dbPTM

MRP_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MRP_MOUSE
UniProt AC	P28667
Protein Name	MARCKS-related protein
Gene Name	Marcksl1
Organism	Mus musculus (Mouse).
Sequence Length	200
Subcellular Localization	Cytoplasm. Cell membrane Lipid-anchor . Associates with the membrane via the insertion of the N-terminal N-myristoyl chain and the partial insertion of the effector domain. Association of the effector domain with membranes may be regulated by Ca(2+
Protein Description	Controls cell movement by regulating actin cytoskeleton homeostasis and filopodium and lamellipodium formation. When unphosphorylated, induces cell migration. When phosphorylated by MAPK8, induces actin bundles formation and stabilization, thereby reducing actin plasticity, hence restricting cell movement, including neuronal migration. May also affect cancer cell migration. May be involved in coupling the protein kinase C and calmodulin signal transduction systems..
Protein Sequence	MGSQSSKAPRGDVTAEEAAGASPAKANGQENGHVRSNGDLTPKGEGESPPVNGTDEAAGATGDAIEPAPPSQEAEAKGEVAPKETPKKKKKFSFKKPFKLSGLSFKRNRKEGGGDSSASSPTEEEQEQGEMSACSDEGTAQEGKAAATPESQEPQAKGAEASAASKEGDTEEEAGPQAAEPSTPSGPESGPTPASAEQNE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	N-myristoyl glycine	------MGSQSSKAP ------CCCCCCCCC	34.10	-
2	Myristoylation	------MGSQSSKAP ------CCCCCCCCC	34.10	1618855
14	Phosphorylation	KAPRGDVTAEEAAGA CCCCCCCCHHHHCCC	32.84	24925903
22	Phosphorylation	AEEAAGASPAKANGQ HHHHCCCCCCHHCCC	25.19	27087446
25	Ubiquitination	AAGASPAKANGQENG HCCCCCCHHCCCCCC	45.85	-
36	Phosphorylation	QENGHVRSNGDLTPK CCCCCCCCCCCCCCC	44.04	27087446
41	Phosphorylation	VRSNGDLTPKGEGES CCCCCCCCCCCCCCC	27.91	21082442
48	Phosphorylation	TPKGEGESPPVNGTD CCCCCCCCCCCCCCC	45.41	22942356
54	Phosphorylation	ESPPVNGTDEAAGAT CCCCCCCCCHHCCCC	26.01	21183079
61	Phosphorylation	TDEAAGATGDAIEPA CCHHCCCCCCCCCCC	34.38	25293948
71	Phosphorylation	AIEPAPPSQEAEAKG CCCCCCCCHHHHHCC	39.32	21082442
85	Phosphorylation	GEVAPKETPKKKKKF CCCCCCCCCCCCCCC	46.68	25521595
93	Phosphorylation	PKKKKKFSFKKPFKL CCCCCCCCCCCCCCC	45.06	22942356
101	Phosphorylation	FKKPFKLSGLSFKRN CCCCCCCCCCEEECC	37.97	26824392
104	Phosphorylation	PFKLSGLSFKRNRKE CCCCCCCEEECCCCC	32.04	27087446
106	Acetylation	KLSGLSFKRNRKEGG CCCCCEEECCCCCCC	45.44	22826441
110	Ubiquitination	LSFKRNRKEGGGDSS CEEECCCCCCCCCCC	65.35	-
116	Phosphorylation	RKEGGGDSSASSPTE CCCCCCCCCCCCCCH	30.95	22942356
117	Phosphorylation	KEGGGDSSASSPTEE CCCCCCCCCCCCCHH	36.59	27087446
119	Phosphorylation	GGGDSSASSPTEEEQ CCCCCCCCCCCHHHH	38.51	27087446
120	Phosphorylation	GGDSSASSPTEEEQE CCCCCCCCCCHHHHH	35.24	25521595
122	Phosphorylation	DSSASSPTEEEQEQG CCCCCCCCHHHHHHC	58.96	25521595
132	Phosphorylation	EQEQGEMSACSDEGT HHHHCCCCCCCCCCC	23.09	25521595
135	Phosphorylation	QGEMSACSDEGTAQE HCCCCCCCCCCCHHC	38.11	25521595
139	Phosphorylation	SACSDEGTAQEGKAA CCCCCCCCHHCCCCC	24.10	25619855
148	Phosphorylation	QEGKAAATPESQEPQ HCCCCCCCCCCCCCH	23.90	25521595
151	Phosphorylation	KAAATPESQEPQAKG CCCCCCCCCCCHHHC	40.84	25521595
157	Ubiquitination	ESQEPQAKGAEASAA CCCCCHHHCHHHHHH	54.10	-
162	Phosphorylation	QAKGAEASAASKEGD HHHCHHHHHHHHCCC	18.84	15345747
165	Phosphorylation	GAEASAASKEGDTEE CHHHHHHHHCCCCCC	30.84	27087446
170	Phosphorylation	AASKEGDTEEEAGPQ HHHHCCCCCCCCCCC	57.03	24925903
182	Phosphorylation	GPQAAEPSTPSGPES CCCCCCCCCCCCCCC	44.44	24925903
183	Phosphorylation	PQAAEPSTPSGPESG CCCCCCCCCCCCCCC	31.99	25521595
185	Phosphorylation	AAEPSTPSGPESGPT CCCCCCCCCCCCCCC	68.05	25521595
189	Phosphorylation	STPSGPESGPTPASA CCCCCCCCCCCCCCH	53.88	25521595
192	Phosphorylation	SGPESGPTPASAEQN CCCCCCCCCCCHHCC	34.70	24925903
195	Phosphorylation	ESGPTPASAEQNE-- CCCCCCCCHHCCC--	33.28	21149613

