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NF-kappa-B inhibitor zeta (I-kappa-B-zeta, IkappaBzeta, IkB-zeta, molecule possessing ankyrin repeats induced by lipopolysaccharide, MAIL, IL-1 inducible nuclear ankyrin-repeat protein, INAP, NFKBIZ, IKBZ, INAP, MAIL)
Function:
- role in regulation of NF-kappa-B transcription factor complexes
- inhibits NF-kappa-B activity without affecting its nuclear translocation upon stimulation
- inhibits DNA-binding of RELA & NFKB1/p50, & of the NF-kappa-B RELA-NFKB1/p50 heterodimer & the NF-kappa-B NFKB1/p50 homodimer
- seems also to activate NF-kappa-B-mediated transcription
- in vitro, upon association with NFKB1/p50 has transcriptional activation activity &, together with NFKB1/p50 & RELA, is recruited to LCN2 promoters
- promotes transcription of LCN2 & DEFB4
- recruited to IL-6 promoters & activates IL-6 but decreases TNF-alpha production in response to LPS
- seems to be involved in the induction of inflammatory genes activated through TLR/IL-1
- receptor signaling
- may promote apoptosis (putative)
- interacts with NFKB1/p50
- interacts with RELA
Structure: contains 7 ANK repeats
Compartment:
- nucleus
- aggregated in dot-like structures
- colocalizes with NCOR2
Alternative splicing: named isoforms=3
Expression:
- expressed in peripheral blood leukocytes & lung > liver, placenta > spleen, kidney, skeletal muscle & heart
- induced by TNFA, IL-1 & LPS
General
ankyrin repeat domain protein (ANKRD)
nuclear protein
Properties
SIZE: entity length = 718 aa
MW = 78 kD
COMPARTMENT: cell nucleus
MOTIF: nuclear translocation signal {164-179}
transcriptional activity {321-394}
NFKB1/p50 interaction {404-718}
MOTIF: ankyrin repeat
NAME: ankyrin repeat
SITE: 443-472
ankyrin repeat
NAME: ankyrin repeat
SITE: 479-508
ankyrin repeat
NAME: ankyrin repeat
SITE: 512-541
ankyrin repeat
NAME: ankyrin repeat
SITE: 551-580
ankyrin repeat
NAME: ankyrin repeat
SITE: 582-607
ankyrin repeat
NAME: ankyrin repeat
SITE: 612-641
ankyrin repeat
NAME: ankyrin repeat
SITE: 648-681
Database Correlations
OMIM 608004
UniProt Q9BYH8
Pfam PF00023
References
UniProt :accession Q9BYH8