LMBL2_HUMAN
ID LMBL2_HUMAN Reviewed; 705 AA.
AC Q969R5; Q8TEN1; Q96SC4; Q9BQI2; Q9UGS4;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Lethal(3)malignant brain tumor-like protein 2;
DE Short=H-l(3)mbt-like protein 2;
DE Short=L(3)mbt-like protein 2;
GN Name=L3MBTL2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RX PubMed=11682070; DOI=10.1016/s0014-5793(01)02959-3;
RA Wismar J.;
RT "Molecular characterization of h-l(3)mbt-like: a new member of the human
RT mbt family.";
RL FEBS Lett. 507:119-121(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Amygdala;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Small intestine, and Spleen;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP IDENTIFICATION OF COMPLEX WITH E2F6; TFDP1; MAX; MGA; EUHMTASE1; CBX3;
RP RING1; RNF2; MBLR; BAT8 AND YAF2.
RX PubMed=12004135; DOI=10.1126/science.1069861;
RA Ogawa H., Ishiguro K., Gaubatz S., Livingston D.M., Nakatani Y.;
RT "A complex with chromatin modifiers that occupies E2F- and Myc-responsive
RT genes in G0 cells.";
RL Science 296:1132-1136(2002).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-683; SER-688 AND
RP SER-689, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67; THR-76 AND SER-689, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-675 AND LYS-700, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-700, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-675, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-675, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-405; LYS-647; LYS-659; LYS-675
RP AND LYS-700, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 170-625 IN COMPLEX WITH
RP MONOMETHYLATED HISTONE H4 PEPTIDE, AND FUNCTION.
RX PubMed=19233876; DOI=10.1093/nar/gkp086;
RA Guo Y., Nady N., Qi C., Allali-Hassani A., Zhu H., Pan P.,
RA Adams-Cioaba M.A., Amaya M.F., Dong A., Vedadi M., Schapira M., Read R.J.,
RA Arrowsmith C.H., Min J.;
RT "Methylation-state-specific recognition of histones by the MBT repeat
RT protein L3MBTL2.";
RL Nucleic Acids Res. 37:2204-2210(2009).
RN [19]
RP STRUCTURE BY NMR OF 82-124 IN COMPLEX WITH ZINC IONS.
RX PubMed=19241375; DOI=10.1002/pro.51;
RA Lechtenberg B.C., Allen M.D., Rutherford T.J., Freund S.M., Bycroft M.;
RT "Solution structure of the FCS zinc finger domain of the human polycomb
RT group protein L(3)mbt-like 2.";
RL Protein Sci. 18:657-661(2009).
CC -!- FUNCTION: Putative Polycomb group (PcG) protein. PcG proteins maintain
CC the transcriptionally repressive state of genes, probably via a
CC modification of chromatin, rendering it heritably changed in its
CC expressibility. Its association with a chromatin-remodeling complex
CC suggests that it may contribute to prevent expression of genes that
CC trigger the cell into mitosis. Binds to monomethylated and dimethylated
CC 'Lys-20' on histone H4. Binds histone H3 peptides that are
CC monomethylated or dimethylated on 'Lys-4', 'Lys-9' or 'Lys-27'.
CC {ECO:0000269|PubMed:19233876}.
CC -!- SUBUNIT: Part of the E2F6.com-1 complex in G0 phase composed of E2F6,
CC MGA, MAX, TFDP1, CBX3, BAT8, EUHMTASE1, RING1, RNF2, MBLR, BAT8 and
CC YAF2. {ECO:0000269|PubMed:19233876, ECO:0000269|PubMed:19241375}.
