MYL9_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: MYL9_HUMAN
• UniProt AC: P24844
• Protein Name: Myosin regulatory light polypeptide 9
• Gene Name: MYL9
• Organism: Homo sapiens (Human).
• 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. Implicated in cytokinesis, receptor capping, and cell locomotion..
• Protein Sequence: MSSKRAKAKTTKKRPQRATSNVFAMFDQSQIQEFKEAFNMIDQNRDGFIDKEDLHDMLASLGKNPTDEYLEGMMSEAPGPINFTMFLTMFGEKLNGTDPEDVIRNAFACFDEEASGFIHEDHLRELLTTMGDRFTDEEVDEMYREAPIDKKGNFNYVEFTRILKHGAKDKDD

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
2	Phosphorylation	------MSSKRAKAK ------CCCHHHHCC	44.56	18835557
2	Acetylation	------MSSKRAKAK ------CCCHHHHCC	44.56	-
3	Phosphorylation	-----MSSKRAKAKT -----CCCHHHHCCC	25.51	18835557
10	Phosphorylation	SKRAKAKTTKKRPQR CHHHHCCCCCCCCHH	49.02	18835557
11	Phosphorylation	KRAKAKTTKKRPQRA HHHHCCCCCCCCHHH	33.58	22817900
19	Phosphorylation	KKRPQRATSNVFAMF CCCCHHHHHHHHHHC	24.03	29255136
20	Phosphorylation	KRPQRATSNVFAMFD CCCHHHHHHHHHHCC	29.97	29255136
25	Sulfoxidation	ATSNVFAMFDQSQIQ HHHHHHHHCCHHHHH	2.30	30846556
29	Phosphorylation	VFAMFDQSQIQEFKE HHHHCCHHHHHHHHH	30.97	30266825
40	Sulfoxidation	EFKEAFNMIDQNRDG HHHHHHHHHHCCCCC	2.63	30846556
51	Acetylation	NRDGFIDKEDLHDML CCCCCCCHHHHHHHH	48.59	72626217
51	Ubiquitination	NRDGFIDKEDLHDML CCCCCCCHHHHHHHH	48.59	21906983
57	Sulfoxidation	DKEDLHDMLASLGKN CHHHHHHHHHHCCCC	2.04	30846556
60	Phosphorylation	DLHDMLASLGKNPTD HHHHHHHHCCCCCCH	33.42	20068231
97	Phosphorylation	FGEKLNGTDPEDVIR HHHHHCCCCHHHHHH	47.51	21712546
115	Phosphorylation	ACFDEEASGFIHEDH HHCCHHHHCCCCHHH	37.20	21712546
128	Phosphorylation	DHLRELLTTMGDRFT HHHHHHHHHHHCCCC	27.62	20068231
129	Phosphorylation	HLRELLTTMGDRFTD HHHHHHHHHHCCCCH	21.08	27251275
130	Sulfoxidation	LRELLTTMGDRFTDE HHHHHHHHHCCCCHH	4.41	30846556
135	Phosphorylation	TTMGDRFTDEEVDEM HHHHCCCCHHHHHHH	43.31	26657352
142	Sulfoxidation	TDEEVDEMYREAPID CHHHHHHHHHHCCCC	3.10	30846556
143	Phosphorylation	DEEVDEMYREAPIDK HHHHHHHHHHCCCCC	11.85	8578591
150	Ubiquitination	YREAPIDKKGNFNYV HHHCCCCCCCCCCCC	64.40	-
151	Ubiquitination	REAPIDKKGNFNYVE HHCCCCCCCCCCCCH	56.17	-
151	Sumoylation	REAPIDKKGNFNYVE HHCCCCCCCCCCCCH	56.17	-
151	Sumoylation	REAPIDKKGNFNYVE HHCCCCCCCCCCCCH	56.17	-
151	Malonylation	REAPIDKKGNFNYVE HHCCCCCCCCCCCCH	56.17	26320211
156	Phosphorylation	DKKGNFNYVEFTRIL CCCCCCCCCHHHHHH	9.38	21253578
164	Ubiquitination	VEFTRILKHGAKDKD CHHHHHHHCCCCCCC	37.31	-
168	Acetylation	RILKHGAKDKDD--- HHHHCCCCCCCC---	70.65	11921007

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
2	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
2	S	Phosphorylation	Kinase	PKCA	P04409	PSP
3	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
3	S	Phosphorylation	Kinase	PKCA	P04409	PSP
10	T	Phosphorylation	Kinase	PRKCA	P17252	GPS
10	T	Phosphorylation	Kinase	PKCA	P04409	PSP
19	T	Phosphorylation	Kinase	MYLK	Q15746	GPS
19	T	Phosphorylation	Kinase	ROCK1	Q13464	PSP
19	T	Phosphorylation	Kinase	ROCK2	O75116	Uniprot
19	T	Phosphorylation	Kinase	DAPK3	O43293	PhosphoELM
19	T	Phosphorylation	Kinase	ROCK2	P70336	PSP
19	T	Phosphorylation	Kinase	MLCK	-	Uniprot
19	T	Phosphorylation	Kinase	CRIK	O14578	PSP
20	S	Phosphorylation	Kinase	ROCK1	Q13464	Uniprot
20	S	Phosphorylation	Kinase	ROCK2	O75116	Uniprot
20	S	Phosphorylation	Kinase	PAK2	Q13177	PhosphoELM
20	S	Phosphorylation	Kinase	MRCK-SUBFAMILY	-	GPS
20	S	Phosphorylation	Kinase	PAK1	Q13153	Uniprot
20	S	Phosphorylation	Kinase	MYLK	Q15746	GPS
20	S	Phosphorylation	Kinase	MLCK	-	Uniprot
20	S	Phosphorylation	Kinase	SMMLCK	P11799	PSP
20	S	Phosphorylation	Kinase	CDC42BP	Q9Y5S2	Uniprot
20	S	Phosphorylation	Kinase	CDC42BPA	Q5VT25	GPS
20	S	Phosphorylation	Kinase	PRKCA	P04409	GPS
20	S	Phosphorylation	Kinase	CAMK1	Q63450	GPS
20	S	Phosphorylation	Kinase	CAMK1A	Q14012	PSP
20	S	Phosphorylation	Kinase	DAPK3	O43293	Uniprot
20	S	Phosphorylation	Kinase	DAPK2	Q9UIK4	Uniprot
20	S	Phosphorylation	Kinase	DAPK1	P53355	Uniprot
20	S	Phosphorylation	Kinase	CRIK	O14578	PSP
143	Y	Phosphorylation	Kinase	EGFR	P00533	PhosphoELM
156	Y	Phosphorylation	Kinase	EGFR	P00533	PhosphoELM

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of MYL9_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 MYL9_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
IF2B_HUMAN	EIF2S2	physical	26344197
EIF3I_HUMAN	EIF3I	physical	26344197
PI42B_HUMAN	PIP4K2B	physical	26344197
PI42C_HUMAN	PIP4K2C	physical	26344197

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

"New modularity of DAP-kinases: alternative splicing of the DRP-1 geneproduces a ZIPk-like isoform.";
Shoval Y., Berissi H., Kimchi A., Pietrokovski S.;
PLoS ONE 6:E17344-E17344(2011).
Cited for: PHOSPHORYLATION AT SER-20 BY DAPK1; DAPK2 AND ZIPK/DAPK3.
PubMed: 21408167

"Chelerythrine perturbs lamellar actomyosin filaments by selectiveinhibition of myotonic dystrophy kinase-related Cdc42-bindingkinase.";
Tan I., Lai J., Yong J., Li S.F., Leung T.;
FEBS Lett. 585:1260-1268(2011).
Cited for: PHOSPHORYLATION AT THR-19 AND SER-20.
PubMed: 21457715

"Caspase-activated ROCK-1 allows erythroblast terminal maturationindependently of cytokine-induced Rho signaling.";
Gabet A.S., Coulon S., Fricot A., Vandekerckhove J., Chang Y.,Ribeil J.A., Lordier L., Zermati Y., Asnafi V., Belaid Z., Debili N.,Vainchenker W., Varet B., Hermine O., Courtois G.;
Cell Death Differ. 18:678-689(2011).
Cited for: PHOSPHORYLATION AT SER-20.
PubMed: 21072057

"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-19 AND SER-20, AND MASSSPECTROMETRY.
PubMed: 18669648

"A tripartite complex containing MRCK modulates lamellar actomyosinretrograde flow.";
Tan I., Yong J., Dong J.M., Lim L., Leung T.;
Cell 135:123-136(2008).
Cited for: PHOSPHORYLATION AT SER-20.
PubMed: 18854160

"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-19 AND SER-20, AND MASSSPECTROMETRY.
PubMed: 17287340

"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] (ISOFORM 1), AND PHOSPHORYLATION AT THR-19AND SER-20.
PubMed: 11942626