BRE1A_ORYSJ
ID BRE1A_ORYSJ Reviewed; 884 AA.
AC Q7XU27; A0A0P0WDG3; B9FGG6; Q0JB84;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 3.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=E3 ubiquitin-protein ligase BRE1-like 1 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000269|PubMed:26143250};
DE AltName: Full=Protein HISTONE MONOUBIQUITINATION 1 {ECO:0000303|PubMed:26143250};
DE Short=OsHUB1 {ECO:0000303|PubMed:26143250};
DE AltName: Full=RING-type E3 ubiquitin transferase BRE1-like 1 {ECO:0000305};
GN Name=HUB1 {ECO:0000303|PubMed:26143250}; Synonyms=BRE1A {ECO:0000305};
GN OrderedLocusNames=Os04g0550400 {ECO:0000312|EMBL:BAS90372.1},
GN LOC_Os04g46450 {ECO:0000305};
GN ORFNames=OsJ_15692 {ECO:0000312|EMBL:EEE61450.1},
GN OSJNBb0034G17.7 {ECO:0000312|EMBL:CAD41603.3};
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=12447439; DOI=10.1038/nature01183;
RA Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA Li J., Hong G., Xue Y., Han B.;
RT "Sequence and analysis of rice chromosome 4.";
RL Nature 420:316-320(2002).
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] OF 23-884.
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 INTERACTION WITH SKIPA.
RX PubMed=19339499; DOI=10.1073/pnas.0901940106;
RA Hou X., Xie K., Yao J., Qi Z., Xiong L.;
RT "A homolog of human ski-interacting protein in rice positively regulates
RT cell viability and stress tolerance.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:6410-6415(2009).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH HUB2, 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).
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. H2B monoubiquitination (H2BK143ub1), mediated by
CC HUB1, modulates transcriptional regulation of anther development,
CC likely by promoting histone H3K4 dimethylation (H3K4me2) in the
CC chromatin of the key tapetum degradation-related genes C4, CP1 and
CC UDT1. {ECO:0000269|PubMed:26143250}.
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 -!- PATHWAY: Protein modification; protein ubiquitination. {ECO:0000305}.
CC -!- SUBUNIT: Interacts with SKIPA (PubMed:19339499). Interacts with HUB2
CC (PubMed:26143250). {ECO:0000269|PubMed:19339499,
CC 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 -!- 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 -!- SIMILARITY: Belongs to the BRE1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK067475; Type=Miscellaneous discrepancy; Note=Due to a cryptic acceptor splice site.; Evidence={ECO:0000305};
CC Sequence=BAF15403.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAS90372.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAD41603.3; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL663000; CAD41603.3; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008210; BAF15403.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014960; BAS90372.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CM000141; EEE61450.1; -; Genomic_DNA.
DR EMBL; AK067475; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015636384.1; XM_015780898.1.
DR AlphaFoldDB; Q7XU27; -.
DR SMR; Q7XU27; -.
DR BioGRID; 805626; 1.
DR STRING; 4530.OS04T0550400-01; -.
DR PaxDb; Q7XU27; -.
DR PRIDE; Q7XU27; -.
DR EnsemblPlants; Os04t0550400-01; Os04t0550400-01; Os04g0550400.
DR GeneID; 4336589; -.
DR Gramene; Os04t0550400-01; Os04t0550400-01; Os04g0550400.
DR KEGG; osa:4336589; -.
DR eggNOG; KOG0978; Eukaryota.
DR HOGENOM; CLU_002640_1_1_1; -.
DR InParanoid; Q7XU27; -.
DR OrthoDB; 782448at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000000763; Chromosome 4.
DR Proteomes; UP000007752; Chromosome 4.
DR Proteomes; UP000059680; Chromosome 4.
DR Genevisible; Q7XU27; 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:0051301; P:cell division; IEA:EnsemblPlants.
DR GO; GO:0044260; P:cellular macromolecule metabolic process; IEA:UniProt.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0050832; P:defense response to fungus; IEA:EnsemblPlants.
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:0051781; P:positive regulation of cell division; IEA:EnsemblPlants.
DR GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; 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 pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..884
FT /note="E3 ubiquitin-protein ligase BRE1-like 1"
FT /id="PRO_0000293110"
FT ZN_FING 832..871
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 49..86
FT /evidence="ECO:0000255"
FT COILED 216..541
FT /evidence="ECO:0000255"
FT COILED 580..663
FT /evidence="ECO:0000255"
FT COILED 696..762
FT /evidence="ECO:0000255"
FT COILED 789..827
FT /evidence="ECO:0000255"
FT COMPBIAS 107..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 884 AA; 100373 MW; C01CB1684FB0DF2A CRC64;
MGSTGEPDRK RRLSSSVAPG GGAPVSPAKR LAVAPTSEDK KLDFTVLKYK NQKLSEQLEA
HKFEYRALEN KFAGLKEKQR THNETLSLVN SSWEQLVADL KSRSFCKSGS PNSSPGSGHN
NVQKDGTCAP IERDTLRSLV ESGATESSGC LPGCHLGSDA PPLHLSTANA LGDIFFPSSD
LLQANEECAL AALTKLPEND RSKQLQSTSS NLLSSLNNVV QALSNLQLKH KQLAEDYQNQ
RDSSARKRAE HRRLKEELAS AASELEETNY KLAALKAQRD NTQGARIPYP TLGNKNMPED
KVRDKQREMQ DLEATHKELS ELISKRLVEI KRLHEERIEI LNKIATFQNI LMDFKSIRSS
KAFQLVNDRL QKSQAELDHY QTLLEKLQVD KDKFVWQERQ FNLKVDLAEI PERVSTYCES
SIADLKKDIQ KLCDEKNMLI LKLEEASREP GRNQVITKFK ALVSSIPREM GAMQSEMTKH
KEASLELNSL RAEVHSLSRI LSRKERDNEE ASCRSARAGS DITQLQSVIS DLKQTNKELK
LFADMYKRES TDSREIMESR DREFLEWAHV HALKSSLDES KLEQRVKAAN EAEAITQQRL
ATAEAEIAES GQKLGTSRKD LVSLSHMLKS KQEECEAYRV EVECIGQAYE DIQAQNQQLL
QQIIERDDDN TKIFMEGVKA KQTQDALHLE TYSLRRNLQQ ESSLMDLYNQ KIVSLEDQLK
MWSDRVGKLQ EDGWQQSVSL SNYQRKLVDV HRDAQKLMQS LDGIQANVGS SRLEVADLLI
ELEKERFSKK RIEDDLEVMS RKASSLRAKA RESAVLEKLR HEVKEYRGIL KCGICHDRQK
EVVITKCYHL FCNQCIQKSL GNRQRRCPSC SLSFGANDVK PIYI
