TNNT2_HUMAN - dbPTM
TNNT2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TNNT2_HUMAN
UniProt AC P45379
Protein Name Troponin T, cardiac muscle
Gene Name TNNT2
Organism Homo sapiens (Human).
Sequence Length 298
Subcellular Localization
Protein Description Troponin T is the tropomyosin-binding subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity..
Protein Sequence MSDIEEVVEEYEEEEQEEAAVEEEEDWREDEDEQEEAAEEDAEAEAETEETRAEEDEEEEEAKEAEDGPMEESKPKPRSFMPNLVPPKIPDGERVDFDDIHRKRMEKDLNELQALIEAHFENRKKEEEELVSLKDRIERRRAERAEQQRIRNEREKERQNRLAEERARREEEENRRKAEDEARKKKALSNMMHFGGYIQKQAQTERKSGKRQTEREKKKKILAERRKVLAIDHLNEDQLREKAKELWQSIYNLEAEKFDLQEKFKQQKYEINVLRNRINDNQKVSKTRGKAKVTGRWK
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
2Phosphorylation------MSDIEEVVE
------CCHHHHHHH
47.5021639091
2Acetylation------MSDIEEVVE
------CCHHHHHHH
47.50-
161 (in isoform 12)Phosphorylation-27.2612819028
165 (in isoform 12)Phosphorylation-46.1412819028
170 (in isoform 12)Phosphorylation-65.292584239
189PhosphorylationARKKKALSNMMHFGG
HHHHHHHHHHHHHHH
27.78-
191 (in isoform 11)Phosphorylation-1.6612819028
195 (in isoform 11)Phosphorylation-17.2012819028
197PhosphorylationNMMHFGGYIQKQAQT
HHHHHHHHHHHHHHH
10.68-
200 (in isoform 11)Phosphorylation-37.732584239
201 (in isoform 10)Phosphorylation-23.4812819028
203 (in isoform 5)Phosphorylation-41.2112819028
204PhosphorylationYIQKQAQTERKSGKR
HHHHHHHHHHHHCCC
40.5512819028
205 (in isoform 10)Phosphorylation-46.1312819028
207 (in isoform 5)Phosphorylation-58.2812819028
208PhosphorylationQAQTERKSGKRQTER
HHHHHHHHCCCHHHH
56.6312819028
210 (in isoform 10)Phosphorylation-48.722584239
213PhosphorylationRKSGKRQTEREKKKK
HHHCCCHHHHHHHHH
40.832584239
249PhosphorylationKAKELWQSIYNLEAE
HHHHHHHHHHHHHHH
18.56-
251PhosphorylationKELWQSIYNLEAEKF
HHHHHHHHHHHHHHC
20.95-
290AcetylationKVSKTRGKAKVTGRW
CCCCCCCCCCCCCCC
41.57133991
292AcetylationSKTRGKAKVTGRWK-
CCCCCCCCCCCCCC-
43.767695157
294PhosphorylationTRGKAKVTGRWK---
CCCCCCCCCCCC---
21.962584239

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
2SPhosphorylationKinaseCK2-Uniprot
189SPhosphorylationKinasePRKCAP17252
GPS
204TPhosphorylationKinasePRKCAP17252
Uniprot
208SPhosphorylationKinasePRKCAP17252
Uniprot
213TPhosphorylationKinasePRKCAP17252
Uniprot
213TPhosphorylationKinaseRAF1P04049
Uniprot
294TPhosphorylationKinasePRKCAP17252
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
213TPhosphorylation

-

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 TNNT2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
KDM1A_HUMANKDM1Aphysical
23455924
MO4L2_HUMANMORF4L2physical
25416956

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
115195Cardiomyopathy, familial hypertrophic 2 (CMH2)
601494Cardiomyopathy, dilated 1D (CMD1D)
612422Cardiomyopathy, familial restrictive 3 (RCM3)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TNNT2_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP