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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;         752 AA.
Q9Y468; B4DRC9; E1P5W7; Q5H8Y8; Q5H8Y9; Q8IUV7; Q9H1E6; Q9H1G5;
Q9UG06; Q9UJB9; Q9Y4C9;
19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
08-MAR-2011, sequence version 3.
22-NOV-2017, entry version 183.
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-49.
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 215-752 (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-248; PHE-272; ASP-355; PHE-379; ASP-459 AND PHE-483.
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-49, 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 197-527.
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 206-519 IN COMPLEX WITH
MONOMETHYLATED AND DIMETHYLATED PEPTIDES, DOMAIN MBT REPEAT, AND
MUTAGENESIS OF ASP-355 AND ASN-358.
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 200-530 IN COMPLEX WITH
DIMETHYLATED HISTONE H4, AND MUTAGENESIS OF ASP-355 AND CYS-363.
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 191-530 IN COMPLEX WITH
MONOMETHYLATED PEPTIDE, FUNCTION, INTERACTION WITH TP53, AND
MUTAGENESIS OF ASP-355; ASN-358; PHE-379; TRP-382 AND TYR-386.
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 200-522.
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=4;
IsoId=Q9Y468-4; Sequence=Displayed;
Name=1; Synonyms=mbt-I;
IsoId=Q9Y468-1; Sequence=VSP_003903;
Note=Variant in position: 759:H->R (dbSNP:rs6030948).;
Name=2; Synonyms=mbt-II;
IsoId=Q9Y468-2; Sequence=VSP_003902;
Name=3;
IsoId=Q9Y468-3; Sequence=VSP_003901, VSP_003902;
Name=5;
IsoId=Q9Y468-5; Sequence=VSP_040719, VSP_003903;
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=CAI23042.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAI42317.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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; CAI23043.1; -; Genomic_DNA.
EMBL; Z98752; CAI23043.1; JOINED; Genomic_DNA.
EMBL; Z98752; CAC16800.1; -; Genomic_DNA.
EMBL; Z98752; CAC18508.1; -; Genomic_DNA.
EMBL; Z98752; CAI42318.1; -; Genomic_DNA.
EMBL; AL031681; CAI42318.1; JOINED; Genomic_DNA.
EMBL; AL031681; CAI23042.1; ALT_SEQ; Genomic_DNA.
EMBL; Z98752; CAI23042.1; JOINED; Genomic_DNA.
EMBL; Z98752; CAI42317.1; ALT_SEQ; Genomic_DNA.
EMBL; AL031681; CAI42317.1; JOINED; 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=197-527.
PDB; 1OZ2; X-ray; 1.55 A; A=197-527.
PDB; 1OZ3; X-ray; 1.85 A; A/B/C=197-527.
PDB; 2PQW; X-ray; 2.00 A; A=200-522.
PDB; 2RHI; X-ray; 1.66 A; A=197-526.
PDB; 2RHU; X-ray; 1.90 A; A=206-519.
PDB; 2RHX; X-ray; 2.10 A; A=197-526.
PDB; 2RHY; X-ray; 1.90 A; A=206-519.
PDB; 2RHZ; X-ray; 2.20 A; A=206-519.
PDB; 2RI2; X-ray; 2.20 A; A=206-519.
PDB; 2RI3; X-ray; 2.00 A; A=206-519.
PDB; 2RI5; X-ray; 2.00 A; A=206-519.
PDB; 2RJC; X-ray; 2.00 A; A/B/C=200-530.
PDB; 2RJD; X-ray; 1.65 A; A=200-530.
PDB; 2RJE; X-ray; 1.86 A; A/B/C=200-530.
PDB; 2RJF; X-ray; 2.05 A; A/C/E=200-530.
PDB; 3OQ5; X-ray; 2.50 A; A/B/C=191-530.
PDB; 3P8H; X-ray; 2.55 A; A/B/C=200-522.
PDB; 3UWN; X-ray; 2.15 A; A=200-530.
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; -.
ProteinModelPortal; Q9Y468; -.
SMR; Q9Y468; -.
BioGrid; 117486; 46.
DIP; DIP-29628N; -.
IntAct; Q9Y468; 64.
MINT; MINT-2830196; -.
STRING; 9606.ENSP00000398516; -.
BindingDB; Q9Y468; -.
ChEMBL; CHEMBL1287622; -.
DrugBank; DB03814; 2-(N-Morpholino)-Ethanesulfonic Acid.
iPTMnet; Q9Y468; -.
PhosphoSitePlus; Q9Y468; -.
BioMuta; L3MBTL1; -.
DMDM; 325511398; -.
PaxDb; Q9Y468; -.
PeptideAtlas; Q9Y468; -.
PRIDE; Q9Y468; -.
DNASU; 26013; -.
