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Q8VDF2

- UHRF1_MOUSE

UniProt

Q8VDF2 - UHRF1_MOUSE

Protein

E3 ubiquitin-protein ligase UHRF1

Gene

Uhrf1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 2 (07 Jun 2005)
      Previous versions | rss
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    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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei321 – 3211Histone H3K4me0By similarity
    Binding sitei332 – 3321Histone H3R2me0By similarity
    Binding sitei335 – 3351Histone H3R2me0By similarity
    Binding sitei474 – 4741MethylcytosineBy similarity
    Sitei484 – 4841Required to confer preferential recognition of cytosine over thymineBy similarity
    Sitei494 – 4941Required to discriminate between hemimethylated DNA versus symmetrically methylated DNA
    Sitei496 – 4961Required for affinity and specificity for 5-mCpG sequence

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri304 – 37168PHD-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri713 – 75240RING-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. hemi-methylated DNA-binding Source: UniProtKB
    2. histone binding Source: UniProtKB
    3. identical protein binding Source: BHF-UCL
    4. ligase activity Source: UniProtKB-KW
    5. methylated histone binding Source: UniProtKB
    6. nucleosomal histone binding Source: BHF-UCL
    7. protein binding Source: UniProtKB
    8. ubiquitin-protein transferase activity Source: BHF-UCL
    9. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. cell cycle Source: UniProtKB-KW
    2. cell proliferation Source: MGI
    3. DNA repair Source: UniProtKB-KW
    4. histone monoubiquitination Source: BHF-UCL
    5. histone ubiquitination Source: UniProtKB
    6. maintenance of DNA methylation Source: UniProtKB
    7. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    8. protein autoubiquitination Source: UniProtKB
    9. protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: UniProtKB
    10. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Ligase, Repressor

    Keywords - Biological processi

    Cell cycle, DNA damage, DNA repair, Transcription, Transcription regulation, Ubl conjugation pathway

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    E3 ubiquitin-protein ligase UHRF1 (EC:6.3.2.-)
    Alternative name(s):
    Nuclear protein 95
    Nuclear zinc finger protein Np95
    Ubiquitin-like PHD and RING finger domain-containing protein 1
    Short name:
    mUhrf1
    Ubiquitin-like-containing PHD and RING finger domains protein 1
    Gene namesi
    Name:Uhrf1
    Synonyms:Np95
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 17

    Organism-specific databases

    MGIiMGI:1338889. Uhrf1.

    Subcellular locationi

    Nucleus 6 PublicationsPROSITE-ProRule annotation
    Note: Localizes to replication foci. Enriched in pericentric heterochromatin. Also localizes to euchromatic regions.

    GO - Cellular componenti

    1. euchromatin Source: UniProtKB
    2. heterochromatin Source: UniProtKB
    3. nuclear chromatin Source: UniProtKB
    4. nuclear heterochromatin Source: MGI
    5. nuclear matrix Source: BHF-UCL
    6. nucleus Source: MGI
    7. replication fork Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Disruption phenotypei

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

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi148 – 1481F → A: Abolishes binding to histone H3K9me3 and ability to repress transcription of target genes. 1 Publication
    Mutagenesisi730 – 7301H → A: Abolishes enzymatic activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 782782E3 ubiquitin-protein ligase UHRF1PRO_0000056145Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei76 – 761PhosphoserineBy similarity
    Modified residuei91 – 911PhosphoserineBy similarity
    Modified residuei303 – 3031Phosphoserine; by PKABy similarity
    Cross-linki390 – 390Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Modified residuei404 – 4041N6-acetyllysineBy similarity
    Modified residuei550 – 5501N6-acetyllysineBy similarity
    Modified residuei639 – 6391Phosphoserine; by CDK1By similarity
    Modified residuei649 – 6491PhosphoserineBy similarity
    Modified residuei656 – 6561Phosphoserine1 Publication

    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.2 Publications

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ8VDF2.
    PaxDbiQ8VDF2.
    PRIDEiQ8VDF2.

    2D gel databases

    REPRODUCTION-2DPAGEQ8VDF2.

    PTM databases

    PhosphoSiteiQ8VDF2.

    Expressioni

    Tissue specificityi

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

    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

    ArrayExpressiQ8VDF2.
    BgeeiQ8VDF2.
    GenevestigatoriQ8VDF2.

    Interactioni

    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.8 Publications

    Protein-protein interaction databases

    BioGridi201816. 19 interactions.
    MINTiMINT-1172910.

    Structurei

    Secondary structure

    1
    782
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni405 – 4084
    Beta strandi434 – 4374
    Helixi438 – 4436
    Beta strandi453 – 4575
    Turni458 – 4603
    Beta strandi461 – 4677
    Beta strandi475 – 4773
    Beta strandi478 – 4847
    Turni492 – 4943
    Helixi508 – 5158
    Beta strandi517 – 5193
    Helixi531 – 5333
    Beta strandi537 – 5437
    Turni546 – 5483
    Beta strandi550 – 5523
    Beta strandi554 – 57219
    Beta strandi576 – 58611
    Helixi596 – 60510
    Helixi615 – 6228

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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. Positions 1-106, 122-369, 405-613, 669-782.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8VDF2.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 7878Ubiquitin-likePROSITE-ProRule annotationAdd
    BLAST
    Domaini424 – 586163YDGPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni129 – 20577Tudor-like 1Add
    BLAST
    Regioni212 – 28069Tudor-like 2Add
    BLAST
    Regioni293 – 30614LinkerBy similarityAdd
    BLAST
    Regioni338 – 3425Histone H3R2me0 bindingBy similarity
    Regioni358 – 3603Histone H3R2me0 bindingBy similarity
    Regioni450 – 4512Required to promote base flipping
    Regioni468 – 4692Methylcytosine bindingBy similarity
    Regioni471 – 4744Required for formation of a 5-methylcytosine-binding pocket
    Regioni483 – 4864Required for formation of a 5-methylcytosine-binding pocket

    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.

    Sequence similaritiesi

    Contains 1 PHD-type zinc finger.PROSITE-ProRule annotation
    Contains 1 RING-type zinc finger.PROSITE-ProRule annotation
    Contains 1 ubiquitin-like domain.PROSITE-ProRule annotation
    Contains 1 YDG domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri304 – 37168PHD-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri713 – 75240RING-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG3440.
    GeneTreeiENSGT00390000008296.
    HOGENOMiHOG000124662.
    HOVERGENiHBG059298.
    InParanoidiQ8VDF2.
    KOiK10638.
    OMAiKSSTHGE.
    OrthoDBiEOG76DTRX.
    PhylomeDBiQ8VDF2.
    TreeFamiTF106434.

    Family and domain databases

    Gene3Di2.30.280.10. 1 hit.
    2.30.30.30. 1 hit.
    3.30.40.10. 2 hits.
    InterProiIPR021991. DUF3590.
    IPR015947. PUA-like_domain.
    IPR014722. Rib_L2_dom2.
    IPR003105. SRA_YDG.
    IPR000626. Ubiquitin-like.
    IPR029071. Ubiquitin-rel_dom.
    IPR011011. Znf_FYVE_PHD.
    IPR001965. Znf_PHD.
    IPR019787. Znf_PHD-finger.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    [Graphical view]
    PfamiPF12148. DUF3590. 1 hit.
    PF00628. PHD. 1 hit.
    PF02182. SAD_SRA. 1 hit.
    PF00240. ubiquitin. 1 hit.
    [Graphical view]
    SMARTiSM00249. PHD. 1 hit.
    SM00184. RING. 2 hits.
    SM00466. SRA. 1 hit.
    SM00213. UBQ. 1 hit.
    [Graphical view]
    SUPFAMiSSF54236. SSF54236. 1 hit.
    SSF57903. SSF57903. 1 hit.
    SSF88697. SSF88697. 1 hit.
    PROSITEiPS50053. 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.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    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.

