ML12B_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ML12B_RAT
• UniProt AC: P18666
• Protein Name: Myosin regulatory light chain 12B
• Gene Name: Myl12b
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 172
• Protein Description: 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..
• Protein Sequence: MSSKKAKTKTTKKRPQRATSNVFAMFDQSQIQEFKEAFNMIDQNRDGFIDKEDLHDMLASLGKNPTDAYLDAMMNEAPGRINFTMFLTMFGEKLNGTDPEDVIRNAFACFDEEATGTIQEDYLRELLTTMGDRFTDEEVDELYREAPIDKKGNFNYIEFTRILKHGAKDKDD

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
19	Phosphorylation	KKRPQRATSNVFAMF CCCCCHHHHHHHHHC	24.03	11384979
20	Phosphorylation	KRPQRATSNVFAMFD CCCCHHHHHHHHHCC	29.97	11384979
29	Phosphorylation	VFAMFDQSQIQEFKE HHHHCCHHHHHHHHH	30.97	28689409
51	Acetylation	NRDGFIDKEDLHDML CCCCCCCHHHHHHHH	48.59	72626221
135	Phosphorylation	TTMGDRFTDEEVDEL HHCCCCCCHHHHHHH	43.31	30181290
156	Phosphorylation	DKKGNFNYIEFTRIL CCCCCCCCEEHHHHH	9.55	27097102

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
19	T	Phosphorylation	Kinase	MYLK	D3ZFU9	GPS
19	T	Phosphorylation	Kinase	DAPK3	O88764	Uniprot
19	T	Phosphorylation	Kinase	PRKACA	P00517	GPS
19	T	Phosphorylation	Kinase	MLCK	-	Uniprot
20	S	Phosphorylation	Kinase	DAPK3	O88764	Uniprot
20	S	Phosphorylation	Kinase	PRKACA	P00517	GPS
20	S	Phosphorylation	Kinase	MYLK	Q15746	GPS
20	S	Phosphorylation	Kinase	MLCK	-	Uniprot

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ML12B_RAT !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of ML12B_RAT !!

Protein-Protein Interaction

Oops, there are no PPI records of ML12B_RAT !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Zipper-interacting protein kinase induces Ca(2+)-free smooth musclecontraction via myosin light chain phosphorylation.";
Niiro N., Ikebe M.;
J. Biol. Chem. 276:29567-29574(2001).
Cited for: PHOSPHORYLATION AT THR-19 AND SER-20 BY ZIPK/DAPK3.
PubMed: 11384979