ID DTX2_HUMAN Reviewed; 622 AA. AC Q86UW9; Q4ZH49; Q6XM87; Q6XM88; Q96H69; Q9H890; Q9P200; DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot. DT 21-JUN-2005, sequence version 3. DT 27-MAR-2024, entry version 176. DE RecName: Full=Probable E3 ubiquitin-protein ligase DTX2; DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q61010}; DE AltName: Full=Protein deltex-2; DE Short=Deltex2; DE Short=hDTX2; DE AltName: Full=RING finger protein 58; DE AltName: Full=RING-type E3 ubiquitin transferase DTX2 {ECO:0000305}; GN Name=DTX2; Synonyms=KIAA1528, RNF58; 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], ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), RP VARIANT GLU-384, SUBUNIT, AND IN VITRO UBIQUITIN LIGASE ACTIVITY. RX PubMed=12670957; DOI=10.1074/jbc.m301157200; RA Takeyama K., Aguiar R.C.T., Gu L., He C., Freeman G.J., Kutok J.L., RA Aster J.C., Shipp M.A.; RT "The BAL-binding protein BBAP and related Deltex family members exhibit RT ubiquitin-protein isopeptide ligase activity."; RL J. Biol. Chem. 278:21930-21937(2003). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ALA-421. RA Yi Z., Yi T., Wu Z.; RT "cDNA cloning, characterization and expression analysis of DTX2, a human RT WWE and RING-finger gene, in human embryos."; RL DNA Seq. 17:175-180(2006). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS GLU-384 RP AND ALA-421. RC TISSUE=Brain; RX PubMed=10819331; DOI=10.1093/dnares/7.2.143; RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XVII. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 7:143-150(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ALA-421. RC TISSUE=Thyroid; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., RA Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLU-384. RC TISSUE=Brain, Lymph, and Muscle; 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 [7] RP SUBCELLULAR LOCATION. RX PubMed=11564735; DOI=10.1074/jbc.m105245200; RA Yamamoto N., Yamamoto S., Inagaki F., Kawaichi M., Fukamizu A., Kishi N., RA Matsuno K., Nakamura K., Weinmaster G., Okano H., Nakafuku M.; RT "Role of Deltex-1 as a transcriptional regulator downstream of the Notch RT receptor."; RL J. Biol. Chem. 276:45031-45040(2001). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360, AND IDENTIFICATION BY RP 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 [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-249, AND IDENTIFICATION BY MASS RP 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 [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=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 [11] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-213; ARG-215; ARG-233 AND RP ARG-256, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). CC -!