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Q9LR78

- BSU1_ARATH

UniProt

Q9LR78 - BSU1_ARATH

Protein

Serine/threonine-protein phosphatase BSU1

Gene

BSU1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 2 (15 Mar 2004)
      Previous versions | rss
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    Functioni

    Phosphatase that acts as a positive regulator of brassinolide signaling. Dephosphorylates BES1, a transcription factor that regulates the expression of brassinolide-response genes, thereby playing an important role in the regulation of response to brassinosteroids.1 Publication

    Catalytic activityi

    [a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.1 Publication

    Cofactori

    Binds 2 manganese ions per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi510 – 5101Manganese 1By similarity
    Metal bindingi512 – 5121Manganese 1By similarity
    Metal bindingi544 – 5441Manganese 1By similarity
    Metal bindingi544 – 5441Manganese 2By similarity
    Metal bindingi576 – 5761Manganese 2By similarity
    Active sitei577 – 5771Proton donorBy similarity
    Metal bindingi629 – 6291Manganese 2By similarity
    Metal bindingi707 – 7071Manganese 2By similarity

    GO - Molecular functioni

    1. iron ion binding Source: InterPro
    2. manganese ion binding Source: InterPro
    3. protein binding Source: TAIR
    4. protein serine/threonine phosphatase activity Source: TAIR

    GO - Biological processi

    1. brassinosteroid mediated signaling pathway Source: TAIR
    2. dephosphorylation Source: GOC
    3. regulation of protein localization Source: TAIR

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Ligandi

    Manganese, Metal-binding

    Enzyme and pathway databases

    BioCyciARA:AT1G03445-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein phosphatase BSU1 (EC:3.1.3.16)
    Alternative name(s):
    Bri1 suppressor protein 1
    Gene namesi
    Name:BSU1
    Ordered Locus Names:At1g03445, At1g03450
    ORF Names:F21B7.7
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 1

    Organism-specific databases

    TAIRiAT1G03445.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. nucleus Source: TAIR

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 793793Serine/threonine-protein phosphatase BSU1PRO_0000058904Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei444 – 4441PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRIDEiQ9LR78.

    Expressioni

    Tissue specificityi

    Mainly expressed in young, elongating tissues. In young seedlings, it is expressed at the base of the hypocotyl, at the tip and most peripheral cell layers of cotyledons, and in the vascular cylinder of roots, particularly in the elongation zone and at the point of emergence of lateral roots. In mature plants, it is still present in the root vasculature, but almost completely absent in fully expanded stems and leaves. In flowers, it is mainly expressed in sepal veins, anther filaments, and in the style, suggesting that BSU1 is expressed in actively growing regions and apparently enriched in vascular tissues.1 Publication

    Gene expression databases

    GenevestigatoriQ9LR78.

    Interactioni

    Protein-protein interaction databases

    BioGridi24043. 1 interaction.
    STRINGi3702.AT1G03445.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9LR78.
    SMRiQ9LR78. Positions 480-757.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati53 – 10957Kelch 1Add
    BLAST
    Repeati110 – 16051Kelch 2Add
    BLAST
    Repeati214 – 26249Kelch 3Add
    BLAST
    Repeati264 – 31451Kelch 4Add
    BLAST
    Repeati329 – 38860Kelch 5Add
    BLAST

    Sequence similaritiesi

    Belongs to the PPP phosphatase family. BSU subfamily.Curated
    Contains 5 Kelch repeats.Curated

    Keywords - Domaini

    Kelch repeat, Repeat

    Phylogenomic databases

    eggNOGiCOG0639.
    HOGENOMiHOG000246464.
    InParanoidiQ9LR78.
    KOiK14501.
    OMAiEGDITHI.
    PhylomeDBiQ9LR78.

