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P48486 (PP16_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 109. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein phosphatase PP1 isozyme 6

EC=3.1.3.16
Gene names
Name:TOPP6
Synonyms:PP1BG
Ordered Locus Names:At4g11240
ORF Names:F8L21.30
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length322 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Cofactor

Binds 2 manganese ions per subunit By similarity.

Tissue specificity

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

Sequence similarities

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

Sequence caution

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

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 322322Serine/threonine-protein phosphatase PP1 isozyme 6
PRO_0000058802

Sites

Active site1221Proton donor By similarity
Metal binding611Manganese 1 By similarity
Metal binding631Manganese 1 By similarity
Metal binding891Manganese 1 By similarity
Metal binding891Manganese 2 By similarity
Metal binding1211Manganese 2 By similarity
Metal binding1701Manganese 2 By similarity
Metal binding2451Manganese 2 By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.8

Experimental info

Sequence conflict2481V → D Ref.1
Sequence conflict2481V → D Ref.2

Sequences

Sequence LengthMass (Da)Tools
P48486 [UniParc].

Last modified May 29, 2007. Version 2.
Checksum: B2320EB8E472AEDF

FASTA32236,567
        10         20         30         40         50         60 
MDETLLDDII RRLLATNNGR TVKQAQITET EIRQLCLASK EVFLSQPNLL ELEAPIKICG 

        70         80         90        100        110        120 
DVHGQFPDLL RLFEYGGYPP AANYLFLGDY VDRGKQSIET ICLLLAYKVK YKFNFFLLRG 

       130        140        150        160        170        180 
NHECASINRV YGFYDECKRR YNVRLWKTFT ECFNCLPVSA LIDDKILCMH GGLSPDIKSL 

       190        200        210        220        230        240 
DDIRRIPRPI DVPDQGILCD LLWADPDREI QGWGENDRGV SYTFGADKVA EFLQTHDLDL 

       250        260        270        280        290        300 
ICRAHQVVED GYEFFAKRQL VTIFSAPNYC GEFDNAGALM SVDDSLTCSF QILKASEKKG 

       310        320 
RFGFNNNVPR PGTPPHKGGK GR 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRT13015.
RefSeqNP_567375.1. NM_117195.4.
UniGeneAt.3651.

3D structure databases

ProteinModelPortalP48486.
SMRP48486. Positions 6-294.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid12025. 2 interactions.
IntActP48486. 2 interactions.

Proteomic databases

PaxDbP48486.
PRIDEP48486.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G11240.1; AT4G11240.1; AT4G11240.
GeneID826726.
KEGGath:AT4G11240.

Organism-specific databases

TAIRAT4G11240.

Phylogenomic databases

eggNOGCOG0639.
HOGENOMHOG000172697.
InParanoidP48486.
KOK06269.
OMAKFNFFLL.
PhylomeDBP48486.

Enzyme and pathway databases

BioCycARA:AT4G11240-MONOMER.

Gene expression databases

GenevestigatorP48486.

Family and domain databases

Gene3D3.60.21.10. 1 hit.
InterProIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSPR00114. STPHPHTASE.
SMARTSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMSSF56300. SSF56300. 1 hit.
PROSITEPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePP16_ARATH
AccessionPrimary (citable) accession number: P48486
Secondary accession number(s): Q8RX64, Q9SUT7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: May 29, 2007
Last modified: June 11, 2014
This is version 109 of the entry and version 2 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