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Q8L7U5

- BSL1_ARATH

UniProt

Q8L7U5 - BSL1_ARATH

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Protein
Serine/threonine-protein phosphatase BSL1
Gene
BSL1, At4g03080, T4I9.4
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Phosphatase involved in elongation process, probably by acting as a regulator of brassinolide signaling.1 Publication

Catalytic activityi

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

Cofactori

Binds 2 manganese ions per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi584 – 5841Manganese 1 By similarity
Metal bindingi586 – 5861Manganese 1 By similarity
Metal bindingi618 – 6181Manganese 1 By similarity
Metal bindingi618 – 6181Manganese 2 By similarity
Metal bindingi650 – 6501Manganese 2 By similarity
Active sitei651 – 6511Proton donor By similarity
Metal bindingi703 – 7031Manganese 2 By similarity
Metal bindingi782 – 7821Manganese 2 By similarity

GO - Molecular functioni

  1. iron ion binding Source: InterPro
  2. manganese ion binding Source: InterPro
  3. phosphoprotein phosphatase activity Source: UniProtKB-KW
  4. protein binding Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BioCyciARA:AT4G03080-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase BSL1 (EC:3.1.3.16)
Alternative name(s):
BSU1-like protein 1
Gene namesi
Name:BSL1
Ordered Locus Names:At4g03080
ORF Names:T4I9.4
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 4

Organism-specific databases

TAIRiAT4G03080.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. nucleus Source: UniProtKB-SubCell
  2. plasma membrane Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 881881Serine/threonine-protein phosphatase BSL1
PRO_0000058905Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei491 – 4911Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ8L7U5.
PRIDEiQ8L7U5.

Expressioni

Tissue specificityi

Expressed in mature cauline leaves and at the tip of influorescence, including flowers. Expressed at lower level in young tissues relative to older ones.1 Publication

Gene expression databases

GenevestigatoriQ8L7U5.

Interactioni

Protein-protein interaction databases

BioGridi13388. 1 interaction.
IntActiQ8L7U5. 1 interaction.
STRINGi3702.AT4G03080.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ8L7U5.
SMRiQ8L7U5. Positions 269-357, 550-832.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati60 – 10950Kelch 1
Add
BLAST
Repeati269 – 32052Kelch 2
Add
BLAST
Repeati338 – 38548Kelch 3
Add
BLAST

Sequence similaritiesi

Contains 3 Kelch repeats.

Keywords - Domaini

Kelch repeat, Repeat

Phylogenomic databases

eggNOGiCOG0639.
HOGENOMiHOG000246464.
InParanoidiQ8L7U5.
KOiK01090.
OMAiIVPKLIH.

Family and domain databases

Gene3Di2.120.10.80. 2 hits.
3.60.21.10. 1 hit.
InterProiIPR004843. Calcineurin-like_PHP_apaH.
IPR015915. Kelch-typ_b-propeller.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
IPR012391. Ser/Thr_prot_Pase_BSU1.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
[Graphical view]
PIRSFiPIRSF036363. PPP_BSU1. 1 hit.
PRINTSiPR00114. STPHPHTASE.
SMARTiSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.
PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8L7U5-1 [UniParc]FASTAAdd to Basket

