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
//