MARCS_HUMAN - dbPTM
MARCS_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MARCS_HUMAN
UniProt AC P29966
Protein Name Myristoylated alanine-rich C-kinase substrate
Gene Name MARCKS
Organism Homo sapiens (Human).
Sequence Length 332
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 MGAQFSKTAAKGEAAAERPGEAAVASSPSKANGQENGHVKVNGDASPAAAESGAKEELQANGSAPAADKEEPAAAGSGAASPSAAEKGEPAAAAAPEAGASPVEKEAPAEGEAAEPGSPTAAEGEAASAASSTSSPKAEDGATPSPSNETPKKKKKRFSFKKSFKLSGFSFKKNKKEAGEGGEAEAPAAEGGKDEAAGGAAAAAAEAGAASGEQAAAPGEEAAAGEEGAAGGDPQEAKPQEAAVAPEKPPASDETKAAEEPSKVEEKKAEEAGASAAACEAPSAAGPGAPPEQEAAPAEEPAAAAASSACAAPSQEAQPECSPEAPPAEAAE
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
2N-myristoyl glycine------MGAQFSKTA
------CCCCCCHHH		28.25-
2Myristoylation------MGAQFSKTA
------CCCCCCHHH		28.2525255805
8PhosphorylationMGAQFSKTAAKGEAA
CCCCCCHHHHHCHHH		30.5623312004
11UbiquitinationQFSKTAAKGEAAAER
CCCHHHHHCHHHHCC		55.6121906983
11AcetylationQFSKTAAKGEAAAER
CCCHHHHHCHHHHCC		55.6126051181
26PhosphorylationPGEAAVASSPSKANG
CCCEEECCCCCCCCC		35.8629255136
27PhosphorylationGEAAVASSPSKANGQ
CCEEECCCCCCCCCC		24.3729255136
29PhosphorylationAAVASSPSKANGQEN
EEECCCCCCCCCCCC		46.4729255136
30UbiquitinationAVASSPSKANGQENG
EECCCCCCCCCCCCC		49.62-
46PhosphorylationVKVNGDASPAAAESG
EEECCCCCHHHHHHC		21.5819664994
52PhosphorylationASPAAAESGAKEELQ
CCHHHHHHCHHHHHH		39.0523403867
55UbiquitinationAAAESGAKEELQANG
HHHHHCHHHHHHHCC		56.0721906983
63PhosphorylationEELQANGSAPAADKE
HHHHHCCCCCCCCCC		30.7729255136
69AcetylationGSAPAADKEEPAAAG
CCCCCCCCCCCCCCC		60.2926051181
69UbiquitinationGSAPAADKEEPAAAG
CCCCCCCCCCCCCCC		60.296983
77PhosphorylationEEPAAAGSGAASPSA
CCCCCCCCCCCCHHH		22.1129255136
81PhosphorylationAAGSGAASPSAAEKG
CCCCCCCCHHHHHHC		20.8919664994
83PhosphorylationGSGAASPSAAEKGEP
CCCCCCHHHHHHCCC		37.3029255136
87UbiquitinationASPSAAEKGEPAAAA
CCHHHHHHCCCHHHH		64.9421906983
87AcetylationASPSAAEKGEPAAAA
CCHHHHHHCCCHHHH		64.9426051181
101PhosphorylationAAPEAGASPVEKEAP
HCCCCCCCCCCCCCC		28.6719664994
105UbiquitinationAGASPVEKEAPAEGE
CCCCCCCCCCCCCCC		60.4521906983
118PhosphorylationGEAAEPGSPTAAEGE
CCCCCCCCCCCHHHH		29.7729255136
120PhosphorylationAAEPGSPTAAEGEAA
CCCCCCCCCHHHHHH		39.9529255136
128PhosphorylationAAEGEAASAASSTSS
CHHHHHHHHCCCCCC		31.2629255136
131PhosphorylationGEAASAASSTSSPKA
HHHHHHCCCCCCCCC		33.5929255136
132PhosphorylationEAASAASSTSSPKAE
HHHHHCCCCCCCCCC		27.8129255136
133PhosphorylationAASAASSTSSPKAED
HHHHCCCCCCCCCCC		30.6329255136
134PhosphorylationASAASSTSSPKAEDG
HHHCCCCCCCCCCCC		46.7429255136
135PhosphorylationSAASSTSSPKAEDGA
HHCCCCCCCCCCCCC		30.4329255136
143PhosphorylationPKAEDGATPSPSNET
CCCCCCCCCCCCCCC		29.8129255136
145PhosphorylationAEDGATPSPSNETPK
CCCCCCCCCCCCCCC		36.2819664994
147PhosphorylationDGATPSPSNETPKKK
CCCCCCCCCCCCCCC		52.1929255136
150PhosphorylationTPSPSNETPKKKKKR
CCCCCCCCCCCCCCC		44.6619664994
152UbiquitinationSPSNETPKKKKKRFS
CCCCCCCCCCCCCCC		82.0121906983
153UbiquitinationPSNETPKKKKKRFSF
CCCCCCCCCCCCCCC		71.65-
159PhosphorylationKKKKKRFSFKKSFKL
CCCCCCCCCCHHCCC		39.9422167270
161MethylationKKKRFSFKKSFKLSG
CCCCCCCCHHCCCCC		46.43115972743
163PhosphorylationKRFSFKKSFKLSGFS
CCCCCCHHCCCCCCE		28.3622167270
165UbiquitinationFSFKKSFKLSGFSFK
CCCCHHCCCCCCEEC		49.1621906983
167PhosphorylationFKKSFKLSGFSFKKN
CCHHCCCCCCEECCC		38.0822167270
170PhosphorylationSFKLSGFSFKKNKKE
HCCCCCCEECCCCHH		39.4229255136
172UbiquitinationKLSGFSFKKNKKEAG
CCCCCEECCCCHHCC		54.9921890473
172AcetylationKLSGFSFKKNKKEAG
CCCCCEECCCCHHCC		54.9921339330
