MO4L2_HUMAN
ID MO4L2_HUMAN Reviewed; 288 AA.
AC Q15014; B3KP92; D3DXA5; Q567V0; Q8J026;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Mortality factor 4-like protein 2;
DE AltName: Full=MORF-related gene X protein;
DE AltName: Full=Protein MSL3-2;
DE AltName: Full=Transcription factor-like protein MRGX;
GN Name=MORF4L2; Synonyms=KIAA0026, MRGX;
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].
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].
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].
RC TISSUE=Bone marrow;
RX PubMed=7584026; DOI=10.1093/dnares/1.1.27;
RA Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S.,
RA Nagase T., Seki N., Ishikawa K., Tabata S.;
RT "Prediction of the coding sequences of unidentified human genes. I. The
RT coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of
RT randomly sampled cDNA clones from human immature myeloid cell line KG-1.";
RL DNA Res. 1:27-35(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas, and Placenta;
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-16.
RA Myokai F., Oyama M.;
RT "Mortality factor related gene X 102 5'.";
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP PROTEIN SEQUENCE OF 12-22; 82-99; 105-116; 154-166; 176-187; 188-201;
RP 235-247 AND 266-277, 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 [10]
RP INTERACTION WITH 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 [11]
RP INTERACTION WITH MRFAP1 AND RB1, AND MUTAGENESIS OF 132-TRP--ASP-136 AND
RP LEU-263.
RX PubMed=14506250; DOI=10.1074/jbc.m309192200;
RA Tominaga K., Leung J.K., Rookard P., Echigo J., Smith J.R.,
RA Pereira-Smith O.M.;
RT "MRGX is a novel transcriptional regulator that exhibits activation or
RT repression of the B-myb promoter in a cell type-dependent manner.";
RL J. Biol. Chem. 278:49618-49624(2003).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71, 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 [13]
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: Component of the NuA4 histone acetyltransferase complex which
CC is involved in transcriptional activation of select genes principally
CC by acetylation of nucleosomal histone H4 and H2A. This modification may
CC both alter nucleosome - DNA interactions and promote interaction of the
CC modified histones with other proteins which positively regulate
CC transcription. This complex may be required for the activation of
CC transcriptional programs associated with oncogene and proto-oncogene
CC mediated growth induction, tumor suppressor mediated growth arrest and
CC replicative senescence, apoptosis, and DNA repair. The NuA4 complex
CC ATPase and helicase activities seem to be, at least in part,
CC contributed by the association of RUVBL1 and RUVBL2 with EP400. NuA4
CC may also play a direct role in DNA repair when directly recruited to
CC sites of DNA damage. Also a component of the MSIN3A complex which acts
CC to repress transcription by deacetylation of nucleosomal histones.
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 and VPS72/YL1. The NuA4 complex interacts with MYC and the
CC adenovirus E1A protein. MORF4L1 may also participate in the formation
CC of NuA4 related complexes which lack the KAT5/TIP60 catalytic subunit,
CC but which include the SWI/SNF related protein SRCAP. Component of the
CC MSIN3A histone deacetylase complex, which includes SIN3A, HDAC2,
CC ARID4B, MORF4L1, RBBP4/RbAp48, and RBBP7/RbAp46. Interacts with MRFAP1
CC and RB1. May also interact with one or more as yet undefined members of
CC the TLE (transducin-like enhancer of split) family of transcriptional
CC repressors. {ECO:0000269|PubMed:12391155, ECO:0000269|PubMed:12963728,
CC ECO:0000269|PubMed:14506250}.
