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Q15746

- MYLK_HUMAN

UniProt

Q15746 - MYLK_HUMAN

Protein

Myosin light chain kinase, smooth muscle

Gene

MYLK

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 162 (01 Oct 2014)
      Sequence version 4 (13 Jul 2010)
      Previous versions | rss
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    Functioni

    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.13 Publications

    Catalytic activityi

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

    Cofactori

    Magnesium.
    Calcium.

    Enzyme regulationi

    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-9.6 Publications

    Kineticsi

    1. KM=6.5 µM for MLC (isoform 1 at 22 degrees Celsius)1 Publication
    2. KM=7.2 µM for MLC (isoform 2 at 22 degrees Celsius)1 Publication

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

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei1493 – 14931ATPPROSITE-ProRule annotation
    Active sitei1585 – 15851Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi1470 – 14789ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. calmodulin-dependent protein kinase activity Source: RefGenome
    3. metal ion binding Source: UniProtKB-KW
    4. myosin light chain kinase activity Source: UniProtKB
    5. protein binding Source: IntAct

    GO - Biological processi

    1. actin filament organization Source: RefGenome
    2. aorta smooth muscle tissue morphogenesis Source: BHF-UCL
    3. bleb assembly Source: UniProtKB
    4. cellular hypotonic response Source: UniProtKB
    5. muscle contraction Source: Reactome
    6. positive regulation of calcium ion transport Source: UniProtKB
    7. positive regulation of cell migration Source: UniProtKB
    8. positive regulation of wound healing Source: UniProtKB
    9. protein phosphorylation Source: ProtInc
    10. smooth muscle contraction Source: UniProtKB
    11. tonic smooth muscle contraction Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    Actin-binding, ATP-binding, Calcium, Calmodulin-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.18. 2681.
    ReactomeiREACT_20558. Smooth Muscle Contraction.
    SignaLinkiQ15746.

    Protein family/group databases

    MEROPSiI43.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Myosin light chain kinase, smooth muscle (EC:2.7.11.18)
    Short name:
    MLCK
    Short name:
    smMLCK
    Alternative name(s):
    Kinase-related protein
    Short name:
    KRP
    Telokin
    Cleaved into the following chain:
    Gene namesi
    Name:MYLK
    Synonyms:MLCK, MLCK1, MYLK1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:7590. MYLK.

    Subcellular locationi

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

    GO - Cellular componenti

    1. cleavage furrow Source: UniProtKB
    2. cytoplasm Source: UniProtKB
    3. cytosol Source: Reactome
    4. extracellular vesicular exosome Source: UniProt
    5. lamellipodium Source: UniProtKB
    6. stress fiber Source: UniProtKB

    Keywords - Cellular componenti

    Cell projection, Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Involvement in diseasei

    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1759 – 17591S → P in AAT7; shows minimal cells endogenous expression; binding to calmodulin is abolished; 6-fold reduction in kinase activity compared to wild-type protein. 1 Publication
    VAR_065577

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi608 – 6081K → A: Loss of acetylation and no kinase activity repression by NAA10/ARD1. 1 Publication

