LMBL1_RAT
ID LMBL1_RAT Reviewed; 826 AA.
AC D3ZWK4; D4A6H6;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Lethal(3)malignant brain tumor-like protein 1;
DE Short=H-l(3)mbt;
DE Short=H-l(3)mbt protein;
DE Short=L(3)mbt-like;
DE AltName: Full=L(3)mbt protein homolog;
GN Name=L3mbtl1; Synonyms=L3mbt, L3mbtl;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Polycomb group (PcG) protein that specifically recognizes and
CC binds mono- and dimethyllysine residues on target proteins, therey
CC acting as a 'reader' of a network of post-translational modifications.
CC PcG proteins maintain the transcriptionally repressive state of genes:
CC acts as a chromatin compaction factor by recognizing and binding
CC mono- and dimethylated histone H1b/H1-4 at 'Lys-26' (H1bK26me1 and
CC H1bK26me2) and histone H4 at 'Lys-20' (H4K20me1 and H4K20me2), leading
CC to condense chromatin and repress transcription. Recognizes and binds
CC p53/TP53 monomethylated at 'Lys-382', leading to repress p53/TP53-
CC target genes. Also recognizes and binds RB1/RB monomethylated at 'Lys-
CC 860'. Participates in the ETV6-mediated repression. Probably plays a
CC role in cell proliferation. Overexpression induces multinucleated
CC cells, suggesting that it is required to accomplish normal mitosis (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Interacts with RB1/RB (when monomethylated at 'Lys-
CC 860'). Interacts with p53/TP53 (when monomethylated at 'Lys-382').
CC Interacts with CBX3, ETV6, KMT5A and VCP/p97 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Excluded from the
CC nucleolus. Does not colocalizes with the PcG protein BMI1, suggesting
CC that these two proteins do not belong to the same complex (By
CC similarity). {ECO:0000250}.
CC -!- DOMAIN: The MBT repeat 2 specifically recognizes and binds
CC monomethylated and dimethylated proteins. In contrast, it does not bind
CC trimethylated proteins. The MBT repeat 1 does not bind methylated
CC peptides but inserts a proline ring in a Pro-Ser-Ser/Thr sequence
CC context (By similarity). {ECO:0000250}.
CC -!- PTM: Ubiquitinated in a VCP/p97-dependent way following DNA damage,
CC leading to its removal from DNA damage sites, promoting accessibility
CC of H4K20me2 mark for DNA repair protein TP53BP1, which is then
CC recruited to DNA damage sites. {ECO:0000250}.
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DR EMBL; CH474005; EDL96599.1; -; Genomic_DNA.
DR AlphaFoldDB; D3ZWK4; -.
DR SMR; D3ZWK4; -.
DR STRING; 10116.ENSRNOP00000049326; -.
DR PaxDb; D3ZWK4; -.
DR Ensembl; ENSRNOT00000045677; ENSRNOP00000049326; ENSRNOG00000007044.
DR RGD; 1307316; L3mbtl1.
DR eggNOG; KOG3766; Eukaryota.
DR GeneTree; ENSGT00940000159708; -.
DR HOGENOM; CLU_004064_0_0_1; -.
DR InParanoid; D3ZWK4; -.
DR OMA; QVASQHK; -.
DR PhylomeDB; D3ZWK4; -.
DR TreeFam; TF316498; -.
DR Reactome; R-RNO-6804760; Regulation of TP53 Activity through Methylation.
DR PRO; PR:D3ZWK4; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Proteomes; UP000234681; Chromosome 3.
DR Bgee; ENSRNOG00000007044; Expressed in frontal cortex and 4 other tissues.
DR ExpressionAtlas; D3ZWK4; baseline.
DR GO; GO:0000785; C:chromatin; ISO:RGD.
DR GO; GO:0061793; C:chromatin lock complex; ISO:RGD.
DR GO; GO:0000793; C:condensed chromosome; ISO:RGD.
DR GO; GO:0005654; C:nucleoplasm; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR GO; GO:0042393; F:histone binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0035064; F:methylated histone binding; ISS:UniProtKB.
DR GO; GO:0031491; F:nucleosome binding; ISO:RGD.
DR GO; GO:0032093; F:SAM domain binding; ISO:RGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; ISO:RGD.
DR GO; GO:0030097; P:hemopoiesis; ISO:RGD.
DR GO; GO:0031507; P:heterochromatin assembly; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0045652; P:regulation of megakaryocyte differentiation; ISO:RGD.
DR GO; GO:0007088; P:regulation of mitotic nuclear division; ISO:RGD.
DR Gene3D; 1.10.150.50; -; 1.
DR InterPro; IPR004092; Mbt.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR002515; Znf_C2H2C.
DR InterPro; IPR036060; Znf_C2H2C_sf.
DR Pfam; PF02820; MBT; 3.
DR Pfam; PF00536; SAM_1; 1.
DR Pfam; PF01530; zf-C2HC; 1.
DR SMART; SM00561; MBT; 3.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF103637; SSF103637; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR PROSITE; PS51079; MBT; 3.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
DR PROSITE; PS51802; ZF_CCHHC; 1.
PE 3: Inferred from homology;
KW Chromatin regulator; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..826
FT /note="Lethal(3)malignant brain tumor-like protein 1"
FT /id="PRO_0000405832"
FT REPEAT 280..380
FT /note="MBT 1"
FT REPEAT 388..487
FT /note="MBT 2"
FT REPEAT 496..591
FT /note="MBT 3"
FT DOMAIN 757..821
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT ZN_FING 619..662
FT /note="CCHHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT REGION 134..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..460
FT /note="Interaction with monomethylated and dimethylated
FT peptides"
FT /evidence="ECO:0000250"
FT REGION 586..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 663..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..696
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 628
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 633
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 646
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 652
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT SITE 429
FT /note="Mediates recognition of monomethylated and
FT dimethylated peptides"
FT /evidence="ECO:0000250"
FT SITE 432
FT /note="Positioned at the entrance of MBT 2 and is required
FT for recognition of monomethylated and dimethylated
FT peptides"
FT /evidence="ECO:0000250"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y468"
SQ SEQUENCE 826 AA; 91761 MW; 84F73339BC6EE6C7 CRC64;
MEGHSDMEII RAVKGSATGE INVHLVARDS AGSHPHLPTT TFIIPTNAAT LGLPSTALDV
SYPREPVHVG AAERVAGSEP VTATILPQLS TGPGTNSTVR LLDWTGVSAP LAGSGMRFRI
NEYATQNMIE IERPRSPEQR HEGGTAGREA DIQHPDVHKD PQEVIPQEPS VDAGSCKCQT
CGPQQSIGLD VGSSGDRCPQ PFQKRSVIVE NSGCTVASEL IKPMKKRKHK EYQSPSEESE
PEAMKQGKGK DPDREPTPGT SENEEWSRSQ LVSSEKKEGW SWESYLEEQK AVTAPVSLFQ
DSQAVTHNKN GFKLGMKLEG VDPQHPSMYF VLTVAEVCGY RLRLHFDGYS ECHDFWVNAN
SPDIHPAGWF EKTGHKLQPP KGYKEEEFSW SQYLRSTKAQ AAPKHLFVSQ SHSPPPVGFQ
VGMKLEAVDR MNPSLVCVAS VTDVVASRFL VHFDDWDDTY DYWCDASSPY IHPVGWCQKQ
GKPLTPPQDY PDPDSFCWEK YLEETGTSAV PTWAFKVRPP HSFLVNMKLE AVDRRNPALI
RVASVEDVED HRIKLHFDGW SHNYDFWIDA DHPDIHPAGW CSKTGHPLEP PLRPRESSSA
SPGGCPPLSH RSPPHTKTSK YSFHHRKCPT PGCDGSGHVT GKFTAHHCLS GCPLAERNQS
RLKAELSDSE TTARKKNQSN LSPRKKPRHQ GRIGRPPKYR KMPDEDFQAL PPSVVHQSLF
MSTLPTHADR PLSVCWEQHC KLLPGVAGIS ASAVSKWTIE EVFGFVQTLT GSEDQARLFK
EEMIDGEAFL LLTQADIVKI MSVKLGPALK IYNAILMFKN NDDVFK