Ensembl; ENST00000373135; ENSP00000362227; ENSG00000185513. [Q9Y468-1]
Ensembl; ENST00000418998; ENSP00000398516; ENSG00000185513. [Q9Y468-5]
Ensembl; ENST00000427442; ENSP00000402107; ENSG00000185513. [Q9Y468-5]
GeneID; 26013; -.
KEGG; hsa:26013; -.
UCSC; uc002xkl.4; human. [Q9Y468-4]
CTD; 26013; -.
DisGeNET; 26013; -.
EuPathDB; HostDB:ENSG00000185513.14; -.
GeneCards; L3MBTL1; -.
H-InvDB; HIX0015827; -.
HGNC; HGNC:15905; L3MBTL1.
HPA; HPA056389; -.
MIM; 608802; gene.
neXtProt; NX_Q9Y468; -.
OpenTargets; ENSG00000185513; -.
PharmGKB; PA30260; -.
eggNOG; KOG3766; Eukaryota.
eggNOG; ENOG410Y4AQ; LUCA.
GeneTree; ENSGT00760000119024; -.
HOVERGEN; HBG071375; -.
InParanoid; Q9Y468; -.
OMA; CQACGPQ; -.
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: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:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0006325; P:chromatin organization; IDA:UniProtKB.
GO; GO:0016569; P:covalent chromatin modification; IEA:UniProtKB-KW.
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; 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.
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 1 752 Lethal(3)malignant brain tumor-like
protein 1.
/FTId=PRO_0000084452.
REPEAT 206 306 MBT 1.
REPEAT 314 413 MBT 2.
REPEAT 422 517 MBT 3.
DOMAIN 683 747 SAM. {ECO:0000255|PROSITE-
ProRule:PRU00184}.
ZN_FING 545 588 CCHHC-type. {ECO:0000255|PROSITE-
ProRule:PRU01143}.
REGION 379 386 Interaction with monomethylated and
dimethylated peptides.
SITE 355 355 Mediates recognition of monomethylated
and dimethylated peptides.
SITE 358 358 Positioned at the entrance of MBT 2 and
is required for recognition of
monomethylated and dimethylated peptides.
MOD_RES 49 49 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 348 Missing (in isoform 3).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_003901.
VAR_SEQ 1 30 MRRREGHGTDSEMGQGPVRESQSSDPPALQ -> MHLVAGD
SPGSGPHLPATAFIIPASSATLGLPSSALDVSCFPREPIHV
GAPEQVAGCEPVSATVLPQLSAGPASSSTSTVRLLEWTEAA
APPPGGGLR (in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_040719.
VAR_SEQ 709 752 MIDGEAFLLLTQADIVKIMSVKLGPALKIYNAILMFKNADD
TLK -> ARIVRVTHVSGKTLVWTVAQLGDLVCSDHLQEGK
GILETGVHSLLCSLPTHLLAKLSFASDSQY (in
isoform 1 and isoform 5).
{ECO:0000303|PubMed:10445843,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_003903.
VAR_SEQ 709 752 MIDGEAFLLLTQADIVKIMSVKLGPALKIYNAILMFKNADD
TLK -> VRCKCRVGDRAGVTVLKTAGSRCPPQRHFC (in
isoform 2 and isoform 3).
{ECO:0000303|PubMed:10445843,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_003902.
VARIANT 49 49 S -> T (in dbSNP:rs17857202).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_051097.
VARIANT 479 479 I -> M (in dbSNP:rs6017104).
/FTId=VAR_051098.
MUTAGEN 248 248 D->N: Does not affect binding to
monomethylated and dimethylated peptides.
{ECO:0000269|PubMed:17540172}.
MUTAGEN 272 272 F->A: Does not affect binding to
monomethylated and dimethylated peptides.
{ECO:0000269|PubMed:17540172}.
MUTAGEN 355 355 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 355 355 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 358 358 N->A: Abolishes binding to monomethylated
and dimethylated peptides.
{ECO:0000269|PubMed:18042461,
ECO:0000269|PubMed:20870725}.
MUTAGEN 358 358 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 363 363 C->F,R: Strongly impairs binding to
monomethylated and dimethylated peptides.
{ECO:0000269|PubMed:18026117}.
MUTAGEN 379 379 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 382 382 W->L: Abolishes binding to p53/TP53
monomethylated at 'Lys-382'.
{ECO:0000269|PubMed:20870725}.
MUTAGEN 386 386 Y->L: Abolishes binding to p53/TP53
monomethylated at 'Lys-382'.
{ECO:0000269|PubMed:20870725}.
MUTAGEN 459 459 D->N: Does not affect binding to
monomethylated and dimethylated peptides.
{ECO:0000269|PubMed:17540172}.
MUTAGEN 483 483 F->A: Does not affect binding to
monomethylated and dimethylated peptides.
{ECO:0000269|PubMed:17540172}.
