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Protein

Protein phosphatase 2C 57

Gene

PPH1

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

Functioni

Catalytic activityi

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

Cofactori

Mg2+By similarity, Mn2+By similarityNote: Binds 2 magnesium or manganese ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi93 – 931Manganese 1By similarity
Metal bindingi93 – 931Manganese 2By similarity
Metal bindingi94 – 941Manganese 1; via carbonyl oxygenBy similarity
Metal bindingi296 – 2961Manganese 2By similarity
Metal bindingi339 – 3391Manganese 2By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. phosphatase activity Source: TAIR
  3. protein serine/threonine phosphatase activity Source: InterPro

GO - Biological processi

  1. dephosphorylation Source: TAIR
  2. photosynthetic electron transport chain Source: TAIR
  3. photosystem stoichiometry adjustment Source: TAIR
  4. protein dephosphorylation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Magnesium, Manganese, Metal-binding

Enzyme and pathway databases

BioCyciARA:AT4G27800-MONOMER.
ARA:GQT-2819-MONOMER.
ARA:GQT-2820-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein phosphatase 2C 57 (EC:3.1.3.16)
Short name:
AtPP2C57
Alternative name(s):
Protein phosphatase 2C PPH1
Short name:
PP2C PPH1
Gene namesi
Name:PPH1
Ordered Locus Names:At4g27800
ORF Names:T27E11.40
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G27800.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei363 – 38321HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. chloroplast Source: TAIR
  2. chloroplast stroma Source: TAIR
  3. cytoplasm Source: TAIR
  4. integral component of membrane Source: UniProtKB-KW
  5. nucleolus Source: TAIR
  6. nucleus Source: TAIR
  7. thylakoid Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 388388Protein phosphatase 2C 57PRO_0000057768Add
BLAST

Proteomic databases

PaxDbiP49599.
PRIDEiP49599.

Expressioni

Gene expression databases

ExpressionAtlasiP49599. baseline and differential.
GenevestigatoriP49599.

Structurei

3D structure databases

ProteinModelPortaliP49599.
SMRiP49599. Positions 60-348.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini59 – 348290PPM-type phosphatasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the PP2C family.Curated
Contains 1 PPM-type phosphatase domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0631.
HOGENOMiHOG000029436.
InParanoidiP49599.
OMAiLYKECAA.
PhylomeDBiP49599.

Family and domain databases

Gene3Di3.60.40.10. 1 hit.
InterProiIPR001932. PP2C-like_dom.
IPR000222. PP2C_Mn2_Asp60_BS.
IPR015655. Protein_Pase_2C.
[Graphical view]
PANTHERiPTHR13832. PTHR13832. 1 hit.
PfamiPF00481. PP2C. 1 hit.
[Graphical view]
SMARTiSM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMiSSF81606. SSF81606. 1 hit.
PROSITEiPS01032. PPM_1. 1 hit.
PS51746. PPM_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P49599-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MALLRPHLHR FHSNTLRHSA YPSADAGGGL VVYPTYGRHR CSAIAIDAPS
60 70 80 90 100
SLTGVTPIRW GYTSVQGFRD EMEDDIVIRS DAVDSFSYAA VFDGHAGSSS
110 120 130 140 150
VKFLREELYK ECVGALQAGS LLNGGDFAAI KEALIKAFES VDRNLLKWLE
160 170 180 190 200
ANGDEEDESG STATVMIIRN DVSFIAHIGD SCAVLSRSGQ IEELTDYHRP
210 220 230 240 250
YGSSRAAIQE VKRVKEAGGW IVNGRICGDI AVSRAFGDIR FKTKKNDMLK
260 270 280 290 300
KGVDEGRWSE KFVSRIEFKG DMVVATPDIF QVPLTSDVEF IILASDGLWD
310 320 330 340 350
YMKSSDVVSY VRDQLRKHGN VQLACESLAQ VALDRRSQDN ISIIIADLGR
360 370 380
TEWKNLPAQR QNVVVELVQA ATTIGLVTVG IWMSSHLS
Length:388
Mass (Da):42,719
Last modified:January 23, 2001 - v2
Checksum:i496ECCC786AEB802
GO
Isoform 2 (identifier: P49599-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     334-335: DR → VK
     336-388: Missing.

Note: Derived from EST data. No experimental confirmation available.

Show »
Length:335
Mass (Da):36,863
Checksum:i5DD6AB6CDFC20D92
GO
Isoform 3 (identifier: P49599-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     323-326: LACE → ATCL
     327-388: Missing.

Note: Derived from EST data. No experimental confirmation available.

