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Q15746 (MYLK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 160. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Myosin light chain kinase, smooth muscle

Short name=MLCK
Short name=smMLCK
EC=2.7.11.18
Alternative name(s):
Kinase-related protein
Short name=KRP
Telokin
Gene names
Name:MYLK
Synonyms:MLCK, MLCK1, MYLK1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1914 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Calcium/calmodulin-dependent myosin light chain kinase implicated in smooth muscle contraction via phosphorylation of myosin light chains (MLC). Also regulates actin-myosin interaction through a non-kinase activity. Phosphorylates PTK2B/PYK2 and myosin light-chains. Involved in the inflammatory response (e.g. apoptosis, vascular permeability, leukocyte diapedesis), cell motility and morphology, airway hyperreactivity and other activities relevant to asthma. Required for tonic airway smooth muscle contraction that is necessary for physiological and asthmatic airway resistance. Necessary for gastrointestinal motility. Implicated in the regulation of endothelial as well as vascular permeability, probably via the regulation of cytoskeletal rearrangements. In the nervous system it has been shown to control the growth initiation of astrocytic processes in culture and to participate in transmitter release at synapses formed between cultured sympathetic ganglion cells. Critical participant in signaling sequences that result in fibroblast apoptosis. Plays a role in the regulation of epithelial cell survival. Required for epithelial wound healing, especially during actomyosin ring contraction during purse-string wound closure. Mediates RhoA-dependent membrane blebbing. Triggers TRPC5 channel activity in a calcium-dependent signaling, by inducing its subcellular localization at the plasma membrane. Promotes cell migration (including tumor cells) and tumor metastasis. PTK2B/PYK2 activation by phosphorylation mediates ITGB2 activation and is thus essential to trigger neutrophil transmigration during acute lung injury (ALI). May regulate optic nerve head astrocyte migration. Probably involved in mitotic cytoskeletal regulation. Regulates tight junction probably by modulating ZO-1 exchange in the perijunctional actomyosin ring. Mediates burn-induced microvascular barrier injury; triggers endothelial contraction in the development of microvascular hyperpermeability by phosphorylating MLC. Essential for intestinal barrier dysfunction. Mediates Giardia spp.-mediated reduced epithelial barrier function during giardiasis intestinal infection via reorganization of cytoskeletal F-actin and tight junctional ZO-1. Necessary for hypotonicity-induced Ca2+ entry and subsequent activation of volume-sensitive organic osmolyte/anion channels (VSOAC) in cervical cancer cells. Responsible for high proliferative ability of breast cancer cells through anti-apoptosis. Ref.4 Ref.7 Ref.15 Ref.17 Ref.19 Ref.20 Ref.21 Ref.23 Ref.27 Ref.28 Ref.29 Ref.32 Ref.33

Catalytic activity

ATP + [myosin light-chain] = ADP + [myosin light-chain] phosphate.

Cofactor

Magnesium.

Calcium.

Enzyme regulation

Isoform 1 is activated by phosphorylation on Tyr-464 and Tyr-471. Isoforms which lack these tyrosine residues are not regulated in this way. All catalytically active isoforms require binding to calcium and calmodulin for activation. Repressed by organometallic pyridylnaphthalimide complexes, wortmannin, ML-7 (a synthetic naphthalenesulphonyl derivative that inhibits the binding of ATP to MLCK) and ML-9. Ref.4 Ref.15 Ref.16 Ref.19 Ref.20 Ref.34

Subunit structure

All isoforms including Telokin bind calmodulin. Interacts with SVIL By similarity. Interacts with CTTN; this interaction is reduced during thrombin-induced endothelial cell (EC) contraction but is promoted by the barrier-protective agonist sphingosine 1-phosphate (S1P) within lamellipodia. A complex made of ABL1, CTTN and MYLK regulates cortical actin-based cytoskeletal rearrangement critical to sphingosine 1-phosphate (S1P)-mediated endothelial cell (EC) barrier enhancement. Binds to NAA10/ARD1 and PTK2B/PYK2. Ref.14 Ref.23 Ref.27 Ref.30 Ref.31

Subcellular location

Cytoplasm. Cell projectionlamellipodium. Cleavage furrow. Cytoplasmcytoskeleton. Note: Localized to stress fibers during interphase and to the cleavage furrow during mitosis. Ref.7 Ref.30

Tissue specificity

Smooth muscle and non-muscle isozymes are expressed in a wide variety of adult and fetal tissues and in cultured endothelium with qualitative expression appearing to be neither tissue- nor development-specific. Non-muscle isoform 2 is the dominant splice variant expressed in various tissues. Telokin has been found in a wide variety of adult and fetal tissues. Accumulates in well differentiated enterocytes of the intestinal epithelium in response to tumor necrosis factor (TNF). Ref.1 Ref.5 Ref.18 Ref.30

Induction

Accumulates in individuals with asthma (at protein levels). Induced by tumor necrosis factor (TNF). Repressed by androgens (e.g. R1881). Ref.4 Ref.15 Ref.16 Ref.18 Ref.19 Ref.20 Ref.26 Ref.34 Ref.35

Post-translational modification

Can probably be down-regulated by phosphorylation. Tyrosine phosphorylation by ABL1 increases kinase activity, reverses MLCK-mediated inhibition of Arp2/3-mediated actin polymerization, and enhances CTTN-binding. Phosphorylation by SRC at Tyr-464 and Tyr-471 promotes CTTN binding.

The C-terminus is deglutamylated by AGTPBP1/CCP1, AGBL1/CCP4 and AGBL4/CCP6, leading to the formation of Myosin light chain kinase, smooth muscle, deglutamylated form. The consequences of C-terminal deglutamylation are unknown By similarity.

