UniProt ID | CSN5_HUMAN | |
---|---|---|
UniProt AC | Q92905 | |
Protein Name | COP9 signalosome complex subunit 5 | |
Gene Name | COPS5 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 334 | |
Subcellular Localization | Cytoplasm, cytosol . Nucleus . Cytoplasm, perinuclear region . Cytoplasmic vesicle, secretory vesicle, synaptic vesicle . Nuclear localization is diminished in the presence of IFIT3. | |
Protein Description | Probable protease subunit 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 the 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, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8, 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. In the complex, it probably acts as the catalytic center that mediates the cleavage of Nedd8 from cullins. It however has no metalloprotease activity by itself and requires the other subunits of the CSN complex. Interacts directly with a large number of proteins that are regulated by the CSN complex, confirming a key role in the complex. Promotes the proteasomal degradation of BRSK2.. | |
Protein Sequence | MAASGSGMAQKTWELANNMQEAQSIDEIYKYDKKQQQEILAAKPWTKDHHYFKYCKISALALLKMVMHARSGGNLEVMGLMLGKVDGETMIIMDSFALPVEGTETRVNAQAAAYEYMAAYIENAKQVGRLENAIGWYHSHPGYGCWLSGIDVSTQMLNQQFQEPFVAVVIDPTRTISAGKVNLGAFRTYPKGYKPPDEGPSEYQTIPLNKIEDFGVHCKQYYALEVSYFKSSLDRKLLELLWNKYWVNTLSSSSLLTNADYTTGQVFDLSEKLEQSEAQLGRGSFMLGLETHDRKSEDKLAKATRDSCKTTIEAIHGLMSQVIKDKLFNQINIS | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
2 | Acetylation | ------MAASGSGMA ------CCCCCCCHH | 15.44 | 18850735 | |
4 | Phosphorylation | ----MAASGSGMAQK ----CCCCCCCHHHH | 24.77 | - | |
11 | Ubiquitination | SGSGMAQKTWELANN CCCCHHHHHHHHHHH | 46.17 | 21906983 | |
24 | Phosphorylation | NNMQEAQSIDEIYKY HHHHHHHHHHHHHCC | 38.77 | 24719451 | |
30 | Ubiquitination | QSIDEIYKYDKKQQQ HHHHHHHCCCHHHHH | 53.27 | 21906983 | |
33 | Ubiquitination | DEIYKYDKKQQQEIL HHHHCCCHHHHHHHH | 49.76 | 21906983 | |
34 | Ubiquitination | EIYKYDKKQQQEILA HHHCCCHHHHHHHHH | 50.90 | 21906983 | |
43 | Ubiquitination | QQEILAAKPWTKDHH HHHHHHCCCCCCCCH | 35.17 | 21906983 | |
47 | Acetylation | LAAKPWTKDHHYFKY HHCCCCCCCCHHHHH | 51.72 | 19608861 | |
47 | Ubiquitination | LAAKPWTKDHHYFKY HHCCCCCCCCHHHHH | 51.72 | 21906983 | |
53 | Ubiquitination | TKDHHYFKYCKISAL CCCCHHHHHHHHHHH | 42.44 | - | |
53 | Acetylation | TKDHHYFKYCKISAL CCCCHHHHHHHHHHH | 42.44 | 26051181 | |
54 | Phosphorylation | KDHHYFKYCKISALA CCCHHHHHHHHHHHH | 6.78 | - | |
56 | Ubiquitination | HHYFKYCKISALALL CHHHHHHHHHHHHHH | 36.28 | 21906983 | |
58 | Phosphorylation | YFKYCKISALALLKM HHHHHHHHHHHHHHH | 11.61 | - | |
71 | Phosphorylation | KMVMHARSGGNLEVM HHHHHHHCCCCCEEE | 52.41 | 21712546 | |
114 | Phosphorylation | VNAQAAAYEYMAAYI HHHHHHHHHHHHHHH | 11.67 | 27642862 | |
120 | Phosphorylation | AYEYMAAYIENAKQV HHHHHHHHHHHHHHH | 10.14 | 18669648 | |
125 | Ubiquitination | AAYIENAKQVGRLEN HHHHHHHHHHCCHHH | 58.03 | 21906983 | |
180 | Ubiquitination | TRTISAGKVNLGAFR CCEEECCCCCCCEEC | 27.89 | - | |
