ID:RNF31_HUMAN DESCRIPTION: RecName: Full=E3 ubiquitin-protein ligase RNF31; EC=6.3.2.-; AltName: Full=HOIL-1-interacting protein; Short=HOIP; AltName: Full=RING finger protein 31; AltName: Full=Zinc in-between-RING-finger ubiquitin-associated domain protein; FUNCTION: E3 ubiquitin-protein ligase component of the LUBAC complex which conjugates linear ('M-1'-linked) polyubiquitin chains to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation. LUBAC conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways. Linear ubiquitination mediated by the LUBAC complex interferes with TNF- induced cell death and thereby prevents inflammation. LUBAC is proposed to be recruited to the TNF-R1 signaling complex (TNF-RSC) following polyubiquitination of TNF-RSC components by BIRC2 and/or BIRC3 and to conjugate linear polyubiquitin to IKBKG and possibly other components contributing to the stability of the complex. Binds polyubiquitin of different linkage types. SUBUNIT: Interacts with MUSK (By similarity). Component of the LUBAC complex (linear ubiquitin chain assembly complex) which consists of SHARPIN, RBCK1 and RNF31. LUBAC has a MW of approximative 600 kDa suggesting a heteromultimeric assembly of its subunits. Associates with the TNF-R1 signaling complex (TNF- RSC) in a stimulation-dependent manner. INTERACTION: Q9QYP6:Azi2 (xeno); NbExp=2; IntAct=EBI-948111, EBI-6115874; P84022:SMAD3; NbExp=2; IntAct=EBI-948111, EBI-347161; Q4VA12:Traf1 (xeno); NbExp=2; IntAct=EBI-948111, EBI-6116765; SUBCELLULAR LOCATION: Cytoplasm (By similarity). TISSUE SPECIFICITY: Expressed in both normal and transformed breast epithelial cell lines. DOMAIN: The RanBP2-type zinc fingers mediate the specific interaction with ubiquitin. DOMAIN: The UBA domain mediates association with RBCK1/HOIL1 via interaction with its UBL domain. DOMAIN: RING 1 and IBR zinc-fingers catalyze the first step transfer of ubiquitin from the E2 onto RING 2, to transiently form a HECT-like covalent thioester intermediate. DOMAIN: The linear ubiquitin chain determining domain (LDD) mediates the final transfer of ubiquitin from RING 2 onto the N- terminus of a target ubiquitin. SIMILARITY: Contains 1 IBR-type zinc finger. SIMILARITY: Contains 3 RanBP2-type zinc fingers. SIMILARITY: Contains 2 RING-type zinc fingers. SIMILARITY: Contains 1 UBA domain. SEQUENCE CAUTION: Sequence=BAB15675.1; Type=Erroneous termination; Positions=1060; Note=Translated as Glu; Sequence=BAB15675.1; Type=Frameshift; Positions=1036; Sequence=BAB15675.1; Type=Miscellaneous discrepancy; Note=Intron retention; Sequence=BAB70948.1; Type=Erroneous initiation;
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 Q96EP0
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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.
US Server
Sequence and Links to Tools and Databases 
Common Gene Haplotype Alleles 
