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Protein

Myosin light chain kinase, smooth muscle

Gene

MYLK

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

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

Protein has several cofactor binding sites:

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
  1. Vmax=11.9 µmol/min/mg enzyme (isoform 1 at 22 degrees Celsius)1 Publication
  2. Vmax=10.9 µmol/min/mg enzyme (isoform 1 at 22 degrees Celsius)1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei1493ATPPROSITE-ProRule annotation1
Active sitei1585Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi1470 – 1478ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW
  • myosin light chain kinase activity Source: UniProtKB

GO - Biological processi

  • aorta smooth muscle tissue morphogenesis Source: BHF-UCL
  • bleb assembly Source: UniProtKB
  • cellular hypotonic response Source: UniProtKB
  • muscle contraction Source: Reactome
  • positive regulation of calcium ion transport Source: UniProtKB
  • positive regulation of cell migration Source: UniProtKB
  • positive regulation of wound healing Source: UniProtKB
  • protein phosphorylation Source: ProtInc
  • smooth muscle contraction Source: UniProtKB
  • tonic smooth muscle contraction Source: UniProtKB
Complete GO annotation...

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

BioCyciZFISH:HS00845-MONOMER.
BRENDAi2.7.11.18. 2681.
ReactomeiR-HSA-445355. Smooth Muscle Contraction.
R-HSA-5627123. RHO GTPases activate PAKs.
SignaLinkiQ15746.
SIGNORiQ15746.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:7590. MYLK.

Subcellular locationi

GO - Cellular componenti

  • cleavage furrow Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • lamellipodium Source: UniProtKB
  • stress fiber Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoskeleton

Pathology & Biotechi

Involvement in diseasei

Aortic aneurysm, familial thoracic 7 (AAT7)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:613780
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0655771759S → 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 PublicationCorresponds to variant rs387906781dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi608K → A: Loss of acetylation and no kinase activity repression by NAA10/ARD1. 1 Publication1

Keywords - Diseasei

Aortic aneurysm, Disease mutation

Organism-specific databases

DisGeNETi4638.
MalaCardsiMYLK.
MIMi613780. phenotype.
OpenTargetsiENSG00000065534.
Orphaneti91387. Familial thoracic aortic aneurysm and aortic dissection.
PharmGKBiPA31388.

Chemistry databases

ChEMBLiCHEMBL2428.
GuidetoPHARMACOLOGYi1552.

Polymorphism and mutation databases

BioMutaiMYLK.
DMDMi300669714.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000243541 – 1914Myosin light chain kinase, smooth muscleAdd BLAST1914
ChainiPRO_00004037311 – 1910Myosin light chain kinase, smooth muscle, deglutamylated formBy similarityAdd BLAST1910
Isoform 6 (identifier: Q15746-8)
Initiator methionineiRemovedCombined sources
Isoform 8 (identifier: Q15746-10)
Initiator methionineiRemovedCombined sources

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi182 ↔ 233PROSITE-ProRule annotation
Modified residuei231Phosphotyrosine; by ABL11 Publication1
Modified residuei305PhosphoserineCombined sources1
Modified residuei343PhosphoserineBy similarity1
Modified residuei365PhosphoserineBy similarity1
Disulfide bondi435 ↔ 487PROSITE-ProRule annotation
Modified residuei464Phosphotyrosine; by ABL1 and SRC3 Publications1
Modified residuei471Phosphotyrosine; by SRC2 Publications1
Disulfide bondi535 ↔ 583PROSITE-ProRule annotation
Modified residuei556Phosphotyrosine; by ABL11 Publication1
Modified residuei608N6-acetyllysine1 Publication1
Modified residuei611Phosphotyrosine; by ABL11 Publication1
Disulfide bondi742 ↔ 805PROSITE-ProRule annotation
Modified residuei792Phosphotyrosine; by ABL11 Publication1
Modified residuei846Phosphotyrosine; by ABL11 Publication1
Modified residuei947PhosphoserineBy similarity1
Disulfide bondi1119 ↔ 1170PROSITE-ProRule annotation
Modified residuei1438PhosphoserineCombined sources1
Modified residuei1449Phosphotyrosine; by ABL11 Publication1
Modified residuei1575Phosphotyrosine; by ABL11 Publication1
Modified residuei1635Phosphotyrosine; by ABL11 Publication1
Modified residuei1759PhosphoserineBy similarity1
Modified residuei1760PhosphoserineBy similarity1
Modified residuei1772PhosphoserineCombined sources1
Modified residuei1773PhosphoserineBy similarity1
Modified residuei1776PhosphoserineCombined sources1
Modified residuei1778PhosphothreonineBy similarity1
Modified residuei1779PhosphoserineCombined sources1
Disulfide bondi1830 ↔ 1882PROSITE-ProRule annotation
Isoform 6 (identifier: Q15746-8)
Modified residuei2N-acetylalanineCombined sources1
Isoform 8 (identifier: Q15746-10)
Modified residuei2N-acetylalanineCombined sources1

