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Protein

Serine/threonine-protein phosphatase PP1

Gene
N/A
Organism
Brassica napus (Rape)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at transcript 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 bindingi2 – 21Manganese 1By similarity
Metal bindingi4 – 41Manganese 1By similarity
Metal bindingi30 – 301Manganese 