P24844 (MYL9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Myosin regulatory light polypeptide 9

Alternative name(s):
20 kDa myosin light chain
Short name=LC20
MLC-2C
Myosin RLC
Myosin regulatory light chain 2, smooth muscle isoform
Myosin regulatory light chain 9
Myosin regulatory light chain MRLC1

Gene names

Name:	MYL9
Synonyms:	MLC2, MRLC1, MYRL2

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	172 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	Myosin regulatory subunit that plays an important role in regulation of both smooth muscle and nonmuscle cell contractile activity via its phosphorylation. Implicated in cytokinesis, receptor capping, and cell locomotion.
Subunit structure	Myosin is an hexamer of 2 heavy chains and 4 light chains.
Tissue specificity	Smooth muscle tissues and in some, but not all, nonmuscle cells.
Post-translational modification	Phosphorylation increases the actin-activated myosin ATPase activity and thereby regulates the contractile activity. It is required to generate the driving force in the migration of the cells but not necessary for localization of myosin-2 at the leading edge By similarity.
Miscellaneous	This chain binds calcium.
Sequence similarities	Contains 3 EF-hand domains.

Ontologies

Keywords
Domain	Repeat
Ligand	Calcium
Molecular function	Motor protein Muscle protein Myosin
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	axon guidance Traceable author statement. Source: Reactome muscle contraction Traceable author statement. Source: Reactome regulation of muscle contraction Traceable author statement. Source: ProtInc
Cellular component	cytosol Traceable author statement. Source: Reactome muscle myosin complex Traceable author statement. Source: ProtInc
Molecular function	calcium ion binding Inferred from electronic annotation. Source: InterPro structural constituent of muscle 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 – 172	171	Myosin regulatory light polypeptide 9		PRO_0000198735
Regions
	Domain	29 – 64	36	EF-hand 1
	Domain	98 – 133	36	EF-hand 2
	Domain	134 – 169	36	EF-hand 3
	Calcium binding	42 – 53	12
Amino acid modifications
	Modified residue	2	1	N-acetylserine By similarity
	Modified residue	19	1	Phosphothreonine; by MLCK, CIT and ROCK2 Ref.2 Ref.5 Ref.7 Ref.9
	Modified residue	20	1	Phosphoserine; by CDC42BP, CIT, MLCK, PAK1, ROCK1, ROCK2, DAPK1; DAPK2 and ZIPK/DAPK3 Ref.2 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10
	Modified residue	29	1	Phosphoserine By similarity
	Modified residue	135	1	Phosphothreonine By similarity
Experimental info
	Sequence conflict	10	1	T → A in AAA59852. Ref.1
	Sequence conflict	81	1	I → Y in AAA59852. Ref.1
	Sequence conflict	114	1	A → S in AAA59852. Ref.1
	Sequence conflict	125	1	E → K in AAA59852. Ref.1
	Sequence conflict	148	1	I → V in AAA59852. Ref.1
	Sequence conflict	171	1	D → H in AAA59852. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P24844 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 4C9839E85154CDA8	FASTA	172	19,827
	10 20 30 40 50 60 MSSKRAKAKT TKKRPQRATS NVFAMFDQSQ IQEFKEAFNM IDQNRDGFID KEDLHDMLAS 70 80 90 100 110 120 LGKNPTDEYL EGMMSEAPGP INFTMFLTMF GEKLNGTDPE DVIRNAFACF DEEASGFIHE 130 140 150 160 170 DHLRELLTTM GDRFTDEEVD EMYREAPIDK KGNFNYVEFT RILKHGAKDK DD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization and differential expression of human vascular smooth muscle myosin light chain 2 isoform in nonmuscle cells." Kumar C.C., Mohan S.R., Zavodny P.J., Narula S.K., Leibowitz P.J. Biochemistry 28:4027-4035(1989) [PubMed: 2526655] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Umbilical artery.
[2]	"Diphosphorylated MRLC is required for organization of stress fibers in interphase cells and the contractile ring in dividing cells." Iwasaki T., Murata-Hori M., Ishitobi S., Hosoya H. Cell Struct. Funct. 26:677-683(2001) [PubMed: 11942626] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION AT THR-19 AND SER-20.
