MYLK
entrez
4638
canonical
uniprot
Q15746
canonical
ensembl
ENSG00000065534
resolver
ensp
ENSP00000320622
resolver
ensp
ENSP00000353452
resolver
ensp
ENSP00000354004
resolver
ensp
ENSP00000422984
resolver
ensp
ENSP00000428967
resolver
ensp
ENSP00000462118
resolver
ensp
ENSP00000508761
resolver
ensp
ENSP00000508777
resolver
ensp
ENSP00000509867
resolver
ensp
ENSP00000510047
resolver
ensp
ENSP00000510503
resolver
ensp
ENSP00000510593
resolver
ensp
ENSP00000641546
resolver
ensp
ENSP00000641548
resolver
ensp
ENSP00000649725
resolver
ensp
ENSP00000789977
resolver
enst
ENST00000685953
resolver
enst
ENST00000687848
resolver
genesymbol
MYLK
resolver
genesymbol_syn
MLCK
resolver
genesymbol_syn
MLCK1
resolver
genesymbol_syn
MYLK1
resolver
hgnc
HGNC:7590
resolver
uniprot
A0A8I5KTQ1
resolver
uniprot
A0A8I5KU53
resolver
uniprot
B4DUE3
resolver
uniprot
D3DN97
resolver
uniprot
O95796
resolver
uniprot
O95797
resolver
uniprot
O95798
resolver
uniprot
O95799
resolver
uniprot
Q05B97
resolver
uniprot
Q05B98
resolver
uniprot
Q14844
resolver
uniprot
Q16794
resolver
uniprot
Q17S15
resolver
uniprot
Q3ZCP9
resolver
uniprot
Q5MY99
resolver
uniprot
Q5MYA0
resolver
uniprot
Q6P2N0
resolver
uniprot
Q7Z4J0
resolver
uniprot
Q9C0L5
resolver
uniprot
Q9UBG5
resolver
uniprot
Q9UBY6
resolver
uniprot
Q9UIT9
resolver
uniprot_entry
A0A8I5KTQ1_HUMAN
resolver
uniprot_entry
A0A8I5KU53_HUMAN
resolver
uniprot_entry
MYLK_HUMAN
resolver
uniprot_entry
Q05B97_HUMAN
resolver
uniprot_entry
Q05B98_HUMAN
resolver
uniprot_sec
B4DUE3
resolver
uniprot_sec
D3DN97
resolver
uniprot_sec
O95796
resolver
uniprot_sec
O95797
resolver
uniprot_sec
O95798
resolver
uniprot_sec
O95799
resolver
uniprot_sec
Q14844
resolver
uniprot_sec
Q16794
resolver
uniprot_sec
Q17S15
resolver
uniprot_sec
Q3ZCP9
resolver
uniprot_sec
Q5MY99
resolver
uniprot_sec
Q5MYA0
resolver
uniprot_sec
Q6P2N0
resolver
uniprot_sec
Q7Z4J0
resolver
uniprot_sec
Q9C0L5
resolver
uniprot_sec
Q9UBG5
resolver
uniprot_sec
Q9UBY6
resolver
uniprot_sec
Q9UIT9
resolver
activity_regulation
ACTIVITY REGULATION: Isoform 1 is activated by phosphorylation on Tyr-464 and Tyr-471. Isoforms which lack these tyrosine residues are not regulated in this way. All catalytically active isoforms require binding to calcium and calmodulin for activation. Repressed by organometallic pyridylnaphthalimide complexes, wortmannin, ML-7 (a synthetic naphthalenesulphonyl derivative that inhibits the binding of ATP to MLCK) and ML-9. {ECO:0000269|PubMed:11113114, ECO:0000269|PubMed:11976941, ECO:0000269|PubMed:14741352, ECO:0000269|PubMed:16284075, ECO:0000269|PubMed:16723733, ECO:0000269|PubMed:21918590}.