CC -!- INTERACTION:
CC Q969R5; Q9Y2J4: AMOTL2; NbExp=3; IntAct=EBI-739909, EBI-746752;
CC Q969R5; Q8N7W2-2: BEND7; NbExp=8; IntAct=EBI-739909, EBI-10181188;
CC Q969R5; Q6PI77: BHLHB9; NbExp=3; IntAct=EBI-739909, EBI-11519926;
CC Q969R5; Q86UB2: BIVM; NbExp=3; IntAct=EBI-739909, EBI-12191873;
CC Q969R5; Q9H257-2: CARD9; NbExp=3; IntAct=EBI-739909, EBI-11530605;
CC Q969R5; Q9BWC9: CCDC106; NbExp=3; IntAct=EBI-739909, EBI-711501;
CC Q969R5; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-739909, EBI-742887;
CC Q969R5; Q5JST6: EFHC2; NbExp=3; IntAct=EBI-739909, EBI-2349927;
CC Q969R5; Q9NRA8: EIF4ENIF1; NbExp=3; IntAct=EBI-739909, EBI-301024;
CC Q969R5; Q9NTX9: FAM217B; NbExp=3; IntAct=EBI-739909, EBI-19153639;
CC Q969R5; O95995: GAS8; NbExp=3; IntAct=EBI-739909, EBI-1052570;
CC Q969R5; Q5VSY0: GKAP1; NbExp=3; IntAct=EBI-739909, EBI-743722;
CC Q969R5; Q08379: GOLGA2; NbExp=3; IntAct=EBI-739909, EBI-618309;
CC Q969R5; O15379: HDAC3; NbExp=6; IntAct=EBI-739909, EBI-607682;
CC Q969R5; O75031: HSF2BP; NbExp=3; IntAct=EBI-739909, EBI-7116203;
CC Q969R5; P61244: MAX; NbExp=6; IntAct=EBI-739909, EBI-751711;
CC Q969R5; Q9HAF1: MEAF6; NbExp=4; IntAct=EBI-739909, EBI-399266;
CC Q969R5; P50221: MEOX1; NbExp=3; IntAct=EBI-739909, EBI-2864512;
CC Q969R5; Q16656-4: NRF1; NbExp=3; IntAct=EBI-739909, EBI-11742836;
CC Q969R5; P22234: PAICS; NbExp=6; IntAct=EBI-739909, EBI-712261;
CC Q969R5; Q8WUB8-2: PHF10; NbExp=6; IntAct=EBI-739909, EBI-10276329;
CC Q969R5; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-739909, EBI-79165;
CC Q969R5; P78424: POU6F2; NbExp=3; IntAct=EBI-739909, EBI-12029004;
CC Q969R5; P31321: PRKAR1B; NbExp=3; IntAct=EBI-739909, EBI-2805516;
CC Q969R5; Q9NYW8: RBAK; NbExp=3; IntAct=EBI-739909, EBI-1210429;
CC Q969R5; Q04864-2: REL; NbExp=3; IntAct=EBI-739909, EBI-10829018;
CC Q969R5; Q9Y2M2-2: SSUH2; NbExp=3; IntAct=EBI-739909, EBI-12231891;
CC Q969R5; Q96MF2: STAC3; NbExp=6; IntAct=EBI-739909, EBI-745680;
CC Q969R5; O75886: STAM2; NbExp=4; IntAct=EBI-739909, EBI-373258;
CC Q969R5; Q86VP1: TAX1BP1; NbExp=3; IntAct=EBI-739909, EBI-529518;
CC Q969R5; A1L3A9: TBC1D9B; NbExp=3; IntAct=EBI-739909, EBI-12133518;
CC Q969R5; Q66K14-2: TBC1D9B; NbExp=3; IntAct=EBI-739909, EBI-10217736;
CC Q969R5; Q969V4: TEKT1; NbExp=3; IntAct=EBI-739909, EBI-10180409;
CC Q969R5; Q9NVV9: THAP1; NbExp=3; IntAct=EBI-739909, EBI-741515;
CC Q969R5; Q08117: TLE5; NbExp=3; IntAct=EBI-739909, EBI-717810;
CC Q969R5; P19237: TNNI1; NbExp=3; IntAct=EBI-739909, EBI-746692;
CC Q969R5; Q8IWZ5: TRIM42; NbExp=3; IntAct=EBI-739909, EBI-5235829;
CC Q969R5; Q86XT4: TRIM50; NbExp=3; IntAct=EBI-739909, EBI-9867283;
CC Q969R5; Q6FI91: TSPYL; NbExp=3; IntAct=EBI-739909, EBI-723389;
CC Q969R5; Q9HCK0: ZBTB26; NbExp=3; IntAct=EBI-739909, EBI-3918996;
CC Q969R5; P10074: ZBTB48; NbExp=3; IntAct=EBI-739909, EBI-744864;
CC Q969R5; Q9NTW7: ZFP64; NbExp=3; IntAct=EBI-739909, EBI-711679;
CC Q969R5; P08048: ZFY; NbExp=6; IntAct=EBI-739909, EBI-12239601;
CC Q969R5; Q7Z7K2: ZNF467; NbExp=3; IntAct=EBI-739909, EBI-11986485;
CC Q969R5; Q3KNS6-3: ZNF829; NbExp=3; IntAct=EBI-739909, EBI-18036029;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=A;
CC IsoId=Q969R5-1; Sequence=Displayed;
CC Name=2; Synonyms=B;
CC IsoId=Q969R5-2; Sequence=VSP_003904, VSP_003905;
CC Name=3;
CC IsoId=Q969R5-3; Sequence=VSP_003906, VSP_003907;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB84917.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=BAC04936.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AJ305226; CAC37794.1; -; mRNA.
DR EMBL; AJ305227; CAC37795.1; -; mRNA.
DR EMBL; AL136564; CAB66499.2; -; mRNA.
DR EMBL; AK074091; BAB84917.1; ALT_SEQ; mRNA.
DR EMBL; AK097052; BAC04936.1; ALT_SEQ; mRNA.
DR EMBL; CR456482; CAG30368.1; -; mRNA.
DR EMBL; AL035658; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL035681; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC017191; AAH17191.1; -; mRNA.
DR CCDS; CCDS14011.1; -. [Q969R5-1]
DR RefSeq; NP_113676.2; NM_031488.4. [Q969R5-1]
DR PDB; 2W0T; NMR; -; A=82-124.
DR PDB; 3CEY; X-ray; 2.20 A; A/B=170-625.
DR PDB; 3F70; X-ray; 2.10 A; A/B=170-625.
DR PDBsum; 2W0T; -.
DR PDBsum; 3CEY; -.
DR PDBsum; 3F70; -.
DR AlphaFoldDB; Q969R5; -.
DR SMR; Q969R5; -.
DR BioGRID; 123753; 193.
DR CORUM; Q969R5; -.
DR DIP; DIP-56748N; -.
DR IntAct; Q969R5; 138.
DR MINT; Q969R5; -.
DR STRING; 9606.ENSP00000216237; -.
DR iPTMnet; Q969R5; -.
DR PhosphoSitePlus; Q969R5; -.
DR BioMuta; L3MBTL2; -.
DR DMDM; 27734418; -.
DR EPD; Q969R5; -.
DR jPOST; Q969R5; -.
DR MassIVE; Q969R5; -.
DR MaxQB; Q969R5; -.
DR PaxDb; Q969R5; -.
DR PeptideAtlas; Q969R5; -.
DR PRIDE; Q969R5; -.
DR ProteomicsDB; 75820; -. [Q969R5-1]
DR ProteomicsDB; 75821; -. [Q969R5-2]
DR ProteomicsDB; 75822; -. [Q969R5-3]
DR ABCD; Q969R5; 3 sequenced antibodies.
DR Antibodypedia; 204; 219 antibodies from 27 providers.
DR DNASU; 83746; -.
DR Ensembl; ENST00000216237.10; ENSP00000216237.5; ENSG00000100395.15. [Q969R5-1]
DR Ensembl; ENST00000452106.5; ENSP00000414423.1; ENSG00000100395.15. [Q969R5-2]
DR GeneID; 83746; -.
DR KEGG; hsa:83746; -.
DR MANE-Select; ENST00000216237.10; ENSP00000216237.5; NM_031488.5; NP_113676.2.
DR UCSC; uc003azo.4; human. [Q969R5-1]
DR CTD; 83746; -.
DR DisGeNET; 83746; -.
DR GeneCards; L3MBTL2; -.
DR HGNC; HGNC:18594; L3MBTL2.
DR HPA; ENSG00000100395; Low tissue specificity.
DR MIM; 611865; gene.
DR neXtProt; NX_Q969R5; -.
DR OpenTargets; ENSG00000100395; -.
DR PharmGKB; PA38356; -.
DR VEuPathDB; HostDB:ENSG00000100395; -.
DR eggNOG; KOG3766; Eukaryota.
DR GeneTree; ENSGT00940000153840; -.
DR HOGENOM; CLU_005352_2_1_1; -.
DR InParanoid; Q969R5; -.
DR OMA; NYPGPSE; -.
DR PhylomeDB; Q969R5; -.
DR TreeFam; TF316498; -.
DR PathwayCommons; Q969R5; -.
DR Reactome; R-HSA-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-HSA-8953750; Transcriptional Regulation by E2F6.
DR SignaLink; Q969R5; -.
DR SIGNOR; Q969R5; -.
DR BioGRID-ORCS; 83746; 24 hits in 1084 CRISPR screens.
DR ChiTaRS; L3MBTL2; human.
DR EvolutionaryTrace; Q969R5; -.
DR GeneWiki; L3MBTL2; -.
DR GenomeRNAi; 83746; -.
DR Pharos; Q969R5; Tbio.
DR PRO; PR:Q969R5; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q969R5; protein.
DR Bgee; ENSG00000100395; Expressed in pancreatic ductal cell and 180 other tissues.
DR ExpressionAtlas; Q969R5; baseline and differential.
DR Genevisible; Q969R5; HS.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:LIFEdb.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IPI:UniProtKB.
DR GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 3.30.60.160; -; 1.
DR IDEAL; IID00095; -.
DR InterPro; IPR038038; L3MBTL2.
DR InterPro; IPR004092; Mbt.
DR InterPro; IPR012313; Znf_FCS.
DR InterPro; IPR038603; Znf_FCS_sf.
DR PANTHER; PTHR12247:SF64; PTHR12247:SF64; 1.
DR Pfam; PF02820; MBT; 4.
DR SMART; SM00561; MBT; 4.
