dbPTM

TPM1_RABIT - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TPM1_RABIT
UniProt AC	P58772
Protein Name	Tropomyosin alpha-1 chain
Gene Name	TPM1
Organism	Oryctolagus cuniculus (Rabbit).
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	7622625
5	Acetylation	---MDAIKKKMQMLK ---CHHHHHHHHHHH	48.32	861209
6	Acetylation	--MDAIKKKMQMLKL --CHHHHHHHHHHHC	47.57	861209
7	Acetylation	-MDAIKKKMQMLKLD -CHHHHHHHHHHHCC	29.39	861209
12	Acetylation	KKKMQMLKLDKENAL HHHHHHHHCCHHHHH	49.66	861209
15	Acetylation	MQMLKLDKENALDRA HHHHHCCHHHHHHHH	64.40	861209
45	Phosphorylation	QLEDELVSLQKKLKG HHHHHHHHHHHHHCC	37.39	-
48	Acetylation	DELVSLQKKLKGTED HHHHHHHHHHCCCHH	66.42	861209
53	Phosphorylation	LQKKLKGTEDELDKY HHHHHCCCHHHHHHH	38.38	-
61	Phosphorylation	EDELDKYSEALKDAQ HHHHHHHHHHHHHHH	23.33	-
65	Acetylation	DKYSEALKDAQEKLE HHHHHHHHHHHHHHH	59.05	861209
70	Acetylation	ALKDAQEKLELAEKK HHHHHHHHHHHHHHH	34.87	861209
79	Phosphorylation	ELAEKKATDAEADVA HHHHHHCCHHHHHHH	44.62	-
87	Phosphorylation	DAEADVASLNRRIQL HHHHHHHHHHHHHHH	26.48	-
108	Phosphorylation	RAQERLATALQKLEE HHHHHHHHHHHHHHH	32.28	-
118	Acetylation	QKLEEAEKAADESER HHHHHHHHHHHHHHH	56.79	861209
128	Acetylation	DESERGMKVIESRAQ HHHHHHHHHHHHHHH	42.77	861209
149	Acetylation	EIQEIQLKEAKHIAE HHHHHHHHHHHHHHH	38.97	861209
152	Acetylation	EIQLKEAKHIAEDAD HHHHHHHHHHHHHHH	36.31	861209
168	Acetylation	KYEEVARKLVIIESD HHHHHHHHHHHHHHH	37.05	861209
174	Phosphorylation	RKLVIIESDLERAEE HHHHHHHHHHHHHHH	36.77	-
186	Phosphorylation	AEERAELSEGKCAEL HHHHHHHCCCHHHHH	35.49	-
206	Phosphorylation	TVTNNLKSLEAQAEK HHHHHHHHHHHHHHH	34.31	-
213	Acetylation	SLEAQAEKYSQKEDK HHHHHHHHHHCCHHH	53.90	861209
215	Phosphorylation	EAQAEKYSQKEDKYE HHHHHHHHCCHHHHH	45.93	-
231	Acetylation	EIKVLSDKLKEAETR HHHHHHHHHHHHHHH	59.07	861209
233	Acetylation	KVLSDKLKEAETRAE HHHHHHHHHHHHHHH	61.70	861209
248	Acetylation	FAERSVTKLEKSIDD HHHHHHHHHHHCHHH	53.12	861209
251	Acetylation	RSVTKLEKSIDDLED HHHHHHHHCHHHHHH	64.25	861209
252	Phosphorylation	SVTKLEKSIDDLEDE HHHHHHHCHHHHHHH	23.13	-
261	Phosphorylation	DDLEDELYAQKLKYK HHHHHHHHHHHHHHH	12.63	-
266	Acetylation	ELYAQKLKYKAISEE HHHHHHHHHHHHHHH	52.30	861209
271	Phosphorylation	KLKYKAISEELDHAL HHHHHHHHHHHHHHH	29.85	-
282	Phosphorylation	DHALNDMTSI----- HHHHHHHCCC-----	26.57	-
283	Phosphorylation	HALNDMTSI------ HHHHHHCCC------	21.47	278975

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	DAPK1	G1SJW2	GPS
283	S	Phosphorylation	Kinase	DAPK1	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TPM1_RABIT !!

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_RABIT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of TPM1_RABIT !!

Drug and Disease Associations

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

Regulatory Network of TPM1_RABIT

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Rabbit skeletal muscle alpha alpha-tropomyosin expressed inbaculovirus-infected insect cells possesses the authentic N-terminusstructure and functions."; Kluwe L., Maeda K., Miegel A., Fujita-Becker S., Maeda Y., Talbo G.,Houthaeve T., Kellner R.; J. Muscle Res. Cell Motil. 16:103-110(1995). Cited for: NUCLEOTIDE SEQUENCE [MRNA].	7622625 [Abstract]
Phosphorylation
Reference	PubMed
"Specific phosphorylation at serine-283 of alpha tropomyosin from frogskeletal and rabbit skeletal and cardiac muscle."; Mak A.S., Smillie L.B., Barany M.; Proc. Natl. Acad. Sci. U.S.A. 75:3588-3592(1978). Cited for: PHOSPHORYLATION AT SER-283.	278975 [Abstract]