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.3 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

EPDiQ15746.
MaxQBiQ15746.
PaxDbiQ15746.
PeptideAtlasiQ15746.
PRIDEiQ15746.

PTM databases

iPTMnetiQ15746.
PhosphoSitePlusiQ15746.

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

BgeeiENSG00000065534.
ExpressionAtlasiQ15746. baseline and differential.
GenevisibleiQ15746. HS.

Organism-specific databases

HPAiCAB020789.
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
GOPCQ9HD263EBI-968482,EBI-349832
NCK1P163332EBI-968482,EBI-389883

Protein-protein interaction databases

BioGridi110722. 17 interactors.
IntActiQ15746. 22 interactors.
MINTiMINT-2807402.
STRINGi9606.ENSP00000353452.

Chemistry databases

BindingDBiQ15746.

Structurei

Secondary structure

11914
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi512 – 518Combined sources7
Beta strandi523 – 526Combined sources4
Beta strandi531 – 534Combined sources4
Beta strandi536 – 541Combined sources6
Beta strandi546 – 553Combined sources8
Beta strandi560 – 562Combined sources3
Beta strandi565 – 570Combined sources6
Beta strandi581 – 586Combined sources6
Beta strandi591 – 595Combined sources5
Beta strandi598 – 601Combined sources4
Beta strandi1239 – 1241Combined sources3
Beta strandi1246 – 1250Combined sources5
Beta strandi1255 – 1266Combined sources12
Beta strandi1268 – 1277Combined sources10
Beta strandi1281 – 1288Combined sources8
Beta strandi1290 – 1297Combined sources8
Turni1302 – 1304Combined sources3
Beta strandi1306 – 1313Combined sources8
Beta strandi1318 – 1320Combined sources3
Beta strandi1323 – 1328Combined sources6
Helixi1743 – 1759Combined sources17

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2CQVNMR-A1238-1338[»]
2K0FNMR-B1742-1760[»]
2YR3NMR-A510-601[»]
ProteinModelPortaliQ15746.
SMRiQ15746.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15746.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini33 – 122Ig-like C2-type 1Add BLAST90
Domaini161 – 249Ig-like C2-type 2Add BLAST89
Domaini414 – 503Ig-like C2-type 3Add BLAST90
Domaini514 – 599Ig-like C2-type 4Add BLAST86
Domaini620 – 711Ig-like C2-type 5Add BLAST92
Domaini721 – 821Ig-like C2-type 6Add BLAST101
Repeati868 – 8951-1Add BLAST28
Repeati896 – 9231-2Add BLAST28
Repeati924 – 9511-3Add BLAST28
Repeati952 – 9791-4Add BLAST28
Repeati980 – 9981-5; truncatedAdd BLAST19
Repeati999 – 10032-1; truncated5
Repeati1004 – 10152-2Add BLAST12
Repeati1016 – 10272-3Add BLAST12
Repeati1028 – 10392-4Add BLAST12
Repeati1040 – 10512-5Add BLAST12
Repeati1052 – 10632-6Add BLAST12
Domaini1098 – 1186Ig-like C2-type 7Add BLAST89
Domaini1238 – 1326Ig-like C2-type 8Add BLAST89
Domaini1334 – 1426Fibronectin type-IIIPROSITE-ProRule annotationAdd BLAST93
Domaini1464 – 1719Protein kinasePROSITE-ProRule annotationAdd BLAST256
Domaini1809 – 1898Ig-like C2-type 9Add BLAST90