    Keywords - Diseasei

    Aortic aneurysm, Disease mutation

    Organism-specific databases

    MIMi613780. phenotype.
    Orphaneti91387. Familial thoracic aortic aneurysm and aortic dissection.
    PharmGKBiPA31388.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 19141914Myosin light chain kinase, smooth musclePRO_0000024354Add
    BLAST
    Chaini1 – 19101910Myosin light chain kinase, smooth muscle, deglutamylated formBy similarityPRO_0000403731Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi182 ↔ 233PROSITE-ProRule annotation
    Modified residuei231 – 2311Phosphotyrosine; by ABL11 Publication
    Modified residuei365 – 3651PhosphoserineBy similarity
    Disulfide bondi435 ↔ 487PROSITE-ProRule annotation
    Modified residuei464 – 4641Phosphotyrosine; by ABL1 and SRC3 Publications
    Modified residuei471 – 4711Phosphotyrosine; by SRC2 Publications
    Disulfide bondi535 ↔ 583PROSITE-ProRule annotation
    Modified residuei556 – 5561Phosphotyrosine; by ABL11 Publication
    Modified residuei608 – 6081N6-acetyllysine1 Publication
    Modified residuei611 – 6111Phosphotyrosine; by ABL11 Publication
    Disulfide bondi742 ↔ 805PROSITE-ProRule annotation
    Modified residuei792 – 7921Phosphotyrosine; by ABL11 Publication
    Modified residuei846 – 8461Phosphotyrosine; by ABL11 Publication
    Disulfide bondi1119 ↔ 1170PROSITE-ProRule annotation
    Modified residuei1438 – 14381Phosphoserine2 Publications
    Modified residuei1449 – 14491Phosphotyrosine; by ABL11 Publication
    Modified residuei1575 – 15751Phosphotyrosine; by ABL11 Publication
    Modified residuei1635 – 16351Phosphotyrosine; by ABL11 Publication
    Modified residuei1760 – 17601PhosphoserineBy similarity
    Modified residuei1776 – 17761PhosphoserineBy similarity
    Disulfide bondi1830 ↔ 1882PROSITE-ProRule annotation

    Post-translational modificationi

    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.5 Publications
    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.By similarity
    Acetylated at Lys-608 by NAA10/ARD1 via a calcium-dependent signaling; this acetylation represses kinase activity and reduces tumor cell migration.1 Publication

    Keywords - PTMi

    Acetylation, Disulfide bond, Phosphoprotein

    Proteomic databases

    MaxQBiQ15746.
    PaxDbiQ15746.
    PRIDEiQ15746.

    PTM databases

    PhosphoSiteiQ15746.

    Expressioni

    Tissue specificityi

    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).4 Publications

    Inductioni

    Accumulates in individuals with asthma (at protein levels). Induced by tumor necrosis factor (TNF). Repressed by androgens (e.g. R1881).3 Publications

    Gene expression databases

    ArrayExpressiQ15746.
    BgeeiQ15746.
    GenevestigatoriQ15746.

    Organism-specific databases

    HPAiCAB009628.
    CAB020789.
    HPA031677.

    Interactioni

    Subunit structurei

    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.By similarity6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NCK1P163332EBI-968482,EBI-389883

    Protein-protein interaction databases

    BioGridi110722. 10 interactions.
    IntActiQ15746. 11 interactions.
    MINTiMINT-2807402.

    Structurei

    Secondary structure

    1
    1914
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi512 – 5187
    Beta strandi523 – 5264
    Beta strandi531 – 5344
    Beta strandi536 – 5416
    Beta strandi546 – 5538
    Beta strandi560 – 5623
    Beta strandi565 – 5706
    Beta strandi581 – 5866
    Beta strandi591 – 5955
    Beta strandi598 – 6014
    Beta strandi1239 – 12413
    Beta strandi1246 – 12505
    Beta strandi1255 – 126612
    Beta strandi1268 – 127710
    Beta strandi1281 – 12888
    Beta strandi1290 – 12978
    Turni1302 – 13043
    Beta strandi1306 – 13138
    Beta strandi1318 – 13203
    Beta strandi1323 – 13286
    Helixi1743 – 175917

