TNNT1_HUMAN - dbPTM
TNNT1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TNNT1_HUMAN
UniProt AC P13805
Protein Name Troponin T, slow skeletal muscle
Gene Name TNNT1
Organism Homo sapiens (Human).
Sequence Length 278
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 MSDTEEQEYEEEQPEEEAAEEEEEAPEEPEPVAEPEEERPKPSRPVVPPLIPPKIPEGERVDFDDIHRKRMEKDLLELQTLIDVHFEQRKKEEEELVALKERIERRRSERAEQQRFRTEKERERQAKLAEEKMRKEEEEAKKRAEDDAKKKKVLSNMGAHFGGYLVKAEQKRGKRQTGREMKVRILSERKKPLDIDYMGEEQLRARSAWLPPSQPSCPAREKAQELSDWIHQLESEKFDLMAKLKQQKYEINVLYNRISHAQKFRKGAGKGRVGGRWK
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------MSDTEEQEY
------CCHHHHHHH
53.92-
2Phosphorylation------MSDTEEQEY
------CCHHHHHHH
53.9222673903
2 (in isoform 2)Phosphorylation-53.9222673903
4Phosphorylation----MSDTEEQEYEE
----CCHHHHHHHHH
33.8322673903
4 (in isoform 2)Phosphorylation-33.8322673903
155PhosphorylationAKKKKVLSNMGAHFG
HHHHHHHHHHCHHHH
27.9722210691
164PhosphorylationMGAHFGGYLVKAEQK
HCHHHHHHHHHHHHH
14.5417053785
186 (in isoform 2)Phosphorylation-2.8126437602
197PhosphorylationKKPLDIDYMGEEQLR
CCCCCCCCCCHHHHH
13.83-
197 (in isoform 3)Phosphorylation-13.8326437602
249PhosphorylationAKLKQQKYEINVLYN
HHHHHHHHHHHHHHH
20.0826437602
255PhosphorylationKYEINVLYNRISHAQ
HHHHHHHHHHHHHHH
9.7122673903
259PhosphorylationNVLYNRISHAQKFRK
HHHHHHHHHHHHHHC
14.9926437602

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

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TNNT1_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 TNNT1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CC85B_HUMANCCDC85Bphysical
16189514
PKHF1_HUMANPLEKHF1physical
16189514
LIPA1_HUMANPPFIA1physical
16189514
TNNT1_HUMANTNNT1physical
16189514
ZMY19_HUMANZMYND19physical
16189514
NINL_HUMANNINLphysical
16189514
FXR2_HUMANFXR2physical
16189514
TPM1_HUMANTPM1physical
6822572
KGP1_HUMANPRKG1physical
10601315
MIC60_HUMANIMMTphysical
21900206
SH3G3_HUMANSH3GL3physical
21900206
ZN768_HUMANZNF768physical
21900206
KAT5_HUMANKAT5physical
21900206
NACAD_HUMANNACADphysical
21900206
EF1G_HUMANEEF1Gphysical
21900206
HMGX4_HUMANHMGXB4physical
21900206
BL1S2_HUMANBLOC1S2physical
21900206
SNW1_HUMANSNW1physical
21900206
ZC3HF_HUMANZC3H15physical
21900206
NSG2_HUMANHMP19physical
21900206
KAIN_HUMANSERPINA4physical
21900206
UB2D1_HUMANUBE2D1physical
21900206
ZN250_HUMANZNF250physical
21900206
ZKSC5_HUMANZKSCAN5physical
21900206
NAGK_HUMANNAGKphysical
21900206
ONCM_HUMANOSMphysical
21900206
OSBP2_HUMANOSBP2physical
21900206
HS90B_HUMANHSP90AB1physical
21900206
TRA2A_HUMANTRA2Aphysical
21900206
TMM98_HUMANTMEM98physical
21900206
SYMC_HUMANMARSphysical
21900206
VIME_HUMANVIMphysical
21900206
HAP1_HUMANHAP1physical
21900206
ARMC8_HUMANARMC8physical
21900206
SC31A_HUMANSEC31Aphysical
21900206
FYN_HUMANFYNphysical
21900206
WDCP_HUMANC2orf44physical
21900206
CHD3_HUMANCHD3physical
21900206
DDX5_HUMANDDX5physical
21900206
FAF1_HUMANFAF1physical
21900206
LARP1_HUMANLARP1physical
21900206
TNNT1_HUMANTNNT1physical
25416956
TPM1_HUMANTPM1physical
25416956
TPM3_HUMANTPM3physical
25416956
TBPL1_HUMANTBPL1physical
25416956
MO4L1_HUMANMORF4L1physical
25416956
LDOC1_HUMANLDOC1physical
25416956
TFP11_HUMANTFIP11physical
25416956
CC136_HUMANCCDC136physical
25416956
K1C40_HUMANKRT40physical
25416956
TPM1_HUMANTPM1physical
21516116

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
605355Nemaline myopathy 5 (NEM5)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TNNT1_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Tyrosine phosphorylated Par3 regulates epithelial tight junctionassembly promoted by EGFR signaling.";
Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A.,Lottspeich F., Chen Z.;
EMBO J. 25:5058-5070(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-164, AND MASSSPECTROMETRY.

TOP