ID NFKB1_MOUSE Reviewed; 971 AA. AC P25799; B2RRQ6; Q3TZE8; Q3V2V6; Q6TDG8; Q75ZL1; Q80Y21; Q8C712; DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 27-MAR-2024, entry version 239. 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=NF-kappa-B1 p84/NF-kappa-B1 p98; 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 Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION. RC TISSUE=Lung, and Spleen; RX PubMed=2203532; DOI=10.1016/0092-8674(90)90276-k; RA Ghosh S., Gifford A.M., Riviere L.R., Tempst P., Nolan G.P., Baltimore D.; RT "Cloning of the p50 DNA binding subunit of NF-kappa B: homology to rel and RT dorsal."; RL Cell 62:1019-1029(1990). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), AND SUBCELLULAR LOCATION. RX PubMed=1339305; DOI=10.1016/0092-8674(92)90082-n; RA Inoue J., Kerr L.D., Kakizuka A., Verma I.M.; RT "I kappa B gamma, a 70 kd protein identical to the C-terminal half of p110 RT NF-kappa B: a new member of the I kappa B family."; RL Cell 68:1109-1120(1992). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), AND PARTIAL PROTEIN SEQUENCE. RX PubMed=8398903; RA Gerondakis S., Morrice N., Richardson I.B., Wettenhall R., Fecondo J., RA Grumont R.J.; RT "The activity of a 70 kilodalton I kappa B molecule identical to the RT carboxyl terminus of the p105 NF-kappa B precursor is modulated by protein RT kinase A."; RL Cell Growth Differ. 4:617-627(1993). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), AND FUNCTION. RX PubMed=7969179; DOI=10.1128/mcb.14.12.8460-8470.1994; RA Grumont R.J., Fecondo J., Gerondakis S.; RT "Alternate RNA splicing of murine nfkb1 generates a nuclear isoform of the RT p50 precursor NF-kappa B1 that can function as a transactivator of NF-kappa RT B-regulated transcription."; RL Mol. Cell. Biol. 14:8460-8470(1994). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC STRAIN=C57BL/6CrSlc; TISSUE=Spleen; RA Ohara O., Kitamura H., Nakagawa T.; RT "Mus musculus transcription factor NF-kappa-B DNA binding subunit(p105) RT mRNA, complete cds."; RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC STRAIN=C3H/HeJBir, and C57BL/6J; RA Bleich A., Hedrich H.J., Schlegelberger B., Maehler M.; RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4). RC TISSUE=Brain, and Embryo; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 54-129. RC STRAIN=C57BL/6J; TISSUE=Lung carcinoma; RA Gerhauser I., Ulrich R., Baumgartner W.; RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 65-971 (ISOFORM 4), AND RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 376-971 (ISOFORM 1). RC STRAIN=C57BL/6J, and NOD; TISSUE=Inner ear, Kidney, and Spleen; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [11] RP ALTERNATIVE SPLICING (ISOFORMS 6 AND 7), AND SUBCELLULAR LOCATION. RX PubMed=8183915; DOI=10.1073/pnas.91.10.4367; RA Grumont R.J., Gerondakis S.; RT "Alternative splicing of RNA transcripts encoded by the murine p105 NF- RT kappa B gene generates I kappa B gamma isoforms with different inhibitory RT activities."; RL Proc. Natl. Acad. Sci. U.S.A. 91:4367-4371(1994). RN [12] RP COTRANSLATIONAL FOLDING OF P105. RX PubMed=9529257; DOI=10.1016/s0092-8674(00)81409-9; RA Lin L., DeMartino G.N., Greene W.C.; RT "Cotranslational biogenesis of NF-kappaB p50 by the 26S proteasome."; RL Cell 92:819-828(1998). RN [13] RP INTERACTION WITH NFKBIZ. RX PubMed=11356851; DOI=10.1074/jbc.m103426200; RA Yamazaki S., Muta T., Takeshige K.; RT "A novel IkappaB protein, IkappaB-zeta, induced by proinflammatory stimuli, RT negatively regulates nuclear factor-kappaB in the nuclei."; RL J. Biol. Chem. 276:27657-27662(2001). RN [14] RP INTERACTION WITH NFKBID. RX PubMed=11931770; DOI=10.1016/s1097-2765(02)00469-0; RA Fiorini E., Schmitz I., Marissen W.E., Osborn S.L., Touma M., Sasada T., RA Reche P.A., Tibaldi E.V., Hussey R.E., Kruisbeek A.M., Reinherz E.L., RA