| UniProt ID | TNNI2_RABIT | |
|---|---|---|
| UniProt AC | P02643 | |
| Protein Name | Troponin I, fast skeletal muscle | |
| Gene Name | TNNI2 | |
| Organism | Oryctolagus cuniculus (Rabbit). | |
| Sequence Length | 182 | |
| Subcellular Localization | ||
| Protein Description | Troponin I is the inhibitory subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity.. | |
| Protein Sequence | MGDEEKRNRAITARRQHLKSVMLQIAATELEKEEGRREAEKQNYLAEHCPPLSLPGSMAEVQELCKQLHAKIDAAEEEKYDMEIKVQKSSKELEDMNQKLFDLRGKFKRPPLRRVRMSADAMLKALLGSKHKVCMDLRANLKQVKKEDTEKERDLRDVGDWRKNIEEKSGMEGRKKMFESES | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
|
|
||
* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MGDEEKRNR ------CCHHHHHHH | 51.54 | 1180911 | |
| 12 | Phosphorylation | EKRNRAITARRQHLK HHHHHHHHHHHHHHH | 17.08 | 4369265 | |
| 20 | Phosphorylation | ARRQHLKSVMLQIAA HHHHHHHHHHHHHHH | 21.08 | 4369265 | |
| 118 | Phosphorylation | PLRRVRMSADAMLKA CHHHHHHCHHHHHHH | 16.66 | 4369265 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 12 | T | Phosphorylation | Kinase | PHK-FAMILY | - | GPS |
| 12 | T | Phosphorylation | Kinase | PHK | - | Uniprot |
| 12 | T | Phosphorylation | Kinase | PHK_GROUP | - | PhosphoELM |
| 20 | S | Phosphorylation | Kinase | PKA-FAMILY | - | GPS |
| 20 | S | Phosphorylation | Kinase | PKA_GROUP | - | PhosphoELM |
| 118 | S | Phosphorylation | Kinase | PKA-FAMILY | - | GPS |
| 118 | S | Phosphorylation | Kinase | PKA | - | Uniprot |
| 118 | S | Phosphorylation | Kinase | PKA_GROUP | - | PhosphoELM |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TNNI2_RABIT !! | ||||||
* 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 TNNI2_RABIT !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of TNNI2_RABIT !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
loading...
| Phosphorylation | |
| Reference | PubMed |
| "The amino acid sequences of the phosphorylated sites in troponin-Ifrom rabbit skeletal muscle."; Huang T.S., Bylund D.B., Stull J.T., Krebs E.G.; FEBS Lett. 42:249-252(1974). Cited for: PHOSPHORYLATION AT THR-12 AND SER-118. | |
| "The phosphorylation sites of troponin I from white skeletal muscle ofthe rabbit."; Moir A.J.G., Wilkinson J.M., Perry S.V.; FEBS Lett. 42:253-256(1974). Cited for: PHOSPHORYLATION AT THR-12 AND SER-118. | |