dbPTM

NEUM_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NEUM_MOUSE
UniProt AC	P06837
Protein Name	Neuromodulin
Gene Name	Gap43
Organism	Mus musculus (Mouse).
Sequence Length	227
Subcellular Localization	Cell membrane Peripheral membrane protein Cytoplasmic side. Cell projection, growth cone membrane Peripheral membrane protein Cytoplasmic side. Cell junction, synapse. Cell projection, filopodium membrane Peripheral membrane protein. Cytoplasmic
Protein Description	This protein is associated with nerve growth. It is a major component of the motile "growth cones" that form the tips of elongating axons. Plays a role in axonal and dendritic filopodia induction..
Protein Sequence	MLCCMRRTKQVEKNDEDQKIEQDGVKPEDKAHKAATKIQASFRGHITRKKLKGEKKGDAPAAEAEAKEKDDAPVADGVEKKEGDGSATTDAAPATSPKAEEPSKAGDAPSEEKKGEGDAAPSEEKAGSAETESAAKATTDNSPSSKAEDGPAKEEPKQADVPAAVTDAAATTPAAEDAATKAAQPPTETAESSQAEEEKDAVDEAKPKESARQDEGKEDPEADQEHA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	S-palmitoylation	-----MLCCMRRTKQ -----CCCCCCCCCC	1.33	8399217
4	S-palmitoylation	----MLCCMRRTKQV ----CCCCCCCCCCC	1.78	8399217
9	Ubiquitination	LCCMRRTKQVEKNDE CCCCCCCCCCCCCHH	51.00	-
13	Ubiquitination	RRTKQVEKNDEDQKI CCCCCCCCCHHHHHH	71.49	27667366
19	Ubiquitination	EKNDEDQKIEQDGVK CCCHHHHHHHHCCCC	61.61	22790023
26	Ubiquitination	KIEQDGVKPEDKAHK HHHHCCCCHHHHHHH	48.49	27667366
30	Ubiquitination	DGVKPEDKAHKAATK CCCCHHHHHHHHHHH	51.21	27667366
36	Phosphorylation	DKAHKAATKIQASFR HHHHHHHHHHHHHHH	33.27	22817900
37	Ubiquitination	KAHKAATKIQASFRG HHHHHHHHHHHHHHC	28.26	22790023
41	Phosphorylation	AATKIQASFRGHITR HHHHHHHHHHCCCCH	10.09	23527152
47	Phosphorylation	ASFRGHITRKKLKGE HHHHCCCCHHHCCCC	30.66	22324799
56	Ubiquitination	KKLKGEKKGDAPAAE HHCCCCCCCCCCHHH	58.69	22790023
67	Ubiquitination	PAAEAEAKEKDDAPV CHHHHHHHHHCCCCC	57.72	22790023
69	Ubiquitination	AEAEAKEKDDAPVAD HHHHHHHHCCCCCCC	61.27	22790023
80	Ubiquitination	PVADGVEKKEGDGSA CCCCCCCEECCCCCC	54.43	22790023
81	Ubiquitination	VADGVEKKEGDGSAT CCCCCCEECCCCCCC	54.12	22790023
86	Phosphorylation	EKKEGDGSATTDAAP CEECCCCCCCCCCCC	27.47	25521595
88	Phosphorylation	KEGDGSATTDAAPAT ECCCCCCCCCCCCCC	27.23	25521595
89	Phosphorylation	EGDGSATTDAAPATS CCCCCCCCCCCCCCC	24.29	22324799
95	Phosphorylation	TTDAAPATSPKAEEP CCCCCCCCCCCCCCC	44.49	25521595
96	Phosphorylation	TDAAPATSPKAEEPS CCCCCCCCCCCCCCC	26.89	25521595
98	Ubiquitination	AAPATSPKAEEPSKA CCCCCCCCCCCCCCC	69.10	27667366
103	Phosphorylation	SPKAEEPSKAGDAPS CCCCCCCCCCCCCCC	38.12	24925903
104	Ubiquitination	PKAEEPSKAGDAPSE CCCCCCCCCCCCCCH	68.08	22790023
110	Phosphorylation	SKAGDAPSEEKKGEG CCCCCCCCHHHCCCC	61.17	25521595
113	Ubiquitination	GDAPSEEKKGEGDAA CCCCCHHHCCCCCCC	63.13	27667366
114	Ubiquitination	DAPSEEKKGEGDAAP CCCCHHHCCCCCCCC	66.53	27667366
122	Phosphorylation	GEGDAAPSEEKAGSA CCCCCCCCHHHCCCC	54.37	25521595
125	Ubiquitination	DAAPSEEKAGSAETE CCCCCHHHCCCCCHH	54.73	22790023
128	Phosphorylation	PSEEKAGSAETESAA CCHHHCCCCCHHHHH	28.00	25521595