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni868 – 9985 X 28 AA approximate tandem repeatsAdd BLAST131
Regioni923 – 963Actin-binding (calcium/calmodulin-sensitive)By similarityAdd BLAST41
Regioni948 – 963Calmodulin-bindingBy similarityAdd BLAST16
Regioni999 – 10636 X 12 AA approximate tandem repeatsAdd BLAST65
Regioni1061 – 1460Actin-binding (calcium/calmodulin-insensitive)By similarityAdd BLAST400
Regioni1711 – 1774Calmodulin-bindingAdd BLAST64

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1906 – 1914Poly-Glu9

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

eggNOGiKOG0613. Eukaryota.
ENOG410XQFD. LUCA.
GeneTreeiENSGT00760000118877.
HOGENOMiHOG000049287.
HOVERGENiHBG052551.
InParanoidiQ15746.
KOiK00907.
OMAiKYTCEAW.
OrthoDBiEOG091G005W.
PhylomeDBiQ15746.
TreeFamiTF314166.

Family and domain databases

CDDicd00063. FN3. 1 hit.
Gene3Di2.60.40.10. 10 hits.
InterProiIPR003961. FN3_dom.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
IPR015725. Telokin/Myosin_light_ch_kin.
[Graphical view]
PANTHERiPTHR10489:SF700. PTHR10489:SF700. 4 hits.
PfamiPF00041. fn3. 1 hit.
PF07679. I-set. 9 hits.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00060. FN3. 1 hit.
SM00409. IG. 9 hits.
SM00408. IGc2. 9 hits.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 9 hits.
SSF49265. 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. AlignAdd to basket

