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IID00710
UniprotP19838
ProteinNuclear factor NF-kappa-B p105 subunit
GeneNFKB1
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
968
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 2-365 Homo dimer :
 Evidence X-RAY 1svc P Reference
       Region 1svc P 2-41 disorder
       Region 1svc P 42-352 order
       Region 1svc P 353-365 disorder
Seq 40-352 Hetero dimer : IID00079Complex,IID00207Complex,IID00491Complex
 Evidence X-RAY 2o61 B Reference
       Region 2o61 B 40-352 order
Seq 41-352 Hetero tetramer : IID00207Complex
 Evidence X-RAY 3gut H Reference
       Region 3gut H 41-352 order
 Evidence X-RAY 3gut F Reference
       Region 3gut F 41-352 order
 Evidence X-RAY 3gut D Reference
       Region 3gut D 41-352 order
 Evidence X-RAY 3gut B Reference
       Region 3gut B 41-352 order
Seq 55-67 Hetero dimer : P10599
 Evidence 1mdk B Reference
       Region 1mdk B 55-67 order
 Evidence 1mdj B Reference
       Region 1mdj B 55-67 order
 Evidence NMR 1mdi B Reference
       Region 1mdi B 55-67 order
Seq 248-354 Hetero trimer : IID00207Complex,IID00654Complex
 Evidence X-RAY 1nfi D Reference
       Region 1nfi D 248-354 order
 Evidence X-RAY 1nfi B Reference
       Region 1nfi B 248-354 order
Seq 806-893 Monomer :
 Evidence NMR 2dbf A Reference
       Region 2dbf A 806-893 order
Seqphosphorylation
    943-943 Phosphothreonine
    932-932 Phosphoserine; by IKKB
    937-937 Phosphoserine
    907-907 Phosphoserine; by GSK3-beta; in vitro
    923-923 Phosphoserine
    927-927 Phosphoserine; by IKKB
    903-903 Phosphoserine; by GSK3-beta; in vitro
    892-892 Phosphoserine
    759-759 Phosphoserine
    449-449 Phosphoserine
    337-337 Phosphoserine; by PKA
Seqacetylation
    441-441 N6-acetyllysine; by EP300
    440-440 N6-acetyllysine; by EP300
    431-431 N6-acetyllysine; by EP300
 
Prediction
NeProc
Disorder 1-26,372-520,752-771,776-809,895-968
Order 27-31,39-371,521-751,772-775,810-894
ProS 4-26,372-379,398-457,466-520,767-771,776-791,809-809,919-941,949-968
AlphaFold
Disorder 1-39,65-66,182-185,354-499,568-572,755-769,795-806,891-968
Order 40-64,67-181,186-353,500-567,573-754,770-794,807-890
Pfam Hmmer
PF00554 44-242 2.4e-110
PF01833 250-350 2.5e-18
PF00023 581-613 2.7e-07
PF00023 650-682 1.2e-05
PF00023 718-750 1.6e-06
PF00531 817-892 6.3e-14
SEG 373-403 ,634-644
Function
Function in SwissProt
NF-kappa-B is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52 and the heterodimeric p65-p50 complex appears to be most abundant one. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. NF-kappa-B heterodimeric p65-p50 and RelB-p50 complexes are transcriptional activators. The NF-kappa-B p50-p50 homodimer is a transcriptional repressor, but can act as a transcriptional activator when associated with BCL3. NFKB1 appears to have dual functions such as cytoplasmic retention of attached NF-kappa-B proteins by p105 and generation of p50 by a cotranslational processing. The proteasome-mediated process ensures the production of both p50 and p105 and preserves their independent function, although processing of NFKB1/p105 also appears to occur post-translationally. p50 binds to the kappa-B consensus sequence 5'-GGRNNYYCC-3', located in the enhancer region of genes involved in immune response and acute phase reactions. In a complex with MAP3K8, NFKB1/p105 represses MAP3K8-induced MAPK signaling; active MAP3K8 is released by proteasome-dependent degradation of NFKB1/p105.