dbPTM

MBP_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MBP_HUMAN
UniProt AC	P02686
Protein Name	Myelin basic protein
Gene Name	MBP
Organism	Homo sapiens (Human).
Sequence Length	304
Subcellular Localization	Myelin membrane Peripheral membrane protein Cytoplasmic side. Cytoplasmic side of myelin. Isoform 3: Nucleus . Targeted to nucleus in oligodendrocytes.
Protein Description	The classic group of MBP isoforms (isoform 4-isoform 14) are with PLP the most abundant protein components of the myelin membrane in the CNS. They have a role in both its formation and stabilization. The smaller isoforms might have an important role in remyelination of denuded axons in multiple sclerosis. The non-classic group of MBP isoforms (isoform 1-isoform 3/Golli-MBPs) may preferentially have a role in the early developing brain long before myelination, maybe as components of transcriptional complexes, and may also be involved in signaling pathways in T-cells and neural cells. Differential splicing events combined with optional post-translational modifications give a wide spectrum of isomers, with each of them potentially having a specialized function. Induces T-cell proliferation..
Protein Sequence	MGNHAGKRELNAEKASTNSETNRGESEKKRNLGELSRTTSEDNEVFGEADANQNNGTSSQDTAVTDSKRTADPKNAWQDAHPADPGSRPHLIRLFSRDAPGREDNTFKDRPSESDELQTIQEDSAATSESLDVMASQKRPSQRHGSKYLATASTMDHARHGFLPRHRDTGILDSIGRFFGGDRGAPKRGSGKDSHHPARTAHYGSLPQKSHGRTQDENPVVHFFKNIVTPRTPPPSQGKGRGLSLSRFSWGAEGQRPGFGYGGRASDYKSAHKGFKGVDAQGTLSKIFKLGGRDSRSGSPMARR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2 (in isoform 3)	Acetylation	-	34.33	7544282
2 (in isoform 4)	Acetylation	-	34.33	7544282
2 (in isoform 5)	Acetylation	-	34.33	7544282
2 (in isoform 6)	Acetylation	-	34.33	7544282
8 (in isoform 3)	Phosphorylation	-	53.36	2413024
8 (in isoform 4)	Phosphorylation	-	53.36	2413024
8 (in isoform 5)	Phosphorylation	-	53.36	2413024
8 (in isoform 6)	Phosphorylation	-	53.36	2413024
16	Phosphorylation	ELNAEKASTNSETNR HCCHHHHHCCCCCCC	38.91	23401153
17	Phosphorylation	LNAEKASTNSETNRG CCHHHHHCCCCCCCC	47.85	23401153
19	Phosphorylation	AEKASTNSETNRGES HHHHHCCCCCCCCHH	45.98	23401153
21	Phosphorylation	KASTNSETNRGESEK HHHCCCCCCCCHHHH	30.00	30108239
26	Phosphorylation	SETNRGESEKKRNLG CCCCCCHHHHHHCHH	58.50	20164059
36	Phosphorylation	KRNLGELSRTTSEDN HHCHHHHHCCCCCCC	24.23	25159151
38	Phosphorylation	NLGELSRTTSEDNEV CHHHHHCCCCCCCCC	31.16	23401153
39	Phosphorylation	LGELSRTTSEDNEVF HHHHHCCCCCCCCCC	29.07	25159151
40	Phosphorylation	GELSRTTSEDNEVFG HHHHCCCCCCCCCCC	42.19	23401153
57	Phosphorylation	DANQNNGTSSQDTAV CCCCCCCCCCCCCCC	27.59	28258704
57 (in isoform 3)	Phosphorylation	-	27.59	2413024
57 (in isoform 4)	Phosphorylation	-	27.59	2413024
58	Phosphorylation	ANQNNGTSSQDTAVT CCCCCCCCCCCCCCC	27.66	28258704
59	Phosphorylation	NQNNGTSSQDTAVTD CCCCCCCCCCCCCCC	31.73	29978859
62	Phosphorylation	NGTSSQDTAVTDSKR CCCCCCCCCCCCCCC	18.52	23927012
65	Phosphorylation	SSQDTAVTDSKRTAD CCCCCCCCCCCCCCC	31.90	23927012
67	Phosphorylation	QDTAVTDSKRTADPK CCCCCCCCCCCCCCC	18.05	23927012
68 (in isoform 3)	Phosphorylation	-	57.49	20886841
68 (in isoform 4)	Phosphorylation	-	57.49	20886841
87	Phosphorylation	AHPADPGSRPHLIRL CCCCCCCCCCHHHHH	48.29	27251275
96	Phosphorylation	PHLIRLFSRDAPGRE CHHHHHHCCCCCCCC	33.57	23401153
106	Phosphorylation	APGREDNTFKDRPSE CCCCCCCCCCCCCCC	44.37	23403867
108	Methylation	GREDNTFKDRPSESD CCCCCCCCCCCCCCH	51.28	4924231
110	Methylation	EDNTFKDRPSESDEL CCCCCCCCCCCCHHH	36.92	-
112	Methylation	NTFKDRPSESDELQT CCCCCCCCCCHHHHH	51.10	4924231
112	Phosphorylation	NTFKDRPSESDELQT CCCCCCCCCCHHHHH	51.10	28102081
114	Phosphorylation	FKDRPSESDELQTIQ CCCCCCCCHHHHHHH	40.50	25159151
119	Phosphorylation	SESDELQTIQEDSAA CCCHHHHHHHHHHHH	36.93	30108239
123	Methylation	ELQTIQEDSAATSES HHHHHHHHHHHCHHH	27.48	4924231
124	O-linked_Glycosylation	LQTIQEDSAATSESL HHHHHHHHHHCHHHH	21.03	OGP
124	Phosphorylation	LQTIQEDSAATSESL HHHHHHHHHHCHHHH	21.03	28450419
127	Phosphorylation	IQEDSAATSESLDVM HHHHHHHCHHHHHHH	32.51	28060719
128	Phosphorylation	QEDSAATSESLDVMA HHHHHHCHHHHHHHH	22.06	28060719
130	Phosphorylation	DSAATSESLDVMASQ HHHHCHHHHHHHHHC	29.63	28060719