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

        10         20         30         40         50
MGDVKLVASS HISKTSLSVD PSRVDSMPLT EAPAFILPPR NLCIKEGATA
60 70 80 90 100
KFEGRVRGYP EPQVTWHRNG QPITSGGRFL LDCGIRGTFS LVIHAVHEED
110 120 130 140 150
RGKYTCEATN GSGARQVTVE LTVEGSFAKQ LGQPVVSKTL GDRFSAPAVE
160 170 180 190 200
TRPSIWGECP PKFATKLGRV VVKEGQMGRF SCKITGRPQP QVTWLKGNVP
210 220 230 240 250
LQPSARVSVS EKNGMQVLEI HGVNQDDVGV YTCLVVNGSG KASMSAELSI
260 270 280 290 300
QGLDSANRSF VRETKATNSD VRKEVTNVIS KESKLDSLEA AAKSKNCSSP
310 320 330 340 350
QRGGSPPWAA NSQPQPPRES KLESCKDSPR TAPQTPVLQK TSSSITLQAA
360 370 380 390 400
RVQPEPRAPG LGVLSPSGEE RKRPAPPRPA TFPTRQPGLG SQDVVSKAAN
410 420 430 440 450
RRIPMEGQRD SAFPKFESKP QSQEVKENQT VKFRCEVSGI PKPEVAWFLE
460 470 480 490 500
GTPVRRQEGS IEVYEDAGSH YLCLLKARTR DSGTYSCTAS NAQGQLSCSW
510 520 530 540 550
TLQVERLAVM EVAPSFSSVL KDCAVIEGQD FVLQCSVRGT PVPRITWLLN
560 570 580 590 600
GQPIQYARST CEAGVAELHI QDALPEDHGT YTCLAENALG QVSCSAWVTV
610 620 630 640 650
HEKKSSRKSE YLLPVAPSKP TAPIFLQGLS DLKVMDGSQV TMTVQVSGNP
660 670 680 690 700
PPEVIWLHNG NEIQESEDFH FEQRGTQHSL CIQEVFPEDT GTYTCEAWNS
710 720 730 740 750
AGEVRTQAVL TVQEPHDGTQ PWFISKPRSV TASLGQSVLI SCAIAGDPFP
760 770 780 790 800
TVHWLRDGKA LCKDTGHFEV LQNEDVFTLV LKKVQPWHAG QYEILLKNRV
810 820 830 840 850
GECSCQVSLM LQNSSARALP RGREPASCED LCGGGVGADG GGSDRYGSLR
860 870 880 890 900
PGWPARGQGW LEEEDGEDVR GVLKRRVETR QHTEEAIRQQ EVEQLDFRDL
910 920 930 940 950
LGKKVSTKTL SEDDLKEIPA EQMDFRANLQ RQVKPKTVSE EERKVHSPQQ
960 970 980 990 1000
VDFRSVLAKK GTSKTPVPEK VPPPKPATPD FRSVLGGKKK LPAENGSSSA
1010 1020 1030 1040 1050
ETLNAKAVES SKPLSNAQPS GPLKPVGNAK PAETLKPMGN AKPAETLKPM
1060 1070 1080 1090 1100
GNAKPDENLK SASKEELKKD VKNDVNCKRG HAGTTDNEKR SESQGTAPAF
1110 1120 1130 1140 1150
KQKLQDVHVA EGKKLLLQCQ VSSDPPATII WTLNGKTLKT TKFIILSQEG
1160 1170 1180 1190 1200
SLCSVSIEKA LPEDRGLYKC VAKNDAGQAE CSCQVTVDDA PASENTKAPE
1210 1220 1230 1240 1250
MKSRRPKSSL PPVLGTESDA TVKKKPAPKT PPKAAMPPQI IQFPEDQKVR
1260 1270 1280 1290 1300
AGESVELFGK VTGTQPITCT WMKFRKQIQE SEHMKVENSE NGSKLTILAA
1310 1320 1330 1340 1350
RQEHCGCYTL LVENKLGSRQ AQVNLTVVDK PDPPAGTPCA SDIRSSSLTL
1360 1370 1380 1390 1400
SWYGSSYDGG SAVQSYSIEI WDSANKTWKE LATCRSTSFN VQDLLPDHEY
1410 1420 1430 1440 1450
KFRVRAINVY GTSEPSQESE LTTVGEKPEE PKDEVEVSDD DEKEPEVDYR
1460 1470 1480 1490 1500
TVTINTEQKV SDFYDIEERL GSGKFGQVFR LVEKKTRKVW AGKFFKAYSA
1510 1520 1530 1540 1550
KEKENIRQEI SIMNCLHHPK LVQCVDAFEE KANIVMVLEI VSGGELFERI
1560 1570 1580 1590 1600
IDEDFELTER ECIKYMRQIS EGVEYIHKQG IVHLDLKPEN IMCVNKTGTR
1610 1620 1630 1640 1650
IKLIDFGLAR RLENAGSLKV LFGTPEFVAP EVINYEPIGY ATDMWSIGVI
1660 1670 1680 1690 1700
CYILVSGLSP FMGDNDNETL ANVTSATWDF DDEAFDEISD DAKDFISNLL
1710 1720 1730 1740 1750
KKDMKNRLDC TQCLQHPWLM KDTKNMEAKK LSKDRMKKYM ARRKWQKTGN
1760 1770 1780 1790 1800
AVRAIGRLSS MAMISGLSGR KSSTGSPTSP LNAEKLESEE DVSQAFLEAV
1810 1820 1830 1840 1850
AEEKPHVKPY FSKTIRDLEV VEGSAARFDC KIEGYPDPEV VWFKDDQSIR
1860 1870 1880 1890 1900
ESRHFQIDYD EDGNCSLIIS DVCGDDDAKY TCKAVNSLGE ATCTAELIVE
1910
TMEEGEGEGE EEEE
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.Combined sources
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.Combined sources
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 differs from that shown. Reason: Frameshift at position 1433.Curated
Isoform 3A : The sequence AAD15922 differs from that shown. Reason: Frameshift at positions 1433 and 1439.Curated
The sequence AAD15923 differs from that shown. Reason: Frameshift at position 1433.Curated
Isoform 3B : The sequence AAD15923 differs from that shown. Reason: Frameshift at positions 1433 and 1439.Curated
The sequence AAD15924 differs from that shown. Reason: Frameshift at position 1433.Curated
