LMBL3_HUMAN
ID LMBL3_HUMAN Reviewed; 780 AA.
AC Q96JM7; Q4VXE1; Q5VUM9; Q6P9B5;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Lethal(3)malignant brain tumor-like protein 3 {ECO:0000305};
DE Short=H-l(3)mbt-like protein 3;
DE Short=L(3)mbt-like protein 3;
DE Short=L3mbt-like 3;
DE AltName: Full=MBT-1;
GN Name=L3MBTL3 {ECO:0000312|HGNC:HGNC:23035}; Synonyms=KIAA1798, MBT1;
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 [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ASN-183.
RC TISSUE=Brain;
RX PubMed=11347906; DOI=10.1093/dnares/8.2.85;
RA Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 8:85-95(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT ASN-183.
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-608, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-608, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-608, AND IDENTIFICATION BY
RP 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-608, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-637 AND LYS-704, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [12]
RP INTERACTION WITH SAMD1, AND SUBCELLULAR LOCATION.
RX PubMed=33980486; DOI=10.1126/sciadv.abf2229;
RA Stielow B., Zhou Y., Cao Y., Simon C., Pogoda H.M., Jiang J., Ren Y.,
RA Phanor S.K., Rohner I., Nist A., Stiewe T., Hammerschmidt M., Shi Y.,
RA Bulyk M.L., Wang Z., Liefke R.;
RT "The SAM domain-containing protein 1 (SAMD1) acts as a repressive chromatin
RT regulator at unmethylated CpG islands.";
RL Sci. Adv. 7:0-0(2021).
RN [13]
RP STRUCTURE BY NMR OF 256-562.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the first and third MBT domain from human KIAA1798
RT protein.";
RL Submitted (NOV-2004) to the PDB data bank.
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. Required for normal maturation of myeloid progenitor
CC cells (By similarity). {ECO:0000250|UniProtKB:Q8BLB7}.
CC -!- SUBUNIT: Interacts with RNF2 (By similarity). Interacts (via SAM
CC domain) with SAMD1 (via SAM domain); the interaction mediates L3MBTL3
CC binding to chromatin (PubMed:33980486). {ECO:0000250|UniProtKB:Q8BLB7,
CC ECO:0000269|PubMed:33980486}.
CC -!- INTERACTION:
CC Q96JM7; Q9NWX5: ASB6; NbExp=3; IntAct=EBI-2686809, EBI-6425205;
CC Q96JM7; Q8N9N5: BANP; NbExp=4; IntAct=EBI-2686809, EBI-744695;
CC Q96JM7; Q13895: BYSL; NbExp=5; IntAct=EBI-2686809, EBI-358049;
CC Q96JM7; O00716: E2F3; NbExp=3; IntAct=EBI-2686809, EBI-765551;
CC Q96JM7; Q96JM7: L3MBTL3; NbExp=3; IntAct=EBI-2686809, EBI-2686809;
CC Q96JM7; Q9Y4Z0: LSM4; NbExp=3; IntAct=EBI-2686809, EBI-372521;
CC Q96JM7; P45984: MAPK9; NbExp=3; IntAct=EBI-2686809, EBI-713568;
CC Q96JM7; Q9UBU8: MORF4L1; NbExp=3; IntAct=EBI-2686809, EBI-399246;
