dbPTM

TPM4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TPM4_HUMAN
UniProt AC	P67936
Protein Name	Tropomyosin alpha-4 chain
Gene Name	TPM4
Organism	Homo sapiens (Human).
Sequence Length	248
Subcellular Localization	Cytoplasm, cytoskeleton . Associates with F-actin stress fibers.
Protein Description	Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments (By similarity). Binds calcium. [PubMed: 1836432]
Protein Sequence	MAGLNSLEAVKRKIQALQQQADEAEDRAQGLQRELDGERERREKAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSELKCGDLEEELKNVTNNLKSLEAASEKYSEKEDKYEEEIKLLSDKLKEAETRAEFAERTVAKLEKTIDDLEEKLAQAKEENVGLHQTLDQTLNELNCI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAGLNSLEA ------CCCHHHHHH	31.05	22223895
6	Phosphorylation	--MAGLNSLEAVKRK --CCCHHHHHHHHHH	32.40	23401153
11	Acetylation	LNSLEAVKRKIQALQ HHHHHHHHHHHHHHH	55.83	23749302
11	Ubiquitination	LNSLEAVKRKIQALQ HHHHHHHHHHHHHHH	55.83	-
11	Malonylation	LNSLEAVKRKIQALQ HHHHHHHHHHHHHHH	55.83	26320211
13	Ubiquitination	SLEAVKRKIQALQQQ HHHHHHHHHHHHHHH	33.19	-
13	Malonylation	SLEAVKRKIQALQQQ HHHHHHHHHHHHHHH	33.19	26320211
13 (in isoform 1)	Ubiquitination	-	33.19	21890473
27	Methylation	QADEAEDRAQGLQRE HHHHHHHHHHHHHHH	21.95	115918825
30 (in isoform 2)	Ubiquitination	-	23.85	-
37 (in isoform 2)	Ubiquitination	-	48.78	-
44	Malonylation	GERERREKAEGDVAA HHHHHHHHHHHHHHH	50.34	26320211
44	Acetylation	GERERREKAEGDVAA HHHHHHHHHHHHHHH	50.34	25953088
61 (in isoform 2)	Phosphorylation	-	57.28	28985074
72	Phosphorylation	RAQERLATALQKLEE HHHHHHHHHHHHHHH	32.28	24692096
76	Acetylation	RLATALQKLEEAEKA HHHHHHHHHHHHHHH	59.73	22632919
76	Ubiquitination	RLATALQKLEEAEKA HHHHHHHHHHHHHHH	59.73	-
79 (in isoform 2)	Phosphorylation	-	72.98	26657352
82 (in isoform 1)	Ubiquitination	-	56.79	21890473
82	Acetylation	QKLEEAEKAADESER HHHHHHHHHHHHHHH	56.79	88217
82	Ubiquitination	QKLEEAEKAADESER HHHHHHHHHHHHHHH	56.79	21906983
87	Phosphorylation	AEKAADESERGMKVI HHHHHHHHHHHHHHH	32.89	26437602
92	Sumoylation	DESERGMKVIENRAM HHHHHHHHHHHHHHC	42.77	-
92	Sumoylation	DESERGMKVIENRAM HHHHHHHHHHHHHHC	42.77	-
92	Ubiquitination	DESERGMKVIENRAM HHHHHHHHHHHHHHC	42.77	-
100	Ubiquitination	VIENRAMKDEEKMEI HHHHHHCCHHHHHHH	62.09	-
105	Sulfoxidation	AMKDEEKMEIQEMQL HCCHHHHHHHHHHHH	6.58	21406390
113	Ubiquitination	EIQEMQLKEAKHIAE HHHHHHHHHHHHHHH	38.44	-
116	Ubiquitination	EMQLKEAKHIAEEAD HHHHHHHHHHHHHHH	36.31	-
116	Acetylation	EMQLKEAKHIAEEAD HHHHHHHHHHHHHHH	36.31	7719623
118 (in isoform 2)	Ubiquitination	-	5.20	21890473
124	Methylation	HIAEEADRKYEEVAR HHHHHHHHHHHHHHH	50.97	-
125	Acetylation	IAEEADRKYEEVARK HHHHHHHHHHHHHHH	58.52	22632901
126	Phosphorylation	AEEADRKYEEVARKL HHHHHHHHHHHHHHH	20.44	21082442
132 (in isoform 1)	Ubiquitination	-	37.05	21890473
132	Ubiquitination	KYEEVARKLVILEGE HHHHHHHHHHHHHHH	37.05	-
153	Acetylation	RAEVSELKCGDLEEE HHHHHHCCCCCHHHH	31.92	25953088
153	Ubiquitination	RAEVSELKCGDLEEE HHHHHHCCCCCHHHH	31.92	-
154	S-nitrosocysteine	AEVSELKCGDLEEEL HHHHHCCCCCHHHHH	8.84	-
154	S-nitrosylation	AEVSELKCGDLEEEL HHHHHCCCCCHHHHH	8.84	20140087
154	Glutathionylation	AEVSELKCGDLEEEL HHHHHCCCCCHHHHH	8.84	22555962
162	Ubiquitination	GDLEEELKNVTNNLK CCHHHHHHHHHHHHH	53.29	-
165	Phosphorylation	EEELKNVTNNLKSLE HHHHHHHHHHHHHHH	27.99	26657352
168 (in isoform 2)	Ubiquitination	-	4.29	21890473
169	Malonylation	KNVTNNLKSLEAASE HHHHHHHHHHHHHHH	55.93	26320211
169	Ubiquitination	KNVTNNLKSLEAASE HHHHHHHHHHHHHHH	55.93	21890473
170	Phosphorylation	NVTNNLKSLEAASEK HHHHHHHHHHHHHHH	34.31	25849741
175	Phosphorylation	LKSLEAASEKYSEKE HHHHHHHHHHHHHHH	41.49	30108239
177	Acetylation	SLEAASEKYSEKEDK HHHHHHHHHHHHHHH	52.13	19608861
177	Ubiquitination	SLEAASEKYSEKEDK HHHHHHHHHHHHHHH	52.13	19608861
177 (in isoform 1)	Ubiquitination	-	52.13	21890473
178	Phosphorylation	LEAASEKYSEKEDKY HHHHHHHHHHHHHHH	20.29	26657352
179	Phosphorylation	EAASEKYSEKEDKYE HHHHHHHHHHHHHHH	53.94	25849741
181	Acetylation	ASEKYSEKEDKYEEE HHHHHHHHHHHHHHH	66.33	26051181
181	Malonylation	ASEKYSEKEDKYEEE HHHHHHHHHHHHHHH	66.33	26320211
184	Methylation	KYSEKEDKYEEEIKL HHHHHHHHHHHHHHH	56.50	22632913
184	Acetylation	KYSEKEDKYEEEIKL HHHHHHHHHHHHHHH	56.50	26051181
184	Ubiquitination	KYSEKEDKYEEEIKL HHHHHHHHHHHHHHH	56.50	21906983
184 (in isoform 1)	Ubiquitination	-	56.50	21890473
185	Phosphorylation	YSEKEDKYEEEIKLL HHHHHHHHHHHHHHH	40.68	26437602
190	Ubiquitination	DKYEEEIKLLSDKLK HHHHHHHHHHHHHHH	46.81	21890473
195	Ubiquitination	EIKLLSDKLKEAETR HHHHHHHHHHHHHHH	59.07	-
195	Malonylation	EIKLLSDKLKEAETR HHHHHHHHHHHHHHH	59.07	26320211
197	Ubiquitination	KLLSDKLKEAETRAE HHHHHHHHHHHHHHH	61.70	-
201	Phosphorylation	DKLKEAETRAEFAER HHHHHHHHHHHHHHH	42.08	26437602
209	Phosphorylation	RAEFAERTVAKLEKT HHHHHHHHHHHHHHH	19.13	21601212
212	Ubiquitination	FAERTVAKLEKTIDD HHHHHHHHHHHHHHH	53.49	-
212	Acetylation	FAERTVAKLEKTIDD HHHHHHHHHHHHHHH	53.49	25953088
213 (in isoform 2)	Ubiquitination	-	6.18	21890473
213	Acetylation	AERTVAKLEKTIDDL HHHHHHHHHHHHHHH	6.18	19608861
213	Ubiquitination	AERTVAKLEKTIDDL HHHHHHHHHHHHHHH	6.18	19608861
215	Malonylation	RTVAKLEKTIDDLEE HHHHHHHHHHHHHHH	62.31	26320211
215	Acetylation	RTVAKLEKTIDDLEE HHHHHHHHHHHHHHH	62.31	19608861
215 (in isoform 1)	Ubiquitination	-	62.31	21890473
215	Ubiquitination	RTVAKLEKTIDDLEE HHHHHHHHHHHHHHH	62.31	-
216	Phosphorylation	TVAKLEKTIDDLEEK HHHHHHHHHHHHHHH	21.91	29255136
220 (in isoform 2)	Ubiquitination	-	8.98	21890473
223	Malonylation	TIDDLEEKLAQAKEE HHHHHHHHHHHHHHH	39.48	26320211
223	Acetylation	TIDDLEEKLAQAKEE HHHHHHHHHHHHHHH	39.48	23236377
223	Ubiquitination	TIDDLEEKLAQAKEE HHHHHHHHHHHHHHH	39.48	-
228	Ubiquitination	EEKLAQAKEENVGLH HHHHHHHHHHCCCHH	54.18	-
237	Phosphorylation	ENVGLHQTLDQTLNE HCCCHHHHHHHHHHH	22.89	30576142
241	Phosphorylation	LHQTLDQTLNELNCI HHHHHHHHHHHHCCC	31.08	30576142
247	Glutathionylation	QTLNELNCI------ HHHHHHCCC------	6.45	22555962
251 (in isoform 2)	Ubiquitination	-		21890473
251	Ubiquitination	ELNCI---------- HHCCC----------		19608861
251	Acetylation	ELNCI---------- HHCCC----------		19608861

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
-	K	Ubiquitination	E3 ubiquitin ligase	SMURF1	Q9HCE7	PMID:20804422

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TPM4_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 TPM4_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ZYX_HUMAN	ZYX	physical	22939629
CAP1_HUMAN	CAP1	physical	22863883
FAS_HUMAN	FASN	physical	22863883
LNX1_HUMAN	LNX1	physical	25416956
ACTN1_HUMAN	ACTN1	physical	26344197
ACTN2_HUMAN	ACTN2	physical	26344197
COX5A_HUMAN	COX5A	physical	26344197
OSTF1_HUMAN	OSTF1	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.

Regulatory Network of TPM4_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-76; LYS-125; LYS-177;LYS-184 AND LYS-215, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-126, AND MASSSPECTROMETRY.	18083107 [Abstract]