Search Results

Overview

Uniprot IDQ15746
Protein NameMyosin light chain kinase, smooth muscle
Gene NameMYLK
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
1113 DVHVAEGKKLLLQCQ
1114 VHVAEGKKLLLQCQV
1207 EMKSRRPKSSLPPVL
1330 VNLTVVDKPDPPAGT
1376 EIWDSANKTWKELAT
14 VASSHISKTSLSVDP
1771 ISGLSGRKSSTGSPT
1831 SAARFDCKIEGYPDP
273 ATNSDVRKEVTNVIS
281 EVTNVISKESKLDSL
293 DSLEAAAKSKNCSSP
295 LEAAAKSKNCSSPQR
321 PQPPRESKLESCKDS
326 ESKLESCKDSPRTAP
397 GSQDVVSKAANRRIP
415 QRDSAFPKFESKPQS
419 AFPKFESKPQSQEVK
970 SKTPVPEKVPPPKPA

Function

Calcium/calmodulin-dependent myosin light chain kinase implicated in smooth muscle contraction via phosphorylation of myosin light chains (MLC). Also regulates actin-myosin interaction through a non-kinase activity. Phosphorylates PTK2B/PYK2 and myosin light-chains. Involved in the inflammatory response (e.g. apoptosis, vascular permeability, leukocyte diapedesis), cell motility and morphology, airway hyperreactivity and other activities relevant to asthma. Required for tonic airway smooth muscle contraction that is necessary for physiological and asthmatic airway resistance. Necessary for gastrointestinal motility. Implicated in the regulation of endothelial as well as vascular permeability, probably via the regulation of cytoskeletal rearrangements. In the nervous system it has been shown to control the growth initiation of astrocytic processes in culture and to participate in transmitter release at synapses formed between cultured sympathetic ganglion cells. Critical participant in signaling sequences that result in fibroblast apoptosis. Plays a role in the regulation of epithelial cell survival. Required for epithelial wound healing, especially during actomyosin ring contraction during purse-string wound closure. Mediates RhoA-dependent membrane blebbing. Triggers TRPC5 channel activity in a calcium-dependent signaling, by inducing its subcellular localization at the plasma membrane. Promotes cell migration (including tumor cells) and tumor metastasis. PTK2B/PYK2 activation by phosphorylation mediates ITGB2 activation and is thus essential to trigger neutrophil transmigration during acute lung injury (ALI). May regulate optic nerve head astrocyte migration. Probably involved in mitotic cytoskeletal regulation. Regulates tight junction probably by modulating ZO-1 exchange in the perijunctional actomyosin ring. Mediates burn-induced microvascular barrier injury; triggers endothelial contraction in the development of microvascular hyperpermeability by phosphorylating MLC. Essential for intestinal barrier dysfunction. Mediates Giardia spp.-mediated reduced epithelial barrier function during giardiasis intestinal infection via reorganization of cytoskeletal F-actin and tight junctional ZO-1. Necessary for hypotonicity-induced Ca(2+) 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

Protein Sequence

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

Gene Ontology

Classification GO ID Description
Cellular Component GO:0015629 actin cytoskeleton
Cellular Component GO:0032154 cleavage furrow
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0030027 lamellipodium
Cellular Component GO:0005886 plasma membrane
Cellular Component GO:0001725 stress fiber
Cellular Component GO:0045202 synapse
Molecular Function GO:0003779 actin binding
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0005516 calmodulin binding
Molecular Function GO:0046872 metal ion binding
Molecular Function GO:0004687 myosin light chain kinase activity
Molecular Function GO:0097110 scaffold protein binding
Biological Process GO:0060414 aorta smooth muscle tissue morphogenesis
Biological Process GO:0032060 bleb assembly
Biological Process GO:0071476 cellular hypotonic response
Biological Process GO:0051928 positive regulation of calcium ion transport
Biological Process GO:0030335 positive regulation of cell migration
Biological Process GO:0090303 positive regulation of wound healing
Biological Process GO:0006468 protein phosphorylation
Biological Process GO:1900242 regulation of synaptic vesicle endocytosis
Biological Process GO:0006939 smooth muscle contraction
Biological Process GO:0014820 tonic smooth muscle contraction

Reference

[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[2] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.

[3] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.

[4] Yang YH, Wang QC, Kong J, Yang JT, Liu JF. Global profiling of lysine lactylation in human lungs.. Proteomics 23(15):e2200437. 2023 Aug. PMID: 37170646.

[5] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.