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 08-MAY-2019, entry version 121. 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; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; OC 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., RA White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., RA Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., RA Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., RA Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., RA Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., RA Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., RA Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., RA Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., RA Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., RA Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., RA Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., RA Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., RA 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., RA Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.; RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis RT 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 RT reference 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 RP LOCATION, AND 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 RT dormancy."; RL Plant Cell 19:433-444(2007). CC -!- FUNCTION: E3 ubiquitin-protein ligase that monoubiquitinates H2B CC to 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 CC gene regulation. Forms a ubiquitin ligase complex in cooperation CC with the E2 enzyme UBC2/RAD6. {ECO:0000269|PubMed:17329563}. CC -!- CATALYTIC ACTIVITY: CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L- CC cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin- CC conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor CC protein]-L-lysine.; EC=2.3.2.27; CC Evidence={ECO:0000269|PubMed:17329563}; CC -!- PATHWAY: Protein modification; protein ubiquitination. CC -!- SUBUNIT: May act as a tetramer consisting of two copies of HUB1 CC and two 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 Note=Derived from EST data. No experimental confirmation CC available.; CC Name=2; CC IsoId=Q9C895-2; Sequence=VSP_038054, VSP_038055; CC Note=May be due to an intron retention. No experimental CC confirmation available.; 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 CC several pleiotropic phenotypes, including alterations in leaf CC color, plant architecture and flower morphology. CC {ECO:0000269|PubMed:17329563}. CC -!- MISCELLANEOUS: HUB1 and HUB2 are involved in the same processes, CC but are weakly or not redundant. 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 SMR; Q9C895; -. DR BioGrid; 27193; 1. DR IntAct; Q9C895; 3. DR STRING; 3702.AT1G55250.1; -. DR iPTMnet; Q9C895; -. DR PaxDb; Q9C895; -. 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 eggNOG; ENOG410Y5C6; LUCA. DR HOGENOM; HOG000006004; -. DR InParanoid; Q9C895; -. DR KO; K10696; -. 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: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:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro. 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; KW Complete proteome; Metal-binding; Nucleus; Reference proteome; KW Transferase; Ubl conjugation pathway; Zinc; Zinc-finger. FT CHAIN 1 900 E3 ubiquitin-protein ligase BRE1-like 2. FT /FTId=PRO_0000293109. FT ZN_FING 848 887 RING-type. {ECO:0000255|PROSITE- FT ProRule:PRU00175}. FT COILED 63 96 {ECO:0000255}. FT COILED 217 300 {ECO:0000255}. FT COILED 437 660 {ECO:0000255}. FT COILED 706 737 {ECO:0000255}. FT COMPBIAS 782 838 Glu-rich. FT VAR_SEQ 1 517 Missing (in isoform 2). FT {ECO:0000303|Ref.3}. FT /FTId=VSP_038054. FT VAR_SEQ 518 520 LSN -> MLT (in isoform 2). FT {ECO:0000303|Ref.3}. FT /FTId=VSP_038055. FT CONFLICT 824 824 G -> D (in Ref. 3; AAM62973). FT {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 //