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Q9SX52 (FYPP1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 94. 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:
Phytochrome-associated serine/threonine-protein phosphatase 1

Short name=AtFyPP1
EC=3.1.3.16
Gene names
Name:FYPP1
Ordered Locus Names:At1g50370
ORF Names:F14I3.5
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length303 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Dephosphorylates phosphorylated phytochromes, with a preference toward Pfr forms. Plays a major role in the photoperiodic control of flowering time in long days by modulating phytochrome signals in flowering time control By similarity. Ref.7

Catalytic activity

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

Cofactor

Binds 2 manganese ions per subunit By similarity. Ref.7

Subunit structure

Interacts with PHYA and PHYB, mostly when they are phosphorylated and in Pfr forms By similarity.

Subcellular location

Cytoplasm By similarity.

Tissue specificity

Mostly expressed in flowers. Also detected to a lower extent in stems and leaves. Ref.7

Sequence similarities

Belongs to the PPP phosphatase family. PP-6 (PP-V) subfamily.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandManganese
Metal-binding
Zinc
   Molecular functionHydrolase
Protein phosphatase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphoprotein phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 303303Phytochrome-associated serine/threonine-protein phosphatase 1
PRO_0000308989

Sites

Active site1111Proton donor By similarity
Metal binding501Manganese 1 By similarity
Metal binding521Manganese 1 By similarity
Metal binding781Manganese 1 By similarity
Metal binding781Manganese 2 By similarity
Metal binding1101Manganese 2 By similarity
Metal binding1601Manganese 2 By similarity
Metal binding2341Manganese 2 By similarity

Experimental info

Sequence conflict681V → F in BAE98396. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q9SX52 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 44598694DD92D626

FASTA30334,819
        10         20         30         40         50         60 
MDLDQWISKV KDGQHLSEDE LQLLCEYVKE ILIEESNVQP VNSPVTVCGD IHGQFHDLMK 

        70         80         90        100        110        120 
LFQTGGHVPE TNYIFMGDFV DRGYNSLEVF TILLLLKARH PANITLLRGN HESRQLTQVY 

       130        140        150        160        170        180 
GFYDECQRKY GNANAWRYCT DVFDYLTLSA IIDGTVLCVH GGLSPDVRTI DQIRLIERNC 

       190        200        210        220        230        240 
EIPHEGPFCD LMWSDPEDIE TWAVSPRGAG WLFGSRVTTE FNHINNLDLV CRAHQLVQEG 

       250        260        270        280        290        300 
LKYMFQDKGL VTVWSAPNYC YRCGNVASIL SFNDNMEREV KFFTETEENN QMRGPRTGVP 


YFL 

« 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]"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]"Arabidopsis ORF clones."
Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.
Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[5]"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].
Strain: cv. Columbia.
[6]"Full-length cDNA from Arabidopsis thaliana."
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]"A phytochrome-associated protein phosphatase 2A modulates light signals in flowering time control in Arabidopsis."
Kim D.-H., Kang J.-G., Yang S.-S., Chung K.-S., Song P.-S., Park C.-M.
Plant Cell 14:3043-3056(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, COFACTOR, TISSUE SPECIFICITY.
[8]"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
AC007980 Genomic DNA. Translation: AAD50050.1.
CP002684 Genomic DNA. Translation: AEE32541.1.
AF428374 mRNA. Translation: AAL16304.1.
BT020404 mRNA. Translation: AAV97795.1.
AK226232 mRNA. Translation: BAE98396.1.
AY087422 mRNA. Translation: AAM64970.1.
PIRH96539.
RefSeqNP_175454.1. NM_103920.3.
UniGeneAt.18962.
At.5940.

3D structure databases

ProteinModelPortalQ9SX52.
SMRQ9SX52. Positions 2-277.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid26684. 11 interactions.
IntActQ9SX52. 1 interaction.

Proteomic databases

PaxDbQ9SX52.
PRIDEQ9SX52.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G50370.1; AT1G50370.1; AT1G50370.
GeneID841459.
KEGGath:AT1G50370.

Organism-specific databases

TAIRAT1G50370.

Phylogenomic databases

eggNOGCOG0639.
HOGENOMHOG000172696.
InParanoidQ9SX52.
KOK15498.
OMAQITHVYG.
PhylomeDBQ9SX52.

Enzyme and pathway databases

BioCycARA:AT1G50370-MONOMER.

Gene expression databases

GenevestigatorQ9SX52.

Family and domain databases

Gene3D3.60.21.10. 1 hit.
InterProIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSPR00114. STPHPHTASE.
SMARTSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMSSF56300. SSF56300. 1 hit.
PROSITEPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFYPP1_ARATH
AccessionPrimary (citable) accession number: Q9SX52
Secondary accession number(s): Q0WWV2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: May 1, 2000
Last modified: June 11, 2014
This is version 94 of the entry and version 1 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