Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P48482

- PP12_ARATH

UniProt

P48482 - PP12_ARATH

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Serine/threonine-protein phosphatase PP1 isozyme 2

Gene

TOPP2

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 bindingi70 – 701Manganese 1By similarity
Metal bindingi72 – 721Manganese 1By similarity
Metal bindingi98 – 981Manganese 1By similarity
Metal bindingi98 – 981Manganese 2By similarity
Metal bindingi130 – 1301Manganese 2By similarity
Active sitei131 – 1311Proton donorBy similarity
Metal bindingi179 – 1791Manganese 2By similarity
Metal bindingi254 – 2541Manganese 2By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. protein dephosphorylation Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BioCyciARA:AT5G59160-MONOMER.
ARA:GQT-2764-MONOMER.
ARA:GQT-2765-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase PP1 isozyme 2 (EC:3.1.3.16)
Gene namesi
Name:TOPP2
Ordered Locus Names:At5g59160
ORF Names:MNC17.7
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 5

Organism-specific databases

TAIRiAT5G59160.

Subcellular locationi

GO - Cellular componenti

  1. protein phosphatase type 1 complex Source: TAIR
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 312311Serine/threonine-protein phosphatase PP1 isozyme 2PRO_0000058798Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP48482.
PRIDEiP48482.

Expressioni

Gene expression databases

ExpressionAtlasiP48482. baseline and differential.
GenevestigatoriP48482.

Structurei

3D structure databases

ProteinModelPortaliP48482.
SMRiP48482. Positions 14-305.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0639.
HOGENOMiHOG000172697.
InParanoidiP48482.
KOiK06269.
OMAiYLSSACY.
PhylomeDBiP48482.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P48482-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAQQGQGSMD PAALDDIIRR LLDYRNPKPG TKQAMLNESE IRQLCIVSRE
60 70 80 90 100
IFLQQPNLLE LEAPIKICGD IHGQYSDLLR LFEYGGFPPT ANYLFLGDYV
110 120 130 140 150
DRGKQSLETI CLLLAYKIKY PENFFLLRGN HECASINRIY GFYDECKRRF
160 170 180 190 200
SVRLWKVFTD SFNCLPVAAV IDDKILCMHG GLSPDLTNVE QIKNIKRPTD
210 220 230 240 250
VPDSGLLCDL LWSDPSKDVK GWGMNDRGVS YTFGPDKVAE FLIKNDMDLI
260 270 280 290 300
CRAHQVVEDG YEFFADRQLV TIFSAPNYCG EFDNAGAMMS VDESLMCSFQ
310
ILKPADRKPR FL
Length:312
Mass (Da):35,532
Last modified:February 1, 1996 - v1
Checksum:iDF71C23B5CB53CC2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti181 – 1822GL → AI in CAA78153. (PubMed:8220477)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M93409 mRNA. Translation: AAA32837.1.
Z12163 mRNA. Translation: CAA78153.1.
AB016890 Genomic DNA. Translation: BAB09762.1.
CP002688 Genomic DNA. Translation: AED97150.1.
CP002688 Genomic DNA. Translation: AED97151.1.
CP002688 Genomic DNA. Translation: AED97152.1.
AY042840 mRNA. Translation: AAK68780.1.
BT002401 mRNA. Translation: AAO00761.1.
BT024861 mRNA. Translation: ABD65592.1.
PIRiS24264.
S31086.
RefSeqiNP_001032103.1. NM_001037026.1.
NP_200724.1. NM_125306.2.
NP_851218.1. NM_180887.4.
UniGeneiAt.20932.
At.311.

Genome annotation databases

EnsemblPlantsiAT5G59160.1; AT5G59160.1; AT5G59160.
AT5G59160.2; AT5G59160.2; AT5G59160.
AT5G59160.3; AT5G59160.3; AT5G59160.
GeneIDi836034.
KEGGiath:AT5G59160.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M93409 mRNA. Translation: AAA32837.1 .
Z12163 mRNA. Translation: CAA78153.1 .
AB016890 Genomic DNA. Translation: BAB09762.1 .
CP002688 Genomic DNA. Translation: AED97150.1 .
CP002688 Genomic DNA. Translation: AED97151.1 .
CP002688 Genomic DNA. Translation: AED97152.1 .
AY042840 mRNA. Translation: AAK68780.1 .
BT002401 mRNA. Translation: AAO00761.1 .
BT024861 mRNA. Translation: ABD65592.1 .
PIRi S24264.
S31086.
RefSeqi NP_001032103.1. NM_001037026.1.
NP_200724.1. NM_125306.2.
NP_851218.1. NM_180887.4.
UniGenei At.20932.
At.311.

3D structure databases

ProteinModelPortali P48482.
SMRi P48482. Positions 14-305.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PaxDbi P48482.
PRIDEi P48482.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT5G59160.1 ; AT5G59160.1 ; AT5G59160 .
AT5G59160.2 ; AT5G59160.2 ; AT5G59160 .
AT5G59160.3 ; AT5G59160.3 ; AT5G59160 .
GeneIDi 836034.
KEGGi ath:AT5G59160.

Organism-specific databases

TAIRi AT5G59160.

Phylogenomic databases

eggNOGi COG0639.
HOGENOMi HOG000172697.
InParanoidi P48482.
KOi K06269.
OMAi YLSSACY.
PhylomeDBi P48482.

Enzyme and pathway databases

BioCyci ARA:AT5G59160-MONOMER.
ARA:GQT-2764-MONOMER.
ARA:GQT-2765-MONOMER.

Gene expression databases

ExpressionAtlasi P48482. baseline and differential.
Genevestigatori P48482.

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. "Expression of multiple type 1 phosphoprotein phosphatases in Arabidopsis thaliana."
    Smith R.D., Walker J.C.
    Plant Mol. Biol. 21:307-316(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "A protein phosphatase 1 from Arabidopsis thaliana restores temperature sensitivity of a Schizosaccharomyces pombe cdc25ts/wee1-double mutant."
    Ferreira P.C.G., Hemerly A.S., van Montagu M., Inze D.
    Plant J. 4:81-87(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence features of the regions of 1,081,958 bp covered by seventeen physically assigned P1 and TAC clones."
    Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N., Tabata S.
    DNA Res. 5:379-391(1998) [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. "Arabidopsis ORF clones."
    Kim C.J., Chen H., Shinn P., Ecker J.R.
    Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPP12_ARATH
AccessioniPrimary (citable) accession number: P48482
Secondary accession number(s): Q24JM8, Q94B57
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: November 26, 2014
This is version 113 of the entry and version 1 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