| UniProt ID | TRIM4_HUMAN | |
|---|---|---|
| UniProt AC | Q9C037 | |
| Protein Name | E3 ubiquitin-protein ligase TRIM4 | |
| Gene Name | TRIM4 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 500 | |
| Subcellular Localization | Cytoplasm . | |
| Protein Description | E3 ubiquitin-protein ligase. Mediates 'Lys-63'-linked polyubiquitination of the innate immune receptor DDX58, this linkage doesn't lead to proteasomal degradation but seems to enhance IFN induction.. | |
| Protein Sequence | MEAEDIQEELTCPICLDYFQDPVSIECGHNFCRGCLHRNWAPGGGPFPCPECRHPSAPAALRPNWALARLTEKTQRRRLGPVPPGLCGRHWEPLRLFCEDDQRPVCLVCRESQEHQTHAMAPIDEAFESYRTGNFDIHVDEWKRRLIRLLLYHFKQEEKLLKSQRNLVAKMKKVMHLQDVEVKNATQWKDKIKSQRMRISTEFSKLHNFLVEEEDLFLQRLNKEEEETKKKLNENTLKLNQTIASLKKLILEVGEKSQAPTLELLQNPKEVLTRSEIQDVNYSLEAVKVKTVCQIPLMKEMLKRFQVAVNLAEDTAHPKLVFSQEGRYVKNTASASSWPVFSSAWNYFAGWRNPQKTAFVERFQHLPCVLGKNVFTSGKHYWEVESRDSLEVAVGVCREDVMGITDRSKMSPDVGIWAIYWSAAGYWPLIGFPGTPTQQEPALHRVGVYLDRGTGNVSFYSAVDGVHLHTFSCSSVSRLRPFFWLSPLASLVIPPVTDRK | |
| 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 |
|---|---|---|---|---|---|
| 56 | Phosphorylation | CPECRHPSAPAALRP CCCCCCCCCCCHHCC | 40.53 | 27251275 | |
| 73 (in isoform 2) | Ubiquitination | - | 44.73 | 22053931 | |
| 73 | Ubiquitination | ALARLTEKTQRRRLG HHHHHHHHHHHHCCC | 44.73 | 22053931 | |
| 129 (in isoform 3) | Phosphorylation | - | 17.29 | - | |
| 129 (in isoform 2) | Phosphorylation | - | 17.29 | - | |
| 130 (in isoform 3) | Phosphorylation | - | 12.66 | - | |
| 130 (in isoform 2) | Phosphorylation | - | 12.66 | - | |
| 147 | Ubiquitination | DEWKRRLIRLLLYHF HHHHHHHHHHHHHHH | 2.50 | 29967540 | |
| 152 | Phosphorylation | RLIRLLLYHFKQEEK HHHHHHHHHHHHHHH | 12.74 | 19658100 | |
| 157 (in isoform 3) | Ubiquitination | - | 58.66 | 21906983 | |
| 157 (in isoform 2) | Ubiquitination | - | 58.66 | 22053931 | |
| 157 | Ubiquitination | LLYHFKQEEKLLKSQ HHHHHHHHHHHHHHH | 58.66 | 32015554 | |
| 163 | Ubiquitination | QEEKLLKSQRNLVAK HHHHHHHHHHHHHHH | 34.05 | 27667366 | |
| 173 | Acetylation | NLVAKMKKVMHLQDV HHHHHHHHHHHHHCC | 41.09 | 22424773 | |
| 173 | Ubiquitination | NLVAKMKKVMHLQDV HHHHHHHHHHHHHCC | 41.09 | 29967540 | |
| 183 (in isoform 1) | Ubiquitination | - | 27.62 | 21906983 | |
| 183 | Ubiquitination | HLQDVEVKNATQWKD HHHCCCCCCCHHHHH | 27.62 | 21906983 | |
| 189 | Ubiquitination | VKNATQWKDKIKSQR CCCCHHHHHHHHHHH | 39.05 | 27667366 | |
