Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q8VDF2 (UHRF1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Uhrf1
Synonyms:Np95
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length782 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Multidomain protein that acts as a key epigenetic regulator by bridging DNA methylation and chromatin modification. Specifically recognizes and binds hemimethylated DNA at replication forks via its YDG domain and recruits DNMT1 methyltransferase to ensure faithful propagation of the DNA methylation patterns through DNA replication. In addition to its role in maintenance of DNA methylation, also plays a key role in chromatin modification: through its tudor-like regions and PHD-type zinc fingers, specifically recognizes and binds histone H3 trimethylated at 'Lys-9' (H3K9me3) and unmethylated at 'Arg-2' (H3R2me0), respectively, and recruits chromatin proteins. Enriched in pericentric heterochromatin where it recruits different chromatin modifiers required for this chromatin replication. Also localizes to euchromatic regions where it negatively regulates transcription possibly by impacting DNA methylation and histone modifications. Has E3 ubiquitin-protein ligase activity by mediating the ubiquitination of target proteins such as histone H3 and PML. It is still unclear how E3 ubiquitin-protein ligase activity is related to its role in chromatin in vivo. May be involved in DNA repair. Ref.6 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.19 Ref.20

Pathway

Protein modification; protein ubiquitination.

Subunit structure

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. Ref.11 Ref.12 Ref.13 Ref.15 Ref.17 Ref.20

Subcellular location

Nucleus. Note: Localizes to replication foci. Enriched in pericentric heterochromatin. Also localizes to euchromatic regions. Ref.7 Ref.8 Ref.9 Ref.11 Ref.13 Ref.19

Tissue specificity

Expressed in thymus, testis, spleen and lung. Within testis, expressed in almost all cells except elongated spermatids. Ref.1 Ref.8

Induction

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. Ref.7 Ref.8 Ref.9 Ref.10

Domain

The tudor-like regions specifically recognize and bind histone H3 unmethylated at 'Arg-2' (H3R2me0), while the PHD-type zinc finger specifically recognizes and binds histone H3 trimethylated at 'Lys-9' (H3K9me3). The tudor-like regions simultaneously recognizes H3K9me3 through a conserved aromatic cage in the first tudor-like subdomain and unmodified H3K4 (H3K4me0) within a groove between the tandem subdomains (Ref.19). 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.

The YDG domain (also named SRA domain) specifically recognizes and binds hemimethylated DNA at replication forks (DNA that is only methylated on the mother strand of replicating DNA) (Ref.13). 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 (Ref.22). The YDG domain also recognizes and binds 5-hydroxymethylcytosine (5hmC).

The RING finger is required for ubiquitin ligase activity.

Post-translational modification

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.

Ubiquitinated; which leads to proteasomal degradation. Autoubiquitinated; interaction with USP7 leads to deubiquitination and prevents degradation. Ubiquitination and degradation takes place during M phase, when phosphorylation at Ser-639 prevents intereaction with USP7 and subsequent deubiquitination. Polyubiquitination may be stimulated by DNA damage. Ref.20

Disruption phenotype

Mice display a sensitization to DNA damage and replication block, and die in mid-gestation. Ref.6

Sequence similarities

Contains 1 PHD-type zinc finger.

Contains 1 RING-type zinc finger.

Contains 1 ubiquitin-like domain.

Contains 1 YDG domain.

Ontologies

Keywords
   Biological processCell cycle
DNA damage
DNA repair
Transcription
Transcription regulation
Ubl conjugation pathway
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainRepeat
Zinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionChromatin regulator
Ligase
Repressor
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA repair

Inferred from electronic annotation. Source: UniProtKB-KW

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cell proliferation

Traceable author statement Ref.1. Source: MGI

histone monoubiquitination

Inferred from direct assay Ref.11. Source: BHF-UCL

histone ubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

maintenance of DNA methylation

Inferred from mutant phenotype Ref.14Ref.13. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.19. Source: UniProtKB

protein autoubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

protein ubiquitination involved in ubiquitin-dependent protein catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componenteuchromatin

Inferred from sequence or structural similarity. Source: UniProtKB

heterochromatin

Inferred from direct assay Ref.19. Source: UniProtKB

nuclear chromatin

Inferred from direct assay Ref.13. Source: UniProtKB

nuclear heterochromatin

Inferred from direct assay PubMed 18692478. Source: MGI

nuclear matrix

Inferred from direct assay Ref.11. Source: BHF-UCL

nucleus

Inferred from direct assay Ref.13. Source: MGI

replication fork

Inferred from direct assay Ref.13. Source: UniProtKB

   Molecular_functionhemi-methylated DNA-binding

Inferred from direct assay Ref.13. Source: UniProtKB

histone binding

Inferred from sequence or structural similarity. Source: UniProtKB

identical protein binding

Inferred from physical interaction Ref.11. Source: BHF-UCL

methylated histone binding

Inferred from direct assay Ref.19. Source: UniProtKB

nucleosomal histone binding

Inferred from direct assay Ref.11. Source: BHF-UCL

protein binding

Inferred from physical interaction Ref.13Ref.20. Source: UniProtKB

ubiquitin-protein transferase activity

Inferred from direct assay Ref.11. Source: BHF-UCL

zinc ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8VDF2-1)

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.
Isoform 2 (identifier: Q8VDF2-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 782782E3 ubiquitin-protein ligase UHRF1
PRO_0000056145

Regions

Domain1 – 7878Ubiquitin-like
Domain424 – 586163YDG
Zinc finger304 – 37168PHD-type
Zinc finger713 – 75240RING-type
Region129 – 20577Tudor-like 1
Region212 – 28069Tudor-like 2
Region293 – 30614Linker By similarity
Region338 – 3425Histone H3R2me0 binding By similarity
Region358 – 3603Histone H3R2me0 binding By similarity
Region450 – 4512Required to promote base flipping
Region468 – 4692Methylcytosine binding By similarity
Region471 – 4744Required for formation of a 5-methylcytosine-binding pocket
Region483 – 4864Required for formation of a 5-methylcytosine-binding pocket

Sites

Binding site3211Histone H3K4me0 By similarity
Binding site3321Histone H3R2me0 By similarity
Binding site3351Histone H3R2me0 By similarity
Binding site4741Methylcytosine By similarity
Site4841Required to confer preferential recognition of cytosine over thymine By similarity
Site4941Required to discriminate between hemimethylated DNA versus symmetrically methylated DNA
Site4961Required for affinity and specificity for 5-mCpG sequence

Amino acid modifications

Modified residue761Phosphoserine By similarity
Modified residue911Phosphoserine By similarity
Modified residue3031Phosphoserine; by PKA By similarity
Modified residue4041N6-acetyllysine By similarity
Modified residue5501N6-acetyllysine By similarity
Modified residue6391Phosphoserine; by CDK1 By similarity
Modified residue6491Phosphoserine By similarity
Modified residue6561Phosphoserine Ref.16
Cross-link390Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Natural variations

Alternative sequence293 – 3019PPPALRNTG → R in isoform 2.
VSP_044395

Experimental info

Mutagenesis1481F → A: Abolishes binding to histone H3K9me3 and ability to repress transcription of target genes. Ref.19
Mutagenesis7301H → A: Abolishes enzymatic activity. Ref.11
Sequence conflict1041S → P in BAE30624. Ref.3
Sequence conflict1181D → G in BAE31708. Ref.3
Sequence conflict1181D → G in BAE31605. Ref.3
Sequence conflict1181D → G in BAE30730. Ref.3
Sequence conflict1181D → G in BAE29605. Ref.3
Sequence conflict2141E → K in BAB79496. Ref.6
Sequence conflict4491P → L in BAB79496. Ref.6
Sequence conflict455 – 4562HG → PW in BAB79496. Ref.6
Sequence conflict4711Y → H in BAE27560. Ref.3
Sequence conflict6371P → A in BAE26398. Ref.3
Sequence conflict7021I → V in BAE31708. Ref.3
Sequence conflict7021I → V in BAE31605. Ref.3
Sequence conflict7021I → V in BAE30730. Ref.3
Sequence conflict7021I → V in BAE29605. Ref.3
Sequence conflict7531F → Y in AAH22167. Ref.5

Secondary structure

................................... 782
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 7, 2005. Version 2.
Checksum: DC5EEDFCDF69619B

FASTA78288,304
        10         20         30         40         50         60 
MWIQVRTMDG KETHTVNSLS RLTKVQELRK KIEEVFHVEP QLQRLFYRGK QMEDGHTLFD 

        70         80         90        100        110        120 
YDVRLNDTIQ LLVRQSLALP LSTKERDSEL SDSDSGYGVG HSESDKSSTH GEGAAEADDK 

       130        140        150        160        170        180 
TVWEDTDLGL YKVNEYVDVR DNIFGAWFEA QVVQVQKRAL SEDEPCSSSA VKTSEDDIMY 

       190        200        210        220        230        240 
HVKYDDYPEH GVDIVKAKNV RARARTVIPW ENLEVGQVVM ANYNVDYPRK RGFWYDVEIC 

       250        260        270        280        290        300 
RKRQTRTARE LYGNIRLLND SQLNNCRIMF VDEVLMIELP KERRPLIASP SQPPPALRNT 

       310        320        330        340        350        360 
GKSGPSCRFC KDDENKPCRK CACHVCGGRE APEKQLLCDE CDMAFHLYCL KPPLTSVPPE 

