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-MAR-2024, entry version 136.
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}.
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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-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; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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: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 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
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