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Q9SJF0 (BSL2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 99. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein phosphatase BSL2

EC=3.1.3.16
Alternative name(s):
BSU1-like protein 2
Gene names
Name:BSL2
Ordered Locus Names:At1g08420
ORF Names:T27G7.10
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length1018 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 By similarity.

Tissue specificity

Expressed throughout the plant, with a higher level in younger parts. Ref.4

Sequence similarities

Belongs to the PPP phosphatase family. BSU subfamily.

Contains 5 Kelch repeats.

Sequence caution

The sequence AAF22889.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.
Isoform 1 (identifier: Q9SJF0-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10181018Serine/threonine-protein phosphatase BSL2
PRO_0000058906

Regions

Repeat149 – 19547Kelch 1
Repeat253 – 30149Kelch 2
Repeat306 – 35651Kelch 3
Repeat362 – 40948Kelch 4
Repeat430 – 47950Kelch 5

Sites

Active site7871Proton donor By similarity
Metal binding7201Iron By similarity
Metal binding7221Iron By similarity
Metal binding7541Iron By similarity
Metal binding7541Manganese By similarity
Metal binding7861Manganese By similarity
Metal binding8391Manganese By similarity
Metal binding9181Manganese By similarity

Amino acid modifications

Modified residue6271Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 23, 2007. Version 2.
Checksum: F2D48037DF4FAAB4

FASTA1,018108,580
        10         20         30         40         50         60 
MDEDSSMVAD NDQDREFQSL DGGQSPSPME RETPQQMNDQ SPPPEGGSVP TPPPSDPNPA 

        70         80         90        100        110        120 
TSQQQAAAVV GQEQQPALVV GPRCAPTYSV VDAMMDKKED GPGPRCGHTL TAVPAVGDEG 

       130        140        150        160        170        180 
TPGYIGPRLV LFGGATALEG NSGGTGTPTS AGSAGIRLAG ATADVHCYDV LSNKWTRLTP 

       190        200        210        220        230        240 
FGEPPTPRAA HVATAVGTMV VIQGGIGPAG LSAEDLHVLD LTQQRPRWHR VVVQGPGPGP 

       250        260        270        280        290        300 
RYGHVMALVG QRYLMAIGGN DGKRPLADVW ALDTAAKPYE WRKLEPEGEG PPPCMYATAS 

       310        320        330        340        350        360 
ARSDGLLLLC GGRDANSVPL ASAYGLAKHR DGRWEWAIAP GVSPSSRYQH AAVFVNARLH 

       370        380        390        400        410        420 
VSGGALGGGR MVEDSSSVAV LDTAAGVWCD TKSVVTSPRT GRYSADAAGG DASVELTRRC 

       430        440        450        460        470        480 
RHAAAAVGDL IFIYGGLRGG VLLDDLLVAE DLAAAETTYA ASHAAAAAAT NSPPGRLPGR 

       490        500        510        520        530        540 
YGFSDERNRE LSESAADGAV VLGSPVAPPV NGDMHTDISP ENALLPGTRR TNKGVEYLVE 

       550        560        570        580        590        600 
ASAAEAEAIS ATLAAAKARQ VNGEVELPDR DCGAEATPSG KPTFSLIKPD SMGSMSVTPA 

       610        620        630        640        650        660 
GIRLHHRAVV VAAETGGALG GMVRQLSIDQ FENEGRRVSY GTPESATAAR KLLDRQMSIN 

       670        680        690        700        710        720 
SVPKKVIAHL LKPRGWKPPV RRQFFLDCNE IADLCDSAER IFASEPTVLQ LKAPIKIFGD 

       730        740        750        760        770        780 
LHGQFGDLMR LFDEYGSPST AGDISYIDYL FLGDYVDRGQ HSLETISLLL ALKVEYQHNV 

       790        800        810        820        830        840 
HLIRGNHEAA DINALFGFRI ECIERMGERD GIWVWHRINR LFNWLPLAAS IEKKIICMHG 

       850        860        870        880        890        900 
GIGRSINHVE QIENIQRPIT MEAGSIVLMD LLWSDPTEND SVEGLRPNAR GPGLVTFGPD 

       910        920        930        940        950        960 
RVMEFCNNND LQLIVRAHEC VMDGFERFAQ GHLITLFSAT NYCGTANNAG AILVLGRDLV 

       970        980        990       1000       1010 
VVPKLIHPLP PALSSPETSP ERHIEDTWMQ ELNANRPATP TRGRPQNSND RGGSLAWM 

« Hide

References

« Hide 'large scale' references
[1]"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.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"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. expand/collapse author list , 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] OF 282-1018.
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]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC006932 Genomic DNA. Translation: AAF22889.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE28287.1.
AK230437 mRNA. Translation: BAF02235.1.
PIRE86217.
RefSeqNP_172318.1. NM_100715.3.
UniGeneAt.27687.

3D structure databases

ProteinModelPortalQ9SJF0.
SMRQ9SJF0. Positions 666-968.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid22603. 1 interaction.

Proteomic databases

PaxDbQ9SJF0.
PRIDEQ9SJF0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G08420.1; AT1G08420.1; AT1G08420. [Q9SJF0-1]
GeneID837362.
KEGGath:AT1G08420.

Organism-specific databases

TAIRAT1G08420.

Phylogenomic databases

eggNOGCOG0639.
HOGENOMHOG000246464.
InParanoidQ9SJF0.
OMAIFASEPT.
PhylomeDBQ9SJF0.
ProtClustDBCLSN2682801.

Enzyme and pathway databases

BioCycARA:AT1G08420-MONOMER.
ARA:GQT-182-MONOMER.

Gene expression databases

GenevestigatorQ9SJF0.

Family and domain databases

Gene3D2.120.10.80. 1 hit.
InterProIPR004843. Calcineurin-like_PHP_apaH.
IPR015915. Kelch-typ_b-propeller.
IPR011498. Kelch_2.
IPR006186. Ser/Thr-sp_prot-phosphatase.
IPR012391. Ser/Thr_prot_Pase_BSU1.
[Graphical view]
PfamPF07646. Kelch_2. 1 hit.
PF00149. 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 nameBSL2_ARATH
AccessionPrimary (citable) accession number: Q9SJF0
Secondary accession number(s): Q0WKX2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: October 23, 2007
Last modified: April 16, 2014
This is version 99 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