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Q9LR78 (BSU1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein phosphatase BSU1

EC=3.1.3.16
Alternative name(s):
Bri1 suppressor protein 1
Gene names
Name:BSU1
Ordered Locus Names:At1g03445, At1g03450
ORF Names:F21B7.7
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length793 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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. Ref.1

Catalytic activity

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

Cofactor

Binds 2 manganese ions per subunit By similarity.

Subcellular location

Nucleus Ref.1.

Tissue specificity

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. Ref.1

Sequence similarities

Belongs to the PPP phosphatase family. BSU subfamily.

Contains 5 Kelch repeats.

Sequence caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 793793Serine/threonine-protein phosphatase BSU1
PRO_0000058904

Regions

Repeat53 – 10957Kelch 1
Repeat110 – 16051Kelch 2
Repeat214 – 26249Kelch 3
Repeat264 – 31451Kelch 4
Repeat329 – 38860Kelch 5

Sites

Active site5771Proton donor By similarity
Metal binding5101Manganese 1 By similarity
Metal binding5121Manganese 1 By similarity
Metal binding5441Manganese 1 By similarity
Metal binding5441Manganese 2 By similarity
Metal binding5761Manganese 2 By similarity
Metal binding6291Manganese 2 By similarity
Metal binding7071Manganese 2 By similarity

Amino acid modifications

Modified residue4441Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9LR78 [UniParc].

Last modified March 15, 2004. Version 2.
Checksum: 07A083BD780EAA79

FASTA79387,789
        10         20         30         40         50         60 
MAPDQSYQYP SPSYESIQTF YDTDEDWPGP RCGHTLTAVF VNNSHQLILF GGSTTAVANH 

        70         80         90        100        110        120 
NSSLPEISLD GVTNSVHSFD VLTRKWTRLN PIGDVPSPRA CHAAALYGTL ILIQGGIGPS 

       130        140        150        160        170        180 
GPSDGDVYML DMTNNKWIKF LVGGETPSPR YGHVMDIAAQ RWLVIFSGNN GNEILDDTWA 

       190        200        210        220        230        240 
LDTRGPFSWD RLNPSGNQPS GRMYASGSSR EDGIFLLCGG IDHSGVTLGD TYGLKMDSDN 

       250        260        270        280        290        300 
VWTPVPAVAP SPRYQHTAVF GGSKLHVIGG ILNRARLIDG EAVVAVLDTE TGEWVDTNQP 

       310        320        330        340        350        360 
ETSASGANRQ NQYQLMRRCH HAAASFGSHL YVHGGIREDV LLDDLLVAET SQSSSPEPEE 

       370        380        390        400        410        420 
DNPDNYMLLD DYLMDEPKPL SSEPEASSFI MRSTSEIAMD RLAEAHNLPT IENAFYDSAI 

       430        440        450        460        470        480 
EGYVPLQHGA ETVGNRGGLV RTASLDQSTQ DLHKKVISTL LRPKTWTPPA NRDFFLSYLE 

       490        500        510        520        530        540 
VKHLCDEVEK IFMNEPTLLQ LKVPIKVFGD IHGQYGDLMR LFHEYGHPSV EGDITHIDYL 

       550        560        570        580        590        600 
FLGDYVDRGQ HSLEIIMLLF ALKIEYPKNI HLIRGNHESL AMNRIYGFLT ECEERMGESY 

       610        620        630        640        650        660 
GFEAWLKINQ VFDYLPLAAL LEKKVLCVHG GIGRAVTIEE IENIERPAFP DTGSMVLKDI 

       670        680        690        700        710        720 
LWSDPTMNDT VLGIVDNARG EGVVSFGPDI VKAFLERNGL EMILRAHECV IDGFERFADG 

       730        740        750        760        770        780 
RLITVFSATN YCGTAQNAGA ILVIGRDMVI YPKLIHPHPP PISSSEEDYT DKAWMQELNI 

       790 
EMPPTPARGE SSE 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY372269 mRNA. Translation: AAR19789.1.
AC002560 Genomic DNA. Translation: AAF86539.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE27572.1.
RefSeqNP_171844.6. NM_100227.6.
UniGeneAt.49845.

3D structure databases

ProteinModelPortalQ9LR78.
SMRQ9LR78. Positions 480-757.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid24043. 1 interaction.
STRING3702.AT1G03445.1-P.

Proteomic databases

PRIDEQ9LR78.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G03445.1; AT1G03445.1; AT1G03445.
GeneID838804.
KEGGath:AT1G03445.

Organism-specific databases

TAIRAT1G03445.

Phylogenomic databases

eggNOGCOG0639.
HOGENOMHOG000246464.
InParanoidQ9LR78.
KOK14501.
OMAEGDITHI.
PhylomeDBQ9LR78.

Enzyme and pathway databases

BioCycARA:AT1G03445-MONOMER.

Gene expression databases

GenevestigatorQ9LR78.

Family and domain databases

Gene3D2.120.10.80. 1 hit.
2.130.10.80. 1 hit.
3.60.21.10. 1 hit.
InterProIPR004843. 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]
PfamPF00149. Metallophos. 1 hit.
[Graphical view]
PIRSFPIRSF036363. PPP_BSU1. 1 hit.
PRINTSPR00114. STPHPHTASE.
SMARTSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMSSF56300. SSF56300. 1 hit.
PROSITEPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROQ9LR78.

Entry information

Entry nameBSU1_ARATH
AccessionPrimary (citable) accession number: Q9LR78
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: March 15, 2004
Last modified: June 11, 2014
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names