Isoform 4 : The sequence AAD15924 differs from that shown. Reason: Frameshift at positions 1433 and 1439.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti147P → S in AAC18423 (PubMed:9160829).Curated1
Sequence conflicti147P → S in AAD15922 (PubMed:10198165).Curated1
Sequence conflicti147P → S in AAD15923 (PubMed:10198165).Curated1
Sequence conflicti147P → S in AAR29062 (PubMed:15507455).Curated1
Sequence conflicti147P → S in AAQ02673 (PubMed:15020676).Curated1
Sequence conflicti147P → S in EAW79438 (Ref. 11) Curated1
Sequence conflicti147P → S in EAW79440 (Ref. 11) Curated1
Sequence conflicti466D → N in AAR29062 (PubMed:15507455).Curated1
Sequence conflicti496L → V in AAC18423 (PubMed:9160829).Curated1
Sequence conflicti496L → V in AAD15922 (PubMed:10198165).Curated1
Sequence conflicti496L → V in AAR29062 (PubMed:15507455).Curated1
Sequence conflicti496L → V in AAQ02673 (PubMed:15020676).Curated1
Sequence conflicti681C → W in AAC18423 (PubMed:9160829).Curated1
Sequence conflicti681C → W in AAD15921 (PubMed:10198165).Curated1
Sequence conflicti681C → W in AAD15922 (PubMed:10198165).Curated1
Sequence conflicti681C → W in AAD15923 (PubMed:10198165).Curated1
Sequence conflicti933V → M in CAA59685 (PubMed:8575746).Curated1
Sequence conflicti963S → P in AAD15922 (PubMed:10198165).Curated1
Sequence conflicti1022P → A in CAA59685 (PubMed:8575746).Curated1
Sequence conflicti1048 – 1050KPM → EAH in CAA59685 (PubMed:8575746).Curated3
Sequence conflicti1048 – 1050KPM → EAH in BAB21504 (Ref. 8) Curated3
Sequence conflicti1162P → L in AAD15922 (PubMed:10198165).Curated1
Sequence conflicti1162P → L in AAD15923 (PubMed:10198165).Curated1
Sequence conflicti1210L → P in CAA59685 (PubMed:8575746).Curated1
Sequence conflicti1280E → D in AAD15922 (PubMed:10198165).Curated1
Sequence conflicti1280E → D in AAD15923 (PubMed:10198165).Curated1
Sequence conflicti1284M → I in AAD15922 (PubMed:10198165).Curated1
Sequence conflicti1284M → I in AAD15923 (PubMed:10198165).Curated1
Sequence conflicti1284M → I in AAD15924 (PubMed:10198165).Curated1
Sequence conflicti1300A → G in CAA59685 (PubMed:8575746).Curated1
Sequence conflicti1316L → S in CAA59685 (PubMed:8575746).Curated1
Sequence conflicti1326T → S in CAA59685 (PubMed:8575746).Curated1
Sequence conflicti1478V → C in CAA59685 (PubMed:8575746).Curated1
Sequence conflicti1511S → T in AAD15922 (PubMed:10198165).Curated1
Sequence conflicti1511S → T in AAD15923 (PubMed:10198165).Curated1
Sequence conflicti1518H → P in AAR29061 (PubMed:15507455).Curated1
Sequence conflicti1518H → P in AAR29062 (PubMed:15507455).Curated1
Sequence conflicti1563I → T in CAA59685 (PubMed:8575746).Curated1
Sequence conflicti1609A → P in CAA59685 (PubMed:8575746).Curated1
Sequence conflicti1634N → I in AAR29061 (PubMed:15507455).Curated1
Sequence conflicti1634N → I in AAR29062 (PubMed:15507455).Curated1
Sequence conflicti1639 – 1640GY → D in AAD15922 (PubMed:10198165).Curated2
Sequence conflicti1639 – 1640GY → D in AAD15923 (PubMed:10198165).Curated2
Sequence conflicti1639 – 1640GY → D in AAD15924 (PubMed:10198165).Curated2
Sequence conflicti1639G → R in CAA59685 (PubMed:8575746).Curated1
Sequence conflicti1648G → R in CAA59685 (PubMed:8575746).Curated1
Sequence conflicti1658 – 1659LS → PF in CAA59685 (PubMed:8575746).Curated2
Sequence conflicti1676A → P in AAR29061 (PubMed:15507455).Curated1
Sequence conflicti1676A → P in AAR29062 (PubMed:15507455).Curated1
Sequence conflicti1710 – 1711CT → LA in CAA59685 (PubMed:8575746).Curated2
Sequence conflicti1897L → H in AAD15922 (PubMed:10198165).Curated1
Sequence conflicti1897L → H in AAD15923 (PubMed:10198165).Curated1
Sequence conflicti1897L → H in AAD15924 (PubMed:10198165).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05710621P → H.Corresponds to variant rs28497577dbSNPEnsembl.1
