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Entry version 171 (13 Feb 2019)
Sequence version 2 (07 Jun 2005)
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Protein

E3 ubiquitin-protein ligase UHRF1

Gene

Uhrf1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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.8 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine. EC:2.3.2.27

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei321Histone H3K4me0By similarity1
Binding sitei332Histone H3R2me0By similarity1
Binding sitei335Histone H3R2me0By similarity1
Binding sitei474MethylcytosineBy similarity1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei484Required to confer preferential recognition of cytosine over thymineBy similarity1
Sitei494Required to discriminate between hemimethylated DNA versus symmetrically methylated DNA1
Sitei496Required for affinity and specificity for 5-mCpG sequence1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri304 – 371PHD-typePROSITE-ProRule annotationAdd BLAST68
Zinc fingeri713 – 752RING-typePROSITE-ProRule annotationAdd BLAST40

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionChromatin regulator, DNA-binding, Repressor, Transferase
Biological processCell cycle, DNA damage, DNA repair, Transcription, Transcription regulation, Ubl conjugation pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00143

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
E3 ubiquitin-protein ligase UHRF1 (EC:2.3.2.27)
Alternative name(s):
Nuclear protein 95
Nuclear zinc finger protein Np95
RING-type E3 ubiquitin transferase UHRF1
Ubiquitin-like PHD and RING finger domain-containing protein 1
Short name:
mUhrf1
Ubiquitin-like-containing PHD and RING finger domains protein 1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Uhrf1
Synonyms:Np95
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 17

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:1338889 Uhrf1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Mice display a sensitization to DNA damage and replication block, and die in mid-gestation.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi148F → A: Abolishes binding to histone H3K9me3 and ability to repress transcription of target genes. 1 Publication1
Mutagenesisi730H → A: Abolishes enzymatic activity. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000561451 – 782E3 ubiquitin-protein ligase UHRF1Add BLAST782

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei76PhosphoserineBy similarity1
Modified residuei91PhosphoserineBy similarity1
Modified residuei93PhosphoserineBy similarity1
Modified residuei95PhosphoserineBy similarity1
Modified residuei161PhosphoserineCombined sources1
Modified residuei303Phosphoserine; by PKABy similarity1
Modified residuei373PhosphoserineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki390Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei404N6-acetyllysineBy similarity1
Modified residuei519PhosphoserineCombined sources1
Modified residuei550N6-acetyllysine; alternateBy similarity1
Cross-linki550Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei639Phosphoserine; by CDK1By similarity1
Modified residuei649PhosphoserineBy similarity1
Modified residuei656PhosphoserineCombined sources1
Cross-linki664Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei759PhosphoserineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylation at Ser-303 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 (By similarity).By similarity
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.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q8VDF2

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q8VDF2

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q8VDF2

PeptideAtlas

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PeptideAtlasi
Q8VDF2

PRoteomics IDEntifications database

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PRIDEi
Q8VDF2

2D gel databases

REPRODUCTION-2DPAGE

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REPRODUCTION-2DPAGEi
Q8VDF2

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q8VDF2

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
Q8VDF2

SwissPalm database of S-palmitoylation events

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SwissPalmi
Q8VDF2

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in thymus, testis, spleen and lung. Within testis, expressed in almost all cells except elongated spermatids.2 Publications

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Up-regulated in proliferating cells, and down-regulated in quiescent or differentiated cells. Early induced by E1A in post-mitotic cells. Down-regulated by aphidicolin.4 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000001228 Expressed in 255 organ(s), highest expression level in primary oocyte

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q8VDF2 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q8VDF2 MM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with DNMT1; the interaction is direct. Interacts with USP7; leading to its deubiquitination. Interacts with HDAC1, but not with HDAC2. Interacts with UHRF1BP1. Interacts with PML. Interacts with EHMT2. Binds hemimethylated CpG containing oligonucleotides. Interacts with histones H3, H1 and H2B. Interacts with DNMT3A and DNMT3B (PubMed:14993289, PubMed:15361834, PubMed:17994007, PubMed:18772888, PubMed:18772891, PubMed:19056828, PubMed:19798101, PubMed:21268065). Interacts with PRAMEL7 (PubMed:28604677).9 Publications

