TPM1_PIG - dbPTM
TPM1_PIG - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TPM1_PIG
UniProt AC P42639
Protein Name Tropomyosin alpha-1 chain
Gene Name TPM1
Organism Sus scrofa (Pig).
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 MDAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKRLEDELVSLQKKLKATEDELDKYSEAPKDAQEKLELAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEELDHALNDMTSI
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-
45PhosphorylationRLEDELVSLQKKLKA
HHHHHHHHHHHHHHC
37.39-
53PhosphorylationLQKKLKATEDELDKY
HHHHHHCCHHHHHHH
42.2429916714
61PhosphorylationEDELDKYSEAPKDAQ
HHHHHHHCCCCHHHH
32.78-
79PhosphorylationELAEKKATDAEADVA
HHHHHHCCHHHHHHH
44.6229916714
87PhosphorylationDAEADVASLNRRIQL
HHHHHHHHHHHHHHH
26.4829916714
108PhosphorylationRAQERLATALQKLEE
HHHHHHHHHHHHHHH
32.2829916714
123PhosphorylationAEKAADESERGMKVI
HHHHHHHHHHHHHHH
32.8929916714
132PhosphorylationRGMKVIESRAQKDEE
HHHHHHHHHHHCCHH
23.0729916714
162PhosphorylationAEDADRKYEEVARKL
HHHHHHHHHHHHHHH
20.4429916714
174PhosphorylationRKLVIIESDLERAEE
HHHHHHHHHHHHHHH
36.7729916714
186PhosphorylationAEERAELSEGKCAEL
HHHHHHHCCCHHHHH
35.4929916714
199PhosphorylationELEEELKTVTNNLKS
HHHHHHHHHHHHHHH
45.2329916714
201PhosphorylationEEELKTVTNNLKSLE
HHHHHHHHHHHHHHH
24.5029916714
206PhosphorylationTVTNNLKSLEAQAEK
HHHHHHHHHHHHHHH
34.3129916714
215PhosphorylationEAQAEKYSQKEDKYE
HHHHHHHHCCHHHHH
45.9329916714
221PhosphorylationYSQKEDKYEEEIKVL
HHCCHHHHHHHHHHH
40.6829916714
229PhosphorylationEEEIKVLSDKLKEAE
HHHHHHHHHHHHHHH
35.3729916714
237PhosphorylationDKLKEAETRAEFAER
HHHHHHHHHHHHHHH
42.0829916714
245PhosphorylationRAEFAERSVTKLEKS
HHHHHHHHHHHHHHC
26.1629916714
247PhosphorylationEFAERSVTKLEKSID
HHHHHHHHHHHHCHH
31.0329916714
252PhosphorylationSVTKLEKSIDDLEDE
HHHHHHHCHHHHHHH
23.1329916714
261PhosphorylationDDLEDELYAQKLKYK
HHHHHHHHHHHHHHH
12.6329916714
271PhosphorylationKLKYKAISEELDHAL
HHHHHHHHHHHHHHH
29.8529916714
282PhosphorylationDHALNDMTSI-----
HHHHHHHCCC-----
26.5729916714
283PhosphorylationHALNDMTSI------
HHHHHHCCC------
21.4729916714

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
283SPhosphorylationKinaseDAPK1-Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TPM1_PIG !!

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_PIG !!

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

Oops, there are no PPI records of TPM1_PIG !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TPM1_PIG

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Related Literatures of Post-Translational Modification

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