CC -!- INTERACTION:
CC Q15014; Q9Y2J4: AMOTL2; NbExp=3; IntAct=EBI-399257, EBI-746752;
CC Q15014; Q99856: ARID3A; NbExp=3; IntAct=EBI-399257, EBI-5458244;
CC Q15014; Q9H165-2: BCL11A; NbExp=3; IntAct=EBI-399257, EBI-10183342;
CC Q15014; Q8N7W2-2: BEND7; NbExp=3; IntAct=EBI-399257, EBI-10181188;
CC Q15014; Q5H9J7: BEX5; NbExp=3; IntAct=EBI-399257, EBI-10243741;
CC Q15014; Q13554-3: CAMK2B; NbExp=3; IntAct=EBI-399257, EBI-11523526;
CC Q15014; Q01850: CDR2; NbExp=6; IntAct=EBI-399257, EBI-1181367;
CC Q15014; Q53EZ4: CEP55; NbExp=6; IntAct=EBI-399257, EBI-747776;
CC Q15014; Q96D03: DDIT4L; NbExp=6; IntAct=EBI-399257, EBI-742054;
CC Q15014; Q9NRI5-2: DISC1; NbExp=3; IntAct=EBI-399257, EBI-11988027;
CC Q15014; O60447: EVI5; NbExp=3; IntAct=EBI-399257, EBI-852291;
CC Q15014; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-399257, EBI-10175124;
CC Q15014; Q8IX29: FBXO16; NbExp=3; IntAct=EBI-399257, EBI-12063229;
CC Q15014; Q08379: GOLGA2; NbExp=3; IntAct=EBI-399257, EBI-618309;
CC Q15014; Q86WP2: GPBP1; NbExp=3; IntAct=EBI-399257, EBI-2349758;
CC Q15014; Q96HH9: GRAMD2B; NbExp=3; IntAct=EBI-399257, EBI-2832937;
CC Q15014; Q6NT76: HMBOX1; NbExp=3; IntAct=EBI-399257, EBI-2549423;
CC Q15014; P42858: HTT; NbExp=12; IntAct=EBI-399257, EBI-466029;
CC Q15014; Q13422: IKZF1; NbExp=3; IntAct=EBI-399257, EBI-745305;
CC Q15014; Q719H9: KCTD1; NbExp=3; IntAct=EBI-399257, EBI-9027502;
CC Q15014; Q8N4I8: KLHL3; NbExp=3; IntAct=EBI-399257, EBI-10230467;
CC Q15014; Q96JM7: L3MBTL3; NbExp=3; IntAct=EBI-399257, EBI-2686809;
CC Q15014; Q96JM7-2: L3MBTL3; NbExp=3; IntAct=EBI-399257, EBI-11985629;
CC Q15014; Q9P127: LUZP4; NbExp=3; IntAct=EBI-399257, EBI-10198848;
CC Q15014; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-399257, EBI-741037;
CC Q15014; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-399257, EBI-16439278;
CC Q15014; Q9Y605: MRFAP1; NbExp=16; IntAct=EBI-399257, EBI-995714;
CC Q15014; Q96HT8: MRFAP1L1; NbExp=11; IntAct=EBI-399257, EBI-748896;
CC Q15014; Q9NV56: MRGBP; NbExp=13; IntAct=EBI-399257, EBI-399076;
CC Q15014; P52815: MRPL12; NbExp=3; IntAct=EBI-399257, EBI-358272;
CC Q15014; Q15742: NAB2; NbExp=3; IntAct=EBI-399257, EBI-8641936;
CC Q15014; Q8IXK0: PHC2; NbExp=3; IntAct=EBI-399257, EBI-713786;
CC Q15014; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-399257, EBI-14066006;
CC Q15014; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-399257, EBI-79165;
CC Q15014; Q9UL42: PNMA2; NbExp=3; IntAct=EBI-399257, EBI-302355;
CC Q15014; P78424: POU6F2; NbExp=3; IntAct=EBI-399257, EBI-12029004;
CC Q15014; Q04864-2: REL; NbExp=3; IntAct=EBI-399257, EBI-10829018;
CC Q15014; Q17R54: SYN3; NbExp=3; IntAct=EBI-399257, EBI-12820047;
CC Q15014; Q9NVV9: THAP1; NbExp=3; IntAct=EBI-399257, EBI-741515;
CC Q15014; Q08117: TLE5; NbExp=3; IntAct=EBI-399257, EBI-717810;
CC Q15014; Q15025: TNIP1; NbExp=4; IntAct=EBI-399257, EBI-357849;
CC Q15014; P45379: TNNT2; NbExp=3; IntAct=EBI-399257, EBI-8485957;
CC Q15014; Q8WV44: TRIM41; NbExp=3; IntAct=EBI-399257, EBI-725997;
CC Q15014; Q15631: TSN; NbExp=3; IntAct=EBI-399257, EBI-1044160;
CC Q15014; Q96DT7: ZBTB10; NbExp=3; IntAct=EBI-399257, EBI-10235384;
CC Q15014; O43829: ZBTB14; NbExp=3; IntAct=EBI-399257, EBI-10176632;
CC Q15014; Q9HCK0: ZBTB26; NbExp=3; IntAct=EBI-399257, EBI-3918996;
CC Q15014; O43298: ZBTB43; NbExp=4; IntAct=EBI-399257, EBI-740718;
CC Q15014; O15156: ZBTB7B; NbExp=3; IntAct=EBI-399257, EBI-740434;
CC Q15014; Q96MX3: ZNF48; NbExp=3; IntAct=EBI-399257, EBI-12006434;
CC Q15014; Q77UV9: KIE-2; Xeno; NbExp=2; IntAct=EBI-399257, EBI-2608731;
CC Q15014; P0DTC9: N; Xeno; NbExp=5; IntAct=EBI-399257, EBI-25475856;
CC -!- SUBCELLULAR LOCATION: Nucleus.
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DR EMBL; AF100620; AAD29873.1; -; mRNA.
DR EMBL; AF167174; AAF80855.1; -; mRNA.
DR EMBL; D14812; BAA03553.1; -; mRNA.
DR EMBL; AK056012; BAG51604.1; -; mRNA.
DR EMBL; AL049610; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471190; EAW54698.1; -; Genomic_DNA.
DR EMBL; CH471190; EAW54699.1; -; Genomic_DNA.
DR EMBL; CH471190; EAW54700.1; -; Genomic_DNA.
DR EMBL; CH471190; EAW54701.1; -; Genomic_DNA.
DR EMBL; BC056899; AAH56899.1; -; mRNA.
DR EMBL; BC093013; AAH93013.1; -; mRNA.
DR EMBL; AB050778; BAC22659.1; -; mRNA.
DR CCDS; CCDS14512.1; -.
DR RefSeq; NP_001135890.1; NM_001142418.1.
DR RefSeq; NP_001135891.1; NM_001142419.1.
DR RefSeq; NP_001135892.1; NM_001142420.1.
DR RefSeq; NP_001135893.1; NM_001142421.1.
DR RefSeq; NP_001135894.1; NM_001142422.1.
DR RefSeq; NP_001135895.1; NM_001142423.1.
DR RefSeq; NP_001135896.1; NM_001142424.1.
DR RefSeq; NP_001135897.1; NM_001142425.1.
DR RefSeq; NP_001135898.1; NM_001142426.1.
DR RefSeq; NP_001135899.1; NM_001142427.1.
DR RefSeq; NP_001135900.1; NM_001142428.1.
DR RefSeq; NP_001135901.1; NM_001142429.1.
DR RefSeq; NP_001135902.1; NM_001142430.1.
DR RefSeq; NP_001135903.1; NM_001142431.1.
DR RefSeq; NP_001135904.1; NM_001142432.1.
DR RefSeq; NP_036418.1; NM_012286.2.
DR AlphaFoldDB; Q15014; -.
DR SMR; Q15014; -.
DR BioGRID; 115001; 161.
DR ComplexPortal; CPX-978; NuA4 histone acetyltransferase complex.
DR CORUM; Q15014; -.
DR IntAct; Q15014; 95.
DR MINT; Q15014; -.
DR STRING; 9606.ENSP00000394417; -.
DR iPTMnet; Q15014; -.
DR MetOSite; Q15014; -.
DR PhosphoSitePlus; Q15014; -.
DR BioMuta; MORF4L2; -.
DR DMDM; 3123049; -.
DR EPD; Q15014; -.
DR jPOST; Q15014; -.
DR MassIVE; Q15014; -.
DR MaxQB; Q15014; -.
DR PaxDb; Q15014; -.
DR PeptideAtlas; Q15014; -.
DR PRIDE; Q15014; -.
DR ProteomicsDB; 60366; -.
DR Antibodypedia; 14953; 168 antibodies from 30 providers.
DR DNASU; 9643; -.
DR Ensembl; ENST00000360458.5; ENSP00000353643.1; ENSG00000123562.18.
DR Ensembl; ENST00000433176.6; ENSP00000415476.2; ENSG00000123562.18.
DR Ensembl; ENST00000441076.7; ENSP00000391969.2; ENSG00000123562.18.
