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P48486

- PP16_ARATH

UniProt

P48486 - PP16_ARATH

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Protein

Serine/threonine-protein phosphatase PP1 isozyme 6

Gene

TOPP6

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

Functioni

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 bindingi61 – 611Manganese 1By similarity
Metal bindingi63 – 631Manganese 1By similarity
Metal bindingi89 – 891Manganese 1By similarity
Metal bindingi89 – 891Manganese 2By similarity
Metal bindingi121 – 1211Manganese 2By similarity
Active sitei122 – 1221Proton donorBy similarity
Metal bindingi170 – 1701Manganese 2By similarity
Metal bindingi245 – 2451Manganese 2By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. dephosphorylation Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BioCyciARA:AT4G11240-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase PP1 isozyme 6 (EC:3.1.3.16)
Gene namesi
Name:TOPP6
Synonyms:PP1BG
Ordered Locus Names:At4g11240
ORF Names:F8L21.30
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 4

Organism-specific databases

TAIRiAT4G11240.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 322322Serine/threonine-protein phosphatase PP1 isozyme 6PRO_0000058802Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP48486.
PRIDEiP48486.

Expressioni

Tissue specificityi

Strongly up-regulated within developing flowers, especially in the tapetum, the developing and mature pollen and in the ovaries.

Gene expression databases

GenevestigatoriP48486.

Interactioni

Protein-protein interaction databases

BioGridi12025. 2 interactions.
IntActiP48486. 2 interactions.

Structurei

3D structure databases

ProteinModelPortaliP48486.
SMRiP48486. Positions 6-294.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PPP phosphatase family. PP-1 subfamily.Curated

Phylogenomic databases

eggNOGiCOG0639.
HOGENOMiHOG000172697.
InParanoidiP48486.
KOiK06269.
OMAiKFNFFLL.
PhylomeDBiP48486.

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.

P48486-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDETLLDDII RRLLATNNGR TVKQAQITET EIRQLCLASK EVFLSQPNLL
60 70 80 90 100
ELEAPIKICG DVHGQFPDLL RLFEYGGYPP AANYLFLGDY VDRGKQSIET
110 120 130 140 150
ICLLLAYKVK YKFNFFLLRG NHECASINRV YGFYDECKRR YNVRLWKTFT
160 170 180 190 200
ECFNCLPVSA LIDDKILCMH GGLSPDIKSL DDIRRIPRPI DVPDQGILCD
210 220 230 240 250
LLWADPDREI QGWGENDRGV SYTFGADKVA EFLQTHDLDL ICRAHQVVED
260 270 280 290 300
GYEFFAKRQL VTIFSAPNYC GEFDNAGALM SVDDSLTCSF QILKASEKKG
310 320
RFGFNNNVPR PGTPPHKGGK GR
Length:322
Mass (Da):36,567
Last modified:May 29, 2007 - v2
Checksum:iB2320EB8E472AEDF
GO

Sequence cautioni

The sequence CAB51408.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAB81225.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti248 – 2481V → D(PubMed:7773310)Curated
Sequence conflicti248 – 2481V → D(PubMed:9617814)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z46253 mRNA. Translation: CAA86339.1.
U80921 Genomic DNA. Translation: AAC39460.1.
AL096882 Genomic DNA. Translation: CAB51408.1. Sequence problems.
AL161531 Genomic DNA. Translation: CAB81225.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE82988.1.
AY090365 mRNA. Translation: AAL91268.1.
AY122904 mRNA. Translation: AAM67437.1.
AY086060 mRNA. Translation: AAM63269.1.
PIRiT13015.
RefSeqiNP_567375.1. NM_117195.4.
UniGeneiAt.3651.

Genome annotation databases

EnsemblPlantsiAT4G11240.1; AT4G11240.1; AT4G11240.
GeneIDi826726.
KEGGiath:AT4G11240.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z46253 mRNA. Translation: CAA86339.1 .
U80921 Genomic DNA. Translation: AAC39460.1 .
AL096882 Genomic DNA. Translation: CAB51408.1 . Sequence problems.
AL161531 Genomic DNA. Translation: CAB81225.1 . Sequence problems.
CP002687 Genomic DNA. Translation: AEE82988.1 .
AY090365 mRNA. Translation: AAL91268.1 .
AY122904 mRNA. Translation: AAM67437.1 .
AY086060 mRNA. Translation: AAM63269.1 .
PIRi T13015.
RefSeqi NP_567375.1. NM_117195.4.
UniGenei At.3651.

3D structure databases

ProteinModelPortali P48486.
SMRi P48486. Positions 6-294.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 12025. 2 interactions.
IntActi P48486. 2 interactions.

Proteomic databases

PaxDbi P48486.
PRIDEi P48486.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT4G11240.1 ; AT4G11240.1 ; AT4G11240 .
GeneIDi 826726.
KEGGi ath:AT4G11240.

Organism-specific databases

TAIRi AT4G11240.

Phylogenomic databases

eggNOGi COG0639.
HOGENOMi HOG000172697.
InParanoidi P48486.
KOi K06269.
OMAi KFNFFLL.
PhylomeDBi P48486.

Enzyme and pathway databases

BioCyci ARA:AT4G11240-MONOMER.

Gene expression databases

Genevestigatori P48486.

Family and domain databases

Gene3Di 3.60.21.10. 1 hit.
InterProi IPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view ]
Pfami PF00149. Metallophos. 1 hit.
[Graphical view ]
PRINTSi PR00114. STPHPHTASE.
SMARTi SM00156. PP2Ac. 1 hit.
[Graphical view ]
SUPFAMi SSF56300. SSF56300. 1 hit.
PROSITEi PS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A novel Arabidopsis type 1 protein phosphatase is highly expressed in male and female tissues and functionally complements a conditional cell cycle mutant of Aspergillus."
    Arundhati A., Feiler H., Traas J., Zhang H., Lunness P.A., Doonan J.H.
    Plant J. 7:823-834(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Molecular cloning and chromosomal mapping of type one serine/threonine protein phosphatases in Arabidopsis thaliana."
    Lin Q., Li J., Smith R.D., Walker J.C.
    Plant Mol. Biol. 37:471-481(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "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(1999) [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. "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.
  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. "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.
  8. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPP16_ARATH
AccessioniPrimary (citable) accession number: P48486
Secondary accession number(s): Q8RX64, Q9SUT7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: May 29, 2007
Last modified: November 26, 2014
This is version 111 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