LMBL2_RAT
ID LMBL2_RAT Reviewed; 703 AA.
AC Q3MIF2;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Lethal(3)malignant brain tumor-like protein 2;
DE Short=L(3)mbt-like protein 2;
GN Name=L3mbtl2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-681; SER-685 AND SER-687, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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; BC101865; AAI01866.1; -; mRNA.
DR RefSeq; NP_001028867.1; NM_001033695.1.
DR AlphaFoldDB; Q3MIF2; -.
DR SMR; Q3MIF2; -.
DR STRING; 10116.ENSRNOP00000031908; -.
DR iPTMnet; Q3MIF2; -.
DR PhosphoSitePlus; Q3MIF2; -.
DR PaxDb; Q3MIF2; -.
DR PRIDE; Q3MIF2; -.
DR Ensembl; ENSRNOT00000034998; ENSRNOP00000031908; ENSRNOG00000024743.
DR GeneID; 300320; -.
DR KEGG; rno:300320; -.
DR UCSC; RGD:1308569; rat.
DR CTD; 83746; -.
DR RGD; 1308569; L3mbtl2.
DR eggNOG; KOG3766; Eukaryota.
DR GeneTree; ENSGT00940000153840; -.
DR HOGENOM; CLU_005352_2_1_1; -.
DR InParanoid; Q3MIF2; -.
DR OMA; NYPGPSE; -.
DR OrthoDB; 1334498at2759; -.
DR PhylomeDB; Q3MIF2; -.
DR Reactome; R-RNO-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-RNO-8953750; Transcriptional Regulation by E2F6.
DR PRO; PR:Q3MIF2; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000024743; Expressed in thymus and 20 other tissues.
DR Genevisible; Q3MIF2; RN.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; ISO:RGD.
DR GO; GO:0035064; F:methylated histone binding; ISS:UniProtKB.
DR GO; GO:1990841; F:promoter-specific chromatin binding; ISO:RGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0007398; P:ectoderm development; ISO:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:0035067; P:negative regulation of histone acetylation; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0031062; P:positive regulation of histone methylation; ISO:RGD.
DR GO; GO:0048863; P:stem cell differentiation; ISO:RGD.
DR GO; GO:0072089; P:stem cell proliferation; ISO:RGD.
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 1: Evidence at protein 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..703
FT /note="Lethal(3)malignant brain tumor-like protein 2"
FT /id="PRO_0000346785"
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..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 604..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..703
FT /note="Disordered"
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 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 338
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q969R5"
FT MOD_RES 681
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 685
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 687
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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 673
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q969R5"
FT CROSSLNK 698
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q969R5"
FT CROSSLNK 698
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q969R5"
SQ SEQUENCE 703 AA; 78967 MW; 6FFFE8B8B4BD88E9 CRC64;
MEKPRGTEET PSSEPMEEEE DDDLELFGGY DSFRSYNSSA GSESSSYLEE SSEAENEDRE
AGELPTSPLH LFSSANNRAL DGSGSEPAVC EMCGIVGTRE AFFSKTKRFC SVSCSRSYSS
NSKKASILAR LQGKPPTKKA KVLHKAAWSA KIGAFLHAQG TGQLADGTPT GQDALVLGFD
WGKFLKDHSY KAAPVGCFKH VPLYDQWEDV MKGMKVEVLN SDAVLPSRVY WIATVIQAAG
YRVLLRYEGF ENDASHDFWC NLGTVDVHPI GWCAINSKIL VPPRTIHAKF TDWKSYLMKR
LVGSRTLPAD FHIKMVESMK YPFRQGMRLE VVDKTQVSRT RMAVVDTVIG GRLRLLYEDG
DSDDDFWCHM WSPLIHPVGW SRRVGHGIKM SERRCDMSHH PTFRKIYCDA VPYLFKKVRA
VYTEGGWFEE GMKLEAIDPL NLGNICVATI CKVLLDGYLM ICVDGGPSTD GSDWFCYHAS
SHAIFPATFC QKNDIELTPP KGYETQPFDW ESYLEKTKSK AAPARLFNMD CPNHGFKVGM
KLEAVDLMEP RLICVATVKR VVHRLLSIHF DGWDNEYDQW VDCESPDIYP VGWCELTGYQ
LQPPVSAEPN TPQKGKDATK KKKKQFGKKR KRIPSAKTRP LRQSSKKPLL EDNLEALGVS
EPVPDDIIAV CVKEEHQDLP SPDRSPSPLL PLPTESIKQE RDS
