LMBL2_PONAB
ID LMBL2_PONAB Reviewed; 705 AA.
AC Q5R737;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Lethal(3)malignant brain tumor-like protein 2;
DE Short=L(3)mbt-like protein 2;
GN Name=L3MBTL2;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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' (By
CC similarity). {ECO:0000250}.
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:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
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DR EMBL; CR860281; CAH92423.1; -; mRNA.
DR RefSeq; NP_001126429.1; NM_001132957.1.
DR AlphaFoldDB; Q5R737; -.
DR SMR; Q5R737; -.
DR STRING; 9601.ENSPPYP00000013237; -.
DR GeneID; 100173412; -.
DR KEGG; pon:100173412; -.
DR CTD; 83746; -.
DR eggNOG; KOG3766; Eukaryota.
DR InParanoid; Q5R737; -.
DR OrthoDB; 1334498at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0035064; F:methylated histone binding; ISS:UniProtKB.
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 transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 3.30.60.160; -; 1.
DR InterPro; IPR038038; L3MBTL2.
DR InterPro; IPR004092; Mbt.
DR InterPro; IPR012313; Znf_FCS.
DR InterPro; IPR038603; Znf_FCS_sf.
DR PANTHER; PTHR12247:SF64; PTHR12247:SF64; 1.
DR Pfam; PF02820; MBT; 4.
DR SMART; SM00561; MBT; 4.
DR PROSITE; PS51079; MBT; 4.
DR PROSITE; PS51024; ZF_FCS; 1.
PE 2: Evidence at transcript level;
KW Chromatin regulator; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..705
FT /note="Lethal(3)malignant brain tumor-like protein 2"
FT /id="PRO_0000346784"
FT REPEAT 179..283
FT /note="MBT 1"
FT REPEAT 291..391
FT /note="MBT 2"
FT REPEAT 397..500
FT /note="MBT 3"
FT REPEAT 508..604
FT /note="MBT 4"
FT ZN_FING 81..116
FT /note="FCS-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 608..705
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 617..637
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..659
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q969R5"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q969R5"
FT MOD_RES 76
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q969R5"
FT MOD_RES 338
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q969R5"
FT MOD_RES 683
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q969R5"
FT MOD_RES 688
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q969R5"
FT MOD_RES 689
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q969R5"
FT CROSSLNK 405
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q969R5"
FT CROSSLNK 647
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q969R5"
FT CROSSLNK 659
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q969R5"
FT CROSSLNK 675
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q969R5"
FT CROSSLNK 700
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q969R5"
FT CROSSLNK 700
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q969R5"
SQ SEQUENCE 705 AA; 79081 MW; 5F9959318996633B 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 VPYLFKKVRA
VYTEGGWFEE GMKLEAIDPL NLGNICVATV CKVLLDGYLM VCVDGGPSTD GSDWFCYHAS
SHAIFPATFC QKNDIELTPP KGYEAQTFNW ENYLEKTKSK AAPSRLFNMD CPNHGFKVGM
KLEAVDLMEP RLICVATVKR VVHRLLSIHF DGWDSEYDQW VDCESPDIYP VGWCELTGYQ
LQPPVAAEPA TPLKAKEATK KKKKQFGKKR KRIPPTKTRP LRQGSKKPLL EDDPQGARKI
SSEPVRGDII AVRVKEEHLD VPSPNKASSP ELPVSVENIK QETDD