Clayton L.K.; RT "Peptide-induced negative selection of thymocytes activates transcription RT of an NF-kappa B inhibitor."; RL Mol. Cell 9:637-648(2002). RN [15] RP IDENTIFICATION IN THE NF-KAPPA-B P65-P50 COMPLEX. RX PubMed=15051764; DOI=10.1084/jem.20031272; RA Goriely S., Van Lint C., Dadkhah R., Libin M., De Wit D., Demonte D., RA Willems F., Goldman M.; RT "A defect in nucleosome remodeling prevents IL-12(p35) gene transcription RT in neonatal dendritic cells."; RL J. Exp. Med. 199:1011-1016(2004). RN [16] RP INTERACTION WITH NFKBIZ. RX PubMed=15241416; DOI=10.1038/nature02738; RA Yamamoto M., Yamazaki S., Uematsu S., Sato S., Hemmi H., Hoshino K., RA Kaisho T., Kuwata H., Takeuchi O., Takeshige K., Saitoh T., Yamaoka S., RA Yamamoto N., Yamamoto S., Muta T., Takeda K., Akira S.; RT "Regulation of Toll/IL-1-receptor-mediated gene expression by the inducible RT nuclear protein IkappaBzeta."; RL Nature 430:218-222(2004). RN [17] RP FUNCTION, AND INTERACTION WITH FEM1AA. RX PubMed=18270204; DOI=10.1074/jbc.m709663200; RA Minami M., Shimizu K., Okamoto Y., Folco E., Ilasaca M.L., Feinberg M.W., RA Aikawa M., Libby P.; RT "Prostaglandin E receptor type 4-associated protein interacts directly with RT NF-kappaB1 and attenuates macrophage activation."; RL J. Biol. Chem. 283:9692-9703(2008). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-447; SER-940 AND THR-946, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, and RC Spleen; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [19] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 39-364, AND FUNCTION. RX PubMed=7530332; DOI=10.1038/373303a0; RA Ghosh G., van Duyne G., Ghosh S., Sigler P.B.; RT "Structure of NF-kappa B p50 homodimer bound to a kappa B site."; RL Nature 373:303-310(1995). RN [20] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 245-350, AND FUNCTION. RX PubMed=9384558; DOI=10.1016/s0969-2126(97)00293-1; RA Huang D.B., Huxford T., Chen Y.Q., Ghosh G.; RT "The role of DNA in the mechanism of NFkappaB dimer formation: crystal RT structures of the dimerization domains of the p50 and p65 subunits."; RL Structure 5:1427-1436(1997). RN [21] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 245-363, AND SUBCELLULAR LOCATION. RX PubMed=9865694; DOI=10.1016/s0092-8674(00)81699-2; RA Huxford T., Huang D.B., Malek S., Ghosh G.; RT "The crystal structure of the IkappaBalpha/NF-kappaB complex reveals RT mechanisms of NF-kappaB inactivation."; RL Cell 95:759-770(1998). RN [22] RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 39-350, AND FUNCTION. RX PubMed=9450761; DOI=10.1038/34956; RA Chen F.E., Huang D.B., Chen Y.Q., Ghosh G.; RT "Crystal structure of p50/p65 heterodimer of transcription factor NF-kappaB RT bound to DNA."; RL Nature 391:410-413(1998). RN [23] RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 39-350, AND FUNCTION. RX PubMed=11970948; DOI=10.1074/jbc.m200006200; RA Berkowitz B., Huang D.B., Chen-Park F.E., Sigler P.B., Ghosh G.; RT "The X-ray crystal structure of the NF-kappa B p50.p65 heterodimer bound to RT the interferon beta -kappa B site."; RL J. Biol. Chem. 277:24694-24700(2002). RN [24] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 39-350. RX PubMed=11970949; DOI=10.1074/jbc.m200007200; RA Chen-Park F.E., Huang D.B., Noro B., Thanos D., Ghosh G.; RT "The kappa B DNA sequence from the HIV long terminal repeat functions as an RT allosteric regulator of HIV transcription."; RL J. Biol. Chem. 277:24701-24708(2002). RN [25] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 38-351 HOMODIMER COMPLEXED WITH RP RNA APTAMER. RX PubMed=12886018; DOI=10.1073/pnas.1632011100; RA Huang D.B., Vu D., Cassiday L.A., Zimmerman J.M., Maher L.J. III, Ghosh G.; RT "Crystal structure of NF-kappaB (p50)2 complexed to a high-affinity RNA RT aptamer."; RL Proc. Natl. Acad. Sci. U.S.A. 100:9268-9273(2003). RN [26] RP X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF 91-378 IN COMPLEX WITH RELB. RX PubMed=17869269; DOI=10.1016/j.jmb.2007.08.039; RA Moorthy A.K., Huang D.B., Wang V.Y., Vu D., Ghosh G.; RT "X-ray structure of a NF-kappaB p50/RelB/DNA complex reveals assembly of RT multiple dimers on tandem kappaB sites."; RL J. Mol. Biol. 373:723-734(2007). 