ID NFKB1_RAT Reviewed; 973 AA. AC Q63369; F1LQH2; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 28-JUN-2023, sequence version 2. DT 27-MAR-2024, entry version 180. DE RecName: Full=Nuclear factor NF-kappa-B p105 subunit; DE AltName: Full=DNA-binding factor KBF1; DE AltName: Full=EBP-1; DE AltName: Full=Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1; DE Contains: DE RecName: Full=Nuclear factor NF-kappa-B p50 subunit; GN Name=Nfkb1; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Brown Norway; RX PubMed=15057822; DOI=10.1038/nature02426; RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., RA Mockrin S., Collins F.S.; RT "Genome sequence of the Brown Norway rat yields insights into mammalian RT evolution."; RL Nature 428:493-521(2004). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 452-973. RC STRAIN=Sprague-Dawley; TISSUE=Testis; RX PubMed=8161377; DOI=10.1210/endo.134.3.8161377; RA Hamil K.G., Hall S.H.; RT "Cloning of rat Sertoli cell follicle-stimulating hormone primary response RT complementary deoxyribonucleic acid: regulation of TSC-22 gene RT expression."; RL Endocrinology 134:1205-1212(1994). RN [3] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-757, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22673903; DOI=10.1038/ncomms1871; RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., RA Olsen J.V.; RT "Quantitative maps of protein phosphorylation sites across 14 different rat RT organs and tissues."; RL Nat. Commun. 3:876-876(2012). CC -!- FUNCTION: NF-kappa-B is a pleiotropic transcription factor present in CC almost all cell types and is the endpoint of a series of signal CC transduction events that are initiated by a vast array of stimuli CC related to many biological processes such as inflammation, immunity, CC differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B CC is a homo- or heterodimeric complex formed by the Rel-like domain- CC containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and CC NFKB2/p52 and the heterodimeric p65-p50 complex appears to be most CC abundant one. The dimers bind at kappa-B sites in the DNA of their CC target genes and the individual dimers have distinct preferences for CC different kappa-B sites that they can bind with distinguishable CC affinity and specificity. Different dimer combinations act as CC transcriptional activators or repressors, respectively. NF-kappa-B is CC controlled by various mechanisms of post-translational modification and CC subcellular compartmentalization as well as by interactions with other CC cofactors or corepressors. NF-kappa-B complexes are held in the CC cytoplasm in an inactive state complexed with members of the NF-kappa-B CC inhibitor (I-kappa-B) family. In a conventional activation pathway, I- CC kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to CC different activators, subsequently degraded thus liberating the active CC NF-kappa-B complex which translocates to the nucleus. NF-kappa-B CC heterodimeric p65-p50 and RelB-p50 complexes are transcriptional CC activators. The NF-kappa-B p50-p50 homodimer is a transcriptional CC repressor, but can act as a transcriptional activator when associated CC with BCL3. NFKB1 appears to have dual functions such as cytoplasmic CC retention of attached NF-kappa-B proteins by p105 and generation of p50 CC by a cotranslational processing. The proteasome-mediated process CC ensures the production of both p50 and p105 and preserves their CC independent function, although processing of NFKB1/p105 also appears to CC occur post-translationally. p50 binds to the kappa-B consensus sequence CC 5'-GGRNNYYCC-3', located in the enhancer region of genes involved in CC immune response and acute phase reactions. In a complex with MAP3K8, CC NFKB1/p105 represses MAP3K8-induced MAPK signaling; active MAP3K8 is CC released by proteasome-dependent degradation of NFKB1/p105. CC {ECO:0000250|UniProtKB:P19838}. CC -!