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Mortality factor 4-like protein 2 (MORF-related gene X protein) (Protein MSL3-2) (Transcription factor-like protein MRGX)

 MO4L2_HUMAN             Reviewed;         288 AA.
Q15014; B3KP92; D3DXA5; Q567V0; Q8J026;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
27-SEP-2017, entry version 167.
RecName: Full=Mortality factor 4-like protein 2;
AltName: Full=MORF-related gene X protein;
AltName: Full=Protein MSL3-2;
AltName: Full=Transcription factor-like protein MRGX;
Name=MORF4L2; Synonyms=KIAA0026, MRGX;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
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].
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].
TISSUE=Bone marrow;
PubMed=7584026; DOI=10.1093/dnares/1.1.27;
Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y.,
Sato S., Nagase T., Seki N., Ishikawa K., Tabata S.;
"Prediction of the coding sequences of unidentified human genes. I.
The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by
analysis of randomly sampled cDNA clones from human immature myeloid
cell line KG-1.";
DNA Res. 1:27-35(1994).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[6]
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.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pancreas, and Placenta;
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).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-16.
Myokai F., Oyama M.;
"Mortality factor related gene X 102 5'.";
Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
[9]
PROTEIN SEQUENCE OF 12-22; 82-99; 105-116; 154-166; 176-187; 188-201;
235-247 AND 266-277, 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).
[10]
INTERACTION WITH 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).
[11]
INTERACTION WITH MRFAP1 AND RB1, AND MUTAGENESIS OF 132-TRP--ASP-136
AND LEU-263.
PubMed=14506250; DOI=10.1074/jbc.M309192200;
Tominaga K., Leung J.K., Rookard P., Echigo J., Smith J.R.,
Pereira-Smith O.M.;
"MRGX is a novel transcriptional regulator that exhibits activation or
repression of the B-myb promoter in a cell type-dependent manner.";
J. Biol. Chem. 278:49618-49624(2003).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[13]
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).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
-!- FUNCTION: Component of the NuA4 histone acetyltransferase complex
which is involved in transcriptional activation of select genes
principally by acetylation of nucleosomal histone 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.
-!- 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 and VPS72/YL1. 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 MRFAP1 and RB1. May
also interact with one or more as yet undefined members of the TLE
(transducin-like enhancer of split) family of transcriptional
repressors. {ECO:0000269|PubMed:12391155,
ECO:0000269|PubMed:12963728, ECO:0000269|PubMed:14506250}.
-!- INTERACTION:
Q08117:AES; NbExp=3; IntAct=EBI-399257, EBI-717810;
Q9H165-2:BCL11A; NbExp=4; IntAct=EBI-399257, EBI-10183342;
Q8N7W2-2:BEND7; NbExp=3; IntAct=EBI-399257, EBI-10181188;
Q01850:CDR2; NbExp=6; IntAct=EBI-399257, EBI-1181367;
Q53EZ4:CEP55; NbExp=5; IntAct=EBI-399257, EBI-747776;
Q96D03:DDIT4L; NbExp=5; IntAct=EBI-399257, EBI-742054;
Q8IZU0:FAM9B; NbExp=3; IntAct=EBI-399257, EBI-10175124;
Q08379:GOLGA2; NbExp=3; IntAct=EBI-399257, EBI-618309;
Q96HH9:GRAMD3; NbExp=3; IntAct=EBI-399257, EBI-2832937;
Q13422:IKZF1; NbExp=3; IntAct=EBI-399257, EBI-745305;
Q77UV9:KIE-2 (xeno); NbExp=2; IntAct=EBI-399257, EBI-2608731;
Q8N4I8:KLHL3; NbExp=3; IntAct=EBI-399257, EBI-10230467;
Q96JM7:L3MBTL3; NbExp=3; IntAct=EBI-399257, EBI-2686809;
Q9BRK4:LZTS2; NbExp=3; IntAct=EBI-399257, EBI-741037;
Q9Y605:MRFAP1; NbExp=13; IntAct=EBI-399257, EBI-995714;
Q96HT8:MRFAP1L1; NbExp=7; IntAct=EBI-399257, EBI-748896;
Q9NV56:MRGBP; NbExp=8; IntAct=EBI-399257, EBI-399076;
Q8IXK0:PHC2; NbExp=3; IntAct=EBI-399257, EBI-713786;
Q9UL42:PNMA2; NbExp=3; IntAct=EBI-399257, EBI-302355;
Q9NVV9:THAP1; NbExp=3; IntAct=EBI-399257, EBI-741515;
Q15025:TNIP1; NbExp=3; IntAct=EBI-399257, EBI-357849;
P45379:TNNT2; NbExp=3; IntAct=EBI-399257, EBI-8485957;
Q96DT7:ZBTB10; NbExp=3; IntAct=EBI-399257, EBI-10235384;
O43829:ZBTB14; NbExp=3; IntAct=EBI-399257, EBI-10176632;
O43298:ZBTB43; NbExp=3; IntAct=EBI-399257, EBI-740718;
O15156:ZBTB7B; NbExp=3; IntAct=EBI-399257, EBI-740434;
-!- SUBCELLULAR LOCATION: Nucleus.
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EMBL; AF100620; AAD29873.1; -; mRNA.
EMBL; AF167174; AAF80855.1; -; mRNA.
EMBL; D14812; BAA03553.1; -; mRNA.
EMBL; AK056012; BAG51604.1; -; mRNA.
EMBL; AL049610; CAB55701.1; -; Genomic_DNA.
EMBL; CH471190; EAW54698.1; -; Genomic_DNA.
EMBL; CH471190; EAW54699.1; -; Genomic_DNA.
EMBL; CH471190; EAW54700.1; -; Genomic_DNA.
EMBL; CH471190; EAW54701.1; -; Genomic_DNA.
EMBL; BC056899; AAH56899.1; -; mRNA.
EMBL; BC093013; AAH93013.1; -; mRNA.
EMBL; AB050778; BAC22659.1; -; mRNA.
CCDS; CCDS14512.1; -.
RefSeq; NP_001135890.1; NM_001142418.1.
RefSeq; NP_001135891.1; NM_001142419.1.
RefSeq; NP_001135892.1; NM_001142420.1.
RefSeq; NP_001135893.1; NM_001142421.1.
RefSeq; NP_001135894.1; NM_001142422.1.
RefSeq; NP_001135895.1; NM_001142423.1.
RefSeq; NP_001135896.1; NM_001142424.1.
RefSeq; NP_001135897.1; NM_001142425.1.
RefSeq; NP_001135898.1; NM_001142426.1.
RefSeq; NP_001135899.1; NM_001142427.1.
RefSeq; NP_001135900.1; NM_001142428.1.
RefSeq; NP_001135901.1; NM_001142429.1.
RefSeq; NP_001135902.1; NM_001142430.1.
RefSeq; NP_001135903.1; NM_001142431.1.
RefSeq; NP_001135904.1; NM_001142432.1.
RefSeq; NP_036418.1; NM_012286.2.
UniGene; Hs.326387; -.
ProteinModelPortal; Q15014; -.
SMR; Q15014; -.
BioGrid; 115001; 101.
CORUM; Q15014; -.
IntAct; Q15014; 67.
MINT; MINT-7944329; -.
STRING; 9606.ENSP00000353643; -.
iPTMnet; Q15014; -.
PhosphoSitePlus; Q15014; -.
BioMuta; MORF4L2; -.
DMDM; 3123049; -.
EPD; Q15014; -.
MaxQB; Q15014; -.
PaxDb; Q15014; -.
PeptideAtlas; Q15014; -.
PRIDE; Q15014; -.
DNASU; 9643; -.
Ensembl; ENST00000360458; ENSP00000353643; ENSG00000123562.
Ensembl; ENST00000422154; ENSP00000394417; ENSG00000123562.
Ensembl; ENST00000433176; ENSP00000415476; ENSG00000123562.
Ensembl; ENST00000441076; ENSP00000391969; ENSG00000123562.
Ensembl; ENST00000451301; ENSP00000410532; ENSG00000123562.
GeneID; 9643; -.
KEGG; hsa:9643; -.
UCSC; uc004ekx.4; human.
CTD; 9643; -.
DisGeNET; 9643; -.
EuPathDB; HostDB:ENSG00000123562.16; -.
GeneCards; MORF4L2; -.
HGNC; HGNC:16849; MORF4L2.
HPA; HPA031872; -.
HPA; HPA054102; -.
MIM; 300409; gene.
neXtProt; NX_Q15014; -.
OpenTargets; ENSG00000123562; -.
PharmGKB; PA134925837; -.
eggNOG; KOG3001; Eukaryota.
eggNOG; ENOG410XR9F; LUCA.
GeneTree; ENSGT00530000063018; -.
HOGENOM; HOG000190863; -.
HOVERGEN; HBG052487; -.
InParanoid; Q15014; -.
KO; K11342; -.
OMA; RGNMQRS; -.
OrthoDB; EOG091G0J32; -.
PhylomeDB; Q15014; -.
TreeFam; TF323400; -.
Reactome; R-HSA-3214847; HATs acetylate histones.
ChiTaRS; MORF4L2; human.
GeneWiki; MORF4L2; -.
GenomeRNAi; 9643; -.
PRO; PR:Q15014; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000123562; -.
CleanEx; HS_MORF4L2; -.
ExpressionAtlas; Q15014; baseline and differential.
Genevisible; Q15014; HS.
GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IBA:GO_Central.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
GO; GO:0006342; P:chromatin silencing; IBA:GO_Central.
GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
GO; GO:0016575; P:histone deacetylation; IBA:GO_Central.
GO; GO:0043968; P:histone H2A acetylation; IBA:GO_Central.
GO; GO:0043967; P:histone H4 acetylation; IBA:GO_Central.
GO; GO:0051155; P:positive regulation of striated muscle cell differentiation; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR008676; MRG.
InterPro; IPR026541; MRG_dom.
PANTHER; PTHR10880; PTHR10880; 1.
Pfam; PF05712; MRG; 1.
PIRSF; PIRSF038133; HAT_Nua4_EAF3/MRG15; 1.
PROSITE; PS51640; MRG; 1.
1: Evidence at protein level;
Chromatin regulator; Complete proteome; Direct protein sequencing;
DNA damage; DNA repair; Growth regulation; Nucleus; Phosphoprotein;
Reference proteome; Transcription; Transcription regulation.
CHAIN 1 288 Mortality factor 4-like protein 2.
/FTId=PRO_0000088768.
DOMAIN 117 288 MRG. {ECO:0000255|PROSITE-
ProRule:PRU00972}.
MOD_RES 71 71 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MUTAGEN 132 136 Missing: Abrogates both transcriptional
activation and repression by MORF4L2.
{ECO:0000269|PubMed:14506250}.
MUTAGEN 263 263 L->A: Abrogates both transcriptional
activation and repression by MORF4L2.
{ECO:0000269|PubMed:14506250}.
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


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