| UniProt ID | ASCC1_HUMAN | |
|---|---|---|
| UniProt AC | Q8N9N2 | |
| Protein Name | Activating signal cointegrator 1 complex subunit 1 | |
| Gene Name | ASCC1 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 400 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Enhances NF-kappa-B, SRF and AP1 transactivation. In cells responding to gastrin-activated paracrine signals, it is involved in the induction of SERPINB2 expression by gastrin. May also play a role in the development of neuromuscular junction.. | |
| Protein Sequence | MEVLRPQLIRIDGRNYRKNPVQEQTYQHEEDEEDFYQGSMECADEPCDAYEVEQTPQGFRSTLRAPSLLYNLIHLNTSNDCGFQKITLDCQNIYTWKSRHIVGKRGDTRKKIEMETKTSISIPKPGQDGEIVITGQHRNGVISARTRIDVLLDTFRRKQPFTHFLAFFLNEVEVQEGFLRFQEEVLAKCSMDHGVDSSIFQNPKKLHLTIGMLVLLSEEEIQQTCEMLQQCKEEFINDISGGKPLEVEMAGIEYMNDDPGMVDVLYAKVHMKDGSNRLQELVDRVLERFQASGLIVKEWNSVKLHATVMNTLFRKDPNAEGRYNLYTAEGKYIFKERESFDGRNILKSFALLPRLEYNDAISAHCNLCLPGSSDSPASASQVAGITGVSDAYSQSLPGKS | |
| 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 |
|---|---|---|---|---|---|
| 25 | Phosphorylation | KNPVQEQTYQHEEDE CCCCCCCCCCCCCCC | 25.13 | - | |
| 36 | Phosphorylation | EEDEEDFYQGSMECA CCCCCHHHCCCHHHC | 25.04 | 27251275 | |
| 39 | Phosphorylation | EEDFYQGSMECADEP CCHHHCCCHHHCCCC | 8.90 | 28348404 | |
| 61 (in isoform 2) | Phosphorylation | - | 29.54 | 24719451 | |
| 67 (in isoform 2) | Phosphorylation | - | 29.98 | 27251275 | |
| 70 (in isoform 2) | Phosphorylation | - | 17.14 | 24719451 | |
| 82 (in isoform 2) | Acetylation | - | 30.77 | - | |
| 110 | Acetylation | GKRGDTRKKIEMETK CCCCCCCCEEEEEEE | 61.26 | 20167786 | |
| 116 | Phosphorylation | RKKIEMETKTSISIP CCEEEEEEECEEECC | 38.01 | 26657352 | |
| 118 | Phosphorylation | KIEMETKTSISIPKP EEEEEEECEEECCCC | 38.42 | 26657352 | |
| 119 | Phosphorylation | IEMETKTSISIPKPG EEEEEECEEECCCCC | 18.85 | 26657352 | |
| 154 | Phosphorylation | RIDVLLDTFRRKQPF HHHHHHHHHHCCCCC | 21.00 | - | |
| 188 | Ubiquitination | FQEEVLAKCSMDHGV HHHHHHHHHCCCCCC | 23.76 | - | |
| 284 | Methylation | RLQELVDRVLERFQA HHHHHHHHHHHHHHH | 27.69 | - | |
| 291 (in isoform 2) | Ubiquitination | - | 11.67 | 21890473 | |
| 297 | Ubiquitination | QASGLIVKEWNSVKL HHCCCEEEECCCEEE | 50.44 | 21906983 | |
| 300 (in isoform 1) | Ubiquitination | - | 37.71 | 21890473 | |
| 323 | Phosphorylation | DPNAEGRYNLYTAEG CCCCCCCEEEEECCC | 22.00 | 25627689 | |
| 325 (in isoform 2) | Ubiquitination | - | 2.74 | 21890473 | |
| 326 | Phosphorylation | AEGRYNLYTAEGKYI CCCCEEEEECCCEEE | 10.56 | 28796482 | |
| 327 | Phosphorylation | EGRYNLYTAEGKYIF CCCEEEEECCCEEEE | 22.77 | 28796482 | |
| 331 | Ubiquitination | NLYTAEGKYIFKERE EEEECCCEEEECCCC | 27.03 | 21890473 | |
| 334 (in isoform 1) | Ubiquitination | - | 6.45 | 21890473 | |
| 335 | Ubiquitination | AEGKYIFKERESFDG CCCEEEECCCCCCCC | 46.43 | - | |
| 347 | Ubiquitination | FDGRNILKSFALLPR CCCCHHHHHHCEECC | 39.47 | - |
| 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 ASCC1_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ASCC1_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 ASCC1_HUMAN !! | ||||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| 614266 | Barrett esophagus (BE) | |||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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