ID MO4L1_HUMAN Reviewed; 362 AA. AC Q9UBU8; B4DKN6; B7Z6R1; D3DW88; O95899; Q5QTS1; Q6NVX8; Q86YT7; Q9HBP6; AC Q9NSW5; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 15-FEB-2005, sequence version 2. DT 22-FEB-2023, entry version 223. DE RecName: Full=Mortality factor 4-like protein 1; DE AltName: Full=MORF-related gene 15 protein; DE AltName: Full=Protein MSL3-1; DE AltName: Full=Transcription factor-like protein MRG15; GN Name=MORF4L1; Synonyms=MRG15; ORFNames=FWP006, HSPC008, HSPC061, PP368; 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 2). RX PubMed=9891081; DOI=10.1128/mcb.19.2.1479; RA Bertram M.J., Berube N.G., Hang-Swanson X., Ran Q., Leung J.K., Bryce S., RA Spurgers K., Bick R.J., Baldini A., Ning Y., Clark L.J., Parkinson E.K., RA Barrett J.C., Smith J.R., Pereira-Smith O.M.; RT "Identification of a gene that reverses the immortal phenotype of a subset RT of cells and is a member of a novel family of transcription factor-like RT genes."; RL Mol. Cell. Biol. 19:1479-1485(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RA D'Esposito M., Cocchia M., Matarazzo M.R., Macmillan S., Mazzarella R.; RT "Two human homologs of the Drosophila dosage compensation gene msl-3 are RT located on the X chromosome."; RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=15498874; DOI=10.1073/pnas.0404089101; RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X., RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.; RT "Large-scale cDNA transfection screening for genes related to cancer RT development and progression."; RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Lung; RA Guo S., Tong T., Zhang Z.; RT "Cloning and identification of cellular senescence associated genes from RT fibroblasts 2BS."; RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Umbilical cord blood; RX PubMed=11042152; DOI=10.1101/gr.140200; RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.; RT "Cloning and functional analysis of cDNAs with open reading frames for 300 RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor RT cells."; RL Genome Res. 10:1546-1560(2000). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Aorta; RA Liu B., Zhao B., Wang X.Y., Xu Y.Y., Liu Y.Q., Song L., Ye J., Sheng H., RA Gao Y., Zhang C.L., Wei Y.J., Zhang J., Song L., Jiang Y.X., Zhao Z.W., RA Ding J.F., Liu L.S., Gao R.L., Wu Q.Y., Qiang B.Q., Yuan J.G., Liew C.C., RA Zhao M.S., Hui R.T.; RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). RC TISSUE=Colon, and Embryonic stem cell; 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 [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Kidney; 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 [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16572171; DOI=10.1038/nature04601; RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S., RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.; RT "Analysis of the DNA sequence and duplication history of human chromosome RT 15."; RL Nature 440:671-675(2006). RN [10] 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). RC TISSUE=Embryonic stem cell, Skin, and Testis; 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 [12] RP PROTEIN SEQUENCE OF 17-29; 42-51; 118-127; 156-173; 179-192; 228-240; RP 244-261 AND 340-359, AND IDENTIFICATION IN NUA4 COMPLEX. RX