ID UHRF1_HUMAN Reviewed; 793 AA. AC Q96T88; A0JBR2; A8K024; B2RBA9; Q2HIX7; Q8J022; Q9H6S6; Q9P115; Q9P1U7; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 27-MAR-2024, entry version 202. DE RecName: Full=E3 ubiquitin-protein ligase UHRF1; DE EC=2.3.2.27 {ECO:0000269|PubMed:37728657}; DE AltName: Full=Inverted CCAAT box-binding protein of 90 kDa; DE AltName: Full=Nuclear protein 95; DE AltName: Full=Nuclear zinc finger protein Np95; DE Short=HuNp95; DE Short=hNp95; DE AltName: Full=RING finger protein 106; DE AltName: Full=RING-type E3 ubiquitin transferase UHRF1; DE AltName: Full=Transcription factor ICBP90; DE AltName: Full=Ubiquitin-like PHD and RING finger domain-containing protein 1; DE Short=hUHRF1; DE AltName: Full=Ubiquitin-like-containing PHD and RING finger domains protein 1; GN Name=UHRF1; Synonyms=ICBP90, NP95, RNF106; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, DEVELOPMENTAL RP STAGE, SUBCELLULAR LOCATION, DNA-BINDING, INDUCTION, AND FUNCTION. RC TISSUE=Thymus; RX PubMed=10646863; RA Hopfner R., Mousli M., Jeltsch J.-M., Voulgaris A., Lutz Y., Marin C., RA Bellocq J.-P., Oudet P., Bronner C.; RT "ICBP90, a novel human CCAAT binding protein, involved in the regulation of RT topoisomerase IIa expression."; RL Cancer Res. 60:121-128(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=17067204; DOI=10.1667/rr0459.1; RA Muto M., Fujimori A., Nenoi M., Daino K., Matsuda Y., Kuroiwa A., Kubo E., RA Kanari Y., Utsuno M., Tsuji H., Ukai H., Mita K., Takahagi M., Tatsumi K.; RT "Isolation and characterization of a novel human radiosusceptibility gene, RT NP95."; RL Radiat. Res. 166:723-733(2006). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Davenport J.W., Fernandes E.R., Neale G.A.M., Goorha R.M.; RT "LMO2-induced T cell leukemias overexpress Np95, a gene containing RING and RT PHD zinc fingers and an ubiquitin-like domain."; RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Testis; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS LYS-379 RP AND THR-638. RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS HIS-240; LYS-379; THR-638; RP MET-642 AND PHE-713. RG NIEHS SNPs program; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [10] RP INDUCTION, AND TISSUE SPECIFICITY. RX PubMed=12838312; DOI=10.1038/sj.bjc.6601068; RA Mousli M., Hopfner R., Abbady A.-Q., Monte D., Jeanblanc M., Oudet P., RA Louis B., Bronner C.; RT "ICBP90 belongs to a new family of proteins with an expression that is RT deregulated in cancer cells."; RL Br. J. Cancer 89:120-127(2003). RN [11] RP PHOSPHORYLATION, PHOSPHORYLATION AT SER-298, AND MUTAGENESIS OF SER-298; RP SER-651 AND SER-666. RX PubMed=15178447; DOI=10.1016/j.bbrc.2004.05.028; RA Trotzier M.-A., Bronner C., Bathami K., Mathieu E., Abbady A.-Q., RA Jeanblanc M., Muller C.D., Rochette-Egly C., Mousli M.; RT "Phosphorylation of ICBP90 by protein kinase A enhances topoisomerase RT IIalpha expression."; RL Biochem. Biophys. Res. Commun. 319:590-595(2004). RN [12] RP INDUCTION, UBIQUITINATION, AND FUNCTION. RX PubMed=15009091; DOI=10.1111/j.1356-9597.2004.00710.x; RA Arima Y., Hirota T., Bronner C., Mousli M., Fujiwara T., Niwa S., RA Ishikawa H., Saya H.; RT "Down-regulation of nuclear protein ICBP90 by p53/p21Cip1/WAF1-dependent RT DNA-damage checkpoint signals contributes to cell cycle arrest at G1/S RT transition."; RL Genes Cells 9:131-142(2004). RN [13] RP FUNCTION, INDUCTION, TISSUE SPECIFICITY, DNA-BINDING, AND INTERACTION WITH RP HDAC1 AND BLTP3A. RX PubMed=15361834; DOI=10.1038/sj.onc.1208053; RA Unoki M., Nishidate T., Nakamura Y.; RT "ICBP90, an E2F-1 target, recruits HDAC1 and binds to methyl-CpG through RT its SRA domain."; RL Oncogene 23:7601-7610(2004). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-287 AND SER-639, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-639, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [16] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH DNMT1. RX PubMed=17673620; DOI=10.1126/science.1147939; RA Bostick M., Kim J.K., Esteve P.O., Clark A., Pradhan S., Jacobsen S.E.; RT "UHRF1 plays a role in maintaining DNA methylation in mammalian cells."; RL Science 317:1760-1764(2007). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-287, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [18] RP FUNCTION, SUBCELLULAR LOCATION, AND AUTOUBIQUITINATION. RX PubMed=17967883; DOI=10.1128/mcb.01598-07; RA Karagianni P., Amazit L., Qin J., Wong J.; RT "ICBP90, a novel methyl K9 H3 binding protein linking protein RT ubiquitination with heterochromatin formation."; RL Mol. Cell. Biol. 28:705-717(2008). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76; SER-91 AND SER-707, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [20] RP INVOLVEMENT IN CANCER. RX PubMed=19491893; DOI=10.1038/sj.bjc.6605123; RA Unoki M., Kelly J.D., Neal D.E., Ponder B.A., Nakamura Y., Hamamoto R.; RT "UHRF1 is a novel molecular marker for diagnosis and the prognosis of RT bladder cancer."; RL Br. J. Cancer 101:98-105(2009). RN [21] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH EHMT2. RX PubMed=19056828; DOI=10.1093/nar/gkn961; RA Kim J.K., Esteve P.O., Jacobsen S.E., Pradhan S.; RT "UHRF1 binds G9a and participates in p21 transcriptional regulation in RT mammalian cells."; RL Nucleic Acids Res. 37:493-505(2009). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-287, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [23] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-399 AND LYS-546, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [24] RP MUTAGENESIS OF TYR-188 AND TYR-191. RX PubMed=20026581; DOI=10.1093/nar/gkp1152; RA Rottach A., Frauer C., Pichler G., Bonapace I.M., Spada F., Leonhardt H.; RT "The multi-domain protein Np95 connects DNA methylation and histone RT modification."; RL Nucleic Acids Res. 38:1796-1804(2010). RN [25] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76; SER-287; SER-639 AND RP SER-707, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [26] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [27] RP FUNCTION, AUTOUBIQUITINATION, DEUBIQUITINATION BY USP7, AND INTERACTION RP WITH USP7 AND DNMT1. RX PubMed=21745816; DOI=10.1093/nar/gkr528; RA Felle M., Joppien S., Nemeth A., Diermeier S., Thalhammer V., Dobner T., RA Kremmer E., Kappler R., Langst G.; RT "The USP7/Dnmt1 complex stimulates the DNA methylation activity of Dnmt1 RT and regulates the stability of UHRF1."; RL Nucleic Acids Res. 39:8355-8365(2011). RN [28] RP HYDROXYMETHYLCYTOSINE-BINDING. RX PubMed=21731699; DOI=10.1371/journal.pone.0021306; RA Frauer C., Hoffmann T., Bultmann S., Casa V., Cardoso M.C., Antes I., RA Leonhardt H.; RT "Recognition of 5-hydroxymethylcytosine by the Uhrf1 SRA domain."; RL PLoS ONE 6:E21306-E21306(2011). RN [29] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-287 AND SER-651, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [30] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76; SER-91; SER-287; SER-368; RP SER-639; SER-707 AND SER-709, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [31] RP FUNCTION, INTERACTION WITH PML, AND MUTAGENESIS OF HIS-741. RX PubMed=22945642; DOI=10.1038/onc.2012.406; RA Guan D., Factor D., Liu Y., Wang Z., Kao H.Y.; RT "The epigenetic regulator UHRF1 promotes ubiquitination-mediated RT degradation of the tumor-suppressor protein promyelocytic leukemia RT protein."; RL Oncogene 32:3819-3828(2013). RN [32] RP INVOLVEMENT IN CANCER. RX PubMed=22286757; DOI=10.1038/onc.2012.3; RA Sabatino L., Fucci A., Pancione M., Carafa V., Nebbioso A., Pistore C., RA Babbio F., Votino C., Laudanna C., Ceccarelli M., Altucci L., RA Bonapace I.M., Colantuoni V.; RT "UHRF1 coordinates peroxisome proliferator activated receptor gamma (PPARG) RT epigenetic silencing and mediates colorectal cancer progression."; RL Oncogene 31:5061-5072(2012). RN [33] RP INVOLVEMENT IN CANCER. RX PubMed=22330138; DOI=10.1038/onc.2011.641; RA Babbio F., Pistore C., Curti L., Castiglioni I., Kunderfranco P., Brino L., RA Oudet P., Seiler R., Thalman G.N., Roggero E., Sarti M., Pinton S., RA Mello-Grand M., Chiorino G., Catapano C.V., Carbone G.M., Bonapace I.M.; RT "The SRA protein UHRF1 promotes epigenetic crosstalks and is involved in RT prostate cancer progression."; RL Oncogene 31:4878-4887(2012). RN [34] RP AUTOUBIQUITINATION, DEUBIQUITINATION BY USP7, INTERACTION WITH USP7, RP PHOSPHORYLATION AT SER-639, AND MUTAGENESIS OF SER-639. RX PubMed=22411829; DOI=10.1073/pnas.1116349109; RA Ma H., Chen H., Guo X., Wang Z., Sowa M.E., Zheng L., Hu S., Zeng P., RA Guo R., Diao J., Lan F., Harper J.W., Shi Y.G., Xu Y., Shi Y.; RT "M phase phosphorylation of the epigenetic regulator UHRF1 regulates its RT physical association with the deubiquitylase USP7 and stability."; RL Proc. Natl. Acad. Sci. U.S.A. 109:4828-4833(2012). RN [35] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-385; LYS-546 AND LYS-670, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25218447; DOI=10.1038/nsmb.2890; RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., RA Vertegaal A.C.; RT "Uncovering global SUMOylation signaling networks in a site-specific RT manner."; RL Nat. Struct. Mol. Biol. 21:927-936(2014). RN [36] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-279 AND LYS-670, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [37] RP FUNCTION, INTERACTION WITH UHRF2 AND FANCD2, AND SUBCELLULAR LOCATION. RX PubMed=30335751; DOI=10.1371/journal.pgen.1007643; RA Motnenko A., Liang C.C., Yang D., Lopez-Martinez D., Yoshikawa Y., Zhan B., RA Ward K.E., Tian J., Haas W., Spingardi P., Kessler B.M., Kriaucionis S., RA Gygi S.P., Cohn M.A.; RT "Identification of UHRF2 as a novel DNA interstrand crosslink sensor RT protein."; RL PLoS Genet. 14:e1007643-e1007643(2018). RN [38] RP INTERACTION WITH ZNF263. RX PubMed=32051553; DOI=10.1038/s41388-020-1206-7; RA Yu Z., Feng J., Wang W., Deng Z., Zhang Y., Xiao L., Wang Z., Liu C., RA Liu Q., Chen S., Wu M.; RT "The EGFR-ZNF263 signaling axis silences SIX3 in glioblastoma RT epigenetically."; RL Oncogene 39:3163-3178(2020). RN [39] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=37728657; DOI=10.1083/jcb.202210093; RA Qi X., Liu Y., Peng Y., Fu Y., Fu Y., Yin L., Li X.; RT "UHRF1 promotes spindle assembly and chromosome congression by catalyzing RT EG5 polyubiquitination."; RL J. Cell Biol. 222:0-0(2023). RN [40] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-76. RG Structural genomics consortium (SGC); RT "Ubiquitin-like domain of human nuclear zinc finger protein NP95."; RL Submitted (JAN-2006) to the PDB data bank. RN [41] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 408-643. RX PubMed=18931436; DOI=10.1107/s1744309108027462; RA Delagoutte B., Lallous N., Birck C., Oudet P., Samama J.P.; RT "Expression, purification, crystallization and preliminary crystallographic RT study of the SRA domain of the human UHRF1 protein."; RL Acta Crystallogr. F 64:922-925(2008). RN [42] RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 414-617, AND MUTAGENESIS OF RP ARG-433; ARG-443; TYR-466 AND ARG-491. RX PubMed=18945682; DOI=10.1074/jbc.c800169200; RA Qian C., Li