ICBP90 / UHRF1 Blocking Peptide | UHRF1 blocking peptide

ICBP90 / UHRF1 Immunizing Peptide

Cat. Num. AAA427844

• Gene Names: UHRF1; Np95; hNP95; ICBP90; RNF106; hUHRF1
• Reactivity: Tested: Human; Expected: Mouse, Rat, Dog
• Synonyms: ICBP90 / UHRF1; ICBP90 / UHRF1 Immunizing Peptide; Goat Anti-UHRF1 / ICBP90 Antibody; UHRF1 antibody; ubiquitin-like; containing PHD and RING finger domains; 1 antibody; Np95 antibody; ICBP90 antibody; FLJ21925 antibody; transcription factor ICBP90 antibody; RNF106 antibody; MGC138707 antibody; RING finger protein 106 antibody; inverted CCAAT box-binding protein of 90 kDa antibody; nuclear zinc finger protein Np95 antibody; ubiquitin-like with PHD and ring finger domains 1 antibody; hNP95 antibody; E3 ubiquitin-protein ligase UHRF1 antibody; UHRF1 blocking peptide

• Reactivity: Tested: Human; Expected: Mouse, Rat, Dog
• Form/Format: 100ug of dried peptide
• Sequence: NKRTAEQSCDQKLTN
• Sequence Length: 12

• Corresponding Antibody: The peptide was used in the production of MBS422968 -
• Preparation and Storage: Shipped at ambient temperature, store at -20 degree C.

NCBI and Uniprot Product Information

• NCBI GI #: 115430235
• NCBI GeneID: 29128
• NCBI Accession #: NP_001041666.1; NP_037414.3
• NCBI GenBank Nucleotide #: NM_001048201.1
• UniProt Accession #: Q96T88; Q2HIX7; Q8J022; Q9H6S6; Q9P115; Q9P1U7; A0JBR2; A8K024; B2RBA9
• Molecular Weight: 89,814 Da
• NCBI Official Full Name: E3 ubiquitin-protein ligase UHRF1 isoform 1
• NCBI Official Synonym Full Names: ubiquitin-like with PHD and ring finger domains 1
• NCBI Official Symbol: UHRF1
• NCBI Official Synonym Symbols: Np95; hNP95; ICBP90; RNF106; hUHRF1
• NCBI Protein Information: E3 ubiquitin-protein ligase UHRF1; huNp95; nuclear protein 95; RING finger protein 106; transcription factor ICBP90; nuclear zinc finger protein Np95; inverted CCAAT box-binding protein of 90 kDa; ubiquitin-like, containing PHD and RING finger domains, 1; ubiquitin-like PHD and RING finger domain-containing protein 1; ubiquitin-like-containing PHD and RING finger domains protein 1
• UniProt Protein Name: E3 ubiquitin-protein ligase UHRF1
• Protein Family: E3 ubiquitin-protein ligase
• UniProt Gene Name: UHRF1
• UniProt Synonym Gene Names: ICBP90; NP95; RNF106; HuNp95; hNp95; hUHRF1
• UniProt Entry Name: UHRF1_HUMAN

NCBI Description

This gene 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. [provided by RefSeq, Jul 2008]

Uniprot Description

Function: Multidomain protein that acts as a key epigenetic regulator by bridging DNA methylation and chromatin modification. Specifically recognizes and binds hemimethylated DNA at replication forks via its YDG domain and recruits DNMT1 methyltransferase to ensure faithful propagation of the DNA methylation patterns through DNA replication. In addition to its role in maintenance of DNA methylation, also plays a key role in chromatin modification: through its tudor-like regions and PHD-type zinc fingers, specifically recognizes and binds histone H3 trimethylated at 'Lys-9' (H3K9me3) and unmethylated at 'Arg-2' (H3R2me0), respectively, and recruits chromatin proteins. Enriched in pericentric heterochromatin where it recruits different chromatin modifiers required for this chromatin replication. Also localizes to euchromatic regions where it negatively regulates transcription possibly by impacting DNA methylation and histone modifications. Has E3 ubiquitin-protein ligase activity by mediating the ubiquitination of target proteins such as histone H3 and PML. It is still unclear how E3 ubiquitin-protein ligase activity is related to its role in chromatin in vivo. May be involved in DNA repair. Ref.1 Ref.12 Ref.13 Ref.17 Ref.19 Ref.22 Ref.28 Ref.31 Ref.42

Pathway: Protein modification; protein ubiquitination.

Subunit structure: Interacts with DNMT3A and DNMT3B

By similarity. Interacts with DNMT1; the interaction is direct. Interacts with USP7; leading to its deubiquitination. Interacts with histone H3. Interacts with HDAC1, but not with HDAC2. Interacts with UHRF1BP1. Interacts with PML. Interacts with EHMT2. Binds hemimethylated CpG containing oligonucleotides. Ref.13 Ref.17 Ref.22 Ref.28 Ref.31 Ref.34

Subcellular location: Nucleus. Note: Localizes to replication foci. Enriched in pericentric heterochromatin. Also localizes to euchromatic regions. Ref.1 Ref.17 Ref.19 Ref.22 Ref.42

Tissue specificity: Expressed in thymus, bone marrow, testis, lung and heart. Overexpressed in breast cancer. Ref.1 Ref.10 Ref.13

Developmental stage: Expressed in fetal thymus, liver and kidney. Ref.1

Induction: Up-regulated in proliferating cells, and down-regulated in quiescent cells. Down-regulated upon adriamycin-induced DNA damage, in a p53/TP53 and CDKN1A-dependent way. Induced by E2F1 transcription factor. Ref.1 Ref.10 Ref.12 Ref.13

Domain: The tudor-like regions specifically recognize and bind histone H3 unmethylated at 'Arg-2' (H3R2me0), while the PHD-type zinc finger specifically recognizes and binds histone H3 trimethylated at 'Lys-9' (H3K9me3). The tudor-like regions simultaneously recognizes H3K9me3 through a conserved aromatic cage in the first tudor-like subdomain and unmodified H3K4 (H3K4me0) within a groove between the tandem subdomains (Ref.41, Ref.42 and Ref.44). The linker region plays a role in the formation of a histone H3-binding hole between the reader modules formed by the tudor-like regions and the PHD-type zinc finger by making extended contacts with the tandem tudor-like regions (Ref.45).The YDG domain (also named SRA domain) specifically recognizes and binds hemimethylated DNA at replication forks (DNA that is only methylated on the mother strand of replicating DNA) (Ref.17). It contains a binding pocket that accommodates the 5-methylcytosine that is flipped out of the duplex DNA. 2 specialized loops reach through the resulting gap in the DNA from both the major and the minor grooves to read the other 3 bases of the CpG duplex. The major groove loop confers both specificity for the CpG dinucleotide and discrimination against methylation of deoxycytidine of the complementary strand (Ref.38). The YDG domain also recognizes and binds 5-hydroxymethylcytosine (5hmC) (Ref.29).The RING finger is required for ubiquitin ligase activity

By similarity.

Post-translational modification: Phosphorylation at Ser-298 of the linker region decreases the binding to H3K9me3. Phosphorylation at Ser-639 by CDK1 during M phase impairs interaction with USP7, preventing deubiquitination and leading to degradation by the proteasome.Ubiquitinated; which leads to proteasomal degradation. Autoubiquitinated; interaction with USP7 leads to deubiquitination and prevents degradation. Ubiquitination and degradation takes place during M phase, when phosphorylation at Ser-639 prevents intereaction with USP7 and subsequent deubiquitination. Polyubiquitination may be stimulated by DNA damage. Ref.12 Ref.19 Ref.28 Ref.34

Involvement in disease: Defects in UHRF1 may be a cause of cancers. Overexpressed in many different forms of human cancers, including bladder, breast, cervical, colorectal and prostate cancers, as well as pancreatic adenocarcinomas, rhabdomyosarcomas and gliomas. Plays an important role in the correlation of histone modification and gene silencing in cancer progression. Expression is associated with a poor prognosis in patients with various cancers, suggesting that it participates in cancer progression.

Sequence similarities: Contains 1 PHD-type zinc finger.Contains 1 RING-type zinc finger.Contains 1 ubiquitin-like domain.Contains 1 YDG domain.

Sequence caution: The sequence BAB15177.1 differs from that shown. Reason: Erroneous initiation.