134	Methylation	TSESLDVMASQKRPS CHHHHHHHHHCCCCC	2.72	4924231
136	Phosphorylation	ESLDVMASQKRPSQR HHHHHHHHCCCCCCC	20.38	27251789
138	Methylation	LDVMASQKRPSQRHG HHHHHHCCCCCCCCC	64.87	4924231
141	Phosphorylation	MASQKRPSQRHGSKY HHHCCCCCCCCCCCE	43.83	22817900
146	Phosphorylation	RPSQRHGSKYLATAS CCCCCCCCCEEEEHH	16.41	23401153
148	Phosphorylation	SQRHGSKYLATASTM CCCCCCCEEEEHHHH	11.85	24927040
149	Methylation	QRHGSKYLATASTMD CCCCCCEEEEHHHHH	3.82	4924231
151	Phosphorylation	HGSKYLATASTMDHA CCCCEEEEHHHHHHH	20.67	24114839
153	Phosphorylation	SKYLATASTMDHARH CCEEEEHHHHHHHHH	21.65	28348404
154	Phosphorylation	KYLATASTMDHARHG CEEEEHHHHHHHHHC	24.93	20886841
159	Citrullination	ASTMDHARHGFLPRH HHHHHHHHHCCCCCC	27.35	-
159	Citrullination	ASTMDHARHGFLPRH HHHHHHHHHCCCCCC	27.35	2466844
165	Citrullination	ARHGFLPRHRDTGIL HHHCCCCCCCCCCCH	39.35	-
165	Citrullination	ARHGFLPRHRDTGIL HHHCCCCCCCCCCCH	39.35	2466844
167	Citrullination	HGFLPRHRDTGILDS HCCCCCCCCCCCHHH	44.45	-
167	Citrullination	HGFLPRHRDTGILDS HCCCCCCCCCCCHHH	44.45	23828821
169	Phosphorylation	FLPRHRDTGILDSIG CCCCCCCCCCHHHHH	26.53	20886841
174	Phosphorylation	RDTGILDSIGRFFGG CCCCCHHHHHHHCCC	24.40	19060867
177	Methylation	GILDSIGRFFGGDRG CCHHHHHHHCCCCCC	23.27	-
183	Methylation	GRFFGGDRGAPKRGS HHHCCCCCCCCCCCC	46.58	-
190	Phosphorylation	RGAPKRGSGKDSHHP CCCCCCCCCCCCCCC	46.86	2413024
190 (in isoform 2)	Phosphorylation	-	46.86	24719451
199	Citrullination	KDSHHPARTAHYGSL CCCCCCCCCCCCCCC	36.58	-
199	Citrullination	KDSHHPARTAHYGSL CCCCCCCCCCCCCCC	36.58	23828821
200	Phosphorylation	DSHHPARTAHYGSLP CCCCCCCCCCCCCCC	21.64	25307156
203	Phosphorylation	HPARTAHYGSLPQKS CCCCCCCCCCCCCCC	13.12	24927040
205	Phosphorylation	ARTAHYGSLPQKSHG CCCCCCCCCCCCCCC	29.70	20886841
210	Phosphorylation	YGSLPQKSHGRTQDE CCCCCCCCCCCCCCC	26.40	25332170
214	Phosphorylation	PQKSHGRTQDENPVV CCCCCCCCCCCCCCE	44.99	24076635
229	O-linked_Glycosylation	HFFKNIVTPRTPPPS EEECCCCCCCCCCCC	11.85	2458139
229	Phosphorylation	HFFKNIVTPRTPPPS EEECCCCCCCCCCCC	11.85	12760422
231	Citrullination	FKNIVTPRTPPPSQG ECCCCCCCCCCCCCC	50.96	-
231	Citrullination	FKNIVTPRTPPPSQG ECCCCCCCCCCCCCC	50.96	23828821
232	O-linked_Glycosylation	KNIVTPRTPPPSQGK CCCCCCCCCCCCCCC	41.15	2458139
232	Phosphorylation	KNIVTPRTPPPSQGK CCCCCCCCCCCCCCC	41.15	26329039
236	Phosphorylation	TPRTPPPSQGKGRGL CCCCCCCCCCCCCCC	58.29	25307156
237	Deamidated glutamine	PRTPPPSQGKGRGLS CCCCCCCCCCCCCCC	64.49	-
237	Deamidation	PRTPPPSQGKGRGLS CCCCCCCCCCCCCCC	64.49	-
241	Dimethylation	PPSQGKGRGLSLSRF CCCCCCCCCCCCCCE	46.49	-
241	Methylation	PPSQGKGRGLSLSRF CCCCCCCCCCCCCCE	46.49	5128665
244	Phosphorylation	QGKGRGLSLSRFSWG CCCCCCCCCCCEECC	27.42	24719451
246	Phosphorylation	KGRGLSLSRFSWGAE CCCCCCCCCEECCCC	28.09	17081983
249	O-linked_Glycosylation	GLSLSRFSWGAEGQR CCCCCCEECCCCCCC	24.40	28657654
249	Phosphorylation	GLSLSRFSWGAEGQR CCCCCCEECCCCCCC	24.40	20886841
256	Citrullination	SWGAEGQRPGFGYGG ECCCCCCCCCCCCCC	44.13	-
256	Citrullination	SWGAEGQRPGFGYGG ECCCCCCCCCCCCCC	44.13	2466844
261	Phosphorylation	GQRPGFGYGGRASDY CCCCCCCCCCCHHHH	17.72	-
264	Citrullination	PGFGYGGRASDYKSA CCCCCCCCHHHHHHH	26.93	-
264	Citrullination	PGFGYGGRASDYKSA CCCCCCCCHHHHHHH	26.93	2466844
266	Phosphorylation	FGYGGRASDYKSAHK CCCCCCHHHHHHHCC	39.86	25307156
281	Deamidated glutamine	GFKGVDAQGTLSKIF CCCCCCCCCHHHHHH	40.72	-
281	Deamidation	GFKGVDAQGTLSKIF CCCCCCCCCHHHHHH	40.72	-
283	Phosphorylation	KGVDAQGTLSKIFKL CCCCCCCHHHHHHHC	18.77	20886841
285	Phosphorylation	VDAQGTLSKIFKLGG CCCCCHHHHHHHCCC	24.44	20886841
293	Citrullination	KIFKLGGRDSRSGSP HHHHCCCCCCCCCCC	36.61	-
293	Citrullination	KIFKLGGRDSRSGSP HHHHCCCCCCCCCCC	36.61	2466844
295	Phosphorylation	FKLGGRDSRSGSPMA HHCCCCCCCCCCCCC	27.30	2413024
296	Citrullination	KLGGRDSRSGSPMAR HCCCCCCCCCCCCCC	49.69	-
296	Citrullination	KLGGRDSRSGSPMAR HCCCCCCCCCCCCCC	49.69	23828821
297	Phosphorylation	LGGRDSRSGSPMARR CCCCCCCCCCCCCCC	47.80	26437602
299	Phosphorylation	GRDSRSGSPMARR-- CCCCCCCCCCCCC--	16.85	23403867
303	Citrullination	RSGSPMARR------ CCCCCCCCC------	38.29	-
303	Citrullination	RSGSPMARR------ CCCCCCCCC------	38.29	23828821
304	Citrullination	SGSPMARR------- CCCCCCCC-------	41.16	-
304	Citrullination	SGSPMARR------- CCCCCCCC-------	41.16	2466844