S., Jakoncic J., Zeng L., Walsh M.J., Zhou M.M.; RT "Structure and hemimethylated CpG binding of the SRA domain from human RT UHRF1."; RL J. Biol. Chem. 283:34490-34494(2008). RN [43] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 414-617 IN COMPLEX WITH RP HEMIMETHYLATED DNA, AND MUTAGENESIS OF GLY-448; ASP-469; ASN-489 AND RP ARG-491. RX PubMed=18772889; DOI=10.1038/nature07273; RA Avvakumov G.V., Walker J.R., Xue S., Li Y., Duan S., Bronner C., RA Arrowsmith C.H., Dhe-Paganon S.; RT "Structural basis for recognition of hemi-methylated DNA by the SRA domain RT of human UHRF1."; RL Nature 455:822-825(2008). RN [44] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 298-366, AND MUTAGENESIS OF RP ASP-334 AND ASP-337. RX PubMed=21808300; DOI=10.1038/cr.2011.124; RA Hu L., Li Z., Wang P., Lin Y., Xu Y.; RT "Crystal structure of PHD domain of UHRF1 and insights into recognition of RT unmodified histone H3 arginine residue 2."; RL Cell Res. 21:1374-1378(2011). RN [45] RP STRUCTURE BY NMR OF 298-366, AND MUTAGENESIS OF ASP-334 AND ASP-337. RX PubMed=21808299; DOI=10.1038/cr.2011.123; RA Wang C., Shen J., Yang Z., Chen P., Zhao B., Hu W., Lan W., Tong X., Wu H., RA Li G., Cao C.; RT "Structural basis for site-specific reading of unmodified R2 of histone H3 RT tail by UHRF1 PHD finger."; RL Cell Res. 21:1379-1382(2011). RN [46] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 126-285, STRUCTURE BY NMR OF RP 126-285, AND MUTAGENESIS OF ASP-142; ASP-145; PHE-152; GLU-153; TYR-188 AND RP ASP-190. RX PubMed=21489993; DOI=10.1074/jbc.m111.234104; RA Nady N., Lemak A., Walker J.R., Avvakumov G.V., Kareta M.S., Achour M., RA Xue S., Duan S., Allali-Hassani A., Zuo X., Wang Y.X., Bronner C., RA Chedin F., Arrowsmith C.H., Dhe-Paganon S.; RT "Recognition of multivalent histone states associated with heterochromatin RT by UHRF1 protein."; RL J. Biol. Chem. 286:24300-24311(2011). RN [47] RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 298-367 IN COMPLEX WITH ZINC AND RP HISTONE H3 PEPTIDE, FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF RP 334-ASP-GLU-335. RX PubMed=21777816; DOI=10.1016/j.molcel.2011.07.006; RA Rajakumara E., Wang Z., Ma H., Hu L., Chen H., Lin Y., Guo R., Wu F., RA Li H., Lan F., Shi Y.G., Xu Y., Patel D.J., Shi Y.; RT "PHD finger recognition of unmodified histone H3R2 links UHRF1 to RT regulation of euchromatic gene expression."; RL Mol. Cell 43:275-284(2011). RN [48] RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 314-367, AND MUTAGENESIS OF RP GLN-330; ASP-334 AND ASP-337. RX PubMed=22096602; DOI=10.1371/journal.pone.0027599; RA Lallous N., Legrand P., McEwen A.G., Ramon-Maiques S., Samama J.P., RA Birck C.; RT "The PHD finger of human UHRF1 reveals a new subgroup of unmethylated RT histone H3 tail readers."; RL PLoS ONE 6:E27599-E27599(2011). RN [49] RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 299-364 IN COMPLEX WITH HISTONE RP H3 PEPTIDE. RX PubMed=22100450; DOI=10.1016/j.jmb.2011.11.012; RA Xie S., Jakoncic J., Qian C.; RT "UHRF1 double tudor domain and the adjacent PHD finger act together to RT recognize K9me3-containing histone H3 tail."; RL J. Mol. Biol. 415:318-328(2012). RN [50] RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 134-367 IN COMPLEX WITH ZINC AND RP HISTONE H3 PEPTIDE, PHOSPHORYLATION AT SER-298, AND MUTAGENESIS OF RP 295-ARG-ARG-296. RX PubMed=22837395; DOI=10.1073/pnas.1203701109; RA Arita K., Isogai S., Oda T., Unoki M., Sugita K., Sekiyama N., Kuwata K., RA Hamamoto R., Tochio H., Sato M., Ariyoshi M., Shirakawa M.; RT "Recognition of modification status on a histone H3 tail by linked histone RT reader modules of the epigenetic regulator UHRF1."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12950-12955(2012). CC -!- FUNCTION: Multidomain protein that acts as a key epigenetic regulator CC by bridging DNA methylation and chromatin modification. Specifically CC recognizes and binds hemimethylated DNA at replication forks via its CC YDG domain and recruits DNMT1 methyltransferase to ensure faithful CC propagation of the DNA methylation patterns through DNA replication. In CC addition to its role in maintenance of DNA methylation, also plays a CC key role in chromatin modification: through its tudor-like regions and CC PHD-type zinc fingers, specifically recognizes and binds histone H3 CC trimethylated at 'Lys-9' (H3K9me3) and unmethylated at 'Arg-2' CC (H3R2me0), respectively, and recruits chromatin proteins. Enriched in CC pericentric heterochromatin where it recruits different chromatin CC modifiers required for this chromatin replication. Also localizes to CC euchromatic regions where it negatively regulates transcription CC possibly by impacting DNA methylation and histone modifications. Has E3 CC ubiquitin-protein ligase activity by mediating the ubiquitination of CC target proteins such as histone H3 and PML. It is still unclear how E3 CC ubiquitin-protein ligase activity is related to its role in chromatin CC in vivo. Plays a role in DNA repair by cooperating with UHRF2 to ensure CC recruitment of FANCD2 to interstrand cross-links (ICLs) leading to CC FANCD2 activation. Acts as a critical player of proper spindle CC architecture by catalyzing the 'Lys-63'-linked ubiquitination of KIF11, CC thereby controlling KIF11 localization on the spindle CC (PubMed:37728657). {ECO:0000269|PubMed:10646863, CC ECO:0000269|PubMed:15009091, ECO:0000269|PubMed:15361834, CC ECO:0000269|PubMed:17673620, ECO:0000269|PubMed:17967883, CC ECO:0000269|PubMed:19056828, ECO:0000269|PubMed:21745816, CC ECO:0000269|PubMed:21777816, ECO:0000269|PubMed:22945642, CC ECO:0000269|PubMed:30335751, ECO:0000269|PubMed:37728657}. CC -!