RNG1B_ARATH
ID RNG1B_ARATH Reviewed; 460 AA.
AC Q0WX00; Q9ZW99;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Putative E3 ubiquitin-protein ligase RING1b;
DE EC=2.3.2.27;
DE AltName: Full=Polycomb complex protein RING1b;
DE AltName: Full=Protein RING1b;
DE Short=AtRING1b;
DE AltName: Full=RING-type E3 ubiquitin transferase RING1b {ECO:0000305};
DE AltName: Full=Ring finger protein 5;
GN Name=RING1B; Synonyms=RF5; OrderedLocusNames=At1g03770; ORFNames=F21M11.30;
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].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP GENE FAMILY ORGANIZATION.
RX PubMed=11983057; DOI=10.1186/gb-2002-3-4-research0016;
RA Kosarev P., Mayer K.F.X., Hardtke C.S.;
RT "Evaluation and classification of RING-finger domains encoded by the
RT Arabidopsis genome.";
RL Genome Biol. 3:RESEARCH0016.1-RESEARCH0016.12(2002).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CLF, COMPONENT OF THE
RP PRC1-LIKE COMPLEX, AND DISRUPTION PHENOTYPE.
RX PubMed=19097900; DOI=10.1016/j.cub.2008.11.019;
RA Xu L., Shen W.H.;
RT "Polycomb silencing of KNOX genes confines shoot stem cell niches in
RT Arabidopsis.";
RL Curr. Biol. 18:1966-1971(2008).
CC -!- FUNCTION: Putative E3 ubiquitin-protein ligase that mediates
CC monoubiquitination of 'Lys-119' of histone H2A (H2AK119ub), thereby
CC playing a central role in histone code and gene regulation.
CC {ECO:0000250}.
CC -!- FUNCTION: As part of the PRC1-like complex, repress class I KNOX gene
CC expression. PcG PRC1 complex maintains the transcriptionally repressive
CC state of many genes, including Hox genes, throughout development. PcG
CC PRC1 complex acts via chromatin remodeling and modification of
CC histones, rendering chromatin heritably changed in its expressibility.
CC {ECO:0000269|PubMed:19097900}.
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;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Heterodimer with RING1A. Interacts with CLF. Component of the
CC PRC1-like complex, at least composed of RING1A, RING1B and LHP1.
CC {ECO:0000269|PubMed:19097900}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19097900}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q0WX00-1; Sequence=Displayed;
CC -!- DOMAIN: The RING-type zinc finger domain mediates binding to an E2
CC ubiquitin-conjugating enzyme. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Normal phenotype. Drastic growth defects like
CC ectopic meristem formation and sterility when associated with the
CC disruption of RING1A. {ECO:0000269|PubMed:19097900}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD10691.1; 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; AC003027; AAD10691.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE27608.1; -; Genomic_DNA.
DR EMBL; AK226183; BAE98348.1; -; mRNA.
DR PIR; B86168; B86168.
DR RefSeq; NP_171873.2; NM_100256.3. [Q0WX00-1]
DR AlphaFoldDB; Q0WX00; -.
DR SMR; Q0WX00; -.
DR STRING; 3702.AT1G03770.2; -.
DR iPTMnet; Q0WX00; -.
DR PaxDb; Q0WX00; -.
DR PRIDE; Q0WX00; -.
DR ProteomicsDB; 227984; -. [Q0WX00-1]
DR EnsemblPlants; AT1G03770.1; AT1G03770.1; AT1G03770. [Q0WX00-1]
DR GeneID; 839413; -.
DR Gramene; AT1G03770.1; AT1G03770.1; AT1G03770. [Q0WX00-1]
DR KEGG; ath:AT1G03770; -.
DR Araport; AT1G03770; -.
DR eggNOG; KOG0311; Eukaryota.
DR InParanoid; Q0WX00; -.
DR OMA; RQSEAMT; -.
DR PhylomeDB; Q0WX00; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q0WX00; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q0WX00; baseline and differential.
DR Genevisible; Q0WX00; AT.
DR GO; GO:0035102; C:PRC1 complex; IPI:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0001709; P:cell fate determination; IMP:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0010076; P:maintenance of floral meristem identity; IMP:UniProtKB.
DR GO; GO:0010077; P:maintenance of inflorescence meristem identity; IMP:UniProtKB.
DR GO; GO:0010492; P:maintenance of shoot apical meristem identity; IMP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IGI:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR044592; RING1A/B.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR46537; PTHR46537; 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; Metal-binding; Nucleus;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..460
FT /note="Putative E3 ubiquitin-protein ligase RING1b"
FT /id="PRO_0000397097"
FT ZN_FING 103..143
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..69
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..271
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 460 AA; 51975 MW; A6713D9E8D34A66F CRC64;
MPSLKSFSAA EEEDDQLGRN SEAERFNPEA VEKEEDPDKM DEKDESGDEE DDVKRDQVEA
EDEEALGEEE DSKERSQSSS AGELSESEYM VVDLADICKD VQCSICLGII RKTRTVMECL
HRFCRECIDK SMRLGNNECP TCRKHCASRR SLRDDPNFDA LIAALFKNID KFEEEELNFR
QDDEARNKQI QASIAQVSQR QSKALVKRKS VGKGTAILSR SRRSGGGSRR RRNCRNIEQD
TSEANDDDDQ NKRGKDSSSD EPCERQRKKR SATQPSSSNA NNNDNCAGNG TEQTHQRDSR
VISPVLVWNS ELIAWGRGGT RSNTRQGNNN QGAISKRNAR LKRLVEYLGS LEGNSVELDI
HLKLVSLDTE GLLNLHEPYL CFRPTLLVKQ LREYVARHLK LKAEEVELLV SKDGDTVIGN
KTSTEKMQSL QDDETVAKLK VDCISSNGYM IVVYRRKQIA
