MARCS_HUMAN
ID MARCS_HUMAN Reviewed; 332 AA.
AC P29966; E1P560; Q2LA83; Q5TDB7;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Myristoylated alanine-rich C-kinase substrate;
DE Short=MARCKS;
DE AltName: Full=Protein kinase C substrate, 80 kDa protein, light chain;
DE Short=80K-L protein;
DE Short=PKCSL;
GN Name=MARCKS; Synonyms=MACS, PRKCSL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34.
RX PubMed=1860846; DOI=10.1016/s0021-9258(18)98698-9;
RA Harlan D.M., Graff J.M., Stumpo D.J., Eddy R.L. Jr., Shows T.B.,
RA Boyle J.M., Blackshear P.J.;
RT "The human myristoylated alanine-rich C kinase substrate (MARCKS) gene
RT (MACS). Analysis of its gene product, promoter, and chromosomal
RT localization.";
RL J. Biol. Chem. 266:14399-14405(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1427823; DOI=10.1016/s0888-7543(05)80301-5;
RA Sakai K., Hirai M., Kudoh J., Minoshima S., Shimizu N.;
RT "Molecular cloning and chromosomal mapping of a cDNA encoding human 80K-L
RT protein: major substrate for protein kinase C.";
RL Genomics 14:175-178(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LEU-250 AND VAL-274.
RG NIEHS SNPs program;
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 189-322.
RX PubMed=1396720; DOI=10.1111/j.1432-1033.1992.tb17255.x;
RA Herget T., Brooks S.F., Broad S., Rozengurt E.;
RT "Relationship between the major protein kinase C substrates acidic 80-kDa
RT protein-kinase-C substrate (80K) and myristoylated alanine-rich C-kinase
RT substrate (MARCKS). Members of a gene family or equivalent genes in
RT different species.";
RL Eur. J. Biochem. 209:7-14(1992).
RN [8]
RP PHOSPHORYLATION AT SER-159; SER-163 AND SER-170.
RX PubMed=8557118; DOI=10.1016/0014-5793(95)01454-3;
RA Palmer R.H., Schonwasser D.C., Rahman D., Pappin D.J., Herget T.,
RA Parker P.J.;
RT "PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and
RT serine 163.";
RL FEBS Lett. 378:281-285(1996).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46; SER-77; SER-101 AND
RP SER-170, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-46; SER-77; SER-81;
RP SER-118; THR-143; SER-145 AND THR-150, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-46; SER-101; THR-150;
RP SER-163; SER-167 AND SER-170, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46; SER-63; SER-77; SER-81;
RP SER-101; THR-150; SER-163 AND SER-170, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-101; THR-150 AND
RP SER-170, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; SER-29; SER-101; SER-135;
RP SER-145; SER-147; SER-170 AND SER-314, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
RP MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=25255805; DOI=10.1038/ncomms5919;
RA Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U., Wright M.H.,
RA Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.;
RT "Global profiling of co- and post-translationally N-myristoylated proteomes
RT in human cells.";
RL Nat. Commun. 5:4919-4919(2014).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: MARCKS is the most prominent cellular substrate for protein
CC kinase C. This protein binds calmodulin, actin, and synapsin. MARCKS is
CC a filamentous (F) actin cross-linking protein.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. Membrane
CC {ECO:0000305}; Lipid-anchor {ECO:0000305}.
CC -!- PTM: Phosphorylation by PKC displaces MARCKS from the membrane. It also
CC inhibits the F-actin cross-linking activity.
CC {ECO:0000269|PubMed:8557118}.
CC -!- SIMILARITY: Belongs to the MARCKS family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/marcks/";
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/MARCKSID50926ch6q21.html";
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DR EMBL; M68956; AAA59555.1; -; mRNA.
DR EMBL; M68955; AAA59554.1; -; Genomic_DNA.
DR EMBL; D10522; BAA01392.1; -; mRNA.
DR EMBL; DQ341274; ABC67467.1; -; Genomic_DNA.
DR EMBL; AL132660; CAI19942.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48258.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48259.1; -; Genomic_DNA.
DR EMBL; BC089040; AAH89040.1; -; mRNA.
DR CCDS; CCDS5101.1; -.
DR PIR; A38873; A38873.
DR RefSeq; NP_002347.5; NM_002356.6.
DR AlphaFoldDB; P29966; -.
DR SMR; P29966; -.
DR BioGRID; 110257; 569.
DR ELM; P29966; -.
DR IntAct; P29966; 41.
DR MINT; P29966; -.
DR STRING; 9606.ENSP00000478061; -.
DR GlyGen; P29966; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P29966; -.
DR PhosphoSitePlus; P29966; -.
DR SwissPalm; P29966; -.
DR BioMuta; MARCKS; -.
DR DMDM; 76803798; -.
DR CPTAC; CPTAC-976; -.
DR EPD; P29966; -.
DR jPOST; P29966; -.
DR MassIVE; P29966; -.
DR MaxQB; P29966; -.
DR PaxDb; P29966; -.
DR PeptideAtlas; P29966; -.
DR PRIDE; P29966; -.
DR ProteomicsDB; 54612; -.
DR TopDownProteomics; P29966; -.
DR Antibodypedia; 72851; 915 antibodies from 43 providers.
DR DNASU; 4082; -.
DR Ensembl; ENST00000612661.2; ENSP00000478061.1; ENSG00000277443.3.
DR GeneID; 4082; -.
DR KEGG; hsa:4082; -.
DR MANE-Select; ENST00000612661.2; ENSP00000478061.1; NM_002356.7; NP_002347.5.
DR UCSC; uc032xir.2; human.
DR CTD; 4082; -.
DR DisGeNET; 4082; -.
DR GeneCards; MARCKS; -.
DR HGNC; HGNC:6759; MARCKS.
DR HPA; ENSG00000277443; Low tissue specificity.
DR MIM; 177061; gene.
DR neXtProt; NX_P29966; -.
DR OpenTargets; ENSG00000277443; -.
DR PharmGKB; PA30637; -.
DR VEuPathDB; HostDB:ENSG00000277443; -.
DR eggNOG; ENOG502RB4V; Eukaryota.
DR GeneTree; ENSGT00730000111419; -.
DR HOGENOM; CLU_073091_0_0_1; -.
DR InParanoid; P29966; -.
DR OMA; PANEKEX; -.
DR OrthoDB; 1636177at2759; -.
DR TreeFam; TF332815; -.
DR PathwayCommons; P29966; -.
DR Reactome; R-HSA-399997; Acetylcholine regulates insulin secretion.
DR SignaLink; P29966; -.
DR SIGNOR; P29966; -.
DR BioGRID-ORCS; 4082; 23 hits in 1085 CRISPR screens.
DR ChiTaRS; MARCKS; human.
DR GeneWiki; MARCKS; -.
DR GenomeRNAi; 4082; -.
DR Pharos; P29966; Tbio.
DR PRO; PR:P29966; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P29966; protein.
DR Bgee; ENSG00000277443; Expressed in ventricular zone and 207 other tissues.
DR Genevisible; P29966; HS.
DR GO; GO:0015629; C:actin cytoskeleton; TAS:ProtInc.
DR GO; GO:0032432; C:actin filament bundle; IBA:GO_Central.
DR GO; GO:0005938; C:cell cortex; IEA:Ensembl.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0042585; C:germinal vesicle; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005516; F:calmodulin binding; TAS:ProtInc.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0005080; F:protein kinase C binding; IEA:Ensembl.
DR GO; GO:0051764; P:actin crosslink formation; IEA:Ensembl.
DR GO; GO:0051017; P:actin filament bundle assembly; IEA:Ensembl.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:Ensembl.
DR GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
DR GO; GO:0007005; P:mitochondrion organization; IEA:Ensembl.
DR GO; GO:0021915; P:neural tube development; IEA:Ensembl.
DR GO; GO:0022008; P:neurogenesis; IEA:Ensembl.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IEA:Ensembl.
DR InterPro; IPR002101; MARCKS.
DR PANTHER; PTHR14353; PTHR14353; 1.
DR Pfam; PF02063; MARCKS; 1.
DR PRINTS; PR00963; MARCKS.
DR PROSITE; PS00826; MARCKS_1; 1.
DR PROSITE; PS00827; MARCKS_2; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Calmodulin-binding; Cytoplasm; Cytoskeleton; Lipoprotein;
KW Membrane; Myristate; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:25255805"
FT CHAIN 2..332
FT /note="Myristoylated alanine-rich C-kinase substrate"
FT /id="PRO_0000157148"
FT REGION 1..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..176
FT /note="Calmodulin-binding (PSD)"
FT COMPBIAS 125..148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..273
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 128
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30009"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 143
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 150
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 159
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000269|PubMed:8557118"
FT MOD_RES 163
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000269|PubMed:8557118,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 167
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0007744|PubMed:17924679,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 170
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000269|PubMed:8557118,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 262
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26645"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:25255805"
FT VARIANT 250
FT /note="P -> L (in dbSNP:rs45593337)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_025825"
FT VARIANT 274
FT /note="A -> V (in dbSNP:rs3734458)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_025826"
FT CONFLICT 84
FT /note="A -> S (in Ref. 2; BAA01392)"
FT /evidence="ECO:0000305"
FT CONFLICT 119
FT /note="P -> A (in Ref. 2; BAA01392)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="G -> R (in Ref. 7)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="P -> S (in Ref. 1; AAA59555)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="Q -> E (in Ref. 7)"
FT /evidence="ECO:0000305"
FT CONFLICT 287..308
FT /note="PGAPPEQEAAPAEEPAAAAASS -> LVCPRRGGSPRGGARGRRSLNQ (in
FT Ref. 1; AAA59555)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 332 AA; 31555 MW; 0AB247801EF8FCBF CRC64;
MGAQFSKTAA KGEAAAERPG EAAVASSPSK ANGQENGHVK VNGDASPAAA ESGAKEELQA
NGSAPAADKE EPAAAGSGAA SPSAAEKGEP AAAAAPEAGA SPVEKEAPAE GEAAEPGSPT
AAEGEAASAA SSTSSPKAED GATPSPSNET PKKKKKRFSF KKSFKLSGFS FKKNKKEAGE
GGEAEAPAAE GGKDEAAGGA AAAAAEAGAA SGEQAAAPGE EAAAGEEGAA GGDPQEAKPQ
EAAVAPEKPP ASDETKAAEE PSKVEEKKAE EAGASAAACE APSAAGPGAP PEQEAAPAEE
PAAAAASSAC AAPSQEAQPE CSPEAPPAEA AE