PubMed=12963728; DOI=10.1074/jbc.c300389200; RA Cai Y., Jin J., Tomomori-Sato C., Sato S., Sorokina I., Parmely T.J., RA Conaway R.C., Conaway J.W.; RT "Identification of new subunits of the multiprotein mammalian TRRAP/TIP60- RT containing histone acetyltransferase complex."; RL J. Biol. Chem. 278:42733-42736(2003). RN [13] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 120-362 (ISOFORMS 1/2). RC TISSUE=Brain; RA Mei G., Yu W., Gibbs R.A.; RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases. RN [14] RP INTERACTION WITH MRFAP1 AND RB1. RX PubMed=11500496; DOI=10.1074/jbc.m103435200; RA Leung J.K., Berube N., Venable S., Ahmed S., Timchenko N., RA Pereira-Smith O.M.; RT "MRG15 activates the B-myb promoter through formation of a nuclear complex RT with the retinoblastoma protein and the novel protein PAM14."; RL J. Biol. Chem. 276:39171-39178(2001). RN [15] RP IDENTIFICATION IN COMPLEX WITH RB1 AND MRFAP1, AND INTERACTION WITH RB1 AND RP KAT8. RX PubMed=12397079; DOI=10.1074/jbc.m203839200; RA Pardo P.S., Leung J.K., Lucchesi J.C., Pereira-Smith O.M.; RT "MRG15, a novel chromodomain protein, is present in two distinct RT multiprotein complexes involved in transcriptional activation."; RL J. Biol. Chem. 277:50860-50866(2002). RN [16] RP INTERACTION WITH PHF12; SIN3A AND TLE FAMILY MEMBERS. RX PubMed=12391155; DOI=10.1128/mcb.22.22.7868-7876.2002; RA Yochum G.S., Ayer D.E.; RT "Role for the mortality factors MORF4, MRGX, and MRG15 in transcriptional RT repression via associations with Pf1, mSin3A, and transducin-like enhancer RT of Split."; RL Mol. Cell. Biol. 22:7868-7876(2002). RN [17] RP REVIEW ON NUA4 COMPLEX. RX PubMed=15196461; DOI=10.1016/j.gde.2004.02.009; RA Doyon Y., Cote J.; RT "The highly conserved and multifunctional NuA4 HAT complex."; RL Curr. Opin. Genet. Dev. 14:147-154(2004). RN [18] RP FUNCTION, IDENTIFICATION IN NUA4 COMPLEX, AND IDENTIFICATION IN SIN3A RP COMPLEX. RX PubMed=14966270; DOI=10.1128/mcb.24.5.1884-1896.2004; RA Doyon Y., Selleck W., Lane W.S., Tan S., Cote J.; RT "Structural and functional conservation of the NuA4 histone RT acetyltransferase complex from yeast to humans."; RL Mol. Cell. Biol. 24:1884-1896(2004). RN [19] RP INTERACTION WITH MSL1 AND NUPR1. RX PubMed=19650074; DOI=10.1002/jcp.21889; RA Gironella M., Malicet C., Cano C., Sandi M.J., Hamidi T., Tauil R.M., RA Baston M., Valaco P., Moreno S., Lopez F., Neira J.L., Dagorn J.C., RA Iovanna J.L.; RT "p8/nupr1 regulates DNA-repair activity after double-strand gamma RT irradiation-induced DNA damage."; RL J. Cell. Physiol. 221:594-602(2009). RN [20] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-143, 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 [21] RP FUNCTION, AND INTERACTION WITH BRCA COMPLEX AND PALB2. RX PubMed=20332121; DOI=10.1242/jcs.060178; RA Hayakawa T., Zhang F., Hayakawa N., Ohtani Y., Shinmyozu K., Nakayama J., RA Andreassen P.R.; RT "MRG15 binds directly to PALB2 and stimulates homology-directed repair of RT chromosomal breaks."; RL J. Cell Sci. 123:1124-1130(2010). RN [22] 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 [23] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 190-362, AND INTERACTION WITH RP MRFAP1. RX PubMed=17008723; DOI=10.1110/ps.062397806; RA Zhang P., Zhao J., Wang B., Du J., Lu Y., Chen J., Ding J.; RT "The MRG domain of human