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 | ||
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* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
75 | Acetylation | NYPPVVFKSRTQVVH CCCCEEEECCCCEEE | 27.67 | 22902405 | |
99 | N-linked_Glycosylation | LGDLGLRNCTLLLST HHHHHHHCCEEEEEC | 28.33 | - | |
223 | N-linked_Glycosylation | GCQAAFPNTTLQFEG ECEEECCCCEEEEEE | 38.96 | - | |
246 | N-linked_Glycosylation | PPVIVEMNSSVEAIE CCEEEEECCCEEEEC | 20.02 | - | |
315 | N-linked_Glycosylation | ENAYGQDNRTVELSV ECCCCCCCCEEEEEE | 33.37 | - | |
332 | N-linked_Glycosylation | APWKPTVNGTVVAVE CCCCCEECCEEEEEC | 42.78 | - | |
406 | N-linked_Glycosylation | GQRATAFNLSVEFAP CCEEEEEEEEEECHH | 29.01 | - | |
450 | N-linked_Glycosylation | AFELPSRNVTVNETE EEECCCCCEECCHHH | 37.84 | - | |
454 | N-linked_Glycosylation | PSRNVTVNETEREFV CCCCEECCHHHHHHE | 40.90 | - | |
531 | S-palmitoylation | AILIAIVCYITQTRR HHHHHHHHHHHHHCC | 1.34 | 1703542 | |
540 (in isoform 2) | Ubiquitination | - | 55.64 | - | |
543 | Phosphorylation | TRRKKNVTESPSFSA HCCCCCCCCCCCCCC | 39.89 | 30411139 | |
545 | Phosphorylation | RKKNVTESPSFSAGD CCCCCCCCCCCCCCC | 19.24 | 27097102 | |
547 | Phosphorylation | KNVTESPSFSAGDNP CCCCCCCCCCCCCCC | 40.90 | 27097102 | |
549 | Phosphorylation | VTESPSFSAGDNPHV CCCCCCCCCCCCCCE | 35.36 | 2438699 | |
558 | Phosphorylation | GDNPHVLYSPEFRIS CCCCCEEECCCEEEC | 22.53 | 27097102 | |
565 (in isoform 2) | Phosphorylation | - | 25.33 | 25403869 | |
565 | Phosphorylation | YSPEFRISGAPDKYE ECCCEEECCCCCHHH | 25.33 | 25403869 | |
570 | Ubiquitination | RISGAPDKYESEKRL EECCCCCHHHHHHHH | 50.27 | - | |
570 (in isoform 2) | Ubiquitination | - | 50.27 | - | |
570 (in isoform 2) | Acetylation | - | 50.27 | - | |
570 | Acetylation | RISGAPDKYESEKRL EECCCCCHHHHHHHH | 50.27 | 22902405 | |
575 | Ubiquitination | PDKYESEKRLGSERR CCHHHHHHHHCCCHH | 63.30 | - | |
620 | Phosphorylation | LTEELAEYAEIRVK- CHHHHHHHHHHEEC- | 12.15 | 22817900 |
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 !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MAG_RAT !! |
* 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 !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of MAG_RAT !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Palmitoylation | |
Reference | PubMed |
"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. |