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
201816, 26 interactors

Molecular INTeraction database

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MINTi
Q8VDF2

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000001258

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1782
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2ZKDX-ray1.60A/B404-613[»]
2ZKEX-ray2.60A404-613[»]
2ZKFX-ray2.55A404-613[»]
2ZKGX-ray1.77A/B/C/D404-613[»]
2ZO0X-ray2.19B419-628[»]
2ZO1X-ray1.96B419-628[»]
2ZO2X-ray3.09B419-628[»]
3F8IX-ray2.29A/B419-628[»]
3F8JX-ray1.99B417-628[»]
3FDEX-ray1.41A/B419-628[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q8VDF2

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q8VDF2

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
Q8VDF2

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini1 – 78Ubiquitin-likePROSITE-ProRule annotationAdd BLAST78
Domaini424 – 586YDGPROSITE-ProRule annotationAdd BLAST163

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni129 – 205Tudor-like 1Add BLAST77
Regioni212 – 280Tudor-like 2Add BLAST69
Regioni293 – 306LinkerBy similarityAdd BLAST14
Regioni338 – 342Histone H3R2me0 bindingBy similarity5
Regioni358 – 360Histone H3R2me0 bindingBy similarity3
Regioni450 – 451Required to promote base flipping2
Regioni468 – 469Methylcytosine bindingBy similarity2
Regioni471 – 474Required for formation of a 5-methylcytosine-binding pocket4
Regioni483 – 486Required for formation of a 5-methylcytosine-binding pocket4

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

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). 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.1 Publication
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:17994007). The YDG domain 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:18772888). The YDG domain also recognizes and binds 5-hydroxymethylcytosine (5hmC).2 Publications
The RING finger is required for ubiquitin ligase activity.

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri304 – 371PHD-typePROSITE-ProRule annotationAdd BLAST68
Zinc fingeri713 – 752RING-typePROSITE-ProRule annotationAdd BLAST40

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410IFAP Eukaryota
COG3440 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00390000008296

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000124662

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG059298

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q8VDF2

KEGG Orthology (KO)

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KOi
K10638

Identification of Orthologs from Complete Genome Data

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OMAi
DECDMAY

Database of Orthologous Groups

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OrthoDBi
705927at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q8VDF2

TreeFam database of animal gene trees

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TreeFami
TF106434

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.30.280.10, 1 hit
3.30.40.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR015947 PUA-like_sf
IPR036987 SRA-YDG_sf
IPR003105 SRA_YDG
IPR021991 TTD_dom
IPR029071 Ubiquitin-like_domsf
IPR000626 Ubiquitin_dom
IPR011011 Znf_FYVE_PHD
IPR001965 Znf_PHD
IPR019787 Znf_PHD-finger
IPR001841 Znf_RING
IPR013083 Znf_RING/FYVE/PHD
IPR017907 Znf_RING_CS

Pfam protein domain database

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Pfami
View protein in Pfam
PF00628 PHD, 1 hit
PF02182 SAD_SRA, 1 hit
PF12148 TTD, 1 hit
PF00240 ubiquitin, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00249 PHD, 1 hit
SM00184 RING, 2 hits
SM00466 SRA, 1 hit
SM00213 UBQ, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF54236 SSF54236, 1 hit
SSF57903 SSF57903, 1 hit
SSF88697 SSF88697, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS50053 UBIQUITIN_2, 1 hit
PS51015 YDG, 1 hit
PS01359 ZF_PHD_1, 1 hit
PS50016 ZF_PHD_2, 1 hit
PS00518 ZF_RING_1, 1 hit
PS50089 ZF_RING_2, 2 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 1 (identifier: Q8VDF2-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

