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Lethal(3)malignant brain tumor-like protein 1 (H-l(3)mbt) (H-l(3)mbt protein) (L(3)mbt-like) (L(3)mbt protein homolog)

 LMBL1_MOUSE             Reviewed;         826 AA.
A2A5N8; Q5DU20;
08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
20-FEB-2007, sequence version 1.
20-JUN-2018, entry version 97.
RecName: Full=Lethal(3)malignant brain tumor-like protein 1;
Short=H-l(3)mbt;
Short=H-l(3)mbt protein;
Short=L(3)mbt-like;
AltName: Full=L(3)mbt protein homolog;
Name=L3mbtl1; Synonyms=Kiaa0681, L3mbt, L3mbtl;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Fetal brain;
Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene.
The complete nucleotide sequences of mouse KIAA-homologous cDNAs
identified by screening of terminal sequences of cDNA clones randomly
sampled from size-fractionated libraries.";
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
PubMed=20592034; DOI=10.1074/jbc.M110.115410;
Qin J., Van Buren D., Huang H.S., Zhong L., Mostoslavsky R.,
Akbarian S., Hock H.;
"Chromatin protein L3MBTL1 is dispensable for development and tumor
suppression in mice.";
J. Biol. Chem. 285:27767-27775(2010).
-!- FUNCTION: Polycomb group (PcG) protein that specifically
recognizes and binds mono- and dimethyllysine residues on target
proteins, therey acting as a 'reader' of a network of post-
translational modifications. PcG proteins maintain the
transcriptionally repressive state of genes: acts as a chromatin
compaction factor by recognizing and binding mono- and
dimethylated histone H1b/HIST1H1E at 'Lys-26' (H1bK26me1 and
H1bK26me2) and histone H4 at 'Lys-20' (H4K20me1 and H4K20me2),
leading to condense chromatin and repress transcription.
Recognizes and binds p53/TP53 monomethylated at 'Lys-382', leading
to repress p53/TP53-target genes. Also recognizes and binds RB1/RB
monomethylated at 'Lys-860'. Participates in the ETV6-mediated
repression. Probably plays a role in cell proliferation.
Overexpression induces multinucleated cells, suggesting that it is
required to accomplish normal mitosis (By similarity).
{ECO:0000250}.
-!- SUBUNIT: Homodimer. Interacts with RB1/RB (when monomethylated at
'Lys-860'). Interacts with p53/TP53 (when monomethylated at 'Lys-
382'). Interacts with CBX3, ETV6, KMT5A and VCP/p97 (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Excluded from
the nucleolus. Does not colocalizes with the PcG protein BMI1,
suggesting that these two proteins do not belong to the same
complex (By similarity). {ECO:0000250}.
-!- TISSUE SPECIFICITY: Highly expressed in brain, testis, eyes, and
ES cells. {ECO:0000269|PubMed:20592034}.
-!- DOMAIN: The MBT repeat 2 specifically recognizes and binds
monomethylated and dimethylated proteins. In contrast, it does not
bind trimethylated proteins. The MBT repeat 1 does not bind
methylated peptides but inserts a proline ring in a Pro-Ser-
Ser/Thr sequence context (By similarity). {ECO:0000250}.
-!- PTM: Ubiquitinated in a VCP/p97-dependent way following DNA
damage, leading to its removal from DNA damage sites, promoting
accessibility of H4K20me2 mark for DNA repair protein TP53BP1,
which is then recruited to DNA damage sites. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: No visible phenotype. Mice develop and
reproduc normally. Mice were followed for more than 2 years,
without any alteration in normal lifespan or survival with or
without sublethal irradiation. {ECO:0000269|PubMed:20592034}.
-----------------------------------------------------------------------
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EMBL; AK220350; BAD90413.1; -; mRNA.
EMBL; AL606473; CAM20950.1; -; Genomic_DNA.
EMBL; AL591584; CAM20950.1; JOINED; Genomic_DNA.
EMBL; AL591584; CAM21343.1; -; Genomic_DNA.
EMBL; AL606473; CAM21343.1; JOINED; Genomic_DNA.
EMBL; CH466551; EDL06309.1; -; Genomic_DNA.
CCDS; CCDS38314.1; -.
RefSeq; NP_001074807.1; NM_001081338.1.
RefSeq; XP_011237848.1; XM_011239546.2.
UniGene; Mm.187086; -.
ProteinModelPortal; A2A5N8; -.
SMR; A2A5N8; -.
ComplexPortal; CPX-470; L3MBTL1 complex.
STRING; 10090.ENSMUSP00000044038; -.
iPTMnet; A2A5N8; -.
PhosphoSitePlus; A2A5N8; -.
PaxDb; A2A5N8; -.
PRIDE; A2A5N8; -.
Ensembl; ENSMUST00000035751; ENSMUSP00000044038; ENSMUSG00000035576.
GeneID; 241764; -.
KEGG; mmu:241764; -.
UCSC; uc008nsd.1; mouse.
CTD; 26013; -.
MGI; MGI:2676663; L3mbtl1.
eggNOG; KOG3766; Eukaryota.
eggNOG; ENOG410Y4AQ; LUCA.
GeneTree; ENSGT00760000119024; -.
HOGENOM; HOG000231019; -.
HOVERGEN; HBG071375; -.
InParanoid; A2A5N8; -.