- FUNCTION: Regulator of Notch signaling, a signaling pathway involved in CC cell-cell communications that regulates a broad spectrum of cell-fate CC determinations. Probably acts both as a positive and negative regulator CC of Notch, depending on the developmental and cell context. Mediates the CC antineural activity of Notch, possibly by inhibiting the CC transcriptional activation mediated by MATCH1. Functions as a ubiquitin CC ligase protein in vitro, suggesting that it may regulate the Notch CC pathway via some ubiquitin ligase activity. 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:0000250|UniProtKB:Q61010}; CC -!- PATHWAY: Protein modification; protein ubiquitination. CC -!- SUBUNIT: Homodimer. May form a heterodimer with other members of the CC Deltex family. Interacts with NOTCH1. {ECO:0000250|UniProtKB:Q61010}. CC -!- INTERACTION: CC Q86UW9; Q8NFV4-4: ABHD11; NbExp=3; IntAct=EBI-740376, EBI-12318443; CC Q86UW9; O95870: ABHD16A; NbExp=7; IntAct=EBI-740376, EBI-348517; CC Q86UW9; Q5BKX5-3: ACTMAP; NbExp=3; IntAct=EBI-740376, EBI-11976299; CC Q86UW9; Q9NXW9: ALKBH4; NbExp=11; IntAct=EBI-740376, EBI-8637516; CC Q86UW9; Q9NYG5-2: ANAPC11; NbExp=3; IntAct=EBI-740376, EBI-12224467; CC Q86UW9; Q9BQD7: ANTKMT; NbExp=3; IntAct=EBI-740376, EBI-713602; CC Q86UW9; Q03989: ARID5A; NbExp=3; IntAct=EBI-740376, EBI-948603; CC Q86UW9; Q9H6L4: ARMC7; NbExp=3; IntAct=EBI-740376, EBI-742909; CC Q86UW9; Q9HBZ2: ARNT2; NbExp=4; IntAct=EBI-740376, EBI-765971; CC Q86UW9; O43521: BCL2L11; NbExp=3; IntAct=EBI-740376, EBI-526406; CC Q86UW9; Q6AI39: BICRAL; NbExp=3; IntAct=EBI-740376, EBI-1012434; CC Q86UW9; A0A0B4J295: BOLA2-SMG1P6; NbExp=3; IntAct=EBI-740376, EBI-12906362; CC Q86UW9; Q5SWW7: C10orf55; NbExp=3; IntAct=EBI-740376, EBI-12809220; CC Q86UW9; Q6P1W5: C1orf94; NbExp=3; IntAct=EBI-740376, EBI-946029; CC Q86UW9; Q6P5X5: C22orf39; NbExp=5; IntAct=EBI-740376, EBI-7317823; CC Q86UW9; Q2TAC2-2: CCDC57; NbExp=3; IntAct=EBI-740376, EBI-10961624; CC Q86UW9; Q9H5F2: CFAP68; NbExp=3; IntAct=EBI-740376, EBI-718615; CC Q86UW9; Q9H1P6: CIMIP1; NbExp=3; IntAct=EBI-740376, EBI-12155483; CC Q86UW9; Q16740: CLPP; NbExp=5; IntAct=EBI-740376, EBI-1056029; CC Q86UW9; Q5JTJ3: COA6; NbExp=3; IntAct=EBI-740376, EBI-2874677; CC Q86UW9; Q8NI60: COQ8A; NbExp=3; IntAct=EBI-740376, EBI-745535; CC Q86UW9; Q15038: DAZAP2; NbExp=3; IntAct=EBI-740376, EBI-724310; CC Q86UW9; Q7L591-3: DOK3; NbExp=3; IntAct=EBI-740376, EBI-10694655; CC Q86UW9; Q16610: ECM1; NbExp=3; IntAct=EBI-740376, EBI-947964; CC Q86UW9; Q9BQ95: ECSIT; NbExp=3; IntAct=EBI-740376, EBI-712452; CC Q86UW9; Q9NRA8: EIF4ENIF1; NbExp=7; IntAct=EBI-740376, EBI-301024; CC Q86UW9; Q04637-9: EIF4G1; NbExp=3; IntAct=EBI-740376, EBI-12012124; CC Q86UW9; O00167-2: EYA2; NbExp=3; IntAct=EBI-740376, EBI-12807776; CC Q86UW9; Q92567: FAM168A; NbExp=6; IntAct=EBI-740376, EBI-7957930; CC Q86UW9; Q92567-2: FAM168A; NbExp=3; IntAct=EBI-740376, EBI-11978259; CC Q86UW9; Q96PJ5: FCRL4; NbExp=3; IntAct=EBI-740376, EBI-4314687; CC Q86UW9; Q14192: FHL2; NbExp=6; IntAct=EBI-740376, EBI-701903; CC Q86UW9; Q5TD97: FHL5; NbExp=3; IntAct=EBI-740376, EBI-750641; CC Q86UW9; Q12951-2: FOXI1; NbExp=3; IntAct=EBI-740376, EBI-12018822; CC Q86UW9; Q9C0B1-2: FTO; NbExp=3; IntAct=EBI-740376, EBI-18138793; CC Q86UW9; Q8IVS8: GLYCTK; NbExp=6; IntAct=EBI-740376, EBI-748515; CC Q86UW9; Q08379: GOLGA2; NbExp=3; IntAct=EBI-740376, EBI-618309; CC Q86UW9; P19113: HDC; NbExp=6; IntAct=EBI-740376, EBI-10200283; CC Q86UW9; O14964: HGS; NbExp=3; IntAct=EBI-740376, EBI-740220; CC Q86UW9; Q14774: HLX; NbExp=3; IntAct=EBI-740376, EBI-6678255; CC Q86UW9; P49639: HOXA1; NbExp=6; IntAct=EBI-740376, EBI-740785; CC Q86UW9; P14652: HOXB2; NbExp=3; IntAct=EBI-740376, EBI-5329558; CC Q86UW9; P35452-2: HOXD12; NbExp=3; IntAct=EBI-740376, EBI-17244356; CC Q86UW9; P84074: HPCA; NbExp=3; IntAct=EBI-740376, EBI-12197079; CC Q86UW9; P37235: HPCAL1; NbExp=4; IntAct=EBI-740376, EBI-749311; CC Q86UW9; Q9UM19: HPCAL4; NbExp=7; IntAct=EBI-740376, EBI-744820; CC Q86UW9; Q96LI6: HSFY2; NbExp=3; IntAct=EBI-740376, EBI-3957665; CC Q86UW9; Q9UKT9: IKZF3; NbExp=3; IntAct=EBI-740376, EBI-747204; CC Q86UW9; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-740376, EBI-2556193; CC Q86UW9; Q6P597: KLC3; NbExp=6; IntAct=EBI-740376, EBI-1643885; CC Q86UW9; Q96G42: KLHDC7B; NbExp=3; IntAct=EBI-740376, EBI-9478422; CC Q86UW9; Q8IUC1: KRTAP11-1; NbExp=3; IntAct=EBI-740376, EBI-1052037; CC Q86UW9; Q3SY46: KRTAP13-3; NbExp=3; IntAct=EBI-740376, EBI-10241252; CC Q86UW9; Q3LI76: KRTAP15-1; NbExp=3; IntAct=EBI-740376, EBI-11992140; CC Q86UW9; Q8IUB9: KRTAP19-1; NbExp=3; IntAct=EBI-740376, EBI-12811111; CC Q86UW9; Q3LI70: KRTAP19-6; NbExp=3; IntAct=EBI-740376, EBI-12805508; CC Q86UW9; Q3SYF9: KRTAP19-7; NbExp=3; IntAct=EBI-740376, EBI-10241353; CC Q86UW9; Q6PEX3: KRTAP26-1; NbExp=3; IntAct=EBI-740376, EBI-3957672; CC Q86UW9; Q3LI64: KRTAP6-1; NbExp=3; IntAct=EBI-740376, EBI-12111050; CC Q86UW9; Q8IUC3: KRTAP7-1; NbExp=3; IntAct=EBI-740376, EBI-18394498; CC Q86UW9; Q8IUC2: KRTAP8-1; NbExp=3; IntAct=EBI-740376, EBI-10261141; CC Q86UW9; Q14847-2: LASP1; NbExp=3; IntAct=EBI-740376, EBI-9088686; CC Q86UW9; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-740376, EBI-739832; CC Q86UW9; Q9P2M1: LRP2BP; NbExp=3; IntAct=EBI-740376, EBI-18273118; CC Q86UW9; Q8WWY6: MBD3L1; NbExp=3; IntAct=EBI-740376, EBI-12516603; CC Q86UW9; A0JLT2-2: MED19; NbExp=3; IntAct=EBI-740376, EBI-13288755; CC Q86UW9; Q4VC12: MSS51; NbExp=3; IntAct=EBI-740376, EBI-11599933; CC Q86UW9; Q14764: MVP; NbExp=3; IntAct=EBI-740376, EBI-2816254; CC Q86UW9; Q9BRK3: MXRA8; NbExp=3; IntAct=EBI-740376, EBI-11721798; CC Q86UW9; P61601: NCALD; NbExp=12; IntAct=EBI-740376, EBI-749635; CC Q86UW9; P62166: NCS1; NbExp=13; IntAct=EBI-740376, EBI-746987; CC Q86UW9; P0CG21: NHLRC4; NbExp=3; IntAct=EBI-740376, EBI-12868744; CC Q86UW9; Q9GZT8: NIF3L1; NbExp=3; IntAct=EBI-740376, EBI-740897; CC Q86UW9; O00746: NME4; NbExp=3; IntAct=EBI-740376, EBI-744871; CC Q86UW9; O43482: OIP5; NbExp=3; IntAct=EBI-740376, EBI-536879; CC Q86UW9; Q02548: PAX5; NbExp=3; IntAct=EBI-740376, EBI-296331; CC Q86UW9; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-740376, EBI-742388; CC Q86UW9; Q58EX7: PLEKHG4; NbExp=3; IntAct=EBI-740376, EBI-949255; CC Q86UW9; Q7Z3K3: POGZ; NbExp=3; IntAct=EBI-740376, EBI-1389308; CC Q86UW9; B1ATL7: PRR32; NbExp=3; IntAct=EBI-740376, EBI-18587059; CC Q86UW9; Q9NV39: PRR34; NbExp=3; IntAct=EBI-740376, EBI-11959565; CC Q86UW9; P28070: PSMB4; NbExp=3; IntAct=EBI-740376, EBI-603350; CC Q86UW9; P47897-2: QARS1; NbExp=3; IntAct=EBI-740376, EBI-10209725; CC Q86UW9; P57052: RBM11; NbExp=3; IntAct=EBI-740376, EBI-741332; CC Q86UW9; Q93062: RBPMS; NbExp=7; IntAct=EBI-740376, EBI-740322; CC Q86UW9; Q8HWS3: RFX6; NbExp=4; IntAct=EBI-740376, EBI-746118; CC Q86UW9; Q9UFD9: RIMBP3; NbExp=3; IntAct=EBI-740376, EBI-10182375; CC Q86UW9; Q9BVN2: RUSC1; NbExp=3; IntAct=EBI-740376, EBI-6257312; CC Q86UW9; Q7Z5V6-2: SAXO4; NbExp=3; IntAct=EBI-740376, EBI-12000762; CC Q86UW9; Q96IW7: SEC22A; NbExp=10; IntAct=EBI-740376, EBI-8652744; CC Q86UW9; Q15436: SEC23A; NbExp=3; IntAct=EBI-740376, EBI-81088; CC Q86UW9; Q15437: SEC23B; NbExp=6; IntAct=EBI-740376, EBI-742673; CC Q86UW9; Q9HD40-3: SEPSECS; NbExp=3; IntAct=EBI-740376, EBI-12190001; CC Q86UW9; Q8N1D0-2: SLC22A18AS; NbExp=3; IntAct=EBI-740376, EBI-12829638; CC Q86UW9; Q5JUK2: SOHLH1; NbExp=3; IntAct=EBI-740376, EBI-12288855; CC Q86UW9; Q99932: SPAG8; NbExp=3; IntAct=EBI-740376, EBI-954419; CC Q86UW9; Q9NZD8: SPG21; NbExp=7; IntAct=EBI-740376, EBI-742688; CC Q86UW9; Q86Y82: STX12; NbExp=7; IntAct=EBI-740376, EBI-2691717; CC Q86UW9; P63165: SUMO1; NbExp=3; IntAct=EBI-740376, EBI-80140; CC Q86UW9; Q96SF7: TBX15; NbExp=3; IntAct=EBI-740376, EBI-10191361; CC Q86UW9; Q96M29: TEKT5; NbExp=3; IntAct=EBI-740376, EBI-10239812; CC Q86UW9; Q6PIY7: TENT2; NbExp=3; IntAct=EBI-740376, EBI-2802204; CC Q86UW9; Q69YG0: TMEM42; NbExp=3; IntAct=EBI-740376, EBI-12038591; CC Q86UW9; Q96RU7: TRIB3; NbExp=3; IntAct=EBI-740376, EBI-492476; CC Q86UW9; Q9UPQ4-2: TRIM35; NbExp=3; IntAct=EBI-740376, EBI-17716262; CC Q86UW9; Q9BYV2: TRIM54; NbExp=9; IntAct=EBI-740376, EBI-2130429; CC Q86UW9; Q15654: TRIP6; NbExp=3; IntAct=EBI-740376, EBI-742327; CC Q86UW9; P51668: UBE2D1; NbExp=7; IntAct=EBI-740376, EBI-743540; CC Q86UW9; P62837: UBE2D2; NbExp=3; IntAct=EBI-740376, EBI-347677; CC Q86UW9; P61077: UBE2D3; NbExp=9; IntAct=EBI-740376, EBI-348268; CC Q86UW9; Q9Y2X8: UBE2D4; NbExp=13; IntAct=EBI-740376, EBI-745527; CC Q86UW9; Q70EL1-9: USP54; NbExp=3; IntAct=EBI-740376, EBI-11975223; CC Q86UW9; A8MV65-2: VGLL3; NbExp=3; IntAct=EBI-740376, EBI-11957216; CC Q86UW9; P62760: VSNL1; NbExp=10; IntAct=EBI-740376, EBI-740943; CC Q86UW9; Q96F45: ZNF503; NbExp=3; IntAct=EBI-740376, EBI-8832437; CC Q86UW9; Q6ZNG0: ZNF620; NbExp=3; IntAct=EBI-740376, EBI-4395669; CC Q86UW9; Q96H86: ZNF764; NbExp=3; IntAct=EBI-740376, EBI-745775; CC Q86UW9; Q6NX45: ZNF774; NbExp=3; IntAct=EBI-740376, EBI-10251462; CC Q86UW9; Q49A12: ZNF85; NbExp=3; IntAct=EBI-740376, EBI-18141506; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11564735}. Nucleus CC {ECO:0000269|PubMed:11564735}. Note=Predominantly cytoplasmic. CC Partially nuclear. {ECO:0000269|PubMed:11564735}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=A; CC IsoId=Q86UW9-1; Sequence=Displayed; CC Name=2; Synonyms=B; CC IsoId=Q86UW9-2; Sequence=VSP_008350; CC -!- DOMAIN: The WWE domains are thought to mediate some protein-protein CC interaction, and are frequently found in ubiquitin ligases. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the Deltex family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA96052.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; AY225124; AAP57518.1; -; mRNA. DR EMBL; AY225125; AAP57519.1; -; mRNA. DR EMBL; DQ010329; AAY27263.1; -; mRNA. DR EMBL; AB040961; BAA96052.1; ALT_INIT; mRNA. DR EMBL; AK023924; BAB14727.1; -; mRNA. DR EMBL; AC005522; AAP21881.1; -; Genomic_DNA. DR EMBL; AC007078; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC008856; AAH08856.1; -; mRNA. DR EMBL; BC018555; AAH18555.1; -; mRNA. DR EMBL; BC026059; AAH26059.1; -; mRNA. DR EMBL; BC093079; AAH93079.1; -; mRNA. DR CCDS; CCDS43605.1; -. [Q86UW9-2] DR CCDS; CCDS5587.1; -. [Q86UW9-1] DR RefSeq; NP_001096064.1; NM_001102594.1. [Q86UW9-1] DR RefSeq; NP_001096065.1; NM_001102595.1. [Q86UW9-1] DR RefSeq; NP_001096066.1; NM_001102596.1. [Q86UW9-2] DR RefSeq; NP_065943.2; NM_020892.2. [Q86UW9-1] DR