Natural variantiVAR_065570128A → V.1 PublicationCorresponds to variant rs143896146dbSNPEnsembl.1
Natural variantiVAR_065571133Q → H.1 PublicationCorresponds to variant rs140148380dbSNPEnsembl.1
Natural variantiVAR_065572160P → R.1 PublicationCorresponds to variant rs111256888dbSNPEnsembl.1
Natural variantiVAR_040847261V → A.1 PublicationCorresponds to variant rs3796164dbSNPEnsembl.1
Natural variantiVAR_040848276T → A.1 PublicationCorresponds to variant rs55846245dbSNPEnsembl.1
Natural variantiVAR_057107336P → L.Corresponds to variant rs35912339dbSNPEnsembl.1
Natural variantiVAR_040849378R → H.1 PublicationCorresponds to variant rs56378658dbSNPEnsembl.1
Natural variantiVAR_040850405M → V.1 PublicationCorresponds to variant rs35436690dbSNPEnsembl.1
Natural variantiVAR_040851443P → S.1 PublicationCorresponds to variant rs35156360dbSNPEnsembl.1
Natural variantiVAR_040852607R → G.1 Publication1
Natural variantiVAR_040853652P → A.1 PublicationCorresponds to variant rs750686734dbSNPEnsembl.1
Natural variantiVAR_040854656W → C.2 PublicationsCorresponds to variant rs138172035dbSNPEnsembl.1
Natural variantiVAR_040855692T → M.1 PublicationCorresponds to variant rs776858093dbSNPEnsembl.1
Natural variantiVAR_040856701A → T.1 PublicationCorresponds to variant rs142835596dbSNPEnsembl.1
Natural variantiVAR_040857709V → M.1 PublicationCorresponds to variant rs112537316dbSNPEnsembl.1
Natural variantiVAR_057108845R → C.Corresponds to variant rs3732485dbSNPEnsembl.1
Natural variantiVAR_019986861L → P.Corresponds to variant rs3732486dbSNPEnsembl.1
Natural variantiVAR_057109877V → M.Corresponds to variant rs34542174dbSNPEnsembl.1
Natural variantiVAR_019987914D → E.Corresponds to variant rs3732487dbSNPEnsembl.1
Natural variantiVAR_0655731085T → A.1 PublicationCorresponds to variant rs75370906dbSNPEnsembl.1
Natural variantiVAR_0655741213V → M Found in a patient with familial aortic dissections. 1 PublicationCorresponds to variant rs368390254dbSNPEnsembl.1
Natural variantiVAR_0655751399E → K Found in a patient with familial aortic dissections. 1 PublicationCorresponds to variant rs181663420dbSNPEnsembl.1
Natural variantiVAR_0408581527A → V.1 PublicationCorresponds to variant rs34982967dbSNPEnsembl.1
Natural variantiVAR_0408591588P → L in an ovarian mucinous carcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_0655761754A → 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 Publication1
Natural variantiVAR_0655771759S → 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 PublicationCorresponds to variant rs387906781dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0188461 – 1760Missing in isoform 6 and isoform 8. 3 PublicationsAdd BLAST1760
Alternative sequenceiVSP_0537911 – 1200Missing in isoform 7. 1 PublicationAdd BLAST1200
Alternative sequenceiVSP_0188451 – 922Missing in isoform 5 and isoform 9. 2 PublicationsAdd BLAST922
Alternative sequenceiVSP_004791437 – 506VSGIP…LQVER → G in isoform 2 and isoform 3B. 2 PublicationsAdd BLAST70
Alternative sequenceiVSP_0047931473 – 1545Missing in isoform 4. 1 PublicationAdd BLAST73
Alternative sequenceiVSP_0047941655 – 1705Missing in isoform 3A and isoform 3B. 1 PublicationAdd BLAST51
Alternative sequenceiVSP_0047951790Missing in isoform Del-1790, isoform 8 and isoform 9. 4 Publications1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_001308238.1. NM_001321309.1.
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_053031.3. [Q15746-10]
NP_444260.1. NM_053032.3. [Q15746-8]
XP_011511162.1. XM_011512860.2. [Q15746-6]
XP_016861958.1. XM_017006469.1. [Q15746-11]
XP_016861960.1. XM_017006471.1. [Q15746-9]
XP_016861961.1. XM_017006472.1. [Q15746-8]
XP_016861962.1. XM_017006473.1. [Q15746-10]
UniGeneiHs.477375.