MRG15 uses a shallow hydrophobic pocket to RT interact with the N-terminal region of PAM14."; RL Protein Sci. 15:2423-2434(2006). RN [24] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 190-362, AND MUTAGENESIS OF RP VAL-208; GLU-234; TYR-251 AND ASN-254. RX PubMed=16407074; DOI=10.1016/j.str.2005.08.019; RA Bowman B.R., Moure C.M., Kirtane B.M., Welschhans R.L., Tominaga K., RA Pereira-Smith O.M., Quiocho F.A.; RT "Multipurpose MRG domain involved in cell senescence and proliferation RT exhibits structural homology to a DNA-interacting domain."; RL Structure 14:151-158(2006). CC -!- FUNCTION: Component of the NuA4 histone acetyltransferase (HAT) complex CC which is involved in transcriptional activation of select genes CC principally by acetylation of nucleosomal histones H4 and H2A. This CC modification may both alter nucleosome - DNA interactions and promote CC interaction of the modified histones with other proteins which CC positively regulate transcription. This complex may be required for the CC activation of transcriptional programs associated with oncogene and CC proto-oncogene mediated growth induction, tumor suppressor mediated CC growth arrest and replicative senescence, apoptosis, and DNA repair. CC The NuA4 complex ATPase and helicase activities seem to be, at least in CC part, contributed by the association of RUVBL1 and RUVBL2 with EP400. CC NuA4 may also play a direct role in DNA repair when directly recruited CC to sites of DNA damage. Also a component of the mSin3A complex which CC acts to repress transcription by deacetylation of nucleosomal histones. CC Required for homologous recombination repair (HRR) and resistance to CC mitomycin C (MMC). Involved in the localization of PALB2, BRCA2 and CC RAD51, but not BRCA1, to DNA-damage foci. {ECO:0000269|PubMed:14966270, CC ECO:0000269|PubMed:20332121}. CC -!- SUBUNIT: Component of the NuA4 histone acetyltransferase complex which CC contains the catalytic subunit KAT5/TIP60 and the subunits EP400, CC TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, CC ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP, CC YEATS4/GAS41, VPS72/YL1 and MEAF6. The NuA4 complex interacts with MYC CC and the adenovirus E1A protein. MORF4L1 may also participate in the CC formation of NuA4 related complexes which lack the KAT5/TIP60 catalytic CC subunit, but which include the SWI/SNF related protein SRCAP. Component CC of the mSin3A histone deacetylase complex, which includes SIN3A, HDAC2, CC ARID4B, MORF4L1, RBBP4/RbAp48, and RBBP7/RbAp46. Interacts with RB1 and CC KAT8. May also interact with PHF12 and one or more as yet undefined CC members of the TLE (transducin-like enhancer of split) family of CC transcriptional repressors. Interacts with the N-terminus of MRFAP1. CC Found in a complex composed of MORF4L1, MRFAP1 and RB1. Interacts with CC the entire BRCA complex, which contains BRCA1, PALB2, BRCA2 and RAD51. CC Interacts with PALB2. Forms a complex with MSL1 and NUPR1. CC {ECO:0000269|PubMed:11500496, ECO:0000269|PubMed:12391155, CC ECO:0000269|PubMed:12397079, ECO:0000269|PubMed:12963728, CC ECO:0000269|PubMed:14966270, ECO:0000269|PubMed:17008723, CC ECO:0000269|PubMed:19650074, ECO:0000269|PubMed:20332121}. CC -!- INTERACTION: CC Q9UBU8; Q96B67: ARRDC3; NbExp=3; IntAct=EBI-399246, EBI-2875665; CC Q9UBU8; Q8N7W2-2: BEND7; NbExp=3; IntAct=EBI-399246, EBI-10181188; CC Q9UBU8; Q13554: CAMK2B; NbExp=3; IntAct=EBI-399246, EBI-1058722; CC Q9UBU8; Q8IYX8-2: CEP57L1; NbExp=3; IntAct=EBI-399246, EBI-10181988; CC Q9UBU8; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-399246, EBI-10175124; CC Q9UBU8; Q53SE7: FLJ13057; NbExp=3; IntAct=EBI-399246, EBI-10172181; CC Q9UBU8; P51116: FXR2; NbExp=3; IntAct=EBI-399246, EBI-740459; CC Q9UBU8; Q08379: GOLGA2; NbExp=3; IntAct=EBI-399246, EBI-618309; CC Q9UBU8; Q6NT76: HMBOX1; NbExp=3; IntAct=EBI-399246, EBI-2549423; CC Q9UBU8; Q6NT76-2: HMBOX1; NbExp=3; IntAct=EBI-399246, EBI-10212206; CC Q9UBU8; Q13422: IKZF1; NbExp=3; IntAct=EBI-399246, EBI-745305; CC Q9UBU8; Q96JM7: L3MBTL3; NbExp=3; IntAct=EBI-399246, EBI-2686809; CC Q9UBU8; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-399246, EBI-741037; CC Q9UBU8; P50221: MEOX1; NbExp=3; IntAct=EBI-399246, EBI-2864512; CC Q9UBU8; Q9Y605: MRFAP1; NbExp=7; IntAct=EBI-399246, EBI-995714; CC Q9UBU8; Q96HT8: MRFAP1L1; NbExp=9; IntAct=EBI-399246, EBI-748896; CC Q9UBU8; Q9NV56: MRGBP; NbExp=7; IntAct=EBI-399246, EBI-399076; CC Q9UBU8; Q15742: NAB2; NbExp=3; IntAct=EBI-399246, EBI-8641936; CC Q9UBU8; Q8IVL1: NAV2; NbExp=3; IntAct=EBI-399246, EBI-741200; CC Q9UBU8; Q96AQ6: PBXIP1; NbExp=3; IntAct=EBI-399246, EBI-740845; CC Q9UBU8; Q9H0H5: RACGAP1; NbExp=3; IntAct=EBI-399246, EBI-717233; CC Q9UBU8; Q04864: REL; NbExp=3; IntAct=EBI-399246, EBI-307352; CC Q9UBU8; Q12800: TFCP2; NbExp=3; IntAct=EBI-399246, EBI-717422; CC Q9UBU8; Q9NVV9: THAP1; NbExp=3; IntAct=EBI-399246, EBI-741515; CC Q9UBU8; Q15025: TNIP1; NbExp=4; IntAct=EBI-399246, EBI-357849; CC Q9UBU8; P13805: TNNT1; NbExp=3; IntAct=EBI-399246, EBI-726527; CC Q9UBU8; Q8WV44: TRIM41; NbExp=3; IntAct=EBI-399246, EBI-725997; CC Q9UBU8; Q96DT7: ZBTB10; NbExp=3; IntAct=EBI-399246, EBI-10235384; CC Q9UBU8; Q96C00: ZBTB9; NbExp=4; IntAct=EBI-399246, EBI-395708; CC Q9UBU8; P0DTC9: N; Xeno; NbExp=4; IntAct=EBI-399246, EBI-25475856; CC Q9UBU8-2; Q99856: ARID3A; NbExp=3; IntAct=EBI-10288852, EBI-5458244; CC Q9UBU8-2; Q96B67: ARRDC3; NbExp=3; IntAct=EBI-10288852, EBI-2875665; CC Q9UBU8-2; Q5H9J7: BEX5; NbExp=3; IntAct=EBI-10288852, EBI-10243741; CC Q9UBU8-2; Q13554: CAMK2B; NbExp=3; IntAct=EBI-10288852, EBI-1058722; CC Q9UBU8-2; Q13554-3: CAMK2B; NbExp=3; IntAct=EBI-10288852, EBI-11523526; CC Q9UBU8-2; Q6UX04-2: CWC27; NbExp=3; IntAct=EBI-10288852, EBI-18939574; CC Q9UBU8-2; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-10288852, EBI-742054; CC Q9UBU8-2; Q9NPF5: DMAP1; NbExp=4; IntAct=EBI-10288852, EBI-399105; CC Q9UBU8-2; Q14919: DRAP1; NbExp=3; IntAct=EBI-10288852, EBI-712941; CC Q9UBU8-2; Q8NE31: FAM13C; NbExp=3; IntAct=EBI-10288852, EBI-751248; CC Q9UBU8-2; Q8IX29: FBXO16; NbExp=3; IntAct=EBI-10288852, EBI-12063229; CC Q9UBU8-2; P51116: FXR2; NbExp=3; IntAct=EBI-10288852, EBI-740459; CC Q9UBU8-2; Q96IK5: GMCL1; NbExp=3; IntAct=EBI-10288852, EBI-2548508; CC Q9UBU8-2; Q08379: GOLGA2; NbExp=3; IntAct=EBI-10288852, EBI-618309; CC Q9UBU8-2; Q9NYA3: GOLGA6A; NbExp=3; IntAct=EBI-10288852, EBI-11163335; CC Q9UBU8-2; O15499: GSC2; NbExp=3; IntAct=EBI-10288852, EBI-19954058; CC Q9UBU8-2; Q6NT76: HMBOX1; NbExp=3; IntAct=EBI-10288852, EBI-2549423; CC Q9UBU8-2; Q9NP66: HMG20A; NbExp=3; IntAct=EBI-10288852, EBI-740641; CC Q9UBU8-2; P52292: KPNA2; NbExp=3; IntAct=EBI-10288852, EBI-349938; CC Q9UBU8-2; Q96JM7-2: L3MBTL3; NbExp=3; IntAct=EBI-10288852, EBI-11985629; CC Q9UBU8-2; P50458: LHX2; NbExp=3; IntAct=EBI-10288852, EBI-12179869; CC Q9UBU8-2; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-10288852, EBI-741037; CC Q9UBU8-2; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-10288852, EBI-16439278; CC Q9UBU8-2; O00566: MPHOSPH10; NbExp=3; IntAct=EBI-10288852, EBI-5235884; CC Q9UBU8-2; Q9Y605: MRFAP1; NbExp=15; IntAct=EBI-10288852, EBI-995714; CC Q9UBU8-2; Q96HT8: MRFAP1L1; NbExp=27; IntAct=EBI-10288852, EBI-748896; CC Q9UBU8-2; Q9NV56: MRGBP; NbExp=18; IntAct=EBI-10288852, EBI-399076; CC Q9UBU8-2; P52815: MRPL12; NbExp=3; IntAct=EBI-10288852, EBI-358272; CC Q9UBU8-2; Q15742: NAB2; NbExp=3; IntAct=EBI-10288852, EBI-8641936; CC Q9UBU8-2; Q8N987: NECAB1; NbExp=3; IntAct=EBI-10288852, EBI-11956853; CC Q9UBU8-2; Q969G9: NKD1; NbExp=3; IntAct=EBI-10288852, EBI-1538217; CC Q9UBU8-2; Q86YC2: PALB2; NbExp=3; IntAct=EBI-10288852, EBI-1222653; CC Q9UBU8-2; Q96AQ6: PBXIP1; NbExp=3; IntAct=EBI-10288852, EBI-740845; CC Q9UBU8-2; Q96QT6: PHF12; NbExp=6; IntAct=EBI-10288852, EBI-2803760; CC Q9UBU8-2; Q96QT6-2: PHF12; NbExp=3; IntAct=EBI-10288852, EBI-10293106; CC Q9UBU8-2; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-10288852, EBI-14066006; CC Q9UBU8-2; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-10288852, EBI-79165; CC Q9UBU8-2; Q9HB20: PLEKHA3; NbExp=3; IntAct=EBI-10288852, EBI-11079894; CC Q9UBU8-2; O95199: RCBTB2; NbExp=3; IntAct=EBI-10288852, EBI-742404; CC Q9UBU8-2; Q17R54: SYN3; NbExp=3; IntAct=EBI-10288852, EBI-12820047; CC Q9UBU8-2; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-10288852, EBI-11139477; CC Q9UBU8-2; Q12800: TFCP2; NbExp=3; IntAct=EBI-10288852, EBI-717422; CC Q9UBU8-2; Q08117-2: TLE5; NbExp=3; IntAct=EBI-10288852, EBI-11741437; CC Q9UBU8-2; P45379-11: TNNT2; NbExp=3; IntAct=EBI-10288852, EBI-17559309; CC Q9UBU8-2; Q12933: TRAF2; NbExp=3; IntAct=EBI-10288852, EBI-355744; CC Q9UBU8-2; Q8WV44: TRIM41; NbExp=5; IntAct=EBI-10288852, EBI-725997; CC Q9UBU8-2; Q9NZI7: UBP1; NbExp=3; IntAct=EBI-10288852, EBI-2795133; CC Q9UBU8-2; O75436: VPS26A; NbExp=3; IntAct=EBI-10288852, EBI-1043891; CC Q9UBU8-2; Q9Y2W2: WBP11; NbExp=3; IntAct=EBI-10288852, EBI-714455; CC Q9UBU8-2; Q9HCK0: ZBTB26; NbExp=3; IntAct=EBI-10288852, EBI-3918996; CC Q9UBU8-2; O43298: ZBTB43; NbExp=3; IntAct=EBI-10288852, EBI-740718; CC Q9UBU8-2; Q8NAP8: ZBTB8B; NbExp=3; IntAct=EBI-10288852, EBI-17494306; CC Q9UBU8-2; Q96C00: ZBTB9; NbExp=3; IntAct=EBI-10288852, EBI-395708; CC Q9UBU8-2; Q8IWR0-2: ZC3H7A; NbExp=3; IntAct=EBI-10288852, EBI-12242934; CC Q9UBU8-2; Q8N554: ZNF276; NbExp=3; IntAct=EBI-10288852, EBI-750821; CC Q9UBU8-2; Q7Z4V0: ZNF438; NbExp=3; IntAct=EBI-10288852, EBI-11962468; CC Q9UBU8-2; Q6P9G9: ZNF449; NbExp=3; IntAct=EBI-10288852, EBI-10215956; CC Q9UBU8-2; Q5SPL2: Phf12; Xeno; NbExp=2; IntAct=EBI-10288852, EBI-15963335; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q9UBU8-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9UBU8-2; Sequence=VSP_012889; CC Name=3; CC IsoId=Q9UBU8-3; Sequence=VSP_046016; CC -!