| UniProt ID | THIOM_HUMAN | |
|---|---|---|
| UniProt AC | Q99757 | |
| Protein Name | Thioredoxin, mitochondrial | |
| Gene Name | TXN2 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 166 | |
| Subcellular Localization | Mitochondrion . | |
| Protein Description | Important for the control of mitochondrial reactive oxygen species homeostasis, apoptosis regulation and cell viability. Possesses a dithiol-reducing activity.. | |
| Protein Sequence | MAQRLLLRRFLASVISRKPSQGQWPPLTSRALQTPQCSPGGLTVTPNPARTIYTTRISLTTFNIQDGPDFQDRVVNSETPVVVDFHAQWCGPCKILGPRLEKMVAKQHGKVVMAKVDIDDHTDLAIEYEVSAVPTVLAMKNGDVVDKFVGIKDEDQLEAFLKKLIG | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 94 | Acetylation | AQWCGPCKILGPRLE CCCCCCCEEHHHHHH | 44.06 | 26051181 | |
| 102 | Acetylation | ILGPRLEKMVAKQHG EHHHHHHHHHHHHCC | 43.18 | 25953088 | |
| 102 | Ubiquitination | ILGPRLEKMVAKQHG EHHHHHHHHHHHHCC | 43.18 | 21890473 | |
| 102 | 2-Hydroxyisobutyrylation | ILGPRLEKMVAKQHG EHHHHHHHHHHHHCC | 43.18 | - | |
| 106 | 2-Hydroxyisobutyrylation | RLEKMVAKQHGKVVM HHHHHHHHHCCCEEE | 31.27 | - | |
| 128 | Phosphorylation | HTDLAIEYEVSAVPT CCCEEEEEEECCCCE | 18.60 | 28258704 | |
| 131 | Phosphorylation | LAIEYEVSAVPTVLA EEEEEEECCCCEEEE | 16.17 | 28258704 | |
| 133 | Ubiquitination | IEYEVSAVPTVLAMK EEEEECCCCEEEEEC | 2.96 | 21890473 | |
| 152 | Acetylation | VDKFVGIKDEDQLEA EEEECCCCCHHHHHH | 49.49 | 19608861 | |
| 152 | Succinylation | VDKFVGIKDEDQLEA EEEECCCCCHHHHHH | 49.49 | - | |
| 152 | 2-Hydroxyisobutyrylation | VDKFVGIKDEDQLEA EEEECCCCCHHHHHH | 49.49 | - | |
| 152 | Succinylation | VDKFVGIKDEDQLEA EEEECCCCCHHHHHH | 49.49 | 23954790 | |
| 162 | 2-Hydroxyisobutyrylation | DQLEAFLKKLIG--- HHHHHHHHHHHC--- | 38.80 | - | |
| 162 | Acetylation | DQLEAFLKKLIG--- HHHHHHHHHHHC--- | 38.80 | 25953088 |
| 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 THIOM_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of THIOM_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 THIOM_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| TOM22_HUMAN | TOMM22 | physical | 22939629 | |
| TPM4_HUMAN | TPM4 | physical | 22939629 | |
| VIME_HUMAN | VIM | physical | 21988832 | |
| GCR_HUMAN | NR3C1 | physical | 19570036 | |
| TF65_HUMAN | RELA | physical | 19570036 | |
| RABX5_HUMAN | RABGEF1 | physical | 25416956 | |
| ATRAP_HUMAN | AGTRAP | physical | 25416956 | |
| PACE1_HUMAN | SCYL3 | physical | 25416956 | |
| COAC_HUMAN | PPCDC | physical | 25416956 | |
| TIFA_HUMAN | TIFA | physical | 25416956 | |
| REEP6_HUMAN | REEP6 | physical | 25416956 | |
| CC114_HUMAN | CCDC114 | physical | 25416956 | |
| MR1L1_HUMAN | MRFAP1L1 | physical | 25416956 | |
| K1C40_HUMAN | KRT40 | physical | 25416956 | |
| RBM45_HUMAN | RBM45 | physical | 25416956 | |
| FAM9B_HUMAN | FAM9B | physical | 25416956 | |
| ANXA6_HUMAN | ANXA6 | physical | 26344197 | |
| FA98B_HUMAN | FAM98B | physical | 26344197 | |
| SODC_HUMAN | SOD1 | physical | 26344197 | |
| THIO_HUMAN | TXN | physical | 26344197 | |
| WDR12_HUMAN | WDR12 | physical | 26344197 |
| 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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| Acetylation | |
| Reference | PubMed |
| "Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-152, AND MASS SPECTROMETRY. | |