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Nuclear factor NF-kappa-B p105 subunit (DNA-binding factor KBF1) (EBP-1) (Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1) [Cleaved into: Nuclear factor NF-kappa-B p50 subunit] (Fragment)

 NFKB1_RAT               Reviewed;         522 AA.
Q63369;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 1.
20-JUN-2018, entry version 153.
RecName: Full=Nuclear factor NF-kappa-B p105 subunit;
AltName: Full=DNA-binding factor KBF1;
AltName: Full=EBP-1;
AltName: Full=Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1;
Contains:
RecName: Full=Nuclear factor NF-kappa-B p50 subunit;
Flags: Fragment;
Name=Nfkb1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Testis;
PubMed=8161377; DOI=10.1210/endo.134.3.8161377;
Hamil K.G., Hall S.H.;
"Cloning of rat Sertoli cell follicle-stimulating hormone primary
response complementary deoxyribonucleic acid: regulation of TSC-22
gene expression.";
Endocrinology 134:1205-1212(1994).
[2]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: 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.
Plays a role in the regulation of apoptosis. Isoform 5, isoform 6
and isoform 7 act as inhibitors of transactivation of p50 NF-
kappa-B subunit, probably by sequestering it in the cytoplasm.
Isoform 3 (p98) (but not p84 or p105) acts as a transactivator of
NF-kappa-B-regulated gene expression. In a complex with MAP3K8,
NFKB1/p105 represses MAP3K8-induced MAPK signaling; active MAP3K8
is released by proteasome-dependent degradation of NFKB1/p105 (By
similarity). {ECO:0000250}.
-!- SUBUNIT: Component of the NF-kappa-B p65-p50 complex. Component of
the NF-kappa-B p65-p50 complex. Homodimer; component of the NF-
kappa-B p50-p50 complex. Component of the NF-kappa-B p105-p50
complex. Component of the NF-kappa-B p50-c-Rel complex. Component
of a complex consisting of the NF-kappa-B p50-p50 homodimer and
BCL3. Also interacts with MAP3K8. NF-kappa-B p50 subunit interacts
with NCOA3 coactivator, which may coactivate NF-kappa-B dependent
expression via its histone acetyltransferase activity. Interacts
with DSIPI; this interaction prevents nuclear translocation and
DNA-binding. Interacts with SPAG9 and UNC5CL. NFKB1/p105 interacts
with CFLAR; the interaction inhibits p105 processing into p50.
NFKB1/p105 forms a ternary complex with MAP3K8 and TNIP2.
Interacts with GSK3B; the interaction prevents processing of p105
to p50. NFKB1/p50 interacts with NFKBIE. NFKB1/p50 interacts with
NFKBIZ. Nuclear factor NF-kappa-B p50 subunit interacts with
NFKBID (By similarity). Directly interacts with MEN1 (By
similarity). Interacts with HIF1AN (By similarity). {ECO:0000250}.
-!- INTERACTION:
P47196:Akt1; NbExp=9; IntAct=EBI-8498561, EBI-7204362;
Q99N34:Dffb; NbExp=2; IntAct=EBI-8498561, EBI-8498730;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm
{ECO:0000250}. Note=Nuclear, but also found in the cytoplasm in an
inactive form complexed to an inhibitor (I-kappa-B).
{ECO:0000250}.
-!- DOMAIN: The C-terminus of p105 might be involved in cytoplasmic
retention, inhibition of DNA-binding by p50 homodimers, and/or
transcription activation.
-!- PTM: While translation occurs, the particular unfolded structure
after the GRR repeat promotes the generation of p50 making it an
acceptable substrate for the proteasome. This process is known as
cotranslational processing. The processed form is active and the
unprocessed form acts as an inhibitor (I kappa B-like), being able
to form cytosolic complexes with NF-kappa B, trapping it in the
cytoplasm. Complete folding of the region downstream of the GRR
repeat precludes processing (By similarity). {ECO:0000250}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; L26267; AAA20684.1; -; mRNA.
PIR; I67414; I67414.
UniGene; Rn.2411; -.
ProteinModelPortal; Q63369; -.
SMR; Q63369; -.
CORUM; Q63369; -.
IntAct; Q63369; 3.
MINT; Q63369; -.
STRING; 10116.ENSRNOP00000028944; -.
iPTMnet; Q63369; -.
PaxDb; Q63369; -.
PeptideAtlas; Q63369; -.
PRIDE; Q63369; -.
RGD; 70498; Nfkb1.
eggNOG; KOG0504; Eukaryota.
eggNOG; COG0666; LUCA.
HOGENOM; HOG000004822; -.
HOVERGEN; HBG052613; -.
InParanoid; Q63369; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0033256; C:I-kappaB/NF-kappaB complex; IBA:GO_Central.
GO; GO:0043005; C:neuron projection; IDA:RGD.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0032991; C:protein-containing complex; IDA:RGD.
GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0003700; F:DNA binding transcription factor activity; TAS:RGD.
GO; GO:0003690; F:double-stranded DNA binding; IDA:RGD.
GO; GO:0031072; F:heat shock protein binding; IPI:RGD.
GO; GO:0046982; F:protein heterodimerization activity; IDA:RGD.
GO; GO:0042803; F:protein homodimerization activity; IDA:RGD.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD.
GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; IDA:RGD.
