ID NFKB1_CANLF Reviewed; 972 AA. AC Q6F3J0; F1PM82; DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot. DT 18-APR-2012, sequence version 2. DT 27-NOV-2024, entry version 139. DE RecName: Full=Nuclear factor NF-kappa-B p105 subunit; 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 Canis lupus familiaris (Dog) (Canis familiaris). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis. OX NCBI_TaxID=9615; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Oguma K., Kano R., Hasegawa A.; RT "Canis familiaris nuclear factor of kappa light polypeptide gene enhancer RT in B-cells 1 (p105) (NFKB1), mRNA."; RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Boxer; RX PubMed=16341006; DOI=10.1038/nature04338; RA Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B., RA Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E., RA Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F., RA Smith D.R., deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W., RA Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S., RA Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A., RA Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P., RA Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A., RA Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P., RA Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P., RA Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B., RA Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A., RA Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M., RA Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S., RA Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L., RA Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S., RA Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C., RA Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G., RA Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N., RA Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A., RA Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A., RA Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M., RA Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L., RA LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A., RA Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S., RA Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T., RA Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A., RA Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N., RA Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S., RA Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M., RA Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F., RA Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T., RA Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C., RA Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C., RA Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D., RA Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H., RA Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J., RA Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J., RA Zembek L., Zimmer A., Lander E.S.; RT "Genome sequence, comparative analysis and haplotype structure of the RT domestic dog."; RL Nature 438:803-819(2005). 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 -!- 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-908 and Ser-912 primes p105 for proteolytic CC processing in response to TNF-alpha stimulation (By similarity). CC Phosphorylation at Ser-927, Ser-931 and Ser-936 are required for CC BTRC/BTRCP-mediated ubiquitination and proteolysis (By similarity). CC Phosphorylation at Ser-931 is also required for ubiquitination by the CC KPC complex and limited processing to generate NF-kappa-B p50 (Nuclear CC factor NF-kappa-B p50 subunit) (By similarity). CC {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 923, Ser-927, Ser-931 and Ser-936, leading to its complete degradation. CC In contrast, polyubiquitination by the KPC complex following CC phosphorylation at Ser-931 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-61 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; AB183419; BAD27479.1; -; mRNA. DR RefSeq; NP_001003344.1; NM_001003344.1. DR AlphaFoldDB; Q6F3J0; -. DR SMR; Q6F3J0; -. DR STRING; 9615.ENSCAFP00000056706; -. DR PaxDb; 9612-ENSCAFP00000015815; -. DR Ensembl; ENSCAFT00000017092.5; ENSCAFP00000015815.5; ENSCAFG00000010730.5. DR Ensembl; ENSCAFT00030037443.1; ENSCAFP00030032664.1; ENSCAFG00030020386.1. DR Ensembl; ENSCAFT00040043145.1; ENSCAFP00040037640.1; ENSCAFG00040022966.1. DR Ensembl; ENSCAFT00805053263; ENSCAFP00805041753; ENSCAFG00805029346. DR Ensembl; ENSCAFT00845045189.1; ENSCAFP00845035432.1; ENSCAFG00845025570.1. DR GeneID; 442859; -. DR KEGG; cfa:442859; -. DR CTD; 4790; -. DR VEuPathDB; HostDB:ENSCAFG00845025570; -. DR VGNC; VGNC:43780; NFKB1. DR eggNOG; KOG0504; Eukaryota. DR GeneTree; ENSGT00940000158625; -. DR InParanoid; Q6F3J0; -. DR Reactome; R-CFA-1169091; Activation of NF-kappaB in B cells. DR Reactome; R-CFA-1810476; RIP-mediated NFkB activation via ZBP1. DR Reactome; R-CFA-193692; Regulated proteolysis of p75NTR. DR Reactome; R-CFA-202424; Downstream TCR signaling. DR Reactome; R-CFA-209560; NF-kB is activated and signals survival. DR Reactome; R-CFA-2871837; FCERI mediated NF-kB activation. DR Reactome; R-CFA-3134963; DEx/H-box helicases activate type I IFN and inflammatory cytokines production. DR Reactome; R-CFA-3214841; PKMTs methylate histone lysines. DR Reactome; R-CFA-445989; TAK1-dependent IKK and NF-kappa-B activation. DR Reactome; R-CFA-448706; Interleukin-1 processing. DR Reactome; R-CFA-5607764; CLEC7A (Dectin-1) signaling. DR Reactome; R-CFA-5621575; CD209 (DC-SIGN) signaling. DR Reactome; R-CFA-5684264; MAP3K8 (TPL2)-dependent MAPK1/3 activation. DR Reactome; R-CFA-6798695; Neutrophil degranulation. DR Reactome; R-CFA-9020702; Interleukin-1 signaling. DR Reactome; R-CFA-933542; TRAF6 mediated NF-kB activation. DR Proteomes; UP000002254; Chromosome 32. DR Proteomes; UP000694429; Chromosome 32. DR Proteomes; UP000694542; Chromosome 32. DR Proteomes; UP000805418; Chromosome 32. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0035525; C:NF-kappaB p50/p65 complex; IBA:GO_Central. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. 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; IBA:GO_Central. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central. DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB. DR GO; GO:0007249; P:canonical NF-kappaB signal transduction; IBA:GO_Central. DR GO; GO:0033554; P:cellular response to stress; IBA:GO_Central. DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central. DR GO; GO:0045087; P:innate immune response; IBA:GO_Central. 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; IBA:GO_Central. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0034097; P:response to cytokine; IBA:GO_Central. DR CDD; cd08797; Death_NFkB1_p105; 1. DR CDD; cd01177; IPT_NFkappaB; 1. DR CDD; cd07935; RHD-n_NFkB1; 1. DR FunFam; 2.60.40.10:FF:000046; Nuclear factor NF-kappa-B p105 subunit; 1. DR FunFam; 1.10.533.10:FF:000018; Nuclear factor NF-kappa-B p105 subunit isoform 1; 1. DR FunFam; 1.25.40.20:FF:000103; Nuclear factor NF-kappa-B p105 subunit isoform 1; 1. DR FunFam; 2.60.40.340:FF:000004; Nuclear factor NF-kappa-B p105 subunit isoform 1; 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. PE 2: Evidence at transcript level; KW Acetylation; Activator; ANK repeat; Cytoplasm; DNA-binding; Hydroxylation; KW Isopeptide bond; Lipoprotein; Nucleus; Phosphoprotein; Reference proteome; KW Repeat; S-nitrosylation; Transcription; Transcription regulation; KW Ubl conjugation. FT CHAIN 1..972 FT /note="Nuclear factor NF-kappa-B p105 subunit" FT /id="PRO_0000223240" FT CHAIN 1..433 FT /note="Nuclear factor NF-kappa-B p50 subunit" FT /evidence="ECO:0000250|UniProtKB:P19838" FT /id="PRO_0000223241" FT DOMAIN 39..246 FT /note="RHD" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00265" FT