ID A0A8C0BU75_9AVES Unreviewed; 725 AA.
AC A0A8C0BU75;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 19.
DE RecName: Full=Inhibitor of nuclear factor kappa-B kinase subunit beta {ECO:0000256|ARBA:ARBA00072641};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.10 {ECO:0000256|ARBA:ARBA00012442};
DE AltName: Full=I-kappa-B kinase 2 {ECO:0000256|ARBA:ARBA00076063};
DE AltName: Full=Nuclear factor NF-kappa-B inhibitor kinase beta {ECO:0000256|ARBA:ARBA00075315};
DE AltName: Full=Serine/threonine protein kinase IKBKB {ECO:0000256|ARBA:ARBA00083976};
OS Buteo japonicus.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Accipitrimorphae;
OC Accipitriformes; Accipitridae; Accipitrinae; Buteo.
OX NCBI_TaxID=224669 {ECO:0000313|Ensembl:ENSBJAP00000021479.1, ECO:0000313|Proteomes:UP000694555};
RN [1] {ECO:0000313|Ensembl:ENSBJAP00000021479.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSBJAP00000021479.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[I-kappa-B protein] + ATP = O-phospho-L-seryl-[I-
CC kappa-B protein] + ADP + H(+); Xref=Rhea:RHEA:19073, Rhea:RHEA-
CC COMP:13698, Rhea:RHEA-COMP:13699, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421,
CC ChEBI:CHEBI:456216; EC=2.7.11.10;
CC Evidence={ECO:0000256|ARBA:ARBA00048789};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +
CC H(+); Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00048679};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +
CC ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00047899};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Membrane raft {ECO:0000256|ARBA:ARBA00004285}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
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DR AlphaFoldDB; A0A8C0BU75; -.
DR Ensembl; ENSBJAT00000022089.1; ENSBJAP00000021479.1; ENSBJAG00000013904.1.
DR Proteomes; UP000694555; Unplaced.
DR GO; GO:0008385; C:IkappaB kinase complex; IEA:TreeGrafter.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008384; F:IkappaB kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:TreeGrafter.
DR GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IEA:TreeGrafter.
DR CDD; cd17046; Ubl_IKKA_like; 1.
DR FunFam; 3.10.20.90:FF:000087; Inhibitor of nuclear factor kappa B kinase subunit beta; 1.
DR FunFam; 1.10.510.10:FF:000147; Inhibitor of nuclear factor kappa-B kinase subunit beta; 1.
DR FunFam; 1.20.1270.250:FF:000002; Putative inhibitor of nuclear factor kappa-B kinase subunit beta; 1.
DR Gene3D; 1.20.1270.250; -; 1.
DR Gene3D; 6.10.250.2110; -; 1.
DR Gene3D; 3.10.20.90; Phosphatidylinositol 3-kinase Catalytic Subunit, Chain A, domain 1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR041185; IKBKB_SDD.
DR InterPro; IPR046375; IKBKB_SDD_sf.
DR InterPro; IPR051180; IKK.
DR InterPro; IPR022007; IKKbetaNEMObind.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR22969; IKB KINASE; 1.
DR PANTHER; PTHR22969:SF7; INHIBITOR OF NUCLEAR FACTOR KAPPA-B KINASE SUBUNIT BETA; 1.
DR Pfam; PF18397; IKBKB_SDD; 1.
DR Pfam; PF12179; IKKbetaNEMObind; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM01239; IKKbetaNEMObind; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000694555};
KW S-nitrosylation {ECO:0000256|ARBA:ARBA00022799};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..725
FT /note="Inhibitor of nuclear factor kappa-B kinase subunit
FT beta"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5034537805"
FT DOMAIN 1..268
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT COILED 498..548
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 725 AA; 83071 MW; 15A00356B2DC21CE CRC64;
RPWSAGLTAA LRTVIFQVLP WFHSSCVLAS FPLLRLNHPN VVAARDVPEG MQKLAPNDLP
LLAMEYCQGG DLRKYLNQLE NCCGLREEAI LILLSDIASA LRYLHENRII HRDLKPENIV
LQQGEQRLIH KIIDLGYAKE LDQGSLCTSF VGTLQYLAPE LLEQQKYTVT VDYWSFGTLA
FECITGFRPF LPNWQPVQWH TKVRQKSELD IVVSEDLSGE VKFSSSLPCP NNLNSVLAGR
LEKWLQLMLM WHPRQRGTDP TYGPNGCFKA LDDILNLKLL HVLNMVTGTV HTYPVTEEET
LQSVKARIQS DTGIPEQDQE LLQEAGLALF SQKLATKHIA DSKVNDTAAA DTDLLFLFDN
QKVAYEAQVA LRPHPESVDC ILQDPKKNLH FFQLRKVWGQ IWHTIRMLKE DCNRLQQGQR
AAMMNLLRYN STLSKMKNSM ASLSQQLKAK LDFFKTSIQI DLEKYKEQIE FGITSEKLLF
AWKEMEQAVE LCGREDDVDQ LVKRMMALQT DIVDLQRSPL GRKQGGTLED LEEQARELYR
RLREKPRDQR TSGDSQEIVR LLLQAIQTFE KKVRVIYAQL SKTVVCKQKA LELFPKVEKV
MNLMNEDEET VVRLQEKRQK ELWNLLKIAC SKVRGPVTGS PESMNTSRLG SPGQLLLQVP
SGTYNLSESV RKSEELLLES QKLCSQLENV MHDTMKDQEQ SFMALDWSWL QLQVEETSSP
EQTQM
//
