BCL3_HUMAN - dbPTM
BCL3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
21UbiquitinationVDLRTRPKAAGLPGA
CCCCCCCCCCCCCCC
47.8015469820
34UbiquitinationGAALPLRKRPLRAPS
CCCCCCCCCCCCCCC
67.081546982
41PhosphorylationKRPLRAPSPEPAAPR
CCCCCCCCCCCCCCC
40.6929255136
83PhosphorylationLARPEALYYPGALLP
CCCHHHHCCCCCCCC
18.0527642862
84PhosphorylationARPEALYYPGALLPL
CCHHHHCCCCCCCCC
8.95-
122PhosphorylationCPMEHPLSADIAMAT
CCCCCCCCCCEEEHH
28.48-
174PhosphorylationIYNNLRQTPLHLAVI
CCCCCCCCCCHHHHH
22.7624043423
182PhosphorylationPLHLAVITTLPSVVR
CCHHHHHHCHHHHHH
18.7124043423
183PhosphorylationLHLAVITTLPSVVRL
CHHHHHHCHHHHHHH
26.0824043423
186PhosphorylationAVITTLPSVVRLLVT
HHHHCHHHHHHHHHH
36.0424043423
193PhosphorylationSVVRLLVTAGASPMA
HHHHHHHHCCCCCCE
21.2424043423
197PhosphorylationLLVTAGASPMALDRH
HHHHCCCCCCEECCC
17.8124043423
338MethylationSGADSSLKNCHNDTP
CCCCHHHHCCCCCCC
60.52-
363PhosphorylationDILRGKATRPASTSQ
HHHCCCCCCCCCCCC
40.4423403867
367PhosphorylationGKATRPASTSQPDPS
CCCCCCCCCCCCCCC
31.1323403867
368PhosphorylationKATRPASTSQPDPSP
CCCCCCCCCCCCCCC
33.2223403867
369PhosphorylationATRPASTSQPDPSPD
CCCCCCCCCCCCCCC
36.9023663014
374PhosphorylationSTSQPDPSPDRSANT
CCCCCCCCCCCCCCC
46.9823401153
378PhosphorylationPDPSPDRSANTSPES
CCCCCCCCCCCCHHH
33.0028985074
381PhosphorylationSPDRSANTSPESSSR
CCCCCCCCCHHHHHH
45.4328985074
382PhosphorylationPDRSANTSPESSSRL
CCCCCCCCHHHHHHH
26.8625849741
385PhosphorylationSANTSPESSSRLSSN
CCCCCHHHHHHHHCC
36.6823927012
386PhosphorylationANTSPESSSRLSSNG
CCCCHHHHHHHHCCC
20.1623927012
387PhosphorylationNTSPESSSRLSSNGL
CCCHHHHHHHHCCCC
46.6623927012
402PhosphorylationLSASPSSSPSQSPPR
CCCCCCCCCCCCCCC
32.6715469820
406PhosphorylationPSSSPSQSPPRDPPG
CCCCCCCCCCCCCCC
41.0115469820
448PhosphorylationPGRPVPPSPAPGGS-
CCCCCCCCCCCCCC-
27.8529396449
454PhosphorylationPSPAPGGS-------
CCCCCCCC-------
42.8521712546

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
41SPhosphorylationKinaseAKT1P31749
PSP
41SPhosphorylationKinaseAKT1P31750
PSP
122SPhosphorylationKinaseMAPK1P63086
GPS
402SPhosphorylationKinaseGSK3AP49840
PSP
402SPhosphorylationKinaseGSK-FAMILY-GPS
402SPhosphorylationKinaseGSK3-Uniprot
406SPhosphorylationKinaseGSK3AP49840
PSP
406SPhosphorylationKinaseGSK-FAMILY-GPS
406SPhosphorylationKinaseGSK3-Uniprot
454SPhosphorylationKinaseCHUKO15111
GPS
454SPhosphorylationKinaseIKBKBO14920
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BCL3_HUMAN !!

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BARD1_HUMANBARD1physical
10362352
NFKB1_HUMANNFKB1physical
14678988
NFKB1_HUMANNFKB1physical
8428580
RELB_HUMANRELBphysical
14678988
N4BP2_HUMANN4BP2physical
12730195
PIR_HUMANPIRphysical
10362352
KAT5_HUMANKAT5physical
10362352
CSN5_HUMANCOPS5physical
10362352
JUN_HUMANJUNphysical
10497212
FOS_HUMANFOSphysical
10497212
EP300_HUMANEP300physical
10497212
NCOA1_HUMANNCOA1physical
10497212
NFKB1_HUMANNFKB1physical
10469655
TBP_HUMANTBPphysical
9812988
RXRA_HUMANRXRAphysical
9812988
TF2AA_HUMANGTF2A1physical
9812988
TF2B_HUMANGTF2Bphysical
9812988
CYLD_HUMANCYLDphysical
19893491
STAT1_HUMANSTAT1physical
16306601
STAT3_HUMANSTAT3physical
16306601
HDAC1_HUMANHDAC1physical
16306601
HSP74_HUMANHSPA4physical
20547759
TBL1R_HUMANTBL1XR1physical
20547759
CTBP1_HUMANCTBP1physical
20547759
CTBP2_HUMANCTBP2physical
20547759
BAG2_HUMANBAG2physical
20547759
HDAC3_HUMANHDAC3physical
20547759
RCOR1_HUMANRCOR1physical
20547759
KDM1A_HUMANKDM1Aphysical
20547759
NFKB1_HUMANNFKB1physical
20547759
GSK3B_HUMANGSK3Bphysical
15469820
HDAC1_HUMANHDAC1physical
15469820
NFKB1_HUMANNFKB1physical
20558726
NFKB2_HUMANNFKB2physical
20558726
PSB1_HUMANPSMB1physical
20558726
FBXW8_HUMANFBXW8physical
20558726
CTNB1_HUMANCTNNB1physical
15829968
CTBP1_HUMANCTBP1physical
20800578
NFKB1_HUMANNFKB1physical
20800578
NFKB2_HUMANNFKB2physical
20800578
RUVB1_HUMANRUVBL1physical
20800578
RUVB2_HUMANRUVBL2physical
20800578
BCL10_HUMANBCL10physical
16280327
CTBP2_HUMANCTBP2physical
21988832
NFKB2_HUMANNFKB2physical
28689659

Drug and Disease Associations
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.
Regulatory Network of BCL3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.

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