uniprot
proteins
amino_acid_sequence
MGDVKLVASSHISKTSLSVDPSRVDSMPLTEAPAFILPPRNLCIKEGATAKFEGRVRGYPEPQVTWHRNGQPITSGGRFLLDCGIRGTFSLVIHAVHEEDRGKYTCEATNGSGARQVTVELTVEGSFAKQLGQPVVSKTLGDRFSAPAVETRPSIWGECPPKFATKLGRVVVKEGQMGRFSCKITGRPQPQVTWLKGNVPLQPSARVSVSEKNGMQVLEIHGVNQDDVGVYTCLVVNGSGKASMSAELSIQGLDSANRSFVRETKATNSDVRKEVTNVISKESKLDSLEAAAKSKNCSSPQRGGSPPWAANSQPQPPRESKLESCKDSPRTAPQTPVLQKTSSSITLQAARVQPEPRAPGLGVLSPSGEERKRPAPPRPATFPTRQPGLGSQDVVSKAANRRIPMEGQRDSAFPKFESKPQSQEVKENQTVKFRCEVSGIPKPEVAWFLEGTPVRRQEGSIEVYEDAGSHYLCLLKARTRDSGTYSCTASNAQGQLSCSWTLQVERLAVMEVAPSFSSVLKDCAVIEGQDFVLQCSVRGTPVPRITWLLNGQPIQYARSTCEAGVAELHIQDALPEDHGTYTCLAENALGQVSCSAWVTVHEKKSSRKSEYLLPVAPSKPTAPIFLQGLSDLKVMDGSQVTMTVQVSGNPPPEVIWLHNGNEIQESEDFHFEQRGTQHSLCIQEVFPEDTGTYTCEAWNSAGEVRTQAVLTVQEPHDGTQPWFISKPRSVTASLGQSVLISCAIAGDPFPTVHWLRDGKALCKDTGHFEVLQNEDVFTLVLKKVQPWHAGQYEILLKNRVGECSCQVSLMLQNSSARALPRGREPASCEDLCGGGVGADGGGSDRYGSLRPGWPARGQGWLEEEDGEDVRGVLKRRVETRQHTEEAIRQQEVEQLDFRDLLGKKVSTKTLSEDDLKEIPAEQMDFRANLQRQVKPKTVSEEERKVHSPQQVDFRSVLAKKGTSKTPVPEKVPPPKPATPDFRSVLGGKKKLPAENGSSSAETLNAKAVESSKPLSNAQPSGPLKPVGNAKPAETLKPMGNAKPAETLKPMGNAKPDENLKSASKEELKKDVKNDVNCKRGHAGTTDNEKRSESQGTAPAFKQKLQDVHVAEGKKLLLQCQVSSDPPATIIWTLNGKTLKTTKFIILSQEGSLCSVSIEKALPEDRGLYKCVAKNDAGQAECSCQVTVDDAPASENTKAPEMKSRRPKSSLPPVLGTESDATVKKKPAPKTPPKAAMPPQIIQFPEDQKVRAGESVELFGKVTGTQPITCTWMKFRKQIQESEHMKVENSENGSKLTILAARQEHCGCYTLLVENKLGSRQAQVNLTVVDKPDPPAGTPCASDIRSSSLTLSWYGSSYDGGSAVQSYSIEIWDSANKTWKELATCRSTSFNVQDLLPDHEYKFRVRAINVYGTSEPSQESELTTVGEKPEEPKDEVEVSDDDEKEPEVDYRTVTINTEQKVSDFYDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTRIKLIDFGLARRLENAGSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFISNLLKKDMKNRLDCTQCLQHPWLMKDTKNMEAKKLSKDRMKKYMARRKWQKTGNAVRAIGRLSSMAMISGLSGRKSSTGSPTSPLNAEKLESEEDVSQAFLEAVAEEKPHVKPYFSKTIRDLEVVEGSAARFDCKIEGYPDPEVVWFKDDQSIRESRHFQIDYDEDGNCSLIISDVCGDDDAKYTCKAVNSLGEATCTAELIVETMEEGEGEGEEEEE
uniprot
proteins
disease_involvement
DISEASE: Aortic aneurysm, familial thoracic 7 (AAT7) [MIM:613780]: A disease characterized by permanent dilation of the thoracic aorta usually due to degenerative changes in the aortic wall. It is primarily associated with a characteristic histologic appearance known as 'medial necrosis' or 'Erdheim cystic medial necrosis' in which there is degeneration and fragmentation of elastic fibers, loss of smooth muscle cells, and an accumulation of basophilic ground substance. {ECO:0000269|PubMed:21055718, ECO:0000269|PubMed:28401540, ECO:0000269|PubMed:29544503}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Megacystis-microcolon-intestinal hypoperistalsis syndrome (MMIHS) [MIM:249210]: A form of megacystis-microcolon-intestinal hypoperistalsis syndrome, a congenital visceral myopathy primarily affecting females, and characterized by loss of smooth muscle contraction in the bladder and intestine. Affected individuals present at birth with functional obstruction of intestine, microcolon, dilation of bladder, and secondary hydronephrosis. The majority of cases have a fatal outcome due to malnutrition and sepsis, followed by multiorgan failure. MMIHS inheritance is autosomal recessive. {ECO:0000269|PubMed:28602422}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.7.11.18
uniprot
proteins
function
FUNCTION: Calcium/calmodulin-dependent myosin light chain kinase implicated in smooth muscle contraction via phosphorylation of myosin light chains (MLC) (PubMed:11113114). Also regulates actin-myosin interaction through a non-kinase activity (PubMed:11113114). Phosphorylates PTK2B/PYK2 and myosin light-chains (PubMed:11113114, PubMed:18587400). Involved in the inflammatory response (e.g. apoptosis, vascular permeability, leukocyte diapedesis), cell motility and morphology, airway hyperreactivity and other activities relevant to asthma (PubMed:20139351). Required for tonic airway smooth muscle contraction that is necessary for physiological and asthmatic airway resistance (By similarity). Necessary for gastrointestinal motility (By similarity). Implicated in the regulation of endothelial as well as vascular permeability, probably via the regulation of cytoskeletal rearrangements (By similarity). 