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. Plays a role in the CC regulation of apoptosis. In a complex with MAP3K8, NFKB1/p105 represses CC MAP3K8-induced MAPK signaling; active MAP3K8 is released by proteasome- CC dependent degradation of NFKB1/p105. {ECO:0000269|PubMed:11970948, CC ECO:0000269|PubMed:18270204, ECO:0000269|PubMed:2203532, CC ECO:0000269|PubMed:7530332, ECO:0000269|PubMed:9384558, CC ECO:0000269|PubMed:9450761}. 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 -!- FUNCTION: [Isoform 3]: Isoform 3 (p98) (but not p84 or p105) acts as a CC transactivator of NF-kappa-B-regulated gene expression. CC {ECO:0000269|PubMed:7969179}. CC -!- FUNCTION: [Isoform 5]: Act as inhibitors of transactivation of p50 NF- CC kappa-B subunit, probably by sequestering it in the cytoplasm. CC {ECO:0000269|PubMed:1339305}. CC -!- FUNCTION: [Isoform 6]: Act as inhibitors of transactivation of p50 NF- CC kappa-B subunit, probably by sequestering it in the cytoplasm. CC {ECO:0000269|PubMed:8183915}. CC -!- FUNCTION: [Isoform 7]: Act as inhibitors of transactivation of p50 NF- CC kappa-B subunit, probably by sequestering it in the cytoplasm. CC {ECO:0000269|PubMed:8183915}. 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 (PubMed:11356851, CC PubMed:15241416). Nuclear factor NF-kappa-B p50 subunit interacts with CC NFKBID (PubMed:11931770). Directly interacts with MEN1 (By similarity). CC Interacts with HIF1AN (By similarity). Interacts with FEM1AA; CC interaction is direct (PubMed:18270204). {ECO:0000250|UniProtKB:P19838, CC ECO:0000269|PubMed:11356851, ECO:0000269|PubMed:11931770, CC ECO:0000269|PubMed:15241416, ECO:0000269|PubMed:18270204}. CC -!- INTERACTION: CC P25799; Q9DBR0: Akap8; NbExp=4; IntAct=EBI-643958, EBI-4285802; CC P25799; O09106: Hdac1; NbExp=2; IntAct=EBI-643958, EBI-301912; CC P25799; Q04207: Rela; NbExp=6; IntAct=EBI-643958, EBI-644400; CC P25799; Q15788: NCOA1; Xeno; NbExp=2; IntAct=EBI-643958, EBI-455189; CC P25799-1; Q04207: Rela; NbExp=6; IntAct=EBI-643974, EBI-644400; CC PRO_0000030312; Q04207: Rela; NbExp=3; IntAct=EBI-1209193, EBI-644400; CC PRO_0000030313; Q3V096: Ankrd42; NbExp=3; IntAct=EBI-1209141, EBI-15861272; CC PRO_0000030313; Q04863: Relb; NbExp=2; IntAct=EBI-1209141, EBI-1209145; 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:0000269|PubMed:9865694}. Cytoplasm {ECO:0000269|PubMed:9865694}. CC Note=Association with NFKBIA inhibitor (I-kappa-B), promotes its CC retention in the cytoplasm in an inactive form. Translocates into the CC nucleus following NFKBIA degradation. {ECO:0000269|PubMed:9865694}. CC -!- SUBCELLULAR LOCATION: [Isoform 5]: Cytoplasm CC {ECO:0000269|PubMed:1339305}. CC -!- SUBCELLULAR LOCATION: [Isoform 6]: Nucleus CC {ECO:0000269|PubMed:8183915}. Cytoplasm {ECO:0000269|PubMed:8183915}. CC -!- SUBCELLULAR LOCATION: [Isoform 7]: Nucleus CC {ECO:0000269|PubMed:8183915}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=7; CC Name=1; Synonyms=p105; CC IsoId=P25799-1; Sequence=Displayed; CC Name=2; Synonyms=p84; CC IsoId=P25799-2; Sequence=VSP_005583; CC Name=3; Synonyms=p98; CC IsoId=P25799-3; Sequence=VSP_005584; CC Name=4; CC IsoId=P25799-4; Sequence=VSP_017237, VSP_017238; CC Name=5; Synonyms=P70, I-kappa-B gamma; CC IsoId=P25799-5; Sequence=VSP_017236; CC Name=6; Synonyms=p63, I-kappa-B gamma-1; CC IsoId=P25799-6; Sequence=VSP_017236, VSP_005584; CC Name=7; Synonyms=p55, I-kappa-B gamma-2; CC IsoId=P25799-7; Sequence=VSP_017236, VSP_005583; CC -!- INDUCTION: By phorbol ester and TNF-alpha. 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 (By CC similarity). A cotranslational processing allows the production of both CC p50 and p105 (Nuclear factor NF-kappa-B p105 subunit) from a single CC NFKB1 mRNA (PubMed:9529257). While translation occurs, the particular CC unfolded structure after the GRR repeat region acts as a substrate for CC the proteasome, promoting degradation of the C-terminus CC (PubMed:9529257). The GRR acts as a proteasomal 'stop signal', CC protecting the region upstream of the GRR from degradation and CC promoting generation of p50 (PubMed:9529257). It is unclear if limited CC proteasome degradation during cotranslational processing depends on CC ubiquitination (PubMed:9529257). NF-kappa-B p50 is also generated post- CC translationally following ubiquitination by the KPC complex, leading to CC limited processing by the proteasome downstream of the GRR region, CC thereby generating p50 (By similarity). {ECO:0000250|UniProtKB:P19838, CC ECO:0000269|PubMed:9529257}. 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-910 primes p105 for proteolytic processing in CC response to TNF-alpha stimulation (By similarity). Phosphorylation at CC Ser-926, Ser-930 and Ser-935 are required for BTRC/BTRCP-mediated CC ubiquitination and proteolysis (By similarity). Phosphorylation at Ser- CC 930 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 (By similarity). CC Polyubiquitinated by the SCF(FBXW11) and SCF(BTRC) complexes following CC phosphorylation at Ser-926, Ser-930 and Ser-935, leading to its CC complete degradation (By similarity). In contrast, polyubiquitination CC by the KPC complex following phosphorylation at Ser-930 leads to CC limited proteosomal processing and generation of the active NF-kappa-B CC p50 (Nuclear factor NF-kappa-B p50 subunit) (By similarity). CC {ECO:0000250|UniProtKB:P19838}. CC -!- PTM: S-nitrosylation of Cys-59 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 -!- SEQUENCE CAUTION: CC Sequence=BAC35117.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; 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; M57999; AAA40415.1; -; mRNA. DR EMBL; S89033; AAB21851.1; -; mRNA. DR EMBL; S66656; AAB28573.1; -; mRNA. DR EMBL; AB119195; BAC84979.1; -; mRNA. DR EMBL; AY521462; AAS00547.1; -; mRNA. DR EMBL; AY521463; AAS00548.1; -; mRNA. DR EMBL; CH466532; EDL12143.1; -; Genomic_DNA. DR EMBL; BC050841; AAH50841.1; -; mRNA. DR EMBL; BC138535; AAI38536.1; -; mRNA. DR EMBL; BC138536; AAI38537.1; -; mRNA. DR EMBL; AY423849; AAR00341.1; -; mRNA. DR EMBL; AK052726; BAC35117.1; ALT_INIT; mRNA. DR EMBL; AK089660; BAE43399.1; -; mRNA. DR EMBL; AK157915; BAE34261.1; -; mRNA. DR CCDS; CCDS17858.1; -. [P25799-1] DR PIR; A35697; A35697. DR RefSeq; NP_032715.2; NM_008689.2. [P25799-1] DR RefSeq; XP_006501169.1; XM_006501106.2. DR PDB; 1BFS; X-ray; 2.20 A; A=245-350. DR PDB; 1IKN; X-ray; 2.30 A; C=245-363. DR PDB; 1LE5; X-ray; 2.75 A; B/F=39-350. DR PDB; 1LE9; X-ray; 3.00 A; B/F=39-350. DR PDB; 1LEI; X-ray; 2.70 A; B=39-350. DR PDB; 1NFK; X-ray; 2.30 A; A/B=39-363. DR PDB; 1OOA; X-ray; 2.45 A; A/B=39-363. DR PDB; 1U36; X-ray; 1.89 A; A=245-350. DR PDB; 1U3J; X-ray; 1.90 A; A=245-350. DR PDB; 1U3Y; X-ray; 1.90 A; A=245-350. DR PDB; 1U3Z; X-ray; 1.90 A; A=245-350. DR PDB; 1U41; X-ray; 2.20 A; A/B/C/D=245-350. DR PDB; 1U42; X-ray; 2.70 A; A=245-350. DR PDB; 1VKX; X-ray; 2.90 A; B=39-350. DR PDB; 2I9T; X-ray; 2.80 A; B=39-350. DR PDB; 2V2T; X-ray; 3.05 A; B=38-363. DR PDB; 3JV4; X-ray; 3.15 A; B/D/F=245-359. DR PDB; 8TKL; X-ray; 3.00 A; A/B=39-350. DR PDB; 8TKM; X-ray; 2.80 A; A/B=39-350. DR PDB; 8TKN; X-ray; 2.80 A; A/B=39-350. DR PDBsum; 1BFS; -. DR PDBsum; 1IKN; -. DR PDBsum; 1LE5; -. DR PDBsum; 1LE9; -. DR PDBsum; 1LEI; -. DR PDBsum; 1NFK; -. DR PDBsum; 1OOA; -. DR PDBsum; 1U36; -. DR PDBsum; 1U3J; -. DR PDBsum; 