« Hide

MGSKPWLHPA PQYKTLETFW DDEDDAPGPR CAHTLTAVAA TKTHGPRLIL    50
FGGATAIEGG SSSVPGIRLA GVTNTVHSYD ILTRKWTRLK PAGEPPSPRA 100
AHAAAAVGTM VVFQGGIGPA GHSTDDLYVL DMTNDKFKWH RVVVQGDGPG 150
PRYGHVMDLV SQRYLVTVTG NDGKRALSDA WALDTAQKPY VWQRLNPDGD 200
RPSARMYASG SARSDGMFLL CGGRDTLGAP LGDAYGLLMH RNGQWEWTLA 250
PGVAPSPRYQ HAAVFVGARL HVSGGVLRGG RVIDAEASVA VLDTAAGVWL 300
DRNGQVTSAR GSKGQIDQDP SFELMRRCRH GAASVGIRIY VHGGLRGDVL 350
LDDFLVAENS TFQSDISSPL LASDRTQQSS TPRFSYAARP PSGSEPSFSM 400
SEGLSLDENS LEKLTEASAA EAEVASSVWR AAQLGAGTLD EEPSTSDASS 450
PIVESTTDGT ANEGDVRLHP RAVVVAKETV GSLGGMVRQL SLDQFQNESR 500
RMVPMNNSDV PQPTKKFTRQ KSPQGLHKKV IAALLRPRNW KPPGNRKFFL 550
DSYEVGELCY AAEQIFMHEQ TVLQLKAPIK VFGDLHGQFG DLMRLFDEYG 600
FPSTAGDITY IDYLFLGDYV DRGQHSLETI TLLLALKIEY PENVHLIRGN 650
HEAADINALF GFRLECIERM GENDGIWAWT RFNQLFNYLP LAALIENKII 700
CMHGGIGRSI STVEQIEKIE RPITMDAGSL VLMDLLWSDP TENDSIEGLR 750
PNARGPGLVT FGPDRVTEFC KRNKLQLIIR AHECVMDGFE RFAQGQLITL 800
FSATNYCGTA NNAGAILVVG RGLVIVPKLI HPLPPPILSP ENSPEHSGDD 850
AWMQELNIQR PPTPTRGRPQ PDFDRSSLAY I 881
Length:881
Mass (Da):96,146
Last modified:May 3, 2011 - v2
Checksum:i6EC45417BAEBD6E0
GO

Sequence cautioni

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti794 – 7941Q → P in AAM83219. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiT01385.
RefSeqiNP_192217.2. NM_116542.4.
UniGeneiAt.26278.
At.48826.

Genome annotation databases

EnsemblPlantsiAT4G03080.1; AT4G03080.1; AT4G03080.
GeneIDi828097.
KEGGiath:AT4G03080.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi T01385.
RefSeqi NP_192217.2. NM_116542.4.
UniGenei At.26278.
At.48826.

3D structure databases

ProteinModelPortali Q8L7U5.
SMRi Q8L7U5. Positions 269-357, 550-832.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 13388. 1 interaction.
IntActi Q8L7U5. 1 interaction.
STRINGi 3702.AT4G03080.1-P.

Proteomic databases

PaxDbi Q8L7U5.
PRIDEi Q8L7U5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT4G03080.1 ; AT4G03080.1 ; AT4G03080 .
GeneIDi 828097.
KEGGi ath:AT4G03080.

Organism-specific databases

TAIRi AT4G03080.

Phylogenomic databases

eggNOGi COG0639.
HOGENOMi HOG000246464.
InParanoidi Q8L7U5.
KOi K01090.
OMAi IVPKLIH.

Enzyme and pathway databases

BioCyci ARA:AT4G03080-MONOMER.

Gene expression databases

Genevestigatori Q8L7U5.

Family and domain databases

Gene3Di 2.120.10.80. 2 hits.
3.60.21.10. 1 hit.
InterProi IPR004843. Calcineurin-like_PHP_apaH.
IPR015915. Kelch-typ_b-propeller.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
IPR012391. Ser/Thr_prot_Pase_BSU1.
[Graphical view ]
Pfami PF00149. Metallophos. 1 hit.
[Graphical view ]
PIRSFi PIRSF036363. PPP_BSU1. 1 hit.
PRINTSi PR00114. STPHPHTASE.
SMARTi SM00156. PP2Ac. 1 hit.
[Graphical view ]
SUPFAMi SSF56300. SSF56300. 1 hit.
PROSITEi PS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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].

Entry informationi

Entry nameiBSL1_ARATH
AccessioniPrimary (citable) accession number: Q8L7U5
Secondary accession number(s): Q9ZTA4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: May 3, 2011
Last modified: June 11, 2014
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi