ID:UHRF2_HUMAN DESCRIPTION: RecName: Full=E3 ubiquitin-protein ligase UHRF2; EC=6.3.2.-; AltName: Full=Np95/ICBP90-like RING finger protein; Short=Np95-like RING finger protein; AltName: Full=Nuclear protein 97; AltName: Full=Nuclear zinc finger protein Np97; AltName: Full=RING finger protein 107; AltName: Full=Ubiquitin-like PHD and RING finger domain-containing protein 2; AltName: Full=Ubiquitin-like-containing PHD and RING finger domains protein 2; FUNCTION: E3 ubiquitin-protein ligase that is an intermolecular hub protein in the cell cycle network. Through cooperative DNA and histone binding, may contribute to a tighter epigenetic control of gene expression in differentiated cells. Ubiquitinates cyclins, CCND1 and CCNE1, in an apparently phosphorylation-independent manner and induces G1 arrest. Also ubiquitinates PCNP leading to its degradation by the proteasome. Appears to contribute to tumorigenesis. PATHWAY: Protein modification; protein ubiquitination. SUBUNIT: Homodimer; disulfide-linked. Binds methylated CpG containing oligonucleotides. Interacts with H3: the interaction has a preference for the 'Lys-9' trimethylated form of H3 (H3K9me3) (By similarity). Interacts with PCNP, HDAC1 and CDK2 (inactive form). Component of a complex at least composed of UHRF2, CDK2 and CCNE1. Interacts directly with CCNE1; the interaction ubiquitinates CCNE1 and appears independent of CCNE1 phosphorylation. Interacts with CCND1; the interaction ubiquitinates CCND1 and appears independent of CCND1 phosphorylation. Interacts with p53/TP53 and RB1. INTERACTION: P20248:CCNA2; NbExp=2; IntAct=EBI-625304, EBI-457097; P14635:CCNB1; NbExp=2; IntAct=EBI-625304, EBI-495332; P24385:CCND1; NbExp=4; IntAct=EBI-625304, EBI-375001; P24864:CCNE1; NbExp=4; IntAct=EBI-625304, EBI-519526; P24941:CDK2; NbExp=5; IntAct=EBI-625304, EBI-375096; P06400:RB1; NbExp=4; IntAct=EBI-625304, EBI-491274; P04637:TP53; NbExp=3; IntAct=EBI-625304, EBI-366083; SUBCELLULAR LOCATION: Nucleus. Note=Enriched at pericentric heterochromatin (PH). This localization is dependent on the interaction with H3K9me3 (By similarity). INDUCTION: Up-regulated in proliferating fetal lung fibroblasts and in U-937 myeloid leukemia cells. Down-regulated in these cells by growth arrest and differentiation. In other cell types which cannot leave the cell cycle, such as tumoral HT-1080 and Hep-G2, levels are consistently up-regulated. PTM: May be autoubiquitinated; which may lead to proteasomal degradation. PTM: Phosphorylated. Phosphorylation may be mediated by CDK2. DISEASE: Note=Associated with various cancers. DNA copy number loss is found in multiple kinds of malignancies originating from the brain, breast, stomach, kidney, hematopoietic tissue and lung. SIMILARITY: Contains 1 PHD-type zinc finger. SIMILARITY: Contains 2 RING-type zinc fingers. SIMILARITY: Contains 1 ubiquitin-like domain. SIMILARITY: Contains 1 YDG domain. SEQUENCE CAUTION: Sequence=CAH74120.1; Type=Erroneous gene model prediction; Sequence=CAI13295.1; Type=Erroneous gene model prediction;
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 Q96PU4
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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 
