TNNI2_RABIT - dbPTM
TNNI2_RABIT - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MGDEEKRNR
------CCHHHHHHH
51.541180911
12PhosphorylationEKRNRAITARRQHLK
HHHHHHHHHHHHHHH
17.084369265
20PhosphorylationARRQHLKSVMLQIAA
HHHHHHHHHHHHHHH
21.084369265
118PhosphorylationPLRRVRMSADAMLKA
CHHHHHHCHHHHHHH
16.664369265

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
12TPhosphorylationKinasePHK-FAMILY-GPS
12TPhosphorylationKinasePHK-Uniprot
12TPhosphorylationKinasePHK_GROUP-PhosphoELM
20SPhosphorylationKinasePKA-FAMILY-GPS
20SPhosphorylationKinasePKA_GROUP-PhosphoELM
118SPhosphorylationKinasePKA-FAMILY-GPS
118SPhosphorylationKinasePKA-Uniprot
118SPhosphorylationKinasePKA_GROUP-PhosphoELM

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TNNI2_RABIT !!

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 TNNI2_RABIT !!

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

Oops, there are no PPI records of TNNI2_RABIT !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TNNI2_RABIT

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.

TOP