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E3 ubiquitin-protein ligase UHRF1 (EC 2.3.2.27) (Inverted CCAAT box-binding protein of 90 kDa) (Nuclear protein 95) (Nuclear zinc finger protein Np95) (HuNp95) (hNp95) (RING finger protein 106) (RING-type E3 ubiquitin transferase UHRF1) (Transcription factor ICBP90) (Ubiquitin-like PHD and RING finger domain-containing protein 1) (hUHRF1) (Ubiquitin-like-containing PHD and RING finger domains protein 1)

 UHRF1_HUMAN             Reviewed;         793 AA.
Q96T88; A0JBR2; A8K024; B2RBA9; Q2HIX7; Q8J022; Q9H6S6; Q9P115;
Q9P1U7;
07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
22-NOV-2017, entry version 158.
RecName: Full=E3 ubiquitin-protein ligase UHRF1;
EC=2.3.2.27;
AltName: Full=Inverted CCAAT box-binding protein of 90 kDa;
AltName: Full=Nuclear protein 95;
AltName: Full=Nuclear zinc finger protein Np95;
Short=HuNp95;
Short=hNp95;
AltName: Full=RING finger protein 106;
AltName: Full=RING-type E3 ubiquitin transferase UHRF1;
AltName: Full=Transcription factor ICBP90;
AltName: Full=Ubiquitin-like PHD and RING finger domain-containing protein 1;
Short=hUHRF1;
AltName: Full=Ubiquitin-like-containing PHD and RING finger domains protein 1;
Name=UHRF1; Synonyms=ICBP90, NP95, RNF106;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY,
DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, DNA-BINDING, INDUCTION, AND
FUNCTION.
TISSUE=Thymus;
PubMed=10646863;
Hopfner R., Mousli M., Jeltsch J.-M., Voulgaris A., Lutz Y., Marin C.,
Bellocq J.-P., Oudet P., Bronner C.;
"ICBP90, a novel human CCAAT binding protein, involved in the
regulation of topoisomerase IIa expression.";
Cancer Res. 60:121-128(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=17067204; DOI=10.1667/RR0459.1;
Muto M., Fujimori A., Nenoi M., Daino K., Matsuda Y., Kuroiwa A.,
Kubo E., Kanari Y., Utsuno M., Tsuji H., Ukai H., Mita K.,
Takahagi M., Tatsumi K.;
"Isolation and characterization of a novel human radiosusceptibility
gene, NP95.";
Radiat. Res. 166:723-733(2006).
[3]
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.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
LYS-379 AND THR-638.
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS HIS-240; LYS-379;
THR-638; MET-642 AND PHE-713.
NIEHS SNPs program;
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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).
[10]
INDUCTION, AND TISSUE SPECIFICITY.
PubMed=12838312; DOI=10.1038/sj.bjc.6601068;
Mousli M., Hopfner R., Abbady A.-Q., Monte D., Jeanblanc M., Oudet P.,
Louis B., Bronner C.;
"ICBP90 belongs to a new family of proteins with an expression that is
deregulated in cancer cells.";
Br. J. Cancer 89:120-127(2003).
[11]
PHOSPHORYLATION, PHOSPHORYLATION AT SER-298, AND MUTAGENESIS OF
SER-298; SER-651 AND SER-666.
PubMed=15178447; DOI=10.1016/j.bbrc.2004.05.028;
Trotzier M.-A., Bronner C., Bathami K., Mathieu E., Abbady A.-Q.,
Jeanblanc M., Muller C.D., Rochette-Egly C., Mousli M.;
"Phosphorylation of ICBP90 by protein kinase A enhances topoisomerase
IIalpha expression.";
Biochem. Biophys. Res. Commun. 319:590-595(2004).
[12]
INDUCTION, UBIQUITINATION, AND FUNCTION.
PubMed=15009091; DOI=10.1111/j.1356-9597.2004.00710.x;
Arima Y., Hirota T., Bronner C., Mousli M., Fujiwara T., Niwa S.,
Ishikawa H., Saya H.;
"Down-regulation of nuclear protein ICBP90 by p53/p21Cip1/WAF1-
dependent DNA-damage checkpoint signals contributes to cell cycle
arrest at G1/S transition.";
Genes Cells 9:131-142(2004).
[13]
FUNCTION, INDUCTION, TISSUE SPECIFICITY, DNA-BINDING, AND INTERACTION
WITH HDAC1 AND UHRF1BP1.
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).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-287 AND SER-639, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-639, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[16]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH DNMT1.
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).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-287, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[18]
FUNCTION, SUBCELLULAR LOCATION, AND AUTOUBIQUITINATION.
PubMed=17967883; DOI=10.1128/MCB.01598-07;
Karagianni P., Amazit L., Qin J., Wong J.;
"ICBP90, a novel methyl K9 H3 binding protein linking protein
ubiquitination with heterochromatin formation.";
Mol. Cell. Biol. 28:705-717(2008).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76; SER-91 AND SER-707,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[20]
INVOLVEMENT IN CANCER.