DR Ensembl; ENST00000451301.5; ENSP00000410532.1; ENSG00000123562.18.
DR GeneID; 9643; -.
DR KEGG; hsa:9643; -.
DR MANE-Select; ENST00000441076.7; ENSP00000391969.2; NM_012286.3; NP_036418.1.
DR UCSC; uc004ekx.4; human.
DR CTD; 9643; -.
DR DisGeNET; 9643; -.
DR GeneCards; MORF4L2; -.
DR HGNC; HGNC:16849; MORF4L2.
DR HPA; ENSG00000123562; Low tissue specificity.
DR MIM; 300409; gene.
DR neXtProt; NX_Q15014; -.
DR OpenTargets; ENSG00000123562; -.
DR PharmGKB; PA134925837; -.
DR VEuPathDB; HostDB:ENSG00000123562; -.
DR eggNOG; KOG3001; Eukaryota.
DR GeneTree; ENSGT00950000182965; -.
DR InParanoid; Q15014; -.
DR OMA; RGNMQRS; -.
DR OrthoDB; 1624495at2759; -.
DR PhylomeDB; Q15014; -.
DR TreeFam; TF323400; -.
DR PathwayCommons; Q15014; -.
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR SignaLink; Q15014; -.
DR BioGRID-ORCS; 9643; 21 hits in 717 CRISPR screens.
DR ChiTaRS; MORF4L2; human.
DR GeneWiki; MORF4L2; -.
DR GenomeRNAi; 9643; -.
DR Pharos; Q15014; Tbio.
DR PRO; PR:Q15014; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q15014; protein.
DR Bgee; ENSG00000123562; Expressed in endothelial cell and 214 other tissues.
DR ExpressionAtlas; Q15014; baseline and differential.
DR Genevisible; Q15014; HS.
DR GO; GO:0000123; C:histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:ComplexPortal.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0000786; C:nucleosome; IDA:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0016573; P:histone acetylation; IBA:GO_Central.
DR GO; GO:0016575; P:histone deacetylation; IBA:GO_Central.
DR GO; GO:0043968; P:histone H2A acetylation; IDA:ComplexPortal.
DR GO; GO:0043967; P:histone H4 acetylation; IDA:ComplexPortal.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; IDA:ComplexPortal.
DR GO; GO:0051155; P:positive regulation of striated muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
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 InterPro; IPR008676; MRG.
DR InterPro; IPR038217; MRG_C_sf.
DR InterPro; IPR026541; MRG_dom.
DR InterPro; IPR038012; MRGX.
DR PANTHER; PTHR10880; PTHR10880; 1.
DR PANTHER; PTHR10880:SF25; PTHR10880:SF25; 1.
DR Pfam; PF05712; MRG; 1.
DR PROSITE; PS51640; MRG; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Direct protein sequencing; DNA damage; DNA repair;
KW Growth regulation; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..288
FT /note="Mortality factor 4-like protein 2"
FT /id="PRO_0000088768"
FT DOMAIN 117..288
FT /note="MRG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00972"
FT REGION 1..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MUTAGEN 132..136
FT /note="Missing: Abrogates both transcriptional activation
FT and repression by MORF4L2."
FT /evidence="ECO:0000269|PubMed:14506250"
FT MUTAGEN 263
FT /note="L->A: Abrogates both transcriptional activation and
FT repression by MORF4L2."
FT /evidence="ECO:0000269|PubMed:14506250"
SQ SEQUENCE 288 AA; 32308 MW; C9EFF517C76A565D CRC64;
MSSRKQGSQP RGQQSAEEEN FKKPTRSNMQ RSKMRGASSG KKTAGPQQKN LEPALPGRWG
GRSAENPPSG SVRKTRKNKQ KTPGNGDGGS TSEAPQPPRK KRARADPTVE SEEAFKNRME
VKVKIPEELK PWLVEDWDLV TRQKQLFQLP AKKNVDAILE EYANCKKSQG NVDNKEYAVN
EVVAGIKEYF NVMLGTQLLY KFERPQYAEI LLAHPDAPMS QVYGAPHLLR LFVRIGAMLA
YTPLDEKSLA LLLGYLHDFL KYLAKNSASL FTASDYKVAS AEYHRKAL
