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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) (L3MBTL1)

 LMBL1_HUMAN             Reviewed;         840 AA.
Q9Y468; B4DRC9; E1P5W7; Q5H8Y8; Q5H8Y9; Q8IUV7; Q9H1E6; Q9H1G5;
Q9UG06; Q9UJB9; Q9Y4C9;
19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
28-MAR-2018, sequence version 4.
20-JUN-2018, entry version 188.
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;
AltName: Full=L3MBTL1;
Name=L3MBTL1; Synonyms=KIAA0681, L3MBT, L3MBTL;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION,
AND TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=10445843; DOI=10.1038/sj.onc.1202732;
Koga H., Matsui S., Hirota T., Takebayashi S., Okumura K., Saya H.;
"A human homolog of Drosophila lethal(3)malignant brain tumor
(l(3)mbt) protein associates with condensed mitotic chromosomes.";
Oncogene 18:3799-3809(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Uterus;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
THR-117.
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 283-840 (ISOFORM 4).
TISSUE=Brain;
PubMed=9734811; DOI=10.1093/dnares/5.3.169;
Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. X.
The complete sequences of 100 new cDNA clones from brain which can
code for large proteins in vitro.";
DNA Res. 5:169-176(1998).
[7]
INTERACTION WITH ETV6.
PubMed=12588862; DOI=10.1074/jbc.M300592200;
Boccuni P., MacGrogan D., Scandura J.M., Nimer S.D.;
"The human L(3)MBT Polycomb group protein is a transcriptional
repressor and interacts physically and functionally with TEL (ETV6).";
J. Biol. Chem. 278:15412-15420(2003).
[8]
IMPRINTING.
PubMed=15123827; DOI=10.1073/pnas.0308195101;
Li J., Bench A.J., Vassiliou G.S., Fourouclas N., Ferguson-Smith A.C.,
Green A.R.;
"Imprinting of the human L3MBTL gene, a polycomb family member located
in a region of chromosome 20 deleted in human myeloid malignancies.";
Proc. Natl. Acad. Sci. U.S.A. 101:7341-7346(2004).
[9]
FUNCTION, INTERACTION WITH CBX3 AND HISTONES, AND MUTAGENESIS OF
ASP-316; PHE-340; ASP-423; PHE-447; ASP-527 AND PHE-551.
PubMed=17540172; DOI=10.1016/j.cell.2007.03.048;
Trojer P., Li G., Sims R.J. III, Vaquero A., Kalakonda N., Boccuni P.,
Lee D., Erdjument-Bromage H., Tempst P., Nimer S.D., Wang Y.H.,
Reinberg D.;
"L3MBTL1, a histone-methylation-dependent chromatin lock.";
Cell 129:915-928(2007).
[10]
FUNCTION, AND INTERACTION WITH KMT5A.
PubMed=18408754; DOI=10.1038/onc.2008.67;
Kalakonda N., Fischle W., Boccuni P., Gurvich N., Hoya-Arias R.,
Zhao X., Miyata Y., Macgrogan D., Zhang J., Sims J.K., Rice J.C.,
Nimer S.D.;
"Histone H4 lysine 20 monomethylation promotes transcriptional
repression by L3MBTL1.";
Oncogene 27:4293-4304(2008).
[11]
FUNCTION, AND INTERACTION WITH RB1.
PubMed=20870719; DOI=10.1074/jbc.M110.137612;
Saddic L.A., West L.E., Aslanian A., Yates J.R. III, Rubin S.M.,
Gozani O., Sage J.;
"Methylation of the retinoblastoma tumor suppressor by SMYD2.";
J. Biol. Chem. 285:37733-37740(2010).
[12]
UBIQUITINATION, AND INTERACTION WITH VCP.
PubMed=22120668; DOI=10.1038/nsmb.2188;
Acs K., Luijsterburg M.S., Ackermann L., Salomons F.A., Hoppe T.,
Dantuma N.P.;
"The AAA-ATPase VCP/p97 promotes 53BP1 recruitment by removing L3MBTL1
from DNA double-strand breaks.";
Nat. Struct. Mol. Biol. 18:1345-1350(2011).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[14]
X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 265-595.
PubMed=12842041; DOI=10.1016/S0969-2126(03)00127-8;
Wang W.K., Tereshko V., Boccuni P., MacGrogan D., Nimer S.D.,
Patel D.J.;
"Malignant brain tumor repeats: a three-leaved propeller architecture
with ligand/peptide binding pockets.";
Structure 11:775-789(2003).