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MWIQVRTMDG KETHTVNSLS RLTKVQELRK KIEEVFHVEP QLQRLFYRGK
60 70 80 90 100
QMEDGHTLFD YDVRLNDTIQ LLVRQSLALP LSTKERDSEL SDSDSGYGVG
110 120 130 140 150
HSESDKSSTH GEGAAEADDK TVWEDTDLGL YKVNEYVDVR DNIFGAWFEA
160 170 180 190 200
QVVQVQKRAL SEDEPCSSSA VKTSEDDIMY HVKYDDYPEH GVDIVKAKNV
210 220 230 240 250
RARARTVIPW ENLEVGQVVM ANYNVDYPRK RGFWYDVEIC RKRQTRTARE
260 270 280 290 300
LYGNIRLLND SQLNNCRIMF VDEVLMIELP KERRPLIASP SQPPPALRNT
310 320 330 340 350
GKSGPSCRFC KDDENKPCRK CACHVCGGRE APEKQLLCDE CDMAFHLYCL
360 370 380 390 400
KPPLTSVPPE PEWYCPSCRT DSSEVVQAGE KLKESKKKAK MASATSSSRR
410 420 430 440 450
DWGKGMACVG RTTECTIVPA NHFGPIPGVP VGTMWRFRVQ VSESGVHRPH
460 470 480 490 500
VAGIHGRSND GAYSLVLAGG YEDDVDNGNY FTYTGSGGRD LSGNKRTAGQ
510 520 530 540 550
SSDQKLTNNN RALALNCHSP INEKGAEAED WRQGKPVRVV RNMKGGKHSK
560 570 580 590 600
YAPAEGNRYD GIYKVVKYWP ERGKSGFLVW RYLLRRDDTE PEPWTREGKD
610 620 630 640 650
RTRQLGLTMQ YPEGYLEALA NKEKSRKRPA KALEQGPSSS KTGKSKQKST
660 670 680 690 700
GPTLSSPRAS KKSKLEPYTL SEQQANLIKE DKGNAKLWDD VLTSLQDGPY
710 720 730 740 750
QIFLSKVKEA FQCICCQELV FRPVTTVCQH NVCKDCLDRS FRAQVFSCPA
760 770 780
CRFELDHSSP TRVNQPLQTI LNQLFPGYGS GR
Length:782
Mass (Da):88,304
Last modified:June 7, 2005 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iDC5EEDFCDF69619B
GO
Isoform 2 (identifier: Q8VDF2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     293-301: PPPALRNTG → R

Show »
Length:774
Mass (Da):87,556
Checksum:i64752A7950497454
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E9Q5Y5E9Q5Y5_MOUSE
E3 ubiquitin-protein ligase UHRF1
Uhrf1
146Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti104S → P in BAE30624 (PubMed:16141072).Curated1
Sequence conflicti118D → G in BAE31708 (PubMed:16141072).Curated1
Sequence conflicti118D → G in BAE31605 (PubMed:16141072).Curated1
Sequence conflicti118D → G in BAE30730 (PubMed:16141072).Curated1
Sequence conflicti118D → G in BAE29605 (PubMed:16141072).Curated1
Sequence conflicti214E → K in BAB79496 (PubMed:12084726).Curated1
Sequence conflicti449P → L in BAB79496 (PubMed:12084726).Curated1
Sequence conflicti455 – 456HG → PW in BAB79496 (PubMed:12084726).Curated2
Sequence conflicti471Y → H in BAE27560 (PubMed:16141072).Curated1
Sequence conflicti637P → A in BAE26398 (PubMed:16141072).Curated1
Sequence conflicti702I → V in BAE31708 (PubMed:16141072).Curated1
Sequence conflicti702I → V in BAE31605 (PubMed:16141072).Curated1
Sequence conflicti702I → V in BAE30730 (PubMed:16141072).Curated1
Sequence conflicti702I → V in BAE29605 (PubMed:16141072).Curated1
Sequence conflicti753F → Y in AAH22167 (PubMed:15489334).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_044395293 – 301PPPALRNTG → R in isoform 2. 1 Publication9