- CATALYTIC ACTIVITY: CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L- CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; CC EC=2.3.2.27; Evidence={ECO:0000269|PubMed:37728657}; CC -!- PATHWAY: Protein modification; protein ubiquitination. CC -!- SUBUNIT: Interacts with DNMT3A and DNMT3B (By similarity). Interacts CC with DNMT1; the interaction is direct. Interacts with USP7; leading to CC its deubiquitination. Interacts with histone H3. Interacts with HDAC1, CC but not with HDAC2. Interacts with BLTP3A. Interacts with PML. CC Interacts with EHMT2. Binds hemimethylated CpG containing CC oligonucleotides. Interacts with ZNF263; recruited to the SIX3 promoter CC along with other proteins involved in chromatin modification and CC transcriptional corepression where it contributes to transcriptional CC repression (PubMed:32051553). Interacts with UHRF2 (PubMed:30335751). CC Interacts with FANCD2 (PubMed:30335751). Interacts with TET1 isoform 2; CC this interaction induces the recruitment of TET1 isoform 2 to CC replicating heterochromatin (By similarity). {ECO:0000250, CC ECO:0000250|UniProtKB:Q8VDF2, ECO:0000269|PubMed:15361834, CC ECO:0000269|PubMed:17673620, ECO:0000269|PubMed:18772889, CC ECO:0000269|PubMed:19056828, ECO:0000269|PubMed:21745816, CC ECO:0000269|PubMed:21777816, ECO:0000269|PubMed:22100450, CC ECO:0000269|PubMed:22411829, ECO:0000269|PubMed:22837395, CC ECO:0000269|PubMed:22945642, ECO:0000269|PubMed:30335751, CC ECO:0000269|PubMed:32051553}. CC -!- INTERACTION: CC Q96T88; P26358: DNMT1; NbExp=12; IntAct=EBI-1548946, EBI-719459; CC Q96T88; Q9Y6K1: DNMT3A; NbExp=7; IntAct=EBI-1548946, EBI-923653; CC Q96T88; Q9UBC3: DNMT3B; NbExp=7; IntAct=EBI-1548946, EBI-80125; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00358, CC ECO:0000269|PubMed:10646863, ECO:0000269|PubMed:17673620, CC ECO:0000269|PubMed:17967883, ECO:0000269|PubMed:19056828, CC ECO:0000269|PubMed:21777816, ECO:0000269|PubMed:30335751}. CC Note=Associated, through the YDG domain (also called SRA domain), with CC replicating DNA from early to late S phase, including at replicating CC pericentric heterochromatin (By similarity). Also localizes to CC euchromatic regions. In non-S-phase cells, homogenously distributed CC through the nucleus (By similarity). {ECO:0000250|UniProtKB:Q8VDF2}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q96T88-1; Sequence=Displayed; CC Name=2; CC IsoId=Q96T88-2; Sequence=VSP_044394; CC -!- TISSUE SPECIFICITY: Expressed in thymus, bone marrow, testis, lung and CC heart. Overexpressed in breast cancer. {ECO:0000269|PubMed:10646863, CC ECO:0000269|PubMed:12838312, ECO:0000269|PubMed:15361834}. CC -!- DEVELOPMENTAL STAGE: Expressed in fetal thymus, liver and kidney. CC {ECO:0000269|PubMed:10646863}. CC -!- INDUCTION: Up-regulated in proliferating cells, and down-regulated in CC quiescent cells. Down-regulated upon adriamycin-induced DNA damage, in CC a p53/TP53 and CDKN1A-dependent way. Induced by E2F1 transcription CC factor. {ECO:0000269|PubMed:10646863, ECO:0000269|PubMed:12838312, CC ECO:0000269|PubMed:15009091, ECO:0000269|PubMed:15361834}. CC -!- DOMAIN: The tudor-like regions specifically recognize and bind histone CC H3 unmethylated at 'Arg-2' (H3R2me0), while the PHD-type zinc finger CC specifically recognizes and binds histone H3 trimethylated at 'Lys-9' CC (H3K9me3). The tudor-like regions simultaneously recognizes H3K9me3 CC through a conserved aromatic cage in the first tudor-like subdomain and CC unmodified H3K4 (H3K4me0) within a groove between the tandem subdomains CC (PubMed:21489993, PubMed:21777816, PubMed:22100450). The linker region CC plays a role in the formation of a histone H3-binding hole between the CC reader modules formed by the tudor-like regions and the PHD-type zinc CC finger by making extended contacts with the tandem tudor-like regions CC (PubMed:22837395). {ECO:0000269|PubMed:22837395}. CC -!- DOMAIN: The YDG domain (also named SRA domain) specifically recognizes CC and binds hemimethylated DNA at replication forks (DNA that is only CC methylated on the mother strand of replicating DNA) (PubMed:17673620). CC It contains a binding pocket that accommodates the 5-methylcytosine CC that is flipped out of the duplex DNA. 2 specialized loops reach CC through the resulting gap in the DNA from both the major and the minor CC grooves to read the other 3 bases of the CpG duplex. The major groove CC loop confers both specificity for the CpG dinucleotide and CC discrimination against methylation of deoxycytidine of the CC complementary strand (PubMed:18772889). The YDG domain also recognizes CC and binds 5-hydroxymethylcytosine (5hmC) (PubMed:21731699). CC {ECO:0000269|PubMed:17673620, ECO:0000269|PubMed:18772889, CC ECO:0000269|PubMed:21731699}. CC -!- DOMAIN: The RING finger is required for ubiquitin ligase activity. CC {ECO:0000250}. CC -!- PTM: Phosphorylation at Ser-298 of the linker region decreases the CC binding to H3K9me3. Phosphorylation at Ser-639 by CDK1 during M phase CC impairs interaction with USP7, preventing deubiquitination and leading CC to degradation by the proteasome. {ECO:0000269|PubMed:15178447, CC ECO:0000269|PubMed:22411829, ECO:0000269|PubMed:22837395}. CC -!