[15]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 274-587 IN COMPLEX WITH
MONOMETHYLATED AND DIMETHYLATED PEPTIDES, DOMAIN MBT REPEAT, AND
MUTAGENESIS OF ASP-423 AND ASN-426.
PubMed=18042461; DOI=10.1016/j.molcel.2007.10.023;
Li H., Fischle W., Wang W., Duncan E.M., Liang L., Murakami-Ishibe S.,
Allis C.D., Patel D.J.;
"Structural basis for lower lysine methylation state-specific readout
by MBT repeats of L3MBTL1 and an engineered PHD finger.";
Mol. Cell 28:677-691(2007).
[16]
X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 268-598 IN COMPLEX WITH
DIMETHYLATED HISTONE H4, AND MUTAGENESIS OF ASP-423 AND CYS-431.
PubMed=18026117; DOI=10.1038/nsmb1340;
Min J., Allali-Hassani A., Nady N., Qi C., Ouyang H., Liu Y.,
MacKenzie F., Vedadi M., Arrowsmith C.H.;
"L3MBTL1 recognition of mono- and dimethylated histones.";
Nat. Struct. Mol. Biol. 14:1229-1230(2007).
[17]
ERRATUM.
Min J., Allali-Hassani A., Nady N., Qi C., Ouyang H., Liu Y.,
MacKenzie F., Vedadi M., Arrowsmith C.H.;
Nat. Struct. Mol. Biol. 15:114-114(2008).
[18]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 259-598 IN COMPLEX WITH
MONOMETHYLATED PEPTIDE, FUNCTION, INTERACTION WITH TP53, AND
MUTAGENESIS OF ASP-423; ASN-426; PHE-447; TRP-450 AND TYR-454.
PubMed=20870725; DOI=10.1074/jbc.M110.139527;
West L.E., Roy S., Lachmi-Weiner K., Hayashi R., Shi X., Appella E.,
Kutateladze T.G., Gozani O.;
"The MBT repeats of L3MBTL1 link SET8-mediated p53 methylation at
lysine 382 to target gene repression.";
J. Biol. Chem. 285:37725-37732(2010).
[19]
X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 268-590.
Structural genomics consortium (SGC);
"Small molecule ligands of methyl-lysine binding proteins.";
Submitted (NOV-2010) to the PDB data bank.
-!- 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.
{ECO:0000269|PubMed:17540172, ECO:0000269|PubMed:18408754,
ECO:0000269|PubMed:20870719, ECO:0000269|PubMed:20870725}.
-!- 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.
{ECO:0000269|PubMed:12588862, ECO:0000269|PubMed:17540172,
ECO:0000269|PubMed:18026117, ECO:0000269|PubMed:18042461,
ECO:0000269|PubMed:18408754, ECO:0000269|PubMed:20870719,
ECO:0000269|PubMed:20870725, ECO:0000269|PubMed:22120668}.
-!- INTERACTION:
P10412:HIST1H1E; NbExp=7; IntAct=EBI-1265089, EBI-358163;
P68431:HIST1H3D; NbExp=2; IntAct=EBI-1265089, EBI-79722;
P62805:HIST2H4B; NbExp=4; IntAct=EBI-1265089, EBI-302023;
P49736:MCM2; NbExp=2; IntAct=EBI-1265089, EBI-374819;
P33992:MCM5; NbExp=2; IntAct=EBI-1265089, EBI-359410;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10445843}.
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.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=5;
IsoId=Q9Y468-5; Sequence=Displayed;
Name=1; Synonyms=mbt-I;
IsoId=Q9Y468-1; Sequence=VSP_059458;
Note=Variant in position: 759:H->R (dbSNP:rs6030948).;
Name=2; Synonyms=mbt-II;
IsoId=Q9Y468-2; Sequence=VSP_059458, VSP_059459;
Name=3;
IsoId=Q9Y468-3; Sequence=VSP_003901, VSP_059459;
Name=4;
IsoId=Q9Y468-4; Sequence=VSP_059458, VSP_059460;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed. Expression is reduced in
colorectal cancer cell line SW480 and promyelocytic leukemia cell
line HL-60. {ECO:0000269|PubMed:10445843}.
-!- DEVELOPMENTAL STAGE: In interphase cells, it is scattered
throughout the nucleoplasm. In mitotic cells, it strongly
associates with condensed chromosomes from the prophase to
telophase.
-!- 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. {ECO:0000269|PubMed:18042461}.
-!- 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:0000269|PubMed:22120668}.
-!- MISCELLANEOUS: The L3MBTL1 locus is imprinted. Paternal inherited
gene is expressed, while the maternal inherited gene is silenced.
-!- SEQUENCE CAUTION:
Sequence=EAW75958.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=EAW75961.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=EAW75962.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; U89358; AAC69438.1; -; mRNA.
EMBL; AK299199; BAG61241.1; -; mRNA.
EMBL; AL110279; CAB53714.1; -; mRNA.
EMBL; AL031681; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z98752; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471077; EAW75958.1; ALT_SEQ; Genomic_DNA.
EMBL; CH471077; EAW75961.1; ALT_SEQ; Genomic_DNA.
EMBL; CH471077; EAW75962.1; ALT_SEQ; Genomic_DNA.
EMBL; BC039820; AAH39820.1; -; mRNA.
EMBL; AB014581; BAA31656.1; -; mRNA.
CCDS; CCDS13319.1; -. [Q9Y468-1]
CCDS; CCDS46602.2; -. [Q9Y468-5]
PIR; T14794; T14794.
RefSeq; NP_056293.4; NM_015478.6. [Q9Y468-1]
RefSeq; NP_115479.4; NM_032107.4. [Q9Y468-5]
UniGene; Hs.709356; -.
UniGene; Hs.736988; -.
PDB; 1OYX; X-ray; 1.85 A; A/B/C=265-595.
PDB; 1OZ2; X-ray; 1.55 A; A=265-595.
PDB; 1OZ3; X-ray; 1.85 A; A/B/C=265-595.
PDB; 2PQW; X-ray; 2.00 A; A=268-590.
PDB; 2RHI; X-ray; 1.66 A; A=265-594.
PDB; 2RHU; X-ray; 1.90 A; A=274-587.
PDB; 2RHX; X-ray; 2.10 A; A=265-594.
PDB; 2RHY; X-ray; 1.90 A; A=274-587.
PDB; 2RHZ; X-ray; 2.20 A; A=274-587.
PDB; 2RI2; X-ray; 2.20 A; A=274-587.
PDB; 2RI3; X-ray; 2.00 A; A=274-587.
PDB; 2RI5; X-ray; 2.00 A; A=274-587.
PDB; 2RJC; X-ray; 2.00 A; A/B/C=268-598.
PDB; 2RJD; X-ray; 1.65 A; A=268-598.
PDB; 2RJE; X-ray; 1.86 A; A/B/C=268-598.
PDB; 2RJF; X-ray; 2.05 A; A/C/E=268-598.
PDB; 3OQ5; X-ray; 2.50 A; A/B/C=259-598.
PDB; 3P8H; X-ray; 2.55 A; A/B/C=268-590.
PDB; 3UWN; X-ray; 2.15 A; A=268-598.
PDB; 6BYB; X-ray; 1.74 A; A=200-522.
PDBsum; 1OYX; -.
PDBsum; 1OZ2; -.
PDBsum; 1OZ3; -.
PDBsum; 2PQW; -.
PDBsum; 2RHI; -.
PDBsum; 2RHU; -.
PDBsum; 2RHX; -.
PDBsum; 2RHY; -.
PDBsum; 2RHZ; -.
PDBsum; 2RI2; -.
PDBsum; 2RI3; -.
PDBsum; 2RI5; -.
PDBsum; 2RJC; -.
PDBsum; 2RJD; -.
PDBsum; 2RJE; -.
PDBsum; 2RJF; -.
PDBsum; 3OQ5; -.
PDBsum; 3P8H; -.
PDBsum; 3UWN; -.
PDBsum; 6BYB; -.
ProteinModelPortal; Q9Y468; -.
SMR; Q9Y468; -.
BioGrid; 117486; 46.
ComplexPortal; CPX-469; L3MBTL1 complex.
DIP; DIP-29628N; -.
IntAct; Q9Y468; 64.
MINT; Q9Y468; -.
STRING; 9606.ENSP00000398516; -.
BindingDB; Q9Y468; -.
ChEMBL; CHEMBL1287622; -.
DrugBank; DB03814; 2-(N-Morpholino)-Ethanesulfonic Acid.
iPTMnet; Q9Y468; -.
PhosphoSitePlus; Q9Y468; -.
BioMuta; L3MBTL1; -.
DMDM; 325511398; -.
EPD; Q9Y468; -.
PaxDb; Q9Y468; -.
PeptideAtlas; Q9Y468; -.
