| Tbio | E3 ubiquitin-protein ligase UHRF2 |
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. E3 SUMO-, but not ubiquitin-, protein ligase for ZNF131.
This gene encodes a nuclear protein which is involved in cell-cycle regulation. The encoded protein is a ubiquitin-ligase capable of ubiquinating PCNP (PEST-containing nuclear protein), and together they may play a role in tumorigenesis. The encoded protein contains an NIRF_N domain, a PHD finger, a set- and ring-associated (SRA) domain, and a RING finger domain and several of these domains have been shown to be essential for the regulation of cell proliferation. This protein may also have a role in intranuclear degradation of polyglutamine aggregates. Alternative splicing results in multiple transcript variants some of which are non-protein coding. [provided by RefSeq, Feb 2012]
This gene encodes a nuclear protein which is involved in cell-cycle regulation. The encoded protein is a ubiquitin-ligase capable of ubiquinating PCNP (PEST-containing nuclear protein), and together they may play a role in tumorigenesis. The encoded protein contains an NIRF_N domain, a PHD finger, a set- and ring-associated (SRA) domain, and a RING finger domain and several of these domains have been shown to be essential for the regulation of cell proliferation. This protein may also have a role in intranuclear degradation of polyglutamine aggregates. Alternative splicing results in multiple transcript variants some of which are non-protein coding. [provided by RefSeq, Feb 2012]
Comments
| Disease | Target Count | P-value |
|---|---|---|
| juvenile dermatomyositis | 1189 | 3.36987686181231E-13 |
| ovarian cancer | 8492 | 1.60965986357611E-7 |
| primary pancreatic ductal adenocarcinoma | 1271 | 0.0161154788558845 |
| Disease | Target Count | Z-score | Confidence |
|---|---|---|---|
| Rheumatoid Arthritis | 1171 | 0.0 | 1.0 |
| Disease | log2 FC | p |
|---|---|---|
| juvenile dermatomyositis | 1.153 | 0.000 |
| primary pancreatic ductal adenocarcinoma | 1.016 | 0.016 |
| ovarian cancer | -1.800 | 0.000 |
| Species | Source |
|---|---|
| Chimp | OMA EggNOG |
| Macaque | OMA EggNOG |
| Mouse | OMA EggNOG Inparanoid |
| Rat | OMA EggNOG Inparanoid |
| Dog | OMA EggNOG Inparanoid |
| Horse | OMA Inparanoid |
| Cow | OMA EggNOG |
| Opossum | OMA EggNOG Inparanoid |
| Anole lizard | OMA Inparanoid |
| Xenopus | OMA EggNOG Inparanoid |
| PMID | Text |
|---|---|
| 24813944 | A hydrogen bond between the hydroxyl group of 5hmC and UHRF2-SRA is critical for their preferential binding. |
| 24573556 | UHRF2 may contribute to the progression of colon carcinogenesis and function as a novel prognostic indicator after curative operation |
| 23833190 | UHRF2 is a transcriptional target of E2F, that it directly interacts with E2F1. |
| 23537643 | UHRF2, the homolog of UHRF1, interacts with N-methylpurine DNA glycosylase (MPG) in cancer cells. |
| 23404503 | UHRF2, a ubiquitin E3 ligase, acts as a small ubiquitin-like modifier E3 ligase for zinc finger protein 131 |
| 23244124 | Low UHRF2 mRNA expression is associated with malignant glioma. |
| 22673569 | NIRF may contribute to the coupling between the cell cycle network and the epigenetic landscape |
| 22072112 | In the present study, ubiquitin ligase, NIRF, binds to hepatitis B virus core protein and leads to the proteasome-mediated degradation of hepatitis B virus core protein in vivo. |
| 22018986 | NIRF is frequently upregulated in colorectal cancer and its oncogenicity can be suppressed by let-7a microRNA. |
| 21952639 | NIRF is immediately adjacent to the single nucleotide polymorphism rs719725, which is reportedly associated with the risk of colorectal cancer. |
| More... |
MWIQVRTIDGSKTCTIEDVSRKATIEELRERVWALFDVRPECQRLFYRGKQLENGYTLFDYDVGLNDIIQ 1 - 70 LLVRPDPDHLPGTSTQIEAKPCSNSPPKVKKAPRVGPSNQPSTSARARLIDPGFGIYKVNELVDARDVGL 71 - 140 GAWFEAHIHSVTRASDGQSRGKTPLKNGSSCKRTNGNIKHKSKENTNKLDSVPSTSNSDCVAADEDVIYH 141 - 210 IQYDEYPESGTLEMNVKDLRPRARTILKWNELNVGDVVMVNYNVESPGQRGFWFDAEITTLKTISRTKKE 211 - 280 LRVKIFLGGSEGTLNDCKIISVDEIFKIERPGAHPLSFADGKFLRRNDPECDLCGGDPEKKCHSCSCRVC 281 - 350 GGKHEPNMQLLCDECNVAYHIYCLNPPLDKVPEEEYWYCPSCKTDSSEVVKAGERLKMSKKKAKMPSAST 351 - 420 ESRRDWGRGMACVGRTRECTIVPSNHYGPIPGIPVGSTWRFRVQVSEAGVHRPHVGGIHGRSNDGAYSLV 421 - 490 LAGGFADEVDRGDEFTYTGSGGKNLAGNKRIGAPSADQTLTNMNRALALNCDAPLDDKIGAESRNWRAGK 491 - 560 PVRVIRSFKGRKISKYAPEEGNRYDGIYKVVKYWPEISSSHGFLVWRYLLRRDDVEPAPWTSEGIERSRR 561 - 630 LCLRLQYPAGYPSDKEGKKPKGQSKKQPSGTTKRPISDDDCPSASKVYKASDSAEAIEAFQLTPQQQHLI 631 - 700 REDCQNQKLWDEVLSHLVEGPNFLKKLEQSFMCVCCQELVYQPVTTECFHNVCKDCLQRSFKAQVFSCPA 701 - 770 CRHDLGQNYIMIPNEILQTLLDLFFPGYSKGR 771 - 802 //
| PMID | Year | Title |
|---|---|---|
| 24813944 | 2014 | Structural basis for hydroxymethylcytosine recognition by the SRA domain of UHRF2. |
| 24573556 | 2014 | Ubiquitin-like with PHD and ring finger domains 2 is a predictor of survival and a potential therapeutic target in colon cancer. |
| 23833190 | 2013 | The nuclear protein UHRF2 is a direct target of the transcription factor E2F1 in the induction of apoptosis. |
| 23537643 | 2013 | Identification of UHRF1/2 as new N-methylpurine DNA glycosylase-interacting proteins. |
| 23404503 | 2013 | UHRF2, a ubiquitin E3 ligase, acts as a small ubiquitin-like modifier E3 ligase for zinc finger protein 131. |
| 23244124 | 2012 | UHRF2 mRNA expression is low in malignant glioma but silencing inhibits the growth of U251 glioma cells in vitro. |
| 23186163 | 2013 | Toward a comprehensive characterization of a human cancer cell phosphoproteome. |
| 22699663 | 2012 | Genome-wide association study of periodontal pathogen colonization. |
| 22673569 | 2012 | NIRF/UHRF2 occupies a central position in the cell cycle network and allows coupling with the epigenetic landscape. |
| 22072112 | 2012 | NIRF, a novel ubiquitin ligase, interacts with hepatitis B virus core protein and promotes its degradation. |
| More... |
