MO4L2_MOUSE
ID MO4L2_MOUSE Reviewed; 288 AA.
AC Q9R0Q4; A2AEB2; Q3UL62; Q6DIB1; Q6ZQK7; Q8C201; Q8C6C2;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Mortality factor 4-like protein 2;
DE AltName: Full=MORF-related gene X protein;
DE AltName: Full=Sid 393;
DE AltName: Full=Transcription factor-like protein MRGX;
GN Name=Morf4l2; Synonyms=Kiaa0026, Sid393;
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].
RA Seki N., Hattori A., Hayashi A., Kozuma S., Muramatsu M., Saito T.;
RT "Mouse homolog of KIAA0026.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C3H/HeJ, C57BL/6J, and NOD;
RC TISSUE=Bone marrow, Embryonic stem cell, Eye, and Thymus;
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].
RC TISSUE=Brain;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=129, and C57BL/6J; TISSUE=Eye, and Mammary tumor;
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Pancreas, and Spleen;
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 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 (By
CC similarity). {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 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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00972}.
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DR EMBL; AB025049; BAA84687.1; -; mRNA.
DR EMBL; AK075946; BAC36075.1; -; mRNA.
DR EMBL; AK088849; BAC40611.1; -; mRNA.
DR EMBL; AK089963; BAC41017.1; -; mRNA.
DR EMBL; AK129038; BAC97848.1; -; mRNA.
DR EMBL; AK131944; BAE20890.1; -; mRNA.
DR EMBL; AK145686; BAE26588.1; -; mRNA.
DR EMBL; AK150401; BAE29527.1; -; mRNA.
DR EMBL; AK150670; BAE29752.1; -; mRNA.
DR EMBL; AK151570; BAE30512.1; -; mRNA.
DR EMBL; AK160012; BAE35559.1; -; mRNA.
DR EMBL; AK161610; BAE36491.1; -; mRNA.
DR EMBL; AK164433; BAE37786.1; -; mRNA.
DR EMBL; AK166637; BAE38909.1; -; mRNA.
DR EMBL; AL671887; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC075653; AAH75653.1; -; mRNA.
DR EMBL; BC088731; AAH88731.1; -; mRNA.
DR CCDS; CCDS30422.1; -.
DR RefSeq; NP_001161697.1; NM_001168225.1.
DR RefSeq; NP_001161698.1; NM_001168226.1.
DR RefSeq; NP_001161699.1; NM_001168227.1.
DR RefSeq; NP_001161700.1; NM_001168228.1.
DR RefSeq; NP_001161701.1; NM_001168229.1.
DR RefSeq; NP_001161702.1; NM_001168230.1.
DR RefSeq; NP_062742.4; NM_019768.4.
DR RefSeq; XP_006528647.1; XM_006528584.1.
DR AlphaFoldDB; Q9R0Q4; -.
DR SMR; Q9R0Q4; -.
DR BioGRID; 207951; 3.
DR ComplexPortal; CPX-990; NuA4 histone acetyltransferase complex.
DR IntAct; Q9R0Q4; 1.
DR STRING; 10090.ENSMUSP00000033797; -.
DR iPTMnet; Q9R0Q4; -.
DR PhosphoSitePlus; Q9R0Q4; -.
DR EPD; Q9R0Q4; -.
DR MaxQB; Q9R0Q4; -.
DR PaxDb; Q9R0Q4; -.
DR PeptideAtlas; Q9R0Q4; -.
DR PRIDE; Q9R0Q4; -.
DR ProteomicsDB; 290269; -.
DR Antibodypedia; 14953; 168 antibodies from 30 providers.
DR DNASU; 56397; -.
DR Ensembl; ENSMUST00000033797; ENSMUSP00000033797; ENSMUSG00000031422.
DR Ensembl; ENSMUST00000080411; ENSMUSP00000108722; ENSMUSG00000031422.
DR Ensembl; ENSMUST00000113097; ENSMUSP00000108720; ENSMUSG00000031422.
DR Ensembl; ENSMUST00000164609; ENSMUSP00000129774; ENSMUSG00000031422.
DR Ensembl; ENSMUST00000166478; ENSMUSP00000131909; ENSMUSG00000031422.
DR Ensembl; ENSMUST00000166930; ENSMUSP00000126363; ENSMUSG00000031422.
DR Ensembl; ENSMUST00000169418; ENSMUSP00000132643; ENSMUSG00000031422.
DR GeneID; 56397; -.
DR KEGG; mmu:56397; -.
DR UCSC; uc009uiu.3; mouse.
DR CTD; 9643; -.
DR MGI; MGI:1927167; Morf4l2.
DR VEuPathDB; HostDB:ENSMUSG00000031422; -.
DR eggNOG; KOG3001; Eukaryota.
DR GeneTree; ENSGT00950000182965; -.
DR HOGENOM; CLU_039566_4_0_1; -.
DR InParanoid; Q9R0Q4; -.
DR OMA; RGNMQRS; -.
DR OrthoDB; 1624495at2759; -.
DR PhylomeDB; Q9R0Q4; -.
DR TreeFam; TF323400; -.
DR BioGRID-ORCS; 56397; 10 hits in 109 CRISPR screens.
DR ChiTaRS; Morf4l2; mouse.
DR PRO; PR:Q9R0Q4; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9R0Q4; protein.
DR Bgee; ENSMUSG00000031422; Expressed in yolk sac and 74 other tissues.
DR ExpressionAtlas; Q9R0Q4; baseline and differential.
DR Genevisible; Q9R0Q4; MM.
DR GO; GO:0000123; C:histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0000786; C:nucleosome; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0043967; P:histone H4 acetylation; ISO:MGI.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; ISO:MGI.
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; 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; 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; DNA damage; DNA repair; Growth regulation; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..288
FT /note="Mortality factor 4-like protein 2"
FT /id="PRO_0000088769"
FT DOMAIN 117..288
FT /note="MRG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00972"
FT REGION 1..115
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 97..115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15014"
FT CONFLICT 37
FT /note="A -> S (in Ref. 5; AAH75653)"
FT /evidence="ECO:0000305"
FT CONFLICT 145
FT /note="Q -> P (in Ref. 2; BAC36075)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="E -> D (in Ref. 3; BAC97848)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="I -> T (in Ref. 2; BAC41017)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 288 AA; 32184 MW; DE371EDD3D4DF4E2 CRC64;
MSSRKQASQT RGQQSAEEDN FKKPTRSNMQ RSKMRGAASG KKSAGSQPKN LDPALPGRWG
GRSAENPPSG SVRKTRKNKQ KAPGNGDGGS TSEVPQPPRK KRARADPTVE SEEAFKSRME
VKVKIPEELK PWLVEDWDLV TRQKQLFQLP AKKNVDAILE EYANCKKSQG NVDNKEYAVN
EVVGGIKEYF NVMLGTQLLY KFERPQYAEI LLAHPDAPMS QIYGAPHLLR LFVRIGAMLA
YTPLDEKSLA LLLGYLHDFL KYLAKNSASL FTASDYKVAS ADYHRKAL
