{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q8VDF2","secondaryAccessions":["Q3U9D7","Q3U9P2","Q3UI74","Q3UIE6","Q3ULF2","Q3ULQ0","Q8C6F1","Q8VIA1","Q9Z1H6"],"uniProtkbId":"UHRF1_MOUSE","entryAudit":{"firstPublicDate":"2005-06-07","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2005-06-07","entryVersion":207,"sequenceVersion":2},"annotationScore":5.0,"organism":{"scientificName":"Mus musculus","commonName":"Mouse","taxonId":10090,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"E3 ubiquitin-protein ligase UHRF1"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26065575"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29053958"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30392929"}],"value":"2.3.2.27"}]},"alternativeNames":[{"fullName":{"value":"Nuclear protein 95"}},{"fullName":{"value":"Nuclear zinc finger protein Np95"}},{"fullName":{"value":"Ubiquitin-like PHD and RING finger domain-containing protein 1"},"shortNames":[{"value":"mUhrf1"}]},{"fullName":{"value":"Ubiquitin-like-containing PHD and RING finger domains protein 1"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"17673620"}],"value":"Uhrf1"},"synonyms":[{"value":"Np95"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q96T88"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12058012"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12084726"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14993289"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15361834"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17673620"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17994007"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18772888"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18772891"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21268065"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21489993"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26065575"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29053958"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30392929"}],"value":"E3 ubiquitin-protein ligase that acts as a key epigenetic regulator by bridging DNA methylation and chromatin modification (PubMed:12058012, PubMed:12084726, PubMed:14993289, PubMed:17673620, PubMed:26065575, PubMed:30392929). Plays a key role in DNA methylation inheritance by promoting recruitment of DNMT1 to hemimethylated DNA and ensure faithful propagation of the DNA methylation patterns through DNA replication (PubMed:17673620, PubMed:21268065, PubMed:26065575). Acts both as a histone reader and writer: specifically recognizes and binds (1) hemimethylated DNA at replication forks and (2) histone H3 trimethylated at 'Lys-9' and unmethylated at 'Arg-2' (H3K9me3 and H3R2me0, respectively), thereby activating its E3 ubiquitin-protein ligase activity (PubMed:15361834, PubMed:17994007, PubMed:18772888, PubMed:18772891, PubMed:21489993, PubMed:26065575). UHRF1 then mediates histone H3 'Lys-18' monoubiquitination (H3K18ub), a docking site for DNMT1, leading to DNMT1 recruitment and replication-coupled DNA methylation maintenance (PubMed:26065575, PubMed:29053958, PubMed:30392929). Also mediates histone H3 'Lys-14' and 'Lys-23' ubiquitination (H3K14ub and H3K23ub) at lower level (PubMed:29053958). Histone ubiquitin ligase activity also stimulates the methyltransferase activity of SUV39H1 and/or SUV39H2, promoting accumulation of H3K9me3 histone mark to reinformce heterochromatin state (By similarity). Enriched in pericentric heterochromatin where it recruits different chromatin modifiers required for this chromatin replication (By similarity). Also localizes to euchromatic regions where it negatively regulates transcription possibly by impacting DNA methylation and histone modifications (By similarity). Plays a role in DNA repair by cooperating with UHRF2 to ensure recruitment of FANCD2 to interstrand cross-links (ICLs) leading to FANCD2 activation (By similarity). Also ubiquitinates non-histone proteins, such as histone H3, KIF11 and PML (By similarity). Acts as a critical player of proper spindle architecture by catalyzing the 'Lys-63'-linked ubiquitination of KIF11, thereby controlling KIF11 localization on the spindle (By similarity)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"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.","ecNumber":"2.3.2.27","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26065575"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29053958"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30392929"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38060382"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"41845018"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"41917274"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"41986725"}],"value":"In oocytes and preimplantation embryos, E3 ubiquitin-protein ligase activity is inhibited by cytoplasmic lattices, which trap UHRF1 in a compact autoinhibited conformation"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26065575"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29053958"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30392929"}],"value":"Protein modification; protein ubiquitination"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q96T88"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15361834"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17994007"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19056828"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19798101"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21268065"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28604677"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36056023"}],"value":"Interacts with DNMT1; the interaction is direct (PubMed:17994007, PubMed:21268065). Interacts with DNMT3A and DNMT3B (PubMed:19798101). Interacts with HDAC1, but not with HDAC2 (PubMed:15361834). Interacts with BLTP3A. Interacts with EHMT2 (PubMed:19056828). Interacts with PRAMEL7 (PubMed:28604677). Interacts with ZNF263; recruited to the SIX3 promoter along with other proteins involved in chromatin modification and transcriptional corepression where it contributes to transcriptional repression (By similarity). Interacts with UHRF2 (By similarity). Interacts with FANCD2 (By similarity). Interacts with TET1 isoform 2; this interaction induces the recruitment of TET1 isoform 2 to replicating heterochromatin (PubMed:36056023)"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36056023"}],"value":"Associated with replicating DNA from early to late S phase, including at replicating pericentric heterochromatin (PubMed:36056023). Also localizes to euchromatic regions (PubMed:36056023). In non-S-phase cells, homogeneously distributed through the nucleus (PubMed:36056023)"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00358"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10984098"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11161719"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14993289"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17994007"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21489993"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26065575"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36056023"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8634372"}],"value":"Nucleus","id":"SL-0191"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17994007"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26065575"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36056023"}],"value":"Chromosome","id":"SL-0468"}}]},{"commentType":"ALTERNATIVE PRODUCTS","events":["Alternative splicing"],"isoforms":[{"name":{"value":"1"},"isoformIds":["Q8VDF2-1"],"isoformSequenceStatus":"Displayed"},{"name":{"value":"2"},"isoformIds":["Q8VDF2-2"],"sequenceIds":["VSP_044395"],"isoformSequenceStatus":"Described"}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10984098"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9880673"}],"value":"Expressed in thymus, testis, spleen and lung. Within testis, expressed in almost all cells except elongated spermatids"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10984098"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11161719"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12058012"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8634372"}],"value":"Up-regulated in proliferating cells, and down-regulated in quiescent or differentiated cells. Early induced by E1A in postmitotic cells. Down-regulated by aphidicolin"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q96T88"}],"value":"The UBL domain is required for the E3 histone H3 ubiquitin-protein ligase activity: it binds the backside of UBE2D E2 ubiquitin-conjugating enzymes (UBE2D1, UBE2D2, UBE2D3 or UBE2D4) and coordinates with other domains that recognize epigenetic marks on DNA and histone H3 to direct ubiquitin to H3"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21489993"}],"value":"The PHD-type zinc finger specifically recognizes and binds histone H3 unmethylated at 'Arg-2' (H3R2me0), while the tudor-like regions specifically recognize and bind histone H3 trimethylated at 'Lys-9' (H3K9me3) (PubMed:21489993). 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"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17994007"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18772888"}],"value":"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)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q96T88"}],"value":"Phosphorylation at Ser-303 of the linker region by PKA decreases the binding to H3K9me3 (By similarity). Phosphorylation at Ser-639 by CDK1 during M phase impairs interaction with USP7, preventing deubiquitination and leading to degradation by the proteasome (By similarity)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21268065"}],"value":"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"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12084726"}],"value":"Mice display a sensitization to DNA damage and replication block, and die in mid-gestation"}],"commentType":"DISRUPTION PHENOTYPE"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":782,"modifier":"EXACT"}},"description":"E3 ubiquitin-protein ligase UHRF1","featureId":"PRO_0000056145"},{"type":"Domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":78,"modifier":"EXACT"}},"description":"Ubiquitin-like","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00214"}]},{"type":"Domain","location":{"start":{"value":424,"modifier":"EXACT"},"end":{"value":586,"modifier":"EXACT"}},"description":"YDG","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00358"}]},{"type":"Zinc 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