ML12A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ML12A_HUMAN
• UniProt AC: P19105
• Protein Name: Myosin regulatory light chain 12A
• Gene Name: MYL12A
• Organism: Homo sapiens (Human).
• Sequence Length: 171
• Protein Description: Myosin regulatory subunit that plays an important role in regulation of both smooth muscle and nonmuscle cell contractile activity via its phosphorylation. Implicated in cytokinesis, receptor capping, and cell locomotion (By similarity)..
• Protein Sequence: MSSKRTKTKTKKRPQRATSNVFAMFDQSQIQEFKEAFNMIDQNRDGFIDKEDLHDMLASLGKNPTDEYLDAMMNEAPGPINFTMFLTMFGEKLNGTDPEDVIRNAFACFDEEATGTIQEDYLRELLTTMGDRFTDEEVDELYREAPIDKKGNFNYIEFTRILKHGAKDKDD

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
10	Phosphorylation	SKRTKTKTKKRPQRA CCCCCCCCCCCCCHH	47.21	22817900
16	Phosphorylation	KTKKRPQRATSNVFA CCCCCCCHHHHHHHH	42.38	-
18	Phosphorylation	KKRPQRATSNVFAMF CCCCCHHHHHHHHHC	24.03	29255136
19	Phosphorylation	KRPQRATSNVFAMFD CCCCHHHHHHHHHCC	29.97	29255136
24	Phosphorylation	ATSNVFAMFDQSQIQ HHHHHHHHCCHHHHH	2.30	15946647
25	Phosphorylation	TSNVFAMFDQSQIQE HHHHHHHCCHHHHHH	7.48	15946647
28	Phosphorylation	VFAMFDQSQIQEFKE HHHHCCHHHHHHHHH	30.97	30266825
34	Phosphorylation	QSQIQEFKEAFNMID HHHHHHHHHHHHHHH	47.59	-
50	Acetylation	NRDGFIDKEDLHDML CCCCCCCHHHHHHHH	48.59	42358353
50	Ubiquitination	NRDGFIDKEDLHDML CCCCCCCHHHHHHHH	48.59	21890473
50	Ubiquitination	NRDGFIDKEDLHDML CCCCCCCHHHHHHHH	48.59	21890473
56	Ubiquitination	DKEDLHDMLASLGKN CHHHHHHHHHHCCCC	2.04	-
56	Acetylation	DKEDLHDMLASLGKN CHHHHHHHHHHCCCC	2.04	-
59	Phosphorylation	DLHDMLASLGKNPTD HHHHHHHHCCCCCCH	33.42	20068231
65	Phosphorylation	ASLGKNPTDEYLDAM HHCCCCCCHHHHHHH	51.35	20068231
96	Phosphorylation	FGEKLNGTDPEDVIR HHHHHCCCCHHHHHH	47.51	21712546
102	Phosphorylation	GTDPEDVIRNAFACF CCCHHHHHHHHHHHC	4.32	-
108	Glutathionylation	VIRNAFACFDEEATG HHHHHHHHCCCCCCC	3.40	22555962
127	Phosphorylation	DYLRELLTTMGDRFT HHHHHHHHHCCCCCC	27.62	30108239
128	O-linked_Glycosylation	YLRELLTTMGDRFTD HHHHHHHHCCCCCCH	21.08	29351928
128	Phosphorylation	YLRELLTTMGDRFTD HHHHHHHHCCCCCCH	21.08	30108239
129	Sulfoxidation	LRELLTTMGDRFTDE HHHHHHHCCCCCCHH	4.41	30846556
132	Methylation	LLTTMGDRFTDEEVD HHHHCCCCCCHHHHH	30.54	-
133	Phosphorylation	LTTMGDRFTDEEVDE HHHCCCCCCHHHHHH	13.86	20068231
134	Phosphorylation	TTMGDRFTDEEVDEL HHCCCCCCHHHHHHH	43.31	30266825
138	Methylation	DRFTDEEVDELYREA CCCCHHHHHHHHHHC	6.97	-
140	Phosphorylation	FTDEEVDELYREAPI CCHHHHHHHHHHCCC	53.53	-
142	Phosphorylation	DEEVDELYREAPIDK HHHHHHHHHHCCCCC	12.36	30108239
148	Phosphorylation	LYREAPIDKKGNFNY HHHHCCCCCCCCCCC	45.62	-
149	Ubiquitination	YREAPIDKKGNFNYI HHHCCCCCCCCCCCE	64.40	21890473
149	Ubiquitination	YREAPIDKKGNFNYI HHHCCCCCCCCCCCE	64.40	21890473
150	Ubiquitination	REAPIDKKGNFNYIE HHCCCCCCCCCCCEE	56.17	21890473
150	Sumoylation	REAPIDKKGNFNYIE HHCCCCCCCCCCCEE	56.17	-
150	Ubiquitination	REAPIDKKGNFNYIE HHCCCCCCCCCCCEE	56.17	21890473
155	Ubiquitination	DKKGNFNYIEFTRIL CCCCCCCCEEHHHHH	9.55	-
155	Phosphorylation	DKKGNFNYIEFTRIL CCCCCCCCEEHHHHH	9.55	28796482
156	Ubiquitination	KKGNFNYIEFTRILK CCCCCCCEEHHHHHH	3.54	-
156	Sumoylation	KKGNFNYIEFTRILK CCCCCCCEEHHHHHH	3.54	-
159	Phosphorylation	NFNYIEFTRILKHGA CCCCEEHHHHHHCCC	12.19	28152594
161	Phosphorylation	NYIEFTRILKHGAKD CCEEHHHHHHCCCCC	5.66	-
163	Ubiquitination	IEFTRILKHGAKDKD EEHHHHHHCCCCCCC	37.31	-
169	Ubiquitination	LKHGAKDKDD----- HHCCCCCCCC-----	64.19	-

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
18	T	Phosphorylation	Kinase	MYLK	P11799	GPS
18	T	Phosphorylation	Kinase	ROCK1	Q13464	PhosphoELM
18	T	Phosphorylation	Kinase	MLCK	-	Uniprot
19	S	Phosphorylation	Kinase	RSK2	P51812	PSP
19	S	Phosphorylation	Kinase	MYLK	P11799	GPS
19	S	Phosphorylation	Kinase	ROCK1	Q13464	PhosphoELM
19	S	Phosphorylation	Kinase	MLCK	-	Uniprot

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ML12A_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of ML12A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RL18_HUMAN	RPL18	physical	22939629
NDUB4_HUMAN	NDUFB4	physical	22939629
RT21_HUMAN	MRPS21	physical	22939629
QCR7_HUMAN	UQCRB	physical	22939629
MPCP_HUMAN	SLC25A3	physical	22939629
RL13_HUMAN	RPL13	physical	22939629
SUV92_HUMAN	SUV39H2	physical	23455924
GLSK_HUMAN	GLS	physical	22863883
HERC1_HUMAN	HERC1	physical	22863883
MYL6_HUMAN	MYL6	physical	22863883
MYL9_HUMAN	MYL9	physical	22863883

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.

Related Literatures of Post-Translational Modification

Phosphorylation

"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-18; SER-19 AND THR-134,AND MASS SPECTROMETRY.
PubMed: 19690332

"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-18 AND SER-19, AND MASSSPECTROMETRY.
PubMed: 17924679