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CQVNMR-A1238-1338[»]
    2K0FNMR-B1742-1760[»]
    2YR3NMR-A510-601[»]
    ProteinModelPortaliQ15746.
    SMRiQ15746. Positions 510-601, 1238-1338, 1801-1902.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ15746.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini33 – 12290Ig-like C2-type 1Add
    BLAST
    Domaini161 – 24989Ig-like C2-type 2Add
    BLAST
    Domaini414 – 50390Ig-like C2-type 3Add
    BLAST
    Domaini514 – 59986Ig-like C2-type 4Add
    BLAST
    Domaini620 – 71192Ig-like C2-type 5Add
    BLAST
    Domaini721 – 821101Ig-like C2-type 6Add
    BLAST
    Repeati868 – 895281-1Add
    BLAST
    Repeati896 – 923281-2Add
    BLAST
    Repeati924 – 951281-3Add
    BLAST
    Repeati952 – 979281-4Add
    BLAST
    Repeati980 – 998191-5; truncatedAdd
    BLAST
    Repeati999 – 100352-1; truncated
    Repeati1004 – 1015122-2Add
    BLAST
    Repeati1016 – 1027122-3Add
    BLAST
    Repeati1028 – 1039122-4Add
    BLAST
    Repeati1040 – 1051122-5Add
    BLAST
    Repeati1052 – 1063122-6Add
    BLAST
    Domaini1098 – 118689Ig-like C2-type 7Add
    BLAST
    Domaini1238 – 132689Ig-like C2-type 8Add
    BLAST
    Domaini1334 – 142693Fibronectin type-IIIPROSITE-ProRule annotationAdd
    BLAST
    Domaini1464 – 1719256Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini1809 – 189890Ig-like C2-type 9Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni868 – 9981315 X 28 AA approximate tandem repeatsAdd
    BLAST
    Regioni923 – 96341Actin-binding (calcium/calmodulin-sensitive)By similarityAdd
    BLAST
    Regioni948 – 96316Calmodulin-bindingBy similarityAdd
    BLAST
    Regioni999 – 1063656 X 12 AA approximate tandem repeatsAdd
    BLAST
    Regioni1061 – 1460400Actin-binding (calcium/calmodulin-insensitive)By similarityAdd
    BLAST
    Regioni1711 – 177464Calmodulin-bindingAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1906 – 19149Poly-Glu

    Sequence similaritiesi

    Contains 1 fibronectin type-III domain.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Immunoglobulin domain, Repeat

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000049287.
    HOVERGENiHBG052551.
    InParanoidiQ15746.
    KOiK00907.
    OMAiKFIILSQ.
    OrthoDBiEOG7WQ7RC.
    PhylomeDBiQ15746.
    TreeFamiTF314166.

    Family and domain databases

    Gene3Di2.60.40.10. 10 hits.
    InterProiIPR003961. 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]
    PANTHERiPTHR22964. PTHR22964. 1 hit.
    PTHR22964:SF44. PTHR22964:SF44. 1 hit.
    PfamiPF00041. fn3. 1 hit.
    PF07679. I-set. 9 hits.
    PF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00060. FN3. 1 hit.
    SM00409. IG. 1 hit.
    SM00408. IGc2. 8 hits.
    SM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF49265. SSF49265. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS50853. 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]

    Sequences (11)i

    Sequence statusi: Complete.

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

    This entry describes 11 isoformsi produced by alternative splicing and alternative initiation. Align

    Note: Additional isoforms seem to exist.