191 | Ubiquitination | GAFRTYPKGYKPPDE CEECCCCCCCCCCCC | 65.54 | 21890473 | |
194 | Ubiquitination | RTYPKGYKPPDEGPS CCCCCCCCCCCCCCC | 59.76 | 21906983 | |
194 | Acetylation | RTYPKGYKPPDEGPS CCCCCCCCCCCCCCC | 59.76 | 25953088 | |
201 | Phosphorylation | KPPDEGPSEYQTIPL CCCCCCCCCCCCEEH | 60.85 | 28796482 | |
203 | Phosphorylation | PDEGPSEYQTIPLNK CCCCCCCCCCEEHHH | 18.46 | 28796482 | |
205 | Phosphorylation | EGPSEYQTIPLNKIE CCCCCCCCEEHHHCC | 24.54 | 28796482 | |
210 | Ubiquitination | YQTIPLNKIEDFGVH CCCEEHHHCCCCCCC | 55.97 | - | |
210 | Acetylation | YQTIPLNKIEDFGVH CCCEEHHHCCCCCCC | 55.97 | 26051181 | |
236 | Ubiquitination | FKSSLDRKLLELLWN HCHHHHHHHHHHHHH | 58.03 | 21906983 | |
261 | Phosphorylation | SLLTNADYTTGQVFD CCCCCCCCCCCCCEE | 12.09 | 20068231 | |
262 | Phosphorylation | LLTNADYTTGQVFDL CCCCCCCCCCCCEEH | 25.62 | 20068231 | |
263 | Phosphorylation | LTNADYTTGQVFDLS CCCCCCCCCCCEEHH | 21.27 | 20068231 | |
270 | Phosphorylation | TGQVFDLSEKLEQSE CCCCEEHHHHHHHHH | 34.23 | 20068231 | |
276 | Phosphorylation | LSEKLEQSEAQLGRG HHHHHHHHHHHHCCC | 26.06 | 20068231 | |
282 | Methylation | QSEAQLGRGSFMLGL HHHHHHCCCCHHHCC | 46.29 | - | |
284 | Phosphorylation | EAQLGRGSFMLGLET HHHHCCCCHHHCCCC | 13.21 | 30108239 | |
286 | Sulfoxidation | QLGRGSFMLGLETHD HHCCCCHHHCCCCCC | 2.88 | 21406390 | |
291 | Phosphorylation | SFMLGLETHDRKSED CHHHCCCCCCCCCHH | 33.83 | - | |
294 | Methylation | LGLETHDRKSEDKLA HCCCCCCCCCHHHHH | 36.47 | - | |
295 | Methylation | GLETHDRKSEDKLAK CCCCCCCCCHHHHHH | 65.34 | - | |
304 | Phosphorylation | EDKLAKATRDSCKTT HHHHHHHHHHHHHHH | 34.01 | - | |
307 | Phosphorylation | LAKATRDSCKTTIEA HHHHHHHHHHHHHHH | 17.77 | - | |
309 | Ubiquitination | KATRDSCKTTIEAIH HHHHHHHHHHHHHHH | 53.29 | - | |
310 | Phosphorylation | ATRDSCKTTIEAIHG HHHHHHHHHHHHHHH | 37.02 | - | |
320 | Phosphorylation | EAIHGLMSQVIKDKL HHHHHHHHHHHHHHH | 26.74 | - | |
324 | Ubiquitination | GLMSQVIKDKLFNQI HHHHHHHHHHHHHCC | 50.37 | - | |
326 | Ubiquitination | MSQVIKDKLFNQINI HHHHHHHHHHHCCCC | 50.40 | - | |
326 | Acetylation | MSQVIKDKLFNQINI HHHHHHHHHHHCCCC | 50.40 | 87811 | |
334 | Phosphorylation | LFNQINIS------- HHHCCCCC------- | 29.67 | 28348404 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
201 | S | Phosphorylation | Kinase | IKKA | O15111 | PSP |
201 | S | Phosphorylation | Kinase | IKKB | O14920 | PSP |
205 | T | Phosphorylation | Kinase | IKKA | O15111 | PSP |
205 | T | Phosphorylation | Kinase | IKKB | O14920 | PSP |
320 | S | Phosphorylation | Kinase | ATM | Q13315 | PSP |
- | K | Ubiquitination | E3 ubiquitin ligase | DDB1 | Q16531 | PMID:23357576 |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CSN5_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 CSN5_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. |
loading...
Acetylation | |
Reference | PubMed |
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY. | |
"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 ALA-2. | |
"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-47, AND MASS SPECTROMETRY. |