TPM3_RAT - dbPTM
TPM3_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TPM3_RAT
UniProt AC Q63610
Protein Name Tropomyosin alpha-3 chain
Gene Name Tpm3
Organism Rattus norvegicus (Rat).
Sequence Length 248
Subcellular Localization Cytoplasm, cytoskeleton .
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 MAGSTTIEAVKRKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESRCREMDEQIRLMDQNLKCLSAAEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEDKLKCTKEEHLCTQRMLDQTLLDLNEM
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 Orthologous
Protein Cluster
2Acetylation------MAGSTTIEA
------CCCCHHHHH
22.20-
4Phosphorylation----MAGSTTIEAVK
----CCCCHHHHHHH
16.9123984901
5Phosphorylation---MAGSTTIEAVKR
---CCCCHHHHHHHH
30.7623984901
6Phosphorylation--MAGSTTIEAVKRK
--CCCCHHHHHHHHH
20.6523984901
11AcetylationSTTIEAVKRKIQVLQ
CHHHHHHHHHHHHHH
55.8322902405
13AcetylationTIEAVKRKIQVLQQQ
HHHHHHHHHHHHHHH
31.6022902405
51PhosphorylationQAEAEVASLNRRIQL
HHHHHHHHHHHHHHH
31.2129779826
72PhosphorylationRAQERLATALQKLEE
HHHHHHHHHHHHHHH
32.2822673903
76AcetylationRLATALQKLEEAEKA
HHHHHHHHHHHHHHH
59.7359120567
82AcetylationQKLEEAEKAADESER
HHHHHHHHHHHHHHH
56.7959120545
92AcetylationDESERGMKVIENRAL
HHHHHHHHHHHHHCC
42.7759120583
100AcetylationVIENRALKDEEKMEL
HHHHHCCCCHHHHHH
63.2122902405
104AcetylationRALKDEEKMELQEIQ
HCCCCHHHHHHHHHH
35.3122902405
113AcetylationELQEIQLKEAKHIAE
HHHHHHHHHHHHHHH
38.9726302492
116AcetylationEIQLKEAKHIAEEAD
HHHHHHHHHHHHHHH
36.3172585823
125AcetylationIAEEADRKYEEVARK
HHHHHHHHHHHHHHH
58.5259120565
126PhosphorylationAEEADRKYEEVARKL
HHHHHHHHHHHHHHH
20.4422673903
169AcetylationRLMDQNLKCLSAAEE
HHHHHHHHHHHHHHH
40.4526302492
177AcetylationCLSAAEEKYSQKEDK
HHHHHHHHHHCCCHH
41.5326302492
179PhosphorylationSAAEEKYSQKEDKYE
HHHHHHHHCCCHHHH
45.93-
181AcetylationAEEKYSQKEDKYEEE
HHHHHHCCCHHHHHH
63.0426302492
184AcetylationKYSQKEDKYEEEIKI
HHHCCCHHHHHHHHH
56.5026302492
190AcetylationDKYEEEIKILTDKLK
HHHHHHHHHHHHHHH
34.6422902405
195AcetylationEIKILTDKLKEAETR
HHHHHHHHHHHHHHH
57.1126302492
197AcetylationKILTDKLKEAETRAE
HHHHHHHHHHHHHHH
61.7026302492
201PhosphorylationDKLKEAETRAEFAER
HHHHHHHHHHHHHHH
42.0822673903
212AcetylationFAERSVAKLEKTIDD
HHHHHHHHHHHHHHH
55.8359120577
215UbiquitinationRSVAKLEKTIDDLED
HHHHHHHHHHHHHHH
62.31-
216PhosphorylationSVAKLEKTIDDLEDK
HHHHHHHHHHHHHHH
21.91-
228 (in isoform 2)Ubiquitination-71.25-
235 (in isoform 3)Phosphorylation-27.9923984901
246 (in isoform 2)Phosphorylation-42.8430181290
247 (in isoform 2)Phosphorylation-54.2728826663

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

Oops, there are no upstream regulatory protein records of TPM3_RAT !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TPM3_RAT !!

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 TPM3_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of TPM3_RAT !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TPM3_RAT

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Related Literatures of Post-Translational Modification

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