- SEQUENCE CAUTION: CC Sequence=AAG17253.1; Type=Frameshift; 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; AF100615; AAD29872.1; -; mRNA. DR EMBL; AF167173; AAF80854.1; -; mRNA. DR EMBL; AF218011; AAG17253.1; ALT_FRAME; mRNA. DR EMBL; AY148481; AAN65338.1; -; mRNA. DR EMBL; AF070664; AAD20970.1; -; mRNA. DR EMBL; AF161546; AAF29033.1; -; mRNA. DR EMBL; AF109188; AAQ13497.1; -; mRNA. DR EMBL; AK296650; BAG59248.1; -; mRNA. DR EMBL; AK300789; BAH13347.1; -; mRNA. DR EMBL; AL137697; CAB70879.2; -; mRNA. DR EMBL; AC011944; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC022748; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC103975; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471136; EAW99145.1; -; Genomic_DNA. DR EMBL; CH471136; EAW99144.1; -; Genomic_DNA. DR EMBL; CH471136; EAW99146.1; -; Genomic_DNA. DR EMBL; CH471136; EAW99147.1; -; Genomic_DNA. DR EMBL; BC022845; AAH22845.1; -; mRNA. DR EMBL; BC002936; AAH02936.1; -; mRNA. DR EMBL; BC067826; AAH67826.1; -; mRNA. DR EMBL; CX165647; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AF131847; AAD20058.1; -; mRNA. DR CCDS; CCDS10307.1; -. [Q9UBU8-1] DR CCDS; CCDS32304.1; -. [Q9UBU8-2] DR CCDS; CCDS58393.1; -. [Q9UBU8-3] DR PIR; T46285; T46285. DR RefSeq; NP_001252532.1; NM_001265603.1. [Q9UBU8-3] DR RefSeq; NP_001252533.1; NM_001265604.1. [Q9UBU8-3] DR RefSeq; NP_001252534.1; NM_001265605.1. [Q9UBU8-3] DR RefSeq; NP_006782.1; NM_006791.3. [Q9UBU8-2] DR RefSeq; NP_996670.1; NM_206839.2. [Q9UBU8-1] DR PDB; 2AQL; X-ray; 2.30 A; A/B=190-362. DR PDB; 2EFI; NMR; -; A=1-132. DR PDB; 2F5J; X-ray; 2.20 A; A/B=190-360. DR PDB; 2F5K; X-ray; 2.20 A; A/B/C/D/E/F=1-129. DR PDB; 2LKM; NMR; -; B=194-362. DR PDB; 2N1D; NMR; -; B=194-362. DR PDB; 6AGO; X-ray; 3.10 A; C/D=190-361. DR PDB; 6INE; X-ray; 2.60 A; B=190-362. DR PDB; 7S4A; X-ray; 2.69 A; A/C=191-362. DR PDBsum; 2AQL; -. DR PDBsum; 2EFI; -. DR PDBsum; 2F5J; -. DR PDBsum; 2F5K; -. DR PDBsum; 2LKM; -. DR PDBsum; 2N1D; -. DR PDBsum; 6AGO; -. DR PDBsum; 6INE; -. DR PDBsum; 7S4A; -. DR AlphaFoldDB; Q9UBU8; -. DR BMRB; Q9UBU8; -. DR SMR; Q9UBU8; -. DR BioGRID; 116134; 214. DR ComplexPortal; CPX-978; NuA4 histone acetyltransferase complex. DR CORUM; Q9UBU8; -. DR DIP; DIP-29017N; -. DR IntAct; Q9UBU8; 130. DR MINT; Q9UBU8; -. DR STRING; 9606.ENSP00000331310; -. DR ChEMBL; CHEMBL4630863; -. DR iPTMnet; Q9UBU8; -. DR MetOSite; Q9UBU8; -. DR PhosphoSitePlus; Q9UBU8; -. DR SwissPalm; Q9UBU8; -. DR BioMuta; MORF4L1; -. DR DMDM; 59803121; -. DR EPD; Q9UBU8; -. DR jPOST; Q9UBU8; -. DR MassIVE; Q9UBU8; -. DR MaxQB; Q9UBU8; -. DR PaxDb; Q9UBU8; -. DR PeptideAtlas; Q9UBU8; -. DR ProteomicsDB; 6799; -. DR ProteomicsDB; 84073; -. [Q9UBU8-1] DR ProteomicsDB; 84074; -. [Q9UBU8-2] DR Antibodypedia; 27748; 397 antibodies from 38 providers. DR DNASU; 10933; -. DR Ensembl; ENST00000331268.9; ENSP00000331310.5; ENSG00000185787.15. [Q9UBU8-1] DR Ensembl; ENST00000426013.7; ENSP00000408880.2; ENSG00000185787.15. [Q9UBU8-2] DR Ensembl; ENST00000558502.5; ENSP00000452808.1; ENSG00000185787.15. [Q9UBU8-3] DR Ensembl; ENST00000559345.5; ENSP00000452717.1; ENSG00000185787.15. [Q9UBU8-3] DR GeneID; 10933; -. DR KEGG; hsa:10933; -. DR MANE-Select; ENST00000426013.7; ENSP00000408880.2; NM_006791.4; NP_006782.1. [Q9UBU8-2] DR UCSC; uc002bel.5; human. [Q9UBU8-1] DR AGR; HGNC:16989; -. DR CTD; 10933; -. DR DisGeNET; 10933; -. DR GeneCards; MORF4L1; -. DR HGNC; HGNC:16989; MORF4L1. DR HPA; ENSG00000185787; Low tissue specificity. DR MIM; 607303; gene. DR neXtProt; NX_Q9UBU8; -. DR OpenTargets; ENSG00000185787; -. DR