    Isoform 1 (identifier: Q15746-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MGDVKLVASS HISKTSLSVD PSRVDSMPLT EAPAFILPPR NLCIKEGATA     50
    KFEGRVRGYP EPQVTWHRNG QPITSGGRFL LDCGIRGTFS LVIHAVHEED 100
    RGKYTCEATN GSGARQVTVE LTVEGSFAKQ LGQPVVSKTL GDRFSAPAVE 150
    TRPSIWGECP PKFATKLGRV VVKEGQMGRF SCKITGRPQP QVTWLKGNVP 200
    LQPSARVSVS EKNGMQVLEI HGVNQDDVGV YTCLVVNGSG KASMSAELSI 250
    QGLDSANRSF VRETKATNSD VRKEVTNVIS KESKLDSLEA AAKSKNCSSP 300
    QRGGSPPWAA NSQPQPPRES KLESCKDSPR TAPQTPVLQK TSSSITLQAA 350
    RVQPEPRAPG LGVLSPSGEE RKRPAPPRPA TFPTRQPGLG SQDVVSKAAN 400
    RRIPMEGQRD SAFPKFESKP QSQEVKENQT VKFRCEVSGI PKPEVAWFLE 450
    GTPVRRQEGS IEVYEDAGSH YLCLLKARTR DSGTYSCTAS NAQGQLSCSW 500
    TLQVERLAVM EVAPSFSSVL KDCAVIEGQD FVLQCSVRGT PVPRITWLLN 550
    GQPIQYARST CEAGVAELHI QDALPEDHGT YTCLAENALG QVSCSAWVTV 600
    HEKKSSRKSE YLLPVAPSKP TAPIFLQGLS DLKVMDGSQV TMTVQVSGNP 650
    PPEVIWLHNG NEIQESEDFH FEQRGTQHSL CIQEVFPEDT GTYTCEAWNS 700
    AGEVRTQAVL TVQEPHDGTQ PWFISKPRSV TASLGQSVLI SCAIAGDPFP 750
    TVHWLRDGKA LCKDTGHFEV LQNEDVFTLV LKKVQPWHAG QYEILLKNRV 800
    GECSCQVSLM LQNSSARALP RGREPASCED LCGGGVGADG GGSDRYGSLR 850
    PGWPARGQGW LEEEDGEDVR GVLKRRVETR QHTEEAIRQQ EVEQLDFRDL 900
    LGKKVSTKTL SEDDLKEIPA EQMDFRANLQ RQVKPKTVSE EERKVHSPQQ 950
    VDFRSVLAKK GTSKTPVPEK VPPPKPATPD FRSVLGGKKK LPAENGSSSA 1000
    ETLNAKAVES SKPLSNAQPS GPLKPVGNAK PAETLKPMGN AKPAETLKPM 1050
    GNAKPDENLK SASKEELKKD VKNDVNCKRG HAGTTDNEKR SESQGTAPAF 1100
    KQKLQDVHVA EGKKLLLQCQ VSSDPPATII WTLNGKTLKT TKFIILSQEG 1150
    SLCSVSIEKA LPEDRGLYKC VAKNDAGQAE CSCQVTVDDA PASENTKAPE 1200
    MKSRRPKSSL PPVLGTESDA TVKKKPAPKT PPKAAMPPQI IQFPEDQKVR 1250
    AGESVELFGK VTGTQPITCT WMKFRKQIQE SEHMKVENSE NGSKLTILAA 1300
    RQEHCGCYTL LVENKLGSRQ AQVNLTVVDK PDPPAGTPCA SDIRSSSLTL 1350
    SWYGSSYDGG SAVQSYSIEI WDSANKTWKE LATCRSTSFN VQDLLPDHEY 1400
    KFRVRAINVY GTSEPSQESE LTTVGEKPEE PKDEVEVSDD DEKEPEVDYR 1450
    TVTINTEQKV SDFYDIEERL GSGKFGQVFR LVEKKTRKVW AGKFFKAYSA 1500
    KEKENIRQEI SIMNCLHHPK LVQCVDAFEE KANIVMVLEI VSGGELFERI 1550
    IDEDFELTER ECIKYMRQIS EGVEYIHKQG IVHLDLKPEN IMCVNKTGTR 1600
    IKLIDFGLAR RLENAGSLKV LFGTPEFVAP EVINYEPIGY ATDMWSIGVI 1650
    CYILVSGLSP FMGDNDNETL ANVTSATWDF DDEAFDEISD DAKDFISNLL 1700
    KKDMKNRLDC TQCLQHPWLM KDTKNMEAKK LSKDRMKKYM ARRKWQKTGN 1750
    AVRAIGRLSS MAMISGLSGR KSSTGSPTSP LNAEKLESEE DVSQAFLEAV 1800
    AEEKPHVKPY FSKTIRDLEV VEGSAARFDC KIEGYPDPEV VWFKDDQSIR 1850
    ESRHFQIDYD EDGNCSLIIS DVCGDDDAKY TCKAVNSLGE ATCTAELIVE 1900
    TMEEGEGEGE EEEE 1914
    Length:1,914
    Mass (Da):210,715
    Last modified:July 13, 2010 - v4
    Checksum:i2D094E161CE2D4BA
    GO
    Isoform 2 (identifier: Q15746-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         437-506: VSGIPKPEVAWFLEGTPVRRQEGSIEVYEDAGSHYLCLLKARTRDSGTYSCTASNAQGQLSCSWTLQVER → G

    Show »
    Length:1,845
    Mass (Da):203,055
    Checksum:i0111D4C5A88349AB
    GO
    Isoform 3A (identifier: Q15746-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1655-1705: Missing.

    Show »
    Length:1,863
    Mass (Da):205,059
    Checksum:iA526210F1B9E546C
    GO
    Isoform 3B (identifier: Q15746-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         437-506: VSGIPKPEVAWFLEGTPVRRQEGSIEVYEDAGSHYLCLLKARTRDSGTYSCTASNAQGQLSCSWTLQVER → G
         1655-1705: Missing.

