dbPTM

NEUM_RAT - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NEUM_RAT
UniProt AC	P07936
Protein Name	Neuromodulin
Gene Name	Gap43
Organism	Rattus norvegicus (Rat).
Sequence Length	226
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 (By similarity)..
Protein Sequence	MLCCMRRTKQVEKNDEDQKIEQDGVKPEDKAHKAATKIQASFRGHITRKKLKDEKKGDAPAAEAEAKEKDDAPVADGVEKKEGDGSATTDAAPATSPKAEEPSKAGDAPSEEKKGEGDAAPSEEKAGSAETESAAKATTDNSPSSKAEDGPAKEEPKQADVPAAVTDAAATTPAAEDAAKAAQPPTETAESSQAEEEKEAVDEAKPKESARQDEGKEDPEADQEHA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	S-palmitoylation	-----MLCCMRRTKQ -----CCCCCCCCCC	1.33	2918027
3	Glutathionylation	-----MLCCMRRTKQ -----CCCCCCCCCC	1.33	11060308
4	S-palmitoylation	----MLCCMRRTKQV ----CCCCCCCCCCC	1.78	2918027
4	Glutathionylation	----MLCCMRRTKQV ----CCCCCCCCCCC	1.78	11060308
19	Ubiquitination	EKNDEDQKIEQDGVK CCCHHHHHHHHCCCC	61.61	-
26	Acetylation	KIEQDGVKPEDKAHK HHHHCCCCHHHHHHH	48.49	22902405
26	Ubiquitination	KIEQDGVKPEDKAHK HHHHCCCCHHHHHHH	48.49	-
30	Ubiquitination	DGVKPEDKAHKAATK CCCCHHHHHHHHHHH	51.21	-
37	Ubiquitination	KAHKAATKIQASFRG HHHHHHHHHHHHHHC	28.26	-
41	Phosphorylation	AATKIQASFRGHITR HHHHHHHHHHCCCCH	10.09	9349568
52	Ubiquitination	HITRKKLKDEKKGDA CCCHHHHCCCCCCCC	73.12	-
55	Ubiquitination	RKKLKDEKKGDAPAA HHHHCCCCCCCCCHH	72.66	-
56	Ubiquitination	KKLKDEKKGDAPAAE HHHCCCCCCCCCHHH	61.03	-
67	Ubiquitination	PAAEAEAKEKDDAPV CHHHHHHHHHCCCCC	57.72	-
69	Ubiquitination	AEAEAKEKDDAPVAD HHHHHHHHCCCCCCC	61.27	-
80	Ubiquitination	PVADGVEKKEGDGSA CCCCCCCEECCCCCC	54.43	-
81	Ubiquitination	VADGVEKKEGDGSAT CCCCCCEECCCCCCC	54.12	-
86	Phosphorylation	EKKEGDGSATTDAAP CEECCCCCCCCCCCC	27.47	30411139
88	Phosphorylation	KEGDGSATTDAAPAT ECCCCCCCCCCCCCC	27.23	30411139
89	Phosphorylation	EGDGSATTDAAPATS CCCCCCCCCCCCCCC	24.29	9349568
95	Phosphorylation	TTDAAPATSPKAEEP CCCCCCCCCCCCCCC	44.49	9349568
96	Phosphorylation	TDAAPATSPKAEEPS CCCCCCCCCCCCCCC	26.89	9349568
98	Ubiquitination	AAPATSPKAEEPSKA CCCCCCCCCCCCCCC	69.10	-
103	Phosphorylation	SPKAEEPSKAGDAPS CCCCCCCCCCCCCCC	38.12	30240740
110	Phosphorylation	SKAGDAPSEEKKGEG CCCCCCCCHHHCCCC	61.17	30240740
122	Phosphorylation	GEGDAAPSEEKAGSA CCCCCCCCHHHCCCC	54.37	28432305
125	Ubiquitination	DAAPSEEKAGSAETE CCCCCHHHCCCCCHH	54.73	-
128	Phosphorylation	PSEEKAGSAETESAA CCHHHCCCCCHHHHH	28.00	30240740
133	Phosphorylation	AGSAETESAAKATTD CCCCCHHHHHHHHCC	40.73	28551015
136	Ubiquitination	AETESAAKATTDNSP CCHHHHHHHHCCCCC	46.08	-
138	Phosphorylation	TESAAKATTDNSPSS HHHHHHHHCCCCCCC	33.69	28551015
139	Phosphorylation	ESAAKATTDNSPSSK HHHHHHHCCCCCCCC	37.73	28432305
142	Phosphorylation	AKATTDNSPSSKAED HHHHCCCCCCCCCCC	29.03	30240740
144	Phosphorylation	ATTDNSPSSKAEDGP HHCCCCCCCCCCCCC	44.27	28432305
145	Phosphorylation	TTDNSPSSKAEDGPA HCCCCCCCCCCCCCC	38.99	30240740
166	Phosphorylation	ADVPAAVTDAAATTP CCCCHHHCCHHHCCH	18.39	28551015
171	Phosphorylation	AVTDAAATTPAAEDA HHCCHHHCCHHHHHH	28.69	27097102
172	Phosphorylation	VTDAAATTPAAEDAA HCCHHHCCHHHHHHH	13.25	25403869
186	Phosphorylation	AKAAQPPTETAESSQ HHHCCCCCHHHHHHH	53.29	28551015
188	Phosphorylation	AAQPPTETAESSQAE HCCCCCHHHHHHHHH	37.90	28551015
191	Phosphorylation	PPTETAESSQAEEEK CCCHHHHHHHHHHHH	25.86	9349568
192	Phosphorylation	PTETAESSQAEEEKE CCHHHHHHHHHHHHH	25.55	30411139
198	Acetylation	SSQAEEEKEAVDEAK HHHHHHHHHHHHHHC	55.01	22902405
205	Acetylation	KEAVDEAKPKESARQ HHHHHHHCCHHHHCC	55.35	22902405
216	Acetylation	SARQDEGKEDPEADQ HHCCCCCCCCHHHHH	57.82	22902405