    « Hide

    MWIQVRTMDG KETHTVNSLS RLTKVQELRK KIEEVFHVEP QLQRLFYRGK    50
    QMEDGHTLFD YDVRLNDTIQ LLVRQSLALP LSTKERDSEL SDSDSGYGVG 100
    HSESDKSSTH GEGAAEADDK TVWEDTDLGL YKVNEYVDVR DNIFGAWFEA 150
    QVVQVQKRAL SEDEPCSSSA VKTSEDDIMY HVKYDDYPEH GVDIVKAKNV 200
    RARARTVIPW ENLEVGQVVM ANYNVDYPRK RGFWYDVEIC RKRQTRTARE 250
    LYGNIRLLND SQLNNCRIMF VDEVLMIELP KERRPLIASP SQPPPALRNT 300
    GKSGPSCRFC KDDENKPCRK CACHVCGGRE APEKQLLCDE CDMAFHLYCL 350
    KPPLTSVPPE PEWYCPSCRT DSSEVVQAGE KLKESKKKAK MASATSSSRR 400
    DWGKGMACVG RTTECTIVPA NHFGPIPGVP VGTMWRFRVQ VSESGVHRPH 450
    VAGIHGRSND GAYSLVLAGG YEDDVDNGNY FTYTGSGGRD LSGNKRTAGQ 500
    SSDQKLTNNN RALALNCHSP INEKGAEAED WRQGKPVRVV RNMKGGKHSK 550
    YAPAEGNRYD GIYKVVKYWP ERGKSGFLVW RYLLRRDDTE PEPWTREGKD 600
    RTRQLGLTMQ YPEGYLEALA NKEKSRKRPA KALEQGPSSS KTGKSKQKST 650
    GPTLSSPRAS KKSKLEPYTL SEQQANLIKE DKGNAKLWDD VLTSLQDGPY 700
    QIFLSKVKEA FQCICCQELV FRPVTTVCQH NVCKDCLDRS FRAQVFSCPA 750
    CRFELDHSSP TRVNQPLQTI LNQLFPGYGS GR 782
    Length:782
    Mass (Da):88,304
    Last modified:June 7, 2005 - v2
    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti104 – 1041S → P in BAE30624. (PubMed:16141072)Curated
    Sequence conflicti118 – 1181D → G in BAE31708. (PubMed:16141072)Curated
    Sequence conflicti118 – 1181D → G in BAE31605. (PubMed:16141072)Curated
    Sequence conflicti118 – 1181D → G in BAE30730. (PubMed:16141072)Curated
    Sequence conflicti118 – 1181D → G in BAE29605. (PubMed:16141072)Curated
    Sequence conflicti214 – 2141E → K in BAB79496. (PubMed:12084726)Curated
    Sequence conflicti449 – 4491P → L in BAB79496. (PubMed:12084726)Curated
    Sequence conflicti455 – 4562HG → PW in BAB79496. (PubMed:12084726)Curated
    Sequence conflicti471 – 4711Y → H in BAE27560. (PubMed:16141072)Curated
    Sequence conflicti637 – 6371P → A in BAE26398. (PubMed:16141072)Curated
    Sequence conflicti702 – 7021I → V in BAE31708. (PubMed:16141072)Curated
    Sequence conflicti702 – 7021I → V in BAE31605. (PubMed:16141072)Curated
    Sequence conflicti702 – 7021I → V in BAE30730. (PubMed:16141072)Curated
    Sequence conflicti702 – 7021I → V in BAE29605. (PubMed:16141072)Curated
    Sequence conflicti753 – 7531F → Y in AAH22167. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei293 – 3019PPPALRNTG → R in isoform 2. 1 PublicationVSP_044395

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.

    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.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS28903.1. [Q8VDF2-1 ]
    CCDS50151.1. [Q8VDF2-2 ]
    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 ]
    UniGenei Mm.42196.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2ZKD X-ray 1.60 A/B 404-613 [» ]
    2ZKE X-ray 2.60 A 404-613 [» ]
    2ZKF X-ray 2.55 A 404-613 [» ]
    2ZKG X-ray 1.77 A/B/C/D 404-613 [» ]
    2ZO0 X-ray 2.19 B 419-628 [» ]
    2ZO1 X-ray 1.96 B 419-628 [» ]
    2ZO2 X-ray 3.09 B 419-628 [» ]
    3F8I X-ray 2.29 A/B 419-628 [» ]
    3F8J X-ray 1.99 B 417-628 [» ]
    3FDE X-ray 1.41 A/B 419-628 [» ]
    ProteinModelPortali Q8VDF2.
    SMRi Q8VDF2. Positions 1-106, 122-369, 405-613, 669-782.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201816. 19 interactions.
    MINTi MINT-1172910.

    PTM databases

    PhosphoSitei Q8VDF2.

    2D gel databases

    REPRODUCTION-2DPAGE Q8VDF2.

    Proteomic databases

    MaxQBi Q8VDF2.
    PaxDbi Q8VDF2.
    PRIDEi Q8VDF2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000001258 ; ENSMUSP00000001258 ; ENSMUSG00000001228 . [Q8VDF2-1 ]
    ENSMUST00000113035 ; ENSMUSP00000108658 ; ENSMUSG00000001228 . [Q8VDF2-2 ]
    ENSMUST00000113038 ; ENSMUSP00000108661 ; ENSMUSG00000001228 . [Q8VDF2-2 ]
    ENSMUST00000113039 ; ENSMUSP00000108662 ; ENSMUSG00000001228 . [Q8VDF2-1 ]
    GeneIDi 18140.
    KEGGi mmu:18140.
    UCSCi uc008dbp.2. mouse. [Q8VDF2-1 ]
    uc008dbq.2. mouse.

    Organism-specific databases

    CTDi 29128.
    MGIi MGI:1338889. Uhrf1.

    Phylogenomic databases

    eggNOGi COG3440.
    GeneTreei ENSGT00390000008296.
    HOGENOMi HOG000124662.
    HOVERGENi HBG059298.
    InParanoidi Q8VDF2.
    KOi K10638.
    OMAi KSSTHGE.
    OrthoDBi EOG76DTRX.
    PhylomeDBi Q8VDF2.
    TreeFami TF106434.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .

    Miscellaneous databases

    EvolutionaryTracei Q8VDF2.
    NextBioi 293384.
    PROi Q8VDF2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8VDF2.
    Bgeei Q8VDF2.
    Genevestigatori Q8VDF2.