    Show »
    Length:1,794
    Mass (Da):197,399
    Checksum:i9EE35F5BADBB0D9A
    GO
    Isoform 4 (identifier: Q15746-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1473-1545: Missing.

    Show »
    Length:1,841
    Mass (Da):202,350
    Checksum:i23EDB48D1A11DE70
    GO
    Isoform Del-1790 (identifier: Q15746-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1790-1790: Missing.

    Show »
    Length:1,913
    Mass (Da):210,586
    Checksum:i6D3029D5CCA13B41
    GO
    Isoform 5 (identifier: Q15746-7) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:992
    Mass (Da):110,205
    Checksum:i27288359F94FE260
    GO
    Isoform 6 (identifier: Q15746-8) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:154
    Mass (Da):16,970
    Checksum:i0E3B6CAD36C563EE
    GO
    Isoform 7 (identifier: Q15746-9) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1200: Missing.

    Show »
    Length:714
    Mass (Da):80,410
    Checksum:i5C3E8AD06D8B855D
    GO
    Isoform 8 (identifier: Q15746-10) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:153
    Mass (Da):16,840
    Checksum:iBF1292FFEB166F7B
    GO
    Isoform 9 (identifier: Q15746-11) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:991
    Mass (Da):110,076
    Checksum:iBCFD66306197E14C
    GO

