TPM3_MOUSE - dbPTM
TPM3_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TPM3_MOUSE
UniProt AC P21107
Protein Name Tropomyosin alpha-3 chain
Gene Name Tpm3
Organism Mus musculus (Mouse).
Sequence Length 285
Subcellular Localization Isoform 2: 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 MMEAIKKKMQMLKLDKENVLDRAEQAEAEQKQAEERSKQLEDELATMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAADAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYAQKLKYKAISDELDHALNDMTSI
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------MMEAIKKKM
------CHHHHHHHH		60.13-
2 (in isoform 2)Acetylation-60.13-
8UbiquitinationMMEAIKKKMQMLKLD
CHHHHHHHHHHHHCC		3.77-
11 (in isoform 2)Ubiquitination-2.54-
13UbiquitinationKKKMQMLKLDKENVL
HHHHHHHHCCHHHHH		11.36-
13 (in isoform 2)Ubiquitination-11.36-
31UbiquitinationEQAEAEQKQAEERSK
HHHHHHHHHHHHHHH		54.42-
50AcetylationELATMQKKLKGTEDE
HHHHHHHHHCCCHHH		8.7819863069
51 (in isoform 2)Phosphorylation-73.0730352176
52UbiquitinationATMQKKLKGTEDELD
HHHHHHHCCCHHHHH		44.78-
54PhosphorylationMQKKLKGTEDELDKY
HHHHHCCCHHHHHHH		59.1528542873
60AcetylationGTEDELDKYSEALKD
CCHHHHHHHHHHHHH		16.0621728379
60UbiquitinationGTEDELDKYSEALKD
CCHHHHHHHHHHHHH		16.06-
61PhosphorylationTEDELDKYSEALKDA
CHHHHHHHHHHHHHH		23.3327742792
62PhosphorylationEDELDKYSEALKDAQ
HHHHHHHHHHHHHHH		55.7326824392
66UbiquitinationDKYSEALKDAQEKLE
HHHHHHHHHHHHHHH		55.10-
71UbiquitinationALKDAQEKLELAEKK
HHHHHHHHHHHHHHH		6.84-
77UbiquitinationEKLELAEKKAADAEA
HHHHHHHHHHHHHHH		40.07-
78AcetylationKLELAEKKAADAEAE
HHHHHHHHHHHHHHH		22.9519863081
88PhosphorylationDAEAEVASLNRRIQL
HHHHHHHHHHHHHHH		4.1025619855
109PhosphorylationRAQERLATALQKLEE
HHHHHHHHHHHHHHH		11.4622210690
113AcetylationRLATALQKLEEAEKA
HHHHHHHHHHHHHHH		4.6621728379
113UbiquitinationRLATALQKLEEAEKA
HHHHHHHHHHHHHHH		4.66-
119UbiquitinationQKLEEAEKAADESER
HHHHHHHHHHHHHHH		16.20-
119AcetylationQKLEEAEKAADESER
HHHHHHHHHHHHHHH		16.2021728379
124PhosphorylationAEKAADESERGMKVI
HHHHHHHHHHHHHHH		51.7329899451
129UbiquitinationDESERGMKVIENRAL
HHHHHHHHHHHHHCC		5.01-
137UbiquitinationVIENRALKDEEKMEL
HHHHHCCCCHHHHHH		70.86-
137AcetylationVIENRALKDEEKMEL
HHHHHCCCCHHHHHH		70.8621728379
137SuccinylationVIENRALKDEEKMEL
HHHHHCCCCHHHHHH		70.8623954790
141AcetylationRALKDEEKMELQEIQ
HCCCCHHHHHHHHHH		7.6121728379
150UbiquitinationELQEIQLKEAKHIAE
HHHHHHHHHHHHHHH		72.10-
150AcetylationELQEIQLKEAKHIAE
HHHHHHHHHHHHHHH		72.1021728379
153AcetylationEIQLKEAKHIAEEAD
HHHHHHHHHHHHHHH		31.3822826441
162AcetylationIAEEADRKYEEVARK
HHHHHHHHHHHHHHH		20.4421728379
163PhosphorylationAEEADRKYEEVARKL
HHHHHHHHHHHHHHH		49.3722499769
181 (in isoform 2)Acetylation-57.49-
184 (in isoform 2)Acetylation-55.52-
189PhosphorylationERAELAESKCSELEE
HHHHHHHHHHHHHHH		33.0322807455
192PhosphorylationELAESKCSELEEELK
HHHHHHHHHHHHHHH		70.4419060867
206UbiquitinationKNVTNNLKSLEAQAE
HHHHHHHHHHHHHHH		34.3122790023
207PhosphorylationNVTNNLKSLEAQAEK
HHHHHHHHHHHHHHH		6.3826824392
214UbiquitinationSLEAQAEKYSQKEDK
HHHHHHHHHHCCHHH		14.0822790023
214AcetylationSLEAQAEKYSQKEDK
HHHHHHHHHHCCHHH		14.0821728379
215PhosphorylationLEAQAEKYSQKEDKY
HHHHHHHHHCCHHHH		45.9327742792
216PhosphorylationEAQAEKYSQKEDKYE
HHHHHHHHCCHHHHH		50.4926824392
218AcetylationQAEKYSQKEDKYEEE
HHHHHHCCHHHHHHH		52.6921728379
218UbiquitinationQAEKYSQKEDKYEEE
HHHHHHCCHHHHHHH		52.69-
221AcetylationKYSQKEDKYEEEIKI
HHHCCHHHHHHHHHH		40.6821728379
221UbiquitinationKYSQKEDKYEEEIKI
HHHCCHHHHHHHHHH		40.68-
222PhosphorylationYSQKEDKYEEEIKIL
HHCCHHHHHHHHHHH		55.6922210690
223 (in isoform 2)Acetylation-63.03-
227AcetylationDKYEEEIKILTDKLK
HHHHHHHHHHHHHHH		6.5121728379
228 (in isoform 2)Acetylation-4.26-
234UbiquitinationKILTDKLKEAETRAE
HHHHHHHHHHHHHHH		63.27-
238PhosphorylationDKLKEAETRAEFAER
HHHHHHHHHHHHHHH		24.5122210690
246PhosphorylationRAEFAERSVAKLEKT
HHHHHHHHHHHHHHH		7.3422210690
249UbiquitinationFAERSVAKLEKTIDD
HHHHHHHHHHHHHHH		6.18-
249AcetylationFAERSVAKLEKTIDD
HHHHHHHHHHHHHHH		6.1821728379
252AcetylationRSVAKLEKTIDDLED
HHHHHHHHHHHHHHH		21.9121728379
253PhosphorylationSVAKLEKTIDDLEDE
HHHHHHHHHHHHHHH		6.0117203969
262PhosphorylationDDLEDELYAQKLKYK
HHHHHHHHHHHHHHH		16.8025367039
265UbiquitinationEDELYAQKLKYKAIS
HHHHHHHHHHHHHHH		4.9522790023
265AcetylationEDELYAQKLKYKAIS
HHHHHHHHHHHHHHH		4.9521728379
269UbiquitinationYAQKLKYKAISDELD
HHHHHHHHHHHHHHH		11.9222790023
272PhosphorylationKLKYKAISDELDHAL
HHHHHHHHHHHHHHH		55.1321082442
283PhosphorylationDHALNDMTSI-----
HHHHHHHCCC-----		21.4728833060
284PhosphorylationHALNDMTSI------
HHHHHHCCC------		4.873244365
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_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TPM3_MOUSE !!
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_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of TPM3_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TPM3_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.

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