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Lethal(3)malignant brain tumor-like protein 2 (H-l(3)mbt-like protein 2) (L(3)mbt-like protein 2)

 LMBL2_HUMAN             Reviewed;         705 AA.
Q969R5; Q8TEN1; Q96SC4; Q9BQI2; Q9UGS4;
10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
18-JUL-2018, entry version 166.
RecName: Full=Lethal(3)malignant brain tumor-like protein 2;
Short=H-l(3)mbt-like protein 2;
Short=L(3)mbt-like protein 2;
Name=L3MBTL2;
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).
PubMed=11682070; DOI=10.1016/S0014-5793(01)02959-3;
Wismar J.;
"Molecular characterization of h-l(3)mbt-like: a new member of the
human mbt family.";
FEBS Lett. 507:119-121(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Amygdala;
PubMed=11230166; DOI=10.1101/gr.GR1547R;
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
Wambutt R., Korn B., Klein M., Poustka A.;
"Towards a catalog of human genes and proteins: sequencing and
analysis of 500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Small intestine, and Spleen;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
Beare D.M., Dunham I.;
"A genome annotation-driven approach to cloning the human ORFeome.";
Genome Biol. 5:R84.1-R84.11(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10591208; DOI=10.1038/990031;
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
Khan A.S., Lane L., Tilahun Y., Wright H.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta;
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).
[7]
IDENTIFICATION OF COMPLEX WITH E2F6; TFDP1; MAX; MGA; EUHMTASE1; CBX3;
RING1; RNF2; MBLR; BAT8 AND YAF2.
PubMed=12004135; DOI=10.1126/science.1069861;
Ogawa H., Ishiguro K., Gaubatz S., Livingston D.M., Nakatani Y.;
"A complex with chromatin modifiers that occupies E2F- and Myc-
responsive genes in G0 cells.";
Science 296:1132-1136(2002).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-683; SER-688 AND
SER-689, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67; THR-76 AND SER-689,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and 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).
[13]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-675 AND LYS-700, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[14]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-700, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[15]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-675, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[16]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-675, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[17]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-405; LYS-647; LYS-659;
LYS-675 AND LYS-700, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[18]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 170-625 IN COMPLEX WITH
MONOMETHYLATED HISTONE H4 PEPTIDE, AND FUNCTION.
PubMed=19233876; DOI=10.1093/nar/gkp086;
Guo Y., Nady N., Qi C., Allali-Hassani A., Zhu H., Pan P.,
Adams-Cioaba M.A., Amaya M.F., Dong A., Vedadi M., Schapira M.,
Read R.J., Arrowsmith C.H., Min J.;
"Methylation-state-specific recognition of histones by the MBT repeat
protein L3MBTL2.";
Nucleic Acids Res. 37:2204-2210(2009).
[19]
STRUCTURE BY NMR OF 82-124 IN COMPLEX WITH ZINC IONS.
PubMed=19241375; DOI=10.1002/pro.51;
Lechtenberg B.C., Allen M.D., Rutherford T.J., Freund S.M.,
Bycroft M.;
"Solution structure of the FCS zinc finger domain of the human
polycomb group protein L(3)mbt-like 2.";
Protein Sci. 18:657-661(2009).
-!- FUNCTION: Putative Polycomb group (PcG) protein. PcG proteins
maintain the transcriptionally repressive state of genes, probably
via a modification of chromatin, rendering it heritably changed in
its expressibility. Its association with a chromatin-remodeling
complex suggests that it may contribute to prevent expression of
genes that trigger the cell into mitosis. Binds to monomethylated
and dimethylated 'Lys-20' on histone H4. Binds histone H3 peptides
that are monomethylated or dimethylated on 'Lys-4', 'Lys-9' or
'Lys-27'. {ECO:0000269|PubMed:19233876}.
-!- SUBUNIT: Part of the E2F6.com-1 complex in G0 phase composed of
E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EUHMTASE1, RING1, RNF2, MBLR,
BAT8 and YAF2. {ECO:0000269|PubMed:19233876,
ECO:0000269|PubMed:19241375}.
-!- INTERACTION:
Q08117:AES; NbExp=3; IntAct=EBI-739909, EBI-717810;
Q8N7W2-2:BEND7; NbExp=5; IntAct=EBI-739909, EBI-10181188;
O15379:HDAC3; NbExp=6; IntAct=EBI-739909, EBI-607682;
P61244:MAX; NbExp=5; IntAct=EBI-739909, EBI-751711;
Q9HAF1:MEAF6; NbExp=3; IntAct=EBI-739909, EBI-399266;
P22234:PAICS; NbExp=6; IntAct=EBI-739909, EBI-712261;
Q8WUB8-2:PHF10; NbExp=5; IntAct=EBI-739909, EBI-10276329;
Q96MF2:STAC3; NbExp=6; IntAct=EBI-739909, EBI-745680;
O75886:STAM2; NbExp=3; IntAct=EBI-739909, EBI-373258;
Q66K14-2:TBC1D9B; NbExp=3; IntAct=EBI-739909, EBI-10217736;
Q8IWZ5:TRIM42; NbExp=3; IntAct=EBI-739909, EBI-5235829;
Q9NTW7:ZFP64; NbExp=3; IntAct=EBI-739909, EBI-745730;
P08048:ZFY; NbExp=5; IntAct=EBI-739909, EBI-12239601;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=A;
IsoId=Q969R5-1; Sequence=Displayed;
Name=2; Synonyms=B;
IsoId=Q969R5-2; Sequence=VSP_003904, VSP_003905;
Name=3;
IsoId=Q969R5-3; Sequence=VSP_003906, VSP_003907;
-!- SEQUENCE CAUTION:
Sequence=BAB84917.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
Sequence=BAC04936.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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EMBL; AJ305226; CAC37794.1; -; mRNA.
EMBL; AJ305227; CAC37795.1; -; mRNA.
EMBL; AL136564; CAB66499.2; -; mRNA.
EMBL; AK074091; BAB84917.1; ALT_SEQ; mRNA.
EMBL; AK097052; BAC04936.1; ALT_SEQ; mRNA.
EMBL; CR456482; CAG30368.1; -; mRNA.
EMBL; AL035658; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL035681; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC017191; AAH17191.1; -; mRNA.
CCDS; CCDS14011.1; -. [Q969R5-1]
RefSeq; NP_113676.2; NM_031488.4. [Q969R5-1]
UniGene; Hs.517641; -.
PDB; 2W0T; NMR; -; A=82-124.
PDB; 3CEY; X-ray; 2.20 A; A/B=170-625.
PDB; 3F70; X-ray; 2.10 A; A/B=170-625.
PDBsum; 2W0T; -.
PDBsum; 3CEY; -.
PDBsum; 3F70; -.
ProteinModelPortal; Q969R5; -.
SMR; Q969R5; -.
BioGrid; 123753; 63.
CORUM; Q969R5; -.
DIP; DIP-56748N; -.
IntAct; Q969R5; 88.
MINT; Q969R5; -.
STRING; 9606.ENSP00000216237; -.
iPTMnet; Q969R5; -.
PhosphoSitePlus; Q969R5; -.
BioMuta; L3MBTL2; -.
DMDM; 27734418; -.
EPD; Q969R5; -.
MaxQB; Q969R5; -.
PaxDb; Q969R5; -.
PeptideAtlas; Q969R5; -.
PRIDE; Q969R5; -.
ProteomicsDB; 75820; -.
ProteomicsDB; 75821; -. [Q969R5-2]
ProteomicsDB; 75822; -. [Q969R5-3]
DNASU; 83746; -.
Ensembl; ENST00000216237; ENSP00000216237; ENSG00000100395. [Q969R5-1]
Ensembl; ENST00000452106; ENSP00000414423; ENSG00000100395. [Q969R5-2]
GeneID; 83746; -.
KEGG; hsa:83746; -.
UCSC; uc003azo.4; human. [Q969R5-1]
CTD; 83746; -.
DisGeNET; 83746; -.
EuPathDB; HostDB:ENSG00000100395.14; -.
GeneCards; L3MBTL2; -.
HGNC; HGNC:18594; L3MBTL2.
HPA; HPA000815; -.
MIM; 611865; gene.
neXtProt; NX_Q969R5; -.
OpenTargets; ENSG00000100395; -.
PharmGKB; PA38356; -.
eggNOG; ENOG410IMEW; Eukaryota.
eggNOG; ENOG410ZYE4; LUCA.
