BEND3_MOUSE
ID BEND3_MOUSE Reviewed; 825 AA.
AC Q6PAL0; Q80TC0;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=BEN domain-containing protein 3;
GN Name=Bend3; Synonyms=Kiaa1553;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 51-825.
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH NURD COMPLEX.
RX PubMed=25457167; DOI=10.1016/j.molcel.2014.10.001;
RA Saksouk N., Barth T.K., Ziegler-Birling C., Olova N., Nowak A., Rey E.,
RA Mateos-Langerak J., Urbach S., Reik W., Torres-Padilla M.E., Imhof A.,
RA Dejardin J., Simboeck E.;
RT "Redundant mechanisms to form silent chromatin at pericentromeric regions
RT rely on BEND3 and DNA methylation.";
RL Mol. Cell 56:580-594(2014).
CC -!- FUNCTION: Transcriptional repressor which associates with the NoRC
CC (nucleolar remodeling complex) complex and plays a key role in
CC repressing rDNA transcription. The sumoylated form modulates the
CC stability of the NoRC complex component BAZ2A/TIP5 by controlling its
CC USP21-mediated deubiquitination (By similarity). Binds to unmethylated
CC major satellite DNA and is involved in the recruitment of the Polycomb
CC repressive complex 2 (PRC2) to major satellites (PubMed:25457167).
CC Stimulates the ERCC6L translocase and ATPase activities (By
CC similarity). {ECO:0000250|UniProtKB:Q5T5X7,
CC ECO:0000269|PubMed:25457167}.
CC -!- SUBUNIT: Homooligomer, probably a homooctamer. Interacts with HDAC2 and
CC HDAC3, but not HDAC1. Interacts with SALL4. Interacts with
CC SMARCA5/SNF2H, BAZ2A/TIP5 and USP21 (By similarity). Interacts with the
CC nucleosome remodeling and histone deacetylase (NuRD) repressor complex
CC (PubMed:25457167). Interacts (via BEN domains 1 and 3) with ERCC6L (via
CC N-terminal TPR repeat); the interaction is direct (By similarity).
CC {ECO:0000250|UniProtKB:Q5T5X7, ECO:0000269|PubMed:25457167}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5T5X7}. Nucleus,
CC nucleolus {ECO:0000250|UniProtKB:Q5T5X7}. Note=In the nucleus, observed
CC in heterochromatic foci containing CBX1, CBX3, CBX5 and histone H3
CC trimethylated at 'Lys-9'. Released from chromatin during
CC decondensation. Association with heterochromatin does not depend on
CC sumoylation. {ECO:0000250|UniProtKB:Q5T5X7}.
CC -!- DOMAIN: The BEN domain 4 is necessary and sufficient for the
CC localization of BEND3 to heterochromatic regions.
CC {ECO:0000250|UniProtKB:Q5T5X7}.
CC -!- PTM: Sumoylated at Lys-20 by SUMO1 and at Lys-509 by SUMO1, SUMO2 and
CC SUMO3. Sumoylation probably occurs sequentially, with that of Lys-20
CC preceding that of Lys-509. It does not alter association with
CC heterochromatin, but is required for the repression of transcription.
CC {ECO:0000250|UniProtKB:Q5T5X7}.
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DR EMBL; BC060240; AAH60240.1; -; mRNA.
DR EMBL; AK122525; BAC65807.1; -; mRNA.
DR CCDS; CCDS35892.1; -.
DR RefSeq; NP_950193.1; NM_199028.2.
DR RefSeq; XP_006512832.1; XM_006512769.3.
DR RefSeq; XP_006512833.1; XM_006512770.3.
DR RefSeq; XP_006512834.1; XM_006512771.3.
DR PDB; 7V9F; X-ray; 2.50 A; A=712-825.
DR PDB; 7V9G; X-ray; 3.50 A; A/D/G/J=712-825.
DR PDB; 7V9H; X-ray; 2.69 A; A=547-647.
DR PDB; 7V9I; X-ray; 3.50 A; A=712-825.
DR PDBsum; 7V9F; -.
DR PDBsum; 7V9G; -.
DR PDBsum; 7V9H; -.
DR PDBsum; 7V9I; -.
DR AlphaFoldDB; Q6PAL0; -.
DR SMR; Q6PAL0; -.
DR BioGRID; 237119; 2.
DR IntAct; Q6PAL0; 2.
DR STRING; 10090.ENSMUSP00000127351; -.
DR iPTMnet; Q6PAL0; -.
DR PhosphoSitePlus; Q6PAL0; -.
DR EPD; Q6PAL0; -.
DR MaxQB; Q6PAL0; -.
DR PaxDb; Q6PAL0; -.
DR PeptideAtlas; Q6PAL0; -.
DR PRIDE; Q6PAL0; -.
DR ProteomicsDB; 273602; -.
DR Antibodypedia; 2976; 123 antibodies from 21 providers.
DR DNASU; 331623; -.
DR Ensembl; ENSMUST00000040147; ENSMUSP00000047251; ENSMUSG00000038214.
DR Ensembl; ENSMUST00000167488; ENSMUSP00000127351; ENSMUSG00000038214.
DR GeneID; 331623; -.
DR KEGG; mmu:331623; -.
DR UCSC; uc011xdl.1; mouse.
DR CTD; 57673; -.
DR MGI; MGI:2677212; Bend3.
DR VEuPathDB; HostDB:ENSMUSG00000038214; -.
DR eggNOG; ENOG502QQWG; Eukaryota.
DR GeneTree; ENSGT00390000010827; -.
DR HOGENOM; CLU_017582_0_0_1; -.
DR InParanoid; Q6PAL0; -.
DR OMA; QCAQRLN; -.
DR OrthoDB; 168652at2759; -.
DR PhylomeDB; Q6PAL0; -.
DR TreeFam; TF300204; -.
DR BioGRID-ORCS; 331623; 6 hits in 76 CRISPR screens.
DR PRO; PR:Q6PAL0; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q6PAL0; protein.
DR Bgee; ENSMUSG00000038214; Expressed in primitive streak and 206 other tissues.
DR ExpressionAtlas; Q6PAL0; baseline and differential.
DR Genevisible; Q6PAL0; MM.
DR GO; GO:0000792; C:heterochromatin; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0000182; F:rDNA binding; ISS:UniProtKB.
DR GO; GO:0006306; P:DNA methylation; ISS:UniProtKB.
DR GO; GO:0098532; P:histone H3-K27 trimethylation; ISS:UniProtKB.
DR GO; GO:0080182; P:histone H3-K4 trimethylation; ISS:UniProtKB.
DR GO; GO:0036124; P:histone H3-K9 trimethylation; ISS:UniProtKB.
DR GO; GO:0043967; P:histone H4 acetylation; ISS:UniProtKB.
DR GO; GO:0034773; P:histone H4-K20 trimethylation; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:1903580; P:positive regulation of ATP metabolic process; ISS:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR GO; GO:0000183; P:rDNA heterochromatin assembly; ISS:UniProtKB.
DR InterPro; IPR018379; BEN_domain.
DR InterPro; IPR033583; BEND3.
DR PANTHER; PTHR28665; PTHR28665; 1.
DR Pfam; PF10523; BEN; 4.
DR SMART; SM01025; BEN; 4.
DR PROSITE; PS51457; BEN; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Chromatin regulator; DNA-binding; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..825
FT /note="BEN domain-containing protein 3"
FT /id="PRO_0000290201"
FT DOMAIN 239..340
FT /note="BEN 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00784"
FT DOMAIN 384..484
FT /note="BEN 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00784"
FT DOMAIN 547..647
FT /note="BEN 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00784"
FT DOMAIN 712..813
FT /note="BEN 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00784"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 52..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 54..56
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q5T5X7"
FT COMPBIAS 52..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 376
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T5X7"
FT MOD_RES 486
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T5X7"
FT CROSSLNK 20
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q5T5X7"
FT CROSSLNK 20
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q5T5X7"
FT CROSSLNK 20
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q5T5X7"
FT CROSSLNK 39
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5T5X7"
FT CROSSLNK 54
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5T5X7"
FT CROSSLNK 56
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5T5X7"
FT CROSSLNK 71
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5T5X7"
FT CROSSLNK 126
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5T5X7"
FT CROSSLNK 127
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5T5X7"
FT CROSSLNK 135
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5T5X7"
FT CROSSLNK 140
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5T5X7"
FT CROSSLNK 156
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5T5X7"
FT CROSSLNK 174
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5T5X7"
FT CROSSLNK 424
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5T5X7"
FT CROSSLNK 509
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q5T5X7"
FT CROSSLNK 509
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q5T5X7"
FT CROSSLNK 525
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5T5X7"
FT CROSSLNK 697
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5T5X7"
SQ SEQUENCE 825 AA; 94155 MW; 9E447AF24F28ED8D CRC64;
MNSTEISEDV EEVLKNNPVK AEGSDATLDC SRNSRASEKH LLESVLTALH DSSKRKQLDS
DGQPDSVPSV KRRRLIPEAL LAGMRTRENS SPCQGNGEPA SRGRSGSCAW PAEEEPSTEA
TVPSYKKPLY GISHKIMEKK NPPSGDLLSP YELFEKANSS SGPSPLRLLS ESQKRECGVG
VATDGDLNIY FLIQKMFYML NGLTTNMSQL HSKMDLLSLE VSRVKKQVSP SELVAKFQPP
PEYQLTASEL KQIAEQSLSC GDLACRLLLQ LFPELFSDVD FSRGCSACGF AAKRKLESLH
LQLIRNYVEV YYPNVKDTAV WQAECLPQLN DFFSRFWAQR EMEDSQPGGQ VTNFFEADQV
DAGHFLDNKD QEEALSLDRS STIASDHVVD TQDLTEFLDE ASSPGEFAVF LLHRLFPELF
DHRKLGEQYS CYGDGGKQEL DPQRLQIIRN YTEIYFPDMQ EEEAWLQQCA QRINDELEGL
GLEGGSEGEA PRDDCYDSSS LPDDISVVKV EDNFEGERPG RRSKKIWLVP IDFDKLEIPQ
PDFEMPGSDC LLSKEQLRSI YESSLSIGNF ASRLLVHLFP ELFTHENLRK QYNCSGSLGK
KQLDPARIRL IRHYVQLLYP RAKNDRVWTL EFVGKLDERC RRRDTEQRRS YQQQRKVHVP
GPECRDLASY AINPERFREE FEGPPLPPER SSKDFCKIPL DELVVPSPDF PVPSPYLLSD
KEVREIVQQS LSVGNFAARL LVRLFPELFT TENLRLQYNH SGACNKKQLD PTRLRLIRHY
VEAVYPVEKM EEVWHYECIP SIDERCRRPN RKKCDILKKA KKVEK
