BRE1A_ARATH
ID BRE1A_ARATH Reviewed; 878 AA.
AC Q8RXD6; O22156; O22157;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 142.
DE RecName: Full=E3 ubiquitin-protein ligase BRE1-like 1;
DE Short=AtBRE1;
DE EC=2.3.2.27 {ECO:0000269|PubMed:17329563, ECO:0000269|PubMed:17329565};
DE AltName: Full=Protein HISTONE MONOUBIQUITINATION 1;
DE Short=AtHUB1;
DE AltName: Full=Protein REDUCED DORMANCY 4 {ECO:0000303|PubMed:21799800};
DE AltName: Full=RING-type E3 ubiquitin transferase BRE1-like 1 {ECO:0000305};
GN Name=HUB1; Synonyms=BRE1A, RDO4 {ECO:0000303|PubMed:21799800};
GN OrderedLocusNames=At2g44950/At2g44960;
GN ORFNames=T13E15.24/T13E15.23, T14P1.25/T14P1.24;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP IDENTIFICATION.
RX PubMed=12535538; DOI=10.1016/s1097-2765(02)00826-2;
RA Hwang W.W., Venkatasubrahmanyam S., Ianculescu A.G., Tong A., Boone C.,
RA Madhani H.D.;
RT "A conserved RING finger protein required for histone H2B
RT monoubiquitination and cell size control.";
RL Mol. Cell 11:261-266(2003).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF 712-GLN--ILE-878,
RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=17329565; DOI=10.1105/tpc.106.041319;
RA Fleury D., Himanen K., Cnops G., Nelissen H., Boccardi T.M., Maere S.,
RA Beemster G.T.S., Neyt P., Anami S., Robles P., Micol J.L., Inze D.,
RA Van Lijsebettens M.;
RT "The Arabidopsis thaliana homolog of yeast BRE1 has a function in cell
RT cycle regulation during early leaf and root growth.";
RL Plant Cell 19:417-432(2007).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=17329563; DOI=10.1105/tpc.106.049221;
RA Liu Y., Koornneef M., Soppe W.J.J.;
RT "The absence of histone H2B monoubiquitination in the Arabidopsis hub1
RT (rdo4) mutant reveals a role for chromatin remodeling in seed dormancy.";
RL Plant Cell 19:433-444(2007).
RN [7]
RP FUNCTION, INTERACTION WITH MED21, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=19286969; DOI=10.1105/tpc.108.062364;
RA Dhawan R., Luo H., Foerster A.M., Abuqamar S., Du H.N., Briggs S.D.,
RA Mittelsten Scheid O., Mengiste T.;
RT "HISTONE MONOUBIQUITINATION1 interacts with a subunit of the mediator
RT complex and regulates defense against necrotrophic fungal pathogens in
RT Arabidopsis.";
RL Plant Cell 21:1000-1019(2009).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21799800; DOI=10.1371/journal.pone.0022241;
RA Liu Y., Geyer R., van Zanten M., Carles A., Li Y., Horold A.,
RA van Nocker S., Soppe W.J.;
RT "Identification of the Arabidopsis REDUCED DORMANCY 2 gene uncovers a role
RT for the polymerase associated factor 1 complex in seed dormancy.";
RL PLoS ONE 6:E22241-E22241(2011).
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 also prerequisite for H3K4me and
CC maybe H3K79me. It thereby plays a central role in histone code and gene
CC regulation. Forms a ubiquitin ligase complex in cooperation with the E2
CC enzyme UBC2/RAD6. Required for the regulation of flowering time and
CC defense against necrotrophic fungal pathogens (PubMed:12535538,
CC PubMed:17329565, PubMed:17329563, PubMed:19286969). Involved in the
CC control of seed dormancy and germination (PubMed:21799800).
CC {ECO:0000269|PubMed:17329563, ECO:0000269|PubMed:17329565,
CC ECO:0000269|PubMed:19286969, ECO:0000269|PubMed:21799800}.
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:17329563,
CC ECO:0000269|PubMed:17329565};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: May act as a tetramer consisting of two copies of HUB1 and two
CC copies of HUB2 (By similarity). Interacts with MED21. {ECO:0000250,
CC ECO:0000269|PubMed:19286969}.