CONFLICT 186 186 T -> A (in Ref. 2; BAG61241).
{ECO:0000305}.
CONFLICT 305 305 P -> L (in Ref. 1; AAC69438).
{ECO:0000305}.
CONFLICT 320 321 LR -> MC (in Ref. 1; AAC69438).
{ECO:0000305}.
CONFLICT 332 332 L -> M (in Ref. 1; AAC69438).
{ECO:0000305}.
CONFLICT 493 493 W -> R (in Ref. 2; BAG61241).
{ECO:0000305}.
CONFLICT 595 595 S -> P (in Ref. 1; AAC69438).
{ECO:0000305}.
HELIX 208 215 {ECO:0000244|PDB:1OZ2}.
HELIX 222 224 {ECO:0000244|PDB:1OZ2}.
HELIX 227 230 {ECO:0000244|PDB:1OZ2}.
STRAND 243 248 {ECO:0000244|PDB:1OZ2}.
STRAND 251 264 {ECO:0000244|PDB:1OZ2}.
STRAND 267 272 {ECO:0000244|PDB:1OZ2}.
HELIX 277 279 {ECO:0000244|PDB:1OZ2}.
STRAND 281 284 {ECO:0000244|PDB:1OZ2}.
STRAND 288 291 {ECO:0000244|PDB:2RJD}.
HELIX 295 299 {ECO:0000244|PDB:1OZ2}.
HELIX 311 313 {ECO:0000244|PDB:1OZ2}.
HELIX 316 323 {ECO:0000244|PDB:1OZ2}.
HELIX 330 332 {ECO:0000244|PDB:1OZ2}.
STRAND 350 354 {ECO:0000244|PDB:1OZ2}.
TURN 356 359 {ECO:0000244|PDB:2RI5}.
STRAND 362 371 {ECO:0000244|PDB:1OZ2}.
STRAND 374 379 {ECO:0000244|PDB:1OZ2}.
HELIX 384 386 {ECO:0000244|PDB:1OZ2}.
STRAND 388 390 {ECO:0000244|PDB:1OZ2}.
HELIX 402 406 {ECO:0000244|PDB:1OZ2}.
HELIX 419 421 {ECO:0000244|PDB:1OZ2}.
HELIX 424 431 {ECO:0000244|PDB:1OZ2}.
HELIX 438 440 {ECO:0000244|PDB:1OZ2}.
STRAND 454 458 {ECO:0000244|PDB:1OZ2}.
STRAND 460 462 {ECO:0000244|PDB:1OZ2}.
STRAND 466 474 {ECO:0000244|PDB:1OZ2}.
STRAND 476 483 {ECO:0000244|PDB:1OZ2}.
HELIX 488 490 {ECO:0000244|PDB:1OZ2}.
STRAND 492 495 {ECO:0000244|PDB:1OZ2}.
HELIX 506 510 {ECO:0000244|PDB:1OZ2}.
SEQUENCE 752 AA; 83884 MW; 6B92FF852FF98CB4 CRC64;
MRRREGHGTD SEMGQGPVRE SQSSDPPALQ FRISEYKPLN MAGVEQPPSP ELRQEGVTEY
EDGGAPAGDG EAGPQQAEDH PQNPPEDPNQ DPPEDDSTCQ CQACGPHQAA GPDLGSSNDG
CPQLFQERSV IVENSSGSTS ASELLKPMKK RKRREYQSPS EEESEPEAME KQEEGKDPEG
QPTASTPESE EWSSSQPATG EKKECWSWES YLEEQKAITA PVSLFQDSQA VTHNKNGFKL
GMKLEGIDPQ HPSMYFILTV AEVCGYRLRL HFDGYSECHD FWVNANSPDI HPAGWFEKTG
HKLQPPKGYK EEEFSWSQYL RSTRAQAAPK HLFVSQSHSP PPLGFQVGMK LEAVDRMNPS
LVCVASVTDV VDSRFLVHFD NWDDTYDYWC DPSSPYIHPV GWCQKQGKPL TPPQDYPDPD
NFCWEKYLEE TGASAVPTWA FKVRPPHSFL VNMKLEAVDR RNPALIRVAS VEDVEDHRIK
IHFDGWSHGY DFWIDADHPD IHPAGWCSKT GHPLQPPLGP REPSSASPGG CPPLSYRSLP
HTRTSKYSFH HRKCPTPGCD GSGHVTGKFT AHHCLSGCPL AERNQSRLKA ELSDSEASAR
KKNLSGFSPR KKPRHHGRIG RPPKYRKIPQ EDFQTLTPDV VHQSLFMSAL SAHPDRSLSV
CWEQHCKLLP GVAGISASTV AKWTIDEVFG FVQTLTGCED QARLFKDEMI DGEAFLLLTQ
ADIVKIMSVK LGPALKIYNA ILMFKNADDT LK


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