    Family and domain databases

    Gene3Di2.120.10.80. 1 hit.
    2.130.10.80. 1 hit.
    3.60.21.10. 1 hit.
    InterProiIPR004843. Calcineurin-like_PHP_apaH.
    IPR015916. Gal_Oxidase_b-propeller.
    IPR015915. Kelch-typ_b-propeller.
    IPR029052. Metallo-depent_PP-like.
    IPR006186. Ser/Thr-sp_prot-phosphatase.
    IPR012391. Ser/Thr_prot_Pase_BSU1.
    [Graphical view]
    PfamiPF00149. Metallophos. 1 hit.
    [Graphical view]
    PIRSFiPIRSF036363. PPP_BSU1. 1 hit.
    PRINTSiPR00114. STPHPHTASE.
    SMARTiSM00156. PP2Ac. 1 hit.
    [Graphical view]
    SUPFAMiSSF56300. SSF56300. 1 hit.
    PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9LR78-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAPDQSYQYP SPSYESIQTF YDTDEDWPGP RCGHTLTAVF VNNSHQLILF    50
    GGSTTAVANH NSSLPEISLD GVTNSVHSFD VLTRKWTRLN PIGDVPSPRA 100
    CHAAALYGTL ILIQGGIGPS GPSDGDVYML DMTNNKWIKF LVGGETPSPR 150
    YGHVMDIAAQ RWLVIFSGNN GNEILDDTWA LDTRGPFSWD RLNPSGNQPS 200
    GRMYASGSSR EDGIFLLCGG IDHSGVTLGD TYGLKMDSDN VWTPVPAVAP 250
    SPRYQHTAVF GGSKLHVIGG ILNRARLIDG EAVVAVLDTE TGEWVDTNQP 300
    ETSASGANRQ NQYQLMRRCH HAAASFGSHL YVHGGIREDV LLDDLLVAET 350
    SQSSSPEPEE DNPDNYMLLD DYLMDEPKPL SSEPEASSFI MRSTSEIAMD 400
    RLAEAHNLPT IENAFYDSAI EGYVPLQHGA ETVGNRGGLV RTASLDQSTQ 450
    DLHKKVISTL LRPKTWTPPA NRDFFLSYLE VKHLCDEVEK IFMNEPTLLQ 500
    LKVPIKVFGD IHGQYGDLMR LFHEYGHPSV EGDITHIDYL FLGDYVDRGQ 550
    HSLEIIMLLF ALKIEYPKNI HLIRGNHESL AMNRIYGFLT ECEERMGESY 600
    GFEAWLKINQ VFDYLPLAAL LEKKVLCVHG GIGRAVTIEE IENIERPAFP 650
    DTGSMVLKDI LWSDPTMNDT VLGIVDNARG EGVVSFGPDI VKAFLERNGL 700
    EMILRAHECV IDGFERFADG RLITVFSATN YCGTAQNAGA ILVIGRDMVI 750
    YPKLIHPHPP PISSSEEDYT DKAWMQELNI EMPPTPARGE SSE 793
    Length:793
    Mass (Da):87,789
    Last modified:March 15, 2004 - v2
    Checksum:i07A083BD780EAA79
    GO

    Sequence cautioni

    The sequence AAF86539.1 differs from that shown. Reason: Erroneous gene model prediction.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY372269 mRNA. Translation: AAR19789.1.
    AC002560 Genomic DNA. Translation: AAF86539.1. Sequence problems.
    CP002684 Genomic DNA. Translation: AEE27572.1.
    RefSeqiNP_171844.6. NM_100227.6.
    UniGeneiAt.49845.

    Genome annotation databases

    EnsemblPlantsiAT1G03445.1; AT1G03445.1; AT1G03445.
    GeneIDi838804.
    KEGGiath:AT1G03445.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY372269 mRNA. Translation: AAR19789.1 .
    AC002560 Genomic DNA. Translation: AAF86539.1 . Sequence problems.
    CP002684 Genomic DNA. Translation: AEE27572.1 .
    RefSeqi NP_171844.6. NM_100227.6.
    UniGenei At.49845.

    3D structure databases

    ProteinModelPortali Q9LR78.
    SMRi Q9LR78. Positions 480-757.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 24043. 1 interaction.
    STRINGi 3702.AT1G03445.1-P.

    Proteomic databases

    PRIDEi Q9LR78.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT1G03445.1 ; AT1G03445.1 ; AT1G03445 .
    GeneIDi 838804.
    KEGGi ath:AT1G03445.

    Organism-specific databases

    TAIRi AT1G03445.

    Phylogenomic databases

    eggNOGi COG0639.
    HOGENOMi HOG000246464.
    InParanoidi Q9LR78.
    KOi K14501.
    OMAi EGDITHI.
    PhylomeDBi Q9LR78.

    Enzyme and pathway databases

    BioCyci ARA:AT1G03445-MONOMER.

    Miscellaneous databases

    PROi Q9LR78.

    Gene expression databases

    Genevestigatori Q9LR78.

    Family and domain databases

    Gene3Di 2.120.10.80. 1 hit.
    2.130.10.80. 1 hit.
    3.60.21.10. 1 hit.
    InterProi IPR004843. Calcineurin-like_PHP_apaH.
    IPR015916. Gal_Oxidase_b-propeller.
    IPR015915. Kelch-typ_b-propeller.
    IPR029052. Metallo-depent_PP-like.
    IPR006186. Ser/Thr-sp_prot-phosphatase.
    IPR012391. Ser/Thr_prot_Pase_BSU1.
    [Graphical view ]
    Pfami PF00149. Metallophos. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF036363. PPP_BSU1. 1 hit.
    PRINTSi PR00114. STPHPHTASE.
    SMARTi SM00156. PP2Ac. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56300. SSF56300. 1 hit.
    PROSITEi PS00125. SER_THR_PHOSPHATASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nuclear protein phosphatases with Kelch-repeat domains modulate the response to brassinosteroids in Arabidopsis."
      Mora-Garcia S., Vert G., Yin Y., Cano-Delgado A., Cheong H., Chory J.
      Genes Dev. 18:448-460(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    2. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
      Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
      , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
      Nature 408:816-820(2000) [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. "Arabidopsis PPP family of serine/threonine phosphatases."
      Farkas I., Dombradi V., Miskei M., Szabados L., Koncz C.
      Trends Plant Sci. 12:169-176(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENE FAMILY, NOMENCLATURE.

    Entry informationi

    Entry nameiBSU1_ARATH
    AccessioniPrimary (citable) accession number: Q9LR78
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 15, 2004
    Last sequence update: March 15, 2004
    Last modified: October 1, 2014
    This is version 101 of the entry and version 2 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3