dbPTM

MARCS_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MARCS_MOUSE
UniProt AC	P26645
Protein Name	Myristoylated alanine-rich C-kinase substrate
Gene Name	Marcks
Organism	Mus musculus (Mouse).
Sequence Length	309
Subcellular Localization	Cytoplasm, cytoskeleton . Membrane Lipid-anchor .
Protein Description	MARCKS is the most prominent cellular substrate for protein kinase C. This protein binds calmodulin, actin, and synapsin. MARCKS is a filamentous (F) actin cross-linking protein..
Protein Sequence	MGAQFSKTAAKGEATAERPGEAAVASSPSKANGQENGHVKVNGDASPAAAEPGAKEELQANGSAPAADKEEPASGSAATPAAAEKDEAAAATEPGAGAADKEAAEAEPAEPSSPAAEAEGASASSTSSPKAEDGAAPSPSSETPKKKKKRFSFKKSFKLSGFSFKKSKKESGEGAEAEGATAEGAKDEAAAAAGGEGAAAPGEQAGGAGAEGAAGGEPREAEAAEPEQPEQPEQPAAEEPQAEEQSEAAGEKAEEPAPGATAGDASSAAGPEQEAPAATDEAAASAAPAASPEPQPECSPEAPPAPTAE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Myristoylation	------MGAQFSKTA ------CCCCCCCCC	28.25	-
8	Phosphorylation	MGAQFSKTAAKGEAT CCCCCCCCCCCCCCC	30.56	25777480
11	Ubiquitination	QFSKTAAKGEATAER CCCCCCCCCCCCCCC	55.61	22790023
15	Phosphorylation	TAAKGEATAERPGEA CCCCCCCCCCCCCCC	25.42	24925903
26	Phosphorylation	PGEAAVASSPSKANG CCCCEEECCCCCCCC	35.86	25521595
27	Phosphorylation	GEAAVASSPSKANGQ CCCEEECCCCCCCCC	24.37	24925903
29	Phosphorylation	AAVASSPSKANGQEN CEEECCCCCCCCCCC	46.47	25521595
46	Phosphorylation	VKVNGDASPAAAEPG EEECCCCCHHHCCCC	21.58	25521595
63	Phosphorylation	EELQANGSAPAADKE HHHHHCCCCCCCCCC	30.77	26824392
74	Phosphorylation	ADKEEPASGSAATPA CCCCCCCCCCCCCHH	43.95	25521595
76	Phosphorylation	KEEPASGSAATPAAA CCCCCCCCCCCHHHH	16.54	25521595
79	Phosphorylation	PASGSAATPAAAEKD CCCCCCCCHHHHHHH	17.12	25521595
85	Ubiquitination	ATPAAAEKDEAAAAT CCHHHHHHHHHHHHC	57.02	27667366
92	Phosphorylation	KDEAAAATEPGAGAA HHHHHHHCCCCCCHH	37.68	23649490
112	Phosphorylation	EAEPAEPSSPAAEAE HCCCCCCCCHHHHHC	40.22	25521595
113	Phosphorylation	AEPAEPSSPAAEAEG CCCCCCCCHHHHHCC	29.31	25521595
122	Phosphorylation	AAEAEGASASSTSSP HHHHCCCCCCCCCCC	39.27	25521595
124	Phosphorylation	EAEGASASSTSSPKA HHCCCCCCCCCCCCC	31.49	25521595
125	Phosphorylation	AEGASASSTSSPKAE HCCCCCCCCCCCCCC	31.83	25521595
126	Phosphorylation	EGASASSTSSPKAED CCCCCCCCCCCCCCC	30.63	25521595
127	Phosphorylation	GASASSTSSPKAEDG CCCCCCCCCCCCCCC	46.74	25521595
128	Phosphorylation	ASASSTSSPKAEDGA CCCCCCCCCCCCCCC	30.43	25521595
138	Phosphorylation	AEDGAAPSPSSETPK CCCCCCCCCCCCCCC	32.46	24925903
140	Phosphorylation	DGAAPSPSSETPKKK CCCCCCCCCCCCCCC	45.18	24925903
141	Phosphorylation	GAAPSPSSETPKKKK CCCCCCCCCCCCCCC	49.20	24925903
143	Phosphorylation	APSPSSETPKKKKKR CCCCCCCCCCCCCCC	42.21	24925903
145	Ubiquitination	SPSSETPKKKKKRFS CCCCCCCCCCCCCCC	82.01	27667366
146	Ubiquitination	PSSETPKKKKKRFSF CCCCCCCCCCCCCCC	71.65	-
152	Phosphorylation	KKKKKRFSFKKSFKL CCCCCCCCCCHHEEC	39.94	22942356
156	Phosphorylation	KRFSFKKSFKLSGFS CCCCCCHHEECCCCE	28.36	26824392
158	Ubiquitination	FSFKKSFKLSGFSFK CCCCHHEECCCCEEE	49.16	22790023
158	Acetylation	FSFKKSFKLSGFSFK CCCCHHEECCCCEEE	49.16	22826441
160	Phosphorylation	FKKSFKLSGFSFKKS CCHHEECCCCEEECC	38.08	24925903
163	Phosphorylation	SFKLSGFSFKKSKKE HEECCCCEEECCCCC	39.42	18388127
165	Ubiquitination	KLSGFSFKKSKKESG ECCCCEEECCCCCCC	55.74	27667366
165	Acetylation	KLSGFSFKKSKKESG ECCCCEEECCCCCCC	55.74	22826441
167	Phosphorylation	SGFSFKKSKKESGEG CCCEEECCCCCCCCC	49.93	26824392
169	Ubiquitination	FSFKKSKKESGEGAE CEEECCCCCCCCCCH	65.29	27667366
171	Phosphorylation	FKKSKKESGEGAEAE EECCCCCCCCCCHHC	51.53	25521595
181	Phosphorylation	GAEAEGATAEGAKDE CCHHCCCCCCHHHHH	35.78	26824392
246	Phosphorylation	EPQAEEQSEAAGEKA CCCHHHHHHHHHHHC	32.27	25521595
261	Phosphorylation	EEPAPGATAGDASSA CCCCCCCCCCCHHHC	36.77	23140645
266	Phosphorylation	GATAGDASSAAGPEQ CCCCCCHHHCCCCCC	25.83	23140645
267	Phosphorylation	ATAGDASSAAGPEQE CCCCCHHHCCCCCCC	24.69	23140645
279	Phosphorylation	EQEAPAATDEAAASA CCCCCCCCHHHHHHH	36.16	23140645
285	Phosphorylation	ATDEAAASAAPAASP CCHHHHHHHCCCCCC	21.90	23140645
291	Phosphorylation	ASAAPAASPEPQPEC HHHCCCCCCCCCCCC	31.72	23140645
299	Phosphorylation	PEPQPECSPEAPPAP CCCCCCCCCCCCCCC	24.90	23140645
307	Phosphorylation	PEAPPAPTAE----- CCCCCCCCCC-----	45.59	29899451

