BRE1B_ARATH
ID BRE1B_ARATH Reviewed; 900 AA.
AC Q9C895; Q058L1; Q8LDW7;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=E3 ubiquitin-protein ligase BRE1-like 2;
DE EC=2.3.2.27 {ECO:0000269|PubMed:17329563};
DE AltName: Full=Protein HISTONE MONOUBIQUITINATION 2;
DE Short=AtHUB2;
DE AltName: Full=RING-type E3 ubiquitin transferase BRE1-like 2 {ECO:0000305};
GN Name=HUB2; Synonyms=BRE1B; OrderedLocusNames=At1g55250/At1g55255;
GN ORFNames=F7A10.17;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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] (ISOFORM 2).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 518-900.
RC STRAIN=cv. Columbia;
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION, 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).
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. {ECO:0000269|PubMed:17329563}.
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 -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: May act as a tetramer consisting of two copies of HUB1 and two
CC copies of HUB2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17329563}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9C895-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9C895-2; Sequence=VSP_038054, VSP_038055;
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 -!- 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 -!- MISCELLANEOUS: HUB1 and HUB2 are involved in the same processes, but
CC are weakly or not redundant.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the BRE1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG51572.1; 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; AC027034; AAG51572.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33210.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33211.1; -; Genomic_DNA.
DR EMBL; AY085755; AAM62973.1; -; mRNA.
DR EMBL; BT029207; ABJ17142.1; -; mRNA.
DR PIR; D96594; D96594.
DR RefSeq; NP_001154428.1; NM_001160956.1. [Q9C895-2]
DR RefSeq; NP_564680.4; NM_104398.4. [Q9C895-1]
DR AlphaFoldDB; Q9C895; -.
DR SMR; Q9C895; -.
DR BioGRID; 27193; 1.
DR IntAct; Q9C895; 3.
DR STRING; 3702.AT1G55250.1; -.
DR iPTMnet; Q9C895; -.
DR PaxDb; Q9C895; -.
DR PRIDE; Q9C895; -.
DR ProteomicsDB; 240410; -. [Q9C895-1]
DR EnsemblPlants; AT1G55250.1; AT1G55250.1; AT1G55250. [Q9C895-1]
DR EnsemblPlants; AT1G55250.2; AT1G55250.2; AT1G55250. [Q9C895-2]
DR GeneID; 841968; -.
DR Gramene; AT1G55250.1; AT1G55250.1; AT1G55250. [Q9C895-1]
DR Gramene; AT1G55250.2; AT1G55250.2; AT1G55250. [Q9C895-2]
DR KEGG; ath:AT1G55250; -.
DR Araport; AT1G55250; -.
DR TAIR; locus:2035726; AT1G55250.
DR eggNOG; KOG0978; Eukaryota.
DR HOGENOM; CLU_002640_1_0_1; -.
DR InParanoid; Q9C895; -.
DR OrthoDB; 782448at2759; -.
DR PhylomeDB; Q9C895; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9C895; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C895; baseline and differential.
DR Genevisible; Q9C895; AT.
DR GO; GO:0033503; C:HULC complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
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:0006325; P:chromatin organization; IEA:UniProtKB-KW.
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: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 Alternative splicing; Chromatin regulator; Coiled coil; Metal-binding;
KW Nucleus; Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..900
FT /note="E3 ubiquitin-protein ligase BRE1-like 2"
FT /id="PRO_0000293109"
FT ZN_FING 848..887
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 63..96
FT /evidence="ECO:0000255"
FT COILED 217..300
FT /evidence="ECO:0000255"
FT COILED 437..660
FT /evidence="ECO:0000255"
FT COILED 706..737
FT /evidence="ECO:0000255"
FT COMPBIAS 17..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..517
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_038054"
FT VAR_SEQ 518..520
FT /note="LSN -> MLT (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_038055"
FT CONFLICT 824
FT /note="G -> D (in Ref. 3; AAM62973)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 900 AA; 103396 MW; 6F42D8C355815CF2 CRC64;
MENQESDEPM QKKPHLLDSV SPNSMARNSS PSHPIAKSVS FFDCDFSLLC LRLVDYEIDV
DATVLQLQNQ KLVQQLDLQK KQLYDVESKI QELQLNQTSY DDELISVNQL WNQLVDDLIL
LGVRAGANQE ALNYLDIVDK KRVPPCAADE TFLCRLLQVD SLDTSKSDEV VRKVEEALAL
RHSSTMELMG LFENTIDTQK TKAESISQSL HAVKSTEDAT IQLSSINDLM KEESKNLREM
IDALHVRHKE HSEQIQAYIS SHSTDQSELK HLKGQLEEIK AELEENRRKL ITLKMQKDAA
CEGHVTSPAI ANGSLSPEKP VDKTKLRELK DSIDEIKIMA EGRLSELQAS QEYNLSLSRQ
CQDIENELKD DQYIYSSRLY SLINDRIHHW NAELDRYKIL TEAIQAERSF VMRRDKELNL
RAESLEAANH KTTTVGSRIE VLEKKLQSCI IEKNGLELET EEAIQDSERQ DIKSEFIAMA
STLSKEMEMM EAQLKRWKDT AQDALYLREQ AQSLRVSLSN KADEQKGLED KCAKQMAEIK
SLKALIEKLL KEKLQLQNLA SICTRECNDD RGLAEIKDSQ RKAQAQAEEL KNVLDEHFLE
LRVKAAHETE SACQERLATA KAEIAELRTQ LDLSEREVLE LKEGIKVKEQ EAEASIAEME
TIGQAYEDMQ TQNQHLLQQV AERDDYNIKL VSESVKTKHA YNTHLSEKQV MEKQLHQVNA
SVENFKARIA HNEEQMKGCF SEAYKLIQED RHLVISLETT KWEVADADKE FRWLKSAVSS
SEKEYEQISR RTDDIKLELD DERREKKKLE EELMELNKEL EELGSESVEA AIVRLQEEVK
NCKNILKCGV CFDRPKEVVI VKCYHLFCQQ CIQRSLEIRH RKCPGCGTAF GQNDVRLVKM