CC -!- INTERACTION:
CC Q8RXD6; Q9FLI3: AHG1; NbExp=3; IntAct=EBI-2012188, EBI-2363348;
CC Q8RXD6; Q9LEU7: CIPK5; NbExp=3; IntAct=EBI-2012188, EBI-2026322;
CC Q8RXD6; Q9SKK0: EBF1; NbExp=3; IntAct=EBI-2012188, EBI-401198;
CC Q8RXD6; Q9SU72: EDS1; NbExp=4; IntAct=EBI-2012188, EBI-1390454;
CC Q8RXD6; Q9LQT8: GAI; NbExp=3; IntAct=EBI-2012188, EBI-963606;
CC Q8RXD6; Q9SQI2: GI; NbExp=3; IntAct=EBI-2012188, EBI-446380;
CC Q8RXD6; Q9LV52: HSFC1; NbExp=3; IntAct=EBI-2012188, EBI-4457746;
CC Q8RXD6; Q8RXD6: HUB1; NbExp=5; IntAct=EBI-2012188, EBI-2012188;
CC Q8RXD6; P46639: KNAT1; NbExp=5; IntAct=EBI-2012188, EBI-530486;
CC Q8RXD6; Q9FIR9: LSU2; NbExp=3; IntAct=EBI-2012188, EBI-4424076;
CC Q8RXD6; Q6ID77: MED11; NbExp=2; IntAct=EBI-2012188, EBI-1386244;
CC Q8RXD6; O80959: PLP6; NbExp=3; IntAct=EBI-2012188, EBI-25515433;
CC Q8RXD6; Q1H5E9: PRDA1; NbExp=3; IntAct=EBI-2012188, EBI-1998055;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17329563,
CC ECO:0000269|PubMed:19286969}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:17329563, ECO:0000269|PubMed:17329565}.
CC -!- DEVELOPMENTAL STAGE: Constant throughout the cell cycle.
CC {ECO:0000269|PubMed:17329565}.
CC -!- INDUCTION: By infection with fungal pathogens.
CC {ECO:0000269|PubMed:19286969}.
CC -!- DOMAIN: The RING-type zinc finger domain mediates binding to an E2
CC ubiquitin-conjugating enzyme. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Plants have reduced seed dormancy and several
CC pleiotropic phenotypes, including alterations in leaf color, plant
CC architecture and flower morphology. {ECO:0000269|PubMed:17329563,
CC ECO:0000269|PubMed:21799800}.
CC -!- MISCELLANEOUS: HUB1 and HUB2 are involved in the same processes, but
CC are weakly or not redundant.
CC -!- SIMILARITY: Belongs to the BRE1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM14833.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At2g44950 and At2g44960.; Evidence={ECO:0000305};
CC Sequence=AAM14834.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At2g44950 and At2g44960.; Evidence={ECO:0000305};
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DR EMBL; AC002388; AAM14833.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC002388; AAM14834.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC10489.1; -; Genomic_DNA.
DR EMBL; BT010360; AAQ56803.1; -; mRNA.
DR EMBL; AY081322; AAL91211.1; -; mRNA.
DR PIR; T00397; T00397.
DR PIR; T00398; T00398.
DR RefSeq; NP_182022.2; NM_130060.4.
DR AlphaFoldDB; Q8RXD6; -.
DR SMR; Q8RXD6; -.
DR BioGRID; 4440; 48.
DR IntAct; Q8RXD6; 48.
DR STRING; 3702.AT2G44950.1; -.
DR iPTMnet; Q8RXD6; -.
DR PaxDb; Q8RXD6; -.
DR PRIDE; Q8RXD6; -.
DR ProteomicsDB; 240477; -.
DR EnsemblPlants; AT2G44950.1; AT2G44950.1; AT2G44950.
DR GeneID; 819104; -.
DR Gramene; AT2G44950.1; AT2G44950.1; AT2G44950.
DR KEGG; ath:AT2G44950; -.
DR Araport; AT2G44950; -.
DR TAIR; locus:2054997; AT2G44950.
DR eggNOG; KOG0978; Eukaryota.
DR HOGENOM; CLU_002640_1_0_1; -.
DR InParanoid; Q8RXD6; -.
DR OMA; THIEIMT; -.
DR OrthoDB; 782448at2759; -.
DR PhylomeDB; Q8RXD6; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q8RXD6; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8RXD6; baseline and differential.
DR Genevisible; Q8RXD6; AT.
DR GO; GO:0033503; C:HULC complex; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:TAIR.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:TAIR.
DR GO; GO:0051301; P:cell division; IMP:TAIR.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR GO; GO:0071894; P:histone H2B conserved C-terminal lysine ubiquitination; IBA:GO_Central.
DR GO; GO:0033523; P:histone H2B ubiquitination; IMP:TAIR.
DR GO; GO:0010390; P:histone monoubiquitination; IMP:TAIR.
DR GO; GO:0045087; P:innate immune response; IGI:TAIR.
DR GO; GO:0009965; P:leaf morphogenesis; IMP:TAIR.
DR GO; GO:0051781; P:positive regulation of cell division; IMP:TAIR.
DR GO; GO:0006513; P:protein monoubiquitination; IDA:TAIR.
DR GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; IMP:TAIR.
DR GO; GO:0010162; P:seed dormancy process; IMP:TAIR.
DR GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IMP:TAIR.
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; Metal-binding; Nucleus;
KW Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..878
FT /note="E3 ubiquitin-protein ligase BRE1-like 1"
FT /id="PRO_0000293108"
FT ZN_FING 826..865
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 48..76
FT /evidence="ECO:0000255"
FT COILED 200..261
FT /evidence="ECO:0000255"
FT COILED 293..382
FT /evidence="ECO:0000255"
FT COILED 537..624
FT /evidence="ECO:0000255"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 712..878
FT /note="Missing: In hub1-1/ang4-1; loss of function."
FT /evidence="ECO:0000269|PubMed:17329565"
SQ SEQUENCE 878 AA; 99719 MW; 483445F94F87C291 CRC64;
MASTGEPDRK RRHFSSISPS EAAAAVKKQP FFWPSSEDKL DTAVLQFQNL KLSQKLEAQQ
VECSILEDKL SQIKEKQLPY NSSLKTVHKS WEKLTASVES CSVRVSDSSS GAHRFVNKED
GSSPAVKNDF INRLLETGAT ESSSSNICSN QMEENGVNTS SQMTQTLYNL VAATEDLRCL
KDELYPTVLR TNLGKDLCGQ LALSELESEI KSFRGDLDDV LVKFKSLSRE LQSHRDADAK
VRVDLKRIRG ELEDEVVELQ QCNGDLSALR AERDATAGAF FPVLSLGNKL ATSDRERDKQ
RDLQDMETVL KELTVLASGR LQQLKNLHEE RTKMLGKMSN LQNKSKSVRC ISSSQACLSL
KDQLEKSKEA VFQYMALLEK LQVEKDSIVW KEREINIKNE LGDVSRKTSA VTDSRMASLD
SEIQKQLDEK MRIKTRLGNI SRERGRKEIF ADMKALISSF PEEMSSMRSQ LNNYKETAGG
IHSLRADVQS LSGVLCRKTK EYEALQLRSA DYASQLGDLN ATVCDLKNSH EELKLFLDMY
KRESTDARDI AEAKEQEYRA WAHVQSLKSS LDEQNLELRV KAANEAEAVS QQMLAAAEAE
IADLRQKMDD CKRDVAKHSD ILKSKHEEHG TYLSEIQTIG SAYEDIVPQN QQLLLQVTER
DDYNIKLFLE GITSRQMQDT LLIDKYIMDK DIQQGSAYAS FLSKKSSRIE DQLRFCTDQF
QKLAEDKYQK SVSLENLQKK RADIGNGLEQ ARSRLEESHS KVEQSRLDYG ALELELEIER
FNRRRIEEEM EIAKKKVSRL RSLIEGSSAI QKLRQELSEF KEILKCKACN DRPKEVVITK
CYHLFCNPCV QKLTGTRQKK CPTCSASFGP NDIKPIYI
