MYL9
entrez
10398
canonical
uniprot
P24844
canonical
ensembl
ENSG00000101335
resolver
ensp
ENSP00000217313
resolver
ensp
ENSP00000279022
resolver
genesymbol
MYL9
resolver
genesymbol_syn
MLC2
resolver
genesymbol_syn
MRLC1
resolver
genesymbol_syn
MYRL2
resolver
hgnc
HGNC:15754
resolver
uniprot
A0A384NY64
resolver
uniprot
E1P5T6
resolver
uniprot
Q9BQL9
resolver
uniprot
Q9BUF9
resolver
uniprot
Q9H136
resolver
uniprot_entry
A0A384NY64_HUMAN
resolver
uniprot_entry
MYL9_HUMAN
resolver
uniprot_sec
E1P5T6
resolver
uniprot_sec
Q9BQL9
resolver
uniprot_sec
Q9BUF9
resolver
uniprot_sec
Q9H136
resolver
amino_acid_sequence
MSSKRAKAKTTKKRPQRATSNVFAMFDQSQIQEFKEAFNMIDQNRDGFIDKEDLHDMLASLGKNPTDEYLEGMMSEAPGPINFTMFLTMFGEKLNGTDPEDVIRNAFACFDEEASGFIHEDHLRELLTTMGDRFTDEEVDEMYREAPIDKKGNFNYVEFTRILKHGAKDKDD
uniprot
proteins
disease_involvement
DISEASE: Megacystis-microcolon-intestinal hypoperistalsis syndrome 4 (MMIHS4) [MIM:619365]: 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. MMIHS4 inheritance is autosomal recessive. {ECO:0000269|PubMed:29453416, ECO:0000269|PubMed:33031641}. Note=The disease may be caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Myosin regulatory subunit that plays an important role in regulation of both smooth muscle and nonmuscle cell contractile activity via its phosphorylation (PubMed:11942626, PubMed:2526655). Implicated in cytokinesis, receptor capping, and cell locomotion (PubMed:11942626, PubMed:2526655). In myoblasts, may regulate PIEZO1-dependent cortical actomyosin assembly involved in myotube formation (By similarity). {ECO:0000250|UniProtKB:Q9CQ19, ECO:0000269|PubMed:11942626, ECO:0000269|PubMed:2526655}.
uniprot
proteins
mass_dalton
19827
uniprot
proteins
post_translational_modification
PTM: Phosphorylation by MLCK/MYLK increases the actin-activated myosin ATPase activity and thereby regulates the contractile activity (PubMed:11942626, PubMed:21457715). It is required to generate the driving force in the migration of the cells but not necessary for localization of myosin-2 at the leading edge (PubMed:11942626, PubMed:21457715). Phosphorylation is required for myotube formation (PubMed:11942626, PubMed:21457715). Phosphorylated by DAPK3; DAPK3-mediated phosphorylation is inhibited by LUZP1 (PubMed:38009294). {ECO:0000269|PubMed:11942626, ECO:0000269|PubMed:21457715, ECO:0000269|PubMed:38009294}.
uniprot
proteins
pubmed
11780052
uniprot
proteins
pubmed
11942626
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
18854160
uniprot
proteins
pubmed
21072057
uniprot
proteins
pubmed
21408167
uniprot
proteins
pubmed
21457715
uniprot
proteins
pubmed
2526655
uniprot
proteins
pubmed
29453416
uniprot
proteins
pubmed
33031641
uniprot
proteins
pubmed
38009294
uniprot
proteins
sequence_length
172
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9CQ19}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q9CQ19}. Note=Colocalizes with F-actin, MYH9 and PIEZO1 at the actomyosin cortex in myoblasts. {ECO:0000250|UniProtKB:Q9CQ19}.
uniprot
proteins