    Family and domain databases

    Gene3Di 2.30.280.10. 1 hit.
    2.30.30.30. 1 hit.
    3.30.40.10. 2 hits.
    InterProi IPR021991. DUF3590.
    IPR015947. PUA-like_domain.
    IPR014722. Rib_L2_dom2.
    IPR003105. SRA_YDG.
    IPR000626. Ubiquitin-like.
    IPR029071. Ubiquitin-rel_dom.
    IPR011011. Znf_FYVE_PHD.
    IPR001965. Znf_PHD.
    IPR019787. Znf_PHD-finger.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    [Graphical view ]
    Pfami PF12148. DUF3590. 1 hit.
    PF00628. PHD. 1 hit.
    PF02182. SAD_SRA. 1 hit.
    PF00240. ubiquitin. 1 hit.
    [Graphical view ]
    SMARTi SM00249. PHD. 1 hit.
    SM00184. RING. 2 hits.
    SM00466. SRA. 1 hit.
    SM00213. UBQ. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54236. SSF54236. 1 hit.
    SSF57903. SSF57903. 1 hit.
    SSF88697. SSF88697. 1 hit.
    PROSITEi 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.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and mapping of Np95 gene which encodes a novel nuclear protein associated with cell proliferation."
      Fujimori A., Matsuda Y., Takemoto Y., Hashimoto Y., Kubo E., Araki R., Fukumura R., Mita K., Tatsumi K., Muto M.
      Mamm. Genome 9:1032-1035(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: T lymphoblast.
    2. "LMO2-induced T cell leukemias overexpress Np95, a gene containing RING and PHD zinc fingers and an ubiquitin-like domain."
      Davenport J.W., Fernandes E.R., Neale G.A.M., Goorha R.M.
      Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Strain: C57BL/6J.
      Tissue: Bone marrow, Heart, Small intestine, Spleen and Stomach.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Strain: Czech II.
      Tissue: Mammary tumor.
    6. "Targeted disruption of Np95 gene renders murine embryonic stem cells hypersensitive to DNA damaging agents and DNA replication blocks."
      Muto M., Kanari Y., Kubo E., Takabe T., Kurihara T., Fujimori A., Tatsumi K.
      J. Biol. Chem. 277:34549-34555(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-474, FUNCTION IN DNA REPAIR, DISRUPTION PHENOTYPE.
    7. "The characterization of the monoclonal antibody Th-10a, specific for a nuclear protein appearing in the S phase of the cell cycle in normal thymocytes and its unregulated expression in lymphoma cell lines."
      Muto M., Utsuyama M., Horiguchi T., Kubo E., Sado T., Hirokawa K.
      Cell Prolif. 28:645-657(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INDUCTION.
    8. "Temporal and spatial localization of novel nuclear protein NP95 in mitotic and meiotic cells."
      Uemura T., Kubo E., Kanari Y., Ikemura T., Tatsumi K., Muto M.
      Cell Struct. Funct. 25:149-159(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.
    9. "Dynamic changes in subnuclear NP95 location during the cell cycle and its spatial relationship with DNA replication foci."
      Miura M., Watanabe H., Sasaki T., Tatsumi K., Muto M.
      Exp. Cell Res. 263:202-208(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INDUCTION.
    10. "Np95 is regulated by E1A during mitotic reactivation of terminally differentiated cells and is essential for S phase entry."
      Bonapace I.M., Latella L., Papait R., Nicassio F., Sacco A., Muto M., Crescenzi M., Di Fiore P.P.
      J. Cell Biol. 157:909-914(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION.
    11. "Np95 is a histone-binding protein endowed with ubiquitin ligase activity."
      Citterio E., Papait R., Nicassio F., Vecchi M., Gomiero P., Mantovani R., Di Fiore P.P., Bonapace I.M.
      Mol. Cell. Biol. 24:2526-2535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HISTONES, MUTAGENESIS OF HIS-730.
    12. "ICBP90, an E2F-1 target, recruits HDAC1 and binds to methyl-CpG through its SRA domain."
      Unoki M., Nishidate T., Nakamura Y.
      Oncogene 23:7601-7610(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH HDAC1.
    13. "The SRA protein Np95 mediates epigenetic inheritance by recruiting Dnmt1 to methylated DNA."
      Sharif J., Muto M., Takebayashi S., Suetake I., Iwamatsu A., Endo T.A., Shinga J., Mizutani-Koseki Y., Toyoda T., Okamura K., Tajima S., Mitsuya K., Okano M., Koseki H.
      Nature 450:908-912(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH DNMT1.
    14. "UHRF1 plays a role in maintaining DNA methylation in mammalian cells."
      Bostick M., Kim J.K., Esteve P.O., Clark A., Pradhan S., Jacobsen S.E.
      Science 317:1760-1764(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    15. "Np95 interacts with de novo DNA methyltransferases, Dnmt3a and Dnmt3b, and mediates epigenetic silencing of the viral CMV promoter in embryonic stem cells."
      Meilinger D., Fellinger K., Bultmann S., Rothbauer U., Bonapace I.M., Klinkert W.E., Spada F., Leonhardt H.
      EMBO Rep. 10:1259-1264(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DNMT3A AND DNMT3B.
    16. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-656, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "UHRF1 binds G9a and participates in p21 transcriptional regulation in mammalian cells."
      Kim J.K., Esteve P.O., Jacobsen S.E., Pradhan S.
      Nucleic Acids Res. 37:493-505(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EHMT2.
    18. "The multi-domain protein Np95 connects DNA methylation and histone modification."
      Rottach A., Frauer C., Pichler G., Bonapace I.M., Spada F., Leonhardt H.
      Nucleic Acids Res. 38:1796-1804(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: DNA-BINDING.
    19. Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF PHE-148.
    20. "Usp7 and Uhrf1 control ubiquitination and stability of the maintenance DNA methyltransferase Dnmt1."
      Qin W., Leonhardt H., Spada F.
      J. Cell. Biochem. 112:439-444(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, AUTOUBIQUITINATION, DEUBIQUITINATION BY USP7, INTERACTION WITH USP7 AND DNMT1.
    21. "Recognition of hemi-methylated DNA by the SRA protein UHRF1 by a base-flipping mechanism."
      Arita K., Ariyoshi M., Tochio H., Nakamura Y., Shirakawa M.
      Nature 455:818-821(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 405-613 IN COMPLEX WITH HEMIMETHYLATED DNA.
    22. "The SRA domain of UHRF1 flips 5-methylcytosine out of the DNA helix."
      Hashimoto H., Horton J.R., Zhang X., Bostick M., Jacobsen S.E., Cheng X.
      Nature 455:826-829(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS) OF 419-628 IN COMPLEX WITH HEMIMETHYLATED DNA.
    23. "UHRF1, a modular multi-domain protein, regulates replication-coupled crosstalk between DNA methylation and histone modifications."
      Hashimoto H., Horton J.R., Zhang X., Cheng X.
      Epigenetics 4:8-14(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) OF 417-628.

    Entry informationi

    Entry nameiUHRF1_MOUSE
    AccessioniPrimary (citable) accession number: Q8VDF2
    Secondary accession number(s): Q3U9D7
    , Q3U9P2, Q3UI74, Q3UIE6, Q3ULF2, Q3ULQ0, Q8C6F1, Q8VIA1, Q9Z1H6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2005
    Last sequence update: June 7, 2005
    Last modified: October 1, 2014
    This is version 126 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3