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Protein

E3 ubiquitin-protein ligase BOI

Gene

BOI

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

E3 ubiquitin-protein ligase involved in the regulation of pathogen and abiotic stress responses by facilitating degradation of MYB108/BOI. Attenuates cell death by preventing caspase activation. Has no effect on the stability of the DELLA proteins. Not regulated by MYB108/BOI.3 Publications

Pathwayi: proteasomal ubiquitin-dependent pathway

This protein is involved in the pathway proteasomal ubiquitin-dependent pathway, which is part of Protein degradation.
View all proteins of this organism that are known to be involved in the pathway proteasomal ubiquitin-dependent pathway and in Protein degradation.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri254 – 29138RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • ligase activity Source: UniProtKB-KW
  • ubiquitin-protein transferase activity Source: TAIR
  • zinc ion binding Source: InterPro

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • defense response to bacterium Source: TAIR
  • defense response to fungus Source: TAIR
  • negative regulation of cysteine-type endopeptidase activity Source: TAIR
  • negative regulation of programmed cell death Source: TAIR
  • proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB-UniPathway
  • regulation of defense response Source: InterPro
  • response to gibberellin Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Apoptosis, Plant defense, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00144.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase BOI (EC:6.3.2.-)
Alternative name(s):
Inhibitor of apoptosis (IAP)-like protein
Short name:
AtILP
Protein BOTRYTIS SUSCEPTIBLE 1 INTERACTOR
Short name:
AtBOI
Gene namesi
Name:BOI
Synonyms:ILP
Ordered Locus Names:At4g19700
ORF Names:T16H5.60
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G19700.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

No effect on germination. Boi, brg1, brg2 and brg3 quadruple mutant shows a higher GA signaling resulting in a higher seed germination in the presence of paclobutrazol, precocious juvenile-to-adult phase transition and early flowering.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 304304E3 ubiquitin-protein ligase BOIPRO_0000424716Add
BLAST

Proteomic databases

PaxDbiO81851.
PRIDEiO81851.

Expressioni

Tissue specificityi

Expressed in leaves, siliques, roots, flowering tissues and stigma tips.1 Publication

Inductioni

Up-regulated by pathogen, methyl violagen, salicylic acid, 1-aminocyclopropane-1-carboxylic acid (ACC) and salt. Down-regulated by methyl jasmonate and gibberellic acid.1 Publication

Gene expression databases

GenevisibleiO81851. AT.

Interactioni

Subunit structurei

Interacts with MYB108/BOS1 and the DELLA proteins GAI, RGA, RGL1, RGL2 and RGL3.2 Publications

Protein-protein interaction databases

BioGridi13007. 43 interactions.
IntActiO81851. 23 interactions.
STRINGi3702.AT4G19700.1.

Structurei

3D structure databases

ProteinModelPortaliO81851.
SMRiO81851. Positions 250-303.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni178 – 21437WRD domainAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili197 – 22024Sequence analysisAdd
BLAST

Domaini

The N-terminal domain (1-150) prevents cell death by suppressing caspase-like protease activation.1 Publication
The WRD domain (178-214) is necessary for interaction with MYB108/BOS1.1 Publication
The RING-type zinc finger domain mediates binding to an E2 ubiquitin-conjugating enzyme. It is required for the ubiquitination activity, but dispensable and not sufficient for interaction with MYB108/BOS1 (PubMed:20921156).1 Publication

Sequence similaritiesi

Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri254 – 29138RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiKOG1100. Eukaryota.
ENOG4111S1X. LUCA.
HOGENOMiHOG000090929.
InParanoidiO81851.
KOiK19042.
OMAiVETQIWR.
PhylomeDBiO81851.

Family and domain databases

InterProiIPR017066. E3ligase_BOI.
IPR001841. Znf_RING.
[Graphical view]
PIRSFiPIRSF036836. RNase_bind_SBP1. 1 hit.
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O81851-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVQAHHMNI FSQFISPNRD CVKFQENMNH GEFEFTGGEV PLITGESFAV
60 70 80 90 100
EPLAAKANFN KAESGLSYNF TVPPLSTKRQ RDFQFSDSNA PVKRRSVAFD
110 120 130 140 150
SSSPSLINVE LVSQIQNQQQ SEIDRFVAQQ TEKLRIEIEA RQQTQTRMLA
160 170 180 190 200
SAVQNVIAKK LKEKDDEIVR IRNLNWVLQE RVKSLYVENQ IWRDIAQTNE
210 220 230 240 250
ANANTLRTNL DQVLAQLETF PTASAVVEDD AESSCGSCCG DGGGEAVTAV
260 270 280 290 300
GGGCKRCGER EASVLVLPCR HLCLCTVCGG SALLRTCPVC DMVMNASVHV

NMSS
Length:304
Mass (Da):33,509
Last modified:November 1, 1998 - v1
Checksum:i132989B291ECC9DD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti37 – 371Missing in AAL32681 (PubMed:14593172).Curated
Sequence conflicti37 – 371Missing in AAM47984 (PubMed:14593172).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL024486 Genomic DNA. Translation: CAA19687.1.
AL161551 Genomic DNA. Translation: CAB78972.1.
CP002687 Genomic DNA. Translation: AEE84218.1.
AY062603 mRNA. Translation: AAL32681.1.
AY114665 mRNA. Translation: AAM47984.1.
PIRiT04751.
RefSeqiNP_193705.1. NM_118090.3.
UniGeneiAt.27286.

Genome annotation databases

EnsemblPlantsiAT4G19700.1; AT4G19700.1; AT4G19700.
GeneIDi827714.
GrameneiAT4G19700.1; AT4G19700.1; AT4G19700.
KEGGiath:AT4G19700.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL024486 Genomic DNA. Translation: CAA19687.1.
AL161551 Genomic DNA. Translation: CAB78972.1.
CP002687 Genomic DNA. Translation: AEE84218.1.
AY062603 mRNA. Translation: AAL32681.1.
AY114665 mRNA. Translation: AAM47984.1.
PIRiT04751.
RefSeqiNP_193705.1. NM_118090.3.
UniGeneiAt.27286.

3D structure databases

ProteinModelPortaliO81851.
SMRiO81851. Positions 250-303.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi13007. 43 interactions.
IntActiO81851. 23 interactions.
STRINGi3702.AT4G19700.1.

Proteomic databases

PaxDbiO81851.
PRIDEiO81851.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G19700.1; AT4G19700.1; AT4G19700.
GeneIDi827714.
GrameneiAT4G19700.1; AT4G19700.1; AT4G19700.
KEGGiath:AT4G19700.

Organism-specific databases

TAIRiAT4G19700.

Phylogenomic databases

eggNOGiKOG1100. Eukaryota.
ENOG4111S1X. LUCA.
HOGENOMiHOG000090929.
InParanoidiO81851.
KOiK19042.
OMAiVETQIWR.
PhylomeDBiO81851.

Enzyme and pathway databases

UniPathwayiUPA00144.

Miscellaneous databases

PROiO81851.

Gene expression databases

GenevisibleiO81851. AT.

Family and domain databases

InterProiIPR017066. E3ligase_BOI.
IPR001841. Znf_RING.
[Graphical view]
PIRSFiPIRSF036836. RNase_bind_SBP1. 1 hit.
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  4. "The Arabidopsis Botrytis Susceptible1 Interactor defines a subclass of RING E3 ligases that regulate pathogen and stress responses."
    Luo H., Laluk K., Lai Z., Veronese P., Song F., Mengiste T.
    Plant Physiol. 154:1766-1782(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MYB108/BOS1, DOMAIN, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION BY PATHOGEN; METHYL VIOLAGEN; SALICYLIC ACID; GIBBERELLIC ACID; ACC; METHYL JASMONATE AND SALT.
  5. "Inhibitor of apoptosis (IAP)-like protein lacks a baculovirus IAP repeat (BIR) domain and attenuates cell death in plant and animal systems."
    Kim W.Y., Lee S.Y., Jung Y.J., Chae H.B., Nawkar G.M., Shin M.R., Kim S.Y., Park J.H., Kang C.H., Chi Y.H., Ahn I.P., Yun D.J., Lee K.O., Kim Y.M., Kim M.G., Lee S.Y.
    J. Biol. Chem. 286:42670-42678(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DOMAIN, SUBCELLULAR LOCATION.
  6. "DELLA proteins and their interacting RING Finger proteins repress gibberellin responses by binding to the promoters of a subset of gibberellin-responsive genes in Arabidopsis."
    Park J., Nguyen K.T., Park E., Jeon J.S., Choi G.
    Plant Cell 25:927-943(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH GAI; RGA; RGL1; RGL2 AND RGL3, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiBOI_ARATH
AccessioniPrimary (citable) accession number: O81851
Secondary accession number(s): Q8W4E8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 11, 2013
Last sequence update: November 1, 1998
Last modified: May 11, 2016
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Shares anti-apoptotic activity with IAP family proteins. However, it lacks the baculovirus IAP repeat (BIR) domain, which was shown to be essential for anti-apoptotic activity in other IAP family members (PubMed:21926169).1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.