MO4L1_HUMAN
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 03-AUG-2022, entry version 220.
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};
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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 PDBsum; 2AQL; -.
DR PDBsum; 2EFI; -.
DR PDBsum; 2F5J; -.
DR PDBsum; 2F5K; -.
DR PDBsum; 2LKM; -.
DR PDBsum; 2N1D; -.
DR PDBsum; 6AGO; -.
DR PDBsum; 6INE; -.
DR AlphaFoldDB; Q9UBU8; -.
DR BMRB; Q9UBU8; -.
DR SMR; Q9UBU8; -.
DR BioGRID; 116134; 204.
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 PRIDE; Q9UBU8; -.
DR ProteomicsDB; 6799; -.
DR ProteomicsDB; 84073; -. [Q9UBU8-1]
DR ProteomicsDB; 84074; -. [Q9UBU8-2]
DR Antibodypedia; 27748; 398 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 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; 1624495at2759; -.
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; 34 hits in 1089 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:1905168; P:positive regulation of double-strand break repair via homologous recombination; IDA:ComplexPortal.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0042981; P:regulation of apoptotic process; IC:ComplexPortal.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:ComplexPortal.
DR GO; GO:2000779; P:regulation of double-strand break repair; IC:ComplexPortal.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR Gene3D; 1.10.274.30; -; 1.
DR IDEAL; IID00330; -.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR008676; MRG.
DR InterPro; IPR038011; MRG15.
DR InterPro; IPR038217; MRG_C_sf.
DR InterPro; IPR026541; MRG_dom.
DR InterPro; IPR025995; Tudor-knot.
DR PANTHER; PTHR10880; PTHR10880; 1.
DR PANTHER; PTHR10880:SF29; PTHR10880:SF29; 1.
DR Pfam; PF05712; MRG; 1.
DR Pfam; PF11717; Tudor-knot; 1.
DR PIRSF; PIRSF038133; HAT_Nua4_EAF3/MRG15; 1.
DR SUPFAM; SSF54160; SSF54160; 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 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
