dbPTM

TPM2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TPM2_MOUSE
UniProt AC	P58774
Protein Name	Tropomyosin beta chain
Gene Name	Tpm2
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. The non-muscle isoform may have a role in agonist-mediated receptor internalization. [PubMed: 16094730]
Protein Sequence	MDAIKKKMQMLKLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKDAQEKLEQAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRKYEEVARKLVILEGELERSEERAEVAESKCGDLEEELKIVTNNLKSLEAQADKYSTKEDKYEEEIKLLEEKLKEAETRAEFAERSVAKLEKTIDDLEDEVYAQKMKYKAISEELDNALNDITSL

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	-
12	Ubiquitination	KKKMQMLKLDKENAI HHHHHHHHCCHHHHH	49.66	-
15	Ubiquitination	MQMLKLDKENAIDRA HHHHHCCHHHHHHHH	64.40	-
15	Acetylation	MQMLKLDKENAIDRA HHHHHCCHHHHHHHH	64.40	21728379
29	Ubiquitination	AEQAEADKKQAEDRC HHHHHHHHHHHHHHH	54.56	-
30	Ubiquitination	EQAEADKKQAEDRCK HHHHHHHHHHHHHHH	56.11	22790023
37	Ubiquitination	KQAEDRCKQLEEEQQ HHHHHHHHHHHHHHH	59.83	22790023
48	Acetylation	EEQQALQKKLKGTED HHHHHHHHHHCCCHH	62.01	21728379
48	Ubiquitination	EEQQALQKKLKGTED HHHHHHHHHHCCCHH	62.01	22790023
51	Ubiquitination	QALQKKLKGTEDEVE HHHHHHHCCCHHHHH	73.07	22790023
53	Phosphorylation	LQKKLKGTEDEVEKY HHHHHCCCHHHHHHH	38.38	28542873
59	Acetylation	GTEDEVEKYSESVKD CCHHHHHHHHHHHHH	60.29	21728379
59	Ubiquitination	GTEDEVEKYSESVKD CCHHHHHHHHHHHHH	60.29	22790023
60	Phosphorylation	TEDEVEKYSESVKDA CHHHHHHHHHHHHHH	12.26	28542873
61	Phosphorylation	EDEVEKYSESVKDAQ HHHHHHHHHHHHHHH	34.17	22210690
63	Phosphorylation	EVEKYSESVKDAQEK HHHHHHHHHHHHHHH	28.64	22210690
65	Ubiquitination	EKYSESVKDAQEKLE HHHHHHHHHHHHHHH	57.54	22790023
70	Ubiquitination	SVKDAQEKLEQAEKK HHHHHHHHHHHHHHH	45.29	22790023
76	Acetylation	EKLEQAEKKATDAEA HHHHHHHHHHHHHHH	51.20	7668185
77	Ubiquitination	KLEQAEKKATDAEAD HHHHHHHHHHHHHHH	48.28	-
79	Phosphorylation	EQAEKKATDAEADVA HHHHHHHHHHHHHHH	44.62	28464351
87	Phosphorylation	DAEADVASLNRRIQL HHHHHHHHHHHHHHH	26.48	27742792
108	Phosphorylation	RAQERLATALQKLEE HHHHHHHHHHHHHHH	32.28	22210690
112	Acetylation	RLATALQKLEEAEKA HHHHHHHHHHHHHHH	59.73	22632939
112	Ubiquitination	RLATALQKLEEAEKA HHHHHHHHHHHHHHH	59.73	-
118	Ubiquitination	QKLEEAEKAADESER HHHHHHHHHHHHHHH	56.79	-
118	Acetylation	QKLEEAEKAADESER HHHHHHHHHHHHHHH	56.79	88211
123	Phosphorylation	AEKAADESERGMKVI HHHHHHHHHHHHHHH	32.89	29899451
128	Ubiquitination	DESERGMKVIENRAM HHHHHHHHHHHHHHC	42.77	22790023
136	Acetylation	VIENRAMKDEEKMEL HHHHHHCCHHHHHHH	62.09	21728379
140	Acetylation	RAMKDEEKMELQEMQ HHCCHHHHHHHHHHH	35.31	21728379
149	Acetylation	ELQEMQLKEAKHIAE HHHHHHHHHHHHHHC	38.44	21728379
149	Ubiquitination	ELQEMQLKEAKHIAE HHHHHHHHHHHHHHC	38.44	22790023
152	Acetylation	EMQLKEAKHIAEDSD HHHHHHHHHHHCCCC	36.31	21728379
158	Phosphorylation	AKHIAEDSDRKYEEV HHHHHCCCCHHHHHH	30.71	30635358
161	Acetylation	IAEDSDRKYEEVARK HHCCCCHHHHHHHHH	63.10	21728379
162	Phosphorylation	AEDSDRKYEEVARKL HCCCCHHHHHHHHHH	20.44	28542873
168	Acetylation	KYEEVARKLVILEGE HHHHHHHHHHHHHCH	37.05	21728379
168	Ubiquitination	KYEEVARKLVILEGE HHHHHHHHHHHHHCH	37.05	22790023
188	Phosphorylation	ERAEVAESKCGDLEE HHHHHHHHHCCCHHH	24.41	28464351
198	Acetylation	GDLEEELKIVTNNLK CCHHHHHHHHHHHHH	38.11	21728379
201	Phosphorylation	EEELKIVTNNLKSLE HHHHHHHHHHHHHHH	23.12	22210690
205 (in isoform 2)	Ubiquitination	-	55.93	-
205	Ubiquitination	KIVTNNLKSLEAQAD HHHHHHHHHHHHHHH	55.93	22790023
206 (in isoform 2)	Phosphorylation	-	34.31	22802335
206	Phosphorylation	IVTNNLKSLEAQADK HHHHHHHHHHHHHHH	34.31	24899341
210 (in isoform 2)	Phosphorylation	-	40.49	26643407
213	Ubiquitination	SLEAQADKYSTKEDK HHHHHHHHCCCHHHH	44.08	22790023
213	Acetylation	SLEAQADKYSTKEDK HHHHHHHHCCCHHHH	44.08	21728379
215 (in isoform 2)	Phosphorylation	-	38.45	22802335
215	Phosphorylation	EAQADKYSTKEDKYE HHHHHHCCCHHHHHH	38.45	24899341
216	Phosphorylation	AQADKYSTKEDKYEE HHHHHCCCHHHHHHH	35.05	29550500
220	Ubiquitination	KYSTKEDKYEEEIKL HCCCHHHHHHHHHHH	56.50	22790023
220	Acetylation	KYSTKEDKYEEEIKL HCCCHHHHHHHHHHH	56.50	22632933
221	Phosphorylation	YSTKEDKYEEEIKLL CCCHHHHHHHHHHHH	40.68	22210690
226	Acetylation	DKYEEEIKLLEEKLK HHHHHHHHHHHHHHH	50.75	21728379
226	Ubiquitination	DKYEEEIKLLEEKLK HHHHHHHHHHHHHHH	50.75	22790023
231	Ubiquitination	EIKLLEEKLKEAETR HHHHHHHHHHHHHHH	56.32	22790023
233	Ubiquitination	KLLEEKLKEAETRAE HHHHHHHHHHHHHHH	66.98	22790023
237	Phosphorylation	EKLKEAETRAEFAER HHHHHHHHHHHHHHH	42.08	22210690
245	Phosphorylation	RAEFAERSVAKLEKT HHHHHHHHHHHHHHH	20.24	26643407
248	Acetylation	FAERSVAKLEKTIDD HHHHHHHHHHHHHHH	55.83	30996313
248	Ubiquitination	FAERSVAKLEKTIDD HHHHHHHHHHHHHHH	55.83	-
251	Ubiquitination	RSVAKLEKTIDDLED HHHHHHHHHHHHHHH	62.31	22790023
251	Acetylation	RSVAKLEKTIDDLED HHHHHHHHHHHHHHH	62.31	44862339
252	Phosphorylation	SVAKLEKTIDDLEDE HHHHHHHHHHHHHHH	21.91	26643407
252 (in isoform 2)	Phosphorylation	-	21.91	25338131
261	Phosphorylation	DDLEDEVYAQKMKYK HHHHHHHHHHHHHHH	10.98	26643407
264	Acetylation	EDEVYAQKMKYKAIS HHHHHHHHHHHHHHH	29.23	21728379
267	Phosphorylation	VYAQKMKYKAISEEL HHHHHHHHHHHHHHH	11.36	22210690
271	Phosphorylation	KMKYKAISEELDNAL HHHHHHHHHHHHHHH	29.85	-
282	Phosphorylation	DNALNDITSL----- HHHHHHHHCC-----	27.17	23737553
283	Phosphorylation	NALNDITSL------ HHHHHHHCC------	32.20	17203969

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
61	S	Phosphorylation	Kinase	PIK3CG	Q9JHG7	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
61	S	Phosphorylation	16094730
Phosphorylated on Ser-61 by PIK3CG.
61	S	Phosphorylation	16094730
Phosphorylation on Ser-61 is required for ADRB2 internalization.

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 TPM2_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of TPM2_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of TPM2_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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 THR-252 AND SER-283, ANDMASS SPECTROMETRY.	17203969 [Abstract]
"Protein kinase activity of phosphoinositide 3-kinase regulates beta-adrenergic receptor endocytosis."; Naga Prasad S.V., Jayatilleke A., Madamanchi A., Rockman H.A.; Nat. Cell Biol. 7:785-796(2005). Cited for: FUNCTION, PHOSPHORYLATION AT SER-61, AND MUTAGENESIS OF SER-61.	16094730 [Abstract]

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