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E3 ubiquitin-protein ligase UHRF1 (EC 2.3.2.27) (Nuclear protein 95) (Nuclear zinc finger protein Np95) (RING-type E3 ubiquitin transferase UHRF1) (Ubiquitin-like PHD and RING finger domain-containing protein 1) (mUhrf1) (Ubiquitin-like-containing PHD and RING finger domains protein 1)

 UHRF1_MOUSE             Reviewed;         782 AA.
Q8VDF2; Q3U9D7; Q3U9P2; Q3UI74; Q3UIE6; Q3ULF2; Q3ULQ0; Q8C6F1;
Q8VIA1; Q9Z1H6;
07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
07-JUN-2005, sequence version 2.
22-NOV-2017, entry version 158.
RecName: Full=E3 ubiquitin-protein ligase UHRF1;
EC=2.3.2.27;
AltName: Full=Nuclear protein 95;
AltName: Full=Nuclear zinc finger protein Np95;
AltName: Full=RING-type E3 ubiquitin transferase UHRF1;
AltName: Full=Ubiquitin-like PHD and RING finger domain-containing protein 1;
Short=mUhrf1;
AltName: Full=Ubiquitin-like-containing PHD and RING finger domains protein 1;
Name=Uhrf1; Synonyms=Np95;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
TISSUE=T lymphoblast;
PubMed=9880673; DOI=10.1007/s003359900920;
Fujimori A., Matsuda Y., Takemoto Y., Hashimoto Y., Kubo E., Araki R.,
Fukumura R., Mita K., Tatsumi K., Muto M.;
"Cloning and mapping of Np95 gene which encodes a novel nuclear
protein associated with cell proliferation.";
Mamm. Genome 9:1032-1035(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Davenport J.W., Fernandes E.R., Neale G.A.M., Goorha R.M.;
"LMO2-induced T cell leukemias overexpress Np95, a gene containing
RING and PHD zinc fingers and an ubiquitin-like domain.";
Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J;
TISSUE=Bone marrow, Heart, Small intestine, Spleen, and Stomach;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
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., 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.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=Czech II; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-474, FUNCTION IN DNA REPAIR,
AND DISRUPTION PHENOTYPE.
PubMed=12084726; DOI=10.1074/jbc.M205189200;
Muto M., Kanari Y., Kubo E., Takabe T., Kurihara T., Fujimori A.,
Tatsumi K.;
"Targeted disruption of Np95 gene renders murine embryonic stem cells
hypersensitive to DNA damaging agents and DNA replication blocks.";
J. Biol. Chem. 277:34549-34555(2002).
[7]
SUBCELLULAR LOCATION, AND INDUCTION.
PubMed=8634372; DOI=10.1111/j.1365-2184.1995.tb00051.x;
Muto M., Utsuyama M., Horiguchi T., Kubo E., Sado T., Hirokawa K.;
"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.";
Cell Prolif. 28:645-657(1995).
[8]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
PubMed=10984098; DOI=10.1247/csf.25.149;
Uemura T., Kubo E., Kanari Y., Ikemura T., Tatsumi K., Muto M.;
"Temporal and spatial localization of novel nuclear protein NP95 in
mitotic and meiotic cells.";
Cell Struct. Funct. 25:149-159(2000).
[9]
SUBCELLULAR LOCATION, AND INDUCTION.
PubMed=11161719; DOI=10.1006/excr.2000.5115;
Miura M., Watanabe H., Sasaki T., Tatsumi K., Muto M.;
"Dynamic changes in subnuclear NP95 location during the cell cycle and
its spatial relationship with DNA replication foci.";
Exp. Cell Res. 263:202-208(2001).
[10]
FUNCTION, AND INDUCTION.
PubMed=12058012; DOI=10.1083/jcb.200201025;
Bonapace I.M., Latella L., Papait R., Nicassio F., Sacco A., Muto M.,
Crescenzi M., Di Fiore P.P.;
"Np95 is regulated by E1A during mitotic reactivation of terminally
differentiated cells and is essential for S phase entry.";
J. Cell Biol. 157:909-914(2002).
[11]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HISTONES, AND
MUTAGENESIS OF HIS-730.
