dbPTM

TPM1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TPM1_MOUSE
UniProt AC	P58771
Protein Name	Tropomyosin alpha-1 chain
Gene Name	Tpm1
Organism	Mus musculus (Mouse).
Sequence Length	284
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..
Protein Sequence	MDAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEDELVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEELDHALNDMTSI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MDAIKKKM -------CHHHHHHH	7.68	-
7	Ubiquitination	-MDAIKKKMQMLKLD -CHHHHHHHHHHHCC	29.39	17451654
12	Ubiquitination	KKKMQMLKLDKENAL HHHHHHHHCCHHHHH	49.66	17451654
12	Acetylation	KKKMQMLKLDKENAL HHHHHHHHCCHHHHH	49.66	22826441
15	Acetylation	MQMLKLDKENALDRA HHHHHCCHHHHHHHH	64.40	21728379
15	Ubiquitination	MQMLKLDKENALDRA HHHHHCCHHHHHHHH	64.40	17451654
29	Ubiquitination	AEQAEADKKAAEDRS HHHHHHHHHHHHHHH	51.89	17451654
30	Ubiquitination	EQAEADKKAAEDRSK HHHHHHHHHHHHHHH	54.07	17451654
37	Ubiquitination	KAAEDRSKQLEDELV HHHHHHHHHHHHHHH	60.85	17451654
45	Phosphorylation	QLEDELVSLQKKLKG HHHHHHHHHHHHHCC	37.39	23737553
48	Acetylation	DELVSLQKKLKGTED HHHHHHHHHHCCCHH	66.42	21728379
48	Ubiquitination	DELVSLQKKLKGTED HHHHHHHHHHCCCHH	66.42	17451654
49	Acetylation	ELVSLQKKLKGTEDE HHHHHHHHHCCCHHH	42.33	19863139
49	Ubiquitination	ELVSLQKKLKGTEDE HHHHHHHHHCCCHHH	42.33	17451654
51	Ubiquitination	VSLQKKLKGTEDELD HHHHHHHCCCHHHHH	73.07	17451654
53	Phosphorylation	LQKKLKGTEDELDKY HHHHHCCCHHHHHHH	38.38	28542873
59	Ubiquitination	GTEDELDKYSEALKD CCHHHHHHHHHHHHH	64.40	17451654
59	Acetylation	GTEDELDKYSEALKD CCHHHHHHHHHHHHH	64.40	19863153
60	Phosphorylation	TEDELDKYSEALKDA CHHHHHHHHHHHHHH	16.06	27742792
61	Phosphorylation	EDELDKYSEALKDAQ HHHHHHHHHHHHHHH	23.33	26824392
65	Ubiquitination	DKYSEALKDAQEKLE HHHHHHHHHHHHHHH	59.05	17451654
70	Ubiquitination	ALKDAQEKLELAEKK HHHHHHHHHHHHHHH	34.87	17451654
76	Ubiquitination	EKLELAEKKATDAEA HHHHHHHHHCCHHHH	41.94	17451654
77	Ubiquitination	KLELAEKKATDAEAD HHHHHHHHCCHHHHH	48.28	17451654
77	Acetylation	KLELAEKKATDAEAD HHHHHHHHCCHHHHH	48.28	19862381
79	Phosphorylation	ELAEKKATDAEADVA HHHHHHCCHHHHHHH	44.62	28464351
87	Phosphorylation	DAEADVASLNRRIQL HHHHHHHHHHHHHHH	26.48	27742792
108	Phosphorylation	RAQERLATALQKLEE HHHHHHHHHHHHHHH	32.28	22210690
112	Ubiquitination	RLATALQKLEEAEKA HHHHHHHHHHHHHHH	59.73	17451654
112	Acetylation	RLATALQKLEEAEKA HHHHHHHHHHHHHHH	59.73	22632953
118	Acetylation	QKLEEAEKAADESER HHHHHHHHHHHHHHH	56.79	88207
118	Ubiquitination	QKLEEAEKAADESER HHHHHHHHHHHHHHH	56.79	17451654
123	Phosphorylation	AEKAADESERGMKVI HHHHHHHHHHHHHHH	32.89	29899451
128	Ubiquitination	DESERGMKVIESRAQ HHHHHHHHHHHHHHH	42.77	17451654
132	Phosphorylation	RGMKVIESRAQKDEE HHHHHHHHHHHCCHH	23.07	22210690
136	Ubiquitination	VIESRAQKDEEKMEI HHHHHHHCCHHHHHH	67.15	17451654
136	Acetylation	VIESRAQKDEEKMEI HHHHHHHCCHHHHHH	67.15	21728379
140	Ubiquitination	RAQKDEEKMEIQEIQ HHHCCHHHHHHHHHH	39.52	17451654
140	Acetylation	RAQKDEEKMEIQEIQ HHHCCHHHHHHHHHH	39.52	21728379
149	Ubiquitination	EIQEIQLKEAKHIAE HHHHHHHHHHHHHHH	38.97	17451654
149	Acetylation	EIQEIQLKEAKHIAE HHHHHHHHHHHHHHH	38.97	21728379
152	Ubiquitination	EIQLKEAKHIAEDAD HHHHHHHHHHHHHHH	36.31	17451654
152	Acetylation	EIQLKEAKHIAEDAD HHHHHHHHHHHHHHH	36.31	21728379
161	Ubiquitination	IAEDADRKYEEVARK HHHHHHHHHHHHHHH	58.52	17451654
