RHB1A_ARATH
ID RHB1A_ARATH Reviewed; 190 AA.
AC Q2HIJ8; F4JH43; Q8GXM5; Q9ZT44;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Probable E3 ubiquitin-protein ligase RHB1A {ECO:0000305};
DE EC=2.3.2.27;
DE AltName: Full=RING-H2 finger B1a {ECO:0000303|PubMed:9781696};
DE AltName: Full=RING-H2 zinc finger protein RHB1a {ECO:0000305};
DE AltName: Full=RING-type E3 ubiquitin transferase RHB1A {ECO:0000305};
GN Name=RHB1A {ECO:0000303|PubMed:9781696};
GN OrderedLocusNames=At4g00335 {ECO:0000312|Araport:AT4G00335};
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 [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=9781696; DOI=10.1016/s0014-5793(98)01143-0;
RA Jensen R.B., Jensen K.L., Jespersen H.M., Skriver K.;
RT "Widespread occurrence of a highly conserved RING-H2 zinc finger motif in
RT the model plant Arabidopsis thaliana.";
RL FEBS Lett. 436:283-287(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.
CC -!- FUNCTION: Probable E3 ubiquitin-protein ligase that may possess E3
CC ubiquitin ligase activity in vitro. {ECO:0000250|UniProtKB:Q9ZT50}.
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. {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences. {ECO:0000305};
CC Name=1;
CC IsoId=Q2HIJ8-1; Sequence=Displayed;
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DR EMBL; AF079179; AAC69853.1; -; mRNA.
DR EMBL; AF195115; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002687; AEE81859.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE81860.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE81861.2; -; Genomic_DNA.
DR EMBL; AK118155; BAC42779.2; -; mRNA.
DR EMBL; BT024583; ABD42981.1; -; mRNA.
DR EMBL; AK228408; BAF00342.1; -; mRNA.
DR EMBL; AY087523; AAM65065.1; -; mRNA.
DR PIR; T51851; T51851.
DR RefSeq; NP_001319828.1; NM_001340240.1. [Q2HIJ8-1]
DR RefSeq; NP_567171.1; NM_116256.4. [Q2HIJ8-1]
DR RefSeq; NP_974488.1; NM_202759.2. [Q2HIJ8-1]
DR AlphaFoldDB; Q2HIJ8; -.
DR SMR; Q2HIJ8; -.
DR STRING; 3702.AT4G00335.1; -.
DR iPTMnet; Q2HIJ8; -.
DR PaxDb; Q2HIJ8; -.
DR PRIDE; Q2HIJ8; -.
DR EnsemblPlants; AT4G00335.1; AT4G00335.1; AT4G00335. [Q2HIJ8-1]
DR EnsemblPlants; AT4G00335.2; AT4G00335.2; AT4G00335. [Q2HIJ8-1]
DR EnsemblPlants; AT4G00335.3; AT4G00335.3; AT4G00335. [Q2HIJ8-1]
DR GeneID; 828093; -.
DR Gramene; AT4G00335.1; AT4G00335.1; AT4G00335. [Q2HIJ8-1]
DR Gramene; AT4G00335.2; AT4G00335.2; AT4G00335. [Q2HIJ8-1]
DR Gramene; AT4G00335.3; AT4G00335.3; AT4G00335. [Q2HIJ8-1]
DR KEGG; ath:AT4G00335; -.
DR Araport; AT4G00335; -.
DR TAIR; locus:505006415; AT4G00335.
DR eggNOG; KOG0800; Eukaryota.
DR InParanoid; Q2HIJ8; -.
DR OMA; VYIYHQQ; -.
DR PhylomeDB; Q2HIJ8; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q2HIJ8; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q2HIJ8; baseline and differential.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Metal-binding; Reference proteome; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..190
FT /note="Probable E3 ubiquitin-protein ligase RHB1A"
FT /id="PRO_0000436414"
FT ZN_FING 139..180
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT CONFLICT 137
FT /note="D -> E (in Ref. 1; AAC69853 and 7; AAM65065)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="T -> A (in Ref. 4; BAC42779)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 190 AA; 20954 MW; 5176550CB88DBFE3 CRC64;
MGGCCSSSRK SHLVGTPVYY YCPESFEELV PSGTRAGVGS AFTTGLLVDI GLETSIPDTF
CAPAPLPYDL LLGRPQCTDS ESIKGRMSGS SFETLATCED LGESDCKTLA SSVILSPRKS
DFSKHQGLKI LVDEEEDCCP ICFEDYDVEN PRLTTKCEHE FHLSCLLEWI ERSDRCPICD
KEVVFDDRLN
