NET1_HUMAN - dbPTM
NET1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NET1_HUMAN
UniProt AC O95631
Protein Name Netrin-1
Gene Name NTN1
Organism Homo sapiens (Human).
Sequence Length 604
Subcellular Localization Secreted, extracellular space, extracellular matrix.
Protein Description Netrins control guidance of CNS commissural axons and peripheral motor axons. Its association with either DCC or some UNC5 receptors will lead to axon attraction or repulsion, respectively. It also serve as a survival factor via its association with its receptors which prevent the initiation of apoptosis. Involved in tumorigenesis by regulating apoptosis..
Protein Sequence MMRAVWEALAALAAVACLVGAVRGGPGLSMFAGQAAQPDPCSDENGHPRRCIPDFVNAAFGKDVRVSSTCGRPPARYCVVSERGEERLRSCHLCNASDPKKAHPPAFLTDLNNPHNLTCWQSENYLQFPHNVTLTLSLGKKFEVTYVSLQFCSPRPESMAIYKSMDYGRTWVPFQFYSTQCRKMYNRPHRAPITKQNEQEAVCTDSHTDMRPLSGGLIAFSTLDGRPSAHDFDNSPVLQDWVTATDIRVAFSRLHTFGDENEDDSELARDSYFYAVSDLQVGGRCKCNGHAARCVRDRDDSLVCDCRHNTAGPECDRCKPFHYDRPWQRATAREANECVACNCNLHARRCRFNMELYKLSGRKSGGVCLNCRHNTAGRHCHYCKEGYYRDMGKPITHRKACKACDCHPVGAAGKTCNQTTGQCPCKDGVTGITCNRCAKGYQQSRSPIAPCIKIPVAPPTTAASSVEEPEDCDSYCKASKGKLKINMKKYCKKDYAVQIHILKADKAGDWWKFTVNIISVYKQGTSRIRRGDQSLWIRSRDIACKCPKIKPLKKYLLLGNAEDSPDQSGIVADKSSLVIQWRDTWARRLRKFQQREKKGKCKKA
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
95N-linked_GlycosylationLRSCHLCNASDPKKA
HHHCCCCCCCCCCCC
49.17UniProtKB CARBOHYD
116N-linked_GlycosylationTDLNNPHNLTCWQSE
CCCCCCCCCCCEECC
38.00UniProtKB CARBOHYD
131N-linked_GlycosylationNYLQFPHNVTLTLSL
CCCCCCCEEEEEEEC
28.80UniProtKB CARBOHYD
158PhosphorylationFCSPRPESMAIYKSM
ECCCCHHHEEEEECC
19.0528270605
162PhosphorylationRPESMAIYKSMDYGR
CHHHEEEEECCCCCC
6.3528270605
164PhosphorylationESMAIYKSMDYGRTW
HHEEEEECCCCCCCC
10.4228270605
167PhosphorylationAIYKSMDYGRTWVPF
EEEECCCCCCCCCCE
10.4028270605
271PhosphorylationDSELARDSYFYAVSD
CCHHHHHCEEEEEEC
16.1622468782
272PhosphorylationSELARDSYFYAVSDL
CHHHHHCEEEEEECC
12.6122468782
274PhosphorylationLARDSYFYAVSDLQV
HHHHCEEEEEECCEE
9.6222468782
357PhosphorylationCRFNMELYKLSGRKS
CCCCEEEHHCCCCCC
9.1426657352
387PhosphorylationCHYCKEGYYRDMGKP
CCCCCCCCCCCCCCC
9.09-
388PhosphorylationHYCKEGYYRDMGKPI
CCCCCCCCCCCCCCC
15.82-
417N-linked_GlycosylationGAAGKTCNQTTGQCP
CCCCCCCCCCCCCCC
47.68UniProtKB CARBOHYD
460O-linked_GlycosylationKIPVAPPTTAASSVE
ECCCCCCCCCCCCCC
28.1855832477
461O-linked_GlycosylationIPVAPPTTAASSVEE
CCCCCCCCCCCCCCC
26.4655832483
490PhosphorylationLKINMKKYCKKDYAV
CEECHHHHCCCCEEE
12.1822817900

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 NET1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NET1_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 NET1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DCC_HUMANDCCphysical
9950216

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 NET1_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP