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Protein

Myosin regulatory light polypeptide 9

Gene

MYL9

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi42 – 5312Add
BLAST

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. structural constituent of muscle Source: ProtInc

GO - Biological processi

  1. axon guidance Source: Reactome
  2. muscle contraction Source: Reactome
  3. platelet aggregation Source: UniProtKB
  4. regulation of muscle contraction Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Motor protein, Muscle protein, Myosin

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_19277. Sema4D induced cell migration and growth-cone collapse.
REACT_20558. Smooth Muscle Contraction.
REACT_228063. EPHA-mediated growth cone collapse.

Names & Taxonomyi

Protein namesi
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 namesi
Name:MYL9
Synonyms:MLC2, MRLC1, MYRL2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 20

Organism-specific databases

HGNCiHGNC:15754. MYL9.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. muscle myosin complex Source: ProtInc
  3. stress fiber Source: Ensembl
  4. Z disc Source: Ensembl
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31387.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 172171Myosin regulatory light polypeptide 9PRO_0000198735Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei19 – 191Phosphothreonine; by MLCK, CIT and ROCK22 Publications
Modified residuei20 – 201Phosphoserine; by CDC42BP, CIT, MLCK, PAK1, ROCK1, ROCK2, DAPK1; DAPK2 and ZIPK/DAPK35 Publications

Post-translational modificationi

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).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP24844.
PaxDbiP24844.
PeptideAtlasiP24844.
PRIDEiP24844.

2D gel databases

OGPiP24844.

PTM databases

PhosphoSiteiP24844.

Expressioni

Tissue specificityi

Smooth muscle tissues and in some, but not all, nonmuscle cells.

Gene expression databases

BgeeiP24844.
CleanExiHS_MYL9.
GenevestigatoriP24844.

Organism-specific databases

HPAiHPA045244.

Interactioni

Subunit structurei

Myosin is a hexamer of 2 heavy chains and 4 light chains.

Protein-protein interaction databases

BioGridi115670. 10 interactions.
DIPiDIP-60525N.
IntActiP24844. 5 interactions.
MINTiMINT-1376455.
STRINGi9606.ENSP00000279022.

Structurei

3D structure databases

ProteinModelPortaliP24844.
SMRiP24844. Positions 26-168.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini29 – 6436EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini98 – 13336EF-hand 2PROSITE-ProRule annotationAdd
BLAST
Domaini134 – 16936EF-hand 3PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 3 EF-hand domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5126.
GeneTreeiENSGT00760000119196.
HOGENOMiHOG000233018.
HOVERGENiHBG012180.
InParanoidiP24844.
KOiK12755.
OMAiITPSKTM.
OrthoDBiEOG7992RX.
PhylomeDBiP24844.
TreeFamiTF314218.

Family and domain databases

Gene3Di1.10.238.10. 2 hits.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PfamiPF13499. EF-hand_7. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 2 hits.
[Graphical view]
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 3 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P24844-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MSSKRAKAKT TKKRPQRATS NVFAMFDQSQ IQEFKEAFNM IDQNRDGFID
60 70 80 90 100
KEDLHDMLAS LGKNPTDEYL EGMMSEAPGP INFTMFLTMF GEKLNGTDPE
110 120 130 140 150
DVIRNAFACF DEEASGFIHE DHLRELLTTM GDRFTDEEVD EMYREAPIDK
160 170
KGNFNYVEFT RILKHGAKDK DD
Length:172
Mass (Da):19,827
Last modified:January 23, 2007 - v4
Checksum:i4C9839E85154CDA8
GO
Isoform 2 (identifier: P24844-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:118
Mass (Da):13,866
Checksum:i37186D25DFC6E8CF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti10 – 101T → A in AAA59852. (PubMed:2526655)Curated
Sequence conflicti81 – 811I → Y in AAA59852. (PubMed:2526655)Curated
Sequence conflicti114 – 1141A → S in AAA59852. (PubMed:2526655)Curated
Sequence conflicti125 – 1251E → K in AAA59852. (PubMed:2526655)Curated
Sequence conflicti148 – 1481I → V in AAA59852. (PubMed:2526655)Curated
Sequence conflicti171 – 1711D → H in AAA59852. (PubMed:2526655)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei62 – 11554Missing in isoform 2. 2 PublicationsVSP_042834Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS13276.1. [P24844-1]
CCDS13277.1. [P24844-2]
PIRiA32031.
RefSeqiNP_006088.2. NM_006097.4. [P24844-1]
NP_852667.1. NM_181526.2. [P24844-2]
UniGeneiHs.504687.

Genome annotation databases

EnsembliENST00000279022; ENSP00000279022; ENSG00000101335. [P24844-1]
ENST00000346786; ENSP00000217313; ENSG00000101335. [P24844-2]
GeneIDi10398.
KEGGihsa:10398.
UCSCiuc002xfl.2. human. [P24844-1]
uc002xfm.2. human. [P24844-2]

Polymorphism databases

DMDMi20141521.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS13276.1. [P24844-1]
CCDS13277.1. [P24844-2]
PIRiA32031.
RefSeqiNP_006088.2. NM_006097.4. [P24844-1]
NP_852667.1. NM_181526.2. [P24844-2]
UniGeneiHs.504687.

3D structure databases

ProteinModelPortaliP24844.
SMRiP24844. Positions 26-168.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115670. 10 interactions.
DIPiDIP-60525N.
IntActiP24844. 5 interactions.
MINTiMINT-1376455.
STRINGi9606.ENSP00000279022.

PTM databases

PhosphoSiteiP24844.

Polymorphism databases

DMDMi20141521.

2D gel databases

OGPiP24844.

Proteomic databases

MaxQBiP24844.
PaxDbiP24844.
PeptideAtlasiP24844.
PRIDEiP24844.

Protocols and materials databases

DNASUi10398.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000279022; ENSP00000279022; ENSG00000101335. [P24844-1]
ENST00000346786; ENSP00000217313; ENSG00000101335. [P24844-2]
GeneIDi10398.
KEGGihsa:10398.
UCSCiuc002xfl.2. human. [P24844-1]
uc002xfm.2. human. [P24844-2]

Organism-specific databases

CTDi10398.
GeneCardsiGC20P035169.
HGNCiHGNC:15754. MYL9.
HPAiHPA045244.
MIMi609905. gene.
neXtProtiNX_P24844.
PharmGKBiPA31387.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5126.
GeneTreeiENSGT00760000119196.
HOGENOMiHOG000233018.
HOVERGENiHBG012180.
InParanoidiP24844.
KOiK12755.
OMAiITPSKTM.
OrthoDBiEOG7992RX.
PhylomeDBiP24844.
TreeFamiTF314218.

Enzyme and pathway databases

ReactomeiREACT_19277. Sema4D induced cell migration and growth-cone collapse.
REACT_20558. Smooth Muscle Contraction.
REACT_228063. EPHA-mediated growth cone collapse.

Miscellaneous databases

GeneWikiiMYL9.
GenomeRNAii10398.
NextBioi39398.
PROiP24844.
SOURCEiSearch...

Gene expression databases

BgeeiP24844.
CleanExiHS_MYL9.
GenevestigatoriP24844.

Family and domain databases

Gene3Di1.10.238.10. 2 hits.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PfamiPF13499. EF-hand_7. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 2 hits.
[Graphical view]
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiMYL9_HUMAN
AccessioniPrimary (citable) accession number: P24844
Secondary accession number(s): E1P5T6
, Q9BQL9, Q9BUF9, Q9H136
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: January 23, 2007
Last modified: January 7, 2015
This is version 136 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Miscellaneous

This chain binds calcium.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.