PubMed=19491893; DOI=10.1038/sj.bjc.6605123;
Unoki M., Kelly J.D., Neal D.E., Ponder B.A., Nakamura Y.,
Hamamoto R.;
"UHRF1 is a novel molecular marker for diagnosis and the prognosis of
bladder cancer.";
Br. J. Cancer 101:98-105(2009).
[21]
FUNCTION, SUBCELLULAR LOCATION, AND 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).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-287, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[23]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-399 AND LYS-546, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[24]
MUTAGENESIS OF TYR-188 AND TYR-191.
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).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76; SER-287; SER-639 AND
SER-707, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[26]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[27]
FUNCTION, AUTOUBIQUITINATION, DEUBIQUITINATION BY USP7, AND
INTERACTION WITH USP7 AND DNMT1.
PubMed=21745816; DOI=10.1093/nar/gkr528;
Felle M., Joppien S., Nemeth A., Diermeier S., Thalhammer V.,
Dobner T., Kremmer E., Kappler R., Langst G.;
"The USP7/Dnmt1 complex stimulates the DNA methylation activity of
Dnmt1 and regulates the stability of UHRF1.";
Nucleic Acids Res. 39:8355-8365(2011).
[28]
HYDROXYMETHYLCYTOSINE-BINDING.
PubMed=21731699; DOI=10.1371/journal.pone.0021306;
Frauer C., Hoffmann T., Bultmann S., Casa V., Cardoso M.C., Antes I.,
Leonhardt H.;
"Recognition of 5-hydroxymethylcytosine by the Uhrf1 SRA domain.";
PLoS ONE 6:E21306-E21306(2011).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-287 AND SER-651, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[30]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76; SER-91; SER-287;
SER-368; SER-639; SER-707 AND SER-709, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[31]
FUNCTION, INTERACTION WITH PML, AND MUTAGENESIS OF HIS-741.
PubMed=22945642; DOI=10.1038/onc.2012.406;
Guan D., Factor D., Liu Y., Wang Z., Kao H.Y.;
"The epigenetic regulator UHRF1 promotes ubiquitination-mediated
degradation of the tumor-suppressor protein promyelocytic leukemia
protein.";
Oncogene 32:3819-3828(2013).
[32]
INVOLVEMENT IN CANCER.
PubMed=22286757; DOI=10.1038/onc.2012.3;
Sabatino L., Fucci A., Pancione M., Carafa V., Nebbioso A.,
Pistore C., Babbio F., Votino C., Laudanna C., Ceccarelli M.,
Altucci L., Bonapace I.M., Colantuoni V.;
"UHRF1 coordinates peroxisome proliferator activated receptor gamma
(PPARG) epigenetic silencing and mediates colorectal cancer
progression.";
Oncogene 31:5061-5072(2012).
[33]
INVOLVEMENT IN CANCER.
PubMed=22330138; DOI=10.1038/onc.2011.641;
Babbio F., Pistore C., Curti L., Castiglioni I., Kunderfranco P.,
Brino L., Oudet P., Seiler R., Thalman G.N., Roggero E., Sarti M.,
Pinton S., Mello-Grand M., Chiorino G., Catapano C.V., Carbone G.M.,
Bonapace I.M.;
"The SRA protein UHRF1 promotes epigenetic crosstalks and is involved
in prostate cancer progression.";
Oncogene 31:4878-4887(2012).
[34]
AUTOUBIQUITINATION, DEUBIQUITINATION BY USP7, INTERACTION WITH USP7,
PHOSPHORYLATION AT SER-639, AND MUTAGENESIS OF SER-639.
PubMed=22411829; DOI=10.1073/pnas.1116349109;
Ma H., Chen H., Guo X., Wang Z., Sowa M.E., Zheng L., Hu S., Zeng P.,
Guo R., Diao J., Lan F., Harper J.W., Shi Y.G., Xu Y., Shi Y.;
"M phase phosphorylation of the epigenetic regulator UHRF1 regulates
its physical association with the deubiquitylase USP7 and stability.";
Proc. Natl. Acad. Sci. U.S.A. 109:4828-4833(2012).
[35]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-385; LYS-546 AND LYS-670,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[36]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-279 AND LYS-670, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[37]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-76.
Structural genomics consortium (SGC);
"Ubiquitin-like domain of human nuclear zinc finger protein NP95.";
Submitted (JAN-2006) to the PDB data bank.
[38]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 408-643.
PubMed=18931436; DOI=10.1107/S1744309108027462;
Delagoutte B., Lallous N., Birck C., Oudet P., Samama J.P.;
"Expression, purification, crystallization and preliminary
crystallographic study of the SRA domain of the human UHRF1 protein.";
Acta Crystallogr. F 64:922-925(2008).
[39]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 414-617, AND MUTAGENESIS OF
ARG-433; ARG-443; TYR-466 AND ARG-491.
PubMed=18945682; DOI=10.1074/jbc.C800169200;
Qian C., Li S., Jakoncic J., Zeng L., Walsh M.J., Zhou M.M.;
"Structure and hemimethylated CpG binding of the SRA domain from human
UHRF1.";
J. Biol. Chem. 283:34490-34494(2008).
[40]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 414-617 IN COMPLEX WITH
HEMIMETHYLATED DNA, AND MUTAGENESIS OF GLY-448; ASN-489 AND ARG-491.