Show »
Length:326
Mass (Da):35,925
Checksum:i3554FE275D389482
GO

Sequence cautioni

The sequence AAA92889.1 differs from that shown. Reason: Frameshift at position 360. Curated
The sequence CAB43968.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 44MALL → SNSS in AAA92889 (PubMed:7569999).Curated
Sequence conflicti69 – 702RD → QY in AAA92889 (PubMed:7569999).Curated
Sequence conflicti271 – 2711D → N in AAA92889 (PubMed:7569999).Curated
Sequence conflicti353 – 3531W → C in AAA92889 (PubMed:7569999).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei323 – 3264LACE → ATCL in isoform 3. CuratedVSP_034835
Alternative sequencei327 – 38862Missing in isoform 3. CuratedVSP_034836Add
BLAST
Alternative sequencei334 – 3352DR → VK in isoform 2. CuratedVSP_034837
Alternative sequencei336 – 38853Missing in isoform 2. CuratedVSP_034838Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL078579 Genomic DNA. Translation: CAB43968.1. Sequence problems.
AL161571 Genomic DNA. Translation: CAB81429.1.
CP002687 Genomic DNA. Translation: AEE85393.1.
CP002687 Genomic DNA. Translation: AEE85394.1.
CP002687 Genomic DNA. Translation: AEE85395.1.
AY080875 mRNA. Translation: AAL87346.1.
AY114060 mRNA. Translation: AAM45108.1.
U34803 mRNA. Translation: AAA92889.1. Frameshift.
PIRiC85323.
T09019.
RefSeqiNP_194509.1. NM_118918.4. [P49599-1]
NP_849459.1. NM_179128.1. [P49599-2]
NP_849460.1. NM_179129.1. [P49599-3]
UniGeneiAt.23824.

Genome annotation databases

EnsemblPlantsiAT4G27800.1; AT4G27800.1; AT4G27800. [P49599-1]
GeneIDi828893.
KEGGiath:AT4G27800.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL078579 Genomic DNA. Translation: CAB43968.1. Sequence problems.
AL161571 Genomic DNA. Translation: CAB81429.1.
CP002687 Genomic DNA. Translation: AEE85393.1.
CP002687 Genomic DNA. Translation: AEE85394.1.
CP002687 Genomic DNA. Translation: AEE85395.1.
AY080875 mRNA. Translation: AAL87346.1.
AY114060 mRNA. Translation: AAM45108.1.
U34803 mRNA. Translation: AAA92889.1. Frameshift.
PIRiC85323.
T09019.
RefSeqiNP_194509.1. NM_118918.4. [P49599-1]
NP_849459.1. NM_179128.1. [P49599-2]
NP_849460.1. NM_179129.1. [P49599-3]
UniGeneiAt.23824.

3D structure databases

ProteinModelPortaliP49599.
SMRiP49599. Positions 60-348.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PaxDbiP49599.
PRIDEiP49599.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G27800.1; AT4G27800.1; AT4G27800. [P49599-1]
GeneIDi828893.
KEGGiath:AT4G27800.

Organism-specific databases

TAIRiAT4G27800.

Phylogenomic databases

eggNOGiCOG0631.
HOGENOMiHOG000029436.
InParanoidiP49599.
OMAiLYKECAA.
PhylomeDBiP49599.

Enzyme and pathway databases

BioCyciARA:AT4G27800-MONOMER.
ARA:GQT-2819-MONOMER.
ARA:GQT-2820-MONOMER.

Gene expression databases

ExpressionAtlasiP49599. baseline and differential.
GenevestigatoriP49599.

Family and domain databases

Gene3Di3.60.40.10. 1 hit.
InterProiIPR001932. PP2C-like_dom.
IPR000222. PP2C_Mn2_Asp60_BS.
IPR015655. Protein_Pase_2C.
[Graphical view]
PANTHERiPTHR13832. PTHR13832. 1 hit.
PfamiPF00481. PP2C. 1 hit.
[Graphical view]
SMARTiSM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMiSSF81606. SSF81606. 1 hit.
PROSITEiPS01032. PPM_1. 1 hit.
PS51746. PPM_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

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(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (MAR-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(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: cv. Columbia.
  4. "Quantitative monitoring of gene expression patterns with a complementary DNA microarray."
    Schena M., Shalon D., Davis R.W., Brown P.O.
    Science 270:467-470(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-365 (ISOFORM 1).
    Strain: cv. Columbia.
  5. "Plant PP2C phosphatases: emerging functions in stress signaling."
    Schweighofer A., Hirt H., Meskiene I.
    Trends Plant Sci. 9:236-243(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY, NOMENCLATURE.
  6. "Genome-wide and expression analysis of protein phosphatase 2C in rice and Arabidopsis."
    Xue T., Wang D., Zhang S., Ehlting J., Ni F., Jacab S., Zheng C., Zhong Y.
    BMC Genomics 9:550-550(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY, NOMENCLATURE.

Entry informationi

Entry nameiP2C57_ARATH
AccessioniPrimary (citable) accession number: P49599
Secondary accession number(s): Q3E9V3
, Q3E9V4, Q9M0J6, Q9STP6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 1996
Last sequence update: January 23, 2001
Last modified: March 31, 2015
This is version 129 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

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.