MYL12B
entrez
103910
canonical
uniprot
O14950
canonical
ensembl
ENSG00000118680
resolver
ensp
ENSP00000237500
resolver
ensp
ENSP00000383037
resolver
ensp
ENSP00000463559
resolver
ensp
ENSP00000464464
resolver
ensp
ENSP00000496809
resolver
ensp
ENSP00000544823
resolver
ensp
ENSP00000544824
resolver
ensp
ENSP00000544825
resolver
ensp
ENSP00000588515
resolver
ensp
ENSP00000588516
resolver
ensp
ENSP00000635149
resolver
enst
ENST00000237500
resolver
enst
ENST00000400175
resolver
enst
ENST00000581193
resolver
enst
ENST00000584539
resolver
enst
ENST00000648965
resolver
enst
ENST00000874764
resolver
enst
ENST00000874765
resolver
enst
ENST00000874766
resolver
enst
ENST00000918456
resolver
enst
ENST00000918457
resolver
enst
ENST00000965090
resolver
genesymbol
MYL12B
resolver
genesymbol_syn
MRLC2
resolver
genesymbol_syn
MYLC2B
resolver
hgnc
HGNC:29827
resolver
uniprot
D3DUH6
resolver
uniprot
Q13182
resolver
uniprot
Q7Z5Z4
resolver
uniprot_entry
ML12B_HUMAN
resolver
uniprot_sec
D3DUH6
resolver
uniprot_sec
Q13182
resolver
uniprot_sec
Q7Z5Z4
resolver
amino_acid_sequence
MSSKKAKTKTTKKRPQRATSNVFAMFDQSQIQEFKEAFNMIDQNRDGFIDKEDLHDMLASLGKNPTDAYLDAMMNEAPGPINFTMFLTMFGEKLNGTDPEDVIRNAFACFDEEATGTIQEDYLRELLTTMGDRFTDEEVDELYREAPIDKKGNFNYIEFTRILKHGAKDKDD
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. Phosphorylation triggers actin polymerization in vascular smooth muscle. Implicated in cytokinesis, receptor capping, and cell locomotion. {ECO:0000269|PubMed:10965042}.
uniprot
proteins
mass_dalton
19779
uniprot
proteins
mutagenesis
MUTAGEN 19..20; /note="TS->AA: Shows a decrease in the number of actin filament bundles."; /evidence="ECO:0000269|PubMed:11942626, ECO:0000269|PubMed:12429016, ECO:0000269|PubMed:12589046"; MUTAGEN 19..20; /note="TS->DD: Shows a larger number of actin filament bundles."; /evidence="ECO:0000269|PubMed:11942626, ECO:0000269|PubMed:12429016, ECO:0000269|PubMed:12589046
uniprot
proteins
post_translational_modification
PTM: Phosphorylation increases the actin-activated myosin ATPase activity and thereby regulates the contractile activity. 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. Phosphorylation is reduced following epigallocatechin-3-O-gallate treatment. {ECO:0000269|PubMed:11942626, ECO:0000269|PubMed:12429016, ECO:0000269|PubMed:15946647, ECO:0000269|PubMed:17126281}.
uniprot
proteins
pubmed
10965042
uniprot
proteins
pubmed
11436981
uniprot
proteins
pubmed
11942626
uniprot
proteins
pubmed
12429016
uniprot
proteins
pubmed
12589046
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15946647
uniprot
proteins
pubmed
17126281
uniprot
proteins
pubmed
18480596
uniprot
proteins
pubmed
24275569
uniprot
proteins
sequence_length
172
uniprot
proteins