    Sequence cautioni

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti147 – 1471P → S in AAC18423. (PubMed:9160829)Curated
    Sequence conflicti147 – 1471P → S in AAD15922. (PubMed:10198165)Curated
    Sequence conflicti147 – 1471P → S in AAD15923. (PubMed:10198165)Curated
    Sequence conflicti147 – 1471P → S in AAR29062. (PubMed:15507455)Curated
    Sequence conflicti147 – 1471P → S in AAQ02673. (PubMed:15020676)Curated
    Sequence conflicti147 – 1471P → S in EAW79438. 1 PublicationCurated
    Sequence conflicti147 – 1471P → S in EAW79440. 1 PublicationCurated
    Sequence conflicti466 – 4661D → N in AAR29062. (PubMed:15507455)Curated
    Sequence conflicti496 – 4961L → V in AAC18423. (PubMed:9160829)Curated
    Sequence conflicti496 – 4961L → V in AAD15922. (PubMed:10198165)Curated
    Sequence conflicti496 – 4961L → V in AAR29062. (PubMed:15507455)Curated
    Sequence conflicti496 – 4961L → V in AAQ02673. (PubMed:15020676)Curated
    Sequence conflicti681 – 6811C → W in AAC18423. (PubMed:9160829)Curated
    Sequence conflicti681 – 6811C → W in AAD15921. (PubMed:10198165)Curated
    Sequence conflicti681 – 6811C → W in AAD15922. (PubMed:10198165)Curated
    Sequence conflicti681 – 6811C → W in AAD15923. (PubMed:10198165)Curated
    Sequence conflicti933 – 9331V → M in CAA59685. (PubMed:8575746)Curated
    Sequence conflicti963 – 9631S → P in AAD15922. (PubMed:10198165)Curated
    Sequence conflicti1022 – 10221P → A in CAA59685. (PubMed:8575746)Curated
    Sequence conflicti1048 – 10503KPM → EAH in CAA59685. (PubMed:8575746)Curated
    Sequence conflicti1048 – 10503KPM → EAH in BAB21504. 1 PublicationCurated
    Sequence conflicti1162 – 11621P → L in AAD15922. (PubMed:10198165)Curated
    Sequence conflicti1162 – 11621P → L in AAD15923. (PubMed:10198165)Curated
    Sequence conflicti1210 – 12101L → P in CAA59685. (PubMed:8575746)Curated
    Sequence conflicti1280 – 12801E → D in AAD15922. (PubMed:10198165)Curated
    Sequence conflicti1280 – 12801E → D in AAD15923. (PubMed:10198165)Curated
    Sequence conflicti1284 – 12841M → I in AAD15922. (PubMed:10198165)Curated
    Sequence conflicti1284 – 12841M → I in AAD15923. (PubMed:10198165)Curated
    Sequence conflicti1284 – 12841M → I in AAD15924. (PubMed:10198165)Curated
    Sequence conflicti1300 – 13001A → G in CAA59685. (PubMed:8575746)Curated
    Sequence conflicti1316 – 13161L → S in CAA59685. (PubMed:8575746)Curated
    Sequence conflicti1326 – 13261T → S in CAA59685. (PubMed:8575746)Curated
    Sequence conflicti1478 – 14781V → C in CAA59685. (PubMed:8575746)Curated
    Sequence conflicti1511 – 15111S → T in AAD15922. (PubMed:10198165)Curated
    Sequence conflicti1511 – 15111S → T in AAD15923. (PubMed:10198165)Curated
    Sequence conflicti1518 – 15181H → P in AAR29061. (PubMed:15507455)Curated
    Sequence conflicti1518 – 15181H → P in AAR29062. (PubMed:15507455)Curated
    Sequence conflicti1563 – 15631I → T in CAA59685. (PubMed:8575746)Curated
    Sequence conflicti1609 – 16091A → P in CAA59685. (PubMed:8575746)Curated
    Sequence conflicti1634 – 16341N → I in AAR29061. (PubMed:15507455)Curated
    Sequence conflicti1634 – 16341N → I in AAR29062. (PubMed:15507455)Curated
    Sequence conflicti1639 – 16402GY → D in AAD15922. (PubMed:10198165)Curated
    Sequence conflicti1639 – 16402GY → D in AAD15923. (PubMed:10198165)Curated
    Sequence conflicti1639 – 16402GY → D in AAD15924. (PubMed:10198165)Curated
    Sequence conflicti1639 – 16391G → R in CAA59685. (PubMed:8575746)Curated
    Sequence conflicti1648 – 16481G → R in CAA59685. (PubMed:8575746)Curated
    Sequence conflicti1658 – 16592LS → PF in CAA59685. (PubMed:8575746)Curated
    Sequence conflicti1676 – 16761A → P in AAR29061. (PubMed:15507455)Curated
    Sequence conflicti1676 – 16761A → P in AAR29062. (PubMed:15507455)Curated
    Sequence conflicti1710 – 17112CT → LA in CAA59685. (PubMed:8575746)Curated
    Sequence conflicti1897 – 18971L → H in AAD15922. (PubMed:10198165)Curated
    Sequence conflicti1897 – 18971L → H in AAD15923. (PubMed:10198165)Curated
    Sequence conflicti1897 – 18971L → H in AAD15924. (PubMed:10198165)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti21 – 211P → H.
    Corresponds to variant rs28497577 [ dbSNP | Ensembl ].
    VAR_057106
    Natural varianti128 – 1281A → V.1 Publication
    Corresponds to variant rs143896146 [ dbSNP | Ensembl ].
    VAR_065570
    Natural varianti133 – 1331Q → H.1 Publication
    Corresponds to variant rs140148380 [ dbSNP | Ensembl ].
    VAR_065571
    Natural varianti160 – 1601P → R.1 Publication
    Corresponds to variant rs111256888 [ dbSNP | Ensembl ].
    VAR_065572
    Natural varianti261 – 2611V → A.1 Publication
    Corresponds to variant rs3796164 [ dbSNP | Ensembl ].
    VAR_040847
    Natural varianti276 – 2761T → A.1 Publication
    VAR_040848
    Natural varianti336 – 3361P → L.
    Corresponds to variant rs35912339 [ dbSNP | Ensembl ].
    VAR_057107
    Natural varianti378 – 3781R → H.1 Publication
    VAR_040849
    Natural varianti405 – 4051M → V.1 Publication
    Corresponds to variant rs35436690 [ dbSNP | Ensembl ].
    VAR_040850
    Natural varianti443 – 4431P → S.1 Publication
    Corresponds to variant rs35156360 [ dbSNP | Ensembl ].
    VAR_040851
    Natural varianti607 – 6071R → G.1 Publication
    VAR_040852
    Natural varianti652 – 6521P → A.1 Publication
    VAR_040853
    Natural varianti656 – 6561W → C.2 Publications
    Corresponds to variant rs138172035 [ dbSNP | Ensembl ].
    VAR_040854
    Natural varianti692 – 6921T → M.1 Publication
    VAR_040855
    Natural varianti701 – 7011A → T.1 Publication
    Corresponds to variant rs142835596 [ dbSNP | Ensembl ].
    VAR_040856
    Natural varianti709 – 7091V → M.1 Publication
    VAR_040857
    Natural varianti845 – 8451R → C.
    Corresponds to variant rs3732485 [ dbSNP | Ensembl ].
    VAR_057108
    Natural varianti861 – 8611L → P.
    Corresponds to variant rs3732486 [ dbSNP | Ensembl ].
    VAR_019986
    Natural varianti877 – 8771V → M.
    Corresponds to variant rs34542174 [ dbSNP | Ensembl ].
    VAR_057109
    Natural varianti914 – 9141D → E.
    Corresponds to variant rs3732487 [ dbSNP | Ensembl ].
    VAR_019987
    Natural varianti1085 – 10851T → A.1 Publication
    Corresponds to variant rs75370906 [ dbSNP | Ensembl ].
    VAR_065573
    Natural varianti1213 – 12131V → M Found in a patient with familial aortic dissections. 1 Publication
    VAR_065574
    Natural varianti1399 – 13991E → K Found in a patient with familial aortic dissections. 1 Publication
    Corresponds to variant rs181663420 [ dbSNP | Ensembl ].
    VAR_065575
    Natural varianti1527 – 15271A → V.1 Publication
    VAR_040858
    Natural varianti1588 – 15881P → L in an ovarian mucinous carcinoma sample; somatic mutation. 1 Publication
    VAR_040859
    Natural varianti1754 – 17541A → T Found in a patient with familial aortic dissections; binding to calmodulin is reduced; significant reduction in kinase activity compared to wild-type protein. 1 Publication
    VAR_065576
    Natural varianti1759 – 17591S → P in AAT7; shows minimal cells endogenous expression; binding to calmodulin is abolished; 6-fold reduction in kinase activity compared to wild-type protein. 1 Publication
    VAR_065577