PRIDE; Q9Y468; -.
ProteomicsDB; 86115; -.
ProteomicsDB; 86116; -. [Q9Y468-1]
ProteomicsDB; 86117; -. [Q9Y468-2]
ProteomicsDB; 86118; -. [Q9Y468-3]
ProteomicsDB; 86119; -. [Q9Y468-5]
DNASU; 26013; -.
Ensembl; ENST00000373135; ENSP00000362227; ENSG00000185513. [Q9Y468-1]
Ensembl; ENST00000418998; ENSP00000398516; ENSG00000185513. [Q9Y468-5]
GeneID; 26013; -.
KEGG; hsa:26013; -.
UCSC; uc002xkl.4; human. [Q9Y468-5]
CTD; 26013; -.
DisGeNET; 26013; -.
EuPathDB; HostDB:ENSG00000185513.14; -.
GeneCards; L3MBTL1; -.
H-InvDB; HIX0015827; -.
HGNC; HGNC:15905; L3MBTL1.
HPA; HPA068051; -.
MIM; 608802; gene.
neXtProt; NX_Q9Y468; -.
OpenTargets; ENSG00000185513; -.
PharmGKB; PA30260; -.
eggNOG; KOG3766; Eukaryota.
eggNOG; ENOG410Y4AQ; LUCA.
GeneTree; ENSGT00760000119024; -.
HOVERGEN; HBG071375; -.
InParanoid; Q9Y468; -.
OMA; RFTAHYC; -.
OrthoDB; EOG091G01BW; -.
PhylomeDB; Q9Y468; -.
TreeFam; TF316498; -.
Reactome; R-HSA-6804760; Regulation of TP53 Activity through Methylation.
ChiTaRS; L3MBTL1; human.
EvolutionaryTrace; Q9Y468; -.
GeneWiki; L3MBTL; -.
GenomeRNAi; 26013; -.
PRO; PR:Q9Y468; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000185513; -.
CleanEx; HS_L3MBTL; -.
ExpressionAtlas; Q9Y468; baseline and differential.
Genevisible; Q9Y468; HS.
GO; GO:0000785; C:chromatin; IDA:UniProtKB.
GO; GO:0000793; C:condensed chromosome; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0003700; F:DNA binding transcription factor activity; IEA:InterPro.
GO; GO:0042393; F:histone binding; IPI:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB.
GO; GO:0031493; F:nucleosomal histone binding; IDA:UniProtKB.
GO; GO:0031491; F:nucleosome binding; IDA:UniProtKB.
GO; GO:0032093; F:SAM domain binding; IPI:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0006325; P:chromatin organization; IDA:UniProtKB.
GO; GO:0030097; P:hemopoiesis; IEP:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0051726; P:regulation of cell cycle; NAS:UniProtKB.
GO; GO:0045652; P:regulation of megakaryocyte differentiation; IDA:UniProtKB.
GO; GO:0007088; P:regulation of mitotic nuclear division; IMP:UniProtKB.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR004092; Mbt.
InterPro; IPR002515; Znf_C2HC.
InterPro; IPR036060; Znf_C2HC_sf.
Pfam; PF02820; MBT; 3.
Pfam; PF01530; zf-C2HC; 1.
SMART; SM00561; MBT; 3.
SUPFAM; SSF103637; SSF103637; 1.
PROSITE; PS51079; MBT; 3.
PROSITE; PS50105; SAM_DOMAIN; 1.
PROSITE; PS51802; ZF_CCHHC; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Chromatin regulator;
Complete proteome; Metal-binding; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Repeat; Repressor; Transcription;
Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 840 Lethal(3)malignant brain tumor-like
protein 1.
/FTId=PRO_0000084452.
REPEAT 274 374 MBT 1.
REPEAT 382 481 MBT 2.
REPEAT 490 585 MBT 3.
DOMAIN 751 824 SAM. {ECO:0000255|PROSITE-
ProRule:PRU00184}.
ZN_FING 613 656 CCHHC-type. {ECO:0000255|PROSITE-
ProRule:PRU01143}.
REGION 447 454 Interaction with monomethylated and
dimethylated peptides.
SITE 423 423 Mediates recognition of monomethylated
and dimethylated peptides.
SITE 426 426 Positioned at the entrance of MBT 2 and
is required for recognition of
monomethylated and dimethylated peptides.
MOD_RES 117 117 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 416 Missing (in isoform 3).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_003901.