172SuccinylationKLSGFSFKKNKKEAG
CCCCCEECCCCHHCC		54.9923954790
172MethylationKLSGFSFKKNKKEAG
CCCCCEECCCCHHCC		54.997297845
176UbiquitinationFSFKKNKKEAGEGGE
CEECCCCHHCCCCCC		63.292190698
211PhosphorylationAAEAGAASGEQAAAP
HHHHHHHCCCCCCCC		42.1829507054
248MethylationEAAVAPEKPPASDET
CCCCCCCCCCCCHHH		56.07115972767
252PhosphorylationAPEKPPASDETKAAE
CCCCCCCCHHHHHCC		41.5829507054
255PhosphorylationKPPASDETKAAEEPS
CCCCCHHHHHCCCCH		30.8523312004
262PhosphorylationTKAAEEPSKVEEKKA
HHHCCCCHHHHHHHH		53.2515345747
263AcetylationKAAEEPSKVEEKKAE
HHCCCCHHHHHHHHH		65.4626051181
263UbiquitinationKAAEEPSKVEEKKAE
HHCCCCHHHHHHHHH		65.46-
267UbiquitinationEPSKVEEKKAEEAGA
CCHHHHHHHHHHHCC		43.72-
275PhosphorylationKAEEAGASAAACEAP
HHHHHCCCHHHHHCC		19.9521601212
308PhosphorylationPAAAAASSACAAPSQ
HHHHHHHHHHCCCCH		23.7321601212
314PhosphorylationSSACAAPSQEAQPEC
HHHHCCCCHHCCCCC		35.6125255805
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
27SPhosphorylationKinaseCDK2P24941
GPS
46SPhosphorylationKinaseMAPK9P45984
GPS
46SPhosphorylationKinaseMAPK8P45983
GPS
46SPhosphorylationKinaseMAPK3P27361
GPS
46SPhosphorylationKinaseMAPK1P28482
GPS
150TPhosphorylationKinaseCDK2P24941
GPS
159SPhosphorylationKinasePKC_GROUP-PhosphoELM
159SPhosphorylationKinasePKC-Uniprot
159SPhosphorylationKinasePRKCAP17252
GPS
159SPhosphorylationKinasePKCAP04409
PSP
159SPhosphorylationKinasePRKACAP00517
GPS
159SPhosphorylationKinaseROCK1Q13464
PSP
159SPhosphorylationKinasePKC-FAMILY-GPS
163SPhosphorylationKinasePRKCAP17252
GPS
163SPhosphorylationKinasePKC_GROUP-PhosphoELM
163SPhosphorylationKinasePKC-Uniprot
163SPhosphorylationKinasePKC-FAMILY-GPS
163SPhosphorylationKinasePKCAP05696
PSP
167SPhosphorylationKinasePKC-FAMILY-GPS
167SPhosphorylationKinasePKCAP05696
PSP
167SPhosphorylationKinasePKC-Uniprot
167SPhosphorylationKinasePKC_GROUP-PhosphoELM
167SPhosphorylationKinasePRKCAP17252
GPS
170SPhosphorylationKinasePKC-FAMILY-GPS
170SPhosphorylationKinasePKC-Uniprot
170SPhosphorylationKinasePKC_GROUP-PhosphoELM
170SPhosphorylationKinasePRKCAP17252
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MARCS_HUMAN !!
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_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TOB1_HUMANTOB1physical
11327693
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 MARCS_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-26; SER-27; SER-29;SER-46; SER-63; SER-77; SER-81; SER-83; SER-101; SER-118; THR-120;SER-131; SER-132; SER-134; THR-143; SER-145; SER-147; THR-150; SER-167AND SER-170, AND MASS 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-27; SER-46; SER-77;SER-81; SER-101; SER-118; THR-143; SER-145; SER-147; THR-150; SER-163;SER-167 AND SER-170, AND MASS SPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-159 AND SER-170,AND MASS SPECTROMETRY.
"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-26; SER-27; SER-29;SER-145; THR-150; SER-163; SER-167 AND SER-170, AND MASS SPECTROMETRY.
"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-27 AND SER-167, 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-46; SER-77; SER-81;SER-101; THR-143; SER-145; SER-159; SER-163; SER-167 AND SER-170, ANDMASS SPECTROMETRY.
"PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156and serine 163.";
Palmer R.H., Schonwasser D.C., Rahman D., Pappin D.J., Herget T.,Parker P.J.;
FEBS Lett. 378:281-285(1996).
Cited for: PHOSPHORYLATION AT SER-159; SER-163 AND SER-170.

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