PubMed=14993289; DOI=10.1128/MCB.24.6.2526-2535.2004;
Citterio E., Papait R., Nicassio F., Vecchi M., Gomiero P.,
Mantovani R., Di Fiore P.P., Bonapace I.M.;
"Np95 is a histone-binding protein endowed with ubiquitin ligase
activity.";
Mol. Cell. Biol. 24:2526-2535(2004).
[12]
FUNCTION, AND INTERACTION WITH HDAC1.
PubMed=15361834; DOI=10.1038/sj.onc.1208053;
Unoki M., Nishidate T., Nakamura Y.;
"ICBP90, an E2F-1 target, recruits HDAC1 and binds to methyl-CpG
through its SRA domain.";
Oncogene 23:7601-7610(2004).
[13]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH DNMT1.
PubMed=17994007; DOI=10.1038/nature06397;
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.;
"The SRA protein Np95 mediates epigenetic inheritance by recruiting
Dnmt1 to methylated DNA.";
Nature 450:908-912(2007).
[14]
FUNCTION.
PubMed=17673620; DOI=10.1126/science.1147939;
Bostick M., Kim J.K., Esteve P.O., Clark A., Pradhan S.,
Jacobsen S.E.;
"UHRF1 plays a role in maintaining DNA methylation in mammalian
cells.";
Science 317:1760-1764(2007).
[15]
INTERACTION WITH DNMT3A AND DNMT3B.
PubMed=19798101; DOI=10.1038/embor.2009.201;
Meilinger D., Fellinger K., Bultmann S., Rothbauer U., Bonapace I.M.,
Klinkert W.E., Spada F., Leonhardt H.;
"Np95 interacts with de novo DNA methyltransferases, Dnmt3a and
Dnmt3b, and mediates epigenetic silencing of the viral CMV promoter in
embryonic stem cells.";
EMBO Rep. 10:1259-1264(2009).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-656, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[17]
INTERACTION WITH EHMT2.
PubMed=19056828; DOI=10.1093/nar/gkn961;
Kim J.K., Esteve P.O., Jacobsen S.E., Pradhan S.;
"UHRF1 binds G9a and participates in p21 transcriptional regulation in
mammalian cells.";
Nucleic Acids Res. 37:493-505(2009).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161 AND SER-519, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Lung, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[19]
DNA-BINDING.
PubMed=20026581; DOI=10.1093/nar/gkp1152;
Rottach A., Frauer C., Pichler G., Bonapace I.M., Spada F.,
Leonhardt H.;
"The multi-domain protein Np95 connects DNA methylation and histone
modification.";
Nucleic Acids Res. 38:1796-1804(2010).
[20]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF PHE-148.
PubMed=21489993; DOI=10.1074/jbc.M111.234104;
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.;
"Recognition of multivalent histone states associated with
heterochromatin by UHRF1 protein.";
J. Biol. Chem. 286:24300-24311(2011).
[21]
FUNCTION, AUTOUBIQUITINATION, DEUBIQUITINATION BY USP7, AND
INTERACTION WITH USP7 AND DNMT1.
PubMed=21268065; DOI=10.1002/jcb.22998;
Qin W., Leonhardt H., Spada F.;
"Usp7 and Uhrf1 control ubiquitination and stability of the
maintenance DNA methyltransferase Dnmt1.";
J. Cell. Biochem. 112:439-444(2011).
[22]
INTERACTION WITH PRAMEL7.
PubMed=28604677; DOI=10.1038/ncb3554;
Graf U., Casanova E.A., Wyck S., Dalcher D., Gatti M.,
Vollenweider E., Okoniewski M.J., Weber F.A., Patel S.S., Schmid M.W.,
Li J., Sharif J., Wanner G.A., Koseki H., Wong J., Pelczar P.,
Penengo L., Santoro R., Cinelli P.;
"Pramel7 mediates ground-state pluripotency through proteasomal-
epigenetic combined pathways.";
Nat. Cell Biol. 19:763-773(2017).