161	Acetylation	IAEDADRKYEEVARK HHHHHHHHHHHHHHH	58.52	21728379
162	Phosphorylation	AEDADRKYEEVARKL HHHHHHHHHHHHHHH	20.44	27742792
168	Ubiquitination	KYEEVARKLVIIESD HHHHHHHHHHHHHHH	37.05	17451654
174	Phosphorylation	RKLVIIESDLERAEE HHHHHHHHHHHHHHH	36.77	26824392
186	Phosphorylation	AEERAELSEGKCAEL HHHHHHHCCCHHHHH	35.49	19060867
189	Ubiquitination	RAELSEGKCAELEEE HHHHCCCHHHHHHHH	26.64	17451654
190	S-nitrosocysteine	AELSEGKCAELEEEL HHHCCCHHHHHHHHH	5.38	-
190	Glutathionylation	AELSEGKCAELEEEL HHHCCCHHHHHHHHH	5.38	24333276
190	S-nitrosylation	AELSEGKCAELEEEL HHHCCCHHHHHHHHH	5.38	20925432
198	Ubiquitination	AELEEELKTVTNNLK HHHHHHHHHHHHHHH	44.20	17451654
199	Phosphorylation	ELEEELKTVTNNLKS HHHHHHHHHHHHHHH	45.23	28542873
201	Phosphorylation	EEELKTVTNNLKSLE HHHHHHHHHHHHHHH	24.50	27742792
205	Ubiquitination	KTVTNNLKSLEAQAE HHHHHHHHHHHHHHH	55.93	17451654
205	Acetylation	KTVTNNLKSLEAQAE HHHHHHHHHHHHHHH	55.93	21728379
206	Phosphorylation	TVTNNLKSLEAQAEK HHHHHHHHHHHHHHH	34.31	26824392
213	Ubiquitination	SLEAQAEKYSQKEDK HHHHHHHHHHCCHHH	53.90	17451654
213	Acetylation	SLEAQAEKYSQKEDK HHHHHHHHHHCCHHH	53.90	22990633
214	Phosphorylation	LEAQAEKYSQKEDKY HHHHHHHHHCCHHHH	14.08	27742792
215	Phosphorylation	EAQAEKYSQKEDKYE HHHHHHHHCCHHHHH	45.93	26824392
217	Ubiquitination	QAEKYSQKEDKYEEE HHHHHHCCHHHHHHH	63.04	17451654
217	Acetylation	QAEKYSQKEDKYEEE HHHHHHCCHHHHHHH	63.04	30996229
220	Ubiquitination	KYSQKEDKYEEEIKV HHHCCHHHHHHHHHH	56.50	17451654
220	Acetylation	KYSQKEDKYEEEIKV HHHCCHHHHHHHHHH	56.50	21728379
221	Phosphorylation	YSQKEDKYEEEIKVL HHCCHHHHHHHHHHH	40.68	22210690
226	Ubiquitination	DKYEEEIKVLSDKLK HHHHHHHHHHHHHHH	40.16	17451654
231	Acetylation	EIKVLSDKLKEAETR HHHHHHHHHHHHHHH	59.07	21728379
231	Ubiquitination	EIKVLSDKLKEAETR HHHHHHHHHHHHHHH	59.07	17451654
233	Acetylation	KVLSDKLKEAETRAE HHHHHHHHHHHHHHH	61.70	21728379
233	Ubiquitination	KVLSDKLKEAETRAE HHHHHHHHHHHHHHH	61.70	17451654
237	Phosphorylation	DKLKEAETRAEFAER HHHHHHHHHHHHHHH	42.08	22210690
245 (in isoform 2)	Phosphorylation	-	26.16	28464351
245	Phosphorylation	RAEFAERSVTKLEKS HHHHHHHHHHHHHHC	26.16	28464351
248	Acetylation	FAERSVTKLEKSIDD HHHHHHHHHHHCHHH	53.12	21728379
248	Ubiquitination	FAERSVTKLEKSIDD HHHHHHHHHHHCHHH	53.12	17451654
251	Acetylation	RSVTKLEKSIDDLED HHHHHHHHCHHHHHH	64.25	21728379
251	Ubiquitination	RSVTKLEKSIDDLED HHHHHHHHCHHHHHH	64.25	17451654
252	Phosphorylation	SVTKLEKSIDDLEDE HHHHHHHCHHHHHHH	23.13	23737553
252 (in isoform 2)	Phosphorylation	-	23.13	25263469
261	Phosphorylation	DDLEDELYAQKLKYK HHHHHHHHHHHHHHH	12.63	27742792
264	Acetylation	EDELYAQKLKYKAIS HHHHHHHHHHHHHHH	38.48	19863167
264	Ubiquitination	EDELYAQKLKYKAIS HHHHHHHHHHHHHHH	38.48	17451654
266	Acetylation	ELYAQKLKYKAISEE HHHHHHHHHHHHHHH	52.30	21728379
266	Ubiquitination	ELYAQKLKYKAISEE HHHHHHHHHHHHHHH	52.30	17451654
267	Phosphorylation	LYAQKLKYKAISEEL HHHHHHHHHHHHHHH	18.98	22210690
268	Ubiquitination	YAQKLKYKAISEELD HHHHHHHHHHHHHHH	37.34	17451654
269 (in isoform 2)	Phosphorylation	-	13.88	26824392
271	Phosphorylation	KLKYKAISEELDHAL HHHHHHHHHHHHHHH	29.85	27742792
277 (in isoform 2)	Phosphorylation	-	14.02	29550500
282	Phosphorylation	DHALNDMTSI----- HHHHHHHCCC-----	26.57	27742792
283	Phosphorylation	HALNDMTSI------ HHHHHHCCC------	21.47	26824392