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 (PubMed:20375339). Critical participant in signaling sequences that result in fibroblast apoptosis (PubMed:20453870). Plays a role in the regulation of epithelial cell survival (PubMed:16723733). Required for epithelial wound healing, especially during actomyosin ring contraction during purse-string wound closure (PubMed:15825080). Mediates RhoA-dependent membrane blebbing (PubMed:20181817). Triggers TRPC5 channel activity in a calcium-dependent signaling, by inducing its subcellular localization at the plasma membrane (PubMed:16284075). Promotes cell migration (including tumor cells) and tumor metastasis (PubMed:18710790, PubMed:19826488). PTK2B/PYK2 activation by phosphorylation mediates ITGB2 activation and is thus essential to trigger neutrophil transmigration during acute lung injury (ALI) (PubMed:18587400). May regulate optic nerve head astrocyte migration (PubMed:20375339). Probably involved in mitotic cytoskeletal regulation (PubMed:15020676). Regulates tight junction probably by modulating ZO-1 exchange in the perijunctional actomyosin ring (By similarity). Mediates burn-induced microvascular barrier injury; triggers endothelial contraction in the development of microvascular hyperpermeability by phosphorylating MLC (By similarity). Essential for intestinal barrier dysfunction (By similarity). Mediates Giardia spp.-mediated reduced epithelial barrier function during giardiasis intestinal infection via reorganization of cytoskeletal F-actin and tight junctional ZO-1 (By similarity). Necessary for hypotonicity-induced Ca(2+) entry and subsequent activation of volume-sensitive organic osmolyte/anion channels (VSOAC) in cervical cancer cells (PubMed:11976941). Responsible for high proliferative ability of breast cancer cells through anti-apoptosis (PubMed:20453870). {ECO:0000250|UniProtKB:Q6PDN3, ECO:0000269|PubMed:11113114, ECO:0000269|PubMed:11976941, ECO:0000269|PubMed:15020676, ECO:0000269|PubMed:15825080, ECO:0000269|PubMed:16284075, ECO:0000269|PubMed:16723733, ECO:0000269|PubMed:18587400, ECO:0000269|PubMed:18710790, ECO:0000269|PubMed:19826488, ECO:0000269|PubMed:20139351, ECO:0000269|PubMed:20181817, ECO:0000269|PubMed:20375339, ECO:0000269|PubMed:20453870}.
uniprot
proteins
mass_dalton
210715
uniprot
proteins
mutagenesis
MUTAGEN 608; /note="K->A: Loss of acetylation and no kinase activity repression by NAA10/ARD1."; /evidence="ECO:0000269|PubMed:19826488
uniprot
proteins
post_translational_modification
PTM: 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. {ECO:0000269|PubMed:11113114, ECO:0000269|PubMed:12408982, ECO:0000269|PubMed:20861316}.; PTM: 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). {ECO:0000250|UniProtKB:Q6PDN3}.; PTM: Acetylated at Lys-608 by NAA10/ARD1 via a calcium-dependent signaling; this acetylation represses kinase activity and reduces tumor cell migration. {ECO:0000269|PubMed:19826488}.
uniprot
proteins
protein_family
CAMK Ser/Thr protein kinase family
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
pubmed
10198165
uniprot
proteins
pubmed
10536370
uniprot
proteins
pubmed
11113114
uniprot
proteins
pubmed
11976941
uniprot
proteins
pubmed
12408982
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14741352
uniprot
proteins
pubmed
15020676
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15507455
uniprot
proteins
pubmed
15825080
uniprot
proteins
pubmed
16284075
uniprot
proteins
pubmed
16641997
uniprot
proteins
pubmed
16723733
uniprot
proteins
pubmed
16835238
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
18088087
uniprot
proteins
pubmed
18318008
uniprot
proteins
pubmed
18462678
uniprot
proteins
pubmed
18587400
uniprot
proteins
pubmed
18710790
uniprot
proteins
pubmed
19011151
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19429448
uniprot
proteins
pubmed
19826488
uniprot
proteins
pubmed
20053363
uniprot
proteins
pubmed
20139351
uniprot
proteins
pubmed
20181817
uniprot
proteins
pubmed
20375339
uniprot
proteins
pubmed
20453870
uniprot
proteins
pubmed
20861316
uniprot
proteins
pubmed
21055718
uniprot
proteins
pubmed
21918590
uniprot
proteins
pubmed
22015949
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
28401540
uniprot
proteins
pubmed
28602422
uniprot
proteins
pubmed
29537095
uniprot
proteins
pubmed
29544503
uniprot
proteins
pubmed
8575746
uniprot
proteins
pubmed
9160829
uniprot
proteins
sequence_length
1914
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20053363}. Cell projection, lamellipodium {ECO:0000269|PubMed:20053363}. Cleavage furrow {ECO:0000269|PubMed:15020676}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000269|PubMed:15020676}. Note=Localized to stress fibers during interphase and to the cleavage furrow during mitosis. {ECO:0000269|PubMed:15020676}.
uniprot
proteins