TNNC2_HUMAN - dbPTM
TNNC2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TNNC2_HUMAN
UniProt AC P02585
Protein Name Troponin C, skeletal muscle
Gene Name TNNC2
Organism Homo sapiens (Human).
Sequence Length 160
Subcellular Localization
Protein Description Troponin is the central regulatory protein of striated muscle contraction. Tn consists of three components: Tn-I which is the inhibitor of actomyosin ATPase, Tn-T which contains the binding site for tropomyosin and Tn-C. The binding of calcium to Tn-C abolishes the inhibitory action of Tn on actin filaments..
Protein Sequence MTDQQAEARSYLSEEMIAEFKAAFDMFDADGGGDISVKELGTVMRMLGQTPTKEELDAIIEEVDEDGSGTIDFEEFLVMMVRQMKEDAKGKSEEELAECFRIFDRNADGYIDPEELAEIFRASGEHVTDEEIESLMKDGDKNNDGRIDFDEFLKMMEGVQ
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------MTDQQAEAR
------CCHHHHHHH
42.38978749
36PhosphorylationADGGGDISVKELGTV
CCCCCCEEHHHHHHH
31.6924719451
38UbiquitinationGGGDISVKELGTVMR
CCCCEEHHHHHHHHH
40.19-
42PhosphorylationISVKELGTVMRMLGQ
EEHHHHHHHHHHHCC
24.6126437602
45MethylationKELGTVMRMLGQTPT
HHHHHHHHHHCCCCC
16.91-
50PhosphorylationVMRMLGQTPTKEELD
HHHHHCCCCCHHHHH
31.0024719451
92PhosphorylationKEDAKGKSEEELAEC
HHHHCCCCHHHHHHH
59.9326437602
134PhosphorylationVTDEEIESLMKDGDK
CCHHHHHHHHHHCCC
39.1526437602

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 TNNC2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TNNC2_HUMAN !!

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 TNNC2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TNNI3_HUMANTNNI3physical
25416956

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB01023Felodipine
Regulatory Network of TNNC2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Human skeletal muscle proteins. The primary structure of troponinC.";
Romero-Herrera A.E., Castillo O., Lehmann H.;
J. Mol. Evol. 8:251-270(1976).
Cited for: PROTEIN SEQUENCE OF 2-160.

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