human UHRF1 shRNA silencing Adenovirus

E3 ubiquitin-protein ligase UHRF1; hNP95; hUHRF1; huNp95; ICBP90; inverted CCAAT box-binding protein of 90 kDa; Np95; nuclear phosphoprotein 95; nuclear protein 95; nuclear zinc finger protein Np95; RING finger protein 106; RING-type E3 ubiquitin transferase UHRF1; RNF106; TDRD22; transcription factor ICBP90; ubiquitin-like PHD and RING finger domain-containing protein 1; Ubiquitin-like-containing PHD and RING finger domains protein 1

NP95/UHRF1 was originally identified as ICBP90 (inverted CCAAT box-binding protein of 90 kDa) in a one-hybrid screen for proteins that bind the topoisomerase IIalpha gene promoter. NP95/UHRF1 is a heterochromatin binding protein that directly interacts with histones and has proposed roles in the DNA damage response, heterochromatin formation, and cell replication. Structurally, NP95/UHRF1 contains an ubiquitin-like domain (NIRF_N), a plant homeodomain (PHD), a SRA domain, and a RING domain. The RING domain imparts ubiquitin E3 ligase activity that is histone-specific. This E3 ligase activity is proposed to be important to tumor growth. NP95/UHRF1 expression begins in the G1/S phase and continues through mitosis. It has been shown to be required for entry from G1/G0 as well as the G1/S transition in some cell types. NP95/UHRF1 has been found to be part of the pericentric heterochromatin duplication body (pHDB) and involved in the replication and formation of heterochromatin.

UHRF1 encodes a member of a subfamily of RING-finger type E3 ubiquitin ligases. The protein binds to specific DNA sequences, and recruits a histone deacetylase to regulate gene expression. Its expression peaks at late G1 phase and continues during G2 and M phases of the cell cycle. It plays a major role in the G1/S transition by regulating topoisomerase IIalpha and retinoblastoma gene expression, and functions in the p53-dependent DNA damage checkpoint. Multiple transcript variants encoding different isoforms have been found for this gene.

29128

ubiquitin like with PHD and ring finger domains 1

ubiquitin like with PHD and ring finger domains 1

UHRF1

HGNC:12556

9606.0

2421

2421 bp

E3 ubiquitin-protein ligase UHRF1

NM_013282

NM_013282, NM_001290052, NM_001290051, NM_001290050, NM_001048201, BC113875,

Cancer,Cell Cycle,DNA Damage/Repair,Epigenetic Regulation of Gene Expression,Histone Modification,Immunology,Replication,Transcription Factor/Regulator,Tumor Suppressors/Oncoproteins,Ubiquitination,Zinc-finger

cancer,cell_biology,cell_cycle,genetics,transcription_translation,immunology

human

NP95/UHRF1 was originally identified as ICBP90 (inverted CCAAT box-binding protein of 90 kDa) in a one-hybrid screen for proteins that bind the topoisomerase IIalpha gene promoter. NP95/UHRF1 is a heterochromatin binding protein that directly interacts with histones and has proposed roles in the DNA damage response, heterochromatin formation, and cell replication. Structurally, NP95/UHRF1 contains an ubiquitin-like domain (NIRF_N), a plant homeodomain (PHD), a SRA domain, and a RING domain. The RING domain imparts ubiquitin E3 ligase activity that is histone-specific. This E3 ligase activity is proposed to be important to tumor growth. NP95/UHRF1 expression begins in the G1/S phase and continues through mitosis. It has been shown to be required for entry from G1/G0 as well as the G1/S transition in some cell types. NP95/UHRF1 has been found to be part of the pericentric heterochromatin duplication body (pHDB) and involved in the replication and formation of heterochromatin.

Hs.108106

Q96T88