Acetylated at Lys-608 by NAA10/ARD1 via a calcium-dependent signaling; this acetylation represses kinase activity and reduces tumor cell migration. Ref.27

Involvement in disease

Aortic aneurysm, familial thoracic 7 (AAT7) [MIM:613780]: A disease characterized by permanent dilation of the thoracic aorta usually due to degenerative changes in the aortic wall. It is primarily associated with a characteristic histologic appearance known as 'medial necrosis' or 'Erdheim cystic medial necrosis' in which there is degeneration and fragmentation of elastic fibers, loss of smooth muscle cells, and an accumulation of basophilic ground substance.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.40

Miscellaneous

In asthmatic patients, overexpression promotes actin filament propulsion, thus contributing to airway hyperresponsiveness. Some MYLK variants may contribute to acute lung injury (ALI) susceptibility. Potential therapeutic target in the treatment of burn edema.

Sequence similarities

Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family.

Contains 1 fibronectin type-III domain.

Contains 9 Ig-like C2-type (immunoglobulin-like) domains.

Contains 1 protein kinase domain.

Biophysicochemical properties

Kinetic parameters:

KM=6.5 µM for MLC (isoform 1 at 22 degrees Celsius) Ref.4

KM=7.2 µM for MLC (isoform 2 at 22 degrees Celsius)

Vmax=11.9 µmol/min/mg enzyme (isoform 1 at 22 degrees Celsius)

Vmax=10.9 µmol/min/mg enzyme (isoform 1 at 22 degrees Celsius)

Sequence caution

The sequence AAD15922.1 differs from that shown. Reason: Frameshift at position 1433.

The sequence AAD15923.1 differs from that shown. Reason: Frameshift at position 1433.

The sequence AAD15924.1 differs from that shown. Reason: Frameshift at position 1433.

Isoform 3A: The sequence AAD15922.1 differs from that shown. Reason: Frameshift at positions 1433 and 1439.

Isoform 3B: The sequence AAD15923.1 differs from that shown. Reason: Frameshift at positions 1433 and 1439.

Isoform 4: The sequence AAD15924.1 differs from that shown. Reason: Frameshift at positions 1433 and 1439.

Ontologies

Keywords
   Cellular componentCell projection
Cytoplasm
Cytoskeleton
   Coding sequence diversityAlternative initiation
Alternative splicing
Polymorphism
   DiseaseAortic aneurysm
Disease mutation
   DomainImmunoglobulin domain
Repeat
   LigandActin-binding
ATP-binding
Calcium
Calmodulin-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMAcetylation
Disulfide bond
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactin filament organization

Inferred from Biological aspect of Ancestor. Source: RefGenome

aorta smooth muscle tissue morphogenesis

Inferred from mutant phenotype Ref.40. Source: BHF-UCL

bleb assembly

Inferred from mutant phenotype Ref.32. Source: UniProtKB

cellular hypotonic response

Inferred from direct assay Ref.15. Source: UniProtKB

muscle contraction

Traceable author statement. Source: Reactome

positive regulation of calcium ion transport

Inferred from direct assay Ref.20. Source: UniProtKB

positive regulation of cell migration

Inferred from direct assay Ref.27. Source: UniProtKB

positive regulation of wound healing

Inferred from direct assay Ref.17. Source: UniProtKB

protein phosphorylation

Traceable author statement Ref.1. Source: ProtInc

smooth muscle contraction

Inferred from sequence or structural similarity. Source: UniProtKB

tonic smooth muscle contraction

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcleavage furrow

Inferred from direct assay Ref.7. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.30. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

lamellipodium

Inferred from direct assay Ref.30. Source: UniProtKB

stress fiber

Inferred from direct assay Ref.7. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

calmodulin-dependent protein kinase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

myosin light chain kinase activity

Inferred from direct assay Ref.20. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 17474147. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NCK1P163332EBI-968482,EBI-389883

Alternative products

This entry describes 11 isoforms produced by alternative splicing and alternative initiation. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: Q15746-1)

Also known as: Non-muscle isozyme;

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: Q15746-2)

The sequence of this isoform differs from the canonical sequence as follows:
     437-506: VSGIPKPEVAWFLEGTPVRRQEGSIEVYEDAGSHYLCLLKARTRDSGTYSCTASNAQGQLSCSWTLQVER → G
Isoform 3A (identifier: Q15746-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1655-1705: Missing.
Isoform 3B (identifier: Q15746-4)

The sequence of this isoform differs from the canonical sequence as follows:
     437-506: VSGIPKPEVAWFLEGTPVRRQEGSIEVYEDAGSHYLCLLKARTRDSGTYSCTASNAQGQLSCSWTLQVER → G
     1655-1705: Missing.
Isoform 4 (identifier: Q15746-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1473-1545: Missing.
Isoform Del-1790 (identifier: Q15746-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1790-1790: Missing.
Isoform 5 (identifier: Q15746-7)

Also known as: Smooth-muscle isozyme;

The sequence of this isoform differs from the canonical sequence as follows:
     1-922: Missing.
Note: Produced by alternative initiation at Met-923 of isoform 1.
Isoform 6 (identifier: Q15746-8)

Also known as: Telokin;

The sequence of this isoform differs from the canonical sequence as follows:
     1-1760: Missing.
Note: Produced by alternative initiation at Met-1761 of isoform 1. Has no catalytic activity.
Isoform 7 (identifier: Q15746-9)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1200: Missing.
Isoform 8 (identifier: Q15746-10)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1760: Missing.
     1790-1790: Missing.
Note: Produced by alternative initiation at Met-1761 of isoform 1.
Isoform 9 (identifier: Q15746-11)

The sequence of this isoform differs from the canonical sequence as follows:
     1-922: Missing.
     1790-1790: Missing.
Note: Produced by alternative initiation at Met-923 of isoform 1.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 19141914Myosin light chain kinase, smooth muscle
PRO_0000024354
Chain1 – 19101910Myosin light chain kinase, smooth muscle, deglutamylated form By similarity
PRO_0000403731

