BET1_CAEEL
ID BET1_CAEEL Reviewed; 853 AA.
AC Q95Y80; H2KZI7;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 3.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Bromodomain-containing protein bet-1 {ECO:0000305};
GN Name=bet-1 {ECO:0000312|WormBase:Y119C1B.8a};
GN ORFNames=Y119C1B.8 {ECO:0000312|WormBase:Y119C1B.8a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, INTERACTION WITH HISTONE H4, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF VAL-113 AND GLU-585.
RX PubMed=20181741; DOI=10.1242/dev.042812;
RA Shibata Y., Takeshita H., Sasakawa N., Sawa H.;
RT "Double bromodomain protein BET-1 and MYST HATs establish and maintain
RT stable cell fates in C. elegans.";
RL Development 137:1045-1053(2010).
RN [3] {ECO:0000305}
RP FUNCTION.
RX PubMed=24285704; DOI=10.1242/bio.20136007;
RA Fisher K., Gee F., Wang S., Xue F., Knapp S., Philpott M., Wells C.,
RA Rodriguez M., Snoek L.B., Kammenga J., Poulin G.B.;
RT "Maintenance of muscle myosin levels in adult C. elegans requires both the
RT double bromodomain protein BET-1 and sumoylation.";
RL Biol. Open 2:1354-1363(2013).
RN [4] {ECO:0000305}
RP FUNCTION, INTERACTION WITH SMO-1 AND UBC-9, DOMAIN, DISRUPTION PHENOTYPE,
RP SUMOYLATION AT LYS-252, AND MUTAGENESIS OF LYS-252; LYS-253; LYS-264;
RP 276-LYS-LYS-277; LYS-304; LYS-313 AND LYS-315.
RX PubMed=24349540; DOI=10.1371/journal.pone.0083659;
RA Gee F., Fisher K., Klemstein U., Poulin G.B.;
RT "An RNAi-based dimorphic genetic screen identified the double bromodomain
RT protein BET-1 as a sumo-dependent attenuator of RAS-mediated signalling.";
RL PLoS ONE 8:E83659-E83659(2013).
RN [5] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24346701; DOI=10.1242/dev.090746;
RA Shibata Y., Sawa H., Nishiwaki K.;
RT "HTZ-1/H2A.z and MYS-1/MYST HAT act redundantly to maintain cell fates in
RT somatic gonadal cells through repression of ceh-22 in C. elegans.";
RL Development 141:209-218(2014).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=34593637; DOI=10.1073/pnas.2104664118;
RA Snoznik C., Medvedeva V., Mojsilovic-Petrovic J., Rudich P., Oosten J.,
RA Kalb R.G., Lamitina T.;
RT "The nuclear ubiquitin ligase adaptor SPOP is a conserved regulator of
RT C9orf72 dipeptide toxicity.";
RL Proc. Natl. Acad. Sci. U.S.A. 118:0-0(2021).
CC -!- FUNCTION: Required for the establishment and maintenance of stable cell
CC fate in several lineages including V5.pa, T, Z1/Z4 and QR lineages
CC probably by repressing the expression of cell fate determinants
CC (PubMed:20181741, PubMed:24346701). Required to maintain non-distal tip
CC cell (DTC) fate of somatic gonadal cells through the htz-1-mediated
CC repression of transcription factor ceh-22. Regulates the subnuclear
CC localization of histone variant htz-1 in somatic gonadal cells
CC (PubMed:24346701). Plays a role in the attenuation of the let-60/ras
CC pathway, probably by preventing expression of activators of the pathway
CC (PubMed:24285704, PubMed:24349540). Involved in adult locomotion. Acts
CC together with the sumoylation pathway to prevent muscle myosin
CC depletion in aging adults probably by preventing myoblast growth factor
CC receptor egl-15 overexpression (PubMed:24285704). May play a role in
CC vulva development (PubMed:24349540). {ECO:0000269|PubMed:20181741,
CC ECO:0000269|PubMed:24285704, ECO:0000269|PubMed:24346701,
CC ECO:0000269|PubMed:24349540}.
CC -!- SUBUNIT: Interacts with acetylated histone H4 (PubMed:20181741).
CC Interacts (via BROMO domain 2) with smo-1 and ubc-9 (PubMed:24349540).
CC {ECO:0000269|PubMed:20181741, ECO:0000269|PubMed:24349540}.
CC -!- INTERACTION:
CC Q95Y80; Q965X6: siah-1; NbExp=2; IntAct=EBI-311872, EBI-311877;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20181741}. Chromosome
CC {ECO:0000269|PubMed:20181741}. Note=Localizes to granular structures in
CC interphase and co-localizes with chromosomes during metaphase.
CC {ECO:0000269|PubMed:20181741}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:Y119C1B.8a};
CC IsoId=Q95Y80-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:Y119C1B.8b};
CC IsoId=Q95Y80-2; Sequence=VSP_057964, VSP_057965;
CC -!- TISSUE SPECIFICITY: Expressed in T-cells, Q-cells, V5-cells and their
CC descendants such as somatic gonad and syncytium.
CC {ECO:0000269|PubMed:20181741}.
CC -!- DOMAIN: The BROMO domain 2 is essential for the interaction with smo-1
CC and E2 enzyme ubc-9. {ECO:0000269|PubMed:24349540}.
CC -!- DISRUPTION PHENOTYPE: Abnormal cell fate determination of several
CC lineages. T.p daughter cells adopt a hypodermal cell fate instead of a
CC neuronal cell fate resulting in the loss of the phasmid socket cell.
CC Generation of ectopic PDE, AVM and PVM neurons, and distal tip cell
CC (DTC) (PubMed:20181741, PubMed:24346701). In addition, ectopic egl-17
CC expression in multiple vulva precursor cells and ectopic che-22
CC expression in extra distal tip cells (PubMed:24349540,
CC PubMed:24346701). Moderate increase in mpk-1 phosphorylation
CC (PubMed:24349540). RNAi-mediated knockdown further suppresses the age-
CC dependent paralysis phenotype of the spop-1 gk630214 or dr95 mutants
CC (PubMed:34593637). {ECO:0000269|PubMed:20181741,
CC ECO:0000269|PubMed:24346701, ECO:0000269|PubMed:24349540,
CC ECO:0000269|PubMed:34593637}.
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DR EMBL; BX284601; CCD68304.1; -; Genomic_DNA.
DR EMBL; BX284601; CCD68309.1; -; Genomic_DNA.
DR RefSeq; NP_491384.3; NM_058983.3.
DR RefSeq; NP_871879.1; NM_182079.3.
DR AlphaFoldDB; Q95Y80; -.
DR DIP; DIP-26262N; -.
DR IntAct; Q95Y80; 2.
DR STRING; 6239.Y119C1B.8a; -.
DR EPD; Q95Y80; -.
DR PaxDb; Q95Y80; -.
DR PeptideAtlas; Q95Y80; -.
DR EnsemblMetazoa; Y119C1B.8a.1; Y119C1B.8a.1; WBGene00022473. [Q95Y80-1]
DR EnsemblMetazoa; Y119C1B.8b.1; Y119C1B.8b.1; WBGene00022473.
DR UCSC; Y119C1B.8a; c. elegans. [Q95Y80-1]
DR WormBase; Y119C1B.8a; CE44037; WBGene00022473; bet-1. [Q95Y80-1]
DR WormBase; Y119C1B.8b; CE33207; WBGene00022473; bet-1. [Q95Y80-2]
DR eggNOG; KOG1474; Eukaryota.
DR GeneTree; ENSGT00940000155359; -.
DR InParanoid; Q95Y80; -.
DR OMA; KYLWRHH; -.
DR OrthoDB; 619848at2759; -.
DR PhylomeDB; Q95Y80; -.
DR Reactome; R-CEL-8951936; RUNX3 regulates p14-ARF.
DR SignaLink; Q95Y80; -.
DR PRO; PR:Q95Y80; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00022473; Expressed in embryo and 4 other tissues.
DR ExpressionAtlas; Q95Y80; baseline and differential.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005694; C:chromosome; IDA:WormBase.
DR GO; GO:0070090; C:metaphase plate; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0070577; F:lysine-acetylated histone binding; IDA:WormBase.
DR GO; GO:0032183; F:SUMO binding; IPI:WormBase.
DR GO; GO:0001708; P:cell fate specification; IGI:WormBase.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0071965; P:multicellular organismal locomotion; IMP:UniProtKB.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IMP:UniProtKB.
DR GO; GO:0009996; P:negative regulation of cell fate specification; IMP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0014018; P:neuroblast fate specification; IMP:WormBase.
DR GO; GO:0071168; P:protein localization to chromatin; IMP:UniProtKB.
DR GO; GO:0031647; P:regulation of protein stability; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:WormBase.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0040028; P:regulation of vulval development; IMP:WormBase.
DR CDD; cd05497; Bromo_Brdt_I_like; 1.
DR CDD; cd05498; Bromo_Brdt_II_like; 1.
DR Gene3D; 1.20.1270.220; -; 1.
DR Gene3D; 1.20.920.10; -; 2.
DR InterPro; IPR043508; Bromo_Brdt_I.
DR InterPro; IPR043509; Bromo_Brdt_II.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR027353; NET_dom.
DR InterPro; IPR038336; NET_sf.
DR Pfam; PF17035; BET; 1.
DR Pfam; PF00439; Bromodomain; 2.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 2.
DR SUPFAM; SSF47370; SSF47370; 2.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 2.
DR PROSITE; PS51525; NET; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Bromodomain; Chromosome; Coiled coil;
KW Isopeptide bond; Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..853
FT /note="Bromodomain-containing protein bet-1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000434603"
FT DOMAIN 56..128
FT /note="Bromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 277..349
FT /note="Bromo 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 516..601
FT /note="NET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00857"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 819..838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 419..458
FT /evidence="ECO:0000255"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..245
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..414
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..625
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..662
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..696
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 712..740
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..761
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 783..812
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 252
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:24349540"
FT VAR_SEQ 739..765
FT /note="APKPAPVPAPTSSRPPAAPRPPSKPKK -> KFYNCFHSYTPPLKVEKKIIK
FT LLVNFC (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_057964"
FT VAR_SEQ 766..853
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_057965"
FT MUTAGEN 113
FT /note="V->I: In os118; 50 percent of animals lack phasmid
FT socket cell and have an ectopic distal tip cell; when
FT associated with K-585."
FT /evidence="ECO:0000269|PubMed:20181741"
FT MUTAGEN 252
FT /note="K->R: Loss of interaction with smo-1 and ubc-9."
FT /evidence="ECO:0000269|PubMed:24349540"
FT MUTAGEN 253
FT /note="K->R: No effect on the interaction with smo-1 and
FT ubc-9."
FT /evidence="ECO:0000269|PubMed:24349540"
FT MUTAGEN 264
FT /note="K->R: No effect on the interaction with smo-1; when
FT associated with R-276 and R-277."
FT /evidence="ECO:0000269|PubMed:24349540"
FT MUTAGEN 276..277
FT /note="KK->RR: No effect on the interaction with smo-1;
FT when associated with R-264."
FT /evidence="ECO:0000269|PubMed:24349540"
FT MUTAGEN 304
FT /note="K->R: No effect on the interaction with smo-1; when
FT associated with R-313 and R-315."
FT /evidence="ECO:0000269|PubMed:24349540"
FT MUTAGEN 313
FT /note="K->R: No effect on the interaction with smo-1; when
FT associated with R-304 and R-315."
FT /evidence="ECO:0000269|PubMed:24349540"
FT MUTAGEN 315
FT /note="K->R: No effect on the interaction with smo-1; when
FT associated with R-304 and R-313."
FT /evidence="ECO:0000269|PubMed:24349540"
FT MUTAGEN 585
FT /note="E->K: In os118; 50 percent of animals lack phasmid
FT socket cell and have an ectopic distal tip cell; when
FT associated with I-113."
FT /evidence="ECO:0000269|PubMed:20181741"
SQ SEQUENCE 853 AA; 94086 MW; 7B4C4A18226A35A5 CRC64;
MSEGSGDQSQ QRPWASPRQQ PIKGIVQPRV LPPFGKPTRH TNKLDYIMTT VLKEAGKHKH
VWPFQKPVDA VALCIPLYHE RVARPMDLKT IENRLKSTYY TCAQECIDDI ETVFQNCYTF
NGKEDDVTIM AQNVHEVIKK SLEQAPREEH DMDVYWGKNK KKPAKSDGGS KSSSSKKNDA
RGPSEAPSEA GSEVSSVTTA SAAAPTVSES ASVAAKPERK VAGKKTGKRK AESEDDEKPE
PLRAKREVAV VKKEVHQPLL PSMKPCLKLL NDFSTKKYQE FAWPFNEPVD AEQLGLHDYH
KIIKEPMDLK SMKAKMESGA YKEPSDFEHD VRLMLRNCFL YNPVGDPVHS FGLRFQEVFD
RRWAELGDSS SRASSVAPQS APIAPTPKVA KSSAPKEPKE SRKEHKKETT FEASGAKSED
LMQINNALSM IREREEKLKA ELAAAQAIKD KLTSVKNRRE DNPNEPFPEK LINETRALCT
TQVGQNASSS SASSAALRNG RSKKAASARL YGYEFDSDDE DNKMALTYEE KRNLSNLINN
LPNNQLNTII SIIQRRERSA LMQQQLDDSE VELDFESLGD MCLREMGAFI KTIPTLNGNG
DDEKPKTSSN PTSSGATGSK GSSSLESKNG KKKKNFNMSE SSDDETSNSR KRRKRESSES
QSSSSSDDDS DDEDRPSIPR KSGQPPSTSR EWNQSSAPPP RMGGMGGQPP MSRVPASSST
SVSAIGKNNA AASSNSYQAP KPAPVPAPTS SRPPAAPRPP SKPKKTGGAS ILDTLLPDTF
GASPPQFFQS QPTTSATIRS PTESQPGNGE DEQTRIQRMR MEAKRARQKE DEGSVSLSNQ
MEMMAAFEFD NTY
