ID:TNIP2_HUMAN DESCRIPTION: RecName: Full=TNFAIP3-interacting protein 2; AltName: Full=A20-binding inhibitor of NF-kappa-B activation 2; Short=ABIN-2; AltName: Full=Fetal liver LKB1-interacting protein; FUNCTION: Inhibits NF-kappa-B activation by blocking the interaction of RIPK1 with its downstream effector NEMO/IKBKG. Forms a ternary complex with NFKB1 and MAP3K8 but appears to function upstream of MAP3K8 in the TLR4 signaling pathway that regulates MAP3K8 activation. Involved in activation of the MEK/ERK signaling pathway during innate immune response; this function seems to be stimulus- and cell type specific. Required for stability of MAP3K8. Involved in regulation of apoptosis in endothelial cells; promotes TEK agonist-stimulated endothelial survival. May act as transcriptional coactivator when translocated to the nucleus. Enhances CHUK-mediated NF-kappa-B activation involving NF-kappa-B p50-p65 and p50-c-Rel complexes. SUBUNIT: Interacts with STK11/LKB1, TNFAIP3, IKBKG, NFKB1, MAP3K8, TEK, RIPK1, CHUK, IKBKB and SMARCD1. Interacts with polyubiquitin. INTERACTION: Q9Y6K9:IKBKG; NbExp=6; IntAct=EBI-359372, EBI-81279; P41279:MAP3K8; NbExp=8; IntAct=EBI-359372, EBI-354900; P19838-1:NFKB1; NbExp=8; IntAct=EBI-359372, EBI-1452239; Q15831:STK11; NbExp=5; IntAct=EBI-359372, EBI-306838; SUBCELLULAR LOCATION: Cytoplasm. Nucleus (Probable). TISSUE SPECIFICITY: Ubiquitously expressed in all tissues examined. PTM: In vitro phosphorylated by CHUK. PTM: Ubiquitinated; undergoes 'Lys-48'-linked polyubiquitination probably leading to constitutive proteasomal degradation which can be impaired by IKK-A/CHUK or IKBKB probbaly involving deubiquitination.
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
Pfam Domains: PF12180 - TSG101 and ALIX binding domain of CEP55
ModBase Predicted Comparative 3D Structure on Q8NFZ5
Front
Top
Side
The pictures above may be empty if there is no ModBase structure for the protein. The ModBase structure frequently covers just a fragment of the protein. You may be asked to log onto ModBase the first time you click on the pictures. It is simplest after logging in to just click on the picture again to get to the specific info on that model.
Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.