Regions

Domain33 – 12290Ig-like C2-type 1
Domain161 – 24989Ig-like C2-type 2
Domain414 – 50390Ig-like C2-type 3
Domain514 – 59986Ig-like C2-type 4
Domain620 – 71192Ig-like C2-type 5
Domain721 – 821101Ig-like C2-type 6
Repeat868 – 895281-1
Repeat896 – 923281-2
Repeat924 – 951281-3
Repeat952 – 979281-4
Repeat980 – 998191-5; truncated
Repeat999 – 100352-1; truncated
Repeat1004 – 1015122-2
Repeat1016 – 1027122-3
Repeat1028 – 1039122-4
Repeat1040 – 1051122-5
Repeat1052 – 1063122-6
Domain1098 – 118689Ig-like C2-type 7
Domain1238 – 132689Ig-like C2-type 8
Domain1334 – 142693Fibronectin type-III
Domain1464 – 1719256Protein kinase
Domain1809 – 189890Ig-like C2-type 9
Nucleotide binding1470 – 14789ATP By similarity
Region868 – 9981315 X 28 AA approximate tandem repeats
Region923 – 96341Actin-binding (calcium/calmodulin-sensitive) By similarity
Region948 – 96316Calmodulin-binding By similarity
Region999 – 1063656 X 12 AA approximate tandem repeats
Region1061 – 1460400Actin-binding (calcium/calmodulin-insensitive) By similarity
Region1711 – 177464Calmodulin-binding
Compositional bias1906 – 19149Poly-Glu

Sites

Active site15851Proton acceptor By similarity
Binding site14931ATP By similarity

Amino acid modifications

Modified residue2311Phosphotyrosine; by ABL1 Ref.31
Modified residue3651Phosphoserine By similarity
Modified residue4641Phosphotyrosine; by ABL1 and SRC Ref.4 Ref.14 Ref.31
Modified residue4711Phosphotyrosine; by SRC Ref.4 Ref.14
Modified residue5561Phosphotyrosine; by ABL1 Ref.31
Modified residue6081N6-acetyllysine Ref.27
Modified residue6111Phosphotyrosine; by ABL1 Ref.31
Modified residue7921Phosphotyrosine; by ABL1 Ref.31
Modified residue8461Phosphotyrosine; by ABL1 Ref.31
Modified residue14381Phosphoserine Ref.22 Ref.24
Modified residue14491Phosphotyrosine; by ABL1 Ref.31
Modified residue15751Phosphotyrosine; by ABL1 Ref.31
Modified residue16351Phosphotyrosine; by ABL1 Ref.31
Modified residue17601Phosphoserine By similarity
Modified residue17761Phosphoserine By similarity
Disulfide bond182 ↔ 233 By similarity
Disulfide bond435 ↔ 487 By similarity
Disulfide bond535 ↔ 583 By similarity
Disulfide bond742 ↔ 805 By similarity
Disulfide bond1119 ↔ 1170 By similarity
Disulfide bond1830 ↔ 1882 By similarity

Natural variations

Alternative sequence1 – 17601760Missing in isoform 6 and isoform 8.
VSP_018846
Alternative sequence1 – 12001200Missing in isoform 7.
VSP_053791
Alternative sequence1 – 922922Missing in isoform 5 and isoform 9.
VSP_018845
Alternative sequence437 – 50670VSGIP…LQVER → G in isoform 2 and isoform 3B.
VSP_004791
Alternative sequence1473 – 154573Missing in isoform 4.
VSP_004793
Alternative sequence1655 – 170551Missing in isoform 3A and isoform 3B.
VSP_004794
Alternative sequence17901Missing in isoform Del-1790, isoform 8 and isoform 9.
VSP_004795
Natural variant211P → H.
Corresponds to variant rs28497577 [ dbSNP | Ensembl ].
VAR_057106
Natural variant1281A → V. Ref.40
Corresponds to variant rs143896146 [ dbSNP | Ensembl ].
VAR_065570
Natural variant1331Q → H. Ref.40
Corresponds to variant rs140148380 [ dbSNP | Ensembl ].
VAR_065571
Natural variant1601P → R. Ref.40
Corresponds to variant rs111256888 [ dbSNP | Ensembl ].
VAR_065572
Natural variant2611V → A. Ref.39
Corresponds to variant rs3796164 [ dbSNP | Ensembl ].
VAR_040847
Natural variant2761T → A. Ref.39
VAR_040848
Natural variant3361P → L.
Corresponds to variant rs35912339 [ dbSNP | Ensembl ].
VAR_057107
Natural variant3781R → H. Ref.39
VAR_040849
Natural variant4051M → V. Ref.39
Corresponds to variant rs35436690 [ dbSNP | Ensembl ].
VAR_040850
Natural variant4431P → S. Ref.39
Corresponds to variant rs35156360 [ dbSNP | Ensembl ].
VAR_040851
Natural variant6071R → G. Ref.39
VAR_040852
Natural variant6521P → A. Ref.39
VAR_040853
Natural variant6561W → C. Ref.39 Ref.40
Corresponds to variant rs138172035 [ dbSNP | Ensembl ].
VAR_040854
Natural variant6921T → M. Ref.39
VAR_040855
Natural variant7011A → T. Ref.39
Corresponds to variant rs142835596 [ dbSNP | Ensembl ].
VAR_040856
Natural variant7091V → M. Ref.39
VAR_040857
Natural variant8451R → C.
Corresponds to variant rs3732485 [ dbSNP | Ensembl ].
VAR_057108
Natural variant8611L → P.
Corresponds to variant rs3732486 [ dbSNP | Ensembl ].
VAR_019986
Natural variant8771V → M.
Corresponds to variant rs34542174 [ dbSNP | Ensembl ].
VAR_057109
Natural variant9141D → E.
Corresponds to variant rs3732487 [ dbSNP | Ensembl ].
VAR_019987
Natural variant10851T → A. Ref.40
Corresponds to variant rs75370906 [ dbSNP | Ensembl ].
VAR_065573
Natural variant12131V → M Found in a patient with familial aortic dissections. Ref.40
VAR_065574
Natural variant13991E → K Found in a patient with familial aortic dissections. Ref.40
Corresponds to variant rs181663420 [ dbSNP | Ensembl ].
VAR_065575
Natural variant15271A → V. Ref.39
VAR_040858
Natural variant15881P → L in an ovarian mucinous carcinoma sample; somatic mutation. Ref.39
VAR_040859
Natural variant17541A → T Found in a patient with familial aortic dissections; binding to calmodulin is reduced; significant reduction in kinase activity compared to wild-type protein. Ref.40
VAR_065576
Natural variant17591S → P in AAT7; shows minimal cells endogenous expression; binding to calmodulin is abolished; 6-fold reduction in kinase activity compared to wild-type protein. Ref.40
VAR_065577