1U3Y; -. DR PDBsum; 1U3Z; -. DR PDBsum; 1U41; -. DR PDBsum; 1U42; -. DR PDBsum; 1VKX; -. DR PDBsum; 2I9T; -. DR PDBsum; 2V2T; -. DR PDBsum; 3JV4; -. DR PDBsum; 8TKL; -. DR PDBsum; 8TKM; -. DR PDBsum; 8TKN; -. DR AlphaFoldDB; P25799; -. DR SASBDB; P25799; -. DR SMR; P25799; -. DR BioGRID; 201751; 15. DR CORUM; P25799; -. DR DIP; DIP-85N; -. DR IntAct; P25799; 24. DR MINT; P25799; -. DR STRING; 10090.ENSMUSP00000029812; -. DR ChEMBL; CHEMBL1949489; -. DR GlyGen; P25799; 5 sites, 1 O-linked glycan (5 sites). DR iPTMnet; P25799; -. DR PhosphoSitePlus; P25799; -. DR EPD; P25799; -. DR jPOST; P25799; -. DR MaxQB; P25799; -. DR PaxDb; 10090-ENSMUSP00000029812; -. DR PeptideAtlas; P25799; -. DR ProteomicsDB; 287411; -. [P25799-1] DR ProteomicsDB; 287412; -. [P25799-2] DR ProteomicsDB; 287413; -. [P25799-3] DR ProteomicsDB; 287414; -. [P25799-4] DR ProteomicsDB; 287415; -. [P25799-5] DR ProteomicsDB; 287416; -. [P25799-6] DR ProteomicsDB; 287417; -. [P25799-7] DR Pumba; P25799; -. DR ABCD; P25799; 1 sequenced antibody. DR Antibodypedia; 3415; 2872 antibodies from 51 providers. DR DNASU; 18033; -. DR Ensembl; ENSMUST00000029812.14; ENSMUSP00000029812.8; ENSMUSG00000028163.18. [P25799-1] DR Ensembl; ENSMUST00000164430.7; ENSMUSP00000128345.3; ENSMUSG00000028163.18. [P25799-1] DR GeneID; 18033; -. DR KEGG; mmu:18033; -. DR UCSC; uc008rlw.1; mouse. [P25799-1] DR UCSC; uc008rly.1; mouse. [P25799-4] DR UCSC; uc012cyf.1; mouse. [P25799-6] DR AGR; MGI:97312; -. DR CTD; 4790; -. DR MGI; MGI:97312; Nfkb1. DR VEuPathDB; HostDB:ENSMUSG00000028163; -. DR eggNOG; KOG0504; Eukaryota. DR GeneTree; ENSGT00940000158625; -. DR HOGENOM; CLU_004343_1_0_1; -. DR InParanoid; P25799; -. DR OMA; GCSPNQQ; -. DR OrthoDB; 1059550at2759; -. DR PhylomeDB; P25799; -. DR TreeFam; TF325632; -. DR Reactome; R-MMU-1169091; Activation of NF-kappaB in B cells. DR Reactome; R-MMU-1810476; RIP-mediated NFkB activation via ZBP1. DR Reactome; R-MMU-193692; Regulated proteolysis of p75NTR. DR Reactome; R-MMU-202424; Downstream TCR signaling. DR Reactome; R-MMU-209560; NF-kB is activated and signals survival. DR Reactome; R-MMU-2871837; FCERI mediated NF-kB activation. DR Reactome; R-MMU-3134963; DEx/H-box helicases activate type I IFN and inflammatory cytokines production. DR Reactome; R-MMU-3214841; PKMTs methylate histone lysines. DR Reactome; R-MMU-445989; TAK1-dependent IKK and NF-kappa-B activation. DR Reactome; R-MMU-448706; Interleukin-1 processing. DR Reactome; R-MMU-5607764; CLEC7A (Dectin-1) signaling. DR Reactome; R-MMU-5621575; CD209 (DC-SIGN) signaling. DR Reactome; R-MMU-5684264; MAP3K8 (TPL2)-dependent MAPK1/3 activation. DR Reactome; R-MMU-6798695; Neutrophil degranulation. DR Reactome; R-MMU-9020702; Interleukin-1 signaling. DR Reactome; R-MMU-933542; TRAF6 mediated NF-kB activation. DR BioGRID-ORCS; 18033; 5 hits in 84 CRISPR screens. DR ChiTaRS; Nfkb1; mouse. DR EvolutionaryTrace; P25799; -. DR PRO; PR:P25799; -. DR Proteomes; UP000000589; Chromosome 3. DR RNAct; P25799; Protein. DR Bgee; ENSMUSG00000028163; Expressed in granulocyte and 267 other cell types or tissues. DR ExpressionAtlas; P25799; baseline and differential. DR GO; GO:0000785; C:chromatin; ISO:MGI. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0005829; C:cytosol; IDA:MGI. DR GO; GO:0005739; C:mitochondrion; ISO:MGI. DR GO; GO:0035525; C:NF-kappaB p50/p65 complex; IDA:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0032991; C:protein-containing complex; ISO:MGI. DR GO; GO:0005667; C:transcription regulator complex; IDA:MGI. DR GO; GO:0042805; F:actinin binding; ISO:MGI. DR GO; GO:0003682; F:chromatin binding; IDA:MGI. DR GO; GO:0003677; F:DNA binding; IDA:MGI. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI. DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISO:MGI. DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:MGI. DR GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI. DR GO; GO:0031072; F:heat shock protein binding; ISO:MGI. DR GO; GO:0042802; F:identical protein binding; IPI:MGI. DR GO; GO:0140311; F:protein sequestering activity; ISO:MGI. DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI. DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI. DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI. DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI. DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB. DR GO; GO:0003712; F:transcription coregulator activity; IDA:MGI. DR GO; GO:0140367; P:antibacterial innate immune response; IEA:Ensembl. DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW. DR GO; GO:0050853; P:B cell receptor signaling pathway; IDA:MGI. DR GO; GO:0007249; P:canonical NF-kappaB signal transduction; ISO:MGI. DR GO; GO:1904385; P:cellular response to angiotensin; ISO:MGI. DR GO; GO:1990416; P:cellular response to brain-derived neurotrophic factor stimulus; ISO:MGI. DR GO; GO:0071322; P:cellular response to carbohydrate stimulus; ISO:MGI. DR GO; GO:0071345; P:cellular response to cytokine stimulus; ISO:MGI. DR GO; GO:1904630; P:cellular response to diterpene; ISO:MGI. DR GO; GO:0071359; P:cellular response to dsRNA; IMP:MGI. DR GO; GO:1904632; P:cellular response to glucoside; ISO:MGI. DR GO; GO:0071347; P:cellular response to interleukin-1; ISO:MGI. DR GO; GO:0097398; P:cellular response to interleukin-17; IDA:MGI. DR GO; GO:0071354; P:cellular response to interleukin-6; ISO:MGI. DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:MGI. DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl. DR GO; GO:0071316; P:cellular response to nicotine; ISO:MGI. DR GO; GO:0071407; P:cellular response to organic cyclic compound; ISO:MGI. DR GO; GO:1901653; P:cellular response to peptide; ISO:MGI. DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IDA:MGI. DR GO; GO:0098586; P:cellular response to virus; IMP:MGI. DR GO; GO:0010467; P:gene expression; IMP:MGI. DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central. DR GO; GO:0045087; P:innate immune response; IBA:GO_Central. DR GO; GO:0007254; P:JNK cascade; IMP:MGI. DR GO; GO:0048535; P:lymph node development; TAS:MGI. DR GO; GO:0060056; P:mammary gland involution; IDA:MGI. DR GO; GO:0000165; P:MAPK cascade; IMP:MGI. DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI. DR GO; GO:0001818; P:negative regulation of cytokine production; IMP:BHF-UCL. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:MGI. DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI. DR GO; GO:0050728; P:negative regulation of inflammatory response; IMP:MGI. DR GO; GO:0032695; P:negative regulation of interleukin-12 production; IDA:MGI. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB. DR GO; GO:0038061; P:non-canonical NF-kappaB signal transduction; ISO:MGI. DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISO:MGI. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS:UniProtKB. DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI. DR GO; GO:1900127; P:positive regulation of hyaluronan biosynthetic process; ISO:MGI. DR GO; GO:2000630; P:positive regulation of miRNA metabolic process; ISO:MGI. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI. DR GO; GO:0060261; P:positive regulation of transcription initiation by RNA polymerase II; IMP:MGI. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI. DR GO; GO:0034097; P:response to cytokine; IBA:GO_Central. DR GO; GO:0035994; P:response to muscle stretch; IDA:MGI. DR GO; GO:0014070; P:response to organic cyclic compound; ISO:MGI. DR GO; GO:0006979; P:response to oxidative stress; ISO:MGI. 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; 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; 5. DR PROSITE; PS01204; REL_1; 1. DR PROSITE; PS50254; REL_2; 1. DR Genevisible; P25799; MM. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Activator; Alternative splicing; ANK repeat; KW Apoptosis; Cytoplasm; Direct protein sequencing; DNA-binding; KW Hydroxylation; Isopeptide bond; Lipoprotein; Nucleus; Phosphoprotein; KW Reference proteome; Repeat; S-nitrosylation; Transcription; KW Transcription regulation; Ubl conjugation. FT CHAIN 1..971 FT /note="Nuclear factor NF-kappa-B p105 subunit" FT /id="PRO_0000030312" FT CHAIN 1..431 FT /note="Nuclear factor NF-kappa-B p50 subunit" FT /evidence="ECO:0000250" FT /id="PRO_0000030313" FT DOMAIN 40..365 FT /note="RHD" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00265" FT REPEAT 538..567 FT /note="ANK 1" FT REPEAT 577..606 FT /note="ANK 2" FT REPEAT 610..639 FT /note="ANK 3" FT REPEAT 646..675 FT /note="ANK 4" FT REPEAT 680..710 FT /note="ANK 5" FT REPEAT 714..743 FT /note="ANK 6" FT REPEAT 767..797 FT /note="ANK 7" FT DOMAIN 801..888 FT /note="Death" FT REGION 370..392 FT /note="GRR" FT /evidence="ECO:0000250|UniProtKB:P19838" FT REGION 433..971 FT /note="Interaction with CFLAR" FT /evidence="ECO:0000250|UniProtKB:P19838" FT REGION 439..470 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 646..680 FT /note="Essential for interaction with HIF1AN" FT /evidence="ECO:0000250|UniProtKB:P19838" FT MOTIF 358..363 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255" FT SITE 431..432 FT /note="Cleavage (when cotranslationally processed)" FT /evidence="ECO:0000250|UniProtKB:P19838" FT MOD_RES 59 FT /note="S-nitrosocysteine; alternate" FT /evidence="ECO:0000250|UniProtKB:P19838" FT MOD_RES 335 FT /note="Phosphoserine; by PKA" FT /evidence="ECO:0000255" FT MOD_RES 438 FT /note="N6-acetyllysine; by EP300" FT /evidence="ECO:0000250|UniProtKB:P19838" FT MOD_RES 447 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 674 FT /note="(3S)-3-hydroxyasparagine; by HIF1AN" FT /evidence="ECO:0000250|UniProtKB:P19838" FT MOD_RES 755 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q63369" FT MOD_RES 896 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P19838" FT MOD_RES 910 FT /note="Phosphoserine; by GSK3-beta; in vitro" FT /evidence="ECO:0000250|UniProtKB:P19838" FT MOD_RES 926 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P19838" FT MOD_RES 930 FT /note="Phosphoserine; by IKKB" FT /evidence="ECO:0000250|UniProtKB:P19838" FT MOD_RES 935 FT /note="Phosphoserine; by IKKB" FT /evidence="ECO:0000250|UniProtKB:P19838" FT MOD_RES 940 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 946 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT LIPID 59 FT /note="S-(15-deoxy-Delta12,14-prostaglandin J2-9- FT yl)cysteine; alternate" FT /evidence="ECO:0000250|UniProtKB:P19838" FT CROSSLNK 323 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P19838" FT VAR_SEQ 1..364 FT /note="Missing (in isoform 5, isoform 6 and isoform 7)" FT /evidence="ECO:0000303|PubMed:1339305, FT ECO:0000303|PubMed:8398903" FT /id="VSP_017236" FT VAR_SEQ 353..356 FT /note="DKEE -> GTWV (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:16141072" FT /id="VSP_017237" FT VAR_SEQ 357..971 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:16141072" FT /id="VSP_017238" FT VAR_SEQ 780..971 FT /note="VFDILNGKPYEPVFTSDDILPQGDMKQLTEDTRLQLCKLLEIPDPDKNWATL FT AQKLGLGILNNAFRLSPAPSKTLMDNYEVSGGTIKELMEALQQMGYTEAIEVIQAAFRT FT PATTASSPVTTAQVHCLPLSSSSTRQHIDELRDSDSVCDSGVETSFRKLSFTESLTGDS FT PLLSLNKMPHGYGQEGPIEGKI -> GT (in isoform 2 and isoform 7)" FT /evidence="ECO:0000303|PubMed:7969179" FT /id="VSP_005583" FT VAR_SEQ 860..971 FT /note="VSGGTIKELMEALQQMGYTEAIEVIQAAFRTPATTASSPVTTAQVHCLPLSS FT SSTRQHIDELRDSDSVCDSGVETSFRKLSFTESLTGDSPLLSLNKMPHGYGQEGPIEGK FT I -> MNSGIVTASVTVVWRHPSANSALQSLLLETAHCYL (in isoform 3 and FT isoform 6)" FT /evidence="ECO:0000303|PubMed:7969179" FT /id="VSP_005584" FT CONFLICT 111 FT /note="L -> P (in Ref. 9; AAR00341)" FT /evidence="ECO:0000305" FT CONFLICT 265 FT /note="E -> G (in Ref. 10; BAC35117)" FT /evidence="ECO:0000305" FT CONFLICT 530 FT /note="H -> D (in Ref. 10; BAE34261)" FT /evidence="ECO:0000305" FT CONFLICT 546 FT /note="A -> G (in Ref. 10; BAE34261)" FT /evidence="ECO:0000305" FT CONFLICT 684 FT /note="A -> P (in Ref. 1; AAA40415, 2; AAB21851 and 3; FT AAB28573)" FT /evidence="ECO:0000305" FT CONFLICT 732 FT /note="A -> T (in Ref. 10; BAE34261)" FT /evidence="ECO:0000305" FT CONFLICT 950 FT /note="P -> A (in Ref. 10; BAE43399)" FT /evidence="ECO:0000305" FT STRAND 41..46 FT /evidence="ECO:0007829|PDB:1NFK" FT STRAND 50..52 FT /evidence="ECO:0007829|PDB:1NFK" FT HELIX 58..60 FT /evidence="ECO:0007829|PDB:1NFK" FT STRAND 62..64 FT /evidence="ECO:0007829|PDB:1VKX" FT STRAND 74..76 FT /evidence="ECO:0007829|PDB:1OOA" FT STRAND 81..85 FT /evidence="ECO:0007829|PDB:1NFK" FT STRAND 92..98 FT /evidence="ECO:0007829|PDB:1NFK" FT STRAND 100..103 FT /evidence="ECO:0007829|PDB:1NFK" FT STRAND 108..113 FT /evidence="ECO:0007829|PDB:1NFK" FT STRAND 117..119 FT /evidence="ECO:0007829|PDB:1LE9" FT STRAND 120..124 FT /evidence="ECO:0007829|PDB:1NFK" FT STRAND 131..133 FT /evidence="ECO:0007829|PDB:1NFK" FT STRAND 138..140 FT /evidence="ECO:0007829|PDB:1NFK" FT HELIX 144..146 FT /evidence="ECO:0007829|PDB:1OOA" FT HELIX 147..160 FT /evidence="ECO:0007829|PDB:1NFK" FT STRAND 162..164 FT /evidence="ECO:0007829|PDB:1VKX" FT HELIX 165..169 FT /evidence="ECO:0007829|PDB:1NFK" FT HELIX 171..173 FT /evidence="ECO:0007829|PDB:1OOA" FT STRAND 179..182 FT /evidence="ECO:0007829|PDB:1NFK" FT HELIX 188..203 FT /evidence="ECO:0007829|PDB:1NFK" FT STRAND 209..219 FT /evidence="ECO:0007829|PDB:1NFK" FT STRAND 221..223 FT /evidence="ECO:0007829|PDB:1NFK" FT STRAND 225..228 FT /evidence="ECO:0007829|PDB:1NFK" FT STRAND 232..239 FT /evidence="ECO:0007829|PDB:1OOA" FT STRAND 240..242 FT /evidence="ECO:0007829|PDB:1VKX" FT TURN 243..246 FT /evidence="ECO:0007829|PDB:1OOA" FT STRAND 250..254 FT /evidence="ECO:0007829|PDB:1U36" FT STRAND 256..259 FT /evidence="ECO:0007829|PDB:1U36" FT STRAND 265..271 FT /evidence="ECO:0007829|PDB:1U36" FT TURN 275..277 FT /evidence="ECO:0007829|PDB:1NFK" FT STRAND 279..284 FT /evidence="ECO:0007829|PDB:1U36" FT HELIX 287..289 FT /evidence="ECO:0007829|PDB:1BFS" FT STRAND 292..295 FT /evidence="ECO:0007829|PDB:1U36" FT HELIX 300..302 FT /evidence="ECO:0007829|PDB:1U36" FT TURN 305..307 FT /evidence="ECO:0007829|PDB:1U36" FT STRAND 308..312 FT /evidence="ECO:0007829|PDB:1U36" FT STRAND 325..332 FT /evidence="ECO:0007829|PDB:1U36" FT TURN 334..336 FT /evidence="ECO:0007829|PDB:1U36" FT STRAND 343..348 FT /evidence="ECO:0007829|PDB:1U36" FT STRAND 351..354 FT /evidence="ECO:0007829|PDB:1IKN" SQ SEQUENCE 971 AA; 105615 MW; 91EA9C595E375C30 CRC64; MADDDPYGTG QMFHLNTALT HSIFNAELYS PEIPLSTDGP YLQILEQPKQ RGFRFRYVCE GPSHGGLPGA SSEKNKKSYP QVKICNYVGP AKVIVQLVTN GKNIHLHAHS LVGKHCEDGV CTVTAGPKDM VVGFANLGIL HVTKKKVFET LEARMTEACI RGYNPGLLVH SDLAYLQAEG GGDRQLTDRE KEIIRQAAVQ QTKEMDLSVV RLMFTAFLPD STGSFTRRLE PVVSDAIYDS KAPNASNLKI VRMDRTAGCV TGGEEIYLLC DKVQKDDIQI RFYEEEENGG VWEGFGDFSP TDVHRQFAIV FKTPKYKDVN ITKPASVFVQ LRRKSDLETS EPKPFLYYPE IKDKEEVQRK RQKLMPNFSD SFGGGSGAGA GGGGMFGSGG GGGSTGSPGP GYGYSNYGFP PYGGITFHPG VTKSNAGVTH GTINTKFKNG PKDCAKSDDE ESLTLPEKET EGEGPSLPMA CTKTEPIALA STMEDKEQDM GFQDNLFLEK ALQLARRHAN ALFDYAVTGD VKMLLAVQRH LTAVQDENGD SVLHLAIIHL HAQLVRDLLE VTSGLISDDI INMRNDLYQT PLHLAVITKQ EDVVEDLLRV GADLSLLDRW GNSVLHLAAK EGHDRILSIL LKSRKAAPLI DHPNGEGLNA IHIAVMSNSL PCLLLLVAAG AEVNAQEQKS GRTALHLAVE YDNISLAGCL LLEGDAHVDS TTYDGTTPLH IAAGRGSTRL AALLKAAGAD PLVENFEPLY DLDDSWEKAG EDEGVVPGTT PLDMAANWQV FDILNGKPYE PVFTSDDILP QGDMKQLTED TRLQLCKLLE IPDPDKNWAT LAQKLGLGIL NNAFRLSPAP SKTLMDNYEV SGGTIKELME ALQQMGYTEA IEVIQAAFRT PATTASSPVT TAQVHCLPLS SSSTRQHIDE LRDSDSVCDS GVETSFRKLS FTESLTGDSP LLSLNKMPHG YGQEGPIEGK I //