- FUNCTION: [Nuclear factor NF-kappa-B p105 subunit]: P105 is the CC precursor of the active p50 subunit (Nuclear factor NF-kappa-B p50 CC subunit) of the nuclear factor NF-kappa-B. Acts as a cytoplasmic CC retention of attached NF-kappa-B proteins by p105. CC {ECO:0000250|UniProtKB:P19838}. CC -!- FUNCTION: [Nuclear factor NF-kappa-B p50 subunit]: Constitutes the CC active form, which associates with RELA/p65 to form the NF-kappa-B p65- CC p50 complex to form a transcription factor. Together with RELA/p65, CC binds to the kappa-B consensus sequence 5'-GGRNNYYCC-3', located in the CC enhancer region of genes involved in immune response and acute phase CC reactions. {ECO:0000250|UniProtKB:P19838}. CC -!- SUBUNIT: Component of the NF-kappa-B p65-p50 complex (By similarity). CC Homodimer; component of the NF-kappa-B p50-p50 complex (By similarity). CC Component of the NF-kappa-B p105-p50 complex (By similarity). Component CC of the NF-kappa-B p50-c-Rel complex (By similarity). Component of a CC complex consisting of the NF-kappa-B p50-p50 homodimer and BCL3 (By CC similarity). Also interacts with MAP3K8 (By similarity). NF-kappa-B p50 CC subunit interacts with NCOA3 coactivator, which may coactivate NF- CC kappa-B dependent expression via its histone acetyltransferase activity CC (By similarity). Interacts with TSC22D3; this interaction prevents CC nuclear translocation and DNA-binding (By similarity). Interacts with CC SPAG9 and UNC5CL (By similarity). NFKB1/p105 interacts with CFLAR; the CC interaction inhibits p105 processing into p50 (By similarity). CC NFKB1/p105 forms a ternary complex with MAP3K8 and TNIP2 (By CC similarity). Interacts with GSK3B; the interaction prevents processing CC of p105 to p50 (By similarity). NFKB1/p50 interacts with NFKBIE (By CC similarity). NFKB1/p50 interacts with NFKBIZ. Nuclear factor NF-kappa-B CC p50 subunit interacts with NFKBID (By similarity). Directly interacts CC with MEN1 (By similarity). Interacts with HIF1AN (By similarity). CC Interacts with FEM1A; interaction is direct (By similarity). CC {ECO:0000250|UniProtKB:P19838, ECO:0000250|UniProtKB:P25799}. CC -!- INTERACTION: CC Q63369; P47196: Akt1; NbExp=9; IntAct=EBI-8498561, EBI-7204362; CC Q63369; Q99N34: Dffb; NbExp=2; IntAct=EBI-8498561, EBI-8498730; CC -!- SUBCELLULAR LOCATION: [Nuclear factor NF-kappa-B p105 subunit]: CC Cytoplasm {ECO:0000250|UniProtKB:P19838}. CC -!- SUBCELLULAR LOCATION: [Nuclear factor NF-kappa-B p50 subunit]: Nucleus CC {ECO:0000250|UniProtKB:P19838}. Cytoplasm CC {ECO:0000250|UniProtKB:P19838}. Note=Association with NFKBIA inhibitor CC (I-kappa-B), promotes its retention in the cytoplasm in an inactive CC form. Translocates into the nucleus following NFKBIA degradation. CC {ECO:0000250|UniProtKB:P19838}. CC -!- DOMAIN: The C-terminus of p105 might be involved in cytoplasmic CC retention, inhibition of DNA-binding, and transcription activation. CC {ECO:0000250|UniProtKB:P19838}. CC -!- DOMAIN: Glycine-rich region (GRR) is a critical element in the CC generation of p50 (Nuclear factor NF-kappa-B p50 subunit) by acting as CC a proteasomal 'stop signal', which leads to limited proteasomal CC degradation of the C-terminus, while generating p50. CC {ECO:0000250|UniProtKB:P19838}. CC -!- PTM: Generation of the NF-kappa-B p50 (Nuclear factor NF-kappa-B p50 CC subunit) transcription factor takes place both cotranslationally and CC post-translationally via non-mutually exclusive mechanisms. A CC cotranslational processing allows the production of both p50 and p105 CC (Nuclear factor NF-kappa-B p105 subunit) from a single NFKB1 mRNA. CC While translation occurs, the particular unfolded structure after the CC GRR repeat region acts as a substrate for the proteasome, promoting CC degradation of the C-terminus. The GRR acts as a proteasomal 'stop CC signal', protecting the region upstream of the GRR from degradation and CC promoting generation of p50. It is unclear if limited proteasome CC degradation during cotranslational processing depends on CC ubiquitination. NF-kappa-B p50 is also generated post-translationally CC following ubiquitination by the KPC complex, leading to limited CC processing by the proteasome downstream of the GRR region, thereby CC generating p50. {ECO:0000250|UniProtKB:P19838}. CC -!- PTM: [Nuclear factor NF-kappa-B p105 subunit]: Phosphorylation at the CC C-terminus by IKBKB/IKKB acts as a signal for ubiquitination and CC promotes either complete degradation or processing to generate the NF- CC kappa-B p50 (Nuclear factor NF-kappa-B p50 subunit) (By similarity). CC Phosphorylation at Ser-912 primes p105 for proteolytic processing in CC response to TNF-alpha stimulation (By similarity). Phosphorylation at CC Ser-928, Ser-932 and Ser-937 are required for BTRC/BTRCP-mediated CC ubiquitination and proteolysis (By similarity). Phosphorylation at Ser- CC 932 is also required for ubiquitination by the KPC complex and limited CC processing to generate NF-kappa-B p50 (Nuclear factor NF-kappa-B p50 CC subunit) (By similarity). {ECO:0000250|UniProtKB:P19838}. CC -!- PTM: [Nuclear factor NF-kappa-B p105 subunit]: Polyubiquitinated at CC multiple Lys residues in the C-terminus. Polyubiquitinated by the CC SCF(FBXW11) and SCF(BTRC) complexes following phosphorylation at Ser- CC 928, Ser-932 and Ser-937, leading to its complete degradation. In CC contrast, polyubiquitination by the KPC complex following CC phosphorylation at Ser-932 leads to limited proteosomal processing and CC generation of the active NF-kappa-B p50 (Nuclear factor NF-kappa-B p50 CC subunit). {ECO:0000250|UniProtKB:P19838}. CC -!- PTM: S-nitrosylation of Cys-60 affects DNA binding. CC {ECO:0000250|UniProtKB:P19838}. CC -!- PTM: The covalent modification of cysteine by 15-deoxy-Delta12,14- CC prostaglandin-J2 is autocatalytic and reversible. It may occur as an CC alternative to other cysteine modifications, such as S-nitrosylation CC and S-palmitoylation. {ECO:0000250|UniProtKB:P19838}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L26267; AAA20684.1; -; mRNA. DR PIR; I67414; I67414. DR RefSeq; XP_006233420.1; XM_006233358.3. DR AlphaFoldDB; Q63369; -. DR SMR; Q63369; -. DR CORUM; Q63369; -. DR IntAct; Q63369; 11. DR MINT; Q63369; -. DR STRING; 10116.ENSRNOP00000028944; -. DR iPTMnet; Q63369; -. DR PhosphoSitePlus; Q63369; -. DR PaxDb; 10116-ENSRNOP00000028944; -. DR PeptideAtlas; Q63369; -. DR