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
283	S	Phosphorylation	Kinase	CK2A1	P68400	PSP
283	S	Phosphorylation	Kinase	CK2B	P67870	PSP
283	S	Phosphorylation	Kinase	TROPOMYOSIN KINASE	-	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
283	S	Oxidation	21183079
Phosphorylated at Ser-283 by DAPK1 in response to oxidative stress and this phosphorylation enhances stress fiber formation in endothelial cells.
283	S	Phosphorylation	21183079
Phosphorylated at Ser-283 by DAPK1 in response to oxidative stress and this phosphorylation enhances stress fiber formation in endothelial cells.

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 TPM1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ACTS_HUMAN	ACTA1	physical	26496610
ACTG_HUMAN	ACTG1	physical	26496610
ACTN4_HUMAN	ACTN4	physical	26496610
AP2A1_HUMAN	AP2A1	physical	26496610
AP2B1_HUMAN	AP2B1	physical	26496610
DYST_HUMAN	DST	physical	26496610
CALD1_HUMAN	CALD1	physical	26496610
CAZA1_HUMAN	CAPZA1	physical	26496610
CAZA2_HUMAN	CAPZA2	physical	26496610
CAPZB_HUMAN	CAPZB	physical	26496610
CD59_HUMAN	CD59	physical	26496610
COF1_HUMAN	CFL1	physical	26496610
COF2_HUMAN	CFL2	physical	26496610
AP2M1_HUMAN	AP2M1	physical	26496610
CLCA_HUMAN	CLTA	physical	26496610
CLCB_HUMAN	CLTB	physical	26496610
CLH1_HUMAN	CLTC	physical	26496610
CBPM_HUMAN	CPM	physical	26496610
DAB2_HUMAN	DAB2	physical	26496610
DAPK3_HUMAN	DAPK3	physical	26496610
DREB_HUMAN	DBN1	physical	26496610
DSG2_HUMAN	DSG2	physical	26496610
E41L1_HUMAN	EPB41L1	physical	26496610
EPS15_HUMAN	EPS15	physical	26496610
FLII_HUMAN	FLII	physical	26496610
FLNA_HUMAN	FLNA	physical	26496610
GNA11_HUMAN	GNA11	physical	26496610
GNAI1_HUMAN	GNAI1	physical	26496610
GNAI2_HUMAN	GNAI2	physical	26496610
GBB2_HUMAN	GNB2	physical	26496610
GELS_HUMAN	GSN	physical	26496610
HNMT_HUMAN	HNMT	physical	26496610
PLAK_HUMAN	JUP	physical	26496610
ABLM1_HUMAN	ABLIM1	physical	26496610
MYO1B_HUMAN	MYO1B	physical	26496610
MYO1C_HUMAN	MYO1C	physical	26496610
MYO5A_HUMAN	MYO5A	physical	26496610
MYO5B_HUMAN	MYO5B	physical	26496610
MYO6_HUMAN	MYO6	physical	26496610
TWF1_HUMAN	TWF1	physical	26496610
RALA_HUMAN	RALA	physical	26496610
SDF2_HUMAN	SDF2	physical	26496610
SPTN1_HUMAN	SPTAN1	physical	26496610
SPTB2_HUMAN	SPTBN1	physical	26496610
SSFA2_HUMAN	SSFA2	physical	26496610
SVIL_HUMAN	SVIL	physical	26496610
TMOD1_HUMAN	TMOD1	physical	26496610
BACD2_HUMAN	TNFAIP1	physical	26496610
TPM2_HUMAN	TPM2	physical	26496610
TPM3_HUMAN	TPM3	physical	26496610
TPM4_HUMAN	TPM4	physical	26496610
