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Database: UniProt
Entry: A0A1L8GNG9_XENLA
LinkDB: A0A1L8GNG9_XENLA
Original site: A0A1L8GNG9_XENLA 
ID   A0A1L8GNG9_XENLA        Unreviewed;       757 AA.
AC   A0A1L8GNG9;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Lethal(3)malignant brain tumor-like protein 2 {ECO:0000256|ARBA:ARBA00015504};
GN   Name=l3mbtl2.L {ECO:0000313|RefSeq:XP_018114259.1,
GN   ECO:0000313|Xenbase:XB-GENE-6488335};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355 {ECO:0000313|Proteomes:UP000186698, ECO:0000313|RefSeq:XP_018114259.1};
RN   [1] {ECO:0000313|RefSeq:XP_018114259.1}
RP   IDENTIFICATION.
RC   STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018114259.1};
RC   TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018114259.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00025314}.
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:0000256|ARBA:ARBA00011444}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   RefSeq; XP_018114259.1; XM_018258770.2.
DR   AlphaFoldDB; A0A1L8GNG9; -.
DR   STRING; 8355.A0A1L8GNG9; -.
DR   PaxDb; 8355-A0A1L8GNG9; -.
DR   GeneID; 108714483; -.
DR   KEGG; xla:108714483; -.
DR   AGR; Xenbase:XB-GENE-6488335; -.
DR   CTD; 108714483; -.
DR   Xenbase; XB-GENE-6488335; l3mbtl2.L.
DR   OMA; QVNYPGP; -.
DR   OrthoDB; 5405166at2759; -.
DR   Proteomes; UP000186698; Chromosome 4L.
DR   Bgee; 108714483; Expressed in blastula and 19 other cell types or tissues.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd20121; MBT_L3MBTL2_rpt1; 1.
DR   CDD; cd20124; MBT_L3MBTL2_rpt2; 1.
DR   CDD; cd20130; MBT_L3MBTL2_rpt4; 1.
DR   Gene3D; 2.30.30.140; -; 4.
DR   Gene3D; 3.30.60.160; -; 1.
DR   InterPro; IPR004092; Mbt.
DR   InterPro; IPR047356; MBT_L3MBTL2_rpt1.
DR   InterPro; IPR047357; MBT_L3MBTL2_rpt2.
DR   InterPro; IPR012313; Znf_FCS.
DR   InterPro; IPR038603; Znf_FCS_sf.
DR   PANTHER; PTHR12247:SF64; LETHAL(3)MALIGNANT BRAIN TUMOR-LIKE PROTEIN 2; 1.
DR   PANTHER; PTHR12247; POLYCOMB GROUP PROTEIN; 1.
DR   Pfam; PF02820; MBT; 4.
DR   Pfam; PF21319; zf-FCS_1; 1.
DR   SMART; SM00561; MBT; 4.
DR   SUPFAM; SSF63748; Tudor/PWWP/MBT; 4.
DR   PROSITE; PS51079; MBT; 4.
DR   PROSITE; PS51024; ZF_FCS; 1.
PE   4: Predicted;
KW   Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW   Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186698};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          62..97
FT                   /note="FCS-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51024"
SQ   SEQUENCE   757 AA;  85484 MW;  26B6D67C3C6155C2 CRC64;
     MDDESEDAYD LFSGYDSYRE YNSSELSDDI SSGIGDSSFD EEENEESSSL QQSSSVTNKA
     NEENSAEPAI CEMCGIVGTR GTFFSKTKRF CNVSCSRSYS SNSKKASILA RLQGKPPTKK
     AKVLHKASWS AKIKAFLNSQ STGQTADGTP AGQDALTLGF DWGKYITEGN FEAAPVTCFR
     HVPLCNQWDD VVEGIKVESL NTDAVLPSRV YWISSVVKIA GYKALLQYEG FEDDSSHNYW
     CNLGTVEIHP IGWCAVNSKI LVPPQSILSK FTNWREYLMK KLVGSHTIPV DFHIKMTESF
     RCPFRQGMRV EAVDKMKMSR VRSAVVDTVI GGRMRLLYED GEKNDDFWCH MTSPLIHPVG
     WAQKVGHNIK PPDLKRFEMS SHPTFRKVYC DAVPHLFKQM RVAYPEGTWF EEGMKLEAID
     PLNLGNICVA TVCKILLDGY LMVGLDSTPS ADGSEWFCYH ASSPSMFPVG FCNKYDIELT
     PPAGYSKEAF SWDEYLEKTG SRAAPARLFN NDCPNHGFEP GMKLEAVDLM EPRLICVATI
     THVARRLLRI NFDGWDVEYD QWVDCESPDI YPVGWCELIG YQLQPPVEDE PKEEPKPKEV
     KRKKKTAFGK RRKKNPQGKK SAKKTKSATN TKNISNQQHE EPKRKYCKKA KAVKETPLTD
     NRENPDLSRP EDKNDLANKL GVEVLPSTST GKSLDLLPAD PEMEENCSRE NICSPKSEEE
     EIFTVQIKEE EMEVCELEQV KSQDMKKEIK EEEEVNI
//
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