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Protein

Serine/threonine-protein phosphatase PP1 isozyme 5

Gene

TOPP5

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: 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
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BioCyciARA:AT3G46820-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase PP1 isozyme 5 (EC:3.1.3.16)
Gene namesi
Name:TOPP5
Ordered Locus Names:At3g46820
ORF Names:T6H20.150
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 3

Organism-specific databases

TAIRiAT3G46820.

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 5PRO_0000058801Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP48485.
PRIDEiP48485.

Expressioni

Gene expression databases

ExpressionAtlasiP48485. baseline and differential.
GenevestigatoriP48485.

Interactioni

Protein-protein interaction databases

MINTiMINT-8060796.

Structurei

3D structure databases

ProteinModelPortaliP48485.
SMRiP48485. Positions 14-304.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0639.
HOGENOMiHOG000172697.
InParanoidiP48485.
KOiK06269.
OMAiQIKNIER.
PhylomeDBiP48485.

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.

P48485-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAQQGQGSMD PAVLDDIIRR LLDYRNPKAG TKQAMLNDSE IRQLCFVSRE
60 70 80 90 100
IFLQQPCLLE LAAPVKICGD IHGQYSDLLR LFEYGGFPPA ANYLFLGDYV
110 120 130 140 150
DRGKQSLETI CLLLAYKIKY PENFFLLRGN HECASINRIY GFYDECKRRF
160 170 180 190 200
NVKLWKVFTD TFNCLPVAAV IDEKILCMHG GLSPELINVE QIKNIERPTD
210 220 230 240 250
VPDAGLLCDL LWSDPSKDVK GWGMNDRGVS YTFGADKVAE FLIKNDMDLV
260 270 280 290 300
CRAHQVVEDG YEFFADRQLV TMFSAPNYCG EFDNAGALMS VDESLMCSFQ
310
ILKPVDRRSR FF
Length:312
Mass (Da):35,519
Last modified:February 1, 1996 - v1
Checksum:i937084D580708A68
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti245 – 2462ND → IP in CAA78152. (PubMed:8220477)Curated
Sequence conflicti288 – 2881L → M in CAA78152. (PubMed:8220477)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M93412 mRNA. Translation: AAA32840.1.
AL096859 Genomic DNA. Translation: CAB51183.1.
CP002686 Genomic DNA. Translation: AEE78208.1.
BT024715 mRNA. Translation: ABD59053.1.
AK220755 mRNA. Translation: BAD93940.1.
AK227072 mRNA. Translation: BAE99129.1.
Z12162 mRNA. Translation: CAA78152.1.
PIRiS25532.
S31089.
RefSeqiNP_190266.1. NM_114549.3.
UniGeneiAt.311.

Genome annotation databases

EnsemblPlantsiAT3G46820.1; AT3G46820.1; AT3G46820.
GeneIDi823835.
KEGGiath:AT3G46820.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M93412 mRNA. Translation: AAA32840.1.
AL096859 Genomic DNA. Translation: CAB51183.1.
CP002686 Genomic DNA. Translation: AEE78208.1.
BT024715 mRNA. Translation: ABD59053.1.
AK220755 mRNA. Translation: BAD93940.1.
AK227072 mRNA. Translation: BAE99129.1.
Z12162 mRNA. Translation: CAA78152.1.
PIRiS25532.
S31089.
RefSeqiNP_190266.1. NM_114549.3.
UniGeneiAt.311.

3D structure databases

ProteinModelPortaliP48485.
SMRiP48485. Positions 14-304.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-8060796.

Proteomic databases

PaxDbiP48485.
PRIDEiP48485.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G46820.1; AT3G46820.1; AT3G46820.
GeneIDi823835.
KEGGiath:AT3G46820.

Organism-specific databases

TAIRiAT3G46820.

Phylogenomic databases

eggNOGiCOG0639.
HOGENOMiHOG000172697.
InParanoidiP48485.
KOiK06269.
OMAiQIKNIER.
PhylomeDBiP48485.

Enzyme and pathway databases

BioCyciARA:AT3G46820-MONOMER.

Gene expression databases

ExpressionAtlasiP48485. baseline and differential.
GenevestigatoriP48485.

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]
ProtoNetiSearch...

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. "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
    Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F.
    , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
    Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Arabidopsis ORF clones."
    Shinn P., Chen H., Kim C.J., Ecker J.R.
    Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  6. "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] OF 245-312.
  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 nameiPP15_ARATH
AccessioniPrimary (citable) accession number: P48485
Secondary accession number(s): Q29Q41, Q570F3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: January 7, 2015
This is version 109 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

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.