NRX4_DROME - dbPTM
NRX4_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NRX4_DROME
UniProt AC Q94887
Protein Name Neurexin-4
Gene Name Nrx-IV
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 1284
Subcellular Localization Membrane
Single-pass type I membrane protein . Cell junction, septate junction.
Protein Description Seems to play a role in the formation and function of septate junctions. Septate junctions, which are the equivalent of vertebrates tight junctions, are characterized by regular arrays of transverse structures that span the intermembrane space and form a physical barrier to diffusion. Required for the blood-brain barrier formation..
Protein Sequence MRPPRSNTKAAFSSLQFGLLCLLLLVNNGIKSVQADAFTDYFSDYDCNQPLMERAVLTATSSLTERGPDKARLNGNAAWTPVENTYNHFLTLDLGDPRMVRKIATMGRMHTDEFVTEYIVQYSDDGEFWRSYVNPTSEPQMFKGNSDGNSIHYNVFEVPIIAQWVRINPTRWHDRISMRVELYGCDYISENLYFNGTGLVRYDLRREPITSTKESIRFRFKTAFANGVMMYSRGTQGDYYALQLKDNKMVLNLDLGSRVMTSLSVGSLLDDNVWHDVVISRNQRDIIFSVDRVIVRGRIQGEFTRLNLNRELYLGGVPNVQEGLIVQQNFSGCLENIYFNSTNFIRVMKDSTELGEGYLFTRVNTIYACPSPPIYPVTFTTRSSFVRLKGYENSQRLNVSFYFRTYEETGVMLHHDFYSGGYLKVFLEFGKVKIDLKVKDKARIILDNYDDQFNDGKWHSFVISIEKNRLILNIDQRPMTTTKSMQVATGAQYYIAGGKDKNGFVGCMRLISVDGNYKLPQDWVKGEEVCCGDDVVVDACQMIDRCNPNPCQHKGLCHQNSREFFCDCGHTGYAGAVCHTSNNPLSCLALKNVQHVQQRVNLNLDVDGSGPLEPFPVTCEFYSDGRVITTLSHSQEHTTTVDGFQEPGSFEQSIMYDANQLQIEALLNRSHSCWQRLSYSCRSSRLFNSPSEAGNFRPFSWWISRHNQPMDYWAGALPGSRKCECGILGKCHDPTKWCNCDSNSLEWMEDGGDIREKEYLPVRAVKFGDTGTPLDEKMGRYTLGPLRCEGDDLFSNVVTFRIADASINLPPFDMGHSGDIYLEFRTTQENSVIFHATGPTDYIKLSLNGGNKLQFQYQAGSGPLGVNVGTSYHLNDNNWHTVSVERNRKEARLVVDGSIKAEVREPPGPVRALHLTSDLVIGATTEYRDGYVGCIRALLLNGKMVDLKEYSKRGLYGISTGCVGRCESNPCLNNGTCIERYDGYSCDCRWSAFKGPICADEIGVNLRSSSIIRYEFEGSFRSTIAENIRVGFTTTIPKGFLLGFSSNLTGEYLTIQISNSGHLRCVFDFGFERQEIIFPKKHFGLGQYHDMHFMRKNGGSTVVLKVDNYEPVEYNFDIKASADAQFNNIQYMYIGKNESMTDGFVGCVSRVQFDDIYPLKLMFQQNPPKNVKSLGTQLTEDFCGVEPVTHPPIEIETRPPPLVDEEKLRKAYNEVDSVLLACLLVILFLLLILMFFLIGRYLHRHKGDYLTHEDQGADGADDPDDAVLHSTTGHQVRKRTEIFI
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
195N-linked_GlycosylationISENLYFNGTGLVRY
EECCEEECCCCEEEE
33.29-
329N-linked_GlycosylationEGLIVQQNFSGCLEN
CCEEEEECCCCCEEE
18.89-
340N-linked_GlycosylationCLENIYFNSTNFIRV
CEEEEEECCCCCEEE
30.84-
398N-linked_GlycosylationYENSQRLNVSFYFRT
CCCCCCEEEEEEEEE
29.58-
668N-linked_GlycosylationLQIEALLNRSHSCWQ
HHHHHHHCCCCHHHH
44.23-
974N-linked_GlycosylationESNPCLNNGTCIERY
CCCCCCCCCCEEEEE
33.91-
1047N-linked_GlycosylationFLLGFSSNLTGEYLT
EEEEECCCCCCCEEE
40.19-
1137N-linked_GlycosylationQYMYIGKNESMTDGF
EEEEEECCCCCCCCC
41.1717893096

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 NRX4_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NRX4_DROME !!

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 NRX4_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PATJ_DROMEPatjphysical
15710747
NRG_DROMENrgphysical
16554482
CONT_DROMEContphysical
15459097
CONT_DROMEContphysical
16554482
CONT_DROMEContphysical
20935638
PATJ_DROMEPatjphysical
10102271

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NRX4_DROME

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Identification of N-glycosylated proteins from the central nervoussystem of Drosophila melanogaster.";
Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L.,Panin V.;
Glycobiology 17:1388-1403(2007).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1137, AND MASSSPECTROMETRY.

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