COR2A_HUMAN	CORO2A	physical	26496610
CLH2_HUMAN	CLTCL1	physical	26496610
PICAL_HUMAN	PICALM	physical	26496610
ASML_HUMAN	ASMTL	physical	26496610
IQGA1_HUMAN	IQGAP1	physical	26496610
ABCG2_HUMAN	ABCG2	physical	26496610
RHGBA_HUMAN	ARHGAP11A	physical	26496610
ARHGH_HUMAN	ARHGEF17	physical	26496610
WDR1_HUMAN	WDR1	physical	26496610
ARPC4_HUMAN	ARPC4	physical	26496610
ARPC3_HUMAN	ARPC3	physical	26496610
ARC1B_HUMAN	ARPC1B	physical	26496610
ARP3_HUMAN	ACTR3	physical	26496610
ARP2_HUMAN	ACTR2	physical	26496610
ARPC2_HUMAN	ARPC2	physical	26496610
BASP1_HUMAN	BASP1	physical	26496610
DEST_HUMAN	DSTN	physical	26496610
SYNPO_HUMAN	SYNPO	physical	26496610
CE162_HUMAN	CEP162	physical	26496610
MPRIP_HUMAN	MPRIP	physical	26496610
COBL_HUMAN	COBL	physical	26496610
COR1C_HUMAN	CORO1C	physical	26496610
PKHG3_HUMAN	PLEKHG3	physical	26496610
RAI14_HUMAN	RAI14	physical	26496610
TMOD3_HUMAN	TMOD3	physical	26496610
PKN3_HUMAN	PKN3	physical	26496610
CDR2L_HUMAN	CDR2L	physical	26496610
LIMA1_HUMAN	LIMA1	physical	26496610
BMP2K_HUMAN	BMP2K	physical	26496610
MYO5C_HUMAN	MYO5C	physical	26496610
COR1B_HUMAN	CORO1B	physical	26496610
AFAP1_HUMAN	AFAP1	physical	26496610
INF2_HUMAN	INF2	physical	26496610
CYBR1_HUMAN	CYBRD1	physical	26496610
MYO19_HUMAN	MYO19	physical	26496610
ARP5L_HUMAN	ARPC5L	physical	26496610
STON2_HUMAN	STON2	physical	26496610
NEXN_HUMAN	NEXN	physical	26496610
CYTSB_HUMAN	SPECC1	physical	26496610
MISP_HUMAN	MISP	physical	26496610
CHM4B_HUMAN	CHMP4B	physical	26496610
PPR18_HUMAN	PPP1R18	physical	26496610
TPRN_HUMAN	TPRN	physical	26496610
ACTBL_HUMAN	ACTBL2	physical	26496610
MICA_HUMAN	MICA	physical	26496610

Drug and Disease Associations

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

Regulatory Network of TPM1_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283, AND MASSSPECTROMETRY.	17242355 [Abstract]
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry."; Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.; J. Proteome Res. 6:250-262(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283, AND MASSSPECTROMETRY.	17203969 [Abstract]
Ubiquitylation
Reference	PubMed
"A proteomics approach to identify the ubiquitinated proteins in mouseheart."; Jeon H.B., Choi E.S., Yoon J.H., Hwang J.H., Chang J.W., Lee E.K.,Choi H.W., Park Z.-Y., Yoo Y.J.; Biochem. Biophys. Res. Commun. 357:731-736(2007). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-77, AND MASSSPECTROMETRY.	17451654 [Abstract]

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