[23]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 405-613 IN COMPLEX WITH
HEMIMETHYLATED DNA.
PubMed=18772891; DOI=10.1038/nature07249;
Arita K., Ariyoshi M., Tochio H., Nakamura Y., Shirakawa M.;
"Recognition of hemi-methylated DNA by the SRA protein UHRF1 by a
base-flipping mechanism.";
Nature 455:818-821(2008).
[24]
X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS) OF 419-628 IN COMPLEX WITH
HEMIMETHYLATED DNA.
PubMed=18772888; DOI=10.1038/nature07280;
Hashimoto H., Horton J.R., Zhang X., Bostick M., Jacobsen S.E.,
Cheng X.;
"The SRA domain of UHRF1 flips 5-methylcytosine out of the DNA
helix.";
Nature 455:826-829(2008).
[25]
X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) OF 417-628.
PubMed=19077538; DOI=10.4161/epi.4.1.7370;
Hashimoto H., Horton J.R., Zhang X., Cheng X.;
"UHRF1, a modular multi-domain protein, regulates replication-coupled
crosstalk between DNA methylation and histone modifications.";
Epigenetics 4:8-14(2009).
-!- 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. {ECO:0000269|PubMed:12058012,
ECO:0000269|PubMed:12084726, ECO:0000269|PubMed:14993289,
ECO:0000269|PubMed:15361834, ECO:0000269|PubMed:17673620,
ECO:0000269|PubMed:17994007, ECO:0000269|PubMed:21268065,
ECO:0000269|PubMed:21489993}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Interacts with DNMT1; the interaction is direct.
Interacts with USP7; leading to its deubiquitination. Interacts
with HDAC1, but not with HDAC2. Interacts with UHRF1BP1. Interacts
with PML. Interacts with EHMT2. Binds hemimethylated CpG
containing oligonucleotides. Interacts with histones H3, H1 and
H2B. Interacts with DNMT3A and DNMT3B (PubMed:14993289,
PubMed:15361834, PubMed:17994007, PubMed:18772888,
PubMed:18772891, PubMed:19056828, PubMed:19798101,
PubMed:21268065). Interacts with PRAMEL7 (PubMed:28604677).
{ECO:0000269|PubMed:14993289, ECO:0000269|PubMed:15361834,
ECO:0000269|PubMed:17994007, ECO:0000269|PubMed:18772888,
ECO:0000269|PubMed:18772891, ECO:0000269|PubMed:19056828,
ECO:0000269|PubMed:19798101, ECO:0000269|PubMed:21268065,
ECO:0000269|PubMed:28604677}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00358, ECO:0000269|PubMed:10984098,
ECO:0000269|PubMed:11161719, ECO:0000269|PubMed:14993289,
ECO:0000269|PubMed:17994007, ECO:0000269|PubMed:21489993,
ECO:0000269|PubMed:8634372}. Note=Localizes to replication foci.
Enriched in pericentric heterochromatin. Also localizes to
euchromatic regions.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8VDF2-1; Sequence=Displayed;
Name=2;
IsoId=Q8VDF2-2; Sequence=VSP_044395;
-!- TISSUE SPECIFICITY: Expressed in thymus, testis, spleen and lung.
Within testis, expressed in almost all cells except elongated
spermatids. {ECO:0000269|PubMed:10984098,
ECO:0000269|PubMed:9880673}.
-!- 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.
{ECO:0000269|PubMed:10984098, ECO:0000269|PubMed:11161719,
ECO:0000269|PubMed:12058012, ECO:0000269|PubMed:8634372}.
-!- 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
(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.
{ECO:0000269|PubMed:21489993}.
-!- DOMAIN: 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). {ECO:0000269|PubMed:17994007,
ECO:0000269|PubMed:18772888}.
-!- DOMAIN: The RING finger is required for ubiquitin ligase activity.
-!- PTM: 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).
{ECO:0000250}.
-!- PTM: 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.
{ECO:0000269|PubMed:21268065}.
-!- DISRUPTION PHENOTYPE: Mice display a sensitization to DNA damage
and replication block, and die in mid-gestation.