VAR_SEQ 1 98 MHLVAGDSPGSGPHLPATAFIIPASSATLGLPSSALDVSCF
PREPIHVGAPEQVAGCEPVSATVLPQLSAGPASSSTSTVRL
LEWTEAAAPPPGGGLR -> MRRREGHGTDSEMGQGPVRES
QSSDPPALQ (in isoform 1, isoform 2 and
isoform 4). {ECO:0000303|PubMed:10445843,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9734811}.
/FTId=VSP_059458.
VAR_SEQ 777 840 ARIVRVTHVSGKTLVWTVAQLGDLVCSDHLQEGKGILETGV
HSLLCSLPTHLLAKLSFASDSQY -> VRCKCRVGDRAGVT
VLKTAGSRCPPQRHFC (in isoform 2 and
isoform 3). {ECO:0000303|PubMed:10445843,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_059459.
VAR_SEQ 777 840 ARIVRVTHVSGKTLVWTVAQLGDLVCSDHLQEGKGILETGV
HSLLCSLPTHLLAKLSFASDSQY -> MIDGEAFLLLTQAD
IVKIMSVKLGPALKIYNAILMFKNADDTLK (in
isoform 4). {ECO:0000303|PubMed:9734811}.
/FTId=VSP_059460.
VARIANT 117 117 S -> T (in dbSNP:rs17857202).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_051097.
VARIANT 547 547 I -> M (in dbSNP:rs6017104).
/FTId=VAR_051098.
MUTAGEN 316 316 D->N: Does not affect binding to
monomethylated and dimethylated peptides.
{ECO:0000269|PubMed:17540172}.
MUTAGEN 340 340 F->A: Does not affect binding to
monomethylated and dimethylated peptides.
{ECO:0000269|PubMed:17540172}.
MUTAGEN 423 423 D->A: Abolishes binding to monomethylated
and dimethylated peptides.
{ECO:0000269|PubMed:17540172,
ECO:0000269|PubMed:18026117,
ECO:0000269|PubMed:18042461,
ECO:0000269|PubMed:20870725}.
MUTAGEN 423 423 D->N: Strongly impairs binding to
monomethylated and dimethylated peptides.
Abolishes binding to p53/TP53
monomethylated at 'Lys-382'.
{ECO:0000269|PubMed:17540172,
ECO:0000269|PubMed:18026117,
ECO:0000269|PubMed:18042461,
ECO:0000269|PubMed:20870725}.
MUTAGEN 426 426 N->A: Abolishes binding to monomethylated
and dimethylated peptides.
{ECO:0000269|PubMed:18042461,
ECO:0000269|PubMed:20870725}.
MUTAGEN 426 426 N->Q: Strongly impairs binding to
monomethylated and dimethylated peptides.
Abolishes binding to p53/TP53
monomethylated at 'Lys-382'.
{ECO:0000269|PubMed:18042461,
ECO:0000269|PubMed:20870725}.
MUTAGEN 431 431 C->F,R: Strongly impairs binding to
monomethylated and dimethylated peptides.
{ECO:0000269|PubMed:18026117}.
MUTAGEN 447 447 F->A: Abolishes binding to monomethylated
and dimethylated peptides. Abolishes
binding to p53/TP53 monomethylated at
'Lys-382'. {ECO:0000269|PubMed:17540172,
ECO:0000269|PubMed:20870725}.
MUTAGEN 450 450 W->L: Abolishes binding to p53/TP53
monomethylated at 'Lys-382'.
{ECO:0000269|PubMed:20870725}.
MUTAGEN 454 454 Y->L: Abolishes binding to p53/TP53
monomethylated at 'Lys-382'.
{ECO:0000269|PubMed:20870725}.
MUTAGEN 527 527 D->N: Does not affect binding to
monomethylated and dimethylated peptides.
{ECO:0000269|PubMed:17540172}.
MUTAGEN 551 551 F->A: Does not affect binding to
monomethylated and dimethylated peptides.
{ECO:0000269|PubMed:17540172}.
CONFLICT 254 254 T -> A (in Ref. 2; BAG61241).
{ECO:0000305}.
CONFLICT 373 373 P -> L (in Ref. 1; AAC69438).
{ECO:0000305}.
CONFLICT 388 389 LR -> MC (in Ref. 1; AAC69438).
{ECO:0000305}.
CONFLICT 400 400 L -> M (in Ref. 1; AAC69438).
{ECO:0000305}.
CONFLICT 561 561 W -> R (in Ref. 2; BAG61241).
{ECO:0000305}.
CONFLICT 663 663 S -> P (in Ref. 1; AAC69438).
