MRGBP_MOUSE
ID MRGBP_MOUSE Reviewed; 204 AA.
AC Q9DAT2; Q14AR7;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=MRG/MORF4L-binding protein;
DE AltName: Full=MRG-binding protein;
GN Name=Mrgbp;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Placenta, and Stomach;
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191 AND SER-195, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, 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 (HAT) complex
CC which is involved in transcriptional activation of select genes
CC principally by acetylation of nucleosomal histones H4 and H2A. This
CC modification may both alter nucleosome - DNA interactions and promote
CC interaction of the modified histones with other proteins which
CC positively regulate transcription. This complex may be required for the
CC activation of transcriptional programs associated with oncogene and
CC proto-oncogene mediated growth induction, tumor suppressor mediated
CC growth arrest and replicative senescence, apoptosis, and DNA repair.
CC NuA4 may also play a direct role in DNA repair when recruited to sites
CC of DNA damage.
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. MRGBP may interact directly with
CC MORF4L1/MRG15 and MORF4L2/MRGX (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9DAT2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9DAT2-2; Sequence=VSP_003793;
CC -!- SIMILARITY: Belongs to the EAF7 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB24117.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK005551; BAB24117.1; ALT_FRAME; mRNA.
DR EMBL; AK052575; BAC35046.1; -; mRNA.
DR EMBL; AL669926; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466626; EDL07342.1; -; Genomic_DNA.
DR EMBL; BC116732; AAI16733.1; -; mRNA.
DR EMBL; BC116734; AAI16735.1; -; mRNA.
DR CCDS; CCDS17178.1; -. [Q9DAT2-1]
DR RefSeq; NP_082755.1; NM_028479.1. [Q9DAT2-1]
DR AlphaFoldDB; Q9DAT2; -.
DR BioGRID; 215861; 5.
DR ComplexPortal; CPX-990; NuA4 histone acetyltransferase complex.
DR IntAct; Q9DAT2; 1.
DR STRING; 10090.ENSMUSP00000029085; -.
DR iPTMnet; Q9DAT2; -.
DR PhosphoSitePlus; Q9DAT2; -.
DR EPD; Q9DAT2; -.
DR jPOST; Q9DAT2; -.
DR MaxQB; Q9DAT2; -.
DR PaxDb; Q9DAT2; -.
DR PeptideAtlas; Q9DAT2; -.
DR PRIDE; Q9DAT2; -.
DR ProteomicsDB; 290313; -. [Q9DAT2-1]
DR ProteomicsDB; 290314; -. [Q9DAT2-2]
DR Antibodypedia; 14923; 178 antibodies from 26 providers.
DR Ensembl; ENSMUST00000029085; ENSMUSP00000029085; ENSMUSG00000027569. [Q9DAT2-1]
DR Ensembl; ENSMUST00000169630; ENSMUSP00000127747; ENSMUSG00000027569. [Q9DAT2-1]
DR GeneID; 73247; -.
DR KEGG; mmu:73247; -.
DR UCSC; uc008ojh.1; mouse. [Q9DAT2-1]
DR CTD; 55257; -.
DR MGI; MGI:1920497; Mrgbp.
DR VEuPathDB; HostDB:ENSMUSG00000027569; -.
DR eggNOG; KOG4051; Eukaryota.
DR GeneTree; ENSGT00390000007823; -.
DR HOGENOM; CLU_080546_0_0_1; -.
DR InParanoid; Q9DAT2; -.
DR OMA; NREMPSD; -.
DR OrthoDB; 1476852at2759; -.
DR PhylomeDB; Q9DAT2; -.
DR TreeFam; TF326334; -.
DR BioGRID-ORCS; 73247; 14 hits in 75 CRISPR screens.
DR ChiTaRS; Mrgbp; mouse.
DR PRO; PR:Q9DAT2; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9DAT2; protein.
DR Bgee; ENSMUSG00000027569; Expressed in spermatocyte and 214 other tissues.
DR Genevisible; Q9DAT2; MM.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0000786; C:nucleosome; ISO:MGI.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016573; P:histone acetylation; 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: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 GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR012423; Eaf7/MRGBP.
DR PANTHER; PTHR13581; PTHR13581; 1.
DR Pfam; PF07904; Eaf7; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Alternative splicing; Chromatin regulator;
KW Growth regulation; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9NV56"
FT CHAIN 2..204
FT /note="MRG/MORF4L-binding protein"
FT /id="PRO_0000215877"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..184
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0000250|UniProtKB:Q9NV56"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NV56"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 127
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NV56"
FT VAR_SEQ 119..204
FT /note="KVVIEEEMKEEMKEDVDPHSGADDVFSSSGSLGKALEKSSKDKEKNSSDLGC
FT KEGADKRKRSRVTDKVLTANSNPSSPSAAKRRRT -> ETRPPPGLGIKKASPGQRWGG
FT LGPPGRCKDPAQTIPPVAPGRFWEPRAGESGAQRQSPDGCRLVMDAEACVGSENRKQSW
FT PDRPPALATTVGFQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_003793"
FT CONFLICT 22
FT /note="P -> S (in Ref. 1; BAC35046)"
FT /evidence="ECO:0000305"
FT CONFLICT 110
FT /note="E -> D (in Ref. 1; BAC35046)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="K -> E (in Ref. 1; BAB24117)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 204 AA; 22436 MW; 3CD4BB2A64C814EA CRC64;
MGEAEVGGTG APGDKGPGEA APSPAEETVV WSPEVEVCLF HAMLGHKPVG VNRHFHMICI
RDKFSQNIGR QVPSKVIWDH LSTMYDMQAL HESEILPFPN PERNFVLPDE IIQEVREGKV
VIEEEMKEEM KEDVDPHSGA DDVFSSSGSL GKALEKSSKD KEKNSSDLGC KEGADKRKRS
RVTDKVLTAN SNPSSPSAAK RRRT
