ID BRE1B_ARATH Reviewed; 899 AA. AC Q9C895; Q058L1; Q8LDW7; DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 16-JUN-2009, entry version 49. 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; eurosids II; 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] OF 518-899. 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 535-899. 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 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). 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 -!- 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 --------------------------------------------------------------------------- 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; -; Genomic_DNA. DR EMBL; BT029207; ABJ17142.1; -; mRNA. DR EMBL; AY085755; AAM62973.1; -; mRNA. DR IPI; IPI00541748; -. DR PIR; D96594; D96594. DR UniGene; At.43011; -. DR HSSP; P38398; 1JM7. DR IntAct; Q9C895; 4. DR PRIDE; Q9C895; -. DR GenomeReviews; CT485782_GR; AT1G55250. DR GenomeReviews; CT485782_GR; AT1G55255. DR TAIR; At1g55250; -. DR TAIR; At1g55255; -. DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-KW. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW. DR GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW. DR GO; GO:0019941; P:modification-dependent protein catabolic pr...; IEA:UniProtKB-KW. DR InterPro; IPR018957; Znf_C3HC4_RING-type. DR InterPro; IPR001841; Znf_RING. DR InterPro; IPR017907; Znf_RING_CS. DR Pfam; PF00097; zf-C3HC4; 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; Chromosomal protein; Coiled coil; KW Complete proteome; Ligase; Metal-binding; Nucleus; KW Ubl conjugation pathway; Zinc; Zinc-finger. FT CHAIN 1 899 E3 ubiquitin-protein ligase BRE1-like 2. FT /FTId=PRO_0000293109. FT ZN_FING 847 886 RING-type. FT COILED 63 96 Potential. FT COILED 217 300 Potential. FT COILED 437 660 Potential. FT COILED 706 737 Potential. FT COMPBIAS 782 837 Glu-rich. FT CONFLICT 518 520 LSN -> MLT (in Ref. 2; ABJ17142). FT CONFLICT 802 802 E -> ER (in Ref. 2; ABJ17142 and 3; FT AAM62973). FT CONFLICT 823 823 G -> D (in Ref. 3; AAM62973). SQ SEQUENCE 899 AA; 103240 MW; F6CF0A4E82787BF0 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 DEREKKKLEE ELMELNKELE ELGSESVEAA IVRLQEEVKN CKNILKCGVC FDRPKEVVIV KCYHLFCQQC IQRSLEIRHR KCPGCGTAFG QNDVRLVKM //