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
D87908 mRNA Translation: BAA74579.1
AF274046 mRNA Translation: AAK55743.1
AK075819 mRNA Translation: BAC35985.1
AK143688 mRNA Translation: BAE25499.1
AK145376 mRNA Translation: BAE26398.1
AK145543 mRNA Translation: BAE26496.1
AK146951 mRNA Translation: BAE27560.1
AK147046 mRNA Translation: BAE27632.1
AK150489 mRNA Translation: BAE29605.1
AK151701 mRNA Translation: BAE30624.1
AK151837 mRNA Translation: BAE30730.1
AK152930 mRNA Translation: BAE31605.1
AK153083 mRNA Translation: BAE31708.1
AC026385 Genomic DNA No translation available.
BC022167 mRNA Translation: AAH22167.1
AB066246 Genomic DNA Translation: BAB79496.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS28903.1 [Q8VDF2-1]
CCDS50151.1 [Q8VDF2-2]

NCBI Reference Sequences

More...
RefSeqi
NP_001104548.1, NM_001111078.1 [Q8VDF2-1]
NP_001104549.1, NM_001111079.1 [Q8VDF2-2]
NP_001104550.1, NM_001111080.1 [Q8VDF2-2]
NP_035061.3, NM_010931.3 [Q8VDF2-1]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Mm.42196

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000001258; ENSMUSP00000001258; ENSMUSG00000001228 [Q8VDF2-1]
ENSMUST00000113035; ENSMUSP00000108658; ENSMUSG00000001228 [Q8VDF2-2]
ENSMUST00000113038; ENSMUSP00000108661; ENSMUSG00000001228 [Q8VDF2-2]
ENSMUST00000113039; ENSMUSP00000108662; ENSMUSG00000001228 [Q8VDF2-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
18140

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:18140

UCSC genome browser

More...
UCSCi
uc008dbp.2 mouse [Q8VDF2-1]
uc008dbq.2 mouse [Q8VDF2-2]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D87908 mRNA Translation: BAA74579.1
AF274046 mRNA Translation: AAK55743.1
AK075819 mRNA Translation: BAC35985.1
AK143688 mRNA Translation: BAE25499.1
AK145376 mRNA Translation: BAE26398.1
AK145543 mRNA Translation: BAE26496.1
AK146951 mRNA Translation: BAE27560.1
AK147046 mRNA Translation: BAE27632.1
AK150489 mRNA Translation: BAE29605.1
AK151701 mRNA Translation: BAE30624.1
AK151837 mRNA Translation: BAE30730.1
AK152930 mRNA Translation: BAE31605.1
AK153083 mRNA Translation: BAE31708.1
AC026385 Genomic DNA No translation available.
BC022167 mRNA Translation: AAH22167.1
AB066246 Genomic DNA Translation: BAB79496.1
CCDSiCCDS28903.1 [Q8VDF2-1]
CCDS50151.1 [Q8VDF2-2]
RefSeqiNP_001104548.1, NM_001111078.1 [Q8VDF2-1]
NP_001104549.1, NM_001111079.1 [Q8VDF2-2]
NP_001104550.1, NM_001111080.1 [Q8VDF2-2]
NP_035061.3, NM_010931.3 [Q8VDF2-1]
UniGeneiMm.42196

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2ZKDX-ray1.60A/B404-613[»]
2ZKEX-ray2.60A404-613[»]
2ZKFX-ray2.55A404-613[»]
2ZKGX-ray1.77A/B/C/D404-613[»]
2ZO0X-ray2.19B419-628[»]
2ZO1X-ray1.96B419-628[»]
2ZO2X-ray3.09B419-628[»]
3F8IX-ray2.29A/B419-628[»]
3F8JX-ray1.99B417-628[»]
3FDEX-ray1.41A/B419-628[»]
ProteinModelPortaliQ8VDF2
SMRiQ8VDF2
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201816, 26 interactors
MINTiQ8VDF2
STRINGi10090.ENSMUSP00000001258

