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 20-APR-2010, entry version 59. DE RecName: Full=E3 ubiquitin-protein ligase BRE1-like 2; DE EC=6.3.2.-; DE AltName: Full=Protein HISTONE MONOUBIQUITINATION 2; DE Short=AtHUB2; 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; core eudicotyledons; OC rosids; malvids; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=21016719; 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 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 [3] 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 [4] 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 [5] RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND DISRUPTION RP 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). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316, AND MASS RP SPECTROMETRY. RC TISSUE=Seedling; RX PubMed=19376835; DOI=10.1104/pp.109.138677; RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., RA Grossmann J., Gruissem W., Baginsky S.; RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel RT chloroplast kinase substrates and phosphorylation networks."; RL Plant Physiol. 150:889-903(2009). 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. 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 (By similarity). CC -!- INTERACTION: CC Self; NbExp=1; IntAct=EBI-2012230, EBI-2012230; CC Q8RXD6:HUB1; NbExp=1; IntAct=EBI-2012230, EBI-2012188; CC -!- SUBCELLULAR LOCATION: Nucleus. 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 -!- DEVELOPMENTAL STAGE: Constant throughout the cell cycle. CC -!- DOMAIN: The RING-type zinc finger domain mediates binding to an E2 CC ubiquitin-conjugating enzyme (By similarity). 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 -!- MISCELLANEOUS: HUB1 and HUB2 are involved in the same processes, CC but are weakly or not redundant. CC -!- SIMILARITY: Belongs to the BRE1 family. CC -!- SIMILARITY: Contains 1 RING-type zinc finger. CC -!- SEQUENCE CAUTION: CC Sequence=AAG51572.1; Type=Erroneous gene model prediction; 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; AY085755; AAM62973.1; -; mRNA. DR EMBL; BT029207; ABJ17142.1; -; mRNA. DR IPI; IPI00541748; -. DR IPI; IPI00891911; -. DR PIR; D96594; D96594. DR RefSeq; NP_564680.4; -. DR UniGene; At.43011; -. DR UniGene; Rsa.21776; -. DR HSSP; P38398; 1JM7. DR IntAct; Q9C895; 4. DR STRING; Q9C895; -. DR PRIDE; Q9C895; -. DR GeneID; 841968; -. DR GenomeReviews; CT485782_GR; AT1G55250. DR TAIR; At1g55250; -. DR eggNOG; KOG0978; -. DR HOGENOM; HBG320274; -. DR InParanoid; Q9C895; -. DR OMA; YECLKTR; -. DR PhylomeDB; Q9C895; -. DR Genevestigator; Q9C895; -. DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-KW. DR GO; GO:0005634; C:nucleus; IDA:TAIR. DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW. DR GO; GO:0042803; F:protein homodimerization activity; IPI:TAIR. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0033523; P:histone H2B ubiquitination; IMP:TAIR. DR GO; GO:0010390; P:histone monoubiquitination; IMP:TAIR. DR GO; GO:0009965; P:leaf morphogenesis; IMP:TAIR. DR GO; GO:0010162; P:seed dormancy; IMP:TAIR. DR GO; GO:0010228; P:vegetative to reproductive phase transition...; IMP:TAIR. DR InterPro; IPR001841; Znf_RING. DR InterPro; IPR017907; Znf_RING_CS. 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; Chromosomal protein; KW Coiled coil; Complete proteome; Ligase; Metal-binding; Nucleus; KW Phosphoprotein; 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. FT COILED 63 96 Potential. FT COILED 217 300 Potential. FT COILED 437 660 Potential. FT COILED 706 737 Potential. FT COMPBIAS 782 838 Glu-rich. FT MOD_RES 316 316 Phosphoserine. FT VAR_SEQ 1 517 Missing (in isoform 2). FT /FTId=VSP_038054. FT VAR_SEQ 518 520 LSN -> MLT (in isoform 2). FT /FTId=VSP_038055. FT CONFLICT 824 824 G -> D (in Ref. 2; AAM62973). 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 //