PubMed=18772889; DOI=10.1038/nature07273;
Avvakumov G.V., Walker J.R., Xue S., Li Y., Duan S., Bronner C.,
Arrowsmith C.H., Dhe-Paganon S.;
"Structural basis for recognition of hemi-methylated DNA by the SRA
domain of human UHRF1.";
Nature 455:822-825(2008).
[41]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 298-366, AND MUTAGENESIS OF
ASP-334 AND ASP-337.
PubMed=21808300; DOI=10.1038/cr.2011.124;
Hu L., Li Z., Wang P., Lin Y., Xu Y.;
"Crystal structure of PHD domain of UHRF1 and insights into
recognition of unmodified histone H3 arginine residue 2.";
Cell Res. 21:1374-1378(2011).
[42]
STRUCTURE BY NMR OF 298-366, AND MUTAGENESIS OF ASP-334 AND ASP-337.
PubMed=21808299; DOI=10.1038/cr.2011.123;
Wang C., Shen J., Yang Z., Chen P., Zhao B., Hu W., Lan W., Tong X.,
Wu H., Li G., Cao C.;
"Structural basis for site-specific reading of unmodified R2 of
histone H3 tail by UHRF1 PHD finger.";
Cell Res. 21:1379-1382(2011).
[43]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 126-285, STRUCTURE BY NMR OF
126-285, AND MUTAGENESIS OF ASP-142; ASP-145; PHE-152; GLU-153;
TYR-188 AND ASP-190.
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).
[44]
X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 298-367 IN COMPLEX WITH ZINC
AND HISTONE H3 PEPTIDE, FUNCTION, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF 334-ASP-GLU-335.
PubMed=21777816; DOI=10.1016/j.molcel.2011.07.006;
Rajakumara E., Wang Z., Ma H., Hu L., Chen H., Lin Y., Guo R., Wu F.,
Li H., Lan F., Shi Y.G., Xu Y., Patel D.J., Shi Y.;
"PHD finger recognition of unmodified histone H3R2 links UHRF1 to
regulation of euchromatic gene expression.";
Mol. Cell 43:275-284(2011).
[45]
X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 314-367, AND MUTAGENESIS OF
GLN-330; ASP-334 AND ASP-337.
PubMed=22096602; DOI=10.1371/journal.pone.0027599;
Lallous N., Legrand P., McEwen A.G., Ramon-Maiques S., Samama J.P.,
Birck C.;
"The PHD finger of human UHRF1 reveals a new subgroup of unmethylated
histone H3 tail readers.";
PLoS ONE 6:E27599-E27599(2011).
[46]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 299-364 IN COMPLEX WITH
HISTONE H3 PEPTIDE.
PubMed=22100450; DOI=10.1016/j.jmb.2011.11.012;
Xie S., Jakoncic J., Qian C.;
"UHRF1 double tudor domain and the adjacent PHD finger act together to
recognize K9me3-containing histone H3 tail.";
J. Mol. Biol. 415:318-328(2012).
[47]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 134-367 IN COMPLEX WITH ZINC
AND HISTONE H3 PEPTIDE, PHOSPHORYLATION AT SER-298, AND MUTAGENESIS OF
295-ARG-ARG-296.
PubMed=22837395; DOI=10.1073/pnas.1203701109;
Arita K., Isogai S., Oda T., Unoki M., Sugita K., Sekiyama N.,
Kuwata K., Hamamoto R., Tochio H., Sato M., Ariyoshi M., Shirakawa M.;
"Recognition of modification status on a histone H3 tail by linked
histone reader modules of the epigenetic regulator UHRF1.";
Proc. Natl. Acad. Sci. U.S.A. 109:12950-12955(2012).
-!- 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:10646863,
ECO:0000269|PubMed:15009091, ECO:0000269|PubMed:15361834,
ECO:0000269|PubMed:17673620, ECO:0000269|PubMed:17967883,
ECO:0000269|PubMed:19056828, ECO:0000269|PubMed:21745816,
ECO:0000269|PubMed:21777816, ECO:0000269|PubMed:22945642}.
-!- 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 DNMT3A and DNMT3B (By similarity).
Interacts with DNMT1; the interaction is direct. Interacts with
USP7; leading to its deubiquitination. Interacts with histone H3.
Interacts with HDAC1, but not with HDAC2. Interacts with UHRF1BP1.
Interacts with PML. Interacts with EHMT2. Binds hemimethylated CpG
containing oligonucleotides. {ECO:0000250,
ECO:0000269|PubMed:15361834, ECO:0000269|PubMed:17673620,
ECO:0000269|PubMed:18772889, ECO:0000269|PubMed:19056828,
ECO:0000269|PubMed:21745816, ECO:0000269|PubMed:21777816,
ECO:0000269|PubMed:22100450, ECO:0000269|PubMed:22411829,
ECO:0000269|PubMed:22837395, ECO:0000269|PubMed:22945642}.