Experimental info

Mutagenesis6081K → A: Loss of acetylation and no kinase activity repression by NAA10/ARD1. Ref.27
Sequence conflict1471P → S in AAC18423. Ref.2
Sequence conflict1471P → S in AAD15922. Ref.3
Sequence conflict1471P → S in AAD15923. Ref.3
Sequence conflict1471P → S in AAR29062. Ref.6
Sequence conflict1471P → S in AAQ02673. Ref.7
Sequence conflict1471P → S in EAW79438. Ref.11
Sequence conflict1471P → S in EAW79440. Ref.11
Sequence conflict4661D → N in AAR29062. Ref.6
Sequence conflict4961L → V in AAC18423. Ref.2
Sequence conflict4961L → V in AAD15922. Ref.3
Sequence conflict4961L → V in AAR29062. Ref.6
Sequence conflict4961L → V in AAQ02673. Ref.7
Sequence conflict6811C → W in AAC18423. Ref.2
Sequence conflict6811C → W in AAD15921. Ref.3
Sequence conflict6811C → W in AAD15922. Ref.3
Sequence conflict6811C → W in AAD15923. Ref.3
Sequence conflict9331V → M in CAA59685. Ref.1
Sequence conflict9631S → P in AAD15922. Ref.3
Sequence conflict10221P → A in CAA59685. Ref.1
Sequence conflict1048 – 10503KPM → EAH in CAA59685. Ref.1
Sequence conflict1048 – 10503KPM → EAH in BAB21504. Ref.8
Sequence conflict11621P → L in AAD15922. Ref.3
Sequence conflict11621P → L in AAD15923. Ref.3
Sequence conflict12101L → P in CAA59685. Ref.1
Sequence conflict12801E → D in AAD15922. Ref.3
Sequence conflict12801E → D in AAD15923. Ref.3
Sequence conflict12841M → I in AAD15922. Ref.3
Sequence conflict12841M → I in AAD15923. Ref.3
Sequence conflict12841M → I in AAD15924. Ref.3
Sequence conflict13001A → G in CAA59685. Ref.1
Sequence conflict13161L → S in CAA59685. Ref.1
Sequence conflict13261T → S in CAA59685. Ref.1
Sequence conflict14781V → C in CAA59685. Ref.1
Sequence conflict15111S → T in AAD15922. Ref.3
Sequence conflict15111S → T in AAD15923. Ref.3
Sequence conflict15181H → P in AAR29061. Ref.6
Sequence conflict15181H → P in AAR29062. Ref.6
Sequence conflict15631I → T in CAA59685. Ref.1
Sequence conflict16091A → P in CAA59685. Ref.1
Sequence conflict16341N → I in AAR29061. Ref.6
Sequence conflict16341N → I in AAR29062. Ref.6
Sequence conflict1639 – 16402GY → D in AAD15922. Ref.3
Sequence conflict1639 – 16402GY → D in AAD15923. Ref.3
Sequence conflict1639 – 16402GY → D in AAD15924. Ref.3
Sequence conflict16391G → R in CAA59685. Ref.1
Sequence conflict16481G → R in CAA59685. Ref.1
Sequence conflict1658 – 16592LS → PF in CAA59685. Ref.1
Sequence conflict16761A → P in AAR29061. Ref.6
Sequence conflict16761A → P in AAR29062. Ref.6
Sequence conflict1710 – 17112CT → LA in CAA59685. Ref.1
Sequence conflict18971L → H in AAD15922. Ref.3
Sequence conflict18971L → H in AAD15923. Ref.3
Sequence conflict18971L → H in AAD15924. Ref.3

Secondary structure

........................................... 1914
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Non-muscle isozyme) [UniParc].

Last modified July 13, 2010. Version 4.
Checksum: 2D094E161CE2D4BA

FASTA1,914210,715
        10         20         30         40         50         60 
MGDVKLVASS HISKTSLSVD PSRVDSMPLT EAPAFILPPR NLCIKEGATA KFEGRVRGYP 

        70         80         90        100        110        120 
EPQVTWHRNG QPITSGGRFL LDCGIRGTFS LVIHAVHEED RGKYTCEATN GSGARQVTVE 

       130        140        150        160        170        180 
LTVEGSFAKQ LGQPVVSKTL GDRFSAPAVE TRPSIWGECP PKFATKLGRV VVKEGQMGRF 

       190        200        210        220        230        240 
SCKITGRPQP QVTWLKGNVP LQPSARVSVS EKNGMQVLEI HGVNQDDVGV YTCLVVNGSG 

       250        260        270        280        290        300 
KASMSAELSI QGLDSANRSF VRETKATNSD VRKEVTNVIS KESKLDSLEA AAKSKNCSSP 

       310        320        330        340        350        360 
QRGGSPPWAA NSQPQPPRES KLESCKDSPR TAPQTPVLQK TSSSITLQAA RVQPEPRAPG 

       370        380        390        400        410        420 
LGVLSPSGEE RKRPAPPRPA TFPTRQPGLG SQDVVSKAAN RRIPMEGQRD SAFPKFESKP 

       430        440        450        460        470        480 
QSQEVKENQT VKFRCEVSGI PKPEVAWFLE GTPVRRQEGS IEVYEDAGSH YLCLLKARTR 

