43.6617929957
747MethylationEDVSLRFRSQRAYGI
HHEEHHHHHHHHEEE		25.9924377075
747DimethylationEDVSLRFRSQRAYGI
HHEEHHHHHHHHEEE		25.99-
758PhosphorylationAYGILMATTSRDSAD
HEEEEEEEECCCCCC		16.02-
760PhosphorylationGILMATTSRDSADTL
EEEEEEECCCCCCEE		29.72-
790N-linked_GlycosylationDCIRINCNSSKGPET
EEEEEECCCCCCCCE		44.84UniProtKB CARBOHYD
820PhosphorylationRVVRRGKSLKLTVDD
EEEECCCEEEEEECH		33.29-
824PhosphorylationRGKSLKLTVDDQQAM
CCCEEEEEECHHHHH		21.94-
1024PhosphorylationARNLDLKSDLYIGGV
CCCCCCCCCEEECCH		39.9029396449
1024O-linked_GlycosylationARNLDLKSDLYIGGV
CCCCCCCCCEEECCH		39.9030379171
1027PhosphorylationLDLKSDLYIGGVAKE
CCCCCCEEECCHHHH		11.5129396449
1036PhosphorylationGGVAKETYKSLPKLV
CCHHHHHHHHHCCHH		10.3218083107
1129PhosphorylationPGTTYIFSKGGGQIT
CCCEEEEECCCCEEE		22.3424719451
1136PhosphorylationSKGGGQITYKWPPND
ECCCCEEEEECCCCC		15.91-
1146PhosphorylationWPPNDRPSTRADRLA
CCCCCCCCCHHHHEE		31.2720860994
1223N-linked_GlycosylationRFTRSGGNATLQVDS
EEEECCCCEEEEEEC		33.02UniProtKB CARBOHYD
1340PhosphorylationARRGKPPTKEPISQT
HCCCCCCCCCCCCCC		57.47-
1441PhosphorylationHVDESRNYISNSAQS
CCCCCCCCCCCCHHH		12.4825884760
1459PhosphorylationVVKEKQPSSAKSSNK
CCCCCCCCCCCCCCC		40.20-
1460PhosphorylationVKEKQPSSAKSSNKN
CCCCCCCCCCCCCCC		46.53-
1463PhosphorylationKQPSSAKSSNKNKKN
CCCCCCCCCCCCCCC		38.57-
1475PhosphorylationKKNKDKEYYV-----
CCCCCCCCCC-----		18.44-
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

Oops, there are no upstream regulatory protein records of NRX1A_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NRX1A_HUMAN !!
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 NRX1A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NLGN1_HUMANNLGN1physical
14522992
NLGN1_HUMANNLGN1physical
8576240
NLGN2_HUMANNLGN2physical
8576240
NLGN3_HUMANNLGN3physical
8576240
PDZD2_HUMANPDZD2physical
12421765
SI1L1_HUMANSIPA1L1physical
12421765
MYO16_HUMANMYO16physical
12421765
MACF1_HUMANMACF1physical
12421765
RHG26_HUMANARHGAP26physical
27173435
ELOA1_HUMANTCEB3physical
27173435
RHG10_HUMANARHGAP10physical
27173435
TULP1_HUMANTULP1physical
27173435
Drug and Disease Associations
Kegg Disease
H00756 Pitt-Hopkins syndrome, including: Pitt-Hopkins syndrome; Pitt-Hopkins-like syndrome
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NRX1A_HUMAN

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Related Literatures of Post-Translational Modification

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