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
93	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
93	S	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM
93	S	Phosphorylation	Kinase	PKC	-	Uniprot
93	S	Phosphorylation	Kinase	PKCG	P05129	PSP
101	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
101	S	Phosphorylation	Kinase	PKC	-	Uniprot
101	S	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM
104	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
104	S	Phosphorylation	Kinase	PKC	-	Uniprot
104	S	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM
104	S	Phosphorylation	Kinase	PKCG	P05129	PSP
120	S	Phosphorylation	Kinase	MAPK8	P45983	GPS
120	S	Phosphorylation	Kinase	JNK1	Q91Y86	PSP
148	T	Phosphorylation	Kinase	JNK1	Q91Y86	PSP
148	T	Phosphorylation	Kinase	MAPK8	P45983	GPS
183	T	Phosphorylation	Kinase	JNK1	Q91Y86	PSP
183	T	Phosphorylation	Kinase	MAPK8	P45983	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
120	S	Phosphorylation	22751924
Phosphorylation at Ser-120 and Thr-183 is non-redundantly catalyzed by MAPK8 in vivo.
148	T	Phosphorylation	22751924
Phosphorylation at Thr-148 is preferentially catalyzed by MAPK8 in vivo, but this modification can also be catalyzed by other kinases in the absence of MAPK8.
183	T	Phosphorylation	22751924
Phosphorylation at Ser-120 and Thr-183 is non-redundantly catalyzed by MAPK8 in vivo.

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 MRP_MOUSE !!

Protein-Protein Interaction

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

Drug and Disease Associations

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

Regulatory Network of MRP_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"The phagosomal proteome in interferon-gamma-activated macrophages."; Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.; Immunity 30:143-154(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-36; THR-85 ANDSER-104, AND MASS SPECTROMETRY.	19144319 [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-22; SER-48; SER-71;SER-120; SER-135; THR-148; SER-162; SER-165; THR-170; THR-183; SER-185AND THR-192, 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-22, AND MASSSPECTROMETRY.	14729942 [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 THR-85, AND MASSSPECTROMETRY.	19367708 [Abstract]

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