PharmGKB; PA134895182; -. DR VEuPathDB; HostDB:ENSG00000185787; -. DR eggNOG; KOG3001; Eukaryota. DR GeneTree; ENSGT00950000182965; -. DR InParanoid; Q9UBU8; -. DR OMA; GLQTYFD; -. DR OrthoDB; 2878816at2759; -. DR PhylomeDB; Q9UBU8; -. DR TreeFam; TF323400; -. DR PathwayCommons; Q9UBU8; -. DR Reactome; R-HSA-3214847; HATs acetylate histones. DR SignaLink; Q9UBU8; -. DR SIGNOR; Q9UBU8; -. DR BioGRID-ORCS; 10933; 36 hits in 1168 CRISPR screens. DR ChiTaRS; MORF4L1; human. DR EvolutionaryTrace; Q9UBU8; -. DR GeneWiki; MORF4L1; -. DR GenomeRNAi; 10933; -. DR Pharos; Q9UBU8; Tbio. DR PRO; PR:Q9UBU8; -. DR Proteomes; UP000005640; Chromosome 15. DR RNAct; Q9UBU8; protein. DR Bgee; ENSG00000185787; Expressed in lateral nuclear group of thalamus and 209 other tissues. DR ExpressionAtlas; Q9UBU8; baseline and differential. DR Genevisible; Q9UBU8; HS. DR GO; GO:0000123; C:histone acetyltransferase complex; IBA:GO_Central. DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:UniProtKB. DR GO; GO:0016607; C:nuclear speck; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0000786; C:nucleosome; IDA:ComplexPortal. DR GO; GO:0016580; C:Sin3 complex; IDA:UniProtKB. DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl. DR GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB. DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW. DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IDA:UniProtKB. DR GO; GO:0048144; P:fibroblast proliferation; IEA:Ensembl. DR GO; GO:0016573; P:histone acetylation; IBA:GO_Central. DR GO; GO:0016575; P:histone deacetylation; IDA:UniProtKB. DR GO; GO:0043968; P:histone H2A acetylation; IDA:UniProtKB. DR GO; GO:0043967; P:histone H4 acetylation; IDA:UniProtKB. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; NAS:ComplexPortal. DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; IDA:ComplexPortal. DR GO; GO:0042981; P:regulation of apoptotic process; NAS:ComplexPortal. DR GO; GO:0051726; P:regulation of cell cycle; IMP:ComplexPortal. DR GO; GO:2000779; P:regulation of double-strand break repair; NAS:ComplexPortal. DR CDD; cd18983; CBD_MSL3_like; 1. DR Gene3D; 2.30.30.140; -; 1. DR Gene3D; 1.10.274.30; MRG domain; 1. DR IDEAL; IID00330; -. DR InterPro; IPR016197; Chromo-like_dom_sf. DR InterPro; IPR008676; MRG. DR InterPro; IPR038217; MRG_C_sf. DR InterPro; IPR026541; MRG_dom. DR InterPro; IPR025995; Tudor-knot. DR PANTHER; PTHR10880; MORTALITY FACTOR 4-LIKE PROTEIN; 1. DR PANTHER; PTHR10880:SF29; MORTALITY FACTOR 4-LIKE PROTEIN 1; 1. DR Pfam; PF05712; MRG; 1. DR Pfam; PF11717; Tudor-knot; 1. DR PIRSF; PIRSF038133; HAT_Nua4_EAF3/MRG15; 1. DR SUPFAM; SSF54160; Chromo domain-like; 1. DR PROSITE; PS51640; MRG; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Chromatin regulator; KW Direct protein sequencing; DNA damage; DNA recombination; DNA repair; KW Growth regulation; Nucleus; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1..362 FT /note="Mortality factor 4-like protein 1" FT /id="PRO_0000088764" FT DOMAIN 12..51 FT /note="Tudor-knot" FT /evidence="ECO:0000255" FT DOMAIN 191..362 FT /note="MRG" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00972" FT REGION 26..62 FT /note="Interaction with KAT8" FT /evidence="ECO:0000269|PubMed:12397079" FT REGION 113..182 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 