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
113	S	Phosphorylation	Kinase	MAPK-FAMILY	-	GPS
113	S	Phosphorylation	Kinase	MAPK1	P63085	GPS
113	S	Phosphorylation	Kinase	MAPK	-	Uniprot
152	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
152	S	Phosphorylation	Kinase	ROCK1	P70335	PSP
152	S	Phosphorylation	Kinase	PKN1	P70268	PhosphoELM
152	S	Phosphorylation	Kinase	PKN1	Q16512	PSP
152	S	Phosphorylation	Kinase	PRKACA	P05132	GPS
152	S	Phosphorylation	Kinase	PRKCZ	Q02956	GPS
152	S	Phosphorylation	Kinase	PRKCE	P16054	GPS
152	S	Phosphorylation	Kinase	PRKCD	P28867	GPS
152	S	Phosphorylation	Kinase	PRKCB1	P68404	GPS
152	S	Phosphorylation	Kinase	PKC	-	Uniprot
156	S	Phosphorylation	Kinase	PRKCE	P16054	GPS
156	S	Phosphorylation	Kinase	PRKCD	P28867	GPS
156	S	Phosphorylation	Kinase	PRKCZ	Q02956	GPS
156	S	Phosphorylation	Kinase	PKC	-	Uniprot
156	S	Phosphorylation	Kinase	PRKCB1	P68404	GPS
156	S	Phosphorylation	Kinase	PKN1	Q16512	PSP
156	S	Phosphorylation	Kinase	PRKACA	P05132	GPS
156	S	Phosphorylation	Kinase	PKN1	P70268	PhosphoELM
156	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
160	S	Phosphorylation	Kinase	ROCK-SUBFAMILY	-	GPS
160	S	Phosphorylation	Kinase	PRKACA	P05132	GPS
160	S	Phosphorylation	Kinase	ROCK_GROUP	-	PhosphoELM
163	S	Phosphorylation	Kinase	PKN1	Q16512	PSP
163	S	Phosphorylation	Kinase	PKC	-	Uniprot
163	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
163	S	Phosphorylation	Kinase	PKN1	P70268	PhosphoELM
163	S	Phosphorylation	Kinase	PRKCZ	Q02956	GPS
163	S	Phosphorylation	Kinase	PRKCE	P16054	GPS
163	S	Phosphorylation	Kinase	PRKCD	P28867	GPS
163	S	Phosphorylation	Kinase	PRKCB1	P68404	GPS
163	S	Phosphorylation	Kinase	PRKACA	P05132	GPS

Functions of PTM Sites

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

Protein-Protein Interaction

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

Drug and Disease Associations

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

Regulatory Network of MARCS_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry."; Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; Mol. Cell. Proteomics 8:904-912(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-143 AND SER-163, ANDMASS SPECTROMETRY.	19131326 [Abstract]
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163 AND SER-171, ANDMASS SPECTROMETRY.	19367708 [Abstract]
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140 AND THR-143, ANDMASS SPECTROMETRY.	17242355 [Abstract]
"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 SER-46; SER-113 AND SER-163,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-46; SER-113; SER-128;THR-143 AND SER-246, AND MASS SPECTROMETRY.	15345747 [Abstract]
"Identification of phosphoproteins and their phosphorylation sites inthe WEHI-231 B lymphoma cell line."; Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.; Mol. Cell. Proteomics 3:279-286(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138 AND THR-143, ANDMASS SPECTROMETRY.	14729942 [Abstract]
"The myristoylated alanine-rich C-kinase substrate (MARCKS) issequentially phosphorylated by conventional, novel and atypicalisotypes of protein kinase C."; Herget T., Oehrlein S.A., Pappin D.J.C., Rozengurt E., Parker P.J.; Eur. J. Biochem. 233:448-457(1995). Cited for: PHOSPHORYLATION AT SER-152; SER-156 AND SER-163.	7588787 [Abstract]
"p42 MAPK phosphorylates 80 kDa MARCKS at Ser-113."; Schoenwasser D.C., Palmer R.H., Herget T., Parker P.J.; FEBS Lett. 395:1-5(1996). Cited for: PROTEIN SEQUENCE OF 102-130, PHOSPHORYLATION AT SER-113, ANDMUTAGENESIS OF SER-113.	8849678 [Abstract]