ID:RIPK4_HUMAN DESCRIPTION: RecName: Full=Receptor-interacting serine/threonine-protein kinase 4; EC=2.7.11.1; AltName: Full=Ankyrin repeat domain-containing protein 3; AltName: Full=PKC-delta-interacting protein kinase; FUNCTION: Involved in stratified epithelial development. It is a direct transcriptional target of TP63. Plays a role in NF-kappa-B activation. CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. SUBUNIT: Interacts with PRKCB (By similarity). Interacts with TRAF1, TRAF2, TRAF3 and TRAF5. Interacts with BIRC2/c-IAP1, BIRC3/c-IAP2 and XIAP/BIRC4. INTERACTION: Q13490:BIRC2; NbExp=3; IntAct=EBI-4422308, EBI-514538; Q13489:BIRC3; NbExp=3; IntAct=EBI-4422308, EBI-517709; P98170:XIAP; NbExp=2; IntAct=EBI-4422308, EBI-517127; SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein (By similarity). PTM: May be phosphorylated by MAP3K2 and MAP3K3 (By similarity). PTM: Proteolytically cleaved by during Fas-induced apoptosis. Cleavage at Asp-388 and Asp-426. PTM: Polyubiquitinated with 'Lys-48' and 'Lys-63'-linked chains by BIRC2/c-IAP1 and BIRC3/c-IAP2, leading to activation of NF-kappa- B. DISEASE: Defects in RIPK4 are the cause of popliteal pterygium syndrome, lethal type (PPS-L) [MIM:263650]. An autosomal recessive disorder characterized by multiple popliteal pterygia leading to severe arthrogryposis, ankyloblepharon filiforme adnatum, filiform bands between the jaws, synostosis of the carpal/tarsal and phalangeal bones in the hands and feet, digital hypoplasia/aplasia, complete soft-tissue syndactyly, lack of nails, lack of scalp hair, eyebrows and eyelashes, blepharophimosis, cleft lip and/or palate, and hypoplastic external genitalia. Early lethality is common, although survival into childhood and beyond has been reported. SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. SIMILARITY: Contains 10 ANK repeats. SIMILARITY: Contains 1 protein kinase domain.
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.
ModBase Predicted Comparative 3D Structure on P57078
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.
Biological Process: GO:0002009 morphogenesis of an epithelium GO:0006468 protein phosphorylation GO:0016310 phosphorylation GO:0051092 positive regulation of NF-kappaB transcription factor activity