| UniProt ID | ZN383_HUMAN | |
|---|---|---|
| UniProt AC | Q8NA42 | |
| Protein Name | Zinc finger protein 383 | |
| Gene Name | ZNF383 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 475 | |
| Subcellular Localization | Nucleus . Cytoplasm . Shuttling between the nucleus and cytoplasm may occur under different stimulation and growth conditions. | |
| Protein Description | May function as a transcriptional repressor, suppressing transcriptional activities mediated by MAPK signaling pathways.. | |
| Protein Sequence | MAEGSVMFSDVSIDFSQEEWDCLDPVQRDLYRDVMLENYGNLVSMGLYTPKPQVISLLEQGKEPWMVGRELTRGLCSDLESMCETKLLSLKKEVYEIELCQREIMGLTKHGLEYSSFGDVLEYRSHLAKQLGYPNGHFSQEIFTPEYMPTFIQQTFLTLHQIINNEDRPYECKKCGKAFSQNSQFIQHQRIHIGEKSYECKECGKFFSCGSHVTRHLKIHTGEKPFECKECGKAFSCSSYLSQHQRIHTGKKPYECKECGKAFSYCSNLIDHQRIHTGEKPYECKVCGKAFTKSSQLFQHARIHTGEKPYECKECGKAFTQSSKLVQHQRIHTGEKPYECKECGKAFSSGSALTNHQRIHTGEKPYDCKECGKAFTQSSQLRQHQRIHAGEKPFECLECGKAFTQNSQLFQHQRIHTDEKPYECNECGKAFNKCSNLTRHLRIHTGEKPYNCKECGKAFSSGSDLIRHQGIHTNK | |
| 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 |
|---|---|---|---|---|---|
| 89 | Phosphorylation | MCETKLLSLKKEVYE HHHHHHHHHHHHHHH | 48.88 | 24719451 | |
| 208 | Phosphorylation | KECGKFFSCGSHVTR CCCCCEEECCCHHHH | 22.24 | - | |
| 211 | Phosphorylation | GKFFSCGSHVTRHLK CCEEECCCHHHHCEE | 21.07 | - | |
| 214 | Phosphorylation | FSCGSHVTRHLKIHT EECCCHHHHCEEEEC | 13.62 | - | |
| 221 | Phosphorylation | TRHLKIHTGEKPFEC HHCEEEECCCCCCCC | 50.97 | 28348404 | |
| 229 | Sumoylation | GEKPFECKECGKAFS CCCCCCCCCCCCEEE | 49.17 | - | |
| 229 | Sumoylation | GEKPFECKECGKAFS CCCCCCCCCCCCEEE | 49.17 | - | |
| 254 | Phosphorylation | IHTGKKPYECKECGK CCCCCCCCCCCCCHH | 42.72 | - | |
| 257 | Sumoylation | GKKPYECKECGKAFS CCCCCCCCCCHHHHH | 44.06 | - | |
| 257 | Sumoylation | GKKPYECKECGKAFS CCCCCCCCCCHHHHH | 44.06 | - | |
| 265 | Phosphorylation | ECGKAFSYCSNLIDH CCHHHHHHHHHHCCC | 8.08 | - | |
| 277 | Phosphorylation | IDHQRIHTGEKPYEC CCCCCCCCCCCCEEC | 44.67 | 29496963 | |
| 305 | Phosphorylation | FQHARIHTGEKPYEC HHHCEECCCCCCCCC | 44.67 | 29496963 | |
| 313 | Sumoylation | GEKPYECKECGKAFT CCCCCCCCHHHHHHH | 44.06 | - | |
| 313 | Sumoylation | GEKPYECKECGKAFT CCCCCCCCHHHHHHH | 44.06 | - | |
| 333 | Phosphorylation | VQHQRIHTGEKPYEC HCCCCCCCCCCCCCC | 44.67 | 29496963 | |
| 341 | Sumoylation | GEKPYECKECGKAFS CCCCCCCCCCCCCCC | 44.06 | - | |
| 341 | Sumoylation | GEKPYECKECGKAFS CCCCCCCCCCCCCCC | 44.06 | - | |
| 361 | Phosphorylation | TNHQRIHTGEKPYDC CCCCCCCCCCCCCCH | 44.67 | 28111955 | |
| 420 | Ubiquitination | QRIHTDEKPYECNEC CCCCCCCCCCCCCHH | 56.56 | - | |
| 445 | Phosphorylation | TRHLRIHTGEKPYNC HHHEEEECCCCCCCC | 44.67 | 28111955 | |
| 460 | Phosphorylation | KECGKAFSSGSDLIR CCCCCCCCCCHHHHH | 38.35 | 23532336 |
| 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 ZN383_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ZN383_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 ZN383_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of ZN383_HUMAN !! | ||||
| 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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