UniProt ID | BCL3_HUMAN | |
---|---|---|
UniProt AC | P20749 | |
Protein Name | B-cell lymphoma 3 protein | |
Gene Name | BCL3 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 454 | |
Subcellular Localization | Nucleus. Cytoplasm. Cytoplasm, perinuclear region. Ubiquitination via 'Lys-63'-linked ubiquitin chains is required for nuclear accumulation.. | |
Protein Description | Contributes to the regulation of transcriptional activation of NF-kappa-B target genes. In the cytoplasm, inhibits the nuclear translocation of the NF-kappa-B p50 subunit. In the nucleus, acts as transcriptional activator that promotes transcription of NF-kappa-B target genes. Contributes to the regulation of cell proliferation (By similarity).. | |
Protein Sequence | MPRCPAGAMDEGPVDLRTRPKAAGLPGAALPLRKRPLRAPSPEPAAPRGAAGLVVPLDPLRGGCDLPAVPGPPHGLARPEALYYPGALLPLYPTRAMGSPFPLVNLPTPLYPMMCPMEHPLSADIAMATRADEDGDTPLHIAVVQGNLPAVHRLVNLFQQGGRELDIYNNLRQTPLHLAVITTLPSVVRLLVTAGASPMALDRHGQTAAHLACEHRSPTCLRALLDSAAPGTLDLEARNYDGLTALHVAVNTECQETVQLLLERGADIDAVDIKSGRSPLIHAVENNSLSMVQLLLQHGANVNAQMYSGSSALHSASGRGLLPLVRTLVRSGADSSLKNCHNDTPLMVARSRRVIDILRGKATRPASTSQPDPSPDRSANTSPESSSRLSSNGLLSASPSSSPSQSPPRDPPGFPMAPPNFFLPSPSPPAFLPFAGVLRGPGRPVPPSPAPGGS | |
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 |
---|---|---|---|---|---|
21 | Ubiquitination | VDLRTRPKAAGLPGA CCCCCCCCCCCCCCC | 47.80 | 15469820 | |
34 | Ubiquitination | GAALPLRKRPLRAPS CCCCCCCCCCCCCCC | 67.08 | 1546982 | |
41 | Phosphorylation | KRPLRAPSPEPAAPR CCCCCCCCCCCCCCC | 40.69 | 29255136 | |
83 | Phosphorylation | LARPEALYYPGALLP CCCHHHHCCCCCCCC | 18.05 | 27642862 | |
84 | Phosphorylation | ARPEALYYPGALLPL CCHHHHCCCCCCCCC | 8.95 | - | |
122 | Phosphorylation | CPMEHPLSADIAMAT CCCCCCCCCCEEEHH | 28.48 | - | |
174 | Phosphorylation | IYNNLRQTPLHLAVI CCCCCCCCCCHHHHH | 22.76 | 24043423 | |
182 | Phosphorylation | PLHLAVITTLPSVVR CCHHHHHHCHHHHHH | 18.71 | 24043423 | |
183 | Phosphorylation | LHLAVITTLPSVVRL CHHHHHHCHHHHHHH | 26.08 | 24043423 | |
186 | Phosphorylation | AVITTLPSVVRLLVT HHHHCHHHHHHHHHH | 36.04 | 24043423 | |
193 | Phosphorylation | SVVRLLVTAGASPMA HHHHHHHHCCCCCCE | 21.24 | 24043423 | |
197 | Phosphorylation | LLVTAGASPMALDRH HHHHCCCCCCEECCC | 17.81 | 24043423 | |
338 | Methylation | SGADSSLKNCHNDTP CCCCHHHHCCCCCCC | 60.52 | - | |
363 | Phosphorylation | DILRGKATRPASTSQ HHHCCCCCCCCCCCC | 40.44 | 23403867 | |
367 | Phosphorylation | GKATRPASTSQPDPS CCCCCCCCCCCCCCC | 31.13 | 23403867 | |
368 | Phosphorylation | KATRPASTSQPDPSP CCCCCCCCCCCCCCC | 33.22 | 23403867 | |
369 | Phosphorylation | ATRPASTSQPDPSPD CCCCCCCCCCCCCCC | 36.90 | 23663014 | |
374 | Phosphorylation | STSQPDPSPDRSANT CCCCCCCCCCCCCCC | 46.98 | 23401153 | |
378 | Phosphorylation | PDPSPDRSANTSPES CCCCCCCCCCCCHHH | 33.00 | 28985074 | |
381 | Phosphorylation | SPDRSANTSPESSSR CCCCCCCCCHHHHHH | 45.43 | 28985074 | |
382 | Phosphorylation | PDRSANTSPESSSRL CCCCCCCCHHHHHHH | 26.86 | 25849741 | |
385 | Phosphorylation | SANTSPESSSRLSSN CCCCCHHHHHHHHCC | 36.68 | 23927012 | |
386 | Phosphorylation | ANTSPESSSRLSSNG CCCCHHHHHHHHCCC | 20.16 | 23927012 | |
387 | Phosphorylation | NTSPESSSRLSSNGL CCCHHHHHHHHCCCC | 46.66 | 23927012 | |
402 | Phosphorylation | LSASPSSSPSQSPPR CCCCCCCCCCCCCCC | 32.67 | 15469820 | |
406 | Phosphorylation | PSSSPSQSPPRDPPG CCCCCCCCCCCCCCC | 41.01 | 15469820 | |
448 | Phosphorylation | PGRPVPPSPAPGGS- CCCCCCCCCCCCCC- | 27.85 | 29396449 | |
454 | Phosphorylation | PSPAPGGS------- CCCCCCCC------- | 42.85 | 21712546 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
41 | S | Phosphorylation | Kinase | AKT1 | P31749 | PSP |
41 | S | Phosphorylation | Kinase | AKT1 | P31750 | PSP |
122 | S | Phosphorylation | Kinase | MAPK1 | P63086 | GPS |
402 | S | Phosphorylation | Kinase | GSK3A | P49840 | PSP |
402 | S | Phosphorylation | Kinase | GSK-FAMILY | - | GPS |
402 | S | Phosphorylation | Kinase | GSK3 | - | Uniprot |
406 | S | Phosphorylation | Kinase | GSK3A | P49840 | PSP |
406 | S | Phosphorylation | Kinase | GSK-FAMILY | - | GPS |
406 | S | Phosphorylation | Kinase | GSK3 | - | Uniprot |
454 | S | Phosphorylation | Kinase | CHUK | O15111 | GPS |
454 | S | Phosphorylation | Kinase | IKBKB | O14920 | GPS |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of BCL3_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 BCL3_HUMAN !! |
Kegg Disease | ||||||
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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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Phosphorylation | |
Reference | PubMed |
"GSK3-mediated BCL-3 phosphorylation modulates its degradation and itsoncogenicity."; Viatour P., Dejardin E., Warnier M., Lair F., Claudio E., Bureau F.,Marine J.C., Merville M.P., Maurer U., Green D., Piette J.,Siebenlist U., Bours V., Chariot A.; Mol. Cell 16:35-45(2004). Cited for: PHOSPHORYLATION AT SER-404 AND SER-406. |