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 17601760Missing in isoform 6 and isoform 8. 3 PublicationsVSP_018846Add
    BLAST
    Alternative sequencei1 – 12001200Missing in isoform 7. 1 PublicationVSP_053791Add
    BLAST
    Alternative sequencei1 – 922922Missing in isoform 5 and isoform 9. 2 PublicationsVSP_018845Add
    BLAST
    Alternative sequencei437 – 50670VSGIP…LQVER → G in isoform 2 and isoform 3B. 2 PublicationsVSP_004791Add
    BLAST
    Alternative sequencei1473 – 154573Missing in isoform 4. 1 PublicationVSP_004793Add
    BLAST
    Alternative sequencei1655 – 170551Missing in isoform 3A and isoform 3B. 1 PublicationVSP_004794Add
    BLAST
    Alternative sequencei1790 – 17901Missing in isoform Del-1790, isoform 8 and isoform 9. 4 PublicationsVSP_004795

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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
    , 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.
    CCDSiCCDS3023.1. [Q15746-3]
    CCDS43141.1. [Q15746-2]
    CCDS46896.1. [Q15746-1]
    CCDS46897.1. [Q15746-8]
    CCDS58849.1. [Q15746-10]
    RefSeqiNP_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]
    UniGeneiHs.477375.

    Genome annotation databases

    EnsembliENST00000346322; ENSP00000320622; ENSG00000065534. [Q15746-2]
    ENST00000354792; ENSP00000346846; ENSG00000065534. [Q15746-9]
    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. [Q15746-10]
    ENST00000583087; ENSP00000462118; ENSG00000065534. [Q15746-8]
    GeneIDi4638.
    KEGGihsa:4638.
    UCSCiuc003egl.3. human. [Q15746-8]
    uc003egm.3. human.
    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]

    Polymorphism databases

    DMDMi300669714.