CC Q96JM7; Q15014: MORF4L2; NbExp=3; IntAct=EBI-2686809, EBI-399257;
CC Q96JM7; Q9NPG2: NGB; NbExp=3; IntAct=EBI-2686809, EBI-10311409;
CC Q96JM7; Q9UMX2: OAZ3; NbExp=3; IntAct=EBI-2686809, EBI-10281601;
CC Q96JM7; P18545: PDE6G; NbExp=3; IntAct=EBI-2686809, EBI-2622029;
CC Q96JM7; Q8IXK0: PHC2; NbExp=6; IntAct=EBI-2686809, EBI-713786;
CC Q96JM7; Q8N381: PIK3R3; NbExp=3; IntAct=EBI-2686809, EBI-749096;
CC Q96JM7; Q96S99: PLEKHF1; NbExp=3; IntAct=EBI-2686809, EBI-745767;
CC Q96JM7; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-2686809, EBI-742388;
CC Q96JM7; P62875: POLR2L; NbExp=3; IntAct=EBI-2686809, EBI-359527;
CC Q96JM7; Q13131: PRKAA1; NbExp=3; IntAct=EBI-2686809, EBI-1181405;
CC Q96JM7; P54646: PRKAA2; NbExp=3; IntAct=EBI-2686809, EBI-1383852;
CC Q96JM7; P14678-2: SNRPB; NbExp=3; IntAct=EBI-2686809, EBI-372475;
CC Q96JM7; P23497: SP100; NbExp=3; IntAct=EBI-2686809, EBI-751145;
CC Q96JM7; G2XKQ0: SUMO1P1; NbExp=3; IntAct=EBI-2686809, EBI-10175576;
CC Q96JM7; P10827: THRA; NbExp=3; IntAct=EBI-2686809, EBI-286285;
CC Q96JM7; Q6DKK2: TTC19; NbExp=3; IntAct=EBI-2686809, EBI-948354;
CC Q96JM7-2; P54253: ATXN1; NbExp=6; IntAct=EBI-11985629, EBI-930964;
CC Q96JM7-2; A0A0S2Z5G4: BANP; NbExp=3; IntAct=EBI-11985629, EBI-16429704;
CC Q96JM7-2; Q13895: BYSL; NbExp=3; IntAct=EBI-11985629, EBI-358049;
CC Q96JM7-2; Q9BXJ3: C1QTNF4; NbExp=3; IntAct=EBI-11985629, EBI-11955105;
CC Q96JM7-2; Q8IUI8: CRLF3; NbExp=3; IntAct=EBI-11985629, EBI-2872414;
CC Q96JM7-2; Q14203-5: DCTN1; NbExp=3; IntAct=EBI-11985629, EBI-25840379;
CC Q96JM7-2; Q9H4E7: DEF6; NbExp=3; IntAct=EBI-11985629, EBI-745369;
CC Q96JM7-2; Q8NFF5-2: FLAD1; NbExp=3; IntAct=EBI-11985629, EBI-11526128;
CC Q96JM7-2; Q53EP0-3: FNDC3B; NbExp=3; IntAct=EBI-11985629, EBI-10242151;
CC Q96JM7-2; O95995: GAS8; NbExp=3; IntAct=EBI-11985629, EBI-1052570;
CC Q96JM7-2; O75031: HSF2BP; NbExp=3; IntAct=EBI-11985629, EBI-7116203;
CC Q96JM7-2; P42858: HTT; NbExp=3; IntAct=EBI-11985629, EBI-466029;
CC Q96JM7-2; Q14005-2: IL16; NbExp=3; IntAct=EBI-11985629, EBI-17178971;
CC Q96JM7-2; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-11985629, EBI-2556193;
CC Q96JM7-2; Q96JM7-2: L3MBTL3; NbExp=3; IntAct=EBI-11985629, EBI-11985629;
CC Q96JM7-2; P61968: LMO4; NbExp=3; IntAct=EBI-11985629, EBI-2798728;
CC Q96JM7-2; P45984: MAPK9; NbExp=3; IntAct=EBI-11985629, EBI-713568;
CC Q96JM7-2; P55081: MFAP1; NbExp=3; IntAct=EBI-11985629, EBI-1048159;
CC Q96JM7-2; Q9UBU8-2: MORF4L1; NbExp=3; IntAct=EBI-11985629, EBI-10288852;
CC Q96JM7-2; Q15014: MORF4L2; NbExp=3; IntAct=EBI-11985629, EBI-399257;
CC Q96JM7-2; Q9NPG2: NGB; NbExp=3; IntAct=EBI-11985629, EBI-10311409;
CC Q96JM7-2; Q16656-4: NRF1; NbExp=3; IntAct=EBI-11985629, EBI-11742836;
CC Q96JM7-2; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-11985629, EBI-741158;
CC Q96JM7-2; Q96BD5: PHF21A; NbExp=3; IntAct=EBI-11985629, EBI-745085;
CC Q96JM7-2; Q92569: PIK3R3; NbExp=3; IntAct=EBI-11985629, EBI-79893;
CC Q96JM7-2; Q96S99: PLEKHF1; NbExp=3; IntAct=EBI-11985629, EBI-745767;
CC Q96JM7-2; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-11985629, EBI-742388;
CC Q96JM7-2; O60568: PLOD3; NbExp=3; IntAct=EBI-11985629, EBI-741582;
CC Q96JM7-2; D3DTS7: PMP22; NbExp=3; IntAct=EBI-11985629, EBI-25882629;
CC Q96JM7-2; P67775: PPP2CA; NbExp=3; IntAct=EBI-11985629, EBI-712311;
CC Q96JM7-2; P54646: PRKAA2; NbExp=3; IntAct=EBI-11985629, EBI-1383852;
CC Q96JM7-2; P63000: RAC1; NbExp=3; IntAct=EBI-11985629, EBI-413628;
CC Q96JM7-2; O94955: RHOBTB3; NbExp=3; IntAct=EBI-11985629, EBI-2367123;
CC Q96JM7-2; Q5VUG0: SFMBT2; NbExp=3; IntAct=EBI-11985629, EBI-12025260;
CC Q96JM7-2; P37840: SNCA; NbExp=3; IntAct=EBI-11985629, EBI-985879;
CC Q96JM7-2; P00441: SOD1; NbExp=3; IntAct=EBI-11985629, EBI-990792;
CC Q96JM7-2; Q5MJ10: SPANXN2; NbExp=3; IntAct=EBI-11985629, EBI-12023934;
CC Q96JM7-2; Q9UMX1: SUFU; NbExp=3; IntAct=EBI-11985629, EBI-740595;
CC Q96JM7-2; Q13148: TARDBP; NbExp=6; IntAct=EBI-11985629, EBI-372899;
CC Q96JM7-2; Q86TI0: TBC1D1; NbExp=3; IntAct=EBI-11985629, EBI-1644036;
CC Q96JM7-2; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-11985629, EBI-11955057;
CC Q96JM7-2; Q9Y228: TRAF3IP3; NbExp=5; IntAct=EBI-11985629, EBI-765817;
CC Q96JM7-2; Q5T7W7: TSTD2; NbExp=3; IntAct=EBI-11985629, EBI-8994397;
CC Q96JM7-2; Q6DKK2: TTC19; NbExp=3; IntAct=EBI-11985629, EBI-948354;
CC Q96JM7-2; P09936: UCHL1; NbExp=3; IntAct=EBI-11985629, EBI-714860;
CC Q96JM7-2; P31930: UQCRC1; NbExp=3; IntAct=EBI-11985629, EBI-1052596;
CC Q96JM7-2; P61758: VBP1; NbExp=3; IntAct=EBI-11985629, EBI-357430;
CC Q96JM7-2; A0A0S2Z6A9: ZCWPW1; NbExp=3; IntAct=EBI-11985629, EBI-16429747;
CC Q96JM7-2; Q9H0M4-4: ZCWPW1; NbExp=3; IntAct=EBI-11985629, EBI-16429732;
CC Q96JM7-2; P36508: ZNF76; NbExp=3; IntAct=EBI-11985629, EBI-7254550;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:33980486}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96JM7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96JM7-2; Sequence=VSP_013508;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB47427.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB058701; BAB47427.1; ALT_INIT; mRNA.
DR EMBL; AL583846; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL355581; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW48073.1; -; Genomic_DNA.
DR EMBL; BC060845; AAH60845.1; -; mRNA.
DR CCDS; CCDS34537.1; -. [Q96JM7-1]
DR CCDS; CCDS34538.1; -. [Q96JM7-2]
DR RefSeq; NP_001007103.1; NM_001007102.3. [Q96JM7-2]
DR RefSeq; NP_001333479.1; NM_001346550.1. [Q96JM7-2]
DR RefSeq; NP_001333480.1; NM_001346551.1. [Q96JM7-2]
DR RefSeq; NP_115814.1; NM_032438.3. [Q96JM7-1]
DR RefSeq; XP_005267218.1; XM_005267161.4. [Q96JM7-1]
DR RefSeq; XP_006715641.1; XM_006715578.3. [Q96JM7-1]
DR RefSeq; XP_011534481.1; XM_011536179.2. [Q96JM7-1]
DR RefSeq; XP_011534482.1; XM_011536180.2. [Q96JM7-1]
DR RefSeq; XP_011534483.1; XM_011536181.2. [Q96JM7-1]
DR RefSeq; XP_011534485.1; XM_011536183.2. [Q96JM7-1]
DR RefSeq; XP_011534486.1; XM_011536184.2. [Q96JM7-1]
DR PDB; 1WJQ; NMR; -; A=469-562.
DR PDB; 1WJS; NMR; -; A=258-371.
DR PDB; 3UT1; X-ray; 2.05 A; A=228-551.
DR PDB; 4FL6; X-ray; 2.55 A; A/B=229-553.
DR PDB; 4L59; X-ray; 2.29 A; A=228-544.
DR PDBsum; 1WJQ; -.
DR PDBsum; 1WJS; -.
DR PDBsum; 3UT1; -.
DR PDBsum; 4FL6; -.
DR PDBsum; 4L59; -.
DR AlphaFoldDB; Q96JM7; -.
DR SMR; Q96JM7; -.
DR BioGRID; 124091; 110.
DR DIP; DIP-42798N; -.
DR IntAct; Q96JM7; 107.
DR MINT; Q96JM7; -.
DR STRING; 9606.ENSP00000431962; -.
DR BindingDB; Q96JM7; -.
DR ChEMBL; CHEMBL1287623; -.
DR DrugCentral; Q96JM7; -.
DR GuidetoPHARMACOLOGY; 2830; -.
DR iPTMnet; Q96JM7; -.
DR PhosphoSitePlus; Q96JM7; -.
DR SwissPalm; Q96JM7; -.
DR BioMuta; L3MBTL3; -.
DR DMDM; 62900619; -.
DR EPD; Q96JM7; -.
DR jPOST; Q96JM7; -.
DR MassIVE; Q96JM7; -.
DR MaxQB; Q96JM7; -.
DR PaxDb; Q96JM7; -.
DR PeptideAtlas; Q96JM7; -.
DR PRIDE; Q96JM7; -.
DR ProteomicsDB; 76987; -. [Q96JM7-1]
DR ProteomicsDB; 76988; -. [Q96JM7-2]
DR ABCD; Q96JM7; 1 sequenced antibody.
DR Antibodypedia; 32840; 166 antibodies from 26 providers.
DR DNASU; 84456; -.
DR Ensembl; ENST00000361794.7; ENSP00000354526.2; ENSG00000198945.8. [Q96JM7-1]
DR Ensembl; ENST00000368136.3; ENSP00000357118.2; ENSG00000198945.8. [Q96JM7-1]
DR Ensembl; ENST00000368139.6; ENSP00000357121.2; ENSG00000198945.8. [Q96JM7-2]
DR Ensembl; ENST00000526019.5; ENSP00000436706.1; ENSG00000198945.8. [Q96JM7-2]
DR Ensembl; ENST00000533560.5; ENSP00000437185.1; ENSG00000198945.8. [Q96JM7-2]
DR GeneID; 84456; -.
DR KEGG; hsa:84456; -.
DR MANE-Select; ENST00000361794.7; ENSP00000354526.2; NM_032438.4; NP_115814.1.
DR UCSC; uc003qbt.4; human. [Q96JM7-1]
DR CTD; 84456; -.
DR DisGeNET; 84456; -.
DR GeneCards; L3MBTL3; -.
DR HGNC; HGNC:23035; L3MBTL3.
DR HPA; ENSG00000198945; Low tissue specificity.
DR MIM; 618844; gene.
DR neXtProt; NX_Q96JM7; -.
DR OpenTargets; ENSG00000198945; -.
DR PharmGKB; PA134943930; -.
DR VEuPathDB; HostDB:ENSG00000198945; -.
DR eggNOG; KOG3766; Eukaryota.
DR GeneTree; ENSGT00940000159800; -.
DR HOGENOM; CLU_004064_0_1_1; -.
DR InParanoid; Q96JM7; -.
DR OMA; DESYDYX; -.
DR OrthoDB; 63195at2759; -.
DR PhylomeDB; Q96JM7; -.
DR TreeFam; TF316498; -.
DR PathwayCommons; Q96JM7; -.
DR SignaLink; Q96JM7; -.
DR BioGRID-ORCS; 84456; 25 hits in 1089 CRISPR screens.
DR ChiTaRS; L3MBTL3; human.
DR EvolutionaryTrace; Q96JM7; -.
DR GenomeRNAi; 84456; -.
DR Pharos; Q96JM7; Tchem.
DR PRO; PR:Q96JM7; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q96JM7; protein.
DR Bgee; ENSG00000198945; Expressed in calcaneal tendon and 144 other tissues.
DR ExpressionAtlas; Q96JM7; baseline and differential.
DR Genevisible; Q96JM7; HS.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0043249; P:erythrocyte maturation; IEA:Ensembl.
DR GO; GO:0030851; P:granulocyte differentiation; IEA:Ensembl.
DR GO; GO:0030225; P:macrophage differentiation; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0090308; P:regulation of DNA methylation-dependent heterochromatin assembly; IDA:UniProtKB.
DR Gene3D; 1.10.150.50; -; 1.
DR InterPro; IPR004092; Mbt.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR002515; Znf_C2H2C.
DR Pfam; PF02820; MBT; 3.
DR Pfam; PF00536; SAM_1; 1.
DR SMART; SM00561; MBT; 3.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR PROSITE; PS51079; MBT; 3.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
DR PROSITE; PS51802; ZF_CCHHC; 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..780
FT /note="Lethal(3)malignant brain tumor-like protein 3"
FT /id="PRO_0000084450"
FT REPEAT 232..332
FT /note="MBT 1"
FT REPEAT 340..439
FT /note="MBT 2"
FT REPEAT 448..543
FT /note="MBT 3"
FT DOMAIN 708..772
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT ZN_FING 549..593
FT /note="CCHHC-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT REGION 149..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 597..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..205
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..659
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 608
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT CROSSLNK 637
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 704
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 72..96
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013508"
FT VARIANT 183
FT /note="T -> N (in dbSNP:rs9388768)"
FT /evidence="ECO:0000269|PubMed:11347906,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_022368"
FT HELIX 234..241
FT /evidence="ECO:0007829|PDB:3UT1"
FT HELIX 248..250
FT /evidence="ECO:0007829|PDB:3UT1"
FT TURN 253..255
FT /evidence="ECO:0007829|PDB:3UT1"
FT STRAND 269..274
FT /evidence="ECO:0007829|PDB:3UT1"
FT STRAND 277..290
FT /evidence="ECO:0007829|PDB:3UT1"
FT STRAND 293..298
FT /evidence="ECO:0007829|PDB:3UT1"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:3UT1"
FT STRAND 307..310
FT /evidence="ECO:0007829|PDB:3UT1"
FT STRAND 314..317
FT /evidence="ECO:0007829|PDB:3UT1"
FT HELIX 321..325
FT /evidence="ECO:0007829|PDB:3UT1"
FT TURN 337..339
FT /evidence="ECO:0007829|PDB:3UT1"
FT HELIX 342..348
FT /evidence="ECO:0007829|PDB:3UT1"
FT HELIX 356..358
FT /evidence="ECO:0007829|PDB:3UT1"
FT TURN 360..363
FT /evidence="ECO:0007829|PDB:3UT1"
FT STRAND 376..381
FT /evidence="ECO:0007829|PDB:3UT1"
FT STRAND 384..397
FT /evidence="ECO:0007829|PDB:3UT1"
FT STRAND 400..405
FT /evidence="ECO:0007829|PDB:3UT1"
FT HELIX 410..412
FT /evidence="ECO:0007829|PDB:3UT1"
FT STRAND 414..416
FT /evidence="ECO:0007829|PDB:3UT1"
FT HELIX 428..431
FT /evidence="ECO:0007829|PDB:3UT1"
FT HELIX 445..447
FT /evidence="ECO:0007829|PDB:4L59"
FT HELIX 450..456
FT /evidence="ECO:0007829|PDB:3UT1"
FT HELIX 464..466
FT /evidence="ECO:0007829|PDB:3UT1"
FT STRAND 472..474
FT /evidence="ECO:0007829|PDB:1WJQ"
FT STRAND 480..484
FT /evidence="ECO:0007829|PDB:3UT1"
FT STRAND 486..488
FT /evidence="ECO:0007829|PDB:3UT1"
FT STRAND 492..500
FT /evidence="ECO:0007829|PDB:3UT1"
FT STRAND 502..509
FT /evidence="ECO:0007829|PDB:3UT1"
FT STRAND 510..512
FT /evidence="ECO:0007829|PDB:1WJQ"
FT HELIX 514..516
FT /evidence="ECO:0007829|PDB:3UT1"
FT STRAND 518..521
FT /evidence="ECO:0007829|PDB:3UT1"
FT HELIX 532..536
FT /evidence="ECO:0007829|PDB:3UT1"
FT TURN 546..549
FT /evidence="ECO:0007829|PDB:1WJQ"
SQ SEQUENCE 780 AA; 88337 MW; 81F92D4423E25C84 CRC64;
MTESASSTSG QEFDVFSVMD WKDGVGTLPG SDLKFRVNEF GALEVITDEN EMENVKKATA
TTTWMVPTAQ EAPTSPPSSR PVFPPAYWTS PPGCPTVFSE KTGMPFRLKD PVKVEGLQFC
ENCCQYGNVD ECLSGGNYCS QNCARHIKDK DQKEERDVEE DNEEEDPKCS RKKKPKLSLK
ADTKEDGEER DDEMENKQDV RILRGSQRAR RKRRGDSAVL KQGLPPKGKK AWCWASYLEE
EKAVAVPAKL FKEHQSFPYN KNGFKVGMKL EGVDPEHQSV YCVLTVAEVC GYRIKLHFDG
YSDCYDFWVN ADALDIHPVG WCEKTGHKLH PPKGYKEEEF NWQTYLKTCK AQAAPKSLFE
NQNITVIPSG FRVGMKLEAV DKKNPSFICV ATVTDMVDNR FLVHFDNWDE SYDYWCEASS
PHIHPVGWCK EHRRTLITPP GYPNVKHFSW DKYLEETNSL PAPARAFKVK PPHGFQKKMK
LEVVDKRNPM FIRVATVADT DDHRVKVHFD GWNNCYDYWI DADSPDIHPV GWCSKTGHPL
QPPLSPLELM EASEHGGCST PGCKGIGHFK RARHLGPHSA ANCPYSEINL NKDRIFPDRL
SGEMPPASPS FPRNKRTDAN ESSSSPEIRD QHADDVKEDF EERTESEMRT SHEARGAREE
PTVQQAQRRS AVFLSFKSPI PCLPLRWEQQ SKLLPTVAGI PASKVSKWST DEVSEFIQSL
PGCEEHGKVF KDEQIDGEAF LLMTQTDIVK IMSIKLGPAL KIFNSILMFK AAEKNSHNEL