{ECO:0000305}.
HELIX 276 283 {ECO:0000244|PDB:1OZ2}.
HELIX 290 292 {ECO:0000244|PDB:1OZ2}.
HELIX 295 298 {ECO:0000244|PDB:1OZ2}.
STRAND 311 316 {ECO:0000244|PDB:1OZ2}.
STRAND 319 332 {ECO:0000244|PDB:1OZ2}.
STRAND 335 340 {ECO:0000244|PDB:1OZ2}.
HELIX 345 347 {ECO:0000244|PDB:1OZ2}.
STRAND 349 352 {ECO:0000244|PDB:1OZ2}.
STRAND 356 359 {ECO:0000244|PDB:2RJD}.
HELIX 363 367 {ECO:0000244|PDB:1OZ2}.
HELIX 379 381 {ECO:0000244|PDB:1OZ2}.
HELIX 384 391 {ECO:0000244|PDB:1OZ2}.
HELIX 398 400 {ECO:0000244|PDB:1OZ2}.
STRAND 418 422 {ECO:0000244|PDB:1OZ2}.
TURN 424 427 {ECO:0000244|PDB:2RI5}.
STRAND 430 439 {ECO:0000244|PDB:1OZ2}.
STRAND 442 447 {ECO:0000244|PDB:1OZ2}.
HELIX 452 454 {ECO:0000244|PDB:1OZ2}.
STRAND 456 458 {ECO:0000244|PDB:1OZ2}.
HELIX 470 474 {ECO:0000244|PDB:1OZ2}.
HELIX 487 489 {ECO:0000244|PDB:1OZ2}.
HELIX 492 499 {ECO:0000244|PDB:1OZ2}.
HELIX 506 508 {ECO:0000244|PDB:1OZ2}.
STRAND 522 526 {ECO:0000244|PDB:1OZ2}.
STRAND 528 530 {ECO:0000244|PDB:1OZ2}.
STRAND 534 542 {ECO:0000244|PDB:1OZ2}.
STRAND 544 551 {ECO:0000244|PDB:1OZ2}.
HELIX 556 558 {ECO:0000244|PDB:1OZ2}.
STRAND 560 563 {ECO:0000244|PDB:1OZ2}.
HELIX 574 578 {ECO:0000244|PDB:1OZ2}.
SEQUENCE 840 AA; 92297 MW; 70004D458897CB24 CRC64;
MHLVAGDSPG SGPHLPATAF IIPASSATLG LPSSALDVSC FPREPIHVGA PEQVAGCEPV
SATVLPQLSA GPASSSTSTV RLLEWTEAAA PPPGGGLRFR ISEYKPLNMA GVEQPPSPEL
RQEGVTEYED GGAPAGDGEA GPQQAEDHPQ NPPEDPNQDP PEDDSTCQCQ ACGPHQAAGP
DLGSSNDGCP QLFQERSVIV ENSSGSTSAS ELLKPMKKRK RREYQSPSEE ESEPEAMEKQ
EEGKDPEGQP TASTPESEEW SSSQPATGEK KECWSWESYL EEQKAITAPV SLFQDSQAVT
HNKNGFKLGM KLEGIDPQHP SMYFILTVAE VCGYRLRLHF DGYSECHDFW VNANSPDIHP
AGWFEKTGHK LQPPKGYKEE EFSWSQYLRS TRAQAAPKHL FVSQSHSPPP LGFQVGMKLE
AVDRMNPSLV CVASVTDVVD SRFLVHFDNW DDTYDYWCDP SSPYIHPVGW CQKQGKPLTP
PQDYPDPDNF CWEKYLEETG ASAVPTWAFK VRPPHSFLVN MKLEAVDRRN PALIRVASVE
DVEDHRIKIH FDGWSHGYDF WIDADHPDIH PAGWCSKTGH PLQPPLGPRE PSSASPGGCP
PLSYRSLPHT RTSKYSFHHR KCPTPGCDGS GHVTGKFTAH HCLSGCPLAE RNQSRLKAEL
SDSEASARKK NLSGFSPRKK PRHHGRIGRP PKYRKIPQED FQTLTPDVVH QSLFMSALSA
HPDRSLSVCW EQHCKLLPGV AGISASTVAK WTIDEVFGFV QTLTGCEDQA RLFKDEARIV
RVTHVSGKTL VWTVAQLGDL VCSDHLQEGK GILETGVHSL LCSLPTHLLA KLSFASDSQY


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