REPEAT 539..568 FT /note="ANK 1" FT REPEAT 578..607 FT /note="ANK 2" FT REPEAT 611..640 FT /note="ANK 3" FT REPEAT 647..676 FT /note="ANK 4" FT REPEAT 681..711 FT /note="ANK 5" FT REPEAT 715..744 FT /note="ANK 6" FT REPEAT 768..798 FT /note="ANK 7" FT DOMAIN 814..889 FT /note="Death" FT REGION 372..394 FT /note="GRR" FT /evidence="ECO:0000250|UniProtKB:P19838" FT REGION 425..473 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 435..972 FT /note="Interaction with CFLAR" FT /evidence="ECO:0000250|UniProtKB:P19838" FT REGION 647..681 FT /note="Essential for interaction with HIF1AN" FT /evidence="ECO:0000250|UniProtKB:P19838" FT REGION 894..926 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 360..365 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255" FT COMPBIAS 425..444 FT /note="Polar 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 61 FT /note="S-nitrosocysteine; alternate" FT /evidence="ECO:0000250|UniProtKB:P19838" FT MOD_RES 337 FT /note="Phosphoserine; by PKA" FT /evidence="ECO:0000255" FT MOD_RES 431 FT /note="N6-acetyllysine; by EP300" FT /evidence="ECO:0000250|UniProtKB:P19838" FT MOD_RES 440 FT /note="N6-acetyllysine; by EP300" FT /evidence="ECO:0000250|UniProtKB:P19838" FT MOD_RES 675 FT /note="(3S)-3-hydroxyasparagine; by HIF1AN" FT /evidence="ECO:0000250|UniProtKB:P19838" FT MOD_RES 756 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q63369" FT MOD_RES 908 FT /note="Phosphoserine; by GSK3-beta; in vitro" 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 927 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P19838" FT MOD_RES 931 FT /note="Phosphoserine; by IKKB" FT /evidence="ECO:0000250|UniProtKB:P19838" FT MOD_RES 936 FT /note="Phosphoserine; by IKKB" FT /evidence="ECO:0000250|UniProtKB:P19838" FT MOD_RES 941 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P19838" FT MOD_RES 947 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P25799" FT LIPID 61 FT /note="S-(15-deoxy-Delta12,14-prostaglandin J2-9- FT yl)cysteine; alternate" FT /evidence="ECO:0000250|UniProtKB:P19838" FT CROSSLNK 325 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P19838" FT CONFLICT 289 FT /note="E -> G (in Ref. 1; BAD27479)" FT /evidence="ECO:0000305" FT CONFLICT 295 FT /note="E -> G (in Ref. 1; BAD27479)" FT /evidence="ECO:0000305" FT CONFLICT 327 FT /note="A -> T (in Ref. 1; BAD27479)" FT /evidence="ECO:0000305" FT CONFLICT 432 FT /note="H -> N (in Ref. 1; BAD27479)" FT /evidence="ECO:0000305" FT CONFLICT 538 FT /note="E -> G (in Ref. 1; BAD27479)" FT /evidence="ECO:0000305" FT CONFLICT 822 FT /note="I -> T (in Ref. 1; BAD27479)" FT /evidence="ECO:0000305" FT CONFLICT 838 FT /note="L -> Q (in Ref. 1; BAD27479)" FT /evidence="ECO:0000305" FT CONFLICT 939 FT /note="K -> R (in Ref. 1; BAD27479)" FT /evidence="ECO:0000305" SQ SEQUENCE 972 AA; 105631 MW; 189557C55699014F CRC64; MAEDDTYLGA HEQMFHLDPL THTIFNPELF QPEMPLPTAD GPYLQILEQP KQRGFRFRYV CEGPSHGGLP GASSEKNKKS YPQVKICNYV GPAKVIVQLV TNGKNIHLHA HSLVGKHCED GICTVTAGPK DMVVGFANLG ILHVTKKKVF ETLEARMTEA CTKGYNPGLL VHPDLAYLQA EGGGDRQLTD REKEIIRQAA LQQTKEMDLS VVRLMFTAFL PDSTGSFTRR LEPVVSDAIY DSKAPNASNL KIVRMDRTAG CVTGGEEIYL LCDKVQKDDI QIRFYEEEEN GGIWEGFGDF SPTDVHRQFA IVFKTPKYKD VNITKPASVF VQLRRKSDLE TSEPKPFLYY PEIKDKEEVQ RKRQKLMPNF SDSFGGGSGA GAGGGGMFGS GGGGGGAGST GPGYGFPHYG FPTYGGITFH PGTTKSNAGM KHGTIDTPSK NDSEGCGKNV DREAVNLSGK VTEPTEQDKE SSMGVDEVTL TYTVGIKEEN SRFQDNLFLE KAMQLAKRHA NALFDYAVTG DVKMLLAVQR HLTAVQDENG DSVLHLAIIH LHAQLVRDLL EVTSGLISDD IINMRNDLYQ TPLHLAVITK QEAVVDDLLR AGADLSLLDR LGNSVLHLAA KEGQDKILSI LLKHKKAALL MDHPNGEGLN AIHIAVMSNS MPCLLLLVAA GADVNAQERK SGRTALHLAV EHDNISLAGC LLLEGDAHVD STTYDGTTPL HIAAGRGSTR LAALLKAAGA DPLVENFEPL YDLDDSWEKD GEDEGVVPGT TPLDMATNWQ VFDILNGKPY EPEFTSDDLL AQGDMKQLTE DAKLQLYKLL EIPDPDKNWA TLAQKLGLGI LNNAFRLSPA PSKTLMDNYE VSGGTIKELV EALRQMGYTE AIEVIQAAFC APETAAPSPG KGAPQTLSLP LSSASTRSPV DEVRDDSICD SGVETSFRKL SFTESLTSGS SLLTLNKAPH EYGQEGPIEG KI //