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
162	S	Phosphorylation	Kinase	PRKD1	Q15139	PSP
232	T	Phosphorylation	Kinase	MAPK1	P28482	GPS
232	T	Phosphorylation	Kinase	MAPK3	P27361	GPS
232	T	Phosphorylation	Kinase	MAPK-FAMILY	-	GPS
295	S	Phosphorylation	Kinase	PKD-FAMILY	-	GPS
299	S	Phosphorylation	Kinase	UHMK1	Q8TAS1	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
241	R	Methylation		-
Arg-241 was found to be 6% monomethylated and 60% symmetrically dimethylated.

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 MBP_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MYPR_HUMAN	PLP1	physical	6083474
MYPR_HUMAN	PLP1	physical	2467009
DDX58_HUMAN	DDX58	physical	23264040
CTDS1_HUMAN	CTDSP1	physical	25416956
CTDSL_HUMAN	CTDSPL	physical	28514442
CTDS1_HUMAN	CTDSP1	physical	28514442
IDE_HUMAN	IDE	physical	28514442

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 MBP_HUMAN

Related Literatures of Post-Translational Modification

Methylation
Reference	PubMed
"Isolation and partial characterization of methylated arginines fromthe encephalitogenic basic protein of myelin."; Baldwin G.S., Carnegie P.R.; Biochem. J. 123:69-74(1971). Cited for: METHYLATION AT ARG-241.	5128665 [Abstract]
Phosphorylation
Reference	PubMed
"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-96, AND MASSSPECTROMETRY.	17081983 [Abstract]

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