Genome annotation databases

EnsembliENST00000346322; ENSP00000320622; ENSG00000065534. [Q15746-2]
ENST00000354792; ENSP00000346846; ENSG00000065534. [Q15746-2]
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.4. human. [Q15746-1]

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:
EMBLi
GenBanki
DDBJi
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_001308238.1. NM_001321309.1.
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_053031.3. [Q15746-10]
NP_444260.1. NM_053032.3. [Q15746-8]
XP_011511162.1. XM_011512860.2. [Q15746-6]
XP_016861958.1. XM_017006469.1. [Q15746-11]
XP_016861960.1. XM_017006471.1. [Q15746-9]
XP_016861961.1. XM_017006472.1. [Q15746-8]
XP_016861962.1. XM_017006473.1. [Q15746-10]
UniGeneiHs.477375.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2CQVNMR-A1238-1338[»]
2K0FNMR-B1742-1760[»]
2YR3NMR-A510-601[»]
ProteinModelPortaliQ15746.
SMRiQ15746.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110722. 17 interactors.
IntActiQ15746. 22 interactors.
MINTiMINT-2807402.
STRINGi9606.ENSP00000353452.

Chemistry databases

BindingDBiQ15746.
ChEMBLiCHEMBL2428.
GuidetoPHARMACOLOGYi1552.

PTM databases

iPTMnetiQ15746.
PhosphoSitePlusiQ15746.

Polymorphism and mutation databases

BioMutaiMYLK.
DMDMi300669714.

Proteomic databases

EPDiQ15746.
MaxQBiQ15746.
PaxDbiQ15746.
PeptideAtlasiQ15746.
PRIDEiQ15746.

Protocols and materials databases

DNASUi4638.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000346322; ENSP00000320622; ENSG00000065534. [Q15746-2]
ENST00000354792; ENSP00000346846; ENSG00000065534. [Q15746-2]
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.4. human. [Q15746-1]

Organism-specific databases

CTDi4638.
DisGeNETi4638.
GeneCardsiMYLK.
GeneReviewsiMYLK.
HGNCiHGNC:7590. MYLK.
HPAiCAB020789.
HPA031677.
MalaCardsiMYLK.
MIMi600922. gene.
613780. phenotype.
neXtProtiNX_Q15746.
OpenTargetsiENSG00000065534.
Orphaneti91387. Familial thoracic aortic aneurysm and aortic dissection.
PharmGKBiPA31388.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0613. Eukaryota.
ENOG410XQFD. LUCA.
GeneTreeiENSGT00760000118877.
HOGENOMiHOG000049287.
HOVERGENiHBG052551.
InParanoidiQ15746.
KOiK00907.
OMAiKYTCEAW.
OrthoDBiEOG091G005W.
PhylomeDBiQ15746.
TreeFamiTF314166.

Enzyme and pathway databases

BioCyciZFISH:HS00845-MONOMER.
BRENDAi2.7.11.18. 2681.
ReactomeiR-HSA-445355. Smooth Muscle Contraction.
R-HSA-5627123. RHO GTPases activate PAKs.
SignaLinkiQ15746.
SIGNORiQ15746.

Miscellaneous databases

ChiTaRSiMYLK. human.
EvolutionaryTraceiQ15746.
GeneWikiiMYLK.
GenomeRNAii4638.
PROiQ15746.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000065534.
ExpressionAtlasiQ15746. baseline and differential.
GenevisibleiQ15746. HS.

Family and domain databases

CDDicd00063. FN3. 1 hit.
Gene3Di2.60.40.10. 10 hits.
InterProiIPR003961. FN3_dom.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
IPR015725. Telokin/Myosin_light_ch_kin.
[Graphical view]
PANTHERiPTHR10489:SF700. PTHR10489:SF700. 4 hits.
PfamiPF00041. fn3. 1 hit.
PF07679. I-set. 9 hits.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00060. FN3. 1 hit.
SM00409. IG. 9 hits.
SM00408. IGc2. 9 hits.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 9 hits.
SSF49265. 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]
ProtoNetiSearch...

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: November 30, 2016
This is version 185 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

Similar proteinsi

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