MRP_HUMAN - dbPTM
MRP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MRP_HUMAN
UniProt AC P49006
Protein Name MARCKS-related protein
Gene Name MARCKSL1
Organism Homo sapiens (Human).
Sequence Length 195
Subcellular Localization Cytoplasm. Cell membrane. 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 regulate
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 (By similarity)..
Protein Sequence MGSQSSKAPRGDVTAEEAAGASPAKANGQENGHVKSNGDLSPKGEGESPPVNGTDEAAGATGDAIEPAPPSQGAEAKGEVPPKETPKKKKKFSFKKPFKLSGLSFKRNRKEGGGDSSASSPTEEEQEQGEIGACSDEGTAQEGKAAATPESQEPQAKGAEASAASEEEAGPQATEPSTPSGPESGPTPASAEQNE
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Myristoylation------MGSQSSKAP
------CCCCCCCCC		34.1025255805
7Acetylation-MGSQSSKAPRGDVT
-CCCCCCCCCCCCCC		68.6025953088
14PhosphorylationKAPRGDVTAEEAAGA
CCCCCCCCHHHHCCC		32.8429255136
22PhosphorylationAEEAAGASPAKANGQ
HHHHCCCCCCHHCCC		25.1919664994
25UbiquitinationAAGASPAKANGQENG
HCCCCCCHHCCCCCC		45.8521906983
35UbiquitinationGQENGHVKSNGDLSP
CCCCCCCCCCCCCCC		32.31-
36PhosphorylationQENGHVKSNGDLSPK
CCCCCCCCCCCCCCC		44.9829255136
41PhosphorylationVKSNGDLSPKGEGES
CCCCCCCCCCCCCCC		29.3429255136
43UbiquitinationSNGDLSPKGEGESPP
CCCCCCCCCCCCCCC		67.2421906983
48PhosphorylationSPKGEGESPPVNGTD
CCCCCCCCCCCCCCC		45.4119664994
54PhosphorylationESPPVNGTDEAAGAT
CCCCCCCCCHHCCCC		26.0119664994
61PhosphorylationTDEAAGATGDAIEPA
CCHHCCCCCCCCCCC		34.3828348404
71PhosphorylationAIEPAPPSQGAEAKG
CCCCCCCCCCCCCCC		39.9423401153
77UbiquitinationPSQGAEAKGEVPPKE
CCCCCCCCCCCCCCC		47.3032142685
83UbiquitinationAKGEVPPKETPKKKK
CCCCCCCCCCCCCCC		69.06-
85PhosphorylationGEVPPKETPKKKKKF
CCCCCCCCCCCCCCC		46.6829255136
88UbiquitinationPPKETPKKKKKFSFK
CCCCCCCCCCCCCCC		71.65-
93PhosphorylationPKKKKKFSFKKPFKL
CCCCCCCCCCCCCCC		45.0623401153
95UbiquitinationKKKKFSFKKPFKLSG
CCCCCCCCCCCCCCC		59.3423000965
96UbiquitinationKKKFSFKKPFKLSGL
CCCCCCCCCCCCCCC		54.3923000965
99UbiquitinationFSFKKPFKLSGLSFK
CCCCCCCCCCCCEEE		50.7123000965
101PhosphorylationFKKPFKLSGLSFKRN
CCCCCCCCCCEEECC		37.9723927012
104PhosphorylationPFKLSGLSFKRNRKE
CCCCCCCEEECCCCC		32.0429255136
106AcetylationKLSGLSFKRNRKEGG
CCCCCEEECCCCCCC		45.4423954790
106UbiquitinationKLSGLSFKRNRKEGG
CCCCCEEECCCCCCC		45.4423000965
110UbiquitinationLSFKRNRKEGGGDSS
CEEECCCCCCCCCCC		65.3523000965
116PhosphorylationRKEGGGDSSASSPTE
CCCCCCCCCCCCCCH		30.9530278072
117PhosphorylationKEGGGDSSASSPTEE
CCCCCCCCCCCCCHH		36.5930278072
119PhosphorylationGGGDSSASSPTEEEQ
CCCCCCCCCCCHHHH		38.5130278072
120PhosphorylationGGDSSASSPTEEEQE
CCCCCCCCCCHHHHH		35.2430278072
122PhosphorylationDSSASSPTEEEQEQG
CCCCCCCCHHHHHCC		58.9630278072
134GlutathionylationEQGEIGACSDEGTAQ
HCCCCCCCCCCCCHH		4.4322555962
135PhosphorylationQGEIGACSDEGTAQE
CCCCCCCCCCCCHHC		37.8622617229
139PhosphorylationGACSDEGTAQEGKAA
CCCCCCCCHHCCCCC		24.1023403867
144UbiquitinationEGTAQEGKAAATPES
CCCHHCCCCCCCCCC		33.8121906983
144PhosphoglycerylationEGTAQEGKAAATPES
CCCHHCCCCCCCCCC		33.81-
148O-linked_GlycosylationQEGKAAATPESQEPQ
HCCCCCCCCCCCCCH		23.90OGP
148PhosphorylationQEGKAAATPESQEPQ
HCCCCCCCCCCCCCH		23.9029255136
151PhosphorylationKAAATPESQEPQAKG
CCCCCCCCCCCHHHC		40.8430266825
157UbiquitinationESQEPQAKGAEASAA
CCCCCHHHCHHHHHH		54.1023503661
162PhosphorylationQAKGAEASAASEEEA
HHHCHHHHHHCHHHH		18.8430266825
165PhosphorylationGAEASAASEEEAGPQ
CHHHHHHCHHHHCCC		45.3030266825
174PhosphorylationEEAGPQATEPSTPSG
HHHCCCCCCCCCCCC		43.0930278072
177PhosphorylationGPQATEPSTPSGPES
CCCCCCCCCCCCCCC		46.8730278072
178PhosphorylationPQATEPSTPSGPESG
CCCCCCCCCCCCCCC		31.9927273156
180PhosphorylationATEPSTPSGPESGPT
CCCCCCCCCCCCCCC		68.0530278072
184PhosphorylationSTPSGPESGPTPASA
CCCCCCCCCCCCCCH		53.8830278072
187PhosphorylationSGPESGPTPASAEQN
CCCCCCCCCCCHHCC		34.7030278072
190PhosphorylationESGPTPASAEQNE--
CCCCCCCCHHCCC--		33.2828287266
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
71SPhosphorylationKinaseATRQ13535
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
120SPhosphorylation