       490        500        510        520        530        540 
DSGTYSCTAS NAQGQLSCSW TLQVERLAVM EVAPSFSSVL KDCAVIEGQD FVLQCSVRGT 

       550        560        570        580        590        600 
PVPRITWLLN GQPIQYARST CEAGVAELHI QDALPEDHGT YTCLAENALG QVSCSAWVTV 

       610        620        630        640        650        660 
HEKKSSRKSE YLLPVAPSKP TAPIFLQGLS DLKVMDGSQV TMTVQVSGNP PPEVIWLHNG 

       670        680        690        700        710        720 
NEIQESEDFH FEQRGTQHSL CIQEVFPEDT GTYTCEAWNS AGEVRTQAVL TVQEPHDGTQ 

       730        740        750        760        770        780 
PWFISKPRSV TASLGQSVLI SCAIAGDPFP TVHWLRDGKA LCKDTGHFEV LQNEDVFTLV 

       790        800        810        820        830        840 
LKKVQPWHAG QYEILLKNRV GECSCQVSLM LQNSSARALP RGREPASCED LCGGGVGADG 

       850        860        870        880        890        900 
GGSDRYGSLR PGWPARGQGW LEEEDGEDVR GVLKRRVETR QHTEEAIRQQ EVEQLDFRDL 

       910        920        930        940        950        960 
LGKKVSTKTL SEDDLKEIPA EQMDFRANLQ RQVKPKTVSE EERKVHSPQQ VDFRSVLAKK 

       970        980        990       1000       1010       1020 
GTSKTPVPEK VPPPKPATPD FRSVLGGKKK LPAENGSSSA ETLNAKAVES SKPLSNAQPS 

      1030       1040       1050       1060       1070       1080 
GPLKPVGNAK PAETLKPMGN AKPAETLKPM GNAKPDENLK SASKEELKKD VKNDVNCKRG 

      1090       1100       1110       1120       1130       1140 
HAGTTDNEKR SESQGTAPAF KQKLQDVHVA EGKKLLLQCQ VSSDPPATII WTLNGKTLKT 

      1150       1160       1170       1180       1190       1200 
TKFIILSQEG SLCSVSIEKA LPEDRGLYKC VAKNDAGQAE CSCQVTVDDA PASENTKAPE 

      1210       1220       1230       1240       1250       1260 
MKSRRPKSSL PPVLGTESDA TVKKKPAPKT PPKAAMPPQI IQFPEDQKVR AGESVELFGK 

      1270       1280       1290       1300       1310       1320 
VTGTQPITCT WMKFRKQIQE SEHMKVENSE NGSKLTILAA RQEHCGCYTL LVENKLGSRQ 

      1330       1340       1350       1360       1370       1380 
AQVNLTVVDK PDPPAGTPCA SDIRSSSLTL SWYGSSYDGG SAVQSYSIEI WDSANKTWKE 

      1390       1400       1410       1420       1430       1440 
LATCRSTSFN VQDLLPDHEY KFRVRAINVY GTSEPSQESE LTTVGEKPEE PKDEVEVSDD 

      1450       1460       1470       1480       1490       1500 
DEKEPEVDYR TVTINTEQKV SDFYDIEERL GSGKFGQVFR LVEKKTRKVW AGKFFKAYSA 

      1510       1520       1530       1540       1550       1560 
KEKENIRQEI SIMNCLHHPK LVQCVDAFEE KANIVMVLEI VSGGELFERI IDEDFELTER 

      1570       1580       1590       1600       1610       1620 
ECIKYMRQIS EGVEYIHKQG IVHLDLKPEN IMCVNKTGTR IKLIDFGLAR RLENAGSLKV 

      1630       1640       1650       1660       1670       1680 
LFGTPEFVAP EVINYEPIGY ATDMWSIGVI CYILVSGLSP FMGDNDNETL ANVTSATWDF 

      1690       1700       1710       1720       1730       1740 
DDEAFDEISD DAKDFISNLL KKDMKNRLDC TQCLQHPWLM KDTKNMEAKK LSKDRMKKYM 

      1750       1760       1770       1780       1790       1800 
ARRKWQKTGN AVRAIGRLSS MAMISGLSGR KSSTGSPTSP LNAEKLESEE DVSQAFLEAV 

      1810       1820       1830       1840       1850       1860 
AEEKPHVKPY FSKTIRDLEV VEGSAARFDC KIEGYPDPEV VWFKDDQSIR ESRHFQIDYD 

      1870       1880       1890       1900       1910 
EDGNCSLIIS DVCGDDDAKY TCKAVNSLGE ATCTAELIVE TMEEGEGEGE EEEE 

« Hide

Isoform 2 [UniParc].

Checksum: 0111D4C5A88349AB
Show »

FASTA1,845203,055
Isoform 3A [UniParc].

Checksum: A526210F1B9E546C
Show »

FASTA1,863205,059
Isoform 3B [UniParc].

Checksum: 9EE35F5BADBB0D9A
Show »

FASTA1,794197,399
Isoform 4 [UniParc].

Checksum: 23EDB48D1A11DE70
Show »

FASTA1,841202,350
Isoform Del-1790 [UniParc].

Checksum: 6D3029D5CCA13B41
Show »

FASTA1,913210,586
Isoform 5 (Smooth-muscle isozyme) [UniParc].

Checksum: 27288359F94FE260
Show »

FASTA992110,205
Isoform 6 (Telokin) [UniParc].

Checksum: 0E3B6CAD36C563EE
Show »

FASTA15416,970
Isoform 7 [UniParc].

Checksum: 5C3E8AD06D8B855D
Show »

FASTA71480,410
Isoform 8 [UniParc].

Checksum: BF1292FFEB166F7B
Show »

FASTA15316,840
Isoform 9 [UniParc].

