Product: UHRF1 Antibody
Catalog: AF6553
Description: Rabbit polyclonal antibody to UHRF1
Application: WB IF/ICC
Reactivity: Human, Mouse, Rat
Mol.Wt.: 90kD(Calculated).
Uniprot: Q96T88
RRID: AB_2847277

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 100ul $280 In stock
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Product Info

Source:
Rabbit
Application:
WB 1:500-1:2000, IF/ICC 1:100-1:500
*The optimal dilutions should be determined by the end user.
*Tips:

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Reactivity:
Human,Mouse,Rat
Clonality:
Polyclonal
Specificity:
UHRF1 Antibody detects endogenous levels of total UHRF1.
RRID:
AB_2847277
Cite Format: Affinity Biosciences Cat# AF6553, RRID:AB_2847277.
Conjugate:
Unconjugated.
Purification:
The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin (Thermo Fisher Scientific).
Storage:
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.
Alias:

Fold/Unfold

Ac2-121; AL022808; E3 ubiquitin-protein ligase UHRF1; EC 6.3.2.-; FLJ21925; hNP95; hUHRF1; HuNp95; ICBP90; Inverted CCAAT box binding protein of 90 kDa; Inverted CCAAT box binding protein, 90-kD; Inverted CCAAT box-binding protein of 90 kDa; Liver regeneration-related protein LRRG126; MGC138707; NP95; Nuclear phosphoprotein 95; Nuclear phosphoprotein, 95-KD; Nuclear protein 95; Nuclear zinc finger protein Np95; RING finger protein 106; RNF106; TDRD22; Transcription factor ICBP90; Ubiquitin like containing PHD and RING finger domains protein 1; Ubiquitin like PHD and RING finger domain containing protein 1; Ubiquitin-like PHD and RING finger domain-containing protein 1; Ubiquitin-like protein containing PHD and RING finger domains 1; Ubiquitin-like with PHD and ring finger domains 1; Ubiquitin-like, containing PHD and RING finger domains, 1; Ubiquitin-like-containing PHD and RING finger domains protein 1; UHRF1; UHRF1_HUMAN;

Immunogens

Immunogen:

A synthesized peptide derived from human UHRF1.

Uniprot:
Gene(ID):
Expression:
Q96T88 UHRF1_HUMAN:

Expressed in thymus, bone marrow, testis, lung and heart. Overexpressed in breast cancer.

Sequence:
MWIQVRTMDGRQTHTVDSLSRLTKVEELRRKIQELFHVEPGLQRLFYRGKQMEDGHTLFDYEVRLNDTIQLLVRQSLVLPHSTKERDSELSDTDSGCCLGQSESDKSSTHGEAAAETDSRPADEDMWDETELGLYKVNEYVDARDTNMGAWFEAQVVRVTRKAPSRDEPCSSTSRPALEEDVIYHVKYDDYPENGVVQMNSRDVRARARTIIKWQDLEVGQVVMLNYNPDNPKERGFWYDAEISRKRETRTARELYANVVLGDDSLNDCRIIFVDEVFKIERPGEGSPMVDNPMRRKSGPSCKHCKDDVNRLCRVCACHLCGGRQDPDKQLMCDECDMAFHIYCLDPPLSSVPSEDEWYCPECRNDASEVVLAGERLRESKKKAKMASATSSSQRDWGKGMACVGRTKECTIVPSNHYGPIPGIPVGTMWRFRVQVSESGVHRPHVAGIHGRSNDGAYSLVLAGGYEDDVDHGNFFTYTGSGGRDLSGNKRTAEQSCDQKLTNTNRALALNCFAPINDQEGAEAKDWRSGKPVRVVRNVKGGKNSKYAPAEGNRYDGIYKVVKYWPEKGKSGFLVWRYLLRRDDDEPGPWTKEGKDRIKKLGLTMQYPEGYLEALANREREKENSKREEEEQQEGGFASPRTGKGKWKRKSAGGGPSRAGSPRRTSKKTKVEPYSLTAQQSSLIREDKSNAKLWNEVLASLKDRPASGSPFQLFLSKVEETFQCICCQELVFRPITTVCQHNVCKDCLDRSFRAQVFSCPACRYDLGRSYAMQVNQPLQTVLNQLFPGYGNGR

PTMs - Q96T88 As Substrate

Site PTM Type Enzyme
T13 Phosphorylation
K24 Sumoylation
K24 Ubiquitination
K31 Ubiquitination
K50 Ubiquitination
T68 Phosphorylation
S76 Phosphorylation
K84 Ubiquitination
S88 Phosphorylation
S91 Phosphorylation
T93 Phosphorylation
S95 Phosphorylation P48730 (CSNK1D)
S104 Phosphorylation
S108 Phosphorylation
T117 Phosphorylation
S119 Phosphorylation
K136 Ubiquitination
S165 Phosphorylation
K233 Ubiquitination
S265 Phosphorylation
S287 Phosphorylation
S298 Phosphorylation P17612 (PRKACA)
K303 Ubiquitination
K306 Ubiquitination
S368 Phosphorylation
K385 Sumoylation
K385 Ubiquitination
S393 Phosphorylation
K399 Acetylation
K399 Sumoylation
K399 Ubiquitination
K408 Ubiquitination
Y418 Phosphorylation
T492 Phosphorylation
S496 Phosphorylation
C497 S-Nitrosylation
K500 Sumoylation
K500 Ubiquitination
K525 Sumoylation
K525 Ubiquitination
K531 Sumoylation
K546 Acetylation
K546 Sumoylation
K546 Ubiquitination
K560 Ubiquitination
K563 Sumoylation
K563 Ubiquitination
K568 Ubiquitination
K570 Sumoylation
K570 Ubiquitination
K592 Ubiquitination
K600 Sumoylation
K600 Ubiquitination
K626 Sumoylation
K626 Ubiquitination
S639 Phosphorylation P06493 (CDK1)
K650 Methylation
S651 Phosphorylation
R658 Methylation
S661 Phosphorylation P24941 (CDK2)
K670 Sumoylation
K670 Ubiquitination
S682 Phosphorylation
K692 Sumoylation
K692 Ubiquitination
K702 Ubiquitination
S707 Phosphorylation
S709 Phosphorylation
S751 Phosphorylation

Research Backgrounds

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.

PTMs:

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 interaction with USP7 and subsequent deubiquitination. Polyubiquitination may be stimulated by DNA damage.

Subcellular Location:

Nucleus.
Note: Localizes to replication foci. Enriched in pericentric heterochromatin. Also localizes to euchromatic regions.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Tissue Specificity:

Expressed in thymus, bone marrow, testis, lung and heart. Overexpressed in breast cancer.

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.

Family&Domains:

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 (PubMed:21489993, PubMed:21777816 and PubMed:22100450). 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 (PubMed:22837395).

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) (PubMed:17673620). 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 (PubMed:18772889). The YDG domain also recognizes and binds 5-hydroxymethylcytosine (5hmC) (PubMed:21731699).

The RING finger is required for ubiquitin ligase activity.

Restrictive clause

 

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