| UniProt ID | CSN7A_HUMAN | |
|---|---|---|
| UniProt AC | Q9UBW8 | |
| Protein Name | COP9 signalosome complex subunit 7a | |
| Gene Name | COPS7A | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 275 | |
| Subcellular Localization | Cytoplasm . Nucleus . | |
| Protein Description | Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, JUN, I-kappa-B-alpha/NFKBIA, ITPK1 and IRF8/ICSBP, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively.. | |
| Protein Sequence | MSAEVKVTGQNQEQFLLLAKSAKGAALATLIHQVLEAPGVYVFGELLDMPNVRELAESDFASTFRLLTVFAYGTYADYLAEARNLPPLTEAQKNKLRHLSVVTLAAKVKCIPYAVLLEALALRNVRQLEDLVIEAVYADVLRGSLDQRNQRLEVDYSIGRDIQRQDLSAIARTLQEWCVGCEVVLSGIEEQVSRANQHKEQQLGLKQQIESEVANLKKTIKVTTAAAAAATSQDPEQHLTELREPAPGTNQRQPSKKASKGKGLRGSAKIWSKSN | |
| 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 |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MSAEVKVTG ------CCCEEEECC | 32.89 | 18850735 | |
| 20 | Ubiquitination | EQFLLLAKSAKGAAL HHHHHHHHHHHHHHH | 51.41 | 21906983 | |
| 23 | Ubiquitination | LLLAKSAKGAALATL HHHHHHHHHHHHHHH | 57.06 | 22817900 | |
| 93 | Ubiquitination | PPLTEAQKNKLRHLS CCCCHHHHHCCHHHH | 64.20 | 24816145 | |
| 93 | Malonylation | PPLTEAQKNKLRHLS CCCCHHHHHCCHHHH | 64.20 | 32601280 | |
| 107 | Ubiquitination | SVVTLAAKVKCIPYA HHHHHHHHCCHHHHH | 36.30 | 33845483 | |
| 109 | Ubiquitination | VTLAAKVKCIPYAVL HHHHHHCCHHHHHHH | 26.24 | - | |
| 137 | Phosphorylation | DLVIEAVYADVLRGS HHHHHHHHHHHHHCC | 12.25 | 21406692 | |
| 199 | Ubiquitination | VSRANQHKEQQLGLK HHHHHHHHHHHHHHH | 47.67 | 21906983 | |
| 206 | Ubiquitination | KEQQLGLKQQIESEV HHHHHHHHHHHHHHH | 38.06 | 21906983 | |
| 217 | Ubiquitination | ESEVANLKKTIKVTT HHHHHHHHHHHHHHH | 47.91 | 21906983 | |
| 218 | Ubiquitination | SEVANLKKTIKVTTA HHHHHHHHHHHHHHH | 59.66 | 22817900 | |
| 219 | Phosphorylation | EVANLKKTIKVTTAA HHHHHHHHHHHHHHH | 25.17 | - | |
| 221 | Ubiquitination | ANLKKTIKVTTAAAA HHHHHHHHHHHHHHH | 38.47 | 21906983 | |
| 221 | Acetylation | ANLKKTIKVTTAAAA HHHHHHHHHHHHHHH | 38.47 | 19825065 | |
| 223 | Phosphorylation | LKKTIKVTTAAAAAA HHHHHHHHHHHHHHH | 13.00 | 26074081 | |
| 224 | Phosphorylation | KKTIKVTTAAAAAAT HHHHHHHHHHHHHHH | 19.79 | 26074081 | |
| 231 | Phosphorylation | TAAAAAATSQDPEQH HHHHHHHHCCCHHHH | 23.38 | 25849741 | |
| 232 | Phosphorylation | AAAAAATSQDPEQHL HHHHHHHCCCHHHHH | 28.05 | 17525332 | |
| 240 | Phosphorylation | QDPEQHLTELREPAP CCHHHHHHHHCCCCC | 30.74 | 23663014 | |
| 243 | Methylation | EQHLTELREPAPGTN HHHHHHHCCCCCCCC | 41.44 | - | |
| 249 | Phosphorylation | LREPAPGTNQRQPSK HCCCCCCCCCCCCCC | 27.41 | 25849741 | |
| 255 | Phosphorylation | GTNQRQPSKKASKGK CCCCCCCCCCCCCCC | 38.15 | 25849741 | |
| 256 | Acetylation | TNQRQPSKKASKGKG CCCCCCCCCCCCCCC | 60.07 | 11792171 | |
| 257 | Ubiquitination | NQRQPSKKASKGKGL CCCCCCCCCCCCCCC | 63.33 | 24816145 | |
| 260 | Acetylation | QPSKKASKGKGLRGS CCCCCCCCCCCCCCC | 70.29 | 130505 | |
| 269 | Ubiquitination | KGLRGSAKIWSKSN- CCCCCCCHHHCCCC- | 46.54 | 33845483 | |
| 269 | Acetylation | KGLRGSAKIWSKSN- CCCCCCCHHHCCCC- | 46.54 | 25953088 | |
| 274 | Phosphorylation | SAKIWSKSN------ CCHHHCCCC------ | 42.11 | 21712546 |
| 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 CSN7A_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CSN7A_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 CSN7A_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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| Acetylation | |
| Reference | PubMed |
| "Characterization of the human COP9 signalosome complex using affinitypurification and mass spectrometry."; Fang L., Wang X., Yamoah K., Chen P.L., Pan Z.Q., Huang L.; J. Proteome Res. 7:4914-4925(2008). Cited for: IDENTIFICATION IN THE CSN COMPLEX, CLEAVAGE OF INITIATOR METHIONINE,AND ACETYLATION AT SER-2. | |
| Phosphorylation | |
| Reference | PubMed |
| "ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, AND MASSSPECTROMETRY. | |
