ID H0ZIB1_TAEGU Unreviewed; 678 AA.
AC H0ZIB1;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Lethal(3)malignant brain tumor-like protein 2 {ECO:0000256|ARBA:ARBA00015504};
GN Name=L3MBTL2 {ECO:0000313|Ensembl:ENSTGUP00000010328.2};
OS Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Taeniopygia.
OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000010328.2, ECO:0000313|Proteomes:UP000007754};
RN [1] {ECO:0000313|Ensembl:ENSTGUP00000010328.2, ECO:0000313|Proteomes:UP000007754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20360741; DOI=10.1038/nature08819;
RA Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W.,
RA Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A.,
RA Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P.,
RA Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., London S.E.,
RA Li Y., Lin Y.C., George J., Sweedler J., Southey B., Gunaratne P.,
RA Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., Itoh Y., Whitney O.,
RA Pfenning A.R., Howard J., Volker M., Skinner B.M., Griffin D.K., Ye L.,
RA McLaren W.M., Flicek P., Quesada V., Velasco G., Lopez-Otin C.,
RA Puente X.S., Olender T., Lancet D., Smit A.F., Hubley R., Konkel M.K.,
RA Walker J.A., Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z.,
RA Eichler E.E., Stapley J., Slate J., Ekblom R., Birkhead T., Burke T.,
RA Burt D., Scharff C., Adam I., Richard H., Sultan M., Soldatov A.,
RA Lehrach H., Edwards S.V., Yang S.P., Li X., Graves T., Fulton L.,
RA Nelson J., Chinwalla A., Hou S., Mardis E.R., Wilson R.K.;
RT "The genome of a songbird.";
RL Nature 464:757-762(2010).
RN [2] {ECO:0000313|Ensembl:ENSTGUP00000010328.2}
RP IDENTIFICATION.
RG Ensembl;
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 AlphaFoldDB; H0ZIB1; -.
DR STRING; 59729.ENSTGUP00000010328; -.
DR Ensembl; ENSTGUT00000010438.2; ENSTGUP00000010328.2; ENSTGUG00000010000.2.
DR GeneTree; ENSGT00940000153840; -.
DR HOGENOM; CLU_005352_2_1_1; -.
DR InParanoid; H0ZIB1; -.
DR OMA; QVNYPGP; -.
DR TreeFam; TF316498; -.
DR Proteomes; UP000007754; Chromosome 1A.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0035064; F:methylated histone binding; IEA:Ensembl.
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:UP000007754};
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 90..125
FT /note="FCS-type"
FT /evidence="ECO:0000259|PROSITE:PS51024"
FT REPEAT 188..292
FT /note="MBT"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00459"
FT REPEAT 300..400
FT /note="MBT"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00459"
FT REPEAT 407..510
FT /note="MBT"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00459"
FT REPEAT 518..614
FT /note="MBT"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00459"
FT REGION 51..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 678 AA; 76667 MW; 6E78DB0DC4E3EED4 CRC64;
MERDRREMVS AFCHKTSSLE RVEEEGDDEE VDDELDIFGG YDSLTCYNSS MGSDSSSCLE
ESSDDEVADR EAGELSTSPM HQPSTGRLTE ENGSEPAVCE MCGIVGTREA FFSKTKRFCS
VSCSRSYSSN SKKASILARL QGKPPTKKAK VLHKASWSAK IGAFLHSQGT GQLADGTLTG
QDALVLGFDW GKYLQEHGYK AAPVSCFKHV PLFDQWDDVV KGMKVEVLNS DAVLPSRVYW
IASVIQIVGY RALLRYEGFE NDAGHDFWCN LGTVDIHPIG WCAINSKILV PPQTIHAKYT
DWRSYLMKKL VGARTIPVDF HIKMAESMKY PFRQGMRVEV VDKNHVSQTR MAVVDTVIGG
RLRLLYEDGD SDDDFWCHMW SPLIHPVGWS RRVGHDIKKT EEKRNDMANH PTFRKIYCDA
VPYLFKKVRA VYSEGGWFER GMKLEAIDPL NLGNICVATV CKVLLDGYLM ISIDGATSDD
GSDWFCYHAS SHAIFPANFC KRNNIELTPP KRHEAKTFSW ERYLEETKSR PAPSRLFNTD
CPNHGFKAGM KVEAVDLMEP RLICVATVKR VVQRLLSIHF DGWDNEYDQW VDCESPDIYP
VGWCELTGYQ LQPPVTPEPT TPAKAKERAQ EEEETLWKEE KKVTCQSPQC QADCQEVFCH
ELKTRSKSCQ PDFARAST
//