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	PRKCA	P17252	GPS
41	S	Phosphorylation	Kinase	PKCA	P05696	PSP
41	S	Phosphorylation	Kinase	PHK-FAMILY	-	GPS
41	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
41	S	Phosphorylation	Kinase	PHK	-	Uniprot
41	S	Phosphorylation	Kinase	PKC	-	Uniprot
41	S	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM
88	T	Phosphorylation	Kinase	CSNK2A1	P19139	GPS
89	T	Phosphorylation	Kinase	CSNK2A1	P19139	GPS
95	T	Phosphorylation	Kinase	CSNK2A1	P19139	GPS
96	S	Phosphorylation	Kinase	CSNK2A1	P19139	GPS
191	S	Phosphorylation	Kinase	CSNK2A1	P19139	GPS
192	S	Phosphorylation	Kinase	CSNK2A1	P19139	GPS

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of NEUM_RAT !!

Drug and Disease Associations

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

Regulatory Network of NEUM_RAT

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Phosphorylase kinase phosphorylates the calmodulin-binding regulatoryregions of neuronal tissue-specific proteins B-50 (GAP-43) andneurogranin."; Paudel H.K., Zwiers H., Wang J.H.; J. Biol. Chem. 268:6207-6213(1993). Cited for: PHOSPHORYLATION AT SER-41 BY PHK.	8454596 [Abstract]
"GAP-43, a protein associated with axon growth, is phosphorylated atthree sites in cultured neurons and rat brain."; Spencer S.A., Schuh S.M., Liu W.-S., Willard M.B.; J. Biol. Chem. 267:9059-9064(1992). Cited for: PHOSPHORYLATION AT SER-41; SER-96 AND THR-172.	1533624 [Abstract]