NRX3B_HUMAN - dbPTM
NRX3B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NRX3B_HUMAN
UniProt AC Q9HDB5
Protein Name Neurexin-3-beta
Gene Name NRXN3
Organism Homo sapiens (Human).
Sequence Length 637
Subcellular Localization Membrane
Single-pass type I membrane protein .
Protein Description Neuronal cell surface protein that may be involved in cell recognition and cell adhesion. May play a role in angiogenesis (By similarity)..
Protein Sequence MHLRIHARRSPPRRPAWTLGIWFLFWGCIVSSVWSSSNVASSSSTSSSPGSHSQHEHHFHGSKHHSVPISIYRSPVSLRGGHAGATYIFGKSGGLILYTWPANDRPSTRSDRLAVGFSTTVKDGILVRIDSAPGLGDFLQLHIEQGKIGVVFNIGTVDISIKEERTPVNDGKYHVVRFTRNGGNATLQVDNWPVNEHYPTGRQLTIFNTQAQIAIGGKDKGRLFQGQLSGLYYDGLKVLNMAAENNPNIKINGSVRLVGEVPSILGTTQTTSMPPEMSTTVMETTTTMATTTTRKNRSTASIQPTSDDLVSSAECSSDDEDFVECEPSTGGELVIPLLVEDPLATPPIATRAPSITLPPTFRPLLTIIETTKDSLSMTSEAGLPCLSDQGSDGCDDDGLVISGYGSGETFDSNLPPTDDEDFYTTFSLVTDKSLSTSIFEGGYKAHAPKWESKDFRPNKVSETSRTTTTSLSPELIRFTASSSSGMVPKLPAGKMNNRDLKPQPDIVLLPLPTAYELDSTKLKSPLITSPMFRNVPTANPTEPGIRRVPGASEVIRESSSTTGMVVGIVAAAALCILILLYAMYKYRNRDEGSYQVDETRNYISNSAQSNGTLMKEKQQSSKSGHKKQKNKDREYYV
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
10 (in isoform 4)Phosphorylation-33.4317081983
10 (in isoform 2)Phosphorylation-33.4317081983
10PhosphorylationLRIHARRSPPRRPAW
CEEECCCCCCCCHHH
33.4317081983
10 (in isoform 3)Phosphorylation-33.4317081983
74PhosphorylationVPISIYRSPVSLRGG
CEEEEEECCCEECCC
16.8119369195
74 (in isoform 4)Phosphorylation-16.8119369195
74 (in isoform 2)Phosphorylation-16.8119369195
74 (in isoform 3)Phosphorylation-16.8119369195
184N-linked_GlycosylationRFTRNGGNATLQVDN
EEEECCCCEEEEECC
31.02UniProtKB CARBOHYD
252N-linked_GlycosylationNNPNIKINGSVRLVG
CCCCCEECCEEEEEE
31.52UniProtKB CARBOHYD
296N-linked_GlycosylationATTTTRKNRSTASIQ
EEECCCCCCCCCEEC
39.58UniProtKB CARBOHYD
328 (in isoform 2)Phosphorylation-19.86-
329 (in isoform 2)Phosphorylation-60.98-
346PhosphorylationVEDPLATPPIATRAP
ECCCCCCCCCCCCCC
16.8224719451
352PhosphorylationTPPIATRAPSITLPP
CCCCCCCCCCCCCCC
9.6124719451
466O-linked_GlycosylationKVSETSRTTTTSLSP
CCCCCCCCCCCCCCH
28.41OGP
479O-linked_GlycosylationSPELIRFTASSSSGM
CHHHHEEEECCCCCC
18.77OGP
481O-linked_GlycosylationELIRFTASSSSGMVP
HHHEEEECCCCCCCC
27.91OGP

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 NRX3B_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NRX3B_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 NRX3B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NLGN1_HUMANNLGN1physical
8576240
NLGN2_HUMANNLGN2physical
8576240
NLGN3_HUMANNLGN3physical
8576240

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
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 NRX3B_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND MASSSPECTROMETRY.

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