Checksum: BCFD66306197E14C
Show »

FASTA991110,076

References

« Hide 'large scale' references
[1]"The human myosin light chain kinase (MLCK) from hippocampus: cloning, sequencing, expression, and localization to 3qcen-q21."
Potier M.-C., Chelot E., Pekarsky Y., Gardiner K., Rossier J., Turnell W.G.
Genomics 29:562-570(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 9), TISSUE SPECIFICITY.
Tissue: Hippocampus.
[2]"Myosin light chain kinase in endothelium: molecular cloning and regulation."
Garcia J.G.N., Lazar V.L., Gilbert-Mcclain L.I., Gallagher P.J., Verin A.D.
Am. J. Respir. Cell Mol. Biol. 16:489-494(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Umbilical vein endothelial cell.
[3]"A single human myosin light chain kinase gene (MLCK; MYLK)."
Lazar V.L., Garcia J.G.N.
Genomics 57:256-267(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3A AND 3B), NUCLEOTIDE SEQUENCE [MRNA] OF 1281-1914 (ISOFORM 4).
Tissue: Umbilical vein.
[4]"Differential regulation of alternatively spliced endothelial cell myosin light chain kinase isoforms by p60(Src)."
Birukov K.G., Csortos C., Marzilli L., Dudek S., Ma S.-F., Bresnick A.R., Verin A.D., Cotter R.J., Garcia J.G.N.
J. Biol. Chem. 276:8567-8573(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF 457-476 AND 968-985, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, PHOSPHORYLATION AT TYR-464 AND TYR-471, CALMODULIN-BINDING, ENZYME REGULATION.
[5]"Analysis of the kinase-related protein gene found at human chromosome 3q21 in a multi-gene cluster: organization, expression, alternative splicing and polymorphic marker."
Watterson D.M., Schavocky J.P., Guo L., Weiss C., Chlenski A., Shrinsky V.P., Van Eldik L.J., Haiech J.
J. Cell. Biochem. 75:481-491(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 8), NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1614-1914 (ISOFORM 9/DEL-1790), TISSUE SPECIFICITY.
Tissue: Lung and Placenta.
[6]"A differentiation-dependent splice variant of myosin light chain kinase, MLCK1, regulates epithelial tight junction permeability."
Clayburgh D.R., Rosen S., Witkowski E.D., Wang F., Blair S., Dudek S., Garcia J.G., Alverdy J.C., Turner J.R.
J. Biol. Chem. 279:55506-55513(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
Tissue: Intestinal epithelium.
[7]"The N-terminus of the long MLCK induces a disruption in normal spindle morphology and metaphase arrest."
Dulyaninova N.G., Patskovsky Y.V., Bresnick A.R.
J. Cell Sci. 117:1481-1493(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION IN CELL CYCLE, SUBCELLULAR LOCATION.
Tissue: Cervix carcinoma.
[8]"HeLa myosin light chain kinase."
Kikuchi A., Murata-Hori M., Hosoya H.
Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
Tissue: Cervix carcinoma.
[9]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 6; 7 AND 8).
Tissue: Testis.
[10]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]Mural R.J., Istrail S., Sutton 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].
[12]"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] (ISOFORMS 6 AND 8).
[13]Watterson D.M.
Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1456-1914 (ISOFORM 9/DEL-1790).
Tissue: Placenta.
[14]"Novel interaction of cortactin with endothelial cell myosin light chain kinase."
Dudek S.M., Birukov K.G., Zhan X., Garcia J.G.N.
Biochem. Biophys. Res. Commun. 298:511-519(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CTTN, PHOSPHORYLATION AT TYR-464 AND TYR-471 BY SRC.
[15]"Myosin light chain kinase modulates hypotonicity-induced Ca2+ entry and Cl- channel activity in human cervical cancer cells."
Shen M.-R., Furla P., Chou C.-Y., Ellory J.C.
Pflugers Arch. 444:276-285(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN HYPOTONICITY RESPONSE, ENZYME REGULATION.
[16]"Quantitative measurements of Ca(2+)/calmodulin binding and activation of myosin light chain kinase in cells."
Geguchadze R., Zhi G., Lau K.S., Isotani E., Persechini A., Kamm K.E., Stull J.T.
FEBS Lett. 557:121-124(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION BY CALCIUM.
[17]"Distinct temporal-spatial roles for rho kinase and myosin light chain kinase in epithelial purse-string wound closure."
Russo J.M., Florian P., Shen L., Graham W.V., Tretiakova M.S., Gitter A.H., Mrsny R.J., Turner J.R.
Gastroenterology 128:987-1001(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN WOUND HEALING.
[18]"Tumor necrosis factor-induced long myosin light chain kinase transcription is regulated by differentiation-dependent signaling events. Characterization of the human long myosin light chain kinase promoter."
Graham W.V., Wang F., Clayburgh D.R., Cheng J.X., Yoon B., Wang Y., Lin A., Turner J.R.
J. Biol. Chem. 281:26205-26215(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY TNF, TISSUE SPECIFICITY.
[19]"Myosin light chain kinase plays a role in the regulation of epithelial cell survival."
Connell L.E., Helfman D.M.
J. Cell Sci. 119:2269-2281(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN EPITHELIAL CELL SURVIVAL, ENZYME REGULATION.
[20]"Ca2+-calmodulin-dependent myosin light chain kinase is essential for activation of TRPC5 channels expressed in HEK293 cells."
Shimizu S., Yoshida T., Wakamori M., Ishii M., Okada T., Takahashi M., Seto M., Sakurada K., Kiuchi Y., Mori Y.
J. Physiol. (Lond.) 570:219-235(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN TRPC5 REGULATION, ENZYME REGULATION.
[21]"Myosin light-chain kinase contributes to the proliferation and migration of breast cancer cells through cross-talk with activated ERK1/2."
Zhou X., Liu Y., You J., Zhang H., Zhang X., Ye L.
Cancer Lett. 270:312-327(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELL MIGRATION.
[22]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1438, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[23]"Nonmuscle myosin light-chain kinase mediates neutrophil transmigration in sepsis-induced lung inflammation by activating beta2 integrins."
Xu J., Gao X.-P., Ramchandran R., Zhao Y.-Y., Vogel S.M., Malik A.B.
Nat. Immunol. 9:880-886(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS PTK2B/PYK2 KINASE, INTERACTION WITH PTK2B/PYK2.
[24]"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1438, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[25]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[26]"Androgens down-regulate myosin light chain kinase in human prostate cancer cells."
