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Mortality factor 4-like protein 1 (MORF-related gene 15 protein) (Protein MSL3-1) (Transcription factor-like protein MRG15)

 MO4L1_HUMAN             Reviewed;         362 AA.
Q9UBU8; B4DKN6; B7Z6R1; D3DW88; O95899; Q5QTS1; Q6NVX8; Q86YT7;
Q9HBP6; Q9NSW5;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
15-FEB-2005, sequence version 2.
27-SEP-2017, entry version 183.
RecName: Full=Mortality factor 4-like protein 1;
AltName: Full=MORF-related gene 15 protein;
AltName: Full=Protein MSL3-1;
AltName: Full=Transcription factor-like protein MRG15;
Name=MORF4L1; Synonyms=MRG15;
ORFNames=FWP006, HSPC008, HSPC061, PP368;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=9891081; DOI=10.1128/MCB.19.2.1479;
Bertram M.J., Berube N.G., Hang-Swanson X., Ran Q., Leung J.K.,
Bryce S., Spurgers K., Bick R.J., Baldini A., Ning Y., Clark L.J.,
Parkinson E.K., Barrett J.C., Smith J.R., Pereira-Smith O.M.;
"Identification of a gene that reverses the immortal phenotype of a
subset of cells and is a member of a novel family of transcription
factor-like genes.";
Mol. Cell. Biol. 19:1479-1485(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
D'Esposito M., Cocchia M., Matarazzo M.R., Macmillan S.,
Mazzarella R.;
"Two human homologs of the Drosophila dosage compensation gene msl-3
are located on the X chromosome.";
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15498874; DOI=10.1073/pnas.0404089101;
Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H.,
Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y.,
Shu H., Chen X., Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S.,
Gu J.;
"Large-scale cDNA transfection screening for genes related to cancer
development and progression.";
Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Lung;
Guo S., Tong T., Zhang Z.;
"Cloning and identification of cellular senescence associated genes
from fibroblasts 2BS.";
Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Umbilical cord blood;
PubMed=11042152; DOI=10.1101/gr.140200;
Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
"Cloning and functional analysis of cDNAs with open reading frames for
300 previously undefined genes expressed in CD34+ hematopoietic
stem/progenitor cells.";
Genome Res. 10:1546-1560(2000).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Aorta;
Liu B., Zhao B., Wang X.Y., Xu Y.Y., Liu Y.Q., Song L., Ye J.,
Sheng H., Gao Y., Zhang C.L., Wei Y.J., Zhang J., Song L., Jiang Y.X.,
Zhao Z.W., Ding J.F., Liu L.S., Gao R.L., Wu Q.Y., Qiang B.Q.,
Yuan J.G., Liew C.C., Zhao M.S., Hui R.T.;
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
TISSUE=Colon, and Embryonic stem cell;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Kidney;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16572171; DOI=10.1038/nature04601;
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R.,
Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
Nusbaum C.;
"Analysis of the DNA sequence and duplication history of human
chromosome 15.";
Nature 440:671-675(2006).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
TISSUE=Embryonic stem cell, Skin, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[12]
PROTEIN SEQUENCE OF 17-29; 42-51; 118-127; 156-173; 179-192; 228-240;
244-261 AND 340-359, AND IDENTIFICATION IN NUA4 COMPLEX.
PubMed=12963728; DOI=10.1074/jbc.C300389200;
Cai Y., Jin J., Tomomori-Sato C., Sato S., Sorokina I., Parmely T.J.,
Conaway R.C., Conaway J.W.;
"Identification of new subunits of the multiprotein mammalian
TRRAP/TIP60-containing histone acetyltransferase complex.";
J. Biol. Chem. 278:42733-42736(2003).
[13]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 120-362 (ISOFORMS 1/2).
TISSUE=Brain;
Mei G., Yu W., Gibbs R.A.;
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
[14]
INTERACTION WITH MRFAP1 AND RB1.