| 197 | Ubiquitination | DKIKSQRMRISTEFS HHHHHHHHHHHHHHH | 3.28 | 33845483 | |
| 200 | Phosphorylation | KSQRMRISTEFSKLH HHHHHHHHHHHHHHH | 16.12 | 24719451 | |
| 205 | Ubiquitination | RISTEFSKLHNFLVE HHHHHHHHHHHHHHC | 60.12 | 29967540 | |
| 212 | Ubiquitination | KLHNFLVEEEDLFLQ HHHHHHHCHHHHHHH | 58.79 | 29967540 | |
| 221 | Ubiquitination | EDLFLQRLNKEEEET HHHHHHHHCHHHHHH | 7.47 | 33845483 | |
| 221 (in isoform 3) | Ubiquitination | - | 7.47 | 21906983 | |
| 221 (in isoform 2) | Ubiquitination | - | 7.47 | 22053931 | |
| 222 | Ubiquitination | DLFLQRLNKEEEETK HHHHHHHCHHHHHHH | 52.46 | 33845483 | |
| 223 | Ubiquitination | LFLQRLNKEEEETKK HHHHHHCHHHHHHHH | 71.71 | 33845483 | |
| 230 | Ubiquitination | KEEEETKKKLNENTL HHHHHHHHHHCHHHH | 70.66 | 29967540 | |
| 231 | Ubiquitination | EEEETKKKLNENTLK HHHHHHHHHCHHHHH | 59.09 | 29967540 | |
| 236 | Phosphorylation | KKKLNENTLKLNQTI HHHHCHHHHHHHHHH | 21.06 | 29978859 | |
| 238 | Ubiquitination | KLNENTLKLNQTIAS HHCHHHHHHHHHHHH | 43.27 | 29967540 | |
| 243 (in isoform 2) | Ubiquitination | - | 1.44 | 22053931 | |
| 243 | Ubiquitination | TLKLNQTIASLKKLI HHHHHHHHHHHHHHH | 1.44 | 23503661 | |
| 243 (in isoform 3) | Ubiquitination | - | 1.44 | 21906983 | |
| 245 | Phosphorylation | KLNQTIASLKKLILE HHHHHHHHHHHHHHH | 36.55 | 24719451 | |
| 247 | Acetylation | NQTIASLKKLILEVG HHHHHHHHHHHHHHH | 42.93 | 25953088 | |
| 247 | 2-Hydroxyisobutyrylation | NQTIASLKKLILEVG HHHHHHHHHHHHHHH | 42.93 | - | |
| 247 (in isoform 1) | Ubiquitination | - | 42.93 | 21906983 | |
| 247 | Ubiquitination | NQTIASLKKLILEVG HHHHHHHHHHHHHHH | 42.93 | 21906983 | |
| 248 | Ubiquitination | QTIASLKKLILEVGE HHHHHHHHHHHHHHH | 46.16 | 33845483 | |
| 256 | Ubiquitination | LILEVGEKSQAPTLE HHHHHHHHCCCCHHH | 41.77 | 29967540 | |
| 262 (in isoform 3) | Ubiquitination | - | 4.20 | 21906983 | |
| 262 | Ubiquitination | EKSQAPTLELLQNPK HHCCCCHHHHHCCHH | 4.20 | 33845483 | |
| 262 (in isoform 2) | Ubiquitination | - | 4.20 | 22053931 | |
| 264 | Ubiquitination | SQAPTLELLQNPKEV CCCCHHHHHCCHHHH | 7.20 | 23503661 | |
| 269 (in isoform 1) | Ubiquitination | - | 68.92 | 21906983 | |
| 269 | Ubiquitination | LELLQNPKEVLTRSE HHHHCCHHHHHCHHH | 68.92 | 21906983 | |
| 273 | Phosphorylation | QNPKEVLTRSEIQDV CCHHHHHCHHHHCCC | 37.01 | 29759185 | |
| 275 | Phosphorylation | PKEVLTRSEIQDVNY HHHHHCHHHHCCCCC | 33.54 | 29759185 | |
| 282 | Phosphorylation | SEIQDVNYSLEAVKV HHHCCCCCCCEECEE | 17.93 | 29759185 | |