Leveille N., Fournier A., Labrie C.
J. Steroid Biochem. Mol. Biol. 114:174-179(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY ANDROGENS.
[27]"Arrest defective-1 controls tumor cell behavior by acetylating myosin light chain kinase."
Shin D.H., Chun Y.-S., Lee K.-H., Shin H.-W., Park J.-W.
PLoS ONE 4:E7451-E7451(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN TUMOR CELL MIGRATION, ACETYLATION AT LYS-608 BY NAA10/ARD1, INTERACTION WITH NAA10/ARD1, MUTAGENESIS OF LYS-608.
[28]"Myosin light chain kinase is responsible for high proliferative ability of breast cancer cells via anti-apoptosis involving p38 pathway."
Cui W.-J., Liu Y., Zhou X.-L., Wang F.-Z., Zhang X.-D., Ye L.-H.
Acta Pharmacol. Sin. 31:725-732(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN BREAST CANCER.
[29]"Modulation of factors affecting optic nerve head astrocyte migration."
Miao H., Crabb A.W., Hernandez M.R., Lukas T.J.
Invest. Ophthalmol. Vis. Sci. 51:4096-4103(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN OPTIC NERVE HEAD ASTROCYTE MIGRATION.
[30]"Quantitative distribution and colocalization of non-muscle myosin light chain kinase isoforms and cortactin in human lung endothelium."
Brown M., Adyshev D., Bindokas V., Moitra J., Garcia J.G.N., Dudek S.M.
Microvasc. Res. 80:75-88(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, INTERACTION WITH CTTN, SUBCELLULAR LOCATION.
[31]"Abl tyrosine kinase phosphorylates nonmuscle Myosin light chain kinase to regulate endothelial barrier function."
Dudek S.M., Chiang E.T., Camp S.M., Guo Y., Zhao J., Brown M.E., Singleton P.A., Wang L., Desai A., Arce F.T., Lal R., Van Eyk J.E., Imam S.Z., Garcia J.G.N.
Mol. Biol. Cell 21:4042-4056(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-231; TYR-464; TYR-556; TYR-611; TYR-792; TYR-846; TYR-1449; TYR-1575 AND TYR-1635 BY ABL1, INTERACTION WITH CTTN AND ABL1.
[32]"The angiotensin II type 1 receptor induces membrane blebbing by coupling to Rho A, Rho kinase, and myosin light chain kinase."
Godin C.M., Ferguson S.S.G.
Mol. Pharmacol. 77:903-911(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN MEMBRANE BLEBBING.
[33]"Non-muscle myosin light chain kinase isoform is a viable molecular target in acute inflammatory lung injury."
Mirzapoiazova T., Moitra J., Moreno-Vinasco L., Sammani S., Turner J.R., Chiang E.T., Evenoski C., Wang T., Singleton P.A., Huang Y., Lussier Y.A., Watterson D.M., Dudek S.M., Garcia J.G.N.
Am. J. Respir. Cell Mol. Biol. 44:40-52(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN INFLAMMATORY RESPONSE.
[34]"Organometallic pyridylnaphthalimide complexes as protein kinase inhibitors."
Blanck S., Cruchter T., Vultur A., Riedel R., Harms K., Herlyn M., Meggers E.
Organometallics 30:4598-4606(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION.
[35]"Myosin, transgelin, and myosin light chain kinase: expression and function in asthma."
Leguillette R., Laviolette M., Bergeron C., Zitouni N., Kogut P., Solway J., Kachmar L., Hamid Q., Lauzon A.-M.
Am. J. Respir. Crit. Care Med. 179:194-204(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON ASTHMA, INDUCTION BY ASTHMA.
[36]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[37]"Solution structure of the eighth Ig-like domain of human myosin light chain kinase."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2005) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 1238-1338.
[38]"A coupled equilibrium shift mechanism in calmodulin-mediated signal transduction."
Gsponer J., Christodoulou J., Cavalli A., Bui J.M., Richter B., Dobson C.M., Vendruscolo M.
Structure 16:736-746(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1742-1760 IN COMPLEX WITH CALMODULIN.
[39]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] ALA-261; ALA-276; HIS-378; VAL-405; SER-443; GLY-607; ALA-652; CYS-656; MET-692; THR-701; MET-709; VAL-1527 AND LEU-1588.
[40]"Mutations in myosin light chain kinase cause familial aortic dissections."
Wang L., Guo D.C., Cao J., Gong L., Kamm K.E., Regalado E., Li L., Shete S., He W.Q., Zhu M.S., Offermanns S., Gilchrist D., Elefteriades J., Stull J.T., Milewicz D.M.
Am. J. Hum. Genet. 87:701-707(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AAT7 PRO-1759, VARIANTS VAL-128; HIS-133; ARG-160; CYS-656; ALA-1085; MET-1213; LYS-1399 AND THR-1754, CHARACTERIZATION OF VARIANT AAT7 PRO-1759, CHARACTERIZATION OF VARIANT THR-1754.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X85337 mRNA. Translation: CAA59685.1.
U48959 mRNA. Translation: AAC18423.2.
AF069601 mRNA. Translation: AAD15921.2.
AF069602 mRNA. Translation: AAD15922.1. Frameshift.
AF069603 mRNA. Translation: AAD15923.1. Frameshift.
AF069604 mRNA. Translation: AAD15924.1. Frameshift.
AF096771 expand/collapse EMBL AC list , AF096766, AF096767, AF096768, AF096769, AF096770 Genomic DNA. Translation: AAD51380.1.
AF096771, AF096769, AF096770 Genomic DNA. Translation: AAD51381.1.
AF096773 mRNA. Translation: AAD54017.1.
AF096774 mRNA. Translation: AAD54018.1.
AF096775 mRNA. Translation: AAD54019.1.
AY424269 mRNA. Translation: AAR29061.1.
AY424270 mRNA. Translation: AAR29062.1.
AY339601 mRNA. Translation: AAQ02673.1.
AB037663 mRNA. Translation: BAB21504.1.
AK300610 mRNA. Translation: BAG62305.1.
AK314412 mRNA. Translation: BAG37033.1.
AK314443 mRNA. Translation: BAG37052.1.
AC020634 Genomic DNA. No translation available.
AC023165 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW79438.1.
CH471052 Genomic DNA. Translation: EAW79439.1.
CH471052 Genomic DNA. Translation: EAW79440.1.
CH471052 Genomic DNA. Translation: EAW79441.1.
BC100761 mRNA. Translation: AAI00762.2.
BC100762 mRNA. Translation: AAI00763.2.
BC100763 mRNA. Translation: AAI00764.2.
BC064420 mRNA. Translation: AAH64420.2.
X90870 mRNA. Translation: CAA62378.1.
CCDSCCDS3023.1. [Q15746-3]
CCDS43141.1. [Q15746-2]
CCDS46896.1. [Q15746-1]
CCDS46897.1. [Q15746-8]
RefSeqNP_444253.3. NM_053025.3. [Q15746-1]
NP_444254.3. NM_053026.3. [Q15746-2]
NP_444255.3. NM_053027.3. [Q15746-3]
NP_444256.3. NM_053028.3. [Q15746-4]
NP_444259.1. NM_053031.2. [Q15746-10]
NP_444260.1. NM_053032.2. [Q15746-8]
UniGeneHs.477375.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CQVNMR-A1238-1338[»]
2K0FNMR-B1742-1760[»]
2YR3NMR-A510-601[»]
ProteinModelPortalQ15746.
SMRQ15746. Positions 510-601, 1238-1338, 1801-1902.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110722. 10 interactions.
IntActQ15746. 10 interactions.
MINTMINT-2807402.