PubMed=11500496; DOI=10.1074/jbc.M103435200;
Leung J.K., Berube N., Venable S., Ahmed S., Timchenko N.,
Pereira-Smith O.M.;
"MRG15 activates the B-myb promoter through formation of a nuclear
complex with the retinoblastoma protein and the novel protein PAM14.";
J. Biol. Chem. 276:39171-39178(2001).
[15]
IDENTIFICATION IN COMPLEX WITH RB1 AND MRFAP1, AND INTERACTION WITH
RB1 AND KAT8.
PubMed=12397079; DOI=10.1074/jbc.M203839200;
Pardo P.S., Leung J.K., Lucchesi J.C., Pereira-Smith O.M.;
"MRG15, a novel chromodomain protein, is present in two distinct
multiprotein complexes involved in transcriptional activation.";
J. Biol. Chem. 277:50860-50866(2002).
[16]
INTERACTION WITH PHF12; SIN3A AND TLE FAMILY MEMBERS.
PubMed=12391155; DOI=10.1128/MCB.22.22.7868-7876.2002;
Yochum G.S., Ayer D.E.;
"Role for the mortality factors MORF4, MRGX, and MRG15 in
transcriptional repression via associations with Pf1, mSin3A, and
transducin-like enhancer of Split.";
Mol. Cell. Biol. 22:7868-7876(2002).
[17]
REVIEW ON NUA4 COMPLEX.
PubMed=15196461; DOI=10.1016/j.gde.2004.02.009;
Doyon Y., Cote J.;
"The highly conserved and multifunctional NuA4 HAT complex.";
Curr. Opin. Genet. Dev. 14:147-154(2004).
[18]
FUNCTION, IDENTIFICATION IN NUA4 COMPLEX, AND IDENTIFICATION IN SIN3A
COMPLEX.
PubMed=14966270; DOI=10.1128/MCB.24.5.1884-1896.2004;
Doyon Y., Selleck W., Lane W.S., Tan S., Cote J.;
"Structural and functional conservation of the NuA4 histone
acetyltransferase complex from yeast to humans.";
Mol. Cell. Biol. 24:1884-1896(2004).
[19]
INTERACTION WITH MSL1 AND NUPR1.
PubMed=19650074; DOI=10.1002/jcp.21889;
Gironella M., Malicet C., Cano C., Sandi M.J., Hamidi T., Tauil R.M.,
Baston M., Valaco P., Moreno S., Lopez F., Neira J.L., Dagorn J.C.,
Iovanna J.L.;
"p8/nupr1 regulates DNA-repair activity after double-strand gamma
irradiation-induced DNA damage.";
J. Cell. Physiol. 221:594-602(2009).
[20]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-143, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[21]
FUNCTION, AND INTERACTION WITH BRCA COMPLEX AND PALB2.
PubMed=20332121; DOI=10.1242/jcs.060178;
Hayakawa T., Zhang F., Hayakawa N., Ohtani Y., Shinmyozu K.,
Nakayama J., Andreassen P.R.;
"MRG15 binds directly to PALB2 and stimulates homology-directed repair
of chromosomal breaks.";
J. Cell Sci. 123:1124-1130(2010).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[23]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 190-362, AND INTERACTION WITH
MRFAP1.
PubMed=17008723; DOI=10.1110/ps.062397806;
Zhang P., Zhao J., Wang B., Du J., Lu Y., Chen J., Ding J.;
"The MRG domain of human MRG15 uses a shallow hydrophobic pocket to
interact with the N-terminal region of PAM14.";
Protein Sci. 15:2423-2434(2006).
[24]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 190-362, AND MUTAGENESIS OF
VAL-208; GLU-234; TYR-251 AND ASN-254.
PubMed=16407074; DOI=10.1016/j.str.2005.08.019;
Bowman B.R., Moure C.M., Kirtane B.M., Welschhans R.L., Tominaga K.,
Pereira-Smith O.M., Quiocho F.A.;
"Multipurpose MRG domain involved in cell senescence and proliferation
exhibits structural homology to a DNA-interacting domain.";
Structure 14:151-158(2006).
