P29966 (MARCS_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Myristoylated alanine-rich C-kinase substrate
Short name=MARCKS

Alternative name(s):
Protein kinase C substrate, 80 kDa protein, light chain
Short name=80K-L protein
Short name=PKCSL

Gene names

Name:	MARCKS
Synonyms:	MACS, PRKCSL

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	332 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Subcellular location	Cytoplasm › cytoskeleton Probable. Membrane; Lipid-anchor By similarity.
Post-translational modification	Phosphorylation by PKC displaces MARCKS from the membrane. It also inhibits the F-actin cross-linking activity.
Sequence similarities	Belongs to the MARCKS family.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton Membrane
Coding sequence diversity	Polymorphism
Ligand	Actin-binding Calmodulin-binding
PTM	Lipoprotein Myristate Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	energy reserve metabolic process Traceable author statement. Source: Reactome regulation of insulin secretion Traceable author statement. Source: Reactome
Cellular component	actin cytoskeleton Traceable author statement. Source: ProtInc plasma membrane Traceable author statement. Source: Reactome
Molecular function	actin filament binding Traceable author statement. Source: ProtInc calmodulin binding Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 332	331	Myristoylated alanine-rich C-kinase substrate		PRO_0000157148
Regions
	Region	152 – 176	25	Calmodulin-binding (PSD)
Amino acid modifications
	Modified residue	26	1	Phosphoserine Ref.11 Ref.14
	Modified residue	27	1	Phosphoserine Ref.10 Ref.11 Ref.12 Ref.13 Ref.14
	Modified residue	29	1	Phosphoserine Ref.11 Ref.14
	Modified residue	46	1	Phosphoserine Ref.9 Ref.13 Ref.14
	Modified residue	63	1	Phosphoserine Ref.14
	Modified residue	77	1	Phosphoserine Ref.9 Ref.13 Ref.14
	Modified residue	81	1	Phosphoserine Ref.9 Ref.13 Ref.14
	Modified residue	83	1	Phosphoserine Ref.14
	Modified residue	101	1	Phosphoserine Ref.9 Ref.13 Ref.14
	Modified residue	118	1	Phosphoserine Ref.13 Ref.14
	Modified residue	120	1	Phosphothreonine Ref.14
	Modified residue	131	1	Phosphoserine Ref.14
	Modified residue	132	1	Phosphoserine Ref.14
	Modified residue	134	1	Phosphoserine Ref.14
	Modified residue	135	1	Phosphoserine By similarity
	Modified residue	143	1	Phosphothreonine Ref.9 Ref.13 Ref.14
	Modified residue	145	1	Phosphoserine Ref.9 Ref.11 Ref.13 Ref.14
	Modified residue	147	1	Phosphoserine Ref.13 Ref.14
	Modified residue	150	1	Phosphothreonine Ref.11 Ref.13 Ref.14
	Modified residue	159	1	Phosphoserine; by PKC Ref.8 Ref.9 Ref.12
	Modified residue	163	1	Phosphoserine; by PKC Ref.8 Ref.9 Ref.11 Ref.13
	Modified residue	167	1	Phosphoserine; by PKC Ref.9 Ref.10 Ref.11 Ref.13 Ref.14
	Modified residue	170	1	Phosphoserine; by PKC Ref.8 Ref.9 Ref.11 Ref.12 Ref.13 Ref.14
	Modified residue	262	1	Phosphoserine By similarity
	Lipidation	2	1	N-myristoyl glycine By similarity
Natural variations
	Natural variant	250	1	P → L. Ref.3 Corresponds to variant rs45593337 [ dbSNP | Ensembl ].		VAR_025825
	Natural variant	274	1	A → V. Ref.3 Corresponds to variant rs3734458 [ dbSNP | Ensembl ].		VAR_025826
Experimental info
	Sequence conflict	84	1	A → S in BAA01392. Ref.2
	Sequence conflict	119	1	P → A in BAA01392. Ref.2
	Sequence conflict	225	1	G → R Ref.7
	Sequence conflict	234	1	P → S in AAA59555. Ref.1
	Sequence conflict	235	1	Q → E Ref.7
	Sequence conflict	287 – 308	22	PGAPP…AAASS → LVCPRRGGSPRGGARGRRSL NQ in AAA59555. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P29966 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 0AB247801EF8FCBF	FASTA	332	31,555
	10 20 30 40 50 60 MGAQFSKTAA KGEAAAERPG EAAVASSPSK ANGQENGHVK VNGDASPAAA ESGAKEELQA 70 80 90 100 110 120 NGSAPAADKE EPAAAGSGAA SPSAAEKGEP AAAAAPEAGA SPVEKEAPAE GEAAEPGSPT 130 140 150 160 170 180 AAEGEAASAA SSTSSPKAED GATPSPSNET PKKKKKRFSF KKSFKLSGFS FKKNKKEAGE 190 200 210 220 230 240 GGEAEAPAAE GGKDEAAGGA AAAAAEAGAA SGEQAAAPGE EAAAGEEGAA GGDPQEAKPQ 250 260 270 280 290 300 EAAVAPEKPP ASDETKAAEE PSKVEEKKAE EAGASAAACE APSAAGPGAP PEQEAAPAEE 310 320 330 PAAAAASSAC AAPSQEAQPE CSPEAPPAEA AE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The human myristoylated alanine-rich C kinase substrate (MARCKS) gene (MACS). Analysis of its gene product, promoter, and chromosomal localization." Harlan D.M., Graff J.M., Stumpo D.J., Eddy R.L. Jr., Shows T.B., Boyle J.M., Blackshear P.J. J. Biol. Chem. 266:14399-14405(1991) [PubMed: 1860846] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34.
[2]	"Molecular cloning and chromosomal mapping of a cDNA encoding human 80K-L protein: major substrate for protein kinase C." Sakai K., Hirai M., Kudoh J., Minoshima S., Shimizu N. Genomics 14:175-178(1992) [PubMed: 1427823] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	NIEHS SNPs program Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LEU-250 AND VAL-274.
[4]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed: 14574404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[7]	"Relationship between the major protein kinase C substrates acidic 80-kDa protein-kinase-C substrate (80K) and myristoylated alanine-rich C-kinase substrate (MARCKS). Members of a gene family or equivalent genes in different species." Herget T., Brooks S.F., Broad S., Rozengurt E. Eur. J. Biochem. 209:7-14(1992) [PubMed: 1396720] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 189-322.
[8]	"PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and serine 163." Palmer R.H., Schonwasser D.C., Rahman D., Pappin D.J., Herget T., Parker P.J. FEBS Lett. 378:281-285(1996) [PubMed: 8557118] [Abstract] Cited for: PHOSPHORYLATION AT SER-159; SER-163 AND SER-170.
[9]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells 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) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27 AND SER-167, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation 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) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; SER-27; SER-29; SER-145; THR-150; SER-163; SER-167 AND SER-170, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[12]	"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) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-159 AND SER-170, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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) [PubMed: 18669648] [Abstract] 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] 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-167 AND SER-170, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[15]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases
EMBL GenBank DDBJ	M68956 mRNA. Translation: AAA59555.1. M68955 Genomic DNA. Translation: AAA59554.1. D10522 mRNA. Translation: BAA01392.1. DQ341274 Genomic DNA. Translation: ABC67467.1. AL132660 Genomic DNA. Translation: CAI19942.1. CH471051 Genomic DNA. Translation: EAW48258.1. CH471051 Genomic DNA. Translation: EAW48259.1. BC089040 mRNA. Translation: AAH89040.1.
IPI	IPI00219301.
PIR	A38873.
RefSeq	NP_002347.5. NM_002356.5.
UniGene	Hs.519909. Hs.712721.
3D structure databases
ProteinModelPortal	P29966.
ModBase	Search...
Protein-protein interaction databases
IntAct	P29966. 2 interactions.
STRING	P29966.
PTM databases
PhosphoSite	P29966.
Polymorphism databases
DMDM	76803798.
Proteomic databases
PeptideAtlas	P29966.
PRIDE	P29966.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000368635; ENSP00000357624; ENSG00000155130.
GeneID	4082.
KEGG	hsa:4082.
UCSC	uc003pvy.2. human.
Organism-specific databases
CTD	4082.
GeneCards	GC06P114224.
H-InvDB	HIX0006152.
HGNC	HGNC:6759. MARCKS.
HPA	CAB022062.
MIM	177061. gene.
neXtProt	NX_P29966.
PharmGKB	PA30637.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG21684.
HOVERGEN	HBG081955.
InParanoid	P29966.
OMA	MGTPLSK.
PhylomeDB	P29966.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism.
Gene expression databases
ArrayExpress	P29966.
Bgee	P29966.
CleanEx	HS_MARCKS.
Genevestigator	P29966.
GermOnline	ENSG00000155130. Homo sapiens.
Family and domain databases
InterPro	IPR002101. MARCKS. [Graphical view]
KO	K12561.
PANTHER	PTHR14353. MARCKS. 1 hit.
Pfam	PF02063. MARCKS. 1 hit. [Graphical view]
PRINTS	PR00963. MARCKS.
PROSITE	PS00826. MARCKS_1. 1 hit. PS00827. MARCKS_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	16000.
SOURCE	Search...

Entry information

Entry name

MARCS_HUMAN

Accession

Primary (citable) accession number: P29966
Secondary accession number(s): E1P560, Q2LA83, Q5TDB7

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 105 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.