AGR; RGD:70498; -. DR CTD; 4790; -. DR RGD; 70498; Nfkb1. DR VEuPathDB; HostDB:ENSRNOG00000023258; -. DR eggNOG; KOG0504; Eukaryota. DR HOGENOM; CLU_004343_1_0_1; -. DR InParanoid; Q63369; -. DR OrthoDB; 1059550at2759; -. DR TreeFam; TF325632; -. DR Proteomes; UP000002494; Chromosome 2. DR Bgee; ENSRNOG00000023258; Expressed in spleen and 19 other cell types or tissues. DR GO; GO:0000785; C:chromatin; ISO:RGD. DR GO; GO:0005737; C:cytoplasm; ISO:RGD. DR GO; GO:0005829; C:cytosol; ISO:RGD. DR GO; GO:0035525; C:NF-kappaB p50/p65 complex; ISO:RGD. DR GO; GO:0005634; C:nucleus; ISO:RGD. DR GO; GO:0032991; C:protein-containing complex; IDA:RGD. DR GO; GO:0005667; C:transcription regulator complex; ISO:RGD. DR GO; GO:0042805; F:actinin binding; ISO:RGD. DR GO; GO:0003682; F:chromatin binding; ISO:RGD. DR GO; GO:0003677; F:DNA binding; IDA:MGI. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD. DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:RGD. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISO:RGD. DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:RGD. DR GO; GO:0003690; F:double-stranded DNA binding; IDA:RGD. DR GO; GO:0031072; F:heat shock protein binding; IPI:RGD. DR GO; GO:0042802; F:identical protein binding; IPI:RGD. DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD. DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:RGD. DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD. DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:RGD. DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:RGD. DR GO; GO:0003712; F:transcription coregulator activity; ISO:RGD. DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW. DR GO; GO:0050853; P:B cell receptor signaling pathway; ISO:RGD. DR GO; GO:0007249; P:canonical NF-kappaB signal transduction; ISO:RGD. DR GO; GO:1904385; P:cellular response to angiotensin; ISO:RGD. DR GO; GO:1990416; P:cellular response to brain-derived neurotrophic factor stimulus; IDA:RGD. DR GO; GO:0071322; P:cellular response to carbohydrate stimulus; IDA:RGD. DR GO; GO:0071345; P:cellular response to cytokine stimulus; IDA:MGI. DR GO; GO:1904630; P:cellular response to diterpene; IDA:RGD. DR GO; GO:0071359; P:cellular response to dsRNA; ISO:RGD. DR GO; GO:1904632; P:cellular response to glucoside; IDA:RGD. DR GO; GO:0071347; P:cellular response to interleukin-1; IDA:RGD. DR GO; GO:0097398; P:cellular response to interleukin-17; ISO:RGD. DR GO; GO:0071354; P:cellular response to interleukin-6; ISO:RGD. DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:RGD. DR GO; GO:0071260; P:cellular response to mechanical stimulus; ISO:RGD. DR GO; GO:0071316; P:cellular response to nicotine; ISO:RGD. DR GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:MGI. DR GO; GO:1901653; P:cellular response to peptide; IDA:RGD. DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IDA:RGD. DR GO; GO:0098586; P:cellular response to virus; ISO:RGD. DR GO; GO:0010467; P:gene expression; ISO:RGD. DR GO; GO:0007254; P:JNK cascade; ISO:RGD. DR GO; GO:0002523; P:leukocyte migration involved in inflammatory response; IEP:RGD. DR GO; GO:0060056; P:mammary gland involution; ISO:RGD. DR GO; GO:0000165; P:MAPK cascade; ISO:RGD. DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD. DR GO; GO:0001818; P:negative regulation of cytokine production; ISO:RGD. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISO:RGD. DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD. DR GO; GO:0050728; P:negative regulation of inflammatory response; ISO:RGD. DR GO; GO:0032695; P:negative regulation of interleukin-12 production; ISO:RGD. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD. DR GO; GO:0038061; P:non-canonical NF-kappaB signal transduction; ISO:RGD. DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISO:RGD. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS:UniProtKB. DR GO; GO:0010628; P:positive regulation of gene expression; IMP:RGD. DR GO; GO:1900127; P:positive regulation of hyaluronan biosynthetic process; ISO:RGD. DR GO; GO:2000630; P:positive regulation of miRNA metabolic process; ISO:RGD. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD. DR GO; GO:0060261; P:positive regulation of transcription initiation by RNA polymerase II; ISO:RGD. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD. DR GO; GO:0009617; P:response to bacterium; IEP:RGD. DR GO; GO:0046688; P:response to copper ion; IEP:RGD. DR GO; GO:0045471; P:response to ethanol; IEP:RGD. DR GO; GO:0035994; P:response to muscle stretch; ISO:RGD. DR GO; GO:0014070; P:response to organic cyclic compound; IDA:RGD. DR GO; GO:0006979; P:response to oxidative stress; IDA:RGD. DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD. DR CDD; cd08797; Death_NFkB1_p105; 1. DR CDD; cd01177; IPT_NFkappaB; 1. DR CDD; cd07935; RHD-n_NFkB1; 1. DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1. DR Gene3D; 1.10.533.10; Death Domain, Fas; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 1. DR Gene3D; 2.60.40.340; Rel homology domain (RHD), DNA-binding domain; 1. DR InterPro; IPR002110; Ankyrin_rpt. DR InterPro; IPR036770; Ankyrin_rpt-contain_sf. DR InterPro; IPR011029; DEATH-like_dom_sf. DR InterPro; IPR000488; Death_domain. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR014756; Ig_E-set. DR InterPro; IPR002909; IPT_dom. DR InterPro; IPR033926; IPT_NFkappaB. DR InterPro; IPR047096; NF-kB_p105_DD. DR InterPro; IPR030503; NF-kB_p105_RHD_N. DR InterPro; IPR000451; NFkB/Dor. DR InterPro; IPR008967; p53-like_TF_DNA-bd_sf. DR InterPro; IPR030492; RHD_CS. DR InterPro; IPR032397; RHD_dimer. DR InterPro; IPR011539; RHD_DNA_bind_dom. DR InterPro; IPR037059; RHD_DNA_bind_dom_sf. DR PANTHER; PTHR24169:SF9; NUCLEAR FACTOR NF-KAPPA-B P105 SUBUNIT; 1. DR PANTHER; PTHR24169; NUCLEAR FACTOR NF-KAPPA-B PROTEIN; 1. DR Pfam; PF00023; Ank; 2. DR Pfam; PF12796; Ank_2; 1. DR Pfam; PF00531; Death; 1. DR Pfam; PF16179; RHD_dimer; 1. DR Pfam; PF00554; RHD_DNA_bind; 1. DR PRINTS; PR01415; ANKYRIN. DR PRINTS; PR00057; NFKBTNSCPFCT. DR SMART; SM00248; ANK; 6. DR SMART; SM00005; DEATH; 1. DR SMART; SM00429; IPT; 1. DR SUPFAM; SSF48403; Ankyrin repeat; 1. DR SUPFAM; SSF47986; DEATH domain; 1. DR SUPFAM; SSF81296; E set domains; 1. DR SUPFAM; SSF49417; p53-like transcription factors; 1. DR PROSITE; PS50297; ANK_REP_REGION; 1. DR PROSITE; PS50088; ANK_REPEAT; 4. DR PROSITE; PS01204; REL_1; 1. DR PROSITE; PS50254; REL_2; 1. PE 1: Evidence at protein level; KW Acetylation; Activator; ANK repeat; Apoptosis; Cytoplasm; DNA-binding; KW Hydroxylation; Isopeptide bond; Lipoprotein; Nucleus; Phosphoprotein; KW Reference proteome; Repeat; S-nitrosylation; Transcription; KW Transcription regulation; Ubl conjugation. FT CHAIN 1..973 FT /note="Nuclear factor NF-kappa-B p105 subunit" FT /id="PRO_0000030314" FT CHAIN 1..483 FT /note="Nuclear factor NF-kappa-B p50 subunit" FT /evidence="ECO:0000250|UniProtKB:P19838" FT /id="PRO_0000030315" FT DOMAIN 38..245 FT /note="RHD" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00265" FT REPEAT 540..570 FT /note="ANK 1" FT REPEAT 579..608 FT /note="ANK 2" FT REPEAT 612..641 FT /note="ANK 3" FT REPEAT 648..677 FT /note="ANK 4" FT REPEAT 682..711 FT /note="ANK 5" FT REPEAT 716..745 FT /note="ANK 6" FT REPEAT 769..799 FT /note="ANK 7" FT DOMAIN 803..890 FT /note="Death" FT REGION 371..394 FT /note="GRR" FT /evidence="ECO:0000250|UniProtKB:P19838" FT REGION 434..467 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 435..973 FT /note="Interaction with CFLAR" FT /evidence="ECO:0000250|UniProtKB:P19838" FT REGION 648..682 FT /note="Essential for interaction with HIF1AN" FT /evidence="ECO:0000250|UniProtKB:P19838" FT MOTIF 359..364 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255" FT COMPBIAS 438..459 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 433..434 FT /note="Cleavage (when cotranslationally processed)" FT /evidence="ECO:0000250|UniProtKB:P19838" FT MOD_RES 60 FT /note="S-nitrosocysteine; alternate" FT /evidence="ECO:0000250|UniProtKB:P19838" FT MOD_RES 336 FT /note="Phosphoserine" FT /evidence="ECO:0000255" FT MOD_RES 440 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P19838" FT MOD_RES 449 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P25799" FT MOD_RES 676 FT /note="(3S)-3-hydroxyasparagine; by HIF1AN" FT /evidence="ECO:0000250|UniProtKB:P19838" FT MOD_RES 757 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 898 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P19838" FT MOD_RES 912 FT /note="Phosphoserine; by GSK3-beta; in vitro" FT /evidence="ECO:0000250|UniProtKB:P19838" FT MOD_RES 928 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P19838" FT MOD_RES 932 FT /note="Phosphoserine; by IKKB" FT /evidence="ECO:0000250|UniProtKB:P19838" FT MOD_RES 937 FT /note="Phosphoserine; by IKKB" FT /evidence="ECO:0000250|UniProtKB:P19838" FT MOD_RES 942 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P19838" FT MOD_RES 948 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P25799" FT LIPID 60 FT /note="S-(15-deoxy-Delta12,14-prostaglandin J2-9- FT yl)cysteine; alternate" FT /evidence="ECO:0000250|UniProtKB:P19838" FT CROSSLNK 324 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P19838" SQ SEQUENCE 973 AA; 105704 MW; D88ECEA20A389AB7 CRC64; MADDDPFGTG QMFHLNTALT HSIFNAELYS TDIPLSTADG PYLQILEQPK QRGFRFRYVC EGPSHGGLPG ASSEKNKKSY PQVKICNYVG PAKVIVQLVT NGKNIHLHAH SLVGKHCEDG ICTVTAGPKD MVVGFANLGI LHVTKKKVFE TLEARMTEAC IRGYNPGLLV HSDLAYLQAE GGGDRQLTDR EKEIIRQAAL QQTKEMDLSV VRLMFTAFLP DSTGSFTRRL EPVVSDAIYD SKAPNASNLK IVRMDRTAGC VTGGEEIYLL CDKVQKDDIQ IRFYEEEENG GVWEGFGDFS PTDVHRQFAI VFKTPKYKDV NITKPASVFV QLRRKSDLET SEPKPFLYYP EIKDKEEVQR KRQKLMPNFS DSFGGGSGAG AGGGGMFGSG GGGGGSTGSP GPGYGFPHYG FPAYGGIAFH PGATKSNTGI THGTINTKFK NEPRDCAKSD DREILNPPEK ETQGEGPSLF MASTKTEAIA PASTMEDKEE DVGFQDNLFL EKALQLAKRH ANALFDYAVT GDVKMLLAVQ RHLTAVQDEN GDSVLHLAII HLHAQLVRDL LEVTSGSISD DIINMRNDLY QTPLHLAVIT KQEDVVEDLL RVGADLSLLD RWGNSVLHLA AKEGHDKILG VLLKNSKAAL LINHPNGEGL NAIHIAVMSN SLSCLQLLVA AGAEVNAQEQ KSGRTALHLA VEYDNISLAG CLLLEGDALV DSTTYDGTTP LHIAAGRGST RLAALLKAAG ADPLVENFEP LYDLDDSWEK AGEDEGVVPG TTPLDMAANW QVFDILNGKP YEPVFTSDDI LPQGDIKQLT EDTRLQLCKL LEIPDPDKNW ATLAQKLGLG ILNNAFRLSP APSKTLMDNY EVSGGTIKEL VEALRQMGYT EAIEVIQAAF RTPETTASSP VTTAQAHLLP LSSSSTRQHI DELRDNDSVC DSGVETSFRK LSFSESLTGD GPLLSLNKMP HNYGQDGPIE GKI //