GeneTree; ENSGT00760000119024; -.
HOGENOM; HOG000231220; -.
HOVERGEN; HBG057974; -.
InParanoid; Q969R5; -.
OMA; DGWDNEY; -.
OrthoDB; EOG091G0312; -.
PhylomeDB; Q969R5; -.
TreeFam; TF316498; -.
Reactome; R-HSA-4551638; SUMOylation of chromatin organization proteins.
Reactome; R-HSA-8953750; Transcriptional Regulation by E2F6.
ChiTaRS; L3MBTL2; human.
EvolutionaryTrace; Q969R5; -.
GeneWiki; L3MBTL2; -.
GenomeRNAi; 83746; -.
PRO; PR:Q969R5; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000100395; -.
CleanEx; HS_L3MBTL2; -.
ExpressionAtlas; Q969R5; baseline and differential.
Genevisible; Q969R5; HS.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:LIFEdb.
GO; GO:0042393; F:histone binding; IPI:UniProtKB.
GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
GO; GO:0070317; P:negative regulation of G0 to G1 transition; TAS:Reactome.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 3.30.60.160; -; 1.
InterPro; IPR038038; L3MBTL2.
InterPro; IPR004092; Mbt.
InterPro; IPR012313; Znf_FCS.
InterPro; IPR038603; Znf_FCS_sf.
PANTHER; PTHR12247:SF64; PTHR12247:SF64; 1.
Pfam; PF02820; MBT; 4.
SMART; SM00561; MBT; 4.
PROSITE; PS51079; MBT; 4.
PROSITE; PS51024; ZF_FCS; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Chromatin regulator;
Complete proteome; Isopeptide bond; Metal-binding; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Repeat;
Transcription; Transcription regulation; Ubl conjugation; Zinc;
Zinc-finger.
CHAIN 1 705 Lethal(3)malignant brain tumor-like
protein 2.
/FTId=PRO_0000084448.
REPEAT 179 283 MBT 1.
REPEAT 291 391 MBT 2.
REPEAT 397 500 MBT 3.
REPEAT 508 604 MBT 4.
ZN_FING 81 116 FCS-type. {ECO:0000255|PROSITE-
ProRule:PRU00367}.
COMPBIAS 17 20 Poly-Glu.
COMPBIAS 620 624 Poly-Lys.
MOD_RES 13 13 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 67 67 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 76 76 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 338 338 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 683 683 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 688 688 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 689 689 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
CROSSLNK 405 405 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 647 647 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 659 659 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 675 675 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 700 700 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate. {ECO:0000244|PubMed:25114211}.
CROSSLNK 700 700 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
VAR_SEQ 608 617 EPATPLKAKE -> GVGSRGPKRL (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_003906.
VAR_SEQ 608 614 EPATPLK -> GKLPRSL (in isoform 2).
{ECO:0000303|PubMed:11682070}.
/FTId=VSP_003904.
VAR_SEQ 615 705 Missing (in isoform 2).
{ECO:0000303|PubMed:11682070}.
/FTId=VSP_003905.
VAR_SEQ 618 705 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_003907.
VARIANT 7 7 I -> V (in dbSNP:rs3804097).
/FTId=VAR_033998.
VARIANT 300 300 R -> W (in dbSNP:rs2277846).
/FTId=VAR_015093.
VARIANT 337 337 V -> A (in dbSNP:rs34289721).
/FTId=VAR_061675.
STRAND 87 89 {ECO:0000244|PDB:2W0T}.
TURN 91 93 {ECO:0000244|PDB:2W0T}.
STRAND 96 98 {ECO:0000244|PDB:2W0T}.
TURN 99 101 {ECO:0000244|PDB:2W0T}.
TURN 104 106 {ECO:0000244|PDB:2W0T}.
STRAND 107 111 {ECO:0000244|PDB:2W0T}.
HELIX 112 120 {ECO:0000244|PDB:2W0T}.
HELIX 181 188 {ECO:0000244|PDB:3F70}.
HELIX 195 197 {ECO:0000244|PDB:3F70}.
HELIX 204 209 {ECO:0000244|PDB:3F70}.
STRAND 215 219 {ECO:0000244|PDB:3F70}.