-!- INTERACTION:
P26358:DNMT1; NbExp=12; IntAct=EBI-1548946, EBI-719459;
Q9Y6K1:DNMT3A; NbExp=7; IntAct=EBI-1548946, EBI-923653;
Q9UBC3:DNMT3B; NbExp=7; IntAct=EBI-1548946, EBI-80125;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00358, ECO:0000269|PubMed:10646863,
ECO:0000269|PubMed:17673620, ECO:0000269|PubMed:17967883,
ECO:0000269|PubMed:19056828, ECO:0000269|PubMed:21777816}.
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=Q96T88-1; Sequence=Displayed;
Name=2;
IsoId=Q96T88-2; Sequence=VSP_044394;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in thymus, bone marrow, testis, lung
and heart. Overexpressed in breast cancer.
{ECO:0000269|PubMed:10646863, ECO:0000269|PubMed:12838312,
ECO:0000269|PubMed:15361834}.
-!- DEVELOPMENTAL STAGE: Expressed in fetal thymus, liver and kidney.
{ECO:0000269|PubMed:10646863}.
-!- INDUCTION: Up-regulated in proliferating cells, and down-regulated
in quiescent cells. Down-regulated upon adriamycin-induced DNA
damage, in a p53/TP53 and CDKN1A-dependent way. Induced by E2F1
transcription factor. {ECO:0000269|PubMed:10646863,
ECO:0000269|PubMed:12838312, ECO:0000269|PubMed:15009091,
ECO:0000269|PubMed:15361834}.
-!- 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, PubMed:21777816 and PubMed:22100450). 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 (PubMed:22837395).
{ECO:0000269|PubMed:22837395}.
-!- 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:17673620). It 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:18772889). The
YDG domain also recognizes and binds 5-hydroxymethylcytosine
(5hmC) (PubMed:21731699). {ECO:0000269|PubMed:17673620,
ECO:0000269|PubMed:18772889, ECO:0000269|PubMed:21731699}.
-!- DOMAIN: The RING finger is required for ubiquitin ligase activity.
{ECO:0000250}.
-!- PTM: Phosphorylation at Ser-298 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.
{ECO:0000269|PubMed:15178447, ECO:0000269|PubMed:22411829,
ECO:0000269|PubMed:22837395}.
-!- 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:15009091, ECO:0000269|PubMed:17967883,
ECO:0000269|PubMed:21745816, ECO:0000269|PubMed:22411829}.
-!- DISEASE: Note=Defects in UHRF1 may be a cause of cancers.
Overexpressed in many different forms of human cancers, including
bladder, breast, cervical, colorectal and prostate cancers, as
well as pancreatic adenocarcinomas, rhabdomyosarcomas and gliomas.
Plays an important role in the correlation of histone modification
and gene silencing in cancer progression. Expression is associated
with a poor prognosis in patients with various cancers, suggesting
that it participates in cancer progression.
-!- SEQUENCE CAUTION:
Sequence=BAB15177.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/uhrf1/";
-----------------------------------------------------------------------
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EMBL; AF129507; AAF28469.1; -; mRNA.
EMBL; AB177623; BAF36719.1; -; mRNA.
EMBL; AB177624; BAF36720.1; -; mRNA.
EMBL; AB075601; BAC20576.1; -; mRNA.
EMBL; AF274048; AAK55744.1; -; mRNA.
EMBL; EF560733; ABQ59043.1; -; mRNA.
EMBL; AK025578; BAB15177.1; ALT_INIT; mRNA.
EMBL; AK289389; BAF82078.1; -; mRNA.
EMBL; AK314579; BAG37156.1; -; mRNA.
EMBL; AY787925; AAV40831.1; -; Genomic_DNA.
EMBL; AC027319; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC053467; AAF64067.1; -; Genomic_DNA.
EMBL; CH471139; EAW69187.1; -; Genomic_DNA.
EMBL; BC113875; AAI13876.2; -; mRNA.
CCDS; CCDS74262.1; -. [Q96T88-2]
CCDS; CCDS74263.1; -. [Q96T88-1]
RefSeq; NP_001041666.1; NM_001048201.2. [Q96T88-1]
RefSeq; NP_001276979.1; NM_001290050.1. [Q96T88-1]
RefSeq; NP_001276980.1; NM_001290051.1. [Q96T88-1]
RefSeq; NP_001276981.1; NM_001290052.1. [Q96T88-1]
RefSeq; NP_037414.3; NM_013282.4.
UniGene; Hs.108106; -.
PDB; 2FAZ; X-ray; 2.00 A; A/B=1-76.
PDB; 2L3R; NMR; -; A=126-285.
PDB; 2LGG; NMR; -; A=298-366.
PDB; 2LGK; NMR; -; A=298-366.
PDB; 2LGL; NMR; -; A=298-366.
PDB; 2PB7; X-ray; 1.90 A; A=408-643.
PDB; 3ASK; X-ray; 2.90 A; A/B/C/D=134-367.
PDB; 3ASL; X-ray; 1.41 A; A=298-367.
PDB; 3BI7; X-ray; 1.70 A; A=414-617.
PDB; 3CLZ; X-ray; 2.20 A; A/B/C/D=414-617.
PDB; 3DB3; X-ray; 2.40 A; A=126-285.
PDB; 3DB4; X-ray; 2.40 A; A=126-285.
PDB; 3DWH; X-ray; 1.95 A; A=414-617.
PDB; 3FL2; X-ray; 1.75 A; A=672-793.
PDB; 3SHB; X-ray; 1.80 A; A=298-366.
PDB; 3SOU; X-ray; 1.80 A; A/B=298-367.
PDB; 3SOW; X-ray; 1.95 A; A/B=298-367.
PDB; 3SOX; X-ray; 2.65 A; A/B=298-367.
PDB; 3T6R; X-ray; 1.95 A; A/B=299-364.
PDB; 3ZVY; X-ray; 1.95 A; A/B=296-367.
PDB; 3ZVZ; X-ray; 1.45 A; B=314-367.
PDB; 4GY5; X-ray; 2.96 A; A/B/C/D=134-366.
PDB; 4QQD; X-ray; 2.28 A; A/B=126-285.
PDB; 5C6D; X-ray; 2.29 A; C/D=634-665.
PDB; 5IAY; NMR; -; A=134-285, B=642-657.
PDBsum; 2FAZ; -.
PDBsum; 2L3R; -.
PDBsum; 2LGG; -.
PDBsum; 2LGK; -.
PDBsum; 2LGL; -.
PDBsum; 2PB7; -.
PDBsum; 3ASK; -.
PDBsum; 3ASL; -.
PDBsum; 3BI7; -.
PDBsum; 3CLZ; -.
PDBsum; 3DB3; -.
PDBsum; 3DB4; -.
PDBsum; 3DWH; -.
PDBsum; 3FL2; -.
PDBsum; 3SHB; -.
PDBsum; 3SOU; -.
PDBsum; 3SOW; -.
PDBsum; 3SOX; -.
PDBsum; 3T6R; -.
PDBsum; 3ZVY; -.
PDBsum; 3ZVZ; -.
PDBsum; 4GY5; -.
PDBsum; 4QQD; -.
PDBsum; 5C6D; -.
PDBsum; 5IAY; -.
ProteinModelPortal; Q96T88; -.
SMR; Q96T88; -.
BioGrid; 118893; 77.
IntAct; Q96T88; 15.
MINT; MINT-2815626; -.
BindingDB; Q96T88; -.
ChEMBL; CHEMBL2424510; -.
iPTMnet; Q96T88; -.
PhosphoSitePlus; Q96T88; -.
BioMuta; UHRF1; -.
DMDM; 67462077; -.
EPD; Q96T88; -.
MaxQB; Q96T88; -.
PeptideAtlas; Q96T88; -.
PRIDE; Q96T88; -.
DNASU; 29128; -.
Ensembl; ENST00000612630; ENSP00000484739; ENSG00000276043. [Q96T88-1]
Ensembl; ENST00000615884; ENSP00000478601; ENSG00000276043. [Q96T88-1]
Ensembl; ENST00000616255; ENSP00000478348; ENSG00000276043. [Q96T88-1]
Ensembl; ENST00000624301; ENSP00000485604; ENSG00000276043. [Q96T88-1]
GeneID; 29128; -.
KEGG; hsa:29128; -.
UCSC; uc032hkj.2; human. [Q96T88-1]
CTD; 29128; -.
DisGeNET; 29128; -.
EuPathDB; HostDB:ENSG00000276043.4; -.
GeneCards; UHRF1; -.
HGNC; HGNC:12556; UHRF1.
HPA; HPA049408; -.
MIM; 607990; gene.
neXtProt; NX_Q96T88; -.
OpenTargets; ENSG00000276043; -.
PharmGKB; PA37196; -.
GeneTree; ENSGT00390000008296; -.
HOGENOM; HOG000124662; -.
HOVERGEN; HBG059298; -.
InParanoid; Q96T88; -.
KO; K10638; -.
PhylomeDB; Q96T88; -.
Reactome; R-HSA-5334118; DNA methylation.
SignaLink; Q96T88; -.
SIGNOR; Q96T88; -.
UniPathway; UPA00143; -.
EvolutionaryTrace; Q96T88; -.
GeneWiki; UHRF1; -.
GenomeRNAi; 29128; -.
PRO; PR:Q96T88; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000276043; -.
CleanEx; HS_UHRF1; -.
ExpressionAtlas; Q96T88; baseline and differential.
Genevisible; Q96T88; HS.
GO; GO:0000791; C:euchromatin; IDA:UniProtKB.
GO; GO:0000792; C:heterochromatin; IDA:UniProtKB.
GO; GO:0000790; C:nuclear chromatin; IDA:UniProtKB.
GO; GO:0005720; C:nuclear heterochromatin; IBA:GO_Central.
GO; GO:0016363; C:nuclear matrix; ISS:BHF-UCL.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0005657; C:replication fork; IDA:UniProtKB.
GO; GO:0000987; F:core promoter proximal region sequence-specific DNA binding; IDA:BHF-UCL.
GO; GO:0044729; F:hemi-methylated DNA-binding; IDA:UniProtKB.
GO; GO:0042393; F:histone binding; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; ISS:BHF-UCL.
GO; GO:0008327; F:methyl-CpG binding; IDA:UniProtKB.
GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB.
GO; GO:0031493; F:nucleosomal histone binding; ISS:BHF-UCL.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; TAS:ProtInc.
GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:BHF-UCL.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0008283; P:cell proliferation; IEP:BHF-UCL.
GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
GO; GO:0010390; P:histone monoubiquitination; ISS:BHF-UCL.
GO; GO:0016574; P:histone ubiquitination; IDA: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; IDA:BHF-UCL.
GO; GO:2000373; P:positive regulation of DNA topoisomerase (ATP-hydrolyzing) activity; IC:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IC:BHF-UCL.
GO; GO:0051865; P:protein autoubiquitination; IDA:UniProtKB.
GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IDA: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;
Polymorphism; Reference proteome; Repeat; Repressor; Transcription;
Transcription regulation; Transferase; Ubl conjugation;
Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 793 E3 ubiquitin-protein ligase UHRF1.
/FTId=PRO_0000056144.
DOMAIN 1 78 Ubiquitin-like. {ECO:0000255|PROSITE-
ProRule:PRU00214}.
DOMAIN 419 582 YDG. {ECO:0000255|PROSITE-
ProRule:PRU00358}.
ZN_FING 310 366 PHD-type. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
ZN_FING 724 763 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
REGION 133 209 Tudor-like 1.
REGION 216 283 Tudor-like 2.
REGION 296 301 Linker.
REGION 333 337 Histone H3R2me0 binding.
REGION 353 355 Histone H3R2me0 binding.
REGION 445 446 Required to promote base flipping.
{ECO:0000250}.
REGION 463 464 Methylcytosine binding.
REGION 466 469 Required for formation of a 5-
methylcytosine-binding pocket.
REGION 478 481 Required for formation of a 5-
methylcytosine-binding pocket.
BINDING 316 316 Histone H3K4me0.
BINDING 327 327 Histone H3R2me0.
BINDING 330 330 Histone H3R2me0.
BINDING 469 469 Methylcytosine.
SITE 479 479 Required to confer preferential
recognition of cytosine over thymine.
SITE 489 489 Required to discriminate between
hemimethylated DNA versus symmetrically
methylated DNA.
SITE 491 491 Required for affinity and specificity for
5-mCpG sequence.
MOD_RES 76 76 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 91 91 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 95 95 Phosphoserine.
{ECO:0000250|UniProtKB:Q7TPK1}.
MOD_RES 165 165 Phosphoserine.
{ECO:0000250|UniProtKB:Q8VDF2}.
MOD_RES 287 287 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 298 298 Phosphoserine; by PKA.
{ECO:0000269|PubMed:15178447,
ECO:0000269|PubMed:22837395}.
MOD_RES 368 368 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 399 399 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 546 546 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 639 639 Phosphoserine; by CDK1.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:22411829}.
MOD_RES 651 651 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 707 707 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 709 709 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 279 279 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 385 385 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447}.
CROSSLNK 546 546 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25218447}.
CROSSLNK 670 670 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 1 M -> MGVFAVPPLSSDTM (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_044394.
VARIANT 240 240 D -> H (in dbSNP:rs17886098).
{ECO:0000269|Ref.6}.
/FTId=VAR_022554.
VARIANT 379 379 E -> K (in dbSNP:rs17885791).
{ECO:0000269|PubMed:14702039,
ECO:0000269|Ref.6}.
/FTId=VAR_022555.
VARIANT 638 638 A -> T (in dbSNP:rs17883331).
{ECO:0000269|PubMed:14702039,
ECO:0000269|Ref.6}.
/FTId=VAR_022556.
VARIANT 642 642 T -> M (in dbSNP:rs17884843).
{ECO:0000269|Ref.6}.
/FTId=VAR_022557.
VARIANT 713 713 L -> F (in dbSNP:rs17883563).
{ECO:0000269|Ref.6}.
/FTId=VAR_022558.
MUTAGEN 142 142 D->A: Impaired binding to histone H3
without affecting the protein folding;
when associated with A-153.
{ECO:0000269|PubMed:21489993}.
MUTAGEN 145 145 D->A: Impaired binding to histone H3.
{ECO:0000269|PubMed:21489993}.
MUTAGEN 152 152 F->A: Impaired binding to histone H3.
{ECO:0000269|PubMed:21489993}.
MUTAGEN 153 153 E->A: Impaired binding to histone H3
without affecting the protein folding;
when associated with A-142.
{ECO:0000269|PubMed:21489993}.
MUTAGEN 188 188 Y->A: Impaired binding to histone H3.
{ECO:0000269|PubMed:20026581,
ECO:0000269|PubMed:21489993}.
MUTAGEN 190 190 D->A: Slightly impaired binding to
histone H3.
{ECO:0000269|PubMed:21489993}.
MUTAGEN 191 191 Y->A: Impaired binding to histone H3.
{ECO:0000269|PubMed:20026581}.
MUTAGEN 295 296 RR->AA: Disrupts the simultaneous binding
to H3R2me0 and H3K9me3.
{ECO:0000269|PubMed:22837395}.
MUTAGEN 298 298 S->A: Diminishes phosphorylation by PKA.
