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Protein

Phytochrome-associated serine/threonine-protein phosphatase 1

Gene

FYPP1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

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).By similarity

Catalytic activityi

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

Cofactori

Mn2+By similarityNote: Binds 2 manganese ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi50 – 501Manganese 1By similarity
Metal bindingi52 – 521Manganese 1By similarity
Metal bindingi78 – 781Manganese 1By similarity
Metal bindingi78 – 781Manganese 2By similarity
Metal bindingi110 – 1101Manganese 2By similarity
Active sitei111 – 1111Proton donorBy similarity
Metal bindingi160 – 1601Manganese 2By similarity
Metal bindingi234 – 2341Manganese 2By similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Manganese, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciARA:AT1G50370-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Phytochrome-associated serine/threonine-protein phosphatase 1 (EC:3.1.3.16)
Short name:
AtFyPP1
Gene namesi
Name:FYPP1
Ordered Locus Names:At1g50370
ORF Names:F14I3.5
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G50370.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 303303Phytochrome-associated serine/threonine-protein phosphatase 1PRO_0000308989Add
BLAST

Proteomic databases

PaxDbiQ9SX52.
PRIDEiQ9SX52.

Expressioni

Tissue specificityi

Mostly expressed in flowers. Also detected to a lower extent in stems and leaves.1 Publication

Gene expression databases

GenevestigatoriQ9SX52.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi26684. 11 interactions.
IntActiQ9SX52. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ9SX52.
SMRiQ9SX52. Positions 2-277.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0639.
HOGENOMiHOG000172696.
InParanoidiQ9SX52.
KOiK15498.
OMAiMTINNLS.
PhylomeDBiQ9SX52.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
InterProiIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSiPR00114. STPHPHTASE.
SMARTiSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.
PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9SX52-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDLDQWISKV KDGQHLSEDE LQLLCEYVKE ILIEESNVQP VNSPVTVCGD
60 70 80 90 100
IHGQFHDLMK LFQTGGHVPE TNYIFMGDFV DRGYNSLEVF TILLLLKARH
110 120 130 140 150
PANITLLRGN HESRQLTQVY GFYDECQRKY GNANAWRYCT DVFDYLTLSA
160 170 180 190 200
IIDGTVLCVH GGLSPDVRTI DQIRLIERNC EIPHEGPFCD LMWSDPEDIE
210 220 230 240 250
TWAVSPRGAG WLFGSRVTTE FNHINNLDLV CRAHQLVQEG LKYMFQDKGL
260 270 280 290 300
VTVWSAPNYC YRCGNVASIL SFNDNMEREV KFFTETEENN QMRGPRTGVP

YFL
Length:303
Mass (Da):34,819
Last modified:May 1, 2000 - v1
Checksum:i44598694DD92D626
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti68 – 681V → F in BAE98396 (Ref. 5) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiH96539.
RefSeqiNP_175454.1. NM_103920.3.
UniGeneiAt.18962.
At.5940.

Genome annotation databases

EnsemblPlantsiAT1G50370.1; AT1G50370.1; AT1G50370.
GeneIDi841459.
KEGGiath:AT1G50370.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiH96539.
RefSeqiNP_175454.1. NM_103920.3.
UniGeneiAt.18962.
At.5940.

3D structure databases

ProteinModelPortaliQ9SX52.
SMRiQ9SX52. Positions 2-277.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi26684. 11 interactions.
IntActiQ9SX52. 1 interaction.

Proteomic databases

PaxDbiQ9SX52.
PRIDEiQ9SX52.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G50370.1; AT1G50370.1; AT1G50370.
GeneIDi841459.
KEGGiath:AT1G50370.

Organism-specific databases

TAIRiAT1G50370.

Phylogenomic databases

eggNOGiCOG0639.
HOGENOMiHOG000172696.
InParanoidiQ9SX52.
KOiK15498.
OMAiMTINNLS.
PhylomeDBiQ9SX52.

Enzyme and pathway databases

BioCyciARA:AT1G50370-MONOMER.

Miscellaneous databases

PROiQ9SX52.

Gene expression databases

GenevestigatoriQ9SX52.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
InterProiIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSiPR00114. STPHPHTASE.
SMARTiSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.
PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

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

Entry informationi

Entry nameiFYPP1_ARATH
AccessioniPrimary (citable) accession number: Q9SX52
Secondary accession number(s): Q0WWV2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: May 1, 2000
Last modified: April 29, 2015
This is version 99 of the entry and version 1 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

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.