GO; GO:1990416; P:cellular response to brain-derived neurotrophic factor stimulus; IDA:RGD.
GO; GO:0071322; P:cellular response to carbohydrate stimulus; IDA:RGD.
GO; GO:0071345; P:cellular response to cytokine stimulus; IDA:MGI.
GO; GO:1904630; P:cellular response to diterpene; IDA:RGD.
GO; GO:1904632; P:cellular response to glucoside; IDA:RGD.
GO; GO:0071347; P:cellular response to interleukin-1; IDA:RGD.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:RGD.
GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:MGI.
GO; GO:1901653; P:cellular response to peptide; IDA:RGD.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IDA:RGD.
GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IBA:GO_Central.
GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
GO; GO:0038061; P:NIK/NF-kappaB signaling; IBA:GO_Central.
GO; GO:0010628; P:positive regulation of gene expression; IMP:RGD.
GO; GO:2000637; P:positive regulation of gene silencing by miRNA; IMP:BHF-UCL.
GO; GO:1902895; P:positive regulation of pri-miRNA transcription by RNA polymerase II; IMP:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0009617; P:response to bacterium; IEP:RGD.
GO; GO:0046688; P:response to copper ion; IEP:RGD.
GO; GO:0014070; P:response to organic cyclic compound; IDA:RGD.
GO; GO:0006979; P:response to oxidative stress; IDA:RGD.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd00204; ANK; 2.
Gene3D; 1.25.40.20; -; 1.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
InterPro; IPR011029; DEATH-like_dom_sf.
InterPro; IPR000488; Death_domain.
InterPro; IPR030503; NF-kB_p105.
InterPro; IPR000451; NFkB/Dor.
PANTHER; PTHR24169; PTHR24169; 1.
PANTHER; PTHR24169:SF9; PTHR24169:SF9; 1.
Pfam; PF12796; Ank_2; 2.
Pfam; PF00531; Death; 1.
PRINTS; PR01415; ANKYRIN.
SMART; SM00248; ANK; 6.
SMART; SM00005; DEATH; 1.
SUPFAM; SSF47986; SSF47986; 1.
SUPFAM; SSF48403; SSF48403; 1.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 4.
1: Evidence at protein level;
Activator; ANK repeat; Complete proteome; Cytoplasm; DNA-binding;
Hydroxylation; Nucleus; Phosphoprotein; Reference proteome; Repeat;
Transcription; Transcription regulation.
CHAIN <1 522 Nuclear factor NF-kappa-B p105 subunit.
/FTId=PRO_0000030314.
CHAIN <1 32 Nuclear factor NF-kappa-B p50 subunit.
{ECO:0000250}.
/FTId=PRO_0000030315.
REPEAT 89 119 ANK 1.
REPEAT 128 157 ANK 2.
REPEAT 161 190 ANK 3.
REPEAT 197 226 ANK 4.
REPEAT 231 260 ANK 5.
REPEAT 265 294 ANK 6.
REPEAT 318 348 ANK 7.
DOMAIN 352 439 Death.
REGION 197 231 Essential for interaction with HIF1AN.
{ECO:0000250}.
MOD_RES 225 225 (3S)-3-hydroxyasparagine; by HIF1AN.
{ECO:0000250}.
MOD_RES 306 306 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 447 447 Phosphoserine.
{ECO:0000250|UniProtKB:P19838}.
MOD_RES 461 461 Phosphoserine; by GSK3-beta; in vitro.
{ECO:0000250|UniProtKB:P19838}.
MOD_RES 481 481 Phosphoserine; by IKKB.
{ECO:0000250|UniProtKB:P19838}.
MOD_RES 486 486 Phosphoserine; by IKKB.
{ECO:0000250|UniProtKB:P19838}.
MOD_RES 491 491 Phosphoserine.
{ECO:0000250|UniProtKB:P19838}.
MOD_RES 497 497 Phosphothreonine.
{ECO:0000250|UniProtKB:P25799}.
NON_TER 1 1
SEQUENCE 522 AA; 56554 MW; 12D89EE61E3163E2 CRC64;
REILNPPEKE TQGEGPSLFM ASTKTEAIAP ASTMEDKEED VGFQDNLFLE KALQLAKRHA
NALFDYAVTG DVKMLLAVQR HLTAVQDENG DSVLHLAIIH LHAQLVRDLL EVTSGSISDD
IINMRNDLYQ TPLHLAVITK QEDVVEDLLR VGADLSLLDR WGNSVLHLAA KEGHDKILGV
LLKNSKAALL INHPNGEGLN AIHIAVMSNS LSCLQLLVAA GAEVNAQEQK SGRTALHLAV
EYDNISLAGC LLLEGDALVD STTYDGTTPL HIAAGRGSTR LAALLKAAGA DPLVENFEPL
YDLDDSWEKA GEDEGVVPGT TPLDMAANWQ VFDILNGKPY EPVFTSDDIL PQGDIKQLTE
DTRLQLCKLL EIPDPDKNWA TLAQKLGLGI LNNAFRLSPA PSKTLMDNYE VSGGTIKELV
EALRQMGYTE AIEVIQAAFR TPETTASSPV TTAQAHLLPL SSSSTRQHID ELRDNDSVCD
SGVETSFRKL SFSESLTGDG PLLSLNKMPH NYGQDGPIEG KI


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