- PTM: Ubiquitinated; which leads to proteasomal degradation. CC Autoubiquitinated; interaction with USP7 leads to deubiquitination and CC prevents degradation. Ubiquitination and degradation takes place during CC M phase, when phosphorylation at Ser-639 prevents interaction with USP7 CC and subsequent deubiquitination. Polyubiquitination may be stimulated CC by DNA damage. {ECO:0000269|PubMed:15009091, CC ECO:0000269|PubMed:17967883, ECO:0000269|PubMed:21745816, CC ECO:0000269|PubMed:22411829}. CC -!- DISEASE: Note=Defects in UHRF1 may be a cause of cancers. Overexpressed CC in many different forms of human cancers, including bladder, breast, CC cervical, colorectal and prostate cancers, as well as pancreatic CC adenocarcinomas, rhabdomyosarcomas and gliomas. Plays an important role CC in the correlation of histone modification and gene silencing in cancer CC progression. Expression is associated with a poor prognosis in patients CC with various cancers, suggesting that it participates in cancer CC progression. CC -!- SEQUENCE CAUTION: CC Sequence=BAB15177.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/uhrf1/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF129507; AAF28469.1; -; mRNA. DR EMBL; AB177623; BAF36719.1; -; mRNA. DR EMBL; AB177624; BAF36720.1; -; mRNA. DR EMBL; AB075601; BAC20576.1; -; mRNA. DR EMBL; AF274048; AAK55744.1; -; mRNA. DR EMBL; EF560733; ABQ59043.1; -; mRNA. DR EMBL; AK025578; BAB15177.1; ALT_INIT; mRNA. DR EMBL; AK289389; BAF82078.1; -; mRNA. DR EMBL; AK314579; BAG37156.1; -; mRNA. DR EMBL; AY787925; AAV40831.1; -; Genomic_DNA. DR EMBL; AC027319; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC053467; AAF64067.1; -; Genomic_DNA. DR EMBL; CH471139; EAW69187.1; -; Genomic_DNA. DR EMBL; BC113875; AAI13876.2; -; mRNA. DR CCDS; CCDS74262.1; -. [Q96T88-2] DR CCDS; CCDS74263.1; -. [Q96T88-1] DR RefSeq; NP_001041666.1; NM_001048201.2. [Q96T88-1] DR RefSeq; NP_001276979.1; NM_001290050.1. [Q96T88-1] DR RefSeq; NP_001276980.1; NM_001290051.1. [Q96T88-1] DR RefSeq; NP_001276981.1; NM_001290052.1. [Q96T88-1] DR RefSeq; NP_037414.3; NM_013282.4. DR PDB; 2FAZ; X-ray; 2.00 A; A/B=1-76. DR PDB; 2L3R; NMR; -; A=126-285. DR PDB; 2LGG; NMR; -; A=298-366. DR PDB; 2LGK; NMR; -; A=298-366. DR PDB; 2LGL; NMR; -; A=298-366. DR PDB; 2PB7; X-ray; 1.90 A; A=408-643. DR PDB; 3ASK; X-ray; 2.90 A; A/B/C/D=134-367. DR PDB; 3ASL; X-ray; 1.41 A; A=298-367. DR PDB; 3BI7; X-ray; 1.70 A; A=414-617. DR PDB; 3CLZ; X-ray; 2.20 A; A/B/C/D=414-617. DR PDB; 3DB3; X-ray; 2.40 A; A=126-285. DR PDB; 3DB4; X-ray; 2.40 A; A=126-285. DR PDB; 3DWH; X-ray; 1.95 A; A=414-617. DR PDB; 3FL2; X-ray; 1.75 A; A=672-793. DR PDB; 3SHB; X-ray; 1.80 A; A=298-366. DR PDB; 3SOU; X-ray; 1.80 A; A/B=298-367. DR PDB; 3SOW; X-ray; 1.95 A; A/B=298-367. DR PDB; 3SOX; X-ray; 2.65 A; A/B=298-367. DR PDB; 3T6R; X-ray; 1.95 A; A/B=299-364. DR PDB; 3ZVY; X-ray; 1.95 A; A/B=296-367. DR PDB; 3ZVZ; X-ray; 1.45 A; B=314-367. DR PDB; 4GY5; X-ray; 2.96 A; A/B/C/D=134-366. DR PDB; 4QQD; X-ray; 2.28 A; A/B=126-285. DR PDB; 5C6D; X-ray; 2.29 A; C/D=634-665. DR PDB; 5IAY; NMR; -; A=134-285, B=642-657. DR PDB; 5XPI; X-ray; 2.20 A; A=127-283. DR PDB; 5YY9; X-ray; 2.65 A; A/B=123-285. DR PDB; 5YYA; X-ray; 1.70 A; A=123-285. DR PDB; 6B9M; X-ray; 1.68 A; D=638-678. DR PDB; 6IIW; X-ray; 1.70 A; A=299-366. DR PDB; 6VCS; X-ray; 1.70 A; A/B/E=414-617. DR PDB; 6VED; NMR; -; A=133-300. DR PDB; 6VYJ; X-ray; 1.39 A; A=122-283. DR PDB; 6W92; X-ray; 1.30 A; A=122-283. DR PDB; 7FB7; X-ray; 1.45 A; A/B=123-285. DR PDBsum; 2FAZ; -. DR PDBsum; 2L3R; -. DR PDBsum; 2LGG; -. DR PDBsum; 2LGK; -. DR PDBsum; 2LGL; -. DR PDBsum; 2PB7; -. DR PDBsum; 3ASK; -. DR PDBsum; 3ASL; -. DR PDBsum; 3BI7; -. DR PDBsum; 3CLZ; -. DR PDBsum; 3DB3; -. DR PDBsum; 3DB4; -. DR PDBsum; 3DWH; -. DR PDBsum; 3FL2; -. DR PDBsum; 3SHB; -. DR PDBsum; 3SOU; -. DR PDBsum; 3SOW; -. DR PDBsum; 3SOX; -. DR PDBsum; 3T6R; -. DR PDBsum; 3ZVY; -. DR PDBsum; 3ZVZ; -. DR PDBsum; 4GY5; -. DR PDBsum; 4QQD; -. DR PDBsum; 5C6D; -. DR PDBsum; 5IAY; -. DR PDBsum; 5XPI; -. DR PDBsum; 5YY9; -. DR PDBsum; 5YYA; -. DR PDBsum; 6B9M; -. DR PDBsum; 6IIW; -. DR PDBsum; 6VCS; -. DR PDBsum; 6VED; -. DR PDBsum; 6VYJ; -. DR PDBsum; 6W92; -. DR PDBsum; 7FB7; -. DR AlphaFoldDB; Q96T88; -. DR BMRB; Q96T88; -. DR SASBDB; Q96T88; -. DR SMR; Q96T88; -. DR BioGRID; 118893; 219. DR IntAct; Q96T88; 38. DR MINT; Q96T88; -. DR STRING; 9606.ENSP00000479617; -. DR BindingDB; Q96T88; -. DR ChEMBL; CHEMBL2424510; -. DR GlyGen; Q96T88; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q96T88; -. DR PhosphoSitePlus; Q96T88; -. DR SwissPalm; Q96T88; -. DR BioMuta; UHRF1; -. DR DMDM; 67462077; -. DR EPD; Q96T88; -. DR jPOST; Q96T88; -. DR MassIVE; Q96T88; -. DR MaxQB; Q96T88; -. DR PaxDb; 9606-ENSP00000479617; -. DR PeptideAtlas; Q96T88; -. DR ProteomicsDB; 78215; -. [Q96T88-1] DR Pumba; Q96T88; -. DR Antibodypedia; 72541; 480 antibodies from 34 providers. DR DNASU; 29128; -. DR Ensembl; ENST00000612630.4; ENSP00000484739.1; ENSG00000276043.5. [Q96T88-1] DR Ensembl; ENST00000615884.4; ENSP00000478601.1; ENSG00000276043.5. [Q96T88-1] DR Ensembl; ENST00000616255.1; ENSP00000478348.1; ENSG00000276043.5. [Q96T88-1] DR Ensembl; ENST00000624301.3; ENSP00000485604.1; ENSG00000276043.5. [Q96T88-1] DR Ensembl; ENST00000650932.1; ENSP00000498698.1; ENSG00000276043.5. [Q96T88-1] DR GeneID; 29128; -. DR KEGG; hsa:29128; -. DR MANE-Select; ENST00000650932.1; ENSP00000498698.1; NM_001048201.3; NP_001041666.1. DR UCSC; uc032hkj.2; human. [Q96T88-1] DR AGR; HGNC:12556; -. DR DisGeNET; 29128; -. DR GeneCards; UHRF1; -. DR HGNC; HGNC:12556; UHRF1. DR HPA; ENSG00000276043; Group enriched (bone marrow, lymphoid tissue). DR MIM; 607990; gene. DR neXtProt; NX_Q96T88; -. DR OpenTargets; ENSG00000276043; -. DR PharmGKB; PA37196; -. DR VEuPathDB; HostDB:ENSG00000276043; -. DR