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Q8VDF2

- UHRF1_MOUSE

UniProt

Q8VDF2 - UHRF1_MOUSE

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Protein
E3 ubiquitin-protein ligase UHRF1
Gene
Uhrf1, Np95
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 H3K4me0 By similarity
Binding sitei332 – 3321Histone H3R2me0 By similarity
Binding sitei335 – 3351Histone H3R2me0 By similarity
Binding sitei474 – 4741Methylcytosine By similarity
Sitei484 – 4841Required to confer preferential recognition of cytosine over thymine By 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-type
Add
BLAST
Zinc fingeri713 – 75240RING-type
Add
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. DNA repair Source: UniProtKB-KW
  2. cell cycle Source: UniProtKB-KW
  3. cell proliferation Source: MGI
  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
Complete GO annotation...

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
Note: Localizes to replication foci. Enriched in pericentric heterochromatin. Also localizes to euchromatic regions.6 Publications

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
Complete GO annotation...

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 UHRF1
PRO_0000056145Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei76 – 761Phosphoserine By similarity
Modified residuei91 – 911Phosphoserine By similarity
Modified residuei303 – 3031Phosphoserine; by PKA By similarity
Cross-linki390 – 390Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Modified residuei404 – 4041N6-acetyllysine By similarity
Modified residuei550 – 5501N6-acetyllysine By similarity
Modified residuei639 – 6391Phosphoserine; by CDK1 By similarity
Modified residuei649 – 6491Phosphoserine By 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.
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

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.6 Publications

Protein-protein interaction databases

BioGridi201816. 19 interactions.
MINTiMINT-1172910.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiQ8VDF2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 7878Ubiquitin-like
Add
BLAST
Domaini424 – 586163YDG
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni129 – 20577Tudor-like 1
Add
BLAST
Regioni212 – 28069Tudor-like 2
Add
BLAST
Regioni293 – 30614Linker By similarity
Add
BLAST
Regioni338 – 3425Histone H3R2me0 binding By similarity
Regioni358 – 3603Histone H3R2me0 binding By similarity
Regioni450 – 4512Required to promote base flipping
Regioni468 – 4692Methylcytosine binding By 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 (1 Publication). 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) (1 Publication). 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 (1 Publication). The YDG domain also recognizes and binds 5-hydroxymethylcytosine (5hmC).
The RING finger is required for ubiquitin ligase activity.

Sequence similaritiesi

Contains 1 YDG domain.

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei293 – 3019PPPALRNTG → R in isoform 2.
VSP_044395

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti104 – 1041S → P in BAE30624. 1 Publication
Sequence conflicti118 – 1181D → G in BAE31708. 1 Publication
Sequence conflicti118 – 1181D → G in BAE31605. 1 Publication
Sequence conflicti118 – 1181D → G in BAE30730. 1 Publication
Sequence conflicti118 – 1181D → G in BAE29605. 1 Publication
Sequence conflicti214 – 2141E → K in BAB79496. 1 Publication
Sequence conflicti449 – 4491P → L in BAB79496. 1 Publication
Sequence conflicti455 – 4562HG → PW in BAB79496. 1 Publication
Sequence conflicti471 – 4711Y → H in BAE27560. 1 Publication
Sequence conflicti637 – 6371P → A in BAE26398. 1 Publication
Sequence conflicti702 – 7021I → V in BAE31708. 1 Publication
Sequence conflicti702 – 7021I → V in BAE31605. 1 Publication
Sequence conflicti702 – 7021I → V in BAE30730. 1 Publication
Sequence conflicti702 – 7021I → V in BAE29605. 1 Publication
Sequence conflicti753 – 7531F → Y in AAH22167. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 125 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

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