-!- FUNCTION: Component of the NuA4 histone acetyltransferase (HAT)
complex which is involved in transcriptional activation of select
genes principally by acetylation of nucleosomal histones H4 and
H2A. This modification may both alter nucleosome - DNA
interactions and promote interaction of the modified histones with
other proteins which positively regulate transcription. This
complex may be required for the activation of transcriptional
programs associated with oncogene and proto-oncogene mediated
growth induction, tumor suppressor mediated growth arrest and
replicative senescence, apoptosis, and DNA repair. The NuA4
complex ATPase and helicase activities seem to be, at least in
part, contributed by the association of RUVBL1 and RUVBL2 with
EP400. NuA4 may also play a direct role in DNA repair when
directly recruited to sites of DNA damage. Also component of the
mSin3A complex which acts to repress transcription by
deacetylation of nucleosomal histones. Required for homologous
recombination repair (HRR) and resistance to mitomycin C (MMC).
Involved in the localization of PALB2, BRCA2 and RAD51, but not
BRCA1, to DNA-damage foci. {ECO:0000269|PubMed:14966270,
ECO:0000269|PubMed:20332121}.
-!- SUBUNIT: Component of the NuA4 histone acetyltransferase complex
which contains the catalytic subunit KAT5/TIP60 and the subunits
EP400, TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49,
RUVBL2, ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX,
MRGBP, YEATS4/GAS41, VPS72/YL1 and MEAF6. The NuA4 complex
interacts with MYC and the adenovirus E1A protein. MORF4L1 may
also participate in the formation of NuA4 related complexes which
lack the KAT5/TIP60 catalytic subunit, but which include the
SWI/SNF related protein SRCAP. Component of the mSin3A histone
deacetylase complex, which includes SIN3A, HDAC2, ARID4B, MORF4L1,
RBBP4/RbAp48, and RBBP7/RbAp46. Interacts with RB1 and KAT8. May
also interact with PHF12 and one or more as yet undefined members
of the TLE (transducin-like enhancer of split) family of
transcriptional repressors. Interacts with the N-terminus of
MRFAP1. Found in a complex composed of MORF4L1, MRFAP1 and RB1.
Interacts with the entire BRCA complex, which contains BRCA1,
PALB2, BRCA2 and RAD51. Interacts with PALB2. Forms a complex with
MSL1 and NUPR1. {ECO:0000269|PubMed:11500496,
ECO:0000269|PubMed:12391155, ECO:0000269|PubMed:12397079,
ECO:0000269|PubMed:12963728, ECO:0000269|PubMed:14966270,
ECO:0000269|PubMed:17008723, ECO:0000269|PubMed:19650074,
ECO:0000269|PubMed:20332121}.
-!- INTERACTION:
Q96B67:ARRDC3; NbExp=3; IntAct=EBI-10288852, EBI-2875665;
Q8N7W2-2:BEND7; NbExp=3; IntAct=EBI-399246, EBI-10181188;
Q13554:CAMK2B; NbExp=3; IntAct=EBI-10288852, EBI-1058722;
Q8IYX8-2:CEP57L1; NbExp=3; IntAct=EBI-399246, EBI-10181988;
Q14919:DRAP1; NbExp=4; IntAct=EBI-10288852, EBI-712941;
Q8IZU0:FAM9B; NbExp=3; IntAct=EBI-399246, EBI-10175124;
Q53SE7:FLJ13057; NbExp=3; IntAct=EBI-399246, EBI-10172181;
P51116:FXR2; NbExp=3; IntAct=EBI-399246, EBI-740459;
Q08379:GOLGA2; NbExp=3; IntAct=EBI-399246, EBI-618309;
Q6NT76:HMBOX1; NbExp=3; IntAct=EBI-399246, EBI-2549423;
Q6NT76-2:HMBOX1; NbExp=3; IntAct=EBI-399246, EBI-10212206;
Q13422:IKZF1; NbExp=3; IntAct=EBI-399246, EBI-745305;
Q96JM7:L3MBTL3; NbExp=3; IntAct=EBI-399246, EBI-2686809;
Q9BRK4:LZTS2; NbExp=3; IntAct=EBI-399246, EBI-741037;
P50221:MEOX1; NbExp=3; IntAct=EBI-399246, EBI-2864512;
Q9Y605:MRFAP1; NbExp=13; IntAct=EBI-10288852, EBI-995714;
Q96HT8:MRFAP1L1; NbExp=22; IntAct=EBI-10288852, EBI-748896;
Q9NV56:MRGBP; NbExp=7; IntAct=EBI-10288852, EBI-399076;
Q15742:NAB2; NbExp=3; IntAct=EBI-399246, EBI-8641936;
Q8IVL1:NAV2; NbExp=3; IntAct=EBI-399246, EBI-741200;
Q96AQ6:PBXIP1; NbExp=3; IntAct=EBI-399246, EBI-740845;
Q96QT6-2:PHF12; NbExp=3; IntAct=EBI-10288852, EBI-10293106;
Q9H0H5:RACGAP1; NbExp=3; IntAct=EBI-399246, EBI-717233;
Q04864:REL; NbExp=3; IntAct=EBI-399246, EBI-307352;
Q12800:TFCP2; NbExp=3; IntAct=EBI-399246, EBI-717422;
Q9NVV9:THAP1; NbExp=3; IntAct=EBI-399246, EBI-741515;
Q15025:TNIP1; NbExp=3; IntAct=EBI-399246, EBI-357849;
P13805:TNNT1; NbExp=3; IntAct=EBI-399246, EBI-726527;
Q8WV44:TRIM41; NbExp=3; IntAct=EBI-399246, EBI-725997;
Q96DT7:ZBTB10; NbExp=3; IntAct=EBI-399246, EBI-10235384;
Q96C00:ZBTB9; NbExp=3; IntAct=EBI-399246, EBI-395708;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q9UBU8-1; Sequence=Displayed;
Name=2;
IsoId=Q9UBU8-2; Sequence=VSP_012889;
Name=3;
IsoId=Q9UBU8-3; Sequence=VSP_046016;
-!- SEQUENCE CAUTION:
Sequence=AAG17253.1; Type=Frameshift; Positions=348, 360; Evidence={ECO:0000305};
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EMBL; AF100615; AAD29872.1; -; mRNA.
EMBL; AF167173; AAF80854.1; -; mRNA.
EMBL; AF218011; AAG17253.1; ALT_FRAME; mRNA.
EMBL; AY148481; AAN65338.1; -; mRNA.
EMBL; AF070664; AAD20970.1; -; mRNA.
EMBL; AF161546; AAF29033.1; -; mRNA.
EMBL; AF109188; AAQ13497.1; -; mRNA.
EMBL; AK296650; BAG59248.1; -; mRNA.
EMBL; AK300789; BAH13347.1; -; mRNA.
EMBL; AL137697; CAB70879.2; -; mRNA.
EMBL; AC011944; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC022748; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC103975; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471136; EAW99145.1; -; Genomic_DNA.
EMBL; CH471136; EAW99144.1; -; Genomic_DNA.
EMBL; CH471136; EAW99146.1; -; Genomic_DNA.
EMBL; CH471136; EAW99147.1; -; Genomic_DNA.
EMBL; BC022845; AAH22845.1; -; mRNA.
EMBL; BC002936; AAH02936.1; -; mRNA.
EMBL; BC067826; AAH67826.1; -; mRNA.
EMBL; CX165647; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AF131847; AAD20058.1; -; mRNA.
CCDS; CCDS10307.1; -. [Q9UBU8-1]
CCDS; CCDS32304.1; -. [Q9UBU8-2]
CCDS; CCDS58393.1; -. [Q9UBU8-3]
PIR; T46285; T46285.
RefSeq; NP_001252532.1; NM_001265603.1. [Q9UBU8-3]
RefSeq; NP_001252533.1; NM_001265604.1. [Q9UBU8-3]
RefSeq; NP_001252534.1; NM_001265605.1. [Q9UBU8-3]
RefSeq; NP_006782.1; NM_006791.3. [Q9UBU8-2]
RefSeq; NP_996670.1; NM_206839.2. [Q9UBU8-1]
UniGene; Hs.374503; -.
PDB; 2AQL; X-ray; 2.30 A; A/B=190-362.
PDB; 2EFI; NMR; -; A=1-132.
PDB; 2F5J; X-ray; 2.20 A; A/B=190-360.
PDB; 2F5K; X-ray; 2.20 A; A/B/C/D/E/F=1-129.
PDB; 2LKM; NMR; -; B=194-362.
PDB; 2N1D; NMR; -; B=194-362.
PDBsum; 2AQL; -.
PDBsum; 2EFI; -.
PDBsum; 2F5J; -.
PDBsum; 2F5K; -.
PDBsum; 2LKM; -.
PDBsum; 2N1D; -.
ProteinModelPortal; Q9UBU8; -.
SMR; Q9UBU8; -.
BioGrid; 116134; 113.
CORUM; Q9UBU8; -.
DIP; DIP-29017N; -.
IntAct; Q9UBU8; 71.
MINT; MINT-1472718; -.
STRING; 9606.ENSP00000331310; -.
iPTMnet; Q9UBU8; -.
PhosphoSitePlus; Q9UBU8; -.
BioMuta; MORF4L1; -.
DMDM; 59803121; -.
EPD; Q9UBU8; -.
PaxDb; Q9UBU8; -.
PeptideAtlas; Q9UBU8; -.
PRIDE; Q9UBU8; -.
DNASU; 10933; -.
Ensembl; ENST00000331268; ENSP00000331310; ENSG00000185787. [Q9UBU8-1]
Ensembl; ENST00000426013; ENSP00000408880; ENSG00000185787. [Q9UBU8-2]
Ensembl; ENST00000558502; ENSP00000452808; ENSG00000185787. [Q9UBU8-3]
Ensembl; ENST00000559345; ENSP00000452717; ENSG00000185787. [Q9UBU8-3]
GeneID; 10933; -.
KEGG; hsa:10933; -.
UCSC; uc002bel.5; human. [Q9UBU8-1]
CTD; 10933; -.
DisGeNET; 10933; -.
EuPathDB; HostDB:ENSG00000185787.14; -.
GeneCards; MORF4L1; -.
HGNC; HGNC:16989; MORF4L1.
HPA; HPA042360; -.
HPA; HPA062010; -.
MIM; 607303; gene.
neXtProt; NX_Q9UBU8; -.
OpenTargets; ENSG00000185787; -.
PharmGKB; PA134895182; -.
eggNOG; KOG3001; Eukaryota.
eggNOG; ENOG410XR9F; LUCA.
GeneTree; ENSGT00530000063018; -.
HOVERGEN; HBG052487; -.
InParanoid; Q9UBU8; -.
KO; K11339; -.
OrthoDB; EOG091G0J32; -.
PhylomeDB; Q9UBU8; -.
TreeFam; TF323400; -.
Reactome; R-HSA-3214847; HATs acetylate histones.
ChiTaRS; MORF4L1; human.
EvolutionaryTrace; Q9UBU8; -.
GeneWiki; MORF4L1; -.
GenomeRNAi; 10933; -.
PRO; PR:Q9UBU8; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000185787; -.
CleanEx; HS_MORF4L1; -.
ExpressionAtlas; Q9UBU8; baseline and differential.
Genevisible; Q9UBU8; HS.
GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:UniProtKB.
GO; GO:0016607; C:nuclear speck; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0016580; C:Sin3 complex; IDA:UniProtKB.
GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
GO; GO:0008283; P:cell proliferation; IEA:Ensembl.
GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
GO; GO:0006342; P:chromatin silencing; IBA:GO_Central.
GO; GO:0000724; P:double-strand break repair via homologous recombination; IDA:UniProtKB.
GO; GO:0016575; P:histone deacetylation; IDA:UniProtKB.
GO; GO:0043968; P:histone H2A acetylation; IDA:UniProtKB.
GO; GO:0043967; P:histone H4 acetylation; IDA:UniProtKB.
GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR016197; Chromodomain-like.
InterPro; IPR008676; MRG.
InterPro; IPR026541; MRG_dom.
InterPro; IPR025995; Tudor-knot.
PANTHER; PTHR10880; PTHR10880; 1.
Pfam; PF05712; MRG; 1.
