ID A0A2K5MRY6_CERAT Unreviewed; 703 AA.
AC A0A2K5MRY6;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Lethal(3)malignant brain tumor-like protein 2 {ECO:0000256|ARBA:ARBA00015504};
GN Name=L3MBTL2 {ECO:0000313|Ensembl:ENSCATP00000027998.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000027998.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000027998.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A2K5MRY6; -.
DR Ensembl; ENSCATT00000052247.1; ENSCATP00000027998.1; ENSCATG00000037314.1.
DR GeneTree; ENSGT00940000153840; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000037314; Expressed in skeletal muscle tissue and 12 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; cd20100; MBT_dSfmbt-like_rpt4; 1.
DR CDD; cd20121; MBT_L3MBTL2_rpt1; 1.
DR CDD; cd20124; MBT_L3MBTL2_rpt2; 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:UP000233060};
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, ECO:0000256|PROSITE-
KW ProRule:PRU00367}.
FT DOMAIN 81..116
FT /note="FCS-type"
FT /evidence="ECO:0000259|PROSITE:PS51024"
FT REPEAT 179..283
FT /note="MBT"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00459"
FT REPEAT 291..391
FT /note="MBT"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00459"
FT REPEAT 397..498
FT /note="MBT"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00459"
FT REPEAT 506..602
FT /note="MBT"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00459"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 606..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 677..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..26
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..635
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..656
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 703 AA; 79076 MW; 44198179556F2F06 CRC64;
MEKPPSIEET 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 VPYLFKKVRL
RTWLFPWDRM KLEAIDPLNL GNICVATVCK VLLDGYLMIC VDGGPSTDGS DWFCYHASSH
AIFPATFCQK NDIELTPPKG YEVQTFSWEN YLEKTKSKAA PSRLFNMDCP NHGFKVGMKL
EAVDLMEPRL ICVATVKRVV HRLLSIHFDG WDSEYDQWVD CESPDIYPVG WCELTGYQLQ
PPVAAEPATP LKAKEATKKK KKQFGKKRKR IPPTKTRPLR QGSKKPLLED DPQGAKKISS
EPVPGEIIAV RVKEEHLDAV SPHKASSPEL PVPVENIKEE TDD
//
