LMBL2_BOVIN
ID LMBL2_BOVIN Reviewed; 706 AA.
AC Q1JQD9; Q0V8P8;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Lethal(3)malignant brain tumor-like protein 2;
DE Short=L(3)mbt-like protein 2;
GN Name=L3MBTL2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-619.
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
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; BC116013; AAI16014.1; -; mRNA.
DR EMBL; BT026170; ABG67009.1; -; mRNA.
DR RefSeq; NP_001069078.1; NM_001075610.1.
DR AlphaFoldDB; Q1JQD9; -.
DR SMR; Q1JQD9; -.
DR STRING; 9913.ENSBTAP00000037474; -.
DR PaxDb; Q1JQD9; -.
DR PRIDE; Q1JQD9; -.
DR GeneID; 513297; -.
DR KEGG; bta:513297; -.
DR CTD; 83746; -.
DR eggNOG; KOG3766; Eukaryota.
DR HOGENOM; CLU_005352_2_1_1; -.
DR InParanoid; Q1JQD9; -.
DR OrthoDB; 1334498at2759; -.
DR TreeFam; TF316498; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
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:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
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..706
FT /note="Lethal(3)malignant brain tumor-like protein 2"
FT /id="PRO_0000346783"
FT REPEAT 180..284
FT /note="MBT 1"
FT REPEAT 292..392
FT /note="MBT 2"
FT REPEAT 398..501
FT /note="MBT 3"
FT REPEAT 509..605
FT /note="MBT 4"
FT ZN_FING 82..117
FT /note="FCS-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT REGION 1..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 606..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 685..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..27
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..638
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT BINDING 115
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 68
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q969R5"
FT MOD_RES 77
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q969R5"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q969R5"
FT MOD_RES 690
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q969R5"
FT CROSSLNK 406
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q969R5"
FT CROSSLNK 648
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q969R5"
FT CROSSLNK 660
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q969R5"
FT CROSSLNK 676
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q969R5"
FT CROSSLNK 701
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q969R5"
FT CROSSLNK 701
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q969R5"
SQ SEQUENCE 706 AA; 79081 MW; F73895F7ABF340BE CRC64;
MEKPRGVEET PSSEPMEEEE EDDDLELFGG YDSFRSYNSS AGSESSSYLE ESSEAEHEDR
EAGELPTSPL HLLSPGTPRS LDGSGSEPAV CEMCGIVGTR EAFFSKTKRF CSVSCSRSYS
SNSKKASILA RLQGKPPTKK AKVLHKAAWS AKIGAFLHSQ GTGQLADGTP TGQDALVLGF
DWGKFLKDHS YKAAPVSCFK HVPLYDQWED VMKGMKVEVL NSDAVLPSRV YWIASVIQAA
GYRVLLRYEG FENDASHDFW CNLGTVDVHP IGWCAINSKI LVPPRTIHAK FTDWKGYLMK
RLVGSRTLPV DFHIKMVESM KYPFRQGMRL EVVDKSQVSR TRMAVVDTVI GGRLRLLYED
GDSDDDFWCH MWSPLIHPVG WSRRVGHGIK LSERRSDMAH HPTFRKIYCD AVPYLFKKVR
AVYTEGGWFE EGMKLEAIDP LNLGNICVAT ICKVLLDGYL MICVDGGPST DGSDWFCYHA
SSHAIFPANF CQKNDIELTP PKGYEAHTFS WEAYLEKTKA KAAPSRLFNM DCPNHGFKVG
MKLEAVDLME PRLICVATVK RVVHRLLSIH FDGWDSEYDQ WVDCESPDIY PVGWCELTGY
QLQPPVATEP TTPLKAKEAT KKKKKQFGKK RKRIPPAKTR PLRQGSKKAL LEEDLQAAAK
APSEPAPDEI ITVRVKEEHL DVATADKALS PELPVPVENI KQETDD