RefSeq; XP_005250188.1; XM_005250131.1. DR RefSeq; XP_005250189.1; XM_005250132.1. DR RefSeq; XP_011514074.1; XM_011515772.1. DR RefSeq; XP_011514075.1; XM_011515773.2. DR RefSeq; XP_011514076.1; XM_011515774.1. [Q86UW9-1] DR RefSeq; XP_011514077.1; XM_011515775.1. DR RefSeq; XP_016867212.1; XM_017011723.1. DR RefSeq; XP_016867213.1; XM_017011724.1. [Q86UW9-1] DR RefSeq; XP_016867214.1; XM_017011725.1. DR RefSeq; XP_016867215.1; XM_017011726.1. [Q86UW9-2] DR RefSeq; XP_016867216.1; XM_017011727.1. DR PDB; 6IR0; NMR; -; A=399-474. DR PDB; 6Y22; X-ray; 2.07 A; A=390-622. DR PDB; 6Y2X; X-ray; 1.77 A; A/B=390-622. DR PDB; 6Y3J; X-ray; 2.60 A; A=390-622. DR PDBsum; 6IR0; -. DR PDBsum; 6Y22; -. DR PDBsum; 6Y2X; -. DR PDBsum; 6Y3J; -. DR AlphaFoldDB; Q86UW9; -. DR SMR; Q86UW9; -. DR BioGRID; 125266; 331. DR IntAct; Q86UW9; 124. DR MINT; Q86UW9; -. DR STRING; 9606.ENSP00000322885; -. DR GlyGen; Q86UW9; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q86UW9; -. DR PhosphoSitePlus; Q86UW9; -. DR BioMuta; DTX2; -. DR DMDM; 68067880; -. DR EPD; Q86UW9; -. DR jPOST; Q86UW9; -. DR MassIVE; Q86UW9; -. DR MaxQB; Q86UW9; -. DR PaxDb; 9606-ENSP00000322885; -. DR PeptideAtlas; Q86UW9; -. DR ProteomicsDB; 69923; -. [Q86UW9-1] DR ProteomicsDB; 69924; -. [Q86UW9-2] DR Pumba; Q86UW9; -. DR Antibodypedia; 35109; 221 antibodies from 31 providers. DR DNASU; 113878; -. DR Ensembl; ENST00000324432.9; ENSP00000322885.5; ENSG00000091073.20. [Q86UW9-1] DR Ensembl; ENST00000413936.6; ENSP00000390218.2; ENSG00000091073.20. [Q86UW9-1] DR Ensembl; ENST00000430490.7; ENSP00000411986.2; ENSG00000091073.20. [Q86UW9-1] DR Ensembl; ENST00000446820.6; ENSP00000392545.2; ENSG00000091073.20. [Q86UW9-2] DR GeneID; 113878; -. DR KEGG; hsa:113878; -. DR MANE-Select; ENST00000430490.7; ENSP00000411986.2; NM_001102594.3; NP_001096064.1. DR UCSC; uc003uff.5; human. [Q86UW9-1] DR AGR; HGNC:15973; -. DR CTD; 113878; -. DR DisGeNET; 113878; -. DR GeneCards; DTX2; -. DR HGNC; HGNC:15973; DTX2. DR HPA; ENSG00000091073; Tissue enhanced (esophagus). DR MIM; 613141; gene. DR neXtProt; NX_Q86UW9; -. DR OpenTargets; ENSG00000091073; -. DR PharmGKB; PA27515; -. DR VEuPathDB; HostDB:ENSG00000091073; -. DR eggNOG; ENOG502QQ9M; Eukaryota. DR GeneTree; ENSGT00940000157641; -. DR HOGENOM; CLU_030422_4_0_1; -. DR InParanoid; Q86UW9; -. DR OMA; DAPEEDC; -. DR OrthoDB; 5487971at2759; -. DR PhylomeDB; Q86UW9; -. DR PathwayCommons; Q86UW9; -. DR Reactome; R-HSA-2122948; Activated NOTCH1 Transmits Signal to the Nucleus. DR SignaLink; Q86UW9; -. DR SIGNOR; Q86UW9; -. DR UniPathway; UPA00143; -. DR BioGRID-ORCS; 113878; 35 hits in 1197 CRISPR screens. DR ChiTaRS; DTX2; human. DR GeneWiki; DTX2; -. DR GenomeRNAi; 113878; -. DR Pharos; Q86UW9; Tbio. DR PRO; PR:Q86UW9; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; Q86UW9; Protein. DR Bgee; ENSG00000091073; Expressed in lower esophagus mucosa and 96 other cell types or tissues. DR ExpressionAtlas; Q86UW9; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0031965; C:nuclear membrane; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0007219; P:Notch signaling pathway; IBA:GO_Central. DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central. DR CDD; cd09633; Deltex_C; 1. DR CDD; cd16672; RING-H2_DTX2; 1. DR Gene3D; 3.30.390.130; -; 1. DR Gene3D; 3.30.720.50; -; 2. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR InterPro; IPR039396; Deltex_C. DR InterPro; IPR039399; Deltex_C_sf. DR InterPro; IPR039398; Deltex_fam. DR InterPro; IPR004170; WWE-dom. DR InterPro; IPR018123; WWE-dom_subgr. DR InterPro; IPR037197; WWE_dom_sf. DR InterPro; IPR018957; Znf_C3HC4_RING-type. DR InterPro; IPR001841; Znf_RING. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR PANTHER; PTHR12622; DELTEX-RELATED; 1. DR PANTHER; PTHR12622:SF21; E3 UBIQUITIN-PROTEIN LIGASE DTX2-RELATED; 1. DR Pfam; PF18102; DTC; 1. DR Pfam; PF02825; WWE; 2. DR Pfam; PF00097; zf-C3HC4; 1. DR SMART; SM00184; RING; 1. DR SMART; SM00678; WWE; 2. DR SUPFAM; SSF57850; RING/U-box; 1. DR SUPFAM; SSF117839; WWE domain; 2. DR PROSITE; PS50918; WWE; 2. DR PROSITE; PS50089; ZF_RING_2; 1. DR Genevisible; Q86UW9; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; Metal-binding; KW Methylation; Notch signaling pathway; Nucleus; Phosphoprotein; KW Reference proteome; Repeat; Transferase; Ubl conjugation pathway; Zinc; KW Zinc-finger. FT CHAIN 1..622 FT /note="Probable E3 ubiquitin-protein ligase DTX2" FT /id="PRO_0000219083" FT DOMAIN 8..97 FT /note="WWE 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00248" FT DOMAIN 98..174 FT /note="WWE 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00248" FT ZN_FING 412..473 FT /note="RING-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175" FT REGION 249..324 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 355..393 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 255..319 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 213 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 215 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 233 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 249 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 256 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 360 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT VAR_SEQ 