MO4L1_MOUSE
ID MO4L1_MOUSE Reviewed; 362 AA.
AC P60762; Q8BNY9; Q99MQ0;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Mortality factor 4-like protein 1;
DE AltName: Full=MORF-related gene 15 protein;
DE AltName: Full=Testis-expressed gene 189 protein;
DE AltName: Full=Transcription factor-like protein MRG15;
GN Name=Morf4l1; Synonyms=Mrg15, Tex189;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RX PubMed=11290425; DOI=10.1016/s0378-1119(01)00372-9;
RA Bertram M.J., Pereira-Smith O.M.;
RT "Conservation of the MORF4 related gene family: identification of a new
RT chromo domain subfamily and novel protein motif.";
RL Gene 266:111-121(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and FVB/N;
RC TISSUE=Mammary tumor, Retina, and Salivary gland;
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 [4]
RP IDENTIFICATION IN COMPLEX WITH MRFAP1 AND RB1.
RX PubMed=15367658; DOI=10.1128/mcb.24.19.8366-8373.2004;
RA Tominaga K., Magee D.M., Matzuk M.M., Pereira-Smith O.M.;
RT "PAM14, a novel MRG- and Rb-associated protein, is not required for
RT development and T-cell function in mice.";
RL Mol. Cell. Biol. 24:8366-8373(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 histones H4 and H2A. This modification
CC may both alter nucleosome - DNA interactions and promote interaction of
CC the 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 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 (By similarity).
CC {ECO:0000250}.
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 MORF4L1 may also participate in the formation of NuA4 related complexes
CC which lack the KAT5/TIP60 catalytic subunit, but which include the
CC SWI/SNF related protein SRCAP. Component of the mSin3A histone
CC deacetylase complex, which includes SIN3A, HDAC2, ARID4B, MORF4L1,
CC RBBP4/RbAp48, and RBBP7/RbAp46. Interacts with RB1 and KAT8. May also
CC interact with PHF12 and one or more as yet undefined members of the TLE
CC (transducin-like enhancer of split) family of transcriptional
CC repressors. Interacts with the N-terminus of MRFAP1 (By similarity).
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 (By similarity). Forms a complex with MSL1 and
CC NUPR1 (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC P60762; Q80Y84: Kdm5b; NbExp=4; IntAct=EBI-2943018, EBI-1249551;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00972}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Mrg15-b;
CC IsoId=P60762-1; Sequence=Displayed;
CC Name=2; Synonyms=Mrg15-a;
CC IsoId=P60762-2; Sequence=VSP_012890;
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DR EMBL; AF319620; AAK07406.1; -; mRNA.
DR EMBL; AF319621; AAK07407.1; -; mRNA.
DR EMBL; AK079115; BAC37546.1; -; mRNA.
DR EMBL; AK016414; BAB30219.1; -; mRNA.
DR EMBL; BC003894; AAH03894.1; -; mRNA.
DR EMBL; BC017619; AAH17619.1; -; mRNA.
DR EMBL; BC083118; AAH83118.1; -; mRNA.
DR EMBL; BC085103; AAH85103.1; -; mRNA.
DR CCDS; CCDS23400.1; -. [P60762-1]
DR CCDS; CCDS52885.1; -. [P60762-2]
DR RefSeq; NP_001034236.1; NM_001039147.2. [P60762-1]
DR RefSeq; NP_077751.1; NM_024431.3. [P60762-2]
DR AlphaFoldDB; P60762; -.
DR BMRB; P60762; -.
DR SMR; P60762; -.
DR BioGRID; 204126; 18.
DR ComplexPortal; CPX-990; NuA4 histone acetyltransferase complex.
DR IntAct; P60762; 4.
DR MINT; P60762; -.
DR STRING; 10090.ENSMUSP00000082346; -.
DR iPTMnet; P60762; -.
DR PhosphoSitePlus; P60762; -.
DR EPD; P60762; -.
DR MaxQB; P60762; -.
DR PaxDb; P60762; -.
DR PeptideAtlas; P60762; -.
DR PRIDE; P60762; -.
DR ProteomicsDB; 252584; -. [P60762-1]
DR ProteomicsDB; 252585; -. [P60762-2]
DR DNASU; 21761; -.
DR Ensembl; ENSMUST00000085248; ENSMUSP00000082346; ENSMUSG00000062270. [P60762-1]
DR Ensembl; ENSMUST00000169860; ENSMUSP00000132020; ENSMUSG00000062270. [P60762-2]
DR GeneID; 21761; -.
DR KEGG; mmu:21761; -.
DR UCSC; uc009qzw.2; mouse. [P60762-1]
DR CTD; 10933; -.
DR MGI; MGI:1096551; Morf4l1.
DR VEuPathDB; HostDB:ENSMUSG00000062270; -.
DR eggNOG; KOG3001; Eukaryota.
DR GeneTree; ENSGT00950000182965; -.
DR InParanoid; P60762; -.
DR OMA; GLQTYFD; -.
DR OrthoDB; 1624495at2759; -.
DR PhylomeDB; P60762; -.
DR TreeFam; TF323400; -.
DR BioGRID-ORCS; 21761; 4 hits in 112 CRISPR screens.
DR ChiTaRS; Morf4l1; mouse.
DR PRO; PR:P60762; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P60762; protein.
DR Bgee; ENSMUSG00000062270; Expressed in embryonic post-anal tail and 68 other tissues.
DR ExpressionAtlas; P60762; baseline and differential.
DR Genevisible; P60762; MM.
DR GO; GO:0000123; C:histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; ISS:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0000786; C:nucleosome; ISO:MGI.
DR GO; GO:0016580; C:Sin3 complex; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR GO; GO:0006338; P:chromatin remodeling; TAS:MGI.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0048144; P:fibroblast proliferation; IMP:MGI.
DR GO; GO:0016573; P:histone acetylation; IBA:GO_Central.
DR GO; GO:0016575; P:histone deacetylation; ISS:UniProtKB.
DR GO; GO:0043968; P:histone H2A acetylation; ISS:UniProtKB.
DR GO; GO:0043967; P:histone H4 acetylation; ISS:UniProtKB.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; ISO:MGI.
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; ISO:MGI.
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; 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 Acetylation; Alternative splicing; Chromatin regulator; DNA damage;
KW DNA recombination; DNA repair; Growth regulation; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..362
FT /note="Mortality factor 4-like protein 1"
FT /id="PRO_0000088765"
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:0000250"
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:0000250"
FT REGION 164..230
FT /note="Interaction with RB1-1"
FT /evidence="ECO:0000250"
FT REGION 188..342
FT /note="Sufficient for interaction with PHF12"
FT /evidence="ECO:0000250"
FT REGION 323..344
FT /note="Interaction with RB1-2"
FT /evidence="ECO:0000250"
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:0000250|UniProtKB:Q9UBU8"
FT VAR_SEQ 52..91
FT /note="KSAVRPRRSEKSLKTREDIVALFPVPEGAPSVHHPLLTSS -> N (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:11290425,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_012890"
SQ SEQUENCE 362 AA; 41493 MW; C044A3DC6A37BFE2 CRC64;
MAPKQDPKPK FQEGERVLCF HGPLLYEAKC VKVAIKDKQV KYFIHYSGWN KKSAVRPRRS
EKSLKTREDI 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
