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P24844 (MYL9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length172 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 a 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.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P24844-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P24844-2)

The sequence of this isoform differs from the canonical sequence as follows:
     62-115: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 172171Myosin regulatory light polypeptide 9
PRO_0000198735

Regions

Domain29 – 6436EF-hand 1
Domain98 – 13336EF-hand 2
Domain134 – 16936EF-hand 3
Calcium binding42 – 5312

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue191Phosphothreonine; by MLCK, CIT and ROCK2 Ref.3 Ref.9
Modified residue201Phosphoserine; by CDC42BP, CIT, MLCK, PAK1, ROCK1, ROCK2, DAPK1; DAPK2 and ZIPK/DAPK3 Ref.3 Ref.7 Ref.8 Ref.9 Ref.10

Natural variations

Alternative sequence62 – 11554Missing in isoform 2.
VSP_042834

Experimental info

Sequence conflict101T → A in AAA59852. Ref.1
Sequence conflict811I → Y in AAA59852. Ref.1
Sequence conflict1141A → S in AAA59852. Ref.1
Sequence conflict1251E → K in AAA59852. Ref.1
Sequence conflict1481I → V in AAA59852. Ref.1
Sequence conflict1711D → H in AAA59852. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 4C9839E85154CDA8

FASTA17219,827
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 37186D25DFC6E8CF
Show »

FASTA11813,866

References

« Hide '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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Umbilical artery.
[2]"Splice variant of regulatory myosin light chain, short version."
Pan J.Y., Li S., Silberstein D.S.
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[3]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PHOSPHORYLATION AT THR-19 AND SER-20.
[4]"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. expand/collapse author list , 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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Uterus.
[7]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-20.
[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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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.
AF176043 mRNA. Translation: AAQ13654.1.
D82057 mRNA. Translation: BAB88917.1.
AL050318 Genomic DNA. Translation: CAB75369.1.
AL050318 Genomic DNA. Translation: CAC34440.2.
CH471077 Genomic DNA. Translation: EAW76129.1.
CH471077 Genomic DNA. Translation: EAW76131.1.
CH471077 Genomic DNA. Translation: EAW76132.1.
CH471077 Genomic DNA. Translation: EAW76133.1.
CH471077 Genomic DNA. Translation: EAW76134.1.
BC002648 mRNA. Translation: AAH02648.1.
PIRA32031.
RefSeqNP_006088.2. NM_006097.4.
NP_852667.1. NM_181526.2.
UniGeneHs.504687.

3D structure databases

ProteinModelPortalP24844.
SMRP24844. Positions 26-168.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115670. 10 interactions.
DIPDIP-60525N.
IntActP24844. 3 interactions.
MINTMINT-1376455.
STRING9606.ENSP00000279022.

PTM databases

PhosphoSiteP24844.

Polymorphism databases

DMDM20141521.

2D gel databases

OGPP24844.

Proteomic databases

PaxDbP24844.
PeptideAtlasP24844.
PRIDEP24844.

Protocols and materials databases

DNASU10398.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000279022; ENSP00000279022; ENSG00000101335. [P24844-1]
ENST00000346786; ENSP00000217313; ENSG00000101335. [P24844-2]
GeneID10398.
KEGGhsa:10398.
UCSCuc002xfl.2. human. [P24844-1]
uc002xfm.2. human. [P24844-2]

Organism-specific databases

CTD10398.
GeneCardsGC20P035169.
HGNCHGNC:15754. MYL9.
HPAHPA045244.
MIM609905. gene.
neXtProtNX_P24844.
PharmGKBPA31387.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5126.
HOGENOMHOG000233018.
HOVERGENHBG012180.
InParanoidP24844.
KOK12755.
OMAITPSKTM.
OrthoDBEOG7992RX.
PhylomeDBP24844.
TreeFamTF314218.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_17044. Muscle contraction.

Gene expression databases

BgeeP24844.
CleanExHS_MYL9.
GenevestigatorP24844.

Family and domain databases

Gene3D1.10.238.10. 2 hits.
InterProIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PfamPF13499. EF-hand_7. 1 hit.
[Graphical view]
SMARTSM00054. EFh. 2 hits.
[Graphical view]
PROSITEPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiMYL9.
GenomeRNAi10398.
NextBio39398.
PROP24844.
SOURCESearch...

Entry information

Entry nameMYL9_HUMAN
AccessionPrimary (citable) accession number: P24844
Secondary accession number(s): E1P5T6 expand/collapse secondary AC list , Q9BQL9, Q9BUF9, Q9H136
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: January 23, 2007
Last modified: March 19, 2014
This is version 129 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM