BRE1B_ORYSJ
ID BRE1B_ORYSJ Reviewed; 844 AA.
AC Q336R3; A3C7E7; B7EV99; Q336R2; Q8S7C5;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=E3 ubiquitin-protein ligase BRE1-like 2 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000269|PubMed:26143250, ECO:0000269|PubMed:26934377};
DE AltName: Full=Flowering-related RING protein 1 {ECO:0000303|PubMed:26934377};
DE AltName: Full=Protein HISTONE MONOUBIQUITINATION 2 {ECO:0000303|PubMed:26143250};
DE Short=OsHUB2 {ECO:0000303|PubMed:26143250};
DE AltName: Full=RING-type E3 ubiquitin transferase BRE1-like 2 {ECO:0000305};
GN Name=HUB2 {ECO:0000303|PubMed:26143250};
GN Synonyms=BRE1B {ECO:0000305}, FRRP1 {ECO:0000303|PubMed:26934377};
GN OrderedLocusNames=Os10g0565600 {ECO:0000312|EMBL:BAT12107.1},
GN LOC_Os10g41590 {ECO:0000312|EMBL:ABB47997.1};
GN ORFNames=OsJ_031219, OsJ_32496 {ECO:0000312|EMBL:EEE51418.1},
GN OSJNBa0057L21 {ECO:0000312|EMBL:AAL79702.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12791992; DOI=10.1126/science.1083523;
RA Yu Y., Rambo T., Currie J., Saski C., Kim H.-R., Collura K., Thompson S.,
RA Simmons J., Yang T.-J., Nah G., Patel A.J., Thurmond S., Henry D.,
RA Oates R., Palmer M., Pries G., Gibson J., Anderson H., Paradkar M.,
RA Crane L., Dale J., Carver M.B., Wood T., Frisch D., Engler F.,
RA Soderlund C., Palmer L.E., Teytelman L., Nascimento L., De la Bastide M.,
RA Spiegel L., Ware D., O'Shaughnessy A., Dike S., Dedhia N., Preston R.,
RA Huang E., Ferraro K., Kuit K., Miller B., Zutavern T., Katzenberger F.,
RA Muller S., Balija V., Martienssen R.A., Stein L., Minx P., Johnson D.,
RA Cordum H., Mardis E., Cheng Z., Jiang J., Wilson R., McCombie W.R.,
RA Wing R.A., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K.,
RA Moffat K., Hill J., Tsitrin T., Overton L., Bera J., Kim M., Jin S.,
RA Tallon L., Ciecko A., Pai G., Van Aken S., Utterback T., Reidmuller S.,
RA Bormann J., Feldblyum T., Hsiao J., Zismann V., Blunt S., de Vazeille A.R.,
RA Shaffer T., Koo H., Suh B., Yang Q., Haas B., Peterson J., Pertea M.,
RA Volfovsky N., Wortman J., White O., Salzberg S.L., Fraser C.M., Buell C.R.,
RA Messing J., Song R., Fuks G., Llaca V., Kovchak S., Young S., Bowers J.E.,
RA Paterson A.H., Johns M.A., Mao L., Pan H., Dean R.A.;
RT "In-depth view of structure, activity, and evolution of rice chromosome
RT 10.";
RL Science 300:1566-1569(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH HUB1, SUBCELLULAR LOCATION,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=26143250; DOI=10.1104/pp.114.256578;
RA Cao H., Li X., Wang Z., Ding M., Sun Y., Dong F., Chen F., Liu L.,
RA Doughty J., Li Y., Liu Y.X.;
RT "Histone H2B monoubiquitination mediated by HISTONE MONOUBIQUITINATION1 and
RT HISTONE MONOUBIQUITINATION2 is involved in anther development by regulating
RT tapetum degradation-related genes in rice.";
RL Plant Physiol. 168:1389-1405(2015).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, UBIQUITINATION, AND MUTAGENESIS OF CYS-830.
RX PubMed=26934377; DOI=10.1371/journal.pone.0150458;
RA Du Y., He W., Deng C., Chen X., Gou L., Zhu F., Guo W., Zhang J., Wang T.;
RT "Flowering-related RING protein 1 (FRRP1) regulates flowering time and
RT yield potential by affecting histone H2B monoubiquitination in rice (Oryza
RT Sativa).";
RL PLoS ONE 11:E0150458-E0150458(2016).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that monoubiquitinates H2B to
CC form H2BK143ub1. H2BK143ub1 gives a specific tag for epigenetic
CC transcriptional activation and is a prerequisite for H3 Lys-4
CC methylation (H3K4me). It thereby plays a central role in histone code
CC and gene regulation (PubMed:26143250, PubMed:26934377). H2B
CC monoubiquitination, mediated by HUB2, modulates transcriptional
CC regulation of anther development, likely by promoting histone H3K4
CC dimethylation (H3K4me2) in the chromatin of the key tapetum
CC degradation-related genes C4, CP1 and UDT1 (PubMed:26143250). H2B
CC monoubiquitination, mediated by HUB2, modulates transcriptional
CC regulation of genes associated with flowering time and plant yield
CC (PubMed:26934377). {ECO:0000269|PubMed:26143250,
CC ECO:0000269|PubMed:26934377}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000269|PubMed:26143250,
CC ECO:0000269|PubMed:26934377};
CC -!- PATHWAY: Protein modification; protein ubiquitination. {ECO:0000305}.
CC -!- SUBUNIT: Interacts with HUB1. {ECO:0000269|PubMed:26143250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26143250}.
CC -!- DOMAIN: The RING-type zinc finger domain mediates binding to an E2
CC ubiquitin-conjugating enzyme. {ECO:0000250}.
CC -!- PTM: Auto-ubiquitinated in vitro. {ECO:0000269|PubMed:26934377}.
CC -!- DISRUPTION PHENOTYPE: Semi-dwarf plants, early heading, and partial
CC sterility of spikelets due to defects in the anther developmental
CC program and pollen formation. {ECO:0000269|PubMed:26143250}.
CC -!- MISCELLANEOUS: Plant silencing HUB2 exhibit early flowering, increased
CC plant height, and increased panicle and grain length.
CC {ECO:0000269|PubMed:26934377}.
CC -!- SIMILARITY: Belongs to the BRE1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL79702.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=ABB47998.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC087599; AAL79702.1; ALT_SEQ; Genomic_DNA.
DR EMBL; DP000086; ABB47997.1; -; Genomic_DNA.
DR EMBL; DP000086; ABB47998.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008216; BAF27258.1; -; Genomic_DNA.
DR EMBL; AP014966; BAT12107.1; -; Genomic_DNA.
DR EMBL; CM000147; EEE51418.1; -; Genomic_DNA.
DR EMBL; AK103864; BAG96296.1; -; mRNA.
DR RefSeq; XP_015614586.1; XM_015759100.1.
DR AlphaFoldDB; Q336R3; -.
DR SMR; Q336R3; -.
DR BioGRID; 818457; 1.
DR STRING; 4530.OS10T0565600-01; -.
DR PaxDb; Q336R3; -.
DR PRIDE; Q336R3; -.
DR EnsemblPlants; Os10t0565600-01; Os10t0565600-01; Os10g0565600.
DR GeneID; 4349420; -.
DR Gramene; Os10t0565600-01; Os10t0565600-01; Os10g0565600.
DR KEGG; osa:4349420; -.
DR eggNOG; KOG0978; Eukaryota.
DR HOGENOM; CLU_002640_1_0_1; -.
DR InParanoid; Q336R3; -.
DR OMA; DENTSCT; -.
DR OrthoDB; 782448at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000000763; Chromosome 10.
DR Proteomes; UP000007752; Chromosome 10.
DR Proteomes; UP000059680; Chromosome 10.
DR Genevisible; Q336R3; OS.
DR GO; GO:0033503; C:HULC complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:EnsemblPlants.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0044260; P:cellular macromolecule metabolic process; IEA:UniProt.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0009908; P:flower development; IEA:UniProtKB-KW.
DR GO; GO:0071894; P:histone H2B conserved C-terminal lysine ubiquitination; IBA:GO_Central.
DR GO; GO:0010390; P:histone monoubiquitination; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IEA:EnsemblPlants.
DR GO; GO:0009965; P:leaf morphogenesis; IEA:EnsemblPlants.
DR GO; GO:0010162; P:seed dormancy process; IEA:EnsemblPlants.
DR GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IEA:EnsemblPlants.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR013956; E3_ubiquit_lig_Bre1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR23163; PTHR23163; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Coiled coil; Flowering; Metal-binding; Nucleus;
KW Reference proteome; Transferase; Ubl conjugation; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..844
FT /note="E3 ubiquitin-protein ligase BRE1-like 2"
FT /id="PRO_0000293112"
FT ZN_FING 792..831
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 244..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1..38
FT /evidence="ECO:0000255"
FT COILED 160..240
FT /evidence="ECO:0000255"
FT COILED 290..604
FT /evidence="ECO:0000255"
FT COILED 640..670
FT /evidence="ECO:0000255"
FT COMPBIAS 244..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 830
FT /note="C->S: Abolishes E3 ubiquitin-protein ligase
FT activity."
FT /evidence="ECO:0000269|PubMed:26934377"
SQ SEQUENCE 844 AA; 96498 MW; 2A57EDD94FDE5E94 CRC64;
MDAAALQYEN QKLVQQLEAQ KSKMRALEGK FKELRDEQCS YDNTLICLNK MWNQLIDDLV
LLGVRAGGDL NGLQALDHEE MSEESLESCP SEEIFLFRLL NSRNFRNNDD SSLSKLVEEA
LALRYSTTVT LMKSLQEAFA VQQARSESLS LALNGQNSSE DVIVALENHN DYLKEVVDNL
RQAVSIINRK HEKYLDEIEA FKNNQSRELH EVKCLSGELE ESMAELEESR RKLAVLQLQT
GGGSLMNTSA PNGVNGSVST DKSSDKGMGW RDLKDAVEEA KTLAANRLFE LHETQEDNLI
LSKQLEDIQD QLKDENYIVT SKPYTILSDQ LHHLNAEIER YRGLVEVLQN EKDQLMQKEE
EMLAKAESVD AVQQSITTYK AKIEDLEHEI QKLMAEKNDL EIKAEEALQD SGKKDFKDEI
HVMAASLSKE MELLDNQMNR SKDAASEALA LREEADYLRT LLAKKIDEQK EISDRYNTQV
TEIKSLKALI ETLDQEKQEL QFIVDMLGKE CSESRAISEI EESENRARKQ AEYLRKCLEE
HNLELRVKAA NEAETACQQR LSIAEAELED LRAKVDASER DVMKLKESIR IKEAEVDGHI
SEIETIGQAY EDMQTQNQHL LQQVADRDDF NIKLVSDSVK MKQAYGSLLA EKNMLQKQLQ
HVNSSLESSK LKITSGEEQM KTYVAQAMKS SSENRHLAIS LERTMLEVSD AEKELKWLRS
ATGSAEKEYE INQKKIAELK MELERERNER IKLEEEYEEV KNEVSELTSE TEETTIQKLQ
DEIKECKAIL KCGVCFDRPK EVVITKCFHL FCSPCIQRNL EIRHRKCPGC GTPFGQSDVR
EVKI
