MAG_RAT - dbPTM
MAG_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MAG_RAT
UniProt AC P07722
Protein Name Myelin-associated glycoprotein
Gene Name Mag
Organism Rattus norvegicus (Rat).
Sequence Length 626
Subcellular Localization Cell membrane
Single-pass type I membrane protein . Membrane raft .
Protein Description Adhesion molecule that mediates interactions between myelinating cells and neurons by binding to neuronal sialic acid-containing gangliosides and to the glycoproteins RTN4R and RTN4RL2. [PubMed: 8995428]
Protein Sequence MIFLTTLPLFWIMISASRGGHWGAWMPSSISAFEGTCVSIPCRFDFPDELRPAVVHGVWYFNSPYPKNYPPVVFKSRTQVVHESFQGRSRLLGDLGLRNCTLLLSTLSPELGGKYYFRGDLGGYNQYTFSEHSVLDIINTPNIVVPPEVVAGTEVEVSCMVPDNCPELRPELSWLGHEGLGEPTVLGRLREDEGTWVQVSLLHFVPTREANGHRLGCQAAFPNTTLQFEGYASLDVKYPPVIVEMNSSVEAIEGSHVSLLCGADSNPPPLLTWMRDGMVLREAVAESLYLDLEEVTPAEDGIYACLAENAYGQDNRTVELSVMYAPWKPTVNGTVVAVEGETVSILCSTQSNPDPILTIFKEKQILATVIYESQLQLELPAVTPEDDGEYWCVAENQYGQRATAFNLSVEFAPIILLESHCAAARDTVQCLCVVKSNPEPSVAFELPSRNVTVNETEREFVYSERSGLLLTSILTLRGQAQAPPRVICTSRNLYGTQSLELPFQGAHRLMWAKIGPVGAVVAFAILIAIVCYITQTRRKKNVTESPSFSAGDNPHVLYSPEFRISGAPDKYESEKRLGSERRLLGLRGEPPELDLSYSHSDLGKRPTKDSYTLTEELAEYAEIRVK
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
75AcetylationNYPPVVFKSRTQVVH
CCCCEEEECCCCEEE
27.6722902405
99N-linked_GlycosylationLGDLGLRNCTLLLST
HHHHHHHCCEEEEEC
28.33-
223N-linked_GlycosylationGCQAAFPNTTLQFEG
ECEEECCCCEEEEEE
38.96-
246N-linked_GlycosylationPPVIVEMNSSVEAIE
CCEEEEECCCEEEEC
20.02-
315N-linked_GlycosylationENAYGQDNRTVELSV
ECCCCCCCCEEEEEE
33.37-
332N-linked_GlycosylationAPWKPTVNGTVVAVE
CCCCCEECCEEEEEC
42.78-
406N-linked_GlycosylationGQRATAFNLSVEFAP
CCEEEEEEEEEECHH
29.01-
450N-linked_GlycosylationAFELPSRNVTVNETE
EEECCCCCEECCHHH
37.84-
454N-linked_GlycosylationPSRNVTVNETEREFV
CCCCEECCHHHHHHE
40.90-
531S-palmitoylationAILIAIVCYITQTRR
HHHHHHHHHHHHHCC
1.341703542
540 (in isoform 2)Ubiquitination-55.64-
543PhosphorylationTRRKKNVTESPSFSA
HCCCCCCCCCCCCCC
39.8930411139
545PhosphorylationRKKNVTESPSFSAGD
CCCCCCCCCCCCCCC
19.2427097102
547PhosphorylationKNVTESPSFSAGDNP
CCCCCCCCCCCCCCC
40.9027097102
549PhosphorylationVTESPSFSAGDNPHV
CCCCCCCCCCCCCCE
35.362438699
558PhosphorylationGDNPHVLYSPEFRIS
CCCCCEEECCCEEEC
22.5327097102
565 (in isoform 2)Phosphorylation-25.3325403869
565PhosphorylationYSPEFRISGAPDKYE
ECCCEEECCCCCHHH
25.3325403869
570UbiquitinationRISGAPDKYESEKRL
EECCCCCHHHHHHHH
50.27-
570 (in isoform 2)Ubiquitination-50.27-
570 (in isoform 2)Acetylation-50.27-
570AcetylationRISGAPDKYESEKRL
EECCCCCHHHHHHHH
50.2722902405
575UbiquitinationPDKYESEKRLGSERR
CCHHHHHHHHCCCHH
63.30-
620PhosphorylationLTEELAEYAEIRVK-
CHHHHHHHHHHEEC-
12.1522817900

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 MAG_RAT !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

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 MAG_RAT !!

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

Oops, there are no PPI records of MAG_RAT !!

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

loading...

Related Literatures of Post-Translational Modification
Palmitoylation
ReferencePubMed
"The myelin-associated glycoproteins: membrane disposition, evidenceof a novel disulfide linkage between immunoglobulin-like domains, andposttranslational palmitylation.";
Pedraza L., Owens G.C., Green L.A.D., Salzer J.L.;
J. Cell Biol. 111:2651-2661(1990).
Cited for: DISULFIDE BONDS, PALMITOYLATION AT CYS-531, AND PARTIAL PROTEINSEQUENCE.

TOP