{ECO:0000269|PubMed:15178447}.
MUTAGEN 330 330 Q->A,K: Does not affect ability to bind
histone H3 peptide.
{ECO:0000269|PubMed:22096602}.
MUTAGEN 334 335 DE->AA: Abolishes binding to histone H3.
{ECO:0000269|PubMed:21777816}.
MUTAGEN 334 334 D->A: Impaired binding to histone H3.
{ECO:0000269|PubMed:21808299,
ECO:0000269|PubMed:21808300,
ECO:0000269|PubMed:22096602}.
MUTAGEN 337 337 D->A: Impaired binding to histone H3.
{ECO:0000269|PubMed:21808299,
ECO:0000269|PubMed:21808300,
ECO:0000269|PubMed:22096602}.
MUTAGEN 433 433 R->A: Does not affect ability to bind
DNA. {ECO:0000269|PubMed:18945682}.
MUTAGEN 443 443 R->A: Decreased ability to bind DNA.
{ECO:0000269|PubMed:18945682}.
MUTAGEN 448 448 G->D: Decreased affinity for DNA.
{ECO:0000269|PubMed:18772889}.
MUTAGEN 466 466 Y->G: Decreased ability to bind DNA.
{ECO:0000269|PubMed:18945682}.
MUTAGEN 469 469 D->G: Abolishes ability to bind
hemimethylated DNA.
MUTAGEN 489 489 N->A: Abolishes specificity to
hemimethylated DNA.
{ECO:0000269|PubMed:18772889}.
MUTAGEN 491 491 R->A: Decreased binding to methylated DNA
but does not affect ability to bind DNA.
{ECO:0000269|PubMed:18772889,
ECO:0000269|PubMed:18945682}.
MUTAGEN 639 639 S->A: Prevents phosphorylation by CDK1
during M phase, leading to increased
stability. {ECO:0000269|PubMed:22411829}.
MUTAGEN 639 639 S->D: Mimics phosphorylation; impaired
interaction with USP7, leading to
decreased stability.
{ECO:0000269|PubMed:22411829}.
MUTAGEN 651 651 S->A: No effect on in vitro
phosphorylation by PKA.
{ECO:0000269|PubMed:15178447}.
MUTAGEN 666 666 S->A: No effect on in vitro
phosphorylation by PKA.
{ECO:0000269|PubMed:15178447}.
MUTAGEN 741 741 H->A: Abolishes E3 ubiquitin-protein
ligase activity.
{ECO:0000269|PubMed:22945642}.
CONFLICT 383 383 K -> E (in Ref. 5; BAF82078).
{ECO:0000305}.
CONFLICT 383 383 K -> N (in Ref. 1; AAF28469).
{ECO:0000305}.
CONFLICT 457 457 A -> S (in Ref. 1; AAF28469).
{ECO:0000305}.
CONFLICT 675 675 S -> N (in Ref. 5; BAF82078).
{ECO:0000305}.
STRAND 1 7 {ECO:0000244|PDB:2FAZ}.
STRAND 13 19 {ECO:0000244|PDB:2FAZ}.
HELIX 25 36 {ECO:0000244|PDB:2FAZ}.
HELIX 40 42 {ECO:0000244|PDB:2FAZ}.
STRAND 43 47 {ECO:0000244|PDB:2FAZ}.
TURN 58 62 {ECO:0000244|PDB:2FAZ}.
STRAND 68 73 {ECO:0000244|PDB:2FAZ}.
TURN 127 129 {ECO:0000244|PDB:2L3R}.
STRAND 140 144 {ECO:0000244|PDB:4QQD}.
TURN 146 148 {ECO:0000244|PDB:4QQD}.
STRAND 151 161 {ECO:0000244|PDB:4QQD}.
STRAND 164 167 {ECO:0000244|PDB:2L3R}.
TURN 179 181 {ECO:0000244|PDB:2L3R}.
STRAND 182 188 {ECO:0000244|PDB:4QQD}.
HELIX 192 194 {ECO:0000244|PDB:4QQD}.
STRAND 196 200 {ECO:0000244|PDB:4QQD}.
HELIX 201 203 {ECO:0000244|PDB:4QQD}.
STRAND 204 206 {ECO:0000244|PDB:4QQD}.
STRAND 210 212 {ECO:0000244|PDB:2L3R}.
HELIX 214 216 {ECO:0000244|PDB:4QQD}.
STRAND 222 227 {ECO:0000244|PDB:4QQD}.
STRAND 229 231 {ECO:0000244|PDB:4QQD}.
STRAND 237 248 {ECO:0000244|PDB:4QQD}.
STRAND 253 260 {ECO:0000244|PDB:4QQD}.
STRAND 262 272 {ECO:0000244|PDB:4QQD}.
HELIX 274 276 {ECO:0000244|PDB:2L3R}.
STRAND 277 279 {ECO:0000244|PDB:2L3R}.
STRAND 283 286 {ECO:0000244|PDB:3ASK}.
TURN 303 307 {ECO:0000244|PDB:3ASL}.
STRAND 309 311 {ECO:0000244|PDB:2LGG}.
TURN 314 316 {ECO:0000244|PDB:3ASL}.
