Q75QN6 (DPHS1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	929 AA.
Sequence status	Complete.
Protein existence	Evidence 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 phosphoprotein + H2O = a protein + 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 process	Abscisic acid signaling pathway
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Molecular function	Hydrolase Protein phosphatase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	abscisic acid mediated signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW cortical microtubule organization Inferred from mutant phenotype Ref.1Ref.6. Source: TAIR peptidyl-tyrosine dephosphorylation Inferred from electronic annotation. Source: GOC 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 stimulus Inferred from mutant phenotype Ref.5. Source: TAIR
Cellular_component	cytoplasm Inferred from direct assay Ref.6. Source: TAIR
Molecular_function	MAP kinase phosphatase activity Inferred from Biological aspect of Ancestor. Source: RefGenome phosphotransferase activity, alcohol group as acceptor Inferred from electronic annotation. Source: InterPro protein tyrosine phosphatase activity Inferred from electronic annotation. Source: EC protein tyrosine/serine/threonine phosphatase activity Inferred from Biological aspect of Ancestor. Source: RefGenome zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MPK18	Q9C5C0	3	EBI-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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 929	929	Dual specificity protein phosphatase PHS1		PRO_0000417331
Regions
	Domain	703 – 847	145	Tyrosine-protein phosphatase
	Region	792 – 798	7	Substrate binding By similarity
	Motif	903 – 911	9	Nuclear export signal Potential
Sites
	Active site	792	1	Phosphocysteine intermediate By similarity
Natural variations
	Alternative sequence	1 – 89	89	MAEPE…MVTSA → MIWSL in isoform 2.		VSP_043502
Experimental info
	Mutagenesis	64	1	R → C in phs1-1; reduces activity 2-fold. Primary roots skewing. No effect on the interaction with MPK18. Ref.1 Ref.6
	Mutagenesis	792	1	C → S: Loss of activity. Ref.1
	Mutagenesis	906	1	L → A: Loss of nuclear export; when associated with A-909. Ref.7
	Mutagenesis	909	1	L → A: Loss of nuclear export; when associated with A-906. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 5FE10C006DD39A07	FASTA	929	104,235
	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
	Isoform 2 [UniParc]. Checksum: FDC18FA704D11838	FASTA	845	94,591
	10 20 30 40 50 60 MIWSLGERNT DPKSPPSRQS SEISLWERLG KASTVDIDSS CFSWNMLSSL HHTEHSSSTD 70 80 90 100 110 120 HSEEDQSKPL EVTVNSGGVV FFALFNSSSS EDASRKEEAA VIKFASSRMA TQSERLGYEF 130 140 150 160 170 180 SKWLGVQIPQ ARVIHSCNPE WTLIKEATEK AQAKATSEGD EVGEMTCSEL LEALELSRCL 190 200 210 220 230 240 LLMSYVHGCP MLESMSSFET EEKAERAAAA LGRILVLDLV IRNEDRLPCR QLRWRGNPAN 250 260 270 280 290 300 LLLTDRIVSS AKHHECSFDE AFDSAIKRYH PKDYRSIQRE RRASSVDSRS RLSISDQMLV 310 320 330 340 350 360 SQASDFSDIT ESPRSYDTGL MSPMSDRSVA ADFHLVAIDS GVPRRPPAGK RASDQEIYPR 370 380 390 400 410 420 LVELLLNSSQ YSSNLLHEIT EGSLGYPQAE DGEETSNVRS VVTPVVREFR NGFRAGLRDL 430 440 450 460 470 480 QEFHIFLVTL HQKLDVLLRA FFSMMDKTMC ADFDREDFAV PESPSHTHGH EVNHYPSPSK 490 500 510 520 530 540 DRVPSDNSSD HSESDMQKSV PRTPNSENKE DGSSPKSRES WHGRSGKGGE SLSSQRLAAK 550 560 570 580 590 600 LRDFHKFAKV DAESNKELDQ WNETLRNEVM KLCQENGFNT GFFEGSDNNS CTDAYELKVR 610 620 630 640 650 660 LEHILERISL ISKAANTEKP SMIQENLFIG GGLAARSIYT LQHLGITHVL CLCANEIGQS 670 680 690 700 710 720 DTQYPDLFEY QNFSITDDED SNIESIFQEA LDFIKHGEET GGKILVHCFE GRSRSATVVL 730 740 750 760 770 780 AYLMLQKKLT LLEAWSKLRK VHRRAQPNDG FARILINLDK KCHGKVSMEW RQRKPTMKVC 790 800 810 820 830 840 PVCGKNAGLS SSSLKLHLQK SHRKLSSGSV DSAMNMEIQK ALEALKLSTG RGSSASSNSF QSHPG

References

	« Hide 'large scale' referencesShow '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.
IPI	IPI00539575.
RefSeq	NP_197761.2. NM_122277.2. NP_851066.2. NM_180735.3.
UniGene	At.22786.
3D structure databases
ProteinModelPortal	Q75QN6.
SMR	Q75QN6. Positions 711-845.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q75QN6. 2 interactions.
STRING	3702.AT5G23720.1-P.
Proteomic databases
PaxDb	Q75QN6.
PRIDE	Q75QN6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT5G23720.1; AT5G23720.1; AT5G23720.
GeneID	832437.
KEGG	ath:AT5G23720.
Organism-specific databases
TAIR	At5g23720.
Phylogenomic databases
eggNOG	COG2453.
HOGENOM	HOG000030291.
InParanoid	Q75QN6.
OMA	VHRRAQP.
PhylomeDB	Q75QN6.
ProtClustDB	CLSN2680206.
Gene expression databases
ArrayExpress	Q75QN6.
Genevestigator	Q75QN6.
Family and domain databases
Gene3D	1.10.1070.11. 2 hits.
InterPro	IPR015275. 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]
PANTHER	PTHR10159. PTHR10159. 1 hit.
Pfam	PF09192. Act-Frag_cataly. 1 hit. PF00782. DSPc. 1 hit. [Graphical view]
SMART	SM00195. DSPc. 1 hit. SM00355. ZnF_C2H2. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00383. TYR_PHOSPHATASE_1. 1 hit. PS50056. TYR_PHOSPHATASE_2. 1 hit. PS50054. TYR_PHOSPHATASE_DUAL. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DPHS1_ARATH

Accession

Primary (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:	May 1, 2013
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program