TPM2_RAT - dbPTM
TPM2_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TPM2_RAT
UniProt AC P58775
Protein Name Tropomyosin beta chain
Gene Name Tpm2
Organism Rattus norvegicus (Rat).
Sequence Length 284
Subcellular Localization Cytoplasm, cytoskeleton . Associates with F-actin stress fibers (PubMed:7568216).
Protein Description Binds to actin filaments in muscle and non-muscle cells. [PubMed: 7568216]
Protein Sequence MDAIKKKMQMLKLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKDAQEKLEQAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRKYEEVARKLVILEGELERSEERAEVAESKCGDLEEELKIVTNNLKSLEAQADKYSTKEDKYEEEIKLLEEKLKEAETRAEFAERSVAKLEKTIDDLEDEVYAQKMKYKAISEELDNALNDITSL
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
1Acetylation-------MDAIKKKM
-------CHHHHHHH
7.68-
12AcetylationKKKMQMLKLDKENAI
HHHHHHHHCCHHHHH
49.6659111967
15AcetylationMQMLKLDKENAIDRA
HHHHHCCHHHHHHHH
64.4026302492
29AcetylationAEQAEADKKQAEDRC
HHHHHHHHHHHHHHH
54.5622902405
30AcetylationEQAEADKKQAEDRCK
HHHHHHHHHHHHHHH
56.1122902405
37AcetylationKQAEDRCKQLEEEQQ
HHHHHHHHHHHHHHH
59.8326302492
48AcetylationEEQQALQKKLKGTED
HHHHHHHHHHCCCHH
62.0122902405
49AcetylationEQQALQKKLKGTEDE
HHHHHHHHHCCCHHH
42.3322902405
51AcetylationQALQKKLKGTEDEVE
HHHHHHHCCCHHHHH
73.0722902405
53PhosphorylationLQKKLKGTEDEVEKY
HHHHHCCCHHHHHHH
38.38-
59AcetylationGTEDEVEKYSESVKD
CCHHHHHHHHHHHHH
60.2922902405
60PhosphorylationTEDEVEKYSESVKDA
CHHHHHHHHHHHHHH
12.2622609512
61PhosphorylationEDEVEKYSESVKDAQ
HHHHHHHHHHHHHHH
34.1722673903
63PhosphorylationEVEKYSESVKDAQEK
HHHHHHHHHHHHHHH
28.6422673903
65AcetylationEKYSESVKDAQEKLE
HHHHHHHHHHHHHHH
57.5422902405
70AcetylationSVKDAQEKLEQAEKK
HHHHHHHHHHHHHHH
45.2922902405
76AcetylationEKLEQAEKKATDAEA
HHHHHHHHHHHHHHH
51.2022902405
77AcetylationKLEQAEKKATDAEAD
HHHHHHHHHHHHHHH
48.2826302492
79PhosphorylationEQAEKKATDAEADVA
HHHHHHHHHHHHHHH
44.6222673903
87PhosphorylationDAEADVASLNRRIQL
HHHHHHHHHHHHHHH
26.4828826663
108PhosphorylationRAQERLATALQKLEE
HHHHHHHHHHHHHHH
32.2822673903
112AcetylationRLATALQKLEEAEKA
HHHHHHHHHHHHHHH
59.7359111965
118AcetylationQKLEEAEKAADESER
HHHHHHHHHHHHHHH
56.7959111929
128AcetylationDESERGMKVIENRAM
HHHHHHHHHHHHHHC
42.7759111991
136AcetylationVIENRAMKDEEKMEL
HHHHHHCCHHHHHHH
62.0922902405
140AcetylationRAMKDEEKMELQEMQ
HHCCHHHHHHHHHHH
35.3122902405
149AcetylationELQEMQLKEAKHIAE
HHHHHHHHHHHHHHC
38.4422902405
152AcetylationEMQLKEAKHIAEDSD
HHHHHHHHHHHCCCC
36.3122902405
158PhosphorylationAKHIAEDSDRKYEEV
HHHHHCCCCHHHHHH
30.7122673903
161AcetylationIAEDSDRKYEEVARK
HHCCCCHHHHHHHHH
63.1026302492
162PhosphorylationAEDSDRKYEEVARKL
HCCCCHHHHHHHHHH
20.4422673903
168AcetylationKYEEVARKLVILEGE
HHHHHHHHHHHHHCH
37.0559113429
179PhosphorylationLEGELERSEERAEVA
HHCHHHCHHHHHHHH
34.1422673903
198AcetylationGDLEEELKIVTNNLK
CCHHHHHHHHHHHHH
38.1122902405
201PhosphorylationEEELKIVTNNLKSLE
HHHHHHHHHHHHHHH
23.1222673903
205AcetylationKIVTNNLKSLEAQAD
HHHHHHHHHHHHHHH
55.9322902405
206PhosphorylationIVTNNLKSLEAQADK
HHHHHHHHHHHHHHH
34.3122673903
210 (in isoform 2)Phosphorylation-40.4922673903
213AcetylationSLEAQADKYSTKEDK
HHHHHHHHCCCHHHH
44.0822902405
215 (in isoform 2)Phosphorylation-38.4522673903
215PhosphorylationEAQADKYSTKEDKYE
HHHHHHCCCHHHHHH
38.4522673903
216PhosphorylationAQADKYSTKEDKYEE
HHHHHCCCHHHHHHH
35.0522673903
216 (in isoform 2)Phosphorylation-35.0522673903
217AcetylationQADKYSTKEDKYEEE
HHHHCCCHHHHHHHH
58.9622902405
217 (in isoform 2)Acetylation-58.96-
220AcetylationKYSTKEDKYEEEIKL
HCCCHHHHHHHHHHH
56.5022902405
226AcetylationDKYEEEIKLLEEKLK
HHHHHHHHHHHHHHH
50.7522902405
231AcetylationEIKLLEEKLKEAETR
HHHHHHHHHHHHHHH
56.3226302492
233AcetylationKLLEEKLKEAETRAE
HHHHHHHHHHHHHHH
66.9859111977
237PhosphorylationEKLKEAETRAEFAER
HHHHHHHHHHHHHHH
42.0822673903
248AcetylationFAERSVAKLEKTIDD
HHHHHHHHHHHHHHH
55.8322902405
251AcetylationRSVAKLEKTIDDLED
HHHHHHHHHHHHHHH
62.3122902405
251 (in isoform 2)Acetylation-62.31-
252 (in isoform 2)Phosphorylation-21.9129779826
252PhosphorylationSVAKLEKTIDDLEDE
HHHHHHHHHHHHHHH
21.9122673903
261PhosphorylationDDLEDEVYAQKMKYK
HHHHHHHHHHHHHHH
10.9822673903
264AcetylationEDEVYAQKMKYKAIS
HHHHHHHHHHHHHHH
29.2322902405
268AcetylationYAQKMKYKAISEELD
HHHHHHHHHHHHHHH
33.4522902405
271PhosphorylationKMKYKAISEELDNAL
HHHHHHHHHHHHHHH
29.8524945867
282PhosphorylationDNALNDITSL-----
HHHHHHHHCC-----
27.1724945867
283PhosphorylationNALNDITSL------
HHHHHHHCC------
32.2029779826

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 TPM2_RAT !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
61SPhosphorylation

22673903
61SPhosphorylation

22673903

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_RAT !!

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

Oops, there are no PPI records of TPM2_RAT !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TPM2_RAT

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Related Literatures of Post-Translational Modification

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