{ECO:0000269|PubMed:12084726}.
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EMBL; D87908; BAA74579.1; -; mRNA.
EMBL; AF274046; AAK55743.1; -; mRNA.
EMBL; AK075819; BAC35985.1; -; mRNA.
EMBL; AK143688; BAE25499.1; -; mRNA.
EMBL; AK145376; BAE26398.1; -; mRNA.
EMBL; AK145543; BAE26496.1; -; mRNA.
EMBL; AK146951; BAE27560.1; -; mRNA.
EMBL; AK147046; BAE27632.1; -; mRNA.
EMBL; AK150489; BAE29605.1; -; mRNA.
EMBL; AK151701; BAE30624.1; -; mRNA.
EMBL; AK151837; BAE30730.1; -; mRNA.
EMBL; AK152930; BAE31605.1; -; mRNA.
EMBL; AK153083; BAE31708.1; -; mRNA.
EMBL; AC026385; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC022167; AAH22167.1; -; mRNA.
EMBL; AB066246; BAB79496.1; -; Genomic_DNA.
CCDS; CCDS28903.1; -. [Q8VDF2-1]
CCDS; CCDS50151.1; -. [Q8VDF2-2]
RefSeq; NP_001104548.1; NM_001111078.1. [Q8VDF2-1]
RefSeq; NP_001104549.1; NM_001111079.1. [Q8VDF2-2]
RefSeq; NP_001104550.1; NM_001111080.1. [Q8VDF2-2]
RefSeq; NP_035061.3; NM_010931.3. [Q8VDF2-1]
UniGene; Mm.42196; -.
PDB; 2ZKD; X-ray; 1.60 A; A/B=404-613.
PDB; 2ZKE; X-ray; 2.60 A; A=404-613.
PDB; 2ZKF; X-ray; 2.55 A; A=404-613.
PDB; 2ZKG; X-ray; 1.77 A; A/B/C/D=404-613.
PDB; 2ZO0; X-ray; 2.19 A; B=419-628.
PDB; 2ZO1; X-ray; 1.96 A; B=419-628.
PDB; 2ZO2; X-ray; 3.09 A; B=419-628.
PDB; 3F8I; X-ray; 2.29 A; A/B=419-628.
PDB; 3F8J; X-ray; 1.99 A; B=417-628.
PDB; 3FDE; X-ray; 1.41 A; A/B=419-628.
PDBsum; 2ZKD; -.
PDBsum; 2ZKE; -.
PDBsum; 2ZKF; -.
PDBsum; 2ZKG; -.
PDBsum; 2ZO0; -.
PDBsum; 2ZO1; -.
PDBsum; 2ZO2; -.
PDBsum; 3F8I; -.
PDBsum; 3F8J; -.
PDBsum; 3FDE; -.
ProteinModelPortal; Q8VDF2; -.
SMR; Q8VDF2; -.
BioGrid; 201816; 25.
MINT; MINT-1172910; -.
STRING; 10090.ENSMUSP00000001258; -.
iPTMnet; Q8VDF2; -.
PhosphoSitePlus; Q8VDF2; -.
REPRODUCTION-2DPAGE; Q8VDF2; -.
EPD; Q8VDF2; -.
PaxDb; Q8VDF2; -.
PeptideAtlas; Q8VDF2; -.
PRIDE; Q8VDF2; -.
Ensembl; ENSMUST00000001258; ENSMUSP00000001258; ENSMUSG00000001228. [Q8VDF2-1]
Ensembl; ENSMUST00000113035; ENSMUSP00000108658; ENSMUSG00000001228. [Q8VDF2-2]
Ensembl; ENSMUST00000113038; ENSMUSP00000108661; ENSMUSG00000001228. [Q8VDF2-2]
Ensembl; ENSMUST00000113039; ENSMUSP00000108662; ENSMUSG00000001228. [Q8VDF2-1]
GeneID; 18140; -.
KEGG; mmu:18140; -.
UCSC; uc008dbp.2; mouse. [Q8VDF2-1]
UCSC; uc008dbq.2; mouse. [Q8VDF2-2]
CTD; 29128; -.
