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Q75QN6 (DPHS1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 83. 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·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dual specificity protein phosphatase PHS1

EC=3.1.3.16
EC=3.1.3.48
Alternative name(s):
Protein PROPYZAMIDE-HYPERSENSITIVE 1
Gene names
Name:PHS1
Ordered Locus Names:At5g23720
ORF Names:MQM1.1
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length929 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Probable dual specificity phosphatase that binds and dephosphorylates MPK18, modulating the organization and dynamics of cortical microtubules. Acts as negative regulator of abscisic acid (ABA) signaling during seed germination and light-induced stomata aperture. Ref.1 Ref.5 Ref.6

Catalytic activity

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

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Subunit structure

Interacts with MPK18. Ref.6

Subcellular location

Cytoplasm Ref.6 Ref.7.

Tissue specificity

Expressed in roots, leaves and flowers. Ref.1 Ref.7

Induction

By abscisic acid. Ref.5

Disruption phenotype

Embryonic lethality when homozygous in the phs1-2 allele (Ref.1), but after several backcrossing, phs1-2 and other homozygous alleles (phs1-4 and phs1-5) are similar to the wild-type (Ref.7). Ref.1

Sequence similarities

Contains 1 tyrosine-protein phosphatase domain.

Sequence caution

The sequence BAB10045.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processAbscisic acid signaling pathway
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   Molecular functionHydrolase
Protein phosphatase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processabscisic acid-activated signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

cortical microtubule organization

Inferred from mutant phenotype Ref.1Ref.6. Source: TAIR

inactivation of MAPK activity

Inferred from Biological aspect of Ancestor. Source: GOC

protein dephosphorylation

Inferred from Biological aspect of Ancestor. Source: RefGenome

regulation of MAP kinase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

regulation of gene expression

Inferred from mutant phenotype Ref.5. Source: TAIR

regulation of stomatal movement

Inferred from mutant phenotype Ref.5. Source: TAIR

response to abscisic acid

Inferred from mutant phenotype Ref.5. Source: TAIR

   Cellular_componentcytoplasm

Inferred from direct assay Ref.6. Source: TAIR

   Molecular_functionMAP kinase phosphatase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

phosphoprotein phosphatase activity

Inferred from direct assay Ref.1. Source: TAIR

phosphotransferase activity, alcohol group as acceptor

Inferred from electronic annotation. Source: InterPro

protein tyrosine phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein tyrosine/serine/threonine phosphatase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MPK18Q9C5C03EBI-2349366,EBI-1238534

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q75QN6-1)

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.
Isoform 2 (identifier: Q75QN6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-89: MAEPEKKRDQ...HRIDDMVTSA → MIWSL
Note: Derived from EST data. No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 929929Dual specificity protein phosphatase PHS1
PRO_0000417331

Regions

Domain703 – 847145Tyrosine-protein phosphatase
Region792 – 7987Substrate binding By similarity
Motif903 – 9119Nuclear export signal Potential

Sites

Active site7921Phosphocysteine intermediate By similarity

Natural variations

Alternative sequence1 – 8989MAEPE…MVTSA → MIWSL in isoform 2.
VSP_043502

Experimental info

Mutagenesis641R → C in phs1-1; reduces activity 2-fold. Primary roots skewing. No effect on the interaction with MPK18. Ref.1 Ref.6
Mutagenesis7921C → S: Loss of activity. Ref.1
Mutagenesis9061L → A: Loss of nuclear export; when associated with A-909. Ref.7
Mutagenesis9091L → A: Loss of nuclear export; when associated with A-906. Ref.7

Sequences

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

Last modified July 5, 2004. Version 1.
Checksum: 5FE10C006DD39A07

FASTA929104,235
        10         20         30         40         50         60 
MAEPEKKRDQ PFSQEKDEEK DLYLVHDEHE SPLPLTVTSR VLYMLGDIAS GPAYRFTQWL 

        70         80         90        100        110        120 
DLVRKRSATY GSSGFPHRLH RIDDMVTSAG ERNTDPKSPP SRQSSEISLW ERLGKASTVD 

       130        140        150        160        170        180 
IDSSCFSWNM LSSLHHTEHS SSTDHSEEDQ SKPLEVTVNS GGVVFFALFN SSSSEDASRK 

       190        200        210        220        230        240 
EEAAVIKFAS SRMATQSERL GYEFSKWLGV QIPQARVIHS CNPEWTLIKE ATEKAQAKAT 

       250        260        270        280        290        300 
SEGDEVGEMT CSELLEALEL SRCLLLMSYV HGCPMLESMS SFETEEKAER AAAALGRILV 

       310        320        330        340        350        360 
LDLVIRNEDR LPCRQLRWRG NPANLLLTDR IVSSAKHHEC SFDEAFDSAI KRYHPKDYRS 

       370        380        390        400        410        420 
IQRERRASSV DSRSRLSISD QMLVSQASDF SDITESPRSY DTGLMSPMSD RSVAADFHLV 

       430        440        450        460        470        480 
AIDSGVPRRP PAGKRASDQE IYPRLVELLL NSSQYSSNLL HEITEGSLGY PQAEDGEETS 