131	Phosphorylation	EKAGSAETESAAKAT HHCCCCCHHHHHHHH	34.65	20415495
133	Phosphorylation	AGSAETESAAKATTD CCCCCHHHHHHHHCC	40.73	25521595
136	Ubiquitination	AETESAAKATTDNSP CCHHHHHHHHCCCCC	46.08	22790023
138	Phosphorylation	TESAAKATTDNSPSS HHHHHHHHCCCCCCC	33.69	24925903
139	Phosphorylation	ESAAKATTDNSPSSK HHHHHHHCCCCCCCC	37.73	24925903
142	Phosphorylation	AKATTDNSPSSKAED HHHHCCCCCCCCCCC	29.03	25521595
144	Phosphorylation	ATTDNSPSSKAEDGP HHCCCCCCCCCCCCC	44.27	24925903
145	Phosphorylation	TTDNSPSSKAEDGPA HCCCCCCCCCCCCCC	38.99	24925903
146	Ubiquitination	TDNSPSSKAEDGPAK CCCCCCCCCCCCCCC	61.20	27667366
153	Ubiquitination	KAEDGPAKEEPKQAD CCCCCCCCCCCCCCC	66.79	27667366
166	Phosphorylation	ADVPAAVTDAAATTP CCCCHHHCCHHHCCH	18.39	24925903
166	O-linked_Glycosylation	ADVPAAVTDAAATTP CCCCHHHCCHHHCCH	18.39	55412081
171	Phosphorylation	AVTDAAATTPAAEDA HHCCHHHCCHHHHHH	28.69	25521595
172	Phosphorylation	VTDAAATTPAAEDAA HCCHHHCCHHHHHHH	13.25	25521595
180	Phosphorylation	PAAEDAATKAAQPPT HHHHHHHHHHCCCCC	23.96	24925903
187	Phosphorylation	TKAAQPPTETAESSQ HHHCCCCCHHHHHHH	53.29	25521595
189	Phosphorylation	AAQPPTETAESSQAE HCCCCCHHHHHHHHH	37.90	25521595
192	Phosphorylation	PPTETAESSQAEEEK CCCHHHHHHHHHHHH	25.86	25521595
193	Phosphorylation	PTETAESSQAEEEKD CCHHHHHHHHHHHHH	25.55	25521595
199	Ubiquitination	SSQAEEEKDAVDEAK HHHHHHHHHHCHHHC	55.02	22790023
217	Ubiquitination	SARQDEGKEDPEADQ HHCCCCCCCCHHHHH	57.82	27667366

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
41	S	Phosphorylation	Kinase	PHK	-	Uniprot
88	T	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
89	T	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
95	T	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
96	S	Phosphorylation	Kinase	JNK1	P45983	PSP
192	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
192	S	Phosphorylation	Kinase	CK2	-	Uniprot
193	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
193	S	Phosphorylation	Kinase	CK2	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of NEUM_MOUSE !!

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 NEUM_MOUSE !!

Protein-Protein Interaction

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

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of NEUM_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations."; Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.; Mol. Cell. Proteomics 6:283-293(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-95; SER-103 AND THR-172,AND MASS SPECTROMETRY.	17114649 [Abstract]
"Phosphoproteomic analysis of the developing mouse brain."; Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.; Mol. Cell. Proteomics 3:1093-1101(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96 AND THR-172, AND MASSSPECTROMETRY.	15345747 [Abstract]
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations."; Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.; Mol. Cell. Proteomics 5:914-922(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-172, AND MASSSPECTROMETRY.	16452087 [Abstract]