| 288 (in isoform 1) | Ubiquitination | - | 45.09 | 21906983 | |
| 288 | Ubiquitination | NYSLEAVKVKTVCQI CCCCEECEEEEEHHC | 45.09 | 21906983 | |
| 290 | Ubiquitination | SLEAVKVKTVCQIPL CCEECEEEEEHHCHH | 29.53 | 23503661 | |
| 304 | Ubiquitination | LMKEMLKRFQVAVNL HHHHHHHHHHHHHHH | 24.22 | 22817900 | |
| 319 | Ubiquitination | AEDTAHPKLVFSQEG CCCCCCCEEEECCCC | 47.63 | - | |
| 330 (in isoform 2) | Ubiquitination | - | 39.38 | 22053931 | |
| 330 | Ubiquitination | SQEGRYVKNTASASS CCCCCEEECCCCHHC | 39.38 | 33845483 | |
| 334 | Phosphorylation | RYVKNTASASSWPVF CEEECCCCHHCCCCC | 27.01 | 24275569 | |
| 337 | Phosphorylation | KNTASASSWPVFSSA ECCCCHHCCCCCHHH | 34.81 | 24275569 | |
| 342 | Phosphorylation | ASSWPVFSSAWNYFA HHCCCCCHHHHHHHC | 21.27 | 24275569 | |
| 343 | Phosphorylation | SSWPVFSSAWNYFAG HCCCCCHHHHHHHCC | 26.32 | 24275569 | |
| 346 | Ubiquitination | PVFSSAWNYFAGWRN CCCHHHHHHHCCCCC | 23.04 | 29967540 | |
| 353 | Ubiquitination | NYFAGWRNPQKTAFV HHHCCCCCHHCCHHH | 36.52 | 23503661 | |
| 353 (in isoform 2) | Ubiquitination | - | 36.52 | - | |
| 356 (in isoform 1) | Ubiquitination | - | 42.98 | 21906983 | |
| 356 | Ubiquitination | AGWRNPQKTAFVERF CCCCCHHCCHHHHHH | 42.98 | 27667366 | |
| 372 | Ubiquitination | HLPCVLGKNVFTSGK CCCEEEECCCCCCCC | 45.86 | 29967540 | |
| 376 | Phosphorylation | VLGKNVFTSGKHYWE EEECCCCCCCCCEEE | 32.08 | 24905233 | |
| 377 | Phosphorylation | LGKNVFTSGKHYWEV EECCCCCCCCCEEEE | 34.09 | 24905233 | |
| 379 | Ubiquitination | KNVFTSGKHYWEVES CCCCCCCCCEEEEEC | 33.03 | 23503661 | |
| 381 | Phosphorylation | VFTSGKHYWEVESRD CCCCCCCEEEEECCC | 13.52 | 29496907 | |
| 386 | Phosphorylation | KHYWEVESRDSLEVA CCEEEEECCCHHEEE | 46.71 | 24905233 | |
| 405 | Phosphorylation | REDVMGITDRSKMSP HHHHCCCCCHHHCCC | 21.45 | 20071362 |
| 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 TRIM4_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TRIM4_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 TRIM4_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| TRIM4_HUMAN | TRIM4 | physical | 17156811 | |
| TRIM4_HUMAN | TRIM4 | physical | 21680743 | |
| PDIA1_HUMAN | P4HB | physical | 26186194 | |
| PRDX1_HUMAN | PRDX1 | physical | 26524401 | |
| PDIA1_HUMAN | P4HB | physical | 28514442 |
| 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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