Pfam; PF11717; Tudor-knot; 1.
PIRSF; PIRSF038133; HAT_Nua4_EAF3/MRG15; 1.
SUPFAM; SSF54160; SSF54160; 2.
PROSITE; PS51640; MRG; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Chromatin regulator;
Complete proteome; Direct protein sequencing; DNA damage;
DNA recombination; DNA repair; Growth regulation; Nucleus;
Reference proteome; Transcription; Transcription regulation.
CHAIN 1 362 Mortality factor 4-like protein 1.
/FTId=PRO_0000088764.
DOMAIN 191 362 MRG. {ECO:0000255|PROSITE-
ProRule:PRU00972}.
REGION 26 62 Interaction with KAT8.
{ECO:0000269|PubMed:12397079}.
REGION 133 266 Sufficient for interaction with SIN3A.
{ECO:0000269|PubMed:12391155}.
REGION 164 230 Interaction with RB1-1.
REGION 188 342 Sufficient for interaction with PHF12.
{ECO:0000269|PubMed:12391155}.
REGION 323 344 Interaction with RB1-2.
MOTIF 135 146 Nuclear localization signal.
{ECO:0000255}.
MOD_RES 143 143 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
VAR_SEQ 1 127 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_046016.
VAR_SEQ 52 91 KSAVRPRRSEKSLKTHEDIVALFPVPEGAPSVHHPLLTSS
-> N (in isoform 2).
{ECO:0000303|PubMed:11042152,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17974005,
ECO:0000303|PubMed:9891081,
ECO:0000303|Ref.2, ECO:0000303|Ref.6}.
/FTId=VSP_012889.
MUTAGEN 208 208 V->E: Abolishes binding to MRFAP1.
{ECO:0000269|PubMed:16407074}.
MUTAGEN 234 234 E->R: No effect on MRFAP1 binding.
{ECO:0000269|PubMed:16407074}.
MUTAGEN 251 251 Y->A: No effect on MRFAP1 binding.
{ECO:0000269|PubMed:16407074}.
MUTAGEN 254 254 N->C: Reduces binding to MRFAP1.
{ECO:0000269|PubMed:16407074}.
CONFLICT 224 224 P -> R (in Ref. 11; AAH67826).
{ECO:0000305}.
CONFLICT 261 261 K -> KK (in Ref. 6; CAB70879).
{ECO:0000305}.
STRAND 16 36 {ECO:0000244|PDB:2F5K}.
STRAND 39 46 {ECO:0000244|PDB:2F5K}.
STRAND 47 49 {ECO:0000244|PDB:2EFI}.
STRAND 94 97 {ECO:0000244|PDB:2F5K}.
HELIX 98 100 {ECO:0000244|PDB:2F5K}.
STRAND 101 105 {ECO:0000244|PDB:2F5K}.
HELIX 106 125 {ECO:0000244|PDB:2F5K}.
HELIX 201 203 {ECO:0000244|PDB:2F5J}.
HELIX 204 215 {ECO:0000244|PDB:2F5J}.
STRAND 219 221 {ECO:0000244|PDB:2F5J}.
STRAND 226 228 {ECO:0000244|PDB:2F5J}.
HELIX 229 241 {ECO:0000244|PDB:2F5J}.
STRAND 244 246 {ECO:0000244|PDB:2LKM}.
HELIX 252 271 {ECO:0000244|PDB:2F5J}.
HELIX 275 277 {ECO:0000244|PDB:2F5J}.
HELIX 278 287 {ECO:0000244|PDB:2F5J}.
HELIX 293 296 {ECO:0000244|PDB:2F5J}.
HELIX 299 313 {ECO:0000244|PDB:2F5J}.
HELIX 320 339 {ECO:0000244|PDB:2F5J}.
HELIX 341 344 {ECO:0000244|PDB:2F5J}.
HELIX 347 349 {ECO:0000244|PDB:2F5J}.
STRAND 350 352 {ECO:0000244|PDB:2F5J}.
HELIX 355 358 {ECO:0000244|PDB:2F5J}.
TURN 359 361 {ECO:0000244|PDB:2LKM}.
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


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