MGI; MGI:1338889; Uhrf1.
eggNOG; ENOG410IFAP; Eukaryota.
eggNOG; COG3440; LUCA.
GeneTree; ENSGT00390000008296; -.
HOGENOM; HOG000124662; -.
HOVERGEN; HBG059298; -.
InParanoid; Q8VDF2; -.
KO; K10638; -.
OMA; EAFQCIC; -.
OrthoDB; EOG091G06BT; -.
PhylomeDB; Q8VDF2; -.
TreeFam; TF106434; -.
UniPathway; UPA00143; -.
EvolutionaryTrace; Q8VDF2; -.
PRO; PR:Q8VDF2; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000001228; -.
ExpressionAtlas; Q8VDF2; baseline and differential.
Genevisible; Q8VDF2; MM.
GO; GO:0000791; C:euchromatin; ISS:UniProtKB.
GO; GO:0000792; C:heterochromatin; IDA:UniProtKB.
GO; GO:0000790; C:nuclear chromatin; IDA:UniProtKB.
GO; GO:0005720; C:nuclear heterochromatin; IDA:MGI.
GO; GO:0016363; C:nuclear matrix; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0005657; C:replication fork; IDA:UniProtKB.
GO; GO:0000987; F:core promoter proximal region sequence-specific DNA binding; ISO:MGI.
GO; GO:0044729; F:hemi-methylated DNA-binding; IDA:UniProtKB.
GO; GO:0042393; F:histone binding; ISS:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:BHF-UCL.
GO; GO:0008327; F:methyl-CpG binding; ISO:MGI.
GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB.
GO; GO:0031493; F:nucleosomal histone binding; IDA:BHF-UCL.
GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:BHF-UCL.
GO; GO:0004842; F:ubiquitin-protein transferase activity; ISO:MGI.
GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0008283; P:cell proliferation; TAS:MGI.
GO; GO:0032776; P:DNA methylation on cytosine; TAS:Reactome.
GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
GO; GO:0010390; P:histone monoubiquitination; IDA:BHF-UCL.
GO; GO:0016574; P:histone ubiquitination; ISS:UniProtKB.
GO; GO:0010216; P:maintenance of DNA methylation; IMP:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0032270; P:positive regulation of cellular protein metabolic process; ISO:MGI.
GO; GO:0051865; P:protein autoubiquitination; IDA:BHF-UCL.
GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
GO; GO:0090308; P:regulation of methylation-dependent chromatin silencing; IBA:GO_Central.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 2.30.280.10; -; 1.
Gene3D; 2.30.30.30; -; 1.
Gene3D; 3.30.40.10; -; 2.
InterPro; IPR015947; PUA-like_sf.
InterPro; IPR014722; Rib_L2_dom2.
InterPro; IPR036987; SRA-YDG_sf.
InterPro; IPR003105; SRA_YDG.
InterPro; IPR021991; TTD_dom.
InterPro; IPR029071; Ubiquitin-like_domsf.
InterPro; IPR000626; Ubiquitin_dom.
InterPro; IPR011011; Znf_FYVE_PHD.
InterPro; IPR001965; Znf_PHD.
InterPro; IPR019787; Znf_PHD-finger.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR017907; Znf_RING_CS.
Pfam; PF00628; PHD; 1.
Pfam; PF02182; SAD_SRA; 1.
Pfam; PF12148; TTD; 1.
Pfam; PF00240; ubiquitin; 1.
SMART; SM00249; PHD; 1.
SMART; SM00184; RING; 2.
SMART; SM00466; SRA; 1.
SMART; SM00213; UBQ; 1.
SUPFAM; SSF54236; SSF54236; 1.
SUPFAM; SSF57903; SSF57903; 1.
SUPFAM; SSF88697; SSF88697; 1.
PROSITE; PS50053; UBIQUITIN_2; 1.
PROSITE; PS51015; YDG; 1.
PROSITE; PS01359; ZF_PHD_1; 1.
PROSITE; PS50016; ZF_PHD_2; 1.