PTM databases

iPTMnetiQ8VDF2
PhosphoSitePlusiQ8VDF2
SwissPalmiQ8VDF2

2D gel databases

REPRODUCTION-2DPAGEiQ8VDF2

Proteomic databases

EPDiQ8VDF2
jPOSTiQ8VDF2
PaxDbiQ8VDF2
PeptideAtlasiQ8VDF2
PRIDEiQ8VDF2

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000001258; ENSMUSP00000001258; ENSMUSG00000001228 [Q8VDF2-1]
ENSMUST00000113035; ENSMUSP00000108658; ENSMUSG00000001228 [Q8VDF2-2]
ENSMUST00000113038; ENSMUSP00000108661; ENSMUSG00000001228 [Q8VDF2-2]
ENSMUST00000113039; ENSMUSP00000108662; ENSMUSG00000001228 [Q8VDF2-1]
GeneIDi18140
KEGGimmu:18140
UCSCiuc008dbp.2 mouse [Q8VDF2-1]
uc008dbq.2 mouse [Q8VDF2-2]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
29128
MGIiMGI:1338889 Uhrf1

Phylogenomic databases

eggNOGiENOG410IFAP Eukaryota
COG3440 LUCA
GeneTreeiENSGT00390000008296
HOGENOMiHOG000124662
HOVERGENiHBG059298
InParanoidiQ8VDF2
KOiK10638
OMAiDECDMAY
OrthoDBi705927at2759
PhylomeDBiQ8VDF2
TreeFamiTF106434

Enzyme and pathway databases

UniPathwayi
UPA00143

Miscellaneous databases

EvolutionaryTraceiQ8VDF2

Protein Ontology

More...
PROi
PR:Q8VDF2

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000001228 Expressed in 255 organ(s), highest expression level in primary oocyte
ExpressionAtlasiQ8VDF2 baseline and differential
GenevisibleiQ8VDF2 MM

Family and domain databases

Gene3Di2.30.280.10, 1 hit
3.30.40.10, 1 hit
InterProiView protein in InterPro
IPR015947 PUA-like_sf
IPR036987 SRA-YDG_sf
IPR003105 SRA_YDG
IPR021991 TTD_dom
IPR029071 Ubiquitin-like_domsf
IPR000626 Ubiquitin_dom
IPR011011 Znf_FYVE_PHD
IPR001965 Znf_PHD
IPR019787 Znf_PHD-finger
IPR001841 Znf_RING
IPR013083 Znf_RING/FYVE/PHD
IPR017907 Znf_RING_CS
PfamiView protein in Pfam
PF00628 PHD, 1 hit
PF02182 SAD_SRA, 1 hit
PF12148 TTD, 1 hit
PF00240 ubiquitin, 1 hit
SMARTiView protein in SMART
SM00249 PHD, 1 hit
SM00184 RING, 2 hits
SM00466 SRA, 1 hit
SM00213 UBQ, 1 hit
SUPFAMiSSF54236 SSF54236, 1 hit
SSF57903 SSF57903, 1 hit
SSF88697 SSF88697, 1 hit
PROSITEiView protein in PROSITE
PS50053 UBIQUITIN_2, 1 hit
PS51015 YDG, 1 hit
PS01359 ZF_PHD_1, 1 hit
PS50016 ZF_PHD_2, 1 hit
PS00518 ZF_RING_1, 1 hit
PS50089 ZF_RING_2, 2 hits

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiUHRF1_MOUSE
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q8VDF2
Secondary accession number(s): Q3U9D7
, Q3U9P2, Q3UI74, Q3UIE6, Q3ULF2, Q3ULQ0, Q8C6F1, Q8VIA1, Q9Z1H6
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: February 13, 2019
This is version 171 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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