STRAND 230 239 {ECO:0000244|PDB:3F70}.
STRAND 242 247 {ECO:0000244|PDB:3F70}.
STRAND 258 261 {ECO:0000244|PDB:3F70}.
HELIX 272 275 {ECO:0000244|PDB:3F70}.
TURN 284 286 {ECO:0000244|PDB:3F70}.
HELIX 287 289 {ECO:0000244|PDB:3F70}.
HELIX 293 301 {ECO:0000244|PDB:3F70}.
HELIX 311 318 {ECO:0000244|PDB:3F70}.
STRAND 328 332 {ECO:0000244|PDB:3F70}.
STRAND 340 349 {ECO:0000244|PDB:3F70}.
STRAND 352 357 {ECO:0000244|PDB:3F70}.
STRAND 366 369 {ECO:0000244|PDB:3F70}.
STRAND 375 377 {ECO:0000244|PDB:3F70}.
HELIX 380 384 {ECO:0000244|PDB:3F70}.
STRAND 387 389 {ECO:0000244|PDB:3F70}.
HELIX 412 414 {ECO:0000244|PDB:3F70}.
STRAND 420 422 {ECO:0000244|PDB:3F70}.
STRAND 433 438 {ECO:0000244|PDB:3F70}.
STRAND 441 453 {ECO:0000244|PDB:3F70}.
HELIX 455 457 {ECO:0000244|PDB:3CEY}.
STRAND 458 463 {ECO:0000244|PDB:3F70}.
STRAND 475 478 {ECO:0000244|PDB:3F70}.
STRAND 482 486 {ECO:0000244|PDB:3CEY}.
HELIX 489 492 {ECO:0000244|PDB:3F70}.
STRAND 505 507 {ECO:0000244|PDB:3F70}.
HELIX 510 517 {ECO:0000244|PDB:3F70}.
HELIX 524 526 {ECO:0000244|PDB:3F70}.
STRAND 541 545 {ECO:0000244|PDB:3F70}.
STRAND 553 562 {ECO:0000244|PDB:3F70}.
STRAND 565 570 {ECO:0000244|PDB:3F70}.
HELIX 575 577 {ECO:0000244|PDB:3F70}.
STRAND 579 582 {ECO:0000244|PDB:3F70}.
HELIX 593 597 {ECO:0000244|PDB:3F70}.
STRAND 604 607 {ECO:0000244|PDB:3F70}.
SEQUENCE 705 AA; 79110 MW; 8FC86A440982FFA7 CRC64;
MEKPRSIEET PSSEPMEEEE DDDLELFGGY DSFRSYNSSV GSESSSYLEE SSEAENEDRE
AGELPTSPLH LLSPGTPRSL DGSGSEPAVC EMCGIVGTRE AFFSKTKRFC SVSCSRSYSS
NSKKASILAR LQGKPPTKKA KVLHKAAWSA KIGAFLHSQG TGQLADGTPT GQDALVLGFD
WGKFLKDHSY KAAPVSCFKH VPLYDQWEDV MKGMKVEVLN SDAVLPSRVY WIASVIQTAG
YRVLLRYEGF ENDASHDFWC NLGTVDVHPI GWCAINSKIL VPPRTIHAKF TDWKGYLMKR
LVGSRTLPVD FHIKMVESMK YPFRQGMRLE VVDKSQVSRT RMAVVDTVIG GRLRLLYEDG
DSDDDFWCHM WSPLIHPVGW SRRVGHGIKM SERRSDMAHH PTFRKIYCDA VPYLFKKVRA
VYTEGGWFEE GMKLEAIDPL NLGNICVATV CKVLLDGYLM ICVDGGPSTD GLDWFCYHAS
SHAIFPATFC QKNDIELTPP KGYEAQTFNW ENYLEKTKSK AAPSRLFNMD CPNHGFKVGM
KLEAVDLMEP RLICVATVKR VVHRLLSIHF DGWDSEYDQW VDCESPDIYP VGWCELTGYQ
LQPPVAAEPA TPLKAKEATK KKKKQFGKKR KRIPPTKTRP LRQGSKKPLL EDDPQGARKI
SSEPVPGEII AVRVKEEHLD VASPDKASSP ELPVSVENIK QETDD


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