CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008099
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 MARCKS-related protein 
Protein Synonyms/Alias
 MARCKS-like protein 1; Macrophage myristoylated alanine-rich C kinase substrate; Mac-MARCKS; MacMARCKS 
Gene Name
 MARCKSL1 
Gene Synonyms/Alias
 MLP; MRP 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
25AAGASPAKANGQENGubiquitination[1, 2, 3]
35GQENGHVKSNGDLSPubiquitination[2]
43SNGDLSPKGEGESPPubiquitination[1, 4]
77PSQGAEAKGEVPPKEubiquitination[1]
95KKKKFSFKKPFKLSGubiquitination[3]
99FSFKKPFKLSGLSFKubiquitination[5, 6, 7]
106KLSGLSFKRNRKEGGacetylation[8]
106KLSGLSFKRNRKEGGubiquitination[2, 5, 6, 7]
110LSFKRNRKEGGGDSSubiquitination[1, 3]
144EGTAQEGKAAATPESphosphoglycerylation[9]
144EGTAQEGKAAATPESubiquitination[1]
157ESQEPQAKGAEASAAubiquitination[1, 4]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [4] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [5] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [6] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [7] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [8] Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome.
 Morselli E, Mariño G, Bennetzen MV, Eisenberg T, Megalou E, Schroeder S, Cabrera S, Bénit P, Rustin P, Criollo A, Kepp O, Galluzzi L, Shen S, Malik SA, Maiuri MC, Horio Y, López-Otín C, Andersen JS, Tavernarakis N, Madeo F, Kroemer G.
 J Cell Biol. 2011 Feb 21;192(4):615-29. [PMID: 21339330]
 [9] Functional lysine modification by an intrinsically reactive primary glycolytic metabolite.
 Moellering RE, Cravatt BF.
 Science. 2013 Aug 2;341(6145):549-53. [PMID: 23908237
Functional 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). 
Sequence Annotation
 REGION 87 110 Effector domain involved in lipid-binding
 REGION 87 100 Calmodulin-binding (PSD).
 MOD_RES 22 22 Phosphoserine.
 MOD_RES 36 36 Phosphoserine.
 MOD_RES 41 41 Phosphoserine.
 MOD_RES 48 48 Phosphoserine (By similarity).
 MOD_RES 71 71 Phosphoserine.
 MOD_RES 85 85 Phosphothreonine (By similarity).
 MOD_RES 93 93 Phosphoserine.
 MOD_RES 101 101 Phosphoserine.
 MOD_RES 104 104 Phosphoserine.
 MOD_RES 120 120 Phosphoserine (By similarity).
 MOD_RES 135 135 Phosphoserine (By similarity).
 MOD_RES 148 148 Phosphothreonine.
 MOD_RES 151 151 Phosphoserine.
 MOD_RES 162 162 Phosphoserine (By similarity).
 MOD_RES 165 165 Phosphoserine (By similarity).
 MOD_RES 178 178 Phosphothreonine.
 MOD_RES 180 180 Phosphoserine (By similarity).
 MOD_RES 187 187 Phosphothreonine (By similarity).
 LIPID 2 2 N-myristoyl glycine (By similarity).  
Keyword
 Actin-binding; Calmodulin-binding; Cell membrane; Complete proteome; Cytoplasm; Lipoprotein; Membrane; Myristate; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 195 AA 
Protein Sequence
MGSQSSKAPR GDVTAEEAAG ASPAKANGQE NGHVKSNGDL SPKGEGESPP VNGTDEAAGA 60
TGDAIEPAPP SQGAEAKGEV PPKETPKKKK KFSFKKPFKL SGLSFKRNRK EGGGDSSASS 120
PTEEEQEQGE IGACSDEGTA QEGKAAATPE SQEPQAKGAE ASAASEEEAG PQATEPSTPS 180
GPESGPTPAS AEQNE 195 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005886; C:plasma membrane; IDA:LIFEdb.
 GO:0008284; P:positive regulation of cell proliferation; IEA:Compara. 
Interpro
 IPR002101; MARCKS. 
Pfam
 PF02063; MARCKS 
SMART
  
PROSITE
 PS00826; MARCKS_1
 PS00827; MARCKS_2 
PRINTS
 PR00963; MARCKS.