133..266 FT /note="Sufficient for interaction with SIN3A" FT /evidence="ECO:0000269|PubMed:12391155" FT REGION 164..230 FT /note="Interaction with RB1-1" FT REGION 188..342 FT /note="Sufficient for interaction with PHF12" FT /evidence="ECO:0000269|PubMed:12391155" FT REGION 323..344 FT /note="Interaction with RB1-2" FT MOTIF 135..146 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255" FT COMPBIAS 156..170 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 143 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT VAR_SEQ 1..127 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_046016" FT VAR_SEQ 52..91 FT /note="KSAVRPRRSEKSLKTHEDIVALFPVPEGAPSVHHPLLTSS -> N (in FT isoform 2)" FT /evidence="ECO:0000303|PubMed:11042152, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005, FT ECO:0000303|PubMed:9891081, ECO:0000303|Ref.2, FT ECO:0000303|Ref.6" FT /id="VSP_012889" FT MUTAGEN 208 FT /note="V->E: Abolishes binding to MRFAP1." FT /evidence="ECO:0000269|PubMed:16407074" FT MUTAGEN 234 FT /note="E->R: No effect on MRFAP1 binding." FT /evidence="ECO:0000269|PubMed:16407074" FT MUTAGEN 251 FT /note="Y->A: No effect on MRFAP1 binding." FT /evidence="ECO:0000269|PubMed:16407074" FT MUTAGEN 254 FT /note="N->C: Reduces binding to MRFAP1." FT /evidence="ECO:0000269|PubMed:16407074" FT CONFLICT 224 FT /note="P -> R (in Ref. 11; AAH67826)" FT /evidence="ECO:0000305" FT CONFLICT 261 FT /note="K -> KK (in Ref. 6; CAB70879)" FT /evidence="ECO:0000305" FT STRAND 16..36 FT /evidence="ECO:0007829|PDB:2F5K" FT STRAND 39..46 FT /evidence="ECO:0007829|PDB:2F5K" FT STRAND 47..49 FT /evidence="ECO:0007829|PDB:2EFI" FT STRAND 94..97 FT /evidence="ECO:0007829|PDB:2F5K" FT HELIX 98..100 FT /evidence="ECO:0007829|PDB:2F5K" FT STRAND 101..105 FT /evidence="ECO:0007829|PDB:2F5K" FT HELIX 106..125 FT /evidence="ECO:0007829|PDB:2F5K" FT HELIX 201..203 FT /evidence="ECO:0007829|PDB:2F5J" FT HELIX 204..215 FT /evidence="ECO:0007829|PDB:2F5J" FT STRAND 219..221 FT /evidence="ECO:0007829|PDB:2F5J" FT STRAND 226..228 FT /evidence="ECO:0007829|PDB:2F5J" FT HELIX 229..241 FT /evidence="ECO:0007829|PDB:2F5J" FT STRAND 242..245 FT /evidence="ECO:0007829|PDB:6AGO" FT STRAND 247..249 FT /evidence="ECO:0007829|PDB:6AGO" FT HELIX 252..271 FT /evidence="ECO:0007829|PDB:2F5J" FT HELIX 275..277 FT /evidence="ECO:0007829|PDB:2F5J" FT HELIX 278..287 FT /evidence="ECO:0007829|PDB:2F5J" FT STRAND 289..291 FT /evidence="ECO:0007829|PDB:7S4A" FT HELIX 293..296 FT /evidence="ECO:0007829|PDB:2F5J" FT HELIX 299..313 FT /evidence="ECO:0007829|PDB:2F5J" FT HELIX 320..339 FT /evidence="ECO:0007829|PDB:2F5J" FT HELIX 341..344 FT /evidence="ECO:0007829|PDB:2F5J" FT HELIX 347..349 FT /evidence="ECO:0007829|PDB:2F5J" FT STRAND 350..352 FT /evidence="ECO:0007829|PDB:2F5J" FT HELIX 355..358 FT /evidence="ECO:0007829|PDB:2F5J" FT TURN 359..361 FT /evidence="ECO:0007829|PDB:2LKM" SQ SEQUENCE 362 AA; 41474 MW; 96B76BCA801F1187 CRC64; MAPKQDPKPK FQEGERVLCF HGPLLYEAKC VKVAIKDKQV KYFIHYSGWN KKSAVRPRRS EKSLKTHEDI VALFPVPEGA PSVHHPLLTS SWDEWVPESR VLKYVDTNLQ KQRELQKANQ EQYAEGKMRG AAPGKKTSGL QQKNVEVKTK KNKQKTPGNG DGGSTSETPQ PPRKKRARVD PTVENEETFM NRVEVKVKIP EELKPWLVDD WDLITRQKQL FYLPAKKNVD SILEDYANYK KSRGNTDNKE YAVNEVVAGI KEYFNVMLGT QLLYKFERPQ YAEILADHPD APMSQVYGAP HLLRLFVRIG AMLAYTPLDE KSLALLLNYL HDFLKYLAKN SATLFSASDY EVAPPEYHRK AV //