PROSITE; PS00518; ZF_RING_1; 1.
PROSITE; PS50089; ZF_RING_2; 2.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Cell cycle;
Chromatin regulator; Complete proteome; DNA damage; DNA repair;
DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Repressor; Transcription;
Transcription regulation; Transferase; Ubl conjugation;
Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 782 E3 ubiquitin-protein ligase UHRF1.
/FTId=PRO_0000056145.
DOMAIN 1 78 Ubiquitin-like. {ECO:0000255|PROSITE-
ProRule:PRU00214}.
DOMAIN 424 586 YDG. {ECO:0000255|PROSITE-
ProRule:PRU00358}.
ZN_FING 304 371 PHD-type. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
ZN_FING 713 752 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
REGION 129 205 Tudor-like 1.
REGION 212 280 Tudor-like 2.
REGION 293 306 Linker. {ECO:0000250}.
REGION 338 342 Histone H3R2me0 binding. {ECO:0000250}.
REGION 358 360 Histone H3R2me0 binding. {ECO:0000250}.
REGION 450 451 Required to promote base flipping.
REGION 468 469 Methylcytosine binding. {ECO:0000250}.
REGION 471 474 Required for formation of a 5-
methylcytosine-binding pocket.
REGION 483 486 Required for formation of a 5-
methylcytosine-binding pocket.
BINDING 321 321 Histone H3K4me0. {ECO:0000250}.
BINDING 332 332 Histone H3R2me0. {ECO:0000250}.
BINDING 335 335 Histone H3R2me0. {ECO:0000250}.
BINDING 474 474 Methylcytosine. {ECO:0000250}.
SITE 484 484 Required to confer preferential
recognition of cytosine over thymine.
{ECO:0000250}.
SITE 494 494 Required to discriminate between
hemimethylated DNA versus symmetrically
methylated DNA.
SITE 496 496 Required for affinity and specificity for
5-mCpG sequence.
MOD_RES 76 76 Phosphoserine.
{ECO:0000250|UniProtKB:Q96T88}.
MOD_RES 91 91 Phosphoserine.
{ECO:0000250|UniProtKB:Q96T88}.
MOD_RES 93 93 Phosphoserine.
{ECO:0000250|UniProtKB:Q7TPK1}.
MOD_RES 95 95 Phosphoserine.
{ECO:0000250|UniProtKB:Q7TPK1}.
MOD_RES 161 161 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 303 303 Phosphoserine; by PKA.
{ECO:0000250|UniProtKB:Q96T88}.
MOD_RES 373 373 Phosphoserine.
{ECO:0000250|UniProtKB:Q96T88}.
MOD_RES 404 404 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q96T88}.
MOD_RES 519 519 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 550 550 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q96T88}.
MOD_RES 639 639 Phosphoserine; by CDK1.
{ECO:0000250|UniProtKB:Q96T88}.
MOD_RES 649 649 Phosphoserine.
{ECO:0000250|UniProtKB:Q96T88}.
MOD_RES 656 656 Phosphoserine.
{ECO:0000244|PubMed:19144319}.
MOD_RES 759 759 Phosphoserine.
{ECO:0000250|UniProtKB:Q7TPK1}.
CROSSLNK 390 390 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q96T88}.
CROSSLNK 550 550 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q96T88}.
CROSSLNK 664 664 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q96T88}.
VAR_SEQ 293 301 PPPALRNTG -> R (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_044395.
MUTAGEN 148 148 F->A: Abolishes binding to histone
H3K9me3 and ability to repress
transcription of target genes.
{ECO:0000269|PubMed:21489993}.
MUTAGEN 730 730 H->A: Abolishes enzymatic activity.
{ECO:0000269|PubMed:14993289}.
CONFLICT 104 104 S -> P (in Ref. 3; BAE30624).
{ECO:0000305}.
CONFLICT 118 118 D -> G (in Ref. 3; BAE31708/BAE31605/
BAE30730/BAE29605). {ECO:0000305}.
CONFLICT 214 214 E -> K (in Ref. 6; BAB79496).
{ECO:0000305}.
