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Q8L7U5 (BSL1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 93. 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 BSL1

EC=3.1.3.16
Alternative name(s):
BSU1-like protein 1
Gene names
Name:BSL1
Ordered Locus Names:At4g03080
ORF Names:T4I9.4
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length881 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Phosphatase involved in elongation process, probably by acting as a regulator of brassinolide signaling. Ref.4

Catalytic activity

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

Cofactor

Binds 1 iron ion per subunit By similarity.

Binds 1 manganese ion per subunit By similarity.

Subcellular location

Nucleus Ref.6.

Tissue specificity

Expressed in mature cauline leaves and at the tip of influorescence, including flowers. Expressed at lower level in young tissues relative to older ones. Ref.4

Sequence similarities

Belongs to the PPP phosphatase family. BSU subfamily.

Contains 3 Kelch repeats.

Sequence caution

The sequence AAC79097.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAB77793.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 881881Serine/threonine-protein phosphatase BSL1
PRO_0000058905

Regions

Repeat60 – 10950Kelch 1
Repeat269 – 32052Kelch 2
Repeat338 – 38548Kelch 3

Sites

Active site6511Proton donor By similarity
Metal binding5841Iron By similarity
Metal binding5861Iron By similarity
Metal binding6181Iron By similarity
Metal binding6181Manganese By similarity
Metal binding6501Manganese By similarity
Metal binding7031Manganese By similarity
Metal binding7821Manganese By similarity

Amino acid modifications

Modified residue4911Phosphoserine Ref.6 Ref.7

Experimental info

Sequence conflict7941Q → P in AAM83219. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8L7U5 [UniParc].

Last modified May 3, 2011. Version 2.
Checksum: 6EC45417BAEBD6E0

FASTA88196,146
        10         20         30         40         50         60 
MGSKPWLHPA PQYKTLETFW DDEDDAPGPR CAHTLTAVAA TKTHGPRLIL FGGATAIEGG 

        70         80         90        100        110        120 
SSSVPGIRLA GVTNTVHSYD ILTRKWTRLK PAGEPPSPRA AHAAAAVGTM VVFQGGIGPA 

       130        140        150        160        170        180 
GHSTDDLYVL DMTNDKFKWH RVVVQGDGPG PRYGHVMDLV SQRYLVTVTG NDGKRALSDA 

       190        200        210        220        230        240 
WALDTAQKPY VWQRLNPDGD RPSARMYASG SARSDGMFLL CGGRDTLGAP LGDAYGLLMH 

       250        260        270        280        290        300 
RNGQWEWTLA PGVAPSPRYQ HAAVFVGARL HVSGGVLRGG RVIDAEASVA VLDTAAGVWL 

       310        320        330        340        350        360 
DRNGQVTSAR GSKGQIDQDP SFELMRRCRH GAASVGIRIY VHGGLRGDVL LDDFLVAENS 

       370        380        390        400        410        420 
TFQSDISSPL LASDRTQQSS TPRFSYAARP PSGSEPSFSM SEGLSLDENS LEKLTEASAA 

       430        440        450        460        470        480 
EAEVASSVWR AAQLGAGTLD EEPSTSDASS PIVESTTDGT ANEGDVRLHP RAVVVAKETV 

       490        500        510        520        530        540 
GSLGGMVRQL SLDQFQNESR RMVPMNNSDV PQPTKKFTRQ KSPQGLHKKV IAALLRPRNW 

       550        560        570        580        590        600 
KPPGNRKFFL DSYEVGELCY AAEQIFMHEQ TVLQLKAPIK VFGDLHGQFG DLMRLFDEYG 

       610        620        630        640        650        660 
FPSTAGDITY IDYLFLGDYV DRGQHSLETI TLLLALKIEY PENVHLIRGN HEAADINALF 

       670        680        690        700        710        720 
GFRLECIERM GENDGIWAWT RFNQLFNYLP LAALIENKII CMHGGIGRSI STVEQIEKIE 

       730        740        750        760        770        780 
RPITMDAGSL VLMDLLWSDP TENDSIEGLR PNARGPGLVT FGPDRVTEFC KRNKLQLIIR 

       790        800        810        820        830        840 
AHECVMDGFE RFAQGQLITL FSATNYCGTA NNAGAILVVG RGLVIVPKLI HPLPPPILSP 

       850        860        870        880 
ENSPEHSGDD AWMQELNIQR PPTPTRGRPQ PDFDRSSLAY I 

« Hide

References

« Hide 'large scale' references
[1]"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. expand/collapse author list , 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.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"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. expand/collapse author list , 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.
[4]"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: FUNCTION, TISSUE SPECIFICITY.
[5]"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.
[6]"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: SUBCELLULAR LOCATION, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-491, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: cv. Columbia.
[7]"Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-491, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF069442 Genomic DNA. Translation: AAC79097.1. Sequence problems.
AL161496 Genomic DNA. Translation: CAB77793.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE82268.1.
AY126992 mRNA. Translation: AAM83219.1.
PIRT01385.
RefSeqNP_192217.2. NM_116542.4.
UniGeneAt.26278.
At.48826.

3D structure databases

ProteinModelPortalQ8L7U5.
SMRQ8L7U5. Positions 129-352, 550-832.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid13388. 1 interaction.
IntActQ8L7U5. 1 interaction.
STRING3702.AT4G03080.1-P.

Proteomic databases

PaxDbQ8L7U5.
PRIDEQ8L7U5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G03080.1; AT4G03080.1; AT4G03080.
GeneID828097.
KEGGath:AT4G03080.

Organism-specific databases

TAIRAT4G03080.

Phylogenomic databases

eggNOGCOG0639.
HOGENOMHOG000246464.
InParanoidQ8L7U5.
KOK01090.
OMAIVPKLIH.

Enzyme and pathway databases

BioCycARA:AT4G03080-MONOMER.

Gene expression databases

GenevestigatorQ8L7U5.

Family and domain databases

Gene3D2.120.10.80. 2 hits.
InterProIPR004843. Calcineurin-like_PHP_apaH.
IPR015915. Kelch-typ_b-propeller.
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]
PROSITEPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBSL1_ARATH
AccessionPrimary (citable) accession number: Q8L7U5
Secondary accession number(s): Q9ZTA4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: May 3, 2011
Last modified: April 16, 2014
This is version 93 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