UniProt ID | TUSC2_HUMAN | |
---|---|---|
UniProt AC | O75896 | |
Protein Name | Tumor suppressor candidate 2 | |
Gene Name | TUSC2 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 110 | |
Subcellular Localization | ||
Protein Description | May function as a tumor suppressor, inhibiting colony formation, causing G1 arrest and ultimately inducing apoptosis in homozygous 3p21.3 120-kb region-deficient cells.. | |
Protein Sequence | MGASGSKARGLWPFASAAGGGGSEAAGAEQALVRPRGRAVPPFVFTRRGSMFYDEDGDLAHEFYEETIVTKNGQKRAKLRRVHKNLIPQGIVKLDHPRIHVDFPVILYEV | |
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 | N-myristoyl glycine | ------MGASGSKAR ------CCCCCCCCC | 28.57 | - | |
2 | Myristoylation | ------MGASGSKAR ------CCCCCCCCC | 28.57 | 15126327 | |
9 | Methylation | GASGSKARGLWPFAS CCCCCCCCCCHHCCC | 44.46 | 54560441 | |
46 | Phosphorylation | AVPPFVFTRRGSMFY CCCCEEEEECCCEEE | 17.72 | 26074081 | |
50 | Phosphorylation | FVFTRRGSMFYDEDG EEEEECCCEEECCCC | 12.14 | 30266825 | |
53 | Phosphorylation | TRRGSMFYDEDGDLA EECCCEEECCCCCCH | 15.13 | 30266825 | |
64 | Phosphorylation | GDLAHEFYEETIVTK CCCHHHEHHEEEECC | 15.18 | 23927012 | |
67 | Phosphorylation | AHEFYEETIVTKNGQ HHHEHHEEEECCCCH | 14.60 | 23927012 | |
70 | Phosphorylation | FYEETIVTKNGQKRA EHHEEEECCCCHHHH | 18.23 | 23927012 | |
93 | Acetylation | LIPQGIVKLDHPRIH CCCCCCEECCCCEEE | 46.40 | 23749302 |
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 TUSC2_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TUSC2_HUMAN !! |
* 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 TUSC2_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
HS74L_HUMAN | HSPA4L | physical | 17353931 | |
EBLN2_HUMAN | EBLN2 | physical | 17353931 | |
SGO2_HUMAN | SGOL2 | physical | 17353931 | |
LRBA_HUMAN | LRBA | physical | 17353931 |
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 | ||||||
There are no disease associations of PTM sites. |
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Myristoylation | |
Reference | PubMed |
"Myristoylation of the fus1 protein is required for tumor suppressionin human lung cancer cells."; Uno F., Sasaki J., Nishizaki M., Carboni G., Xu K., Atkinson E.N.,Kondo M., Minna J.D., Roth J.A., Ji L.; Cancer Res. 64:2969-2976(2004). Cited for: MYRISTOYLATION AT GLY-2. | |
Phosphorylation | |
Reference | PubMed |
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND MASSSPECTROMETRY. |