       490        500        510        520        530        540 
NVRSVVTPVV REFRNGFRAG LRDLQEFHIF LVTLHQKLDV LLRAFFSMMD KTMCADFDRE 

       550        560        570        580        590        600 
DFAVPESPSH THGHEVNHYP SPSKDRVPSD NSSDHSESDM QKSVPRTPNS ENKEDGSSPK 

       610        620        630        640        650        660 
SRESWHGRSG KGGESLSSQR LAAKLRDFHK FAKVDAESNK ELDQWNETLR NEVMKLCQEN 

       670        680        690        700        710        720 
GFNTGFFEGS DNNSCTDAYE LKVRLEHILE RISLISKAAN TEKPSMIQEN LFIGGGLAAR 

       730        740        750        760        770        780 
SIYTLQHLGI THVLCLCANE IGQSDTQYPD LFEYQNFSIT DDEDSNIESI FQEALDFIKH 

       790        800        810        820        830        840 
GEETGGKILV HCFEGRSRSA TVVLAYLMLQ KKLTLLEAWS KLRKVHRRAQ PNDGFARILI 

       850        860        870        880        890        900 
NLDKKCHGKV SMEWRQRKPT MKVCPVCGKN AGLSSSSLKL HLQKSHRKLS SGSVDSAMNM 

       910        920 
EIQKALEALK LSTGRGSSAS SNSFQSHPG 

« Hide

Isoform 2 [UniParc].

Checksum: FDC18FA704D11838
Show »

FASTA84594,591

References

« Hide 'large scale' references
[1]"A semidominant mutation in an Arabidopsis mitogen-activated protein kinase phosphatase-like gene compromises cortical microtubule organization."
Naoi K., Hashimoto T.
Plant Cell 16:1841-1853(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, MUTAGENESIS OF ARG-64 AND CYS-792.
[2]"Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence features of the 1.6 Mb regions covered by twenty physically assigned P1 clones."
Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M., Miyajima N., Tabata S.
DNA Res. 4:215-230(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]"Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence features of the regions of 3,076,755 bp covered by sixty P1 and TAC clones."
Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H., Tabata S.
DNA Res. 7:31-63(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[4]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[5]"The phs1-3 mutation in a putative dual-specificity protein tyrosine phosphatase gene provokes hypersensitive responses to abscisic acid in Arabidopsis thaliana."
Quettier A.L., Bertrand C., Habricot Y., Miginiac E., Agnes C., Jeannette E., Maldiney R.
Plant J. 47:711-719(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION BY ABSCISIC ACID.
[6]"Arabidopsis mitogen-activated protein kinase MPK18 mediates cortical microtubule functions in plant cells."
Walia A., Lee J.S., Wasteneys G., Ellis B.
Plant J. 59:565-575(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MPK18, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-64.
[7]"Mitogen-activated protein kinase phosphatase PHS1 is retained in the cytoplasm by nuclear extrusion signal-dependent and independent mechanisms."
Pytela J., Kato T., Hashimoto T.
Planta 231:1311-1322(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF LEU-906 AND LEU-909.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB161693 mRNA. Translation: BAD18373.1.
AB005244, AB025633 Genomic DNA. Translation: BAB10045.1. Sequence problems.
CP002688 Genomic DNA. Translation: AED93202.1.
CP002688 Genomic DNA. Translation: AED93203.1.
RefSeqNP_197761.2. NM_122277.2.
NP_851066.2. NM_180735.3.
UniGeneAt.22786.

3D structure databases

ProteinModelPortalQ75QN6.
SMRQ75QN6. Positions 661-845.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ75QN6. 2 interactions.
STRING3702.AT5G23720.1-P.

Proteomic databases

PaxDbQ75QN6.
PRIDEQ75QN6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G23720.1; AT5G23720.1; AT5G23720. [Q75QN6-1]
GeneID832437.
KEGGath:AT5G23720.

Organism-specific databases

TAIRAT5G23720.

Phylogenomic databases

eggNOGCOG2453.
HOGENOMHOG000030291.
InParanoidQ75QN6.
OMADRLPCRQ.
PhylomeDBQ75QN6.
ProtClustDBCLSN2680206.

Enzyme and pathway databases

BioCycARA:AT5G23720-MONOMER.

Gene expression databases

GenevestigatorQ75QN6.

Family and domain databases

Gene3D1.10.1070.11. 2 hits.
InterProIPR015275. Actin-fragmin_kin_cat_dom.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR011009. Kinase-like_dom.
IPR000403. PI3/4_kinase_cat_dom.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR015880. Znf_C2H2-like.
[Graphical view]
PANTHERPTHR10159. PTHR10159. 1 hit.
PfamPF09192. Act-Frag_cataly. 1 hit.
PF00782. DSPc. 1 hit.
[Graphical view]
SMARTSM00195. DSPc. 1 hit.
SM00355. ZnF_C2H2. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 2 hits.
PROSITEPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDPHS1_ARATH
AccessionPrimary (citable) accession number: Q75QN6
Secondary accession number(s): F4KE97, Q9FFA8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2012
Last sequence update: July 5, 2004
Last modified: April 16, 2014
This is version 83 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