Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9SR37

- BGL23_ARATH

UniProt

Q9SR37 - BGL23_ARATH

Protein

Beta-glucosidase 23

Gene

BGLU23

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Beta-D-glucosidase active on scopolin > esculin >> 4-MU-glucoside >> DIMBOA-glucoside. No activity with pNP-glucoside, oNP-glucoside and sinigrin as substrates. May possess beta-D-fucosidase activity. Required for the beneficial interaction with the endophytic fungus P.indica. May participate in the control of root colonization by P.indica by repressing defense responses and modulating other responses required for a mutualistic interaction.4 Publications

    Catalytic activityi

    Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.1 Publication

    Enzyme regulationi

    Activated by tissue damage and upon binding to PBP1 or PBP2.2 Publications

    Kineticsi

    1. KM=0.81 mM for scopolin (with recombinant enzyme)1 Publication
    2. KM=0.73 mM for scopolin (with native enzyme)1 Publication
    3. KM=9.7 mM for esculin (with recombinant enzyme)1 Publication
    4. KM=5.8 mM for esculin (with native enzyme)1 Publication

    pH dependencei

    Optimum pH is 5.5.1 Publication

    Temperature dependencei

    Optimum temperature is 35 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei54 – 541SubstrateBy similarity
    Binding sitei157 – 1571SubstrateBy similarity
    Binding sitei202 – 2021SubstrateBy similarity
    Active sitei203 – 2031Proton donorBy similarity
    Binding sitei346 – 3461SubstrateBy similarity
    Active sitei418 – 4181NucleophileBy similarity
    Binding sitei468 – 4681SubstrateBy similarity

    GO - Molecular functioni

    1. beta-glucosidase activity Source: TAIR
    2. copper ion binding Source: TAIR
    3. fucosidase activity Source: TAIR
    4. protease binding Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. protein homodimerization activity Source: UniProtKB

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro
    2. cellular response to cold Source: TAIR
    3. ER body organization Source: TAIR
    4. negative regulation of defense response Source: UniProtKB
    5. response to osmotic stress Source: TAIR
    6. response to salt stress Source: TAIR
    7. response to symbiotic fungus Source: TAIR

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Enzyme and pathway databases

    BioCyciARA:AT3G09260-MONOMER.

    Protein family/group databases

    CAZyiGH1. Glycoside Hydrolase Family 1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-glucosidase 23 (EC:3.2.1.21)
    Short name:
    AtBGLU23
    Alternative name(s):
    Protein PHOSPHATE STARVATION-RESPONSE 3.1
    Gene namesi
    Name:BGLU23
    Synonyms:PSR3.1, PYK10
    Ordered Locus Names:At3g09260
    ORF Names:F3L24.13
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 3

    Organism-specific databases

    TAIRiAT3G09260.

    Subcellular locationi

    Endoplasmic reticulum lumen 5 PublicationsPROSITE-ProRule annotation
    Note: Located in ER bodies.

    GO - Cellular componenti

    1. endoplasmic reticulum Source: TAIR
    2. endoplasmic reticulum lumen Source: UniProtKB-SubCell
    3. ER body Source: TAIR
    4. membrane Source: TAIR
    5. nucleus Source: TAIR
    6. peroxisome Source: TAIR
    7. plasmodesma Source: TAIR
    8. vacuole Source: TAIR

    Keywords - Cellular componenti

    Endoplasmic reticulum

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi29 – 291C → Y in leb-1; loss of homodimerization resulting in fewer and larger ER bodies. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 24241 PublicationAdd
    BLAST
    Chaini25 – 524500Beta-glucosidase 23PRO_0000389585Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi60 – 601N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi222 ↔ 230By similarity
    Glycosylationi461 – 4611N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi494 – 4941N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    Forms interchain disulfide bonds.

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ9SR37.
    PRIDEiQ9SR37.

    Expressioni

    Tissue specificityi

    Expressed exclusively in roots.2 Publications

    Inductioni

    Up-regulated by wounding, 2,4-D and methyl jasmonate (MeJA). Down-regulated by salt and manitol.2 Publications

    Gene expression databases

    GenevestigatoriQ9SR37.

    Interactioni

    Subunit structurei

    Homodimers. Binds to the deubiquitinating enzyme AMSH3. The inactive form interacts with PBP1/JAL30 to form the PYK10 complex, at least composed of PYK10/BGLU23, BGLU21, BGLU22, JAL22, JAL23, PBP1/JAL30, PBP2/JAL31, JAL32, JAL33, JAL34, JAL35, GLL22 and GLL23.4 Publications

    Protein-protein interaction databases

    BioGridi5416. 4 interactions.
    STRINGi3702.AT3G09260.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9SR37.
    SMRiQ9SR37. Positions 32-503.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni475 – 4762Substrate bindingBy similarity

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi521 – 5244Prevents secretion from ERPROSITE-ProRule annotation

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 1 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG2723.
    HOGENOMiHOG000088630.
    InParanoidiQ9SR37.
    KOiK01188.
    OMAiLITWESK.
    PhylomeDBiQ9SR37.

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR001360. Glyco_hydro_1.
    IPR018120. Glyco_hydro_1_AS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PANTHERiPTHR10353. PTHR10353. 1 hit.
    PfamiPF00232. Glyco_hydro_1. 1 hit.
    [Graphical view]
    PRINTSiPR00131. GLHYDRLASE1.
    SUPFAMiSSF51445. SSF51445. 1 hit.
    PROSITEiPS00014. ER_TARGET. 1 hit.
    PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9SR37-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVLQKLPLIG LLLLLTIVAS PANADGPVCP PSNKLSRASF PEGFLFGTAT    50
    AAYQVEGAIN ETCRGPALWD IYCRRYPERC NNDNGDVAVD FFHRYKEDIQ 100
    LMKNLNTDAF RMSIAWPRIF PHGRKEKGVS QAGVQFYHDL IDELIKNGIT 150
    PFVTVFHWDT PQDLEDEYGG FLSERIVKDF REYADFVFQE YGGKVKHWIT 200
    FNEPWVFSHA GYDVGKKAPG RCSSYVNAKC QDGRSGYEAY LVTHNLLISH 250
    AEAVEAYRKC EKCKGGKIGI AHSPAWFEAH DLADSQDGAS IDRALDFILG 300
    WHLDTTTFGD YPQIMKDIVG HRLPKFTTEQ KAKLKASTDF VGLNYYTSVF 350
    SNHLEKPDPS KPRWMQDSLI TWESKNAQNY AIGSKPLTAA LNVYSRGFRS 400
    LLKYIKDKYA NPEIMIMENG YGEELGASDS VAVGTADHNR KYYLQRHLLS 450
    MQEAVCIDKV NVTGYFVWSL LDNFEWQDGY KNRFGLYYVD FKNNLTRYEK 500
    ESGKYYKDFL SQGVRPSALK KDEL 524
    Length:524
    Mass (Da):59,721
    Last modified:May 1, 2000 - v1
    Checksum:i4758EA7A9B8336E1
    GO

    Sequence cautioni

    The sequence AAB38783.1 differs from that shown. Reason: Frameshift at positions 56 and 63.
    The sequence BAD94012.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti208 – 2081S → L in CAB50792. (PubMed:11448764)Curated
    Sequence conflicti208 – 2081S → L in CAA61592. (PubMed:11448764)Curated
    Sequence conflicti222 – 2221C → S in AAB38783. 1 PublicationCurated
    Sequence conflicti400 – 4001S → G in BAD94012. 1 PublicationCurated
    Sequence conflicti459 – 4591K → E in BAH20034. (PubMed:19423640)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U72153 mRNA. Translation: AAB38783.1. Frameshift.
    X89413 mRNA. Translation: CAA61592.1.
    AJ243490 Genomic DNA. Translation: CAB50792.1.
    AC011436 Genomic DNA. Translation: AAF14024.1.
    CP002686 Genomic DNA. Translation: AEE74744.1.
    AF386967 mRNA. Translation: AAK62412.1.
    AY136440 mRNA. Translation: AAM97105.1.
    AY140060 mRNA. Translation: AAM98201.1.
    BT000230 mRNA. Translation: AAN15549.1.
    AK221291 mRNA. Translation: BAD94012.1. Different initiation.
    AK226844 mRNA. Translation: BAE98937.1.
    AK230345 mRNA. Translation: BAF02144.1.
    AK317362 mRNA. Translation: BAH20034.1.
    AK317443 mRNA. Translation: BAH20110.1.
    PIRiS57621.
    RefSeqiNP_187537.1. NM_111760.3.
    UniGeneiAt.18035.
    At.47576.
    At.71001.

    Genome annotation databases

    EnsemblPlantsiAT3G09260.1; AT3G09260.1; AT3G09260.
    GeneIDi820082.
    KEGGiath:AT3G09260.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U72153 mRNA. Translation: AAB38783.1 . Frameshift.
    X89413 mRNA. Translation: CAA61592.1 .
    AJ243490 Genomic DNA. Translation: CAB50792.1 .
    AC011436 Genomic DNA. Translation: AAF14024.1 .
    CP002686 Genomic DNA. Translation: AEE74744.1 .
    AF386967 mRNA. Translation: AAK62412.1 .
    AY136440 mRNA. Translation: AAM97105.1 .
    AY140060 mRNA. Translation: AAM98201.1 .
    BT000230 mRNA. Translation: AAN15549.1 .
    AK221291 mRNA. Translation: BAD94012.1 . Different initiation.
    AK226844 mRNA. Translation: BAE98937.1 .
    AK230345 mRNA. Translation: BAF02144.1 .
    AK317362 mRNA. Translation: BAH20034.1 .
    AK317443 mRNA. Translation: BAH20110.1 .
    PIRi S57621.
    RefSeqi NP_187537.1. NM_111760.3.
    UniGenei At.18035.
    At.47576.
    At.71001.

    3D structure databases

    ProteinModelPortali Q9SR37.
    SMRi Q9SR37. Positions 32-503.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 5416. 4 interactions.
    STRINGi 3702.AT3G09260.1-P.

    Protein family/group databases

    CAZyi GH1. Glycoside Hydrolase Family 1.

    Proteomic databases

    PaxDbi Q9SR37.
    PRIDEi Q9SR37.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT3G09260.1 ; AT3G09260.1 ; AT3G09260 .
    GeneIDi 820082.
    KEGGi ath:AT3G09260.

    Organism-specific databases

    TAIRi AT3G09260.

    Phylogenomic databases

    eggNOGi COG2723.
    HOGENOMi HOG000088630.
    InParanoidi Q9SR37.
    KOi K01188.
    OMAi LITWESK.
    PhylomeDBi Q9SR37.

    Enzyme and pathway databases

    BioCyci ARA:AT3G09260-MONOMER.

    Gene expression databases

    Genevestigatori Q9SR37.

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    InterProi IPR001360. Glyco_hydro_1.
    IPR018120. Glyco_hydro_1_AS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    PANTHERi PTHR10353. PTHR10353. 1 hit.
    Pfami PF00232. Glyco_hydro_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00131. GLHYDRLASE1.
    SUPFAMi SSF51445. SSF51445. 1 hit.
    PROSITEi PS00014. ER_TARGET. 1 hit.
    PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification and nucleotide sequences of cDNA clones of phosphate-starvation inducible beta-glucosidase genes of Brassicaceae."
      Malboobi M.A., Tremblay L., Lefebvre D.D.
      Plant Gene Register PGR96-114
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: cv. Columbia.
      Tissue: Root.
    2. "Pyk10, a seedling and root specific gene and promoter from Arabidopsis thaliana."
      Nitz I., Berkefeld H., Puzio P.S., Grundler F.M.
      Plant Sci. 161:337-346(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY.
      Strain: cv. C24.
    3. "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
      Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F.
      , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
      Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    4. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    5. "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.
    6. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
      Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
      , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
      Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    7. "Analysis of multiple occurrences of alternative splicing events in Arabidopsis thaliana using novel sequenced full-length cDNAs."
      Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M., Shinozaki K.
      DNA Res. 16:155-164(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    8. "A novel ER-derived compartment, the ER body, selectively accumulates a beta-glucosidase with an ER-retention signal in Arabidopsis."
      Matsushima R., Kondo M., Nishimura M., Hara-Nishimura I.
      Plant J. 33:493-502(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 25-41, SUBCELLULAR LOCATION.
    9. "NAI1 gene encodes a basic-helix-loop-helix-type putative transcription factor that regulates the formation of an endoplasmic reticulum-derived structure, the ER body."
      Matsushima R., Fukao Y., Nishimura M., Hara-Nishimura I.
      Plant Cell 16:1536-1549(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
    10. Cited for: GENE FAMILY, NOMENCLATURE.
    11. "Activation of an ER-body-localized beta-glucosidase via a cytosolic binding partner in damaged tissues of Arabidopsis thaliana."
      Nagano A.J., Matsushima R., Hara-Nishimura I.
      Plant Cell Physiol. 46:1140-1148(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION, ENZYME REGULATION, SUBUNIT, DISULFIDE BOND, SUBCELLULAR LOCATION, INTERACTION WITH PBP1.
      Strain: cv. Columbia.
    12. "Antagonistic jacalin-related lectins regulate the size of ER body-type beta-glucosidase complexes in Arabidopsis thaliana."
      Nagano A.J., Fukao Y., Fujiwara M., Nishimura M., Hara-Nishimura I.
      Plant Cell Physiol. 49:969-980(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE PYK10 COMPLEX.
    13. "PYK10, a beta-glucosidase located in the endoplasmatic reticulum, is crucial for the beneficial interaction between Arabidopsis thaliana and the endophytic fungus Piriformospora indica."
      Sherameti I., Venus Y., Drzewiecki C., Tripathi S., Dan V.M., Nitz I., Varma A., Grundler F.M., Oelmueller R.
      Plant J. 54:428-439(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
    14. "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana."
      Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E., Rathjen J.P., Peck S.C.
      J. Proteomics 72:439-451(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: cv. Columbia.
    15. "Constitutive and inducible ER bodies of Arabidopsis thaliana accumulate distinct beta-glucosidases."
      Ogasawara K., Yamada K., Christeller J.T., Kondo M., Hatsugai N., Hara-Nishimura I., Nishimura M.
      Plant Cell Physiol. 50:480-488(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    16. Cited for: MUTAGENESIS OF CYS-29, SUBUNIT.
      Strain: cv. Columbia.
    17. "The deubiquitinating enzyme AMSH3 is required for intracellular trafficking and vacuole biogenesis in Arabidopsis thaliana."
      Isono E., Katsiarimpa A., Mueller I.K., Anzenberger F., Stierhof Y.-D., Geldner N., Chory J., Schwechheimer C.
      Plant Cell 22:1826-1837(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AMSH3.
    18. "Scopolin-hydrolyzing beta-glucosidases in roots of Arabidopsis."
      Ahn Y.O., Shimizu B., Sakata K., Gantulga D., Zhou C., Zhou Z., Bevan D.R., Esen A.
      Plant Cell Physiol. 51:132-143(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, INDUCTION, ENZYME REGULATION.

    Entry informationi

    Entry nameiBGL23_ARATH
    AccessioniPrimary (citable) accession number: Q9SR37
    Secondary accession number(s): B9DH17
    , O24433, Q42585, Q56YN0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 24, 2009
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 106 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, Direct protein sequencing, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3