MYLK

Gene of the immunoglobulin superfamily
MYLK
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2CQV, 2K0F, 2YR3

Identifiers
AliasesMYLK, AAT7, KRP, MLCK, MLCK1, MLCK108, MLCK210, MSTP083, MYLK1, smMLCK, myosin light chain kinase, MMIHS, MMIHS1, MYLK-L
External IDsOMIM: 600922; MGI: 894806; HomoloGene: 14202; GeneCards: MYLK; OMA:MYLK - orthologs
Gene location (Human)
Chromosome 3 (human)
Chr.Chromosome 3 (human)[1]
Chromosome 3 (human)
Genomic location for MYLK
Genomic location for MYLK
Band3q21.1Start123,610,049 bp[1]
End123,884,332 bp[1]
Gene location (Mouse)
Chromosome 16 (mouse)
Chr.Chromosome 16 (mouse)[2]
Chromosome 16 (mouse)
Genomic location for MYLK
Genomic location for MYLK
Band16|16 B3Start34,565,580 bp[2]
End34,822,790 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • tail of epididymis

  • saphenous vein

  • seminal vesicula

  • nipple

  • urethra

  • vena cava

  • superficial temporal artery

  • myometrium

  • caput epididymis

  • corpus epididymis
Top expressed in
  • iris

  • ascending aorta

  • belly cord

  • migratory enteric neural crest cell

  • uterus

  • aortic valve

  • tunica media of zone of aorta

  • ciliary body

  • cervix

  • pineal gland
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • transferase activity
  • nucleotide binding
  • protein kinase activity
  • metal ion binding
  • calmodulin binding
  • myosin light chain kinase activity
  • kinase activity
  • protein serine/threonine kinase activity
  • protein binding
  • actin binding
  • ATP binding
Cellular component
  • cytoplasm
  • cytosol
  • cell projection
  • stress fiber
  • cleavage furrow
  • cytoskeleton
  • lamellipodium
  • plasma membrane
  • actin cytoskeleton
Biological process
  • smooth muscle contraction
  • muscle contraction
  • phosphorylation
  • tonic smooth muscle contraction
  • positive regulation of cell migration
  • positive regulation of wound healing
  • bleb assembly
  • cellular hypotonic response
  • protein phosphorylation
  • aorta smooth muscle tissue morphogenesis
  • positive regulation of calcium ion transport
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

4638

107589

Ensembl

ENSG00000065534

ENSMUSG00000022836

UniProt

Q15746

Q6PDN3

RefSeq (mRNA)
NM_001321309
NM_005965
NM_053025
NM_053026
NM_053027

NM_053028
NM_053029
NM_053030
NM_053031
NM_053032

NM_139300

RefSeq (protein)
NP_001308238
NP_444253
NP_444254
NP_444255
NP_444256

NP_444259
NP_444260

NP_647461
NP_001395190
NP_001395191
NP_001395192

Location (UCSC)Chr 3: 123.61 – 123.88 MbChr 16: 34.57 – 34.82 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Myosin light chain kinase, smooth muscle also known as kinase-related protein (KRP) or telokin is an enzyme that in humans is encoded by the MYLK gene.[5]

Function

This gene, a muscle member of the immunoglobulin superfamily, encodes a myosin light-chain kinase, which is a calcium-/calmodulin-dependent enzyme. This kinase phosphorylates myosin regulatory light chains to facilitate myosin interaction with actin filaments to produce contractile activity. This gene encodes both smooth muscle and nonmuscle isoforms. In addition, using a separate promoter in an intron in the 3' region, it encodes telokin, a small protein identical in sequence to the C-terminus of myosin light chain kinase, that is independently expressed in smooth muscle and functions to stabilize unphosphorylated myosin filaments. A pseudogene is located on the p arm of chromosome 3. Four transcript variants that produce four isoforms of the calcium/calmodulin dependent enzyme have been identified as well as two transcripts that produce two isoforms of telokin. Additional variants have been identified but lack full length transcripts.[6]

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000065534 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000022836 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Potier MC, Chelot E, Pekarsky Y, Gardiner K, Rossier J, Turnell WG (Mar 1996). "The human myosin light chain kinase (MLCK) from hippocampus: cloning, sequencing, expression, and localization to 3qcen-q21". Genomics. 29 (3): 562–70. doi:10.1006/geno.1995.9965. PMID 8575746.
  6. ^ "Entrez Gene: MYLK myosin, light chain kinase".

Further reading

  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
  • Clayburgh DR, Rosen S, Witkowski ED, et al. (2005). "A Differentiation-dependent Splice Variant of Myosin Light Chain Kinase, MLCK1, Regulates Epithelial Tight Junction Permeability". J. Biol. Chem. 279 (53): 55506–13. doi:10.1074/jbc.M408822200. PMC 1237105. PMID 15507455.
  • Wang F, Graham WV, Wang Y, et al. (2005). "Interferon-γ and Tumor Necrosis Factor-α Synergize to Induce Intestinal Epithelial Barrier Dysfunction by Up-Regulating Myosin Light Chain Kinase Expression". Am. J. Pathol. 166 (2): 409–19. doi:10.1016/S0002-9440(10)62264-X. PMC 1237049. PMID 15681825.
  • Russo JM, Florian P, Shen L, et al. (2005). "Distinct Temporal-Spatial Roles for Rho Kinase and Myosin Light Chain Kinase in Epithelial Purse-String Wound Closure". Gastroenterology. 128 (4): 987–1001. doi:10.1053/j.gastro.2005.01.004. PMC 1237051. PMID 15825080.
  • Shimizu S, Yoshida T, Wakamori M, et al. (2006). "Ca2+–calmodulin-dependent myosin light chain kinase is essential for activation of TRPC5 channels expressed in HEK293 cells". J. Physiol. 570 (Pt 2): 219–35. doi:10.1113/jphysiol.2005.097998. PMC 1464317. PMID 16284075.
  • Kim MT, Kim BJ, Lee JH, et al. (2006). "Involvement of calmodulin and myosin light chain kinase in activation of mTRPC5 expressed in HEK cells". Am. J. Physiol., Cell Physiol. 290 (4): C1031–40. doi:10.1152/ajpcell.00602.2004. PMID 16306123.
  • Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: Large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
  • Connell LE, Helfman DM (2007). "Myosin light chain kinase plays a role in the regulation of epithelial cell survival". J. Cell Sci. 119 (Pt 11): 2269–81. doi:10.1242/jcs.02926. PMID 16723733.
  • Seguchi O, Takashima S, Yamazaki S, et al. (2007). "A cardiac myosin light chain kinase regulates sarcomere assembly in the vertebrate heart". J. Clin. Invest. 117 (10): 2812–24. doi:10.1172/JCI30804. PMC 1978424. PMID 17885681.

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

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  • 2cqv: Solution structure of the eighth Ig-like domain of human myosin light chain kinase
    2cqv: Solution structure of the eighth Ig-like domain of human myosin light chain kinase
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Non-specific serine/threonine protein kinases (EC 2.7.11.1)
Pyruvate dehydrogenase kinase (EC 2.7.11.2)
Dephospho-(reductase kinase) kinase (EC 2.7.11.3)
3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring) kinase (EC 2.7.11.4)
(isocitrate dehydrogenase (NADP+)) kinase (EC 2.7.11.5)
(tyrosine 3-monooxygenase) kinase (EC 2.7.11.6)
Myosin-heavy-chain kinase (EC 2.7.11.7)
Fas-activated serine/threonine kinase (EC 2.7.11.8)
Goodpasture-antigen-binding protein kinase (EC 2.7.11.9)
  • -
IκB kinase (EC 2.7.11.10)
cAMP-dependent protein kinase (EC 2.7.11.11)
cGMP-dependent protein kinase (EC 2.7.11.12)
Protein kinase C (EC 2.7.11.13)
Rhodopsin kinase (EC 2.7.11.14)
Beta adrenergic receptor kinase (EC 2.7.11.15)
G-protein coupled receptor kinases (EC 2.7.11.16)
Ca2+/calmodulin-dependent (EC 2.7.11.17)
Myosin light-chain kinase (EC 2.7.11.18)
Phosphorylase kinase (EC 2.7.11.19)
Elongation factor 2 kinase (EC 2.7.11.20)
Polo kinase (EC 2.7.11.21)
Serine/threonine-specific protein kinases (EC 2.7.11.21-EC 2.7.11.30)
Polo kinase (EC 2.7.11.21)
Cyclin-dependent kinase (EC 2.7.11.22)
(RNA-polymerase)-subunit kinase (EC 2.7.11.23)
Mitogen-activated protein kinase (EC 2.7.11.24)
MAP3K (EC 2.7.11.25)
Tau-protein kinase (EC 2.7.11.26)
(acetyl-CoA carboxylase) kinase (EC 2.7.11.27)
  • -
Tropomyosin kinase (EC 2.7.11.28)
  • -
Low-density-lipoprotein receptor kinase (EC 2.7.11.29)
  • -
Receptor protein serine/threonine kinase (EC 2.7.11.30)
MAP2K
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Human
Microfilaments
and ABPs
Myofilament
Actins
Myosins
Other
Other
Intermediate
filaments
Type 1/2
(Keratin,
Cytokeratin)
Epithelial keratins
(soft alpha-keratins)
Hair keratins
(hard alpha-keratins)
Ungrouped alpha
Not alpha
Type 3
Type 4
Type 5
Microtubules
and MAPs
Tubulins
MAPs
Kinesins
Dyneins
Microtubule organising proteins
Microtubule severing proteins
Other
Catenins
Membrane
Other
Nonhuman
See also: cytoskeletal defects
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