TURN 319 321 {ECO:0000244|PDB:3ASL}.
STRAND 323 325 {ECO:0000244|PDB:2LGL}.
HELIX 327 329 {ECO:0000244|PDB:3ASL}.
STRAND 330 332 {ECO:0000244|PDB:3ASL}.
TURN 334 336 {ECO:0000244|PDB:3ASL}.
STRAND 339 341 {ECO:0000244|PDB:3ASL}.
HELIX 342 344 {ECO:0000244|PDB:3ASL}.
STRAND 345 347 {ECO:0000244|PDB:3ASL}.
STRAND 354 356 {ECO:0000244|PDB:3ASL}.
TURN 361 363 {ECO:0000244|PDB:3ASL}.
STRAND 417 419 {ECO:0000244|PDB:3DWH}.
STRAND 429 432 {ECO:0000244|PDB:3BI7}.
HELIX 433 438 {ECO:0000244|PDB:3BI7}.
TURN 439 442 {ECO:0000244|PDB:3DWH}.
STRAND 448 452 {ECO:0000244|PDB:3BI7}.
TURN 453 455 {ECO:0000244|PDB:3BI7}.
STRAND 456 462 {ECO:0000244|PDB:3BI7}.
STRAND 473 479 {ECO:0000244|PDB:3BI7}.
TURN 487 489 {ECO:0000244|PDB:3CLZ}.
HELIX 503 511 {ECO:0000244|PDB:3BI7}.
STRAND 512 514 {ECO:0000244|PDB:3BI7}.
TURN 518 520 {ECO:0000244|PDB:3BI7}.
HELIX 527 529 {ECO:0000244|PDB:3BI7}.
STRAND 533 538 {ECO:0000244|PDB:3BI7}.
HELIX 539 544 {ECO:0000244|PDB:3BI7}.
STRAND 546 548 {ECO:0000244|PDB:3CLZ}.
STRAND 550 568 {ECO:0000244|PDB:3BI7}.
STRAND 572 582 {ECO:0000244|PDB:3BI7}.
HELIX 592 601 {ECO:0000244|PDB:3BI7}.
HELIX 611 617 {ECO:0000244|PDB:3BI7}.
HELIX 678 686 {ECO:0000244|PDB:3FL2}.
HELIX 688 690 {ECO:0000244|PDB:3FL2}.
HELIX 691 699 {ECO:0000244|PDB:3FL2}.
STRAND 706 708 {ECO:0000244|PDB:3FL2}.
HELIX 710 721 {ECO:0000244|PDB:3FL2}.
TURN 725 727 {ECO:0000244|PDB:3FL2}.
STRAND 728 730 {ECO:0000244|PDB:3FL2}.
STRAND 732 736 {ECO:0000244|PDB:3FL2}.
STRAND 742 744 {ECO:0000244|PDB:3FL2}.
HELIX 745 753 {ECO:0000244|PDB:3FL2}.
TURN 760 762 {ECO:0000244|PDB:3FL2}.
HELIX 776 785 {ECO:0000244|PDB:3FL2}.
TURN 787 792 {ECO:0000244|PDB:3FL2}.
SEQUENCE 793 AA; 89814 MW; E65B15657525C89F CRC64;
MWIQVRTMDG RQTHTVDSLS RLTKVEELRR KIQELFHVEP GLQRLFYRGK QMEDGHTLFD
YEVRLNDTIQ LLVRQSLVLP HSTKERDSEL SDTDSGCCLG QSESDKSSTH GEAAAETDSR
PADEDMWDET ELGLYKVNEY VDARDTNMGA WFEAQVVRVT RKAPSRDEPC SSTSRPALEE
DVIYHVKYDD YPENGVVQMN SRDVRARART IIKWQDLEVG QVVMLNYNPD NPKERGFWYD
AEISRKRETR TARELYANVV LGDDSLNDCR IIFVDEVFKI ERPGEGSPMV DNPMRRKSGP
SCKHCKDDVN RLCRVCACHL CGGRQDPDKQ LMCDECDMAF HIYCLDPPLS SVPSEDEWYC
PECRNDASEV VLAGERLRES KKKAKMASAT SSSQRDWGKG MACVGRTKEC TIVPSNHYGP
IPGIPVGTMW RFRVQVSESG VHRPHVAGIH GRSNDGAYSL VLAGGYEDDV DHGNFFTYTG
SGGRDLSGNK RTAEQSCDQK LTNTNRALAL NCFAPINDQE GAEAKDWRSG KPVRVVRNVK
GGKNSKYAPA EGNRYDGIYK VVKYWPEKGK SGFLVWRYLL RRDDDEPGPW TKEGKDRIKK
LGLTMQYPEG YLEALANRER EKENSKREEE EQQEGGFASP RTGKGKWKRK SAGGGPSRAG
SPRRTSKKTK VEPYSLTAQQ SSLIREDKSN AKLWNEVLAS LKDRPASGSP FQLFLSKVEE
TFQCICCQEL VFRPITTVCQ HNVCKDCLDR SFRAQVFSCP ACRYDLGRSY AMQVNQPLQT
VLNQLFPGYG NGR


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