       370        380        390        400        410        420 
PEWYCPSCRT DSSEVVQAGE KLKESKKKAK MASATSSSRR DWGKGMACVG RTTECTIVPA 

       430        440        450        460        470        480 
NHFGPIPGVP VGTMWRFRVQ VSESGVHRPH VAGIHGRSND GAYSLVLAGG YEDDVDNGNY 

       490        500        510        520        530        540 
FTYTGSGGRD LSGNKRTAGQ SSDQKLTNNN RALALNCHSP INEKGAEAED WRQGKPVRVV 

       550        560        570        580        590        600 
RNMKGGKHSK YAPAEGNRYD GIYKVVKYWP ERGKSGFLVW RYLLRRDDTE PEPWTREGKD 

       610        620        630        640        650        660 
RTRQLGLTMQ YPEGYLEALA NKEKSRKRPA KALEQGPSSS KTGKSKQKST GPTLSSPRAS 

       670        680        690        700        710        720 
KKSKLEPYTL SEQQANLIKE DKGNAKLWDD VLTSLQDGPY QIFLSKVKEA FQCICCQELV 

       730        740        750        760        770        780 
FRPVTTVCQH NVCKDCLDRS FRAQVFSCPA CRFELDHSSP TRVNQPLQTI LNQLFPGYGS 


GR 

« Hide

Isoform 2 [UniParc].

Checksum: 64752A7950497454
Show »

FASTA77487,556

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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]"Recognition of multivalent histone states associated with heterochromatin by UHRF1 protein."
Nady N., Lemak A., Walker J.R., Avvakumov G.V., Kareta M.S., Achour M., Xue S., Duan S., Allali-Hassani A., Zuo X., Wang Y.X., Bronner C., Chedin F., Arrowsmith C.H., Dhe-Paganon S.
J. Biol. Chem. 286:24300-24311(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS28903.1. [Q8VDF2-1]
CCDS50151.1. [Q8VDF2-2]
RefSeqNP_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]
UniGeneMm.42196.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalQ8VDF2.
SMRQ8VDF2. Positions 1-106, 122-369, 405-613, 669-782.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201816. 18 interactions.
MINTMINT-1172910.

PTM databases

PhosphoSiteQ8VDF2.

2D gel databases

REPRODUCTION-2DPAGEQ8VDF2.

Proteomic databases

MaxQBQ8VDF2.
PaxDbQ8VDF2.
PRIDEQ8VDF2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000001258; ENSMUSP00000001258; ENSMUSG00000001228. [Q8VDF2-1]
ENSMUST00000113035; ENSMUSP00000108658; ENSMUSG00000001228. [Q8VDF2-2]
ENSMUST00000113038; ENSMUSP00000108661; ENSMUSG00000001228. [Q8VDF2-2]
ENSMUST00000113039; ENSMUSP00000108662; ENSMUSG00000001228. [Q8VDF2-1]
GeneID18140.
KEGGmmu:18140.
UCSCuc008dbp.2. mouse. [Q8VDF2-1]
uc008dbq.2. mouse.

Organism-specific databases

CTD29128.
MGIMGI:1338889. Uhrf1.

Phylogenomic databases

eggNOGCOG3440.
GeneTreeENSGT00390000008296.
HOGENOMHOG000124662.
HOVERGENHBG059298.
InParanoidQ8VDF2.
KOK10638.
OMAKSSTHGE.
OrthoDBEOG76DTRX.
PhylomeDBQ8VDF2.
TreeFamTF106434.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ8VDF2.
BgeeQ8VDF2.
GenevestigatorQ8VDF2.

Family and domain databases

Gene3D2.30.280.10. 1 hit.
2.30.30.30. 1 hit.
3.30.40.10. 2 hits.
InterProIPR021991. 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]
PfamPF12148. DUF3590. 1 hit.
PF00628. PHD. 1 hit.
PF02182. SAD_SRA. 1 hit.
PF00240. ubiquitin. 1 hit.
[Graphical view]
SMARTSM00249. PHD. 1 hit.
SM00184. RING. 2 hits.
SM00466. SRA. 1 hit.
SM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMSSF54236. SSF54236. 1 hit.
SSF57903. SSF57903. 1 hit.
SSF88697. SSF88697. 1 hit.
PROSITEPS50053. 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]
ProtoNetSearch...

Other

EvolutionaryTraceQ8VDF2.
NextBio293384.
PROQ8VDF2.
SOURCESearch...

Entry information

Entry nameUHRF1_MOUSE
AccessionPrimary (citable) accession number: Q8VDF2
Secondary accession number(s): Q3U9D7 expand/collapse secondary AC list , Q3U9P2, Q3UI74, Q3UIE6, Q3ULF2, Q3ULQ0, Q8C6F1, Q8VIA1, Q9Z1H6
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: July 9, 2014
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot