LMBL3_MOUSE
ID LMBL3_MOUSE Reviewed; 883 AA.
AC Q8BLB7; Q0VGT0; Q641L7; Q6ZPI2; Q8C0G4;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Lethal(3)malignant brain tumor-like protein 3 {ECO:0000305};
DE Short=L(3)mbt-like protein 3;
DE AltName: Full=MBT-1;
GN Name=L3mbtl3 {ECO:0000312|MGI:MGI:2143628}; Synonyms=Mbt1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, and Fetal testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Eye;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 123-883.
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [4]
RP DISRUPTION PHENOTYPE, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=15889154; DOI=10.1038/sj.emboj.7600654;
RA Arai S., Miyazaki T.;
RT "Impaired maturation of myeloid progenitors in mice lacking novel Polycomb
RT group protein MBT-1.";
RL EMBO J. 24:1863-1873(2005).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
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).
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 (By similarity). Required for normal maturation of
CC myeloid progenitor cells. {ECO:0000250, ECO:0000269|PubMed:15889154}.
CC -!- SUBUNIT: Interacts with RNF2. Interacts (via SAM domain) with SAMD1
CC (via SAM domain); the interaction mediates L3MBTL3 binding to chromatin
CC (PubMed:33980486). {ECO:0000269|PubMed:15889154,
CC ECO:0000269|PubMed:33980486}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15889154,
CC ECO:0000269|PubMed:33980486}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8BLB7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BLB7-2; Sequence=VSP_013509;
CC Name=3;
CC IsoId=Q8BLB7-3; Sequence=VSP_013510, VSP_013511;
CC -!- TISSUE SPECIFICITY: Detected in hematopoietic progenitor cells in fetal
CC liver. Detected in adult bone marrow, heart, brain, spleen, lung,
CC liver, kidney and testis. {ECO:0000269|PubMed:15889154}.
CC -!- DISRUPTION PHENOTYPE: Death at a late embryonic stage due defective
CC erythropoiesis, defects in the maturation of other types of myeloid
CC lineage cells and anemia. {ECO:0000269|PubMed:15889154}.
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DR EMBL; AK031398; BAC27386.1; -; mRNA.
DR EMBL; AK045667; BAC32449.1; -; mRNA.
DR EMBL; BC082309; AAH82309.1; -; mRNA.
DR EMBL; BC085192; AAH85192.1; -; mRNA.
DR EMBL; AK129443; BAC98253.1; -; mRNA.
DR CCDS; CCDS23756.1; -. [Q8BLB7-1]
DR CCDS; CCDS83689.1; -. [Q8BLB7-2]
DR RefSeq; NP_001334396.1; NM_001347467.1. [Q8BLB7-2]
DR RefSeq; NP_766375.1; NM_172787.3. [Q8BLB7-1]
DR RefSeq; XP_006512794.1; XM_006512731.3.
DR RefSeq; XP_006512795.1; XM_006512732.3. [Q8BLB7-1]
DR RefSeq; XP_006512796.1; XM_006512733.3. [Q8BLB7-1]
DR RefSeq; XP_006512798.1; XM_006512735.3. [Q8BLB7-2]
DR AlphaFoldDB; Q8BLB7; -.
DR SMR; Q8BLB7; -.
DR BioGRID; 231865; 7.
DR STRING; 10090.ENSMUSP00000037619; -.
DR iPTMnet; Q8BLB7; -.
DR PhosphoSitePlus; Q8BLB7; -.
DR EPD; Q8BLB7; -.
DR jPOST; Q8BLB7; -.
DR MaxQB; Q8BLB7; -.
DR PaxDb; Q8BLB7; -.
DR PeptideAtlas; Q8BLB7; -.
DR PRIDE; Q8BLB7; -.
DR ProteomicsDB; 286214; -. [Q8BLB7-1]
DR ProteomicsDB; 286215; -. [Q8BLB7-2]
DR ProteomicsDB; 286216; -. [Q8BLB7-3]
DR Antibodypedia; 32840; 166 antibodies from 26 providers.
DR DNASU; 237339; -.
DR Ensembl; ENSMUST00000040219; ENSMUSP00000037619; ENSMUSG00000039089. [Q8BLB7-1]
DR Ensembl; ENSMUST00000105519; ENSMUSP00000101158; ENSMUSG00000039089. [Q8BLB7-2]
DR Ensembl; ENSMUST00000174766; ENSMUSP00000133479; ENSMUSG00000039089. [Q8BLB7-1]
DR GeneID; 237339; -.
DR KEGG; mmu:237339; -.
DR UCSC; uc007esa.1; mouse. [Q8BLB7-2]
DR UCSC; uc007esb.1; mouse. [Q8BLB7-1]
DR UCSC; uc007esd.1; mouse. [Q8BLB7-3]
DR CTD; 84456; -.
DR MGI; MGI:2143628; L3mbtl3.
DR VEuPathDB; HostDB:ENSMUSG00000039089; -.
DR eggNOG; KOG3766; Eukaryota.
DR GeneTree; ENSGT00940000159800; -.
DR HOGENOM; CLU_004064_0_1_1; -.
DR InParanoid; Q8BLB7; -.
DR OMA; SADTMYH; -.
DR OrthoDB; 63195at2759; -.
DR PhylomeDB; Q8BLB7; -.
DR TreeFam; TF316498; -.
DR BioGRID-ORCS; 237339; 4 hits in 76 CRISPR screens.
DR ChiTaRS; L3mbtl3; mouse.
DR PRO; PR:Q8BLB7; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q8BLB7; protein.
DR Bgee; ENSMUSG00000039089; Expressed in manus and 226 other tissues.
DR Genevisible; Q8BLB7; MM.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
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; IDA:MGI.
DR GO; GO:0030851; P:granulocyte differentiation; IMP:MGI.
DR GO; GO:0030225; P:macrophage differentiation; IMP:MGI.
DR GO; GO:0030099; P:myeloid cell differentiation; IMP:MGI.
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; ISS: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 Alternative splicing; Chromatin regulator; Isopeptide bond; Metal-binding;
KW Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..883
FT /note="Lethal(3)malignant brain tumor-like protein 3"
FT /id="PRO_0000084451"
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 811..875
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 146..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 595..768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..205
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..657
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..768
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 638
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96JM7"
FT VAR_SEQ 72..96
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013509"
FT VAR_SEQ 290..302
FT /note="CGYRIKLHFDGYS -> SSALYLFGKRDDG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013510"
FT VAR_SEQ 303..883
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013511"
FT CONFLICT 146
FT /note="H -> Y (in Ref. 3; BAC98253)"
FT /evidence="ECO:0000305"
FT CONFLICT 275
FT /note="P -> H (in Ref. 1; BAC27386)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 883 AA; 99137 MW; 7A6417202A0E5532 CRC64;
MTESASSTSG QEFDVFSVMD WKDGVGTLPG SDLKFRVNEF GALEVITDES EMESVKKATA
TTTWMVPTAQ DAPTSPPSSR PVFPPAYWTS PPGCPTVFSE KTGVPFRLKE QSKADGLQFC
ENCCQYGNGD ECLSGGKYCS QNCARHAKDK DQKDERDGGE DNDEEDPKCS RKKKPKLSLK
ADSKDDGEER DDEMENKQDG RILRGSQRAR RKRRGDSAVL KQGLPPKGKK TWCWASYLEE
EKAVAVPTKL FKEHQSFPYN KNGFKVGMKL EGVDPDHQAM YCVLTVAEVC GYRIKLHFDG
YSDCYDFWVN ADALDIHPVG WCEKTGHKLR PPKGYKEEEF NWQSYLKTCK AQAAPKSLFE
NQNITVIPSG FRVGMKLEAA DKKSPSVICV ATVTDMVDNR FLVHFDNWDE SYDYWCESNS
PHIHPVGWCK EHRRTLITPP GYSHVKHFSW DKYLEETNSL PAPARAFKVK PPHGFQKKMK
LEAVDKRNPL FIRVATVADT DDHRIKVHFD GWSSCYDYWI DADSPDIHPV GWCSKTGHPL
QAPLSPAELM EPSETGGCPT LGCRGVGHFK KSRYLGTQSG ANCPYSEINL SKERIFPDRL
SGDTSPPTTP SFPRSKRMDT RESSSSPETR EKHANNFKED SEKKKENEVK TSAEAKVVRE
EPTPSVQQSQ PPQQVQQVQH AQPPQQAQKA PQAQQAQQAQ QAQQAPQAPQ TPQPQQAPQV
QQAQQAPQAQ QAQQPQQAQQ PQQAPPVQQP QQVQQAQPTQ QQAQTQQQAQ RRSAVFLSFK
PPIPCLPLRW EQQSKLLPTV AGIPASRVSK WSTDEVSEFI QSLPGCEEHG KVFKDEQIDG
EAFLLMTQTD IVKIMSIKLG PALKIFNSIL MFKAAEKNSH NEL