337..383 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_008350" FT VARIANT 94 FT /note="A -> T (in dbSNP:rs2462312)" FT /id="VAR_016920" FT VARIANT 384 FT /note="G -> E (in dbSNP:rs1638152)" FT /evidence="ECO:0000269|PubMed:10819331, FT ECO:0000269|PubMed:12670957, ECO:0000269|PubMed:15489334" FT /id="VAR_016921" FT VARIANT 421 FT /note="T -> A (in dbSNP:rs6979487)" FT /evidence="ECO:0000269|PubMed:10819331, FT ECO:0000269|PubMed:14702039, ECO:0000269|Ref.2" FT /id="VAR_016922" FT HELIX 393..399 FT /evidence="ECO:0007829|PDB:6Y2X" FT STRAND 401..403 FT /evidence="ECO:0007829|PDB:6Y2X" FT STRAND 409..411 FT /evidence="ECO:0007829|PDB:6Y22" FT TURN 413..415 FT /evidence="ECO:0007829|PDB:6Y2X" FT TURN 419..421 FT /evidence="ECO:0007829|PDB:6IR0" FT TURN 424..428 FT /evidence="ECO:0007829|PDB:6Y2X" FT STRAND 439..442 FT /evidence="ECO:0007829|PDB:6Y2X" FT TURN 443..445 FT /evidence="ECO:0007829|PDB:6Y2X" FT STRAND 448..450 FT /evidence="ECO:0007829|PDB:6Y2X" FT HELIX 451..457 FT /evidence="ECO:0007829|PDB:6Y2X" FT TURN 458..460 FT /evidence="ECO:0007829|PDB:6IR0" FT STRAND 464..466 FT /evidence="ECO:0007829|PDB:6IR0" FT TURN 470..472 FT /evidence="ECO:0007829|PDB:6Y2X" FT STRAND 475..477 FT /evidence="ECO:0007829|PDB:6Y2X" FT STRAND 487..494 FT /evidence="ECO:0007829|PDB:6Y2X" FT STRAND 505..511 FT /evidence="ECO:0007829|PDB:6Y2X" FT STRAND 521..523 FT /evidence="ECO:0007829|PDB:6Y2X" FT STRAND 526..529 FT /evidence="ECO:0007829|PDB:6Y2X" FT STRAND 534..542 FT /evidence="ECO:0007829|PDB:6Y2X" FT HELIX 543..557 FT /evidence="ECO:0007829|PDB:6Y2X" FT STRAND 561..565 FT /evidence="ECO:0007829|PDB:6Y2X" FT TURN 568..570 FT /evidence="ECO:0007829|PDB:6Y2X" FT STRAND 573..578 FT /evidence="ECO:0007829|PDB:6Y2X" FT TURN 589..592 FT /evidence="ECO:0007829|PDB:6Y2X" FT HELIX 601..611 FT /evidence="ECO:0007829|PDB:6Y2X" FT HELIX 616..619 FT /evidence="ECO:0007829|PDB:6Y2X" SQ SEQUENCE 622 AA; 67246 MW; ABE1398204F2273A CRC64; MAMAPSPSLV QVYTSPAAVA VWEWQDGLGT WHPYSATVCS FIEQQFVQQK GQRFGLGSLA HSIPLGQADP SLAPYIIDLP SWTQFRQDTG TMRAVRRHLF PQHSAPGRGV VWEWLSDDGS WTAYEASVCD YLEQQVARGN QLVDLAPLGY NYTVNYTTHT QTNKTSSFCR SVRRQAGPPY PVTTIIAPPG HTGVACSCHQ CLSGSRTGPV SGRYRHSMTN LPAYPVPQHP PHRTASVFGT HQAFAPYNKP SLSGARSAPR LNTTNAWGAA PPSLGSQPLY RSSLSHLGPQ HLPPGSSTSG AVSASLPSGP SSSPGSVPAT VPMQMPKPSR VQQALAGMTS VLMSAIGLPV CLSRAPQPTS PPASRLASKS HGSVKRLRKM SVKGATPKPE PEPEQVIKNY TEELKVPPDE DCIICMEKLS TASGYSDVTD SKAIGSLAVG HLTKCSHAFH LLCLLAMYCN GNKDGSLQCP SCKTIYGEKT GTQPQGKMEV LRFQMSLPGH EDCGTILIVY SIPHGIQGPE HPNPGKPFTA RGFPRQCYLP DNAQGRKVLE LLKVAWKRRL IFTVGTSSTT GETDTVVWNE IHHKTEMDRN ITGHGYPDPN YLQNVLAELA AQGVTEDCLE QQ //