dbPTM

ML12B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ML12B_HUMAN
UniProt AC	O14950
Protein Name	Myosin regulatory light chain 12B
Gene Name	MYL12B
Organism	Homo sapiens (Human).
Sequence Length	172
Subcellular Localization
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	MSSKKAKTKTTKKRPQRATSNVFAMFDQSQIQEFKEAFNMIDQNRDGFIDKEDLHDMLASLGKNPTDAYLDAMMNEAPGPINFTMFLTMFGEKLNGTDPEDVIRNAFACFDEEATGTIQEDYLRELLTTMGDRFTDEEVDELYREAPIDKKGNFNYIEFTRILKHGAKDKDD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
9	Ubiquitination	SSKKAKTKTTKKRPQ CCCCCCCCCCCCCCC	54.19	24816145
10	Phosphorylation	SKKAKTKTTKKRPQR CCCCCCCCCCCCCCH	49.43	-
11	Phosphorylation	KKAKTKTTKKRPQRA CCCCCCCCCCCCCHH	35.80	22817900
13	Ubiquitination	AKTKTTKKRPQRATS CCCCCCCCCCCHHHH	68.19	24816145
15	Ubiquitination	TKTTKKRPQRATSNV CCCCCCCCCHHHHHH	36.57	24816145
18	Phosphorylation	TKKRPQRATSNVFAM CCCCCCHHHHHHHHH	15.33	32142685
19	Phosphorylation	KKRPQRATSNVFAMF CCCCCHHHHHHHHHC	24.03	11384979
20	Phosphorylation	KRPQRATSNVFAMFD CCCCHHHHHHHHHCC	29.97	11384979
24	Phosphorylation	RATSNVFAMFDQSQI HHHHHHHHHCCHHHH	8.08	32142685
25	Phosphorylation	ATSNVFAMFDQSQIQ HHHHHHHHCCHHHHH	2.30	32645325
25	Sulfoxidation	ATSNVFAMFDQSQIQ HHHHHHHHCCHHHHH	2.30	21406390
29	Phosphorylation	VFAMFDQSQIQEFKE HHHHCCHHHHHHHHH	30.97	30266825
34	Ubiquitination	DQSQIQEFKEAFNMI CHHHHHHHHHHHHHH	5.06	23503661
35	Ubiquitination	QSQIQEFKEAFNMID HHHHHHHHHHHHHHH	47.59	23503661
40	Ubiquitination	EFKEAFNMIDQNRDG HHHHHHHHHHCCCCC	2.63	23503661
40	Sulfoxidation	EFKEAFNMIDQNRDG HHHHHHHHHHCCCCC	2.63	21406390
50	Ubiquitination	QNRDGFIDKEDLHDM CCCCCCCCHHHHHHH	46.13	23000965
51	2-Hydroxyisobutyrylation	NRDGFIDKEDLHDML CCCCCCCHHHHHHHH	48.59	-
51	Acetylation	NRDGFIDKEDLHDML CCCCCCCHHHHHHHH	48.59	25825284
51	Ubiquitination	NRDGFIDKEDLHDML CCCCCCCHHHHHHHH	48.59	23000965
56	Ubiquitination	IDKEDLHDMLASLGK CCHHHHHHHHHHCCC	40.88	23000965
60	Phosphorylation	DLHDMLASLGKNPTD HHHHHHHHCCCCHHH	33.42	20068231
97	Phosphorylation	FGEKLNGTDPEDVIR HHHHHCCCCHHHHHH	47.51	21712546
109	Glutathionylation	VIRNAFACFDEEATG HHHHHHHHCCCCCCC	3.40	22555962
128	Phosphorylation	DYLRELLTTMGDRFT HHHHHHHHHCCCCCC	27.62	30108239
129	Phosphorylation	YLRELLTTMGDRFTD HHHHHHHHCCCCCCH	21.08	30108239
130	Sulfoxidation	LRELLTTMGDRFTDE HHHHHHHCCCCCCHH	4.41	21406390
133	Methylation	LLTTMGDRFTDEEVD HHHHCCCCCCHHHHH	30.54	-
135	Phosphorylation	TTMGDRFTDEEVDEL HHCCCCCCHHHHHHH	43.31	30266825
143	Phosphorylation	DEEVDELYREAPIDK HHHHHHHHHHCCCCC	12.36	30108239
149	Ubiquitination	LYREAPIDKKGNFNY HHHHCCCCCCCCCCC	45.62	23000965
150	Ubiquitination	YREAPIDKKGNFNYI HHHCCCCCCCCCCCE	64.40	23000965
150	Acetylation	YREAPIDKKGNFNYI HHHCCCCCCCCCCCE	64.40	25953088
151	Acetylation	REAPIDKKGNFNYIE HHCCCCCCCCCCCEE	56.17	26051181
151	Sumoylation	REAPIDKKGNFNYIE HHCCCCCCCCCCCEE	56.17	-
151	Ubiquitination	REAPIDKKGNFNYIE HHCCCCCCCCCCCEE	56.17	23000965
151	Sumoylation	REAPIDKKGNFNYIE HHCCCCCCCCCCCEE	56.17	-
155	Ubiquitination	IDKKGNFNYIEFTRI CCCCCCCCCEEHHHH	40.65	23000965
156	Ubiquitination	DKKGNFNYIEFTRIL CCCCCCCCEEHHHHH	9.55	23000965
156	Phosphorylation	DKKGNFNYIEFTRIL CCCCCCCCEEHHHHH	9.55	28796482
160	Phosphorylation	NFNYIEFTRILKHGA CCCCEEHHHHHHCCC	12.19	28152594
163	Ubiquitination	YIEFTRILKHGAKDK CEEHHHHHHCCCCCC	2.78	33845483
164	Ubiquitination	IEFTRILKHGAKDKD EEHHHHHHCCCCCCC	37.31	33845483
167	Ubiquitination	TRILKHGAKDKDD-- HHHHHCCCCCCCC--	19.32	24816145
168	Ubiquitination	RILKHGAKDKDD--- HHHHCCCCCCCC---	70.65	24816145
168	Acetylation	RILKHGAKDKDD--- HHHHCCCCCCCC---	70.65	11920981
169	Ubiquitination	ILKHGAKDKDD---- HHHCCCCCCCC----	60.11	33845483
173	Ubiquitination	GAKDKDD-------- CCCCCCC--------		24816145

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	DAPK3	O43293	Uniprot
19	T	Phosphorylation	Kinase	ILK	Q13418	PSP
19	T	Phosphorylation	Kinase	MAP3K12	Q12852	GPS
19	T	Phosphorylation	Kinase	MYLK	Q15746	GPS
19	T	Phosphorylation	Kinase	ROCK1	Q13464	PSP
19	T	Phosphorylation	Kinase	MLCK	-	Uniprot
20	S	Phosphorylation	Kinase	AURKB	Q96GD4	GPS
20	S	Phosphorylation	Kinase	DAPK1	P53355	PSP
20	S	Phosphorylation	Kinase	DAPK1	Q80YE7	PSP
20	S	Phosphorylation	Kinase	DAPK3	O43293	Uniprot
20	S	Phosphorylation	Kinase	ILK	Q13418	PSP
20	S	Phosphorylation	Kinase	MAP3K12	Q12852	GPS
20	S	Phosphorylation	Kinase	MYLK	Q15746	GPS
20	S	Phosphorylation	Kinase	ROCK1	Q13464	PSP
20	S	Phosphorylation	Kinase	MLCK	-	Uniprot
135	T	Phosphorylation	Kinase	CSNK2A1	P68400	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ML12B_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of ML12B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PA2G4_HUMAN	PA2G4	physical	27173435
TRAP1_HUMAN	TRAP1	physical	27173435
SND1_HUMAN	SND1	physical	27173435
CPSF6_HUMAN	CPSF6	physical	27173435
UBE2N_HUMAN	UBE2N	physical	27173435

Drug and Disease Associations

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

Regulatory Network of ML12B_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Epigallocatechin-3-O-gallate disrupts stress fibers and thecontractile ring by reducing myosin regulatory light chainphosphorylation mediated through the target molecule 67 kDa lamininreceptor."; Umeda D., Tachibana H., Yamada K.; Biochem. Biophys. Res. Commun. 333:628-635(2005). Cited for: PHOSPHORYLATION AT THR-19 AND SER-20.	15946647 [Abstract]
"Phosphorylation of myosin II regulatory light chain is necessary formigration of HeLa cells but not for localization of myosin II at theleading edge."; Fumoto K., Uchimura T., Iwasaki T., Ueda K., Hosoya H.; Biochem. J. 370:551-556(2003). Cited for: PHOSPHORYLATION AT THR-19 AND SER-20, AND MUTAGENESIS OF19-THR-SER-20.	12429016 [Abstract]
"Diphosphorylated MRLC is required for organization of stress fibersin interphase cells and the contractile ring in dividing cells."; Iwasaki T., Murata-Hori M., Ishitobi S., Hosoya H.; Cell Struct. Funct. 26:677-683(2001). Cited for: NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION AT THR-19 AND SER-20, ANDMUTAGENESIS OF 19-THR-SER-20.	11942626 [Abstract]