    Keywords - Coding sequence diversityi

    Alternative initiation, Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Myosin light-chain kinase entry

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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
    , 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 .
    CCDSi CCDS3023.1. [Q15746-3 ]
    CCDS43141.1. [Q15746-2 ]
    CCDS46896.1. [Q15746-1 ]
    CCDS46897.1. [Q15746-8 ]
    CCDS58849.1. [Q15746-10 ]
    RefSeqi NP_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 ]
    UniGenei Hs.477375.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2CQV NMR - A 1238-1338 [» ]
    2K0F NMR - B 1742-1760 [» ]
    2YR3 NMR - A 510-601 [» ]
    ProteinModelPortali Q15746.
    SMRi Q15746. Positions 510-601, 1238-1338, 1801-1902.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110722. 10 interactions.
    IntActi Q15746. 11 interactions.
    MINTi MINT-2807402.

    Chemistry

    BindingDBi Q15746.
    ChEMBLi CHEMBL2428.
    GuidetoPHARMACOLOGYi 1552.

    Protein family/group databases

    MEROPSi I43.001.

    PTM databases

    PhosphoSitei Q15746.

    Polymorphism databases

    DMDMi 300669714.

    Proteomic databases

    MaxQBi Q15746.
    PaxDbi Q15746.
    PRIDEi Q15746.

    Protocols and materials databases

    DNASUi 4638.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000346322 ; ENSP00000320622 ; ENSG00000065534 . [Q15746-2 ]
    ENST00000354792 ; ENSP00000346846 ; ENSG00000065534 . [Q15746-9 ]
    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 . [Q15746-10 ]
    ENST00000583087 ; ENSP00000462118 ; ENSG00000065534 . [Q15746-8 ]
    GeneIDi 4638.
    KEGGi hsa:4638.
    UCSCi uc003egl.3. human. [Q15746-8 ]
    uc003egm.3. human.
    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

    CTDi 4638.
    GeneCardsi GC03M123281.
    GeneReviewsi MYLK.
    HGNCi HGNC:7590. MYLK.
    HPAi CAB009628.
    CAB020789.
    HPA031677.
    MIMi 600922. gene.
    613780. phenotype.
    neXtProti NX_Q15746.
    Orphaneti 91387. Familial thoracic aortic aneurysm and aortic dissection.
    PharmGKBi PA31388.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000049287.
    HOVERGENi HBG052551.
    InParanoidi Q15746.
    KOi K00907.
    OMAi KFIILSQ.
    OrthoDBi EOG7WQ7RC.
    PhylomeDBi Q15746.
    TreeFami TF314166.

    Enzyme and pathway databases

    BRENDAi 2.7.11.18. 2681.
    Reactomei REACT_20558. Smooth Muscle Contraction.
    SignaLinki Q15746.

    Miscellaneous databases

    ChiTaRSi MYLK. human.
    EvolutionaryTracei Q15746.
    GeneWikii MYLK.
    GenomeRNAii 4638.
    NextBioi 17860.
    PROi Q15746.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15746.
    Bgeei Q15746.
    Genevestigatori Q15746.

    Family and domain databases

    Gene3Di 2.60.40.10. 10 hits.
    InterProi IPR003961. 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 ]
    PANTHERi PTHR22964. PTHR22964. 1 hit.
    PTHR22964:SF44. PTHR22964:SF44. 1 hit.
    Pfami PF00041. fn3. 1 hit.
    PF07679. I-set. 9 hits.
    PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00060. FN3. 1 hit.
    SM00409. IG. 1 hit.
    SM00408. IGc2. 8 hits.
    SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49265. SSF49265. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS50853. 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 ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.
      , 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. 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. 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. 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. 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.
      , 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. 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.

    Entry informationi

    Entry nameiMYLK_HUMAN
    AccessioniPrimary (citable) accession number: Q15746
    Secondary accession number(s): B4DUE3
    , D3DN97, O95796, O95797, O95798, O95799, Q14844, Q16794, Q17S15, Q3ZCP9, Q5MY99, Q5MYA0, Q6P2N0, Q7Z4J0, Q9C0L5, Q9UBG5, Q9UBY6, Q9UIT9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: July 13, 2010
    Last modified: October 1, 2014
    This is version 162 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

    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.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3