CONFLICT 449 449 P -> L (in Ref. 6; BAB79496).
{ECO:0000305}.
CONFLICT 455 456 HG -> PW (in Ref. 6; BAB79496).
{ECO:0000305}.
CONFLICT 471 471 Y -> H (in Ref. 3; BAE27560).
{ECO:0000305}.
CONFLICT 637 637 P -> A (in Ref. 3; BAE26398).
{ECO:0000305}.
CONFLICT 702 702 I -> V (in Ref. 3; BAE31708/BAE31605/
BAE30730/BAE29605). {ECO:0000305}.
CONFLICT 753 753 F -> Y (in Ref. 5; AAH22167).
{ECO:0000305}.
TURN 405 408 {ECO:0000244|PDB:2ZKD}.
STRAND 434 437 {ECO:0000244|PDB:3FDE}.
HELIX 438 443 {ECO:0000244|PDB:3FDE}.
STRAND 453 457 {ECO:0000244|PDB:3FDE}.
TURN 458 460 {ECO:0000244|PDB:3FDE}.
STRAND 461 467 {ECO:0000244|PDB:3FDE}.
STRAND 475 477 {ECO:0000244|PDB:2ZO1}.
STRAND 478 484 {ECO:0000244|PDB:3FDE}.
TURN 492 494 {ECO:0000244|PDB:3FDE}.
HELIX 508 515 {ECO:0000244|PDB:3FDE}.
STRAND 517 519 {ECO:0000244|PDB:3FDE}.
HELIX 531 533 {ECO:0000244|PDB:3FDE}.
STRAND 537 543 {ECO:0000244|PDB:3FDE}.
TURN 546 548 {ECO:0000244|PDB:2ZO2}.
STRAND 550 552 {ECO:0000244|PDB:3FDE}.
STRAND 554 572 {ECO:0000244|PDB:3FDE}.
STRAND 576 586 {ECO:0000244|PDB:3FDE}.
HELIX 596 605 {ECO:0000244|PDB:3FDE}.
HELIX 615 622 {ECO:0000244|PDB:3FDE}.
SEQUENCE 782 AA; 88304 MW; DC5EEDFCDF69619B CRC64;
MWIQVRTMDG KETHTVNSLS RLTKVQELRK KIEEVFHVEP QLQRLFYRGK QMEDGHTLFD
YDVRLNDTIQ LLVRQSLALP LSTKERDSEL SDSDSGYGVG HSESDKSSTH GEGAAEADDK
TVWEDTDLGL YKVNEYVDVR DNIFGAWFEA QVVQVQKRAL SEDEPCSSSA VKTSEDDIMY
HVKYDDYPEH GVDIVKAKNV RARARTVIPW ENLEVGQVVM ANYNVDYPRK RGFWYDVEIC
RKRQTRTARE LYGNIRLLND SQLNNCRIMF VDEVLMIELP KERRPLIASP SQPPPALRNT
GKSGPSCRFC KDDENKPCRK CACHVCGGRE APEKQLLCDE CDMAFHLYCL KPPLTSVPPE
PEWYCPSCRT DSSEVVQAGE KLKESKKKAK MASATSSSRR DWGKGMACVG RTTECTIVPA
NHFGPIPGVP VGTMWRFRVQ VSESGVHRPH VAGIHGRSND GAYSLVLAGG YEDDVDNGNY
FTYTGSGGRD LSGNKRTAGQ SSDQKLTNNN RALALNCHSP INEKGAEAED WRQGKPVRVV
RNMKGGKHSK YAPAEGNRYD GIYKVVKYWP ERGKSGFLVW RYLLRRDDTE PEPWTREGKD
RTRQLGLTMQ YPEGYLEALA NKEKSRKRPA KALEQGPSSS KTGKSKQKST GPTLSSPRAS
KKSKLEPYTL SEQQANLIKE DKGNAKLWDD VLTSLQDGPY QIFLSKVKEA FQCICCQELV
FRPVTTVCQH NVCKDCLDRS FRAQVFSCPA CRFELDHSSP TRVNQPLQTI LNQLFPGYGS
GR


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