MBTD1_XENLA
ID MBTD1_XENLA Reviewed; 621 AA.
AC Q32N90; Q6GP59;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=MBT domain-containing protein 1 {ECO:0000305};
GN Name=mbtd1 {ECO:0000250|UniProtKB:Q05BQ5};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Oocyte, and Spleen;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000250|UniProtKB:Q05BQ5}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q05BQ5}.
CC Chromosome {ECO:0000250|UniProtKB:Q05BQ5}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC073284; AAH73284.1; -; mRNA.
DR EMBL; BC108771; AAI08772.1; -; mRNA.
DR RefSeq; NP_001085289.1; NM_001091820.1.
DR AlphaFoldDB; Q32N90; -.
DR SMR; Q32N90; -.
DR BioGRID; 101803; 2.
DR IntAct; Q32N90; 1.
DR DNASU; 443638; -.
DR GeneID; 443638; -.
DR KEGG; xla:443638; -.
DR CTD; 443638; -.
DR Xenbase; XB-GENE-949662; mbtd1.L.
DR OMA; WFARVMK; -.
DR OrthoDB; 1334498at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 443638; Expressed in egg cell and 19 other tissues.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; ISS:UniProtKB.
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:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
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 2: Evidence at transcript level;
KW Chromatin regulator; Chromosome; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..621
FT /note="MBT domain-containing protein 1"
FT /id="PRO_0000313719"
FT REPEAT 164..268
FT /note="MBT 1"
FT REPEAT 276..373
FT /note="MBT 2"
FT REPEAT 374..479
FT /note="MBT 3"
FT REPEAT 487..583
FT /note="MBT 4"
FT ZN_FING 68..103
FT /note="FCS-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 581..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..621
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT BINDING 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT CONFLICT 602
FT /note="S -> K (in Ref. 1; AAH73284)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 621 AA; 69812 MW; F292D4D3915E79BC CRC64;
MEKTKDPADR SSRSERKRRD SFGMFDGYDS CSEDTSSSSS SDESEEEVAP LPSSLPIIKN
NGQVYTYPDG KSGMATCEMC GMVGVRDAFY SKTKRFCSVS CSRSYSSNSK KASILARLQG
KPPTKKAKVL QKKPLVAKLA AYAQYKATLK NQSVNKAPVT VEGFSWGNYI TSNNVIAAPV
TCFRHAPMGN CWGDIAEGVR IEVPNTDSNL PTKVFWISGI VKLAGYNALL RYEGFENDSS
LDFWCNICGP DIHPVGWCAT SGKPLVPPQS IQHKYTNWKA FLVKRLTGAK TLPPDFSQKV
SENMQYPFKP SMRVEVVDKT HLCRTRVAVV ESVIGGRLRL VYEESEDKTD DFWCHMYSPL
IHPIGWSRSI GHRFKRTDIL KKQESNYDAP SHLFIKVKDV EQGSEWFKEG MKLEAIDPLN
LSAICVATIR KVLAEGYLMI GIDGSEAADG SDWFCYHASS PSIFPVGFCE INKIELTPPR
GYTKLPFKWF DYLRETGSIA APVKLFNKDV PNHGFRVGMK LEAVDLMEPR LVCVATVTRI
IHRLLRIHFD GWEDEYDQWV DCESPDLYPV GWCQLTGYQL QPPAPQSNKD GQSNVSKQKK
KSKSQPYKGH KKNFRKPGNR P