eggNOG; ENOG502QRDQ; Eukaryota. DR GeneTree; ENSGT00390000008296; -. DR HOGENOM; CLU_022357_0_0_1; -. DR InParanoid; Q96T88; -. DR OrthoDB; 5481936at2759; -. DR PhylomeDB; Q96T88; -. DR PathwayCommons; Q96T88; -. DR Reactome; R-HSA-5334118; DNA methylation. DR Reactome; R-HSA-9821002; Chromatin modifications during the maternal to zygotic transition (MZT). DR SignaLink; Q96T88; -. DR SIGNOR; Q96T88; -. DR UniPathway; UPA00143; -. DR BioGRID-ORCS; 29128; 65 hits in 331 CRISPR screens. DR ChiTaRS; UHRF1; human. DR EvolutionaryTrace; Q96T88; -. DR GeneWiki; UHRF1; -. DR GenomeRNAi; 29128; -. DR Pharos; Q96T88; Tbio. DR PRO; PR:Q96T88; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; Q96T88; Protein. DR Bgee; ENSG00000276043; Expressed in oocyte and 139 other cell types or tissues. DR ExpressionAtlas; Q96T88; baseline and differential. DR GO; GO:0000785; C:chromatin; IDA:UniProtKB. DR GO; GO:0000791; C:euchromatin; IDA:UniProtKB. DR GO; GO:0000792; C:heterochromatin; IDA:UniProtKB. DR GO; GO:0016363; C:nuclear matrix; ISS:BHF-UCL. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL. DR GO; GO:0005657; C:replication fork; IDA:UniProtKB. DR GO; GO:0005819; C:spindle; IC:UniProt. DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:BHF-UCL. DR GO; GO:0140612; F:DNA damage sensor activity; TAS:BHF-UCL. DR GO; GO:0062072; F:H3K9me3 modified histone binding; TAS:BHF-UCL. DR GO; GO:0044729; F:hemi-methylated DNA-binding; IDA:UniProtKB. DR GO; GO:0042393; F:histone binding; IDA:UniProtKB. DR GO; GO:0141055; F:histone H3 ubiquitin ligase activity; ISS:BHF-UCL. DR GO; GO:0042802; F:identical protein binding; ISS:BHF-UCL. DR GO; GO:0008327; F:methyl-CpG binding; IDA:UniProtKB. DR GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB. DR GO; GO:0003676; F:nucleic acid binding; EXP:DisProt. DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProt. DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB. DR GO; GO:0006974; P:DNA damage response; TAS:BHF-UCL. DR GO; GO:0000724; P:double-strand break repair via homologous recombination; TAS:BHF-UCL. DR GO; GO:0040029; P:epigenetic regulation of gene expression; TAS:BHF-UCL. DR GO; GO:0031507; P:heterochromatin formation; IDA:UniProtKB. DR GO; GO:0035825; P:homologous recombination; TAS:BHF-UCL. DR GO; GO:0090307; P:mitotic spindle assembly; IDA:UniProt. DR GO; GO:0044027; P:negative regulation of gene expression via CpG island methylation; IMP:UniProtKB. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:2000373; P:positive regulation of DNA topoisomerase (ATP-hydrolyzing) activity; IC:BHF-UCL. DR GO; GO:0051247; P:positive regulation of protein metabolic process; IDA:BHF-UCL. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IC:BHF-UCL. DR GO; GO:0051865; P:protein autoubiquitination; IDA:UniProtKB. DR GO; GO:0050678; P:regulation of epithelial cell proliferation; IMP:BHF-UCL. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:UniProtKB. DR CDD; cd15616; PHD_UHRF1; 1. DR CDD; cd16769; RING-HC_UHRF1; 1. DR CDD; cd20455; Tudor_UHRF1_rpt1; 1. DR CDD; cd20457; Tudor_UHRF1_rpt2; 1. DR CDD; cd17122; Ubl_UHRF1; 1. DR DisProt; DP01651; -. DR Gene3D; 2.30.30.1150; -; 1. DR Gene3D; 2.30.30.140; -; 1. DR Gene3D; 2.30.280.10; SRA-YDG; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR IDEAL; IID00327; -. DR InterPro; IPR015947; PUA-like_sf. DR InterPro; IPR036987; SRA-YDG_sf. DR InterPro; IPR003105; SRA_YDG. DR InterPro; IPR021991; TTD_dom. DR InterPro; IPR000626; Ubiquitin-like_dom. DR InterPro; IPR029071; Ubiquitin-like_domsf. DR InterPro; IPR047406; Ubl_UHRF1. DR InterPro; IPR045134; UHRF1/2-like. DR InterPro; IPR011011; Znf_FYVE_PHD. DR InterPro; IPR001965; Znf_PHD. DR InterPro; IPR019787; Znf_PHD-finger. DR InterPro; IPR001841; Znf_RING. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR InterPro; IPR017907; Znf_RING_CS. DR PANTHER; PTHR14140; E3 UBIQUITIN-PROTEIN LIGASE UHRF-RELATED; 1. DR PANTHER; PTHR14140:SF2; E3 UBIQUITIN-PROTEIN LIGASE UHRF1; 1. DR Pfam; PF00628; PHD; 1. DR Pfam; PF02182; SAD_SRA; 1. DR Pfam; PF12148; TTD; 1. DR Pfam; PF00240; ubiquitin; 1. DR SMART; SM00249; PHD; 1. DR SMART; SM00184; RING; 2. DR SMART; SM00466; SRA; 1. DR SMART; SM00213; UBQ; 1. DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1. DR SUPFAM; SSF88697; PUA domain-like; 1. DR SUPFAM; SSF57850; RING/U-box; 1. DR SUPFAM; SSF54236; Ubiquitin-like; 1. DR PROSITE; PS50053; UBIQUITIN_2; 1. DR PROSITE; PS51015; YDG; 1. DR PROSITE; PS01359; ZF_PHD_1; 1. DR PROSITE; PS50016; ZF_PHD_2; 1. DR PROSITE; PS00518; ZF_RING_1; 1. DR PROSITE; PS50089; ZF_RING_2; 2. DR Genevisible; Q96T88; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cell cycle; KW Chromatin regulator; DNA damage; DNA repair; DNA-binding; Isopeptide bond; KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat; KW Repressor; Transcription; Transcription regulation; Transferase; KW Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger. FT CHAIN 1..793 FT /note="E3 ubiquitin-protein ligase UHRF1" FT /id="PRO_0000056144" FT DOMAIN 1..78 FT /note="Ubiquitin-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214" FT DOMAIN 419..582 FT /note="YDG" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00358" FT ZN_FING 310..366 FT /note="PHD-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146" FT ZN_FING 724..763 FT /note="RING-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175" FT REGION 82..124 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 133..209 FT /note="Tudor-like 1" FT REGION 216..283 FT /note="Tudor-like 2" FT REGION 296..301 FT /note="Linker" FT REGION 