DR PROSITE; PS51079; MBT; 4.
DR PROSITE; PS51024; ZF_FCS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromatin regulator; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..705
FT /note="Lethal(3)malignant brain tumor-like protein 2"
FT /id="PRO_0000084448"
FT REPEAT 179..283
FT /note="MBT 1"
FT REPEAT 291..391
FT /note="MBT 2"
FT REPEAT 397..500
FT /note="MBT 3"
FT REPEAT 508..604
FT /note="MBT 4"
FT ZN_FING 81..116
FT /note="FCS-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 608..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 680..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..637
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..658
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 76
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 338
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 683
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 688
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 689
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 405
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 647
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 659
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 675
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 700
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 700
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 608..617
FT /note="EPATPLKAKE -> GVGSRGPKRL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_003906"
FT VAR_SEQ 608..614
FT /note="EPATPLK -> GKLPRSL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11682070"
FT /id="VSP_003904"
FT VAR_SEQ 615..705
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11682070"
FT /id="VSP_003905"
FT VAR_SEQ 618..705
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_003907"
FT VARIANT 7
FT /note="I -> V (in dbSNP:rs3804097)"
FT /id="VAR_033998"
FT VARIANT 300
FT /note="R -> W (in dbSNP:rs2277846)"
FT /id="VAR_015093"
FT VARIANT 337
FT /note="V -> A (in dbSNP:rs34289721)"
FT /id="VAR_061675"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:2W0T"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:2W0T"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:2W0T"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:2W0T"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:2W0T"
FT STRAND 107..111
FT /evidence="ECO:0007829|PDB:2W0T"
FT HELIX 112..120
FT /evidence="ECO:0007829|PDB:2W0T"
FT HELIX 181..188
FT /evidence="ECO:0007829|PDB:3F70"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:3F70"
FT HELIX 204..209
FT /evidence="ECO:0007829|PDB:3F70"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:3F70"
FT STRAND 230..239
FT /evidence="ECO:0007829|PDB:3F70"
FT STRAND 242..247
FT /evidence="ECO:0007829|PDB:3F70"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:3F70"
FT HELIX 272..275
FT /evidence="ECO:0007829|PDB:3F70"
FT TURN 284..286
FT /evidence="ECO:0007829|PDB:3F70"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:3F70"
FT HELIX 293..301
FT /evidence="ECO:0007829|PDB:3F70"
FT HELIX 311..318
FT /evidence="ECO:0007829|PDB:3F70"
FT STRAND 328..332
FT /evidence="ECO:0007829|PDB:3F70"
FT STRAND 340..349
FT /evidence="ECO:0007829|PDB:3F70"
FT STRAND 352..357
FT /evidence="ECO:0007829|PDB:3F70"
FT STRAND 366..369
FT /evidence="ECO:0007829|PDB:3F70"
FT STRAND 375..377
FT /evidence="ECO:0007829|PDB:3F70"
FT HELIX 380..384
FT /evidence="ECO:0007829|PDB:3F70"
FT STRAND 387..389
FT /evidence="ECO:0007829|PDB:3F70"
FT HELIX 412..414
FT /evidence="ECO:0007829|PDB:3F70"
FT STRAND 420..422
FT /evidence="ECO:0007829|PDB:3F70"
FT STRAND 433..438
FT /evidence="ECO:0007829|PDB:3F70"
FT STRAND 441..453
FT /evidence="ECO:0007829|PDB:3F70"
FT HELIX 455..457
FT /evidence="ECO:0007829|PDB:3CEY"
FT STRAND 458..463
FT /evidence="ECO:0007829|PDB:3F70"
FT STRAND 475..478
FT /evidence="ECO:0007829|PDB:3F70"
FT STRAND 482..486
FT /evidence="ECO:0007829|PDB:3CEY"
FT HELIX 489..492
FT /evidence="ECO:0007829|PDB:3F70"
FT STRAND 505..507
FT /evidence="ECO:0007829|PDB:3F70"
FT HELIX 510..517
FT /evidence="ECO:0007829|PDB:3F70"
FT HELIX 524..526
FT /evidence="ECO:0007829|PDB:3F70"
FT STRAND 541..545
FT /evidence="ECO:0007829|PDB:3F70"
FT STRAND 553..562
FT /evidence="ECO:0007829|PDB:3F70"
FT STRAND 565..570
FT /evidence="ECO:0007829|PDB:3F70"
FT HELIX 575..577
FT /evidence="ECO:0007829|PDB:3F70"
FT STRAND 579..582
FT /evidence="ECO:0007829|PDB:3F70"
FT HELIX 593..597
FT /evidence="ECO:0007829|PDB:3F70"
FT STRAND 604..607
FT /evidence="ECO:0007829|PDB:3F70"
SQ 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