OMA; RFTAHYC; -.
OrthoDB; EOG091G01BW; -.
PhylomeDB; A2A5N8; -.
TreeFam; TF316498; -.
Reactome; R-MMU-6804760; Regulation of TP53 Activity through Methylation.
PRO; PR:A2A5N8; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000035576; -.
ExpressionAtlas; A2A5N8; baseline and differential.
GO; GO:0000785; C:chromatin; ISS:UniProtKB.
GO; GO:0000793; C:condensed chromosome; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
GO; GO:0003700; F:DNA binding transcription factor activity; IEA:InterPro.
GO; GO:0042393; F:histone binding; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0035064; F:methylated histone binding; ISS:UniProtKB.
GO; GO:0031493; F:nucleosomal histone binding; ISS:UniProtKB.
GO; GO:0031491; F:nucleosome binding; ISS:UniProtKB.
GO; GO:0032093; F:SAM domain binding; ISO:MGI.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0006325; P:chromatin organization; ISS:UniProtKB.
GO; GO:0030097; P:hemopoiesis; ISS:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0040029; P:regulation of gene expression, epigenetic; NAS:UniProtKB.
GO; GO:0045652; P:regulation of megakaryocyte differentiation; ISS:UniProtKB.
GO; GO:0007088; P:regulation of mitotic nuclear division; ISS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR004092; Mbt.
InterPro; IPR001660; SAM.
InterPro; IPR013761; SAM/pointed_sf.
InterPro; IPR002515; Znf_C2HC.
InterPro; IPR036060; Znf_C2HC_sf.
Pfam; PF02820; MBT; 3.
Pfam; PF00536; SAM_1; 1.
Pfam; PF01530; zf-C2HC; 1.
SMART; SM00561; MBT; 3.
SMART; SM00454; SAM; 1.
SUPFAM; SSF103637; SSF103637; 1.
SUPFAM; SSF47769; SSF47769; 1.
PROSITE; PS51079; MBT; 3.
PROSITE; PS50105; SAM_DOMAIN; 1.
PROSITE; PS51802; ZF_CCHHC; 1.
2: Evidence at transcript level;
Chromatin regulator; Complete proteome; Metal-binding; Nucleus;
Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 826 Lethal(3)malignant brain tumor-like
protein 1.
/FTId=PRO_0000405831.
REPEAT 280 380 MBT 1.
REPEAT 388 487 MBT 2.
REPEAT 496 591 MBT 3.
DOMAIN 757 821 SAM. {ECO:0000255|PROSITE-
ProRule:PRU00184}.
ZN_FING 619 662 CCHHC-type. {ECO:0000255|PROSITE-
ProRule:PRU01143}.
REGION 453 460 Interaction with monomethylated and
dimethylated peptides. {ECO:0000250}.
SITE 429 429 Mediates recognition of monomethylated
and dimethylated peptides. {ECO:0000250}.
SITE 432 432 Positioned at the entrance of MBT 2 and
is required for recognition of
monomethylated and dimethylated peptides.
{ECO:0000250}.
MOD_RES 136 136 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y468}.
CONFLICT 824 824 A -> V (in Ref. 1; BAD90413).
{ECO:0000305}.
SEQUENCE 826 AA; 91781 MW; F27CE3D490434A44 CRC64;
MEGHTDMEIL RTVKGSSTGE VNVHLVARDS AGPHPQLPTT AFIIPTNAAT LGLPSTALDV
PYPREPVHVG ALERVAGSEP VTATILPQLS TGTGTNSTVR LLDWTGVSAP LPGSGMRFRI
NEYAPLNMIG VERPRSPEQR HEGGMARRDA GIQHPDVHQD RQDITSLEPP VDASSCKCQA
CGPQQSSGLD VGSSGDRCSQ PFQKRSVIVE NSGCTIASEL LKPMKKRKHK EYQSPSEESE
PEAVKQGEGK DAEREPTPST PENEEWSRSQ LVSSEKKDGW SWESYLEEQK AVTAPVSLFQ
DSQAVTHNKN GFKLGMKLEG IDPQHPSMYF ILTVAEVCGY RLRLHFDGYS ECHDFWVNAN
SPDIHPAGWF EKTGHKLQLP KGYKEEEFSW SQYLRSTKAQ AAPKHLFVSQ SHSTPPVGFQ
VGMKLEAVDR MNPSLVCVAS VTDVVDSRFL VHFDDWGDTY DYWCDPSSPY IHPVGWCQKQ
GKPLTPPQDY PDPDSFCWEK YLEETGTSAV PNWAFKVRPP HSFLVNMKLE AVDRRNPALI
RVASVEDVED HRIKLHFDGW SHNYDFWIDA DHPDIHPAGW CSKTGHPLEP PLRPRESSSV
SPGGCPPLSH RSPPHTKTSK YNFHHRKCPT PGCDGSGHVT GKFTAHHCLS GCPLAEKNQS
RLKAELSDSE TAARKKNPSN LSPRKKPRHQ GRIGRPPKYR KIPEEDLQAL PPSVVHQSLF
MSTLPTHADR PLSVCWEQHC KLLPGVAGIS ASTVSKWTIE EVFGFVQTLT GSEDQARLFK
DEMIDGEAFL LLTQADIVKI MSVKLGPALK IYNAILMFKN TDDAFK


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