[3]	"The DNA sequence and comparative analysis of human chromosome 20." Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J. Nature 414:865-871(2001) [PubMed: 11780052] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	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].
[5]	"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 THR-19 AND SER-20, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[6]	"A tripartite complex containing MRCK modulates lamellar actomyosin retrograde flow." Tan I., Yong J., Dong J.M., Lim L., Leung T. Cell 135:123-136(2008) [PubMed: 18854160] [Abstract] Cited for: PHOSPHORYLATION AT SER-20.
[7]	"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 THR-19 AND SER-20, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"Caspase-activated ROCK-1 allows erythroblast terminal maturation independently of cytokine-induced Rho signaling." Gabet A.S., Coulon S., Fricot A., Vandekerckhove J., Chang Y., Ribeil J.A., Lordier L., Zermati Y., Asnafi V., Belaid Z., Debili N., Vainchenker W., Varet B., Hermine O., Courtois G. Cell Death Differ. 18:678-689(2011) [PubMed: 21072057] [Abstract] Cited for: PHOSPHORYLATION AT SER-20.
[9]	"Chelerythrine perturbs lamellar actomyosin filaments by selective inhibition of myotonic dystrophy kinase-related Cdc42-binding kinase." Tan I., Lai J., Yong J., Li S.F., Leung T. FEBS Lett. 585:1260-1268(2011) [PubMed: 21457715] [Abstract] Cited for: PHOSPHORYLATION AT THR-19 AND SER-20.
[10]	"New modularity of DAP-kinases: alternative splicing of the DRP-1 gene produces a ZIPk-like isoform." Shoval Y., Berissi H., Kimchi A., Pietrokovski S. PLoS ONE 6:E17344-E17344(2011) [PubMed: 21408167] [Abstract] Cited for: PHOSPHORYLATION AT SER-20 BY DAPK1; DAPK2 AND ZIPK/DAPK3.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	J02854 mRNA. Translation: AAA59852.1. D82057 mRNA. Translation: BAB88917.1. AL050318 Genomic DNA. Translation: CAB75369.1. CH471077 Genomic DNA. Translation: EAW76129.1. CH471077 Genomic DNA. Translation: EAW76131.1. CH471077 Genomic DNA. Translation: EAW76134.1.
IPI	IPI00220278.
PIR	A32031.
RefSeq	NP_006088.2. NM_006097.3.
UniGene	Hs.504687.
3D structure databases
ProteinModelPortal	P24844.
SMR	P24844. Positions 21-168.
ModBase	Search...
Protein-protein interaction databases
IntAct	P24844. 3 interactions.
STRING	P24844.
PTM databases
PhosphoSite	P24844.
Polymorphism databases
DMDM	20141521.
2D gel databases
OGP	P24844.
Proteomic databases
PeptideAtlas	P24844.
PRIDE	P24844.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000279022; ENSP00000279022; ENSG00000101335.
GeneID	10398.
KEGG	hsa:10398.
UCSC	uc002xfl.1. human.
Organism-specific databases
CTD	10398.
GeneCards	GC20P035169.
H-InvDB	HIX0015780.
HGNC	HGNC:15754. MYL9.
MIM	609905. gene.
neXtProt	NX_P24844.
PharmGKB	PA31387.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	HBG746798.
HOVERGEN	HBG012180.
InParanoid	P24844.
OMA	FRDAPIK.
OrthoDB	EOG4FTW1S.
PhylomeDB	P24844.
Enzyme and pathway databases
Reactome	REACT_111045. Developmental Biology. REACT_17044. Muscle contraction.
Gene expression databases
ArrayExpress	P24844.
Bgee	P24844.
CleanEx	HS_MYL9.
Genevestigator	P24844.
GermOnline	ENSG00000101335. Homo sapiens.
Family and domain databases
InterPro	IPR018248. EF-hand. IPR011992. EF-hand-like_dom. IPR018247. EF_Hand_1_Ca_BS. IPR018249. EF_HAND_2. IPR002048. EF_hand_Ca-bd. [Graphical view]
Gene3D	G3DSA:1.10.238.10. EF-Hand_type. 2 hits.
KO	K12755.
Pfam	PF00036. efhand. 1 hit. [Graphical view]
SMART	SM00054. EFh. 2 hits. [Graphical view]
PROSITE	PS00018. EF_HAND_1. 1 hit. PS50222. EF_HAND_2. 3 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	39398.
SOURCE	Search...

Entry information

Entry name

MYL9_HUMAN

Accession

Primary (citable) accession number: P24844
Secondary accession number(s): E1P5T6, Q9H136

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 1992
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 108 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.