333..337 FT /note="Histone H3R2me0 binding" FT REGION 353..355 FT /note="Histone H3R2me0 binding" FT REGION 445..446 FT /note="Required to promote base flipping" FT /evidence="ECO:0000250" FT REGION 466..469 FT /note="Required for formation of a 5-methylcytosine-binding FT pocket" FT REGION 478..481 FT /note="Required for formation of a 5-methylcytosine-binding FT pocket" FT REGION 618..673 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 94..108 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 109..124 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 618..635 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 463..464 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /ligand_part="5-methylcytosine group" FT /ligand_part_id="ChEBI:CHEBI:65274" FT BINDING 469 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /ligand_part="5-methylcytosine group" FT /ligand_part_id="ChEBI:CHEBI:65274" FT SITE 316 FT /note="Histone H3K4me0 binding" FT SITE 327 FT /note="Histone H3R2me0 binding" FT SITE 330 FT /note="Histone H3R2me0 binding" FT SITE 479 FT /note="Required to confer preferential recognition of FT cytosine over thymine" FT SITE 489 FT /note="Required to discriminate between hemimethylated DNA FT versus symmetrically methylated DNA" FT SITE 491 FT /note="Required for affinity and specificity for 5-mCpG FT sequence" FT MOD_RES 76 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 91 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 95 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q7TPK1" FT MOD_RES 165 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8VDF2" FT MOD_RES 287 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 298 FT /note="Phosphoserine; by PKA" FT /evidence="ECO:0000269|PubMed:15178447, FT ECO:0000269|PubMed:22837395" FT MOD_RES 368 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 399 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 546 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 639 FT /note="Phosphoserine; by CDK1" FT /evidence="ECO:0000269|PubMed:22411829, FT ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 651 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 707 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 709 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT CROSSLNK 279 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 385 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447" FT CROSSLNK 546 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:25218447" FT CROSSLNK 670 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:28112733" FT VAR_SEQ 1 FT /note="M -> MGVFAVPPLSSDTM (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_044394" FT VARIANT 240 FT /note="D -> H (in dbSNP:rs17886098)" FT /evidence="ECO:0000269|Ref.6" FT /id="VAR_022554" FT VARIANT 379 FT /note="E -> K (in dbSNP:rs17885791)" FT /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.6" FT /id="VAR_022555" FT VARIANT 638 FT /note="A -> T (in dbSNP:rs2307209)" FT /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.6" FT /id="VAR_022556" FT VARIANT 642 FT /note="T -> M (in dbSNP:rs17884843)" FT /evidence="ECO:0000269|Ref.6" FT /id="VAR_022557" FT VARIANT 713 FT /note="L -> F (in dbSNP:rs17883563)" FT /evidence="ECO:0000269|Ref.6" FT /id="VAR_022558" FT MUTAGEN 142 FT /note="D->A: Impaired binding to histone H3 without FT affecting the protein folding; when associated with A-153." FT /evidence="ECO:0000269|PubMed:21489993" FT MUTAGEN 145 FT /note="D->A: Impaired binding to histone H3." FT /evidence="ECO:0000269|PubMed:21489993" FT MUTAGEN 152 FT /note="F->A: Impaired binding to histone H3." FT /evidence="ECO:0000269|PubMed:21489993" FT MUTAGEN 153 FT /note="E->A: Impaired binding to histone H3 without FT affecting the protein folding; when associated with A-142." FT /evidence="ECO:0000269|PubMed:21489993" FT MUTAGEN 188 FT /note="Y->A: Impaired binding to histone H3." FT /evidence="ECO:0000269|PubMed:20026581, FT ECO:0000269|PubMed:21489993" FT MUTAGEN 190 FT /note="D->A: Slightly impaired binding to histone H3." FT /evidence="ECO:0000269|PubMed:21489993" FT MUTAGEN 191 FT /note="Y->A: Impaired binding to histone H3." FT /evidence="ECO:0000269|PubMed:20026581" FT MUTAGEN 295..296 FT /note="RR->AA: Disrupts the simultaneous binding to H3R2me0 FT and H3K9me3." FT /evidence="ECO:0000269|PubMed:22837395" FT MUTAGEN 298 FT /note="S->A: Diminishes phosphorylation by PKA." FT /evidence="ECO:0000269|PubMed:15178447" FT MUTAGEN 330 FT /note="Q->A,K: Does not affect ability to bind histone H3 FT peptide." FT /evidence="ECO:0000269|PubMed:22096602" FT MUTAGEN 334..335 FT /note="DE->AA: Abolishes binding to histone H3." FT /evidence="ECO:0000269|PubMed:21777816" FT MUTAGEN 334 FT /note="D->A: Impaired binding to histone H3." FT /evidence="ECO:0000269|PubMed:21808299, FT ECO:0000269|PubMed:21808300, ECO:0000269|PubMed:22096602" FT MUTAGEN 337 FT /note="D->A: Impaired binding to histone H3." FT /evidence="ECO:0000269|PubMed:21808299, FT ECO:0000269|PubMed:21808300, ECO:0000269|PubMed:22096602" FT MUTAGEN 433 FT /note="R->A: Does not affect ability to bind DNA." FT /evidence="ECO:0000269|PubMed:18945682" FT MUTAGEN 443 FT /note="R->A: Decreased ability to bind DNA." FT /evidence="ECO:0000269|PubMed:18945682" FT MUTAGEN 448 FT /note="G->D: Decreased affinity for DNA." FT /evidence="ECO:0000269|PubMed:18772889" FT MUTAGEN 466 FT /note="Y->G: Decreased ability to bind DNA." FT /evidence="ECO:0000269|PubMed:18945682" FT MUTAGEN 469 FT /note="D->G: Abolishes ability to bind hemimethylated DNA." FT /evidence="ECO:0000269|PubMed:18772889" FT MUTAGEN 489 FT /note="N->A: Abolishes specificity to hemimethylated DNA." FT /evidence="ECO:0000269|PubMed:18772889" FT MUTAGEN 491 FT /note="R->A: Decreased binding to methylated DNA but does FT not affect ability to bind DNA." FT /evidence="ECO:0000269|PubMed:18772889, FT ECO:0000269|PubMed:18945682" FT MUTAGEN 639 FT /note="S->A: Prevents phosphorylation by CDK1 during M FT phase, leading to increased stability." FT /evidence="ECO:0000269|PubMed:22411829" FT MUTAGEN 639 FT /note="S->D: Mimics phosphorylation; impaired interaction FT with USP7, leading to decreased stability." FT /evidence="ECO:0000269|PubMed:22411829" FT MUTAGEN 651 FT /note="S->A: No effect on in vitro phosphorylation by PKA." FT /evidence="ECO:0000269|PubMed:15178447" FT MUTAGEN 666 FT /note="S->A: No effect on in vitro phosphorylation by PKA." FT /evidence="ECO:0000269|PubMed:15178447" FT MUTAGEN 741 FT /note="H->A: Abolishes E3 ubiquitin-protein ligase FT activity." FT /evidence="ECO:0000269|PubMed:22945642" FT CONFLICT 383 FT /note="K -> E (in Ref. 5; BAF82078)" FT /evidence="ECO:0000305" FT CONFLICT 383 FT /note="K -> N (in Ref. 1; AAF28469)" FT /evidence="ECO:0000305" FT CONFLICT 457 FT /note="A -> S (in Ref. 1; AAF28469)" FT /evidence="ECO:0000305" FT CONFLICT 675 FT /note="S -> N (in Ref. 5; BAF82078)" FT /evidence="ECO:0000305" FT STRAND 1..7 FT /evidence="ECO:0007829|PDB:2FAZ" FT STRAND 13..19 FT /evidence="ECO:0007829|PDB:2FAZ" FT HELIX 25..36 FT /evidence="ECO:0007829|PDB:2FAZ" FT HELIX 40..42 FT /evidence="ECO:0007829|PDB:2FAZ" FT STRAND 43..47 FT /evidence="ECO:0007829|PDB:2FAZ" FT TURN 58..62 FT /evidence="ECO:0007829|PDB:2FAZ" FT STRAND 68..73 FT /evidence="ECO:0007829|PDB:2FAZ" FT STRAND 126..128 FT /evidence="ECO:0007829|PDB:6W92" FT STRAND 130..132 FT /evidence="ECO:0007829|PDB:6W92" FT STRAND 133..135 FT /evidence="ECO:0007829|PDB:7FB7" FT STRAND 140..144 FT /evidence="ECO:0007829|PDB:6W92" FT TURN 146..148 FT /evidence="ECO:0007829|PDB:6W92" FT STRAND 151..162 FT /evidence="ECO:0007829|PDB:6W92" FT STRAND 164..167 FT /evidence="ECO:0007829|PDB:2L3R" FT STRAND 173..175 FT /evidence="ECO:0007829|PDB:6W92" FT HELIX 179..181 FT /evidence="ECO:0007829|PDB:6W92" FT STRAND 183..190 FT /evidence="ECO:0007829|PDB:6W92" FT HELIX 192..194 FT /evidence="ECO:0007829|PDB:6W92" FT STRAND 196..200 FT /evidence="ECO:0007829|PDB:6W92" FT HELIX 201..203 FT /evidence="ECO:0007829|PDB:6W92" FT STRAND 204..206 FT /evidence="ECO:0007829|PDB:7FB7" FT STRAND 210..212 FT /evidence="ECO:0007829|PDB:2L3R" FT HELIX 214..216 FT /evidence="ECO:0007829|PDB:6W92" FT STRAND 222..227 FT /evidence="ECO:0007829|PDB:6W92" FT STRAND 229..231 FT /evidence="ECO:0007829|PDB:6W92" FT STRAND 237..248 FT /evidence="ECO:0007829|PDB:6W92" FT STRAND 253..260 FT /evidence="ECO:0007829|PDB:6W92" FT STRAND 266..270 FT /evidence="ECO:0007829|PDB:6W92" FT HELIX 274..276 FT /evidence="ECO:0007829|PDB:2L3R" FT STRAND 277..279 FT /evidence="ECO:0007829|PDB:2L3R" FT STRAND 283..286 FT /evidence="ECO:0007829|PDB:3ASK" FT TURN 303..307 FT /evidence="ECO:0007829|PDB:3ASL" FT STRAND 309..311 FT /evidence="ECO:0007829|PDB:2LGG" FT TURN 314..316 FT /evidence="ECO:0007829|PDB:3ASL" FT TURN 319..321 FT /evidence="ECO:0007829|PDB:3ASL" FT STRAND 323..325 FT /evidence="ECO:0007829|PDB:2LGL" FT HELIX 327..329 FT /evidence="ECO:0007829|PDB:3ASL" FT STRAND 330..332 FT /evidence="ECO:0007829|PDB:3ASL" FT TURN 334..336 FT /evidence="ECO:0007829|PDB:3ASL" FT STRAND 339..341 FT /evidence="ECO:0007829|PDB:3ASL" FT HELIX 342..344 FT /evidence="ECO:0007829|PDB:3ASL" FT STRAND 345..347 FT /evidence="ECO:0007829|PDB:3ASL" FT STRAND 354..356 FT /evidence="ECO:0007829|PDB:3ASL" FT TURN 361..363 FT /evidence="ECO:0007829|PDB:3ASL" FT STRAND 417..419 FT /evidence="ECO:0007829|PDB:3DWH" FT STRAND 429..432 FT /evidence="ECO:0007829|PDB:3BI7" FT HELIX 433..438 FT /evidence="ECO:0007829|PDB:3BI7" FT TURN 439..442 FT /evidence="ECO:0007829|PDB:3DWH" FT STRAND 448..452 FT /evidence="ECO:0007829|PDB:3BI7" FT TURN 453..455 FT /evidence="ECO:0007829|PDB:3BI7" FT STRAND 456..462 FT /evidence="ECO:0007829|PDB:3BI7" FT STRAND 473..479 FT /evidence="ECO:0007829|PDB:3BI7" FT TURN 487..489 FT /evidence="ECO:0007829|PDB:3CLZ" FT HELIX 503..511 FT /evidence="ECO:0007829|PDB:3BI7" FT STRAND 512..514 FT /evidence="ECO:0007829|PDB:3BI7" FT TURN 518..520 FT /evidence="ECO:0007829|PDB:3BI7" FT HELIX 527..529 FT /evidence="ECO:0007829|PDB:3BI7" FT STRAND 533..538 FT /evidence="ECO:0007829|PDB:3BI7" FT HELIX 539..544 FT /evidence="ECO:0007829|PDB:3BI7" FT STRAND 546..548 FT /evidence="ECO:0007829|PDB:3CLZ" FT STRAND 550..568 FT /evidence="ECO:0007829|PDB:3BI7" FT STRAND 572..582 FT /evidence="ECO:0007829|PDB:3BI7" FT HELIX 592..601 FT /evidence="ECO:0007829|PDB:3BI7" FT HELIX 611..617 FT /evidence="ECO:0007829|PDB:3BI7" FT HELIX 678..686 FT /evidence="ECO:0007829|PDB:3FL2" FT HELIX 688..690 FT /evidence="ECO:0007829|PDB:3FL2" FT HELIX 691..699 FT /evidence="ECO:0007829|PDB:3FL2" FT STRAND 706..708 FT /evidence="ECO:0007829|PDB:3FL2" FT HELIX 710..721 FT /evidence="ECO:0007829|PDB:3FL2" FT TURN 725..727 FT /evidence="ECO:0007829|PDB:3FL2" FT STRAND 728..730 FT /evidence="ECO:0007829|PDB:3FL2" FT STRAND 732..736 FT /evidence="ECO:0007829|PDB:3FL2" FT STRAND 742..744 FT /evidence="ECO:0007829|PDB:3FL2" FT HELIX 745..753 FT /evidence="ECO:0007829|PDB:3FL2" FT TURN 760..762 FT /evidence="ECO:0007829|PDB:3FL2" FT HELIX 776..785 FT /evidence="ECO:0007829|PDB:3FL2" FT TURN 787..792 FT /evidence="ECO:0007829|PDB:3FL2" SQ 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 //