-
148TPhosphorylation

-
178TPhosphorylation

-
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_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DCTN2_HUMANDCTN2physical
10827182
RM16_HUMANMRPL16physical
22939629
VPP1_HUMANATP6V0A1physical
22939629
RALB_HUMANRALBphysical
22939629
ZBT43_HUMANZBTB43physical
22939629
NDUB5_HUMANNDUFB5physical
22939629
RM46_HUMANMRPL46physical
22939629
RALA_HUMANRALAphysical
22939629
MRM3_HUMANRNMTL1physical
22939629
RM30_HUMANMRPL30physical
22939629
PTN1_HUMANPTPN1physical
22939629
VATA_HUMANATP6V1Aphysical
22939629
PCDH7_HUMANPCDH7physical
22939629
RM22_HUMANMRPL22physical
22939629
BRCA1_HUMANBRCA1physical
25184681
SNX21_HUMANSNX21physical
28514442
RET4_HUMANRBP4physical
28514442
NMT2_HUMANNMT2physical
28514442
RMI1_HUMANRMI1physical
28514442
BCCIP_HUMANBCCIPphysical
28514442
NMT1_HUMANNMT1physical
28514442
P4R3A_HUMANSMEK1physical
28514442
TOP3A_HUMANTOP3Aphysical
28514442
SCRN2_HUMANSCRN2physical
28514442
VATD_HUMANATP6V1Dphysical
28514442
AT11C_HUMANATP11Cphysical
28514442
KBTB7_HUMANKBTBD7physical
28514442
VPP2_HUMANATP6V0A2physical
28514442
PP4R2_HUMANPPP4R2physical
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 MRP_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14; SER-22; SER-41 ANDSER-71, AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-48; SER-101;SER-104; SER-117; SER-119; SER-120; THR-122; THR-148; SER-151;SER-162; SER-165; THR-174; SER-177; THR-178; SER-180 AND SER-184, ANDMASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; THR-85; SER-93;SER-101; SER-104; THR-148 AND THR-178, AND MASS SPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71, AND MASSSPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; THR-85; SER-101;SER-104; SER-116; THR-122; SER-135; THR-174 AND THR-178, AND MASSSPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, AND MASSSPECTROMETRY.
"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-22, AND MASSSPECTROMETRY.

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