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Q9SR37

- BGL23_ARATH

UniProt

Q9SR37 - BGL23_ARATH

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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

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 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 cytokinin Source: TAIR
  6. response to osmotic stress Source: TAIR
  7. response to salt stress Source: TAIR
  8. response to symbiotic fungus Source: TAIR
Complete GO annotation...

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. ER body Source: TAIR
  3. membrane Source: TAIR
  4. nucleus Source: TAIR
  5. peroxisome Source: TAIR
  6. plasmodesma Source: TAIR
  7. vacuole Source: TAIR
Complete GO annotation...

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 35-510.
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

        10         20         30         40         50
MVLQKLPLIG LLLLLTIVAS PANADGPVCP PSNKLSRASF PEGFLFGTAT
60 70 80 90 100
AAYQVEGAIN ETCRGPALWD IYCRRYPERC NNDNGDVAVD FFHRYKEDIQ
110 120 130 140 150
LMKNLNTDAF RMSIAWPRIF PHGRKEKGVS QAGVQFYHDL IDELIKNGIT
160 170 180 190 200
PFVTVFHWDT PQDLEDEYGG FLSERIVKDF REYADFVFQE YGGKVKHWIT
210 220 230 240 250
FNEPWVFSHA GYDVGKKAPG RCSSYVNAKC QDGRSGYEAY LVTHNLLISH
260 270 280 290 300
AEAVEAYRKC EKCKGGKIGI AHSPAWFEAH DLADSQDGAS IDRALDFILG
310 320 330 340 350
WHLDTTTFGD YPQIMKDIVG HRLPKFTTEQ KAKLKASTDF VGLNYYTSVF
360 370 380 390 400
SNHLEKPDPS KPRWMQDSLI TWESKNAQNY AIGSKPLTAA LNVYSRGFRS
410 420 430 440 450
LLKYIKDKYA NPEIMIMENG YGEELGASDS VAVGTADHNR KYYLQRHLLS
460 470 480 490 500
MQEAVCIDKV NVTGYFVWSL LDNFEWQDGY KNRFGLYYVD FKNNLTRYEK
510 520
ESGKYYKDFL SQGVRPSALK KDEL
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 35-510.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 107 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