MBTD1_MOUSE
ID MBTD1_MOUSE Reviewed; 631 AA.
AC Q6P5G3; Q6P3F0; Q8VE12;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=MBT domain-containing protein 1 {ECO:0000305};
GN Name=Mbtd1 {ECO:0000312|MGI:MGI:2143977};
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 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and Czech II; TISSUE=Brain, Embryo, 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 [3]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-115, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Chromatin reader component of the NuA4 histone
CC acetyltransferase complex, a multiprotein complex involved in
CC transcriptional activation of select genes principally by acetylation
CC of nucleosomal histones H4 and H2A. The NuA4 complex plays a direct
CC role in repair of DNA double-strand breaks (DSBs) by promoting
CC homologous recombination (HR). MBTD1 specifically recognizes and binds
CC monomethylated and dimethylated 'Lys-20' on histone H4 (H4K20me1 and
CC H4K20me2, respectively). In the NuA4 complex, MBTD1 promotes
CC recruitment of the complex to H4K20me marks by competing with TP53BP1
CC for binding to H4K20me. Following recruitment to H4K20me at DNA breaks,
CC the NuA4 complex catalyzes acetylation of 'Lys-15' on histone H2A
CC (H2AK15), blocking the ubiquitination mark required for TP53BP1
CC localization at DNA breaks, thereby promoting homologous recombination
CC (HR). {ECO:0000250|UniProtKB:Q05BQ5}.
CC -!- SUBUNIT: Monomer. Component of the NuA4 histone acetyltransferase
CC complex. Interacts with EPC1; interaction is direct and promotes
CC recruitment of MBTD1 into the NuA4 histone acetyltransferase complex.
CC {ECO:0000250|UniProtKB:Q05BQ5}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q05BQ5}.
CC Chromosome {ECO:0000250|UniProtKB:Q05BQ5}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6P5G3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P5G3-2; Sequence=VSP_030119, VSP_030120;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH20018.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL662838; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL663078; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC020018; AAH20018.1; ALT_INIT; mRNA.
DR EMBL; BC062907; AAH62907.1; -; mRNA.
DR EMBL; BC064014; AAH64014.1; -; mRNA.
DR CCDS; CCDS48883.1; -. [Q6P5G3-1]
DR CCDS; CCDS83868.1; -. [Q6P5G3-2]
DR RefSeq; NP_001333454.1; NM_001346525.1. [Q6P5G3-2]
DR RefSeq; NP_598773.2; NM_134012.3. [Q6P5G3-1]
DR RefSeq; XP_006531973.1; XM_006531910.3.
DR RefSeq; XP_017169693.1; XM_017314204.1.
DR RefSeq; XP_017169694.1; XM_017314205.1.
DR RefSeq; XP_017169695.1; XM_017314206.1.
DR AlphaFoldDB; Q6P5G3; -.
DR SMR; Q6P5G3; -.
DR BioGRID; 222109; 6.
DR ComplexPortal; CPX-990; NuA4 histone acetyltransferase complex.
DR IntAct; Q6P5G3; 2.
DR MINT; Q6P5G3; -.
DR STRING; 10090.ENSMUSP00000103486; -.
DR iPTMnet; Q6P5G3; -.
DR PhosphoSitePlus; Q6P5G3; -.
DR EPD; Q6P5G3; -.
DR MaxQB; Q6P5G3; -.
DR PaxDb; Q6P5G3; -.
DR PeptideAtlas; Q6P5G3; -.
DR PRIDE; Q6P5G3; -.
DR ProteomicsDB; 295975; -. [Q6P5G3-1]
DR ProteomicsDB; 295976; -. [Q6P5G3-2]
DR Antibodypedia; 18227; 109 antibodies from 21 providers.
DR DNASU; 103537; -.
DR Ensembl; ENSMUST00000063718; ENSMUSP00000065442; ENSMUSG00000059474. [Q6P5G3-2]
DR Ensembl; ENSMUST00000107853; ENSMUSP00000103485; ENSMUSG00000059474. [Q6P5G3-1]
DR Ensembl; ENSMUST00000107854; ENSMUSP00000103486; ENSMUSG00000059474. [Q6P5G3-1]
DR GeneID; 103537; -.
DR KEGG; mmu:103537; -.
DR UCSC; uc007kxn.2; mouse. [Q6P5G3-2]
DR UCSC; uc007kxo.2; mouse. [Q6P5G3-1]
DR CTD; 54799; -.
DR MGI; MGI:2143977; Mbtd1.
DR VEuPathDB; HostDB:ENSMUSG00000059474; -.
DR eggNOG; KOG3766; Eukaryota.
DR GeneTree; ENSGT00940000153840; -.
DR HOGENOM; CLU_005352_2_1_1; -.
DR InParanoid; Q6P5G3; -.
DR OMA; WFARVMK; -.
DR OrthoDB; 1334498at2759; -.
DR PhylomeDB; Q6P5G3; -.
DR TreeFam; TF316498; -.
DR BioGRID-ORCS; 103537; 7 hits in 77 CRISPR screens.
DR ChiTaRS; Mbtd1; mouse.
DR PRO; PR:Q6P5G3; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q6P5G3; protein.
DR Bgee; ENSMUSG00000059474; Expressed in rostral migratory stream and 266 other tissues.
DR ExpressionAtlas; Q6P5G3; baseline and differential.
DR Genevisible; Q6P5G3; MM.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; ISS:UniProtKB.
DR GO; GO:0000786; C:nucleosome; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0035064; F:methylated histone binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0048706; P:embryonic skeletal system development; IMP:MGI.
DR GO; GO:0016573; P:histone acetylation; IC:ComplexPortal.
DR GO; GO:0043968; P:histone H2A acetylation; ISO:MGI.
DR GO; GO:0043967; P:histone H4 acetylation; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
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 Gene3D; 3.30.60.160; -; 1.
DR InterPro; IPR004092; Mbt.
DR InterPro; IPR012313; Znf_FCS.
DR InterPro; IPR038603; Znf_FCS_sf.
DR Pfam; PF02820; MBT; 4.
DR SMART; SM00561; MBT; 4.
DR PROSITE; PS51079; MBT; 4.
DR PROSITE; PS51024; ZF_FCS; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Chromatin regulator; Chromosome;
KW Metal-binding; Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..631
FT /note="MBT domain-containing protein 1"
FT /id="PRO_0000313718"
FT REPEAT 144..248
FT /note="MBT 1"
FT REPEAT 256..353
FT /note="MBT 2"
FT REPEAT 354..459
FT /note="MBT 3"
FT REPEAT 467..563
FT /note="MBT 4"
FT ZN_FING 45..80
FT /note="FCS-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..607
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 54
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT BINDING 57
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT MOD_RES 115
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT VAR_SEQ 1
FT /note="M -> MITAIKKQNILHNPKEKADWFGM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030119"
FT VAR_SEQ 593..631
FT /note="MTTSQLKEELLDGEDYSFLHGASDQESNGSATVYIKQEP -> STEEMTES
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030120"
SQ SEQUENCE 631 AA; 70669 MW; 6F6018713F7FB83A CRC64;
MFDGYDSCSE DTSSSSSSEE SEEEVAPLPS NLPIIKNNGQ VYTYPDGKSG MATCEMCGMV
GVRDAFYSKT KRFCSVSCSR SYSSNSKKAS ILARLQGKPP TKKAKVLQKQ PLVAKLAAYA
QYQATLQNQA KTKAGNSAIS VEGFSWGNYI NSNSFIAAPV ACFKHAPMGT CWGDISENVR
IEVPNTDCSL PTKVFWIAGI IKLAGYNALL RYEGFENDSS LDFWCNICGS DIHPVGWCAA
SGKPLVPPRT VQHKYTNWKA FLVKRLTGAK TLPPDFSQKV SESMQYPFKP CMRVEVVDKR
HLCRTRVAVV ESVIGGRLRL VYEESEDRTD DFWCHMHSPL IHHIGWSRSI GHRFKRSDIT
KKQDGHFDTP PHLFAKVKEV DQSGEWFKEG MKLEAIDPLN LSTICVATIR KVLADGFLMI
GIDGSEAADG SDWFCYHATS PSIFPVGFCE INMIELTPPR GYTKLPFKWF DYLRETGSIA
APVKLFNKDV PNHGFRVGMK LEAVDLMEPR LICVATVTRI IHRLLRIHFD GWEEEYDQWV
DCESPDLYPV GWCQLTGYQL QPPASQSSRE SQSASSKQKK KAKSQQYKGH KKMTTSQLKE
ELLDGEDYSF LHGASDQESN GSATVYIKQE P