Chemistry

BindingDBQ15746.
ChEMBLCHEMBL2428.
GuidetoPHARMACOLOGY1552.

Protein family/group databases

MEROPSI43.001.

PTM databases

PhosphoSiteQ15746.

Polymorphism databases

DMDM300669714.

Proteomic databases

MaxQBQ15746.
PaxDbQ15746.
PRIDEQ15746.

Protocols and materials databases

DNASU4638.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000346322; ENSP00000320622; ENSG00000065534. [Q15746-2]
ENST00000354792; ENSP00000346846; ENSG00000065534.
ENST00000359169; ENSP00000352088; ENSG00000065534. [Q15746-3]
ENST00000360304; ENSP00000353452; ENSG00000065534. [Q15746-1]
ENST00000360772; ENSP00000354004; ENSG00000065534. [Q15746-3]
ENST00000418370; ENSP00000428967; ENSG00000065534. [Q15746-8]
ENST00000475616; ENSP00000418335; ENSG00000065534. [Q15746-1]
ENST00000578202; ENSP00000463691; ENSG00000065534.
ENST00000583087; ENSP00000462118; ENSG00000065534. [Q15746-8]
GeneID4638.
KEGGhsa:4638.
UCSCuc003egl.3. human. [Q15746-8]
uc003ego.3. human. [Q15746-1]
uc003egp.3. human. [Q15746-2]
uc003egq.3. human. [Q15746-3]
uc003egr.3. human. [Q15746-4]
uc011bjw.2. human. [Q15746-6]

Organism-specific databases

CTD4638.
GeneCardsGC03M123281.
GeneReviewsMYLK.
HGNCHGNC:7590. MYLK.
HPACAB009628.
CAB020789.
HPA031677.
MIM600922. gene.
613780. phenotype.
neXtProtNX_Q15746.
Orphanet91387. Familial thoracic aortic aneurysm and aortic dissection.
PharmGKBPA31388.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000049287.
HOVERGENHBG052551.
InParanoidQ15746.
KOK00907.
OMAKFIILSQ.
OrthoDBEOG7WQ7RC.
PhylomeDBQ15746.
TreeFamTF314166.

Enzyme and pathway databases

BRENDA2.7.11.18. 2681.
ReactomeREACT_17044. Muscle contraction.
SignaLinkQ15746.

Gene expression databases

ArrayExpressQ15746.
BgeeQ15746.
GenevestigatorQ15746.

Family and domain databases

Gene3D2.60.40.10. 10 hits.
InterProIPR003961. Fibronectin_type3.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR011009. Kinase-like_dom.
IPR020675. Myosin_light_ch_kinase-rel.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR015725. Telokin/Myosin_light_ch_kin.
[Graphical view]
PANTHERPTHR22964. PTHR22964. 1 hit.
PTHR22964:SF44. PTHR22964:SF44. 1 hit.
PfamPF00041. fn3. 1 hit.
PF07679. I-set. 9 hits.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00060. FN3. 1 hit.
SM00409. IG. 1 hit.
SM00408. IGc2. 8 hits.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF49265. SSF49265. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS50853. FN3. 1 hit.
PS50835. IG_LIKE. 9 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMYLK. human.
EvolutionaryTraceQ15746.
GeneWikiMYLK.
GenomeRNAi4638.
NextBio17860.
PROQ15746.
SOURCESearch...

Entry information

Entry nameMYLK_HUMAN
AccessionPrimary (citable) accession number: Q15746
Secondary accession number(s): B4DUE3 expand/collapse secondary AC list , D3DN97, O95796, O95797, O95798, O95799, Q14844, Q16794, Q17S15, Q3ZCP9, Q5MY99, Q5MYA0, Q6P2N0, Q7Z4J0, Q9C0L5, Q9UBG5, Q9UBY6, Q9UIT9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 13, 2010
Last modified: July 9, 2014
This is version 160 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

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM