MAG_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: MAG_HUMAN
• UniProt AC: P20916
• Protein Name: Myelin-associated glycoprotein
• Gene Name: MAG
• Organism: Homo sapiens (Human).
• 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 (By similarity). Not required for initial myelination, but seems to play a role in the maintenance of normal axon myelination. Protects motoneurons against apoptosis, also after injury; protection against apoptosis is probably mediated via interaction with neuronal RTN4R and RTN4RL2. Required to prevent degeneration of myelinated axons in adults; this probably depends on binding to gangliosides on the axon cell membrane (By similarity). Negative regulator of neurite outgrowth; in dorsal root ganglion neurons the inhibition is mediated primarily via binding to neuronal RTN4R or RTN4RL2 and to a lesser degree via binding to neuronal gangliosides. In cerebellar granule cells the inhibition is mediated primarily via binding to neuronal gangliosides. In sensory neurons, inhibition of neurite extension depends only partially on RTN4R, RTN4RL2 and gangliosides. Inhibits axon longitudinal growth (By similarity). Inhibits axon outgrowth by binding to RTN4R (By similarity). Preferentially binds to alpha-2,3-linked sialic acid. Binds ganglioside Gt1b (By similarity)..
• Protein Sequence: MIFLTALPLFWIMISASRGGHWGAWMPSSISAFEGTCVSIPCRFDFPDELRPAVVHGVWYFNSPYPKNYPPVVFKSRTQVVHESFQGRSRLLGDLGLRNCTLLLSNVSPELGGKYYFRGDLGGYNQYTFSEHSVLDIVNTPNIVVPPEVVAGTEVEVSCMVPDNCPELRPELSWLGHEGLGEPAVLGRLREDEGTWVQVSLLHFVPTREANGHRLGCQASFPNTTLQFEGYASMDVKYPPVIVEMNSSVEAIEGSHVSLLCGADSNPPPLLTWMRDGTVLREAVAESLLLELEEVTPAEDGVYACLAENAYGQDNRTVGLSVMYAPWKPTVNGTMVAVEGETVSILCSTQSNPDPILTIFKEKQILSTVIYESELQLELPAVSPEDDGEYWCVAENQYGQRATAFNLSVEFAPVLLLESHCAAARDTVQCLCVVKSNPEPSVAFELPSRNVTVNESEREFVYSERSGLVLTSILTLRGQAQAPPRVICTARNLYGAKSLELPFQGAHRLMWAKIGPVGAVVAFAILIAIVCYITQTRRKKNVTESPSFSAGDNPPVLFSSDFRISGAPEKYESERRLGSERRLLGLRGEPPELDLSYSHSDLGKRPTKDSYTLTEELAEYAEIRVK

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
5	Phosphorylation	---MIFLTALPLFWI ---CCEECHHHHHHH	18.52	25072903
15	Phosphorylation	PLFWIMISASRGGHW HHHHHHHHCCCCCCC	11.65	25072903
17	Phosphorylation	FWIMISASRGGHWGA HHHHHHCCCCCCCCC	25.35	25072903
29	Phosphorylation	WGAWMPSSISAFEGT CCCCCCCCEEECCCE	18.07	30631047
31	Phosphorylation	AWMPSSISAFEGTCV CCCCCCEEECCCEEE	28.93	30631047
36	Phosphorylation	SISAFEGTCVSIPCR CEEECCCEEEECCCC	11.53	30631047
99	N-linked_Glycosylation	LGDLGLRNCTLLLSN HHHHCCCCCEEEEEC	28.33	7505568
99	N-linked_Glycosylation	LGDLGLRNCTLLLSN HHHHCCCCCEEEEEC	28.33	7505568
101	O-linked_Glycosylation	DLGLRNCTLLLSNVS HHCCCCCEEEEECCC	24.80	28657654
106	N-linked_Glycosylation	NCTLLLSNVSPELGG CCEEEEECCCHHHCC	37.95	7505568
106	N-linked_Glycosylation	NCTLLLSNVSPELGG CCEEEEECCCHHHCC	37.95	7505568
223	N-linked_Glycosylation	GCQASFPNTTLQFEG EEEEECCCCEEEEEE	43.62	7505568
223	N-linked_Glycosylation	GCQASFPNTTLQFEG EEEEECCCCEEEEEE	43.62	7505568
246	N-linked_Glycosylation	PPVIVEMNSSVEAIE CCEEEEECCCEEEEC	20.02	7505568
246	N-linked_Glycosylation	PPVIVEMNSSVEAIE CCEEEEECCCEEEEC	20.02	7505568
315	N-linked_Glycosylation	ENAYGQDNRTVGLSV ECCCCCCCCEEEEEE	33.37	7505568
315	N-linked_Glycosylation	ENAYGQDNRTVGLSV ECCCCCCCCEEEEEE	33.37	7505568
406	N-linked_Glycosylation	GQRATAFNLSVEFAP CCEEEEEEEEEECHH	29.01	7505568
406	N-linked_Glycosylation	GQRATAFNLSVEFAP CCEEEEEEEEEECHH	29.01	7505568
430	S-palmitoylation	AARDTVQCLCVVKSN HHCCEEEEEEEECCC	2.50	29575903
432	S-palmitoylation	RDTVQCLCVVKSNPE CCEEEEEEEECCCCC	4.32	29575903
436	Phosphorylation	QCLCVVKSNPEPSVA EEEEEECCCCCCCEE	46.11	-
441	Phosphorylation	VKSNPEPSVAFELPS ECCCCCCCEEEECCC	25.15	-
450	N-linked_Glycosylation	AFELPSRNVTVNESE EEECCCCCEECCHHH	37.84	7505568
450	N-linked_Glycosylation	AFELPSRNVTVNESE EEECCCCCEECCHHH	37.84	7505568
454	N-linked_Glycosylation	PSRNVTVNESEREFV CCCCEECCHHHHHEE	37.40	7505568
454	N-linked_Glycosylation	PSRNVTVNESEREFV CCCCEECCHHHHHEE	37.40	7505568
531	S-palmitoylation	AILIAIVCYITQTRR HHHHHHHHHHHHHCC	1.34	1703542
543	Phosphorylation	TRRKKNVTESPSFSA HCCCCCCCCCCCCCC	39.89	18510355
545	Phosphorylation	RKKNVTESPSFSAGD CCCCCCCCCCCCCCC	19.24	25332170
547	Phosphorylation	KNVTESPSFSAGDNP CCCCCCCCCCCCCCC	40.90	18510355
549	Phosphorylation	VTESPSFSAGDNPPV CCCCCCCCCCCCCCE	35.36	24076635
571	Phosphorylation	ISGAPEKYESERRLG ECCCCHHHHHHHHHC	24.03	-
575	Methylation	PEKYESERRLGSERR CHHHHHHHHHCCCHH	48.69	54487783
620	Phosphorylation	LTEELAEYAEIRVK- CHHHHHHHHHHEEC-	12.15	7525550

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of MAG_HUMAN !!

Functions of PTM Sites

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

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of MAG_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CO1A1_HUMAN	COL1A1	physical	2446864
CO2A1_HUMAN	COL2A1	physical	2446864
CO3A1_HUMAN	COL3A1	physical	2446864
CO4A1_HUMAN	COL4A1	physical	2446864
CO5A1_HUMAN	COL5A1	physical	2446864
CO6A1_HUMAN	COL6A1	physical	2446864
CO9A1_HUMAN	COL9A1	physical	2446864
FYN_HUMAN	FYN	physical	7525550
MAP1B_HUMAN	MAP1B	physical	11733546
A4_HUMAN	APP	physical	21832049

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.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"Identification of the glycosylated sequons of human myelin-associatedglycoprotein.";
Burger D., Pidoux L., Steck A.J.;
Biochem. Biophys. Res. Commun. 197:457-464(1993).
Cited for: GLYCOSYLATION AT ASN-99; ASN-106; ASN-223; ASN-246; ASN-315; ASN-406;ASN-450 AND ASN-454, AND LACK OF GLYCOSYLATION AT ASN-332.
PubMed: 7505568