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Protein

Regulatory protein NPR4

Gene

NPR4

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

Functioni

May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). Involved in the regulation of basal defense responses against pathogens, and may be implicated in the cross-talk between the SA- and JA-dependent signaling pathways.By similarity2 Publications

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

GO - Molecular functioni

  • salicylic acid binding Source: TAIR

GO - Biological processi

  • defense response to bacterium Source: UniProtKB
  • defense response to bacterium, incompatible interaction Source: TAIR
  • defense response to fungus Source: UniProtKB
  • defense response to fungus, incompatible interaction Source: TAIR
  • effector dependent induction by symbiont of host immune response Source: TAIR
  • protein ubiquitination Source: UniProtKB-UniPathway
  • regulation of jasmonic acid mediated signaling pathway Source: UniProtKB
  • regulation of salicylic acid mediated signaling pathway Source: UniProtKB
  • response to bacterium Source: TAIR
  • response to fungus Source: TAIR
  • systemic acquired resistance Source: TAIR
Complete GO annotation...

Keywords - Biological processi

Plant defense, Ubl conjugation pathway

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Regulatory protein NPR4
Alternative name(s):
BTB/POZ domain-containing protein NPR4
Gene namesi
Name:NPR4
Ordered Locus Names:At4g19660
ORF Names:T16H5.20
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G19660.

Subcellular locationi

  • Nucleus 1 Publication

GO - Cellular componenti

  • nucleus Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

Enhanced susceptibility to the virulent bacterial pathogen Pseudomonas syringe and to the fungal pathogen Erysiphe cichoracearum (powdery mildew).1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi321 – 3211H → Y: Abolishes interaction with TGA2 or with TGA7. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 574574Regulatory protein NPR4PRO_0000407993Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei11 – 111PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ5ICL9.
PRIDEiQ5ICL9.

Expressioni

Inductioni

Up-regulated following pathogen challenge or salicylic acid (SA) treatment, and down-regulated by methyl jasmonic acid (MeJA) treatment.2 Publications

Gene expression databases

GenevisibleiQ5ICL9. AT.

Interactioni

Subunit structurei

Interacts with TGA2, TGA3, TGA5, TGA6 and TGA7.2 Publications

Protein-protein interaction databases

BioGridi13003. 5 interactions.
DIPiDIP-40035N.
IntActiQ5ICL9. 5 interactions.
STRINGi3702.AT4G19660.1.

Structurei

3D structure databases

ProteinModelPortaliQ5ICL9.
SMRiQ5ICL9. Positions 267-357.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini54 – 13077BTBPROSITE-ProRule annotationAdd
BLAST
Repeati252 – 28029ANK 1Add
BLAST
Repeati281 – 31131ANK 2Add
BLAST
Repeati315 – 34430ANK 3Add
BLAST

Domaini

The BTB/POZ domain mediates the interaction with some component of ubiquitin ligase complexes.1 Publication

Sequence similaritiesi

Contains 3 ANK repeats.PROSITE-ProRule annotation
Contains 1 BTB (POZ) domain.PROSITE-ProRule annotation

Keywords - Domaini

ANK repeat, Repeat

Phylogenomic databases

eggNOGiKOG0504. Eukaryota.
COG0666. LUCA.
HOGENOMiHOG000240298.
InParanoidiQ5ICL9.
KOiK14508.
OMAiISDPVHE.
PhylomeDBiQ5ICL9.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR000210. BTB/POZ_dom.
IPR021094. NPR1/NIM1-like_C.
IPR024228. NPR_central_dom.
IPR011333. SKP1/BTB/POZ.
[Graphical view]
PfamiPF00651. BTB. 1 hit.
PF11900. DUF3420. 1 hit.
PF12313. NPR1_like_C. 1 hit.
[Graphical view]
SMARTiSM00248. ANK. 2 hits.
SM00225. BTB. 1 hit.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
SSF54695. SSF54695. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 1 hit.
PS50097. BTB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5ICL9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAATAIEPSS SISFTSSHLS NPSPVVTTYH SAANLEELSS NLEQLLTNPD
60 70 80 90 100
CDYTDAEIII EEEANPVSVH RCVLAARSKF FLDLFKKDKD SSEKKPKYQM
110 120 130 140 150
KDLLPYGNVG REAFLHFLSY IYTGRLKPFP IEVSTCVDSV CAHDSCKPAI
160 170 180 190 200
DFAVELMYAS FVFQIPDLVS SFQRKLRNYV EKSLVENVLP ILLVAFHCDL
210 220 230 240 250
TQLLDQCIER VARSDLDRFC IEKELPLEVL EKIKQLRVKS VNIPEVEDKS
260 270 280 290 300
IERTGKVLKA LDSDDVELVK LLLTESDITL DQANGLHYAV AYSDPKVVTQ
310 320 330 340 350
VLDLDMADVN FRNSRGYTVL HIAAMRREPT IIIPLIQKGA NASDFTFDGR
360 370 380 390 400
SAVNICRRLT RPKDYHTKTS RKEPSKYRLC IDILEREIRR NPLVSGDTPT
410 420 430 440 450
CSHSMPEDLQ MRLLYLEKRV GLAQLFFPAE ANVAMDVANV EGTSECTGLL
460 470 480 490 500
TPPPSNDTTE NLGKVDLNET PYVQTKRMLT RMKALMKTVE TGRRYFPSCY
510 520 530 540 550
EVLDKYMDQY MDEEIPDMSY PEKGTVKERR QKRMRYNELK NDVKKAYSKD
560 570
KVARSCLSSS SPASSLREAL ENPT
Length:574
Mass (Da):65,115
Last modified:February 15, 2005 - v1
Checksum:i11DCA45A220A7F46
GO

Sequence cautioni

The sequence CAA19683.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAB78968.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY785951 mRNA. Translation: AAW31628.1.
AL024486 Genomic DNA. Translation: CAA19683.1. Sequence problems.
AL161551 Genomic DNA. Translation: CAB78968.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE84211.1.
PIRiT04747.
RefSeqiNP_193701.2. NM_118086.2.
UniGeneiAt.32792.

Genome annotation databases

EnsemblPlantsiAT4G19660.1; AT4G19660.1; AT4G19660.
GeneIDi827710.
GrameneiAT4G19660.1; AT4G19660.1; AT4G19660.
KEGGiath:AT4G19660.

Cross-referencesi

Web resourcesi

PlantsUBQ

A functional genomics database for the ubiquitin/26S proteasome proteolytic pathway in plants

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY785951 mRNA. Translation: AAW31628.1.
AL024486 Genomic DNA. Translation: CAA19683.1. Sequence problems.
AL161551 Genomic DNA. Translation: CAB78968.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE84211.1.
PIRiT04747.
RefSeqiNP_193701.2. NM_118086.2.
UniGeneiAt.32792.

3D structure databases

ProteinModelPortaliQ5ICL9.
SMRiQ5ICL9. Positions 267-357.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi13003. 5 interactions.
DIPiDIP-40035N.
IntActiQ5ICL9. 5 interactions.
STRINGi3702.AT4G19660.1.

Proteomic databases

PaxDbiQ5ICL9.
PRIDEiQ5ICL9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G19660.1; AT4G19660.1; AT4G19660.
GeneIDi827710.
GrameneiAT4G19660.1; AT4G19660.1; AT4G19660.
KEGGiath:AT4G19660.

Organism-specific databases

TAIRiAT4G19660.

Phylogenomic databases

eggNOGiKOG0504. Eukaryota.
COG0666. LUCA.
HOGENOMiHOG000240298.
InParanoidiQ5ICL9.
KOiK14508.
OMAiISDPVHE.
PhylomeDBiQ5ICL9.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

PROiQ5ICL9.

Gene expression databases

GenevisibleiQ5ICL9. AT.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR000210. BTB/POZ_dom.
IPR021094. NPR1/NIM1-like_C.
IPR024228. NPR_central_dom.
IPR011333. SKP1/BTB/POZ.
[Graphical view]
PfamiPF00651. BTB. 1 hit.
PF11900. DUF3420. 1 hit.
PF12313. NPR1_like_C. 1 hit.
[Graphical view]
SMARTiSM00248. ANK. 2 hits.
SM00225. BTB. 1 hit.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
SSF54695. SSF54695. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 1 hit.
PS50097. BTB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "An Arabidopsis NPR1-like gene, NPR4, is required for disease resistance."
    Liu G., Holub E.B., Alonso J.M., Ecker J.R., Fobert P.R.
    Plant J. 41:304-318(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], GENE FAMILY, NOMENCLATURE, FUNCTION, DISRUPTION PHENOTYPE, INDUCTION, SUBCELLULAR LOCATION, INTERACTION WITH TGA FACTORS, MUTAGENESIS OF HIS-321.
    Strain: cv. Columbia.
    Tissue: Leaf.
  2. "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.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Cullins 3a and 3b assemble with members of the broad complex/tramtrack/bric-a-brac (BTB) protein family to form essential ubiquitin-protein ligases (E3s) in Arabidopsis."
    Gingerich D.J., Gagne J.M., Salter D.W., Hellmann H., Estelle M., Ma L., Vierstra R.D.
    J. Biol. Chem. 280:18810-18821(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN BTB.
  5. "Negative regulation of defense responses in Arabidopsis by two NPR1 paralogs."
    Zhang Y., Cheng Y.T., Qu N., Zhao Q., Bi D., Li X.
    Plant J. 48:647-656(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION, INTERACTION WITH TGA FACTORS.

Entry informationi

Entry nameiNPR4_ARATH
AccessioniPrimary (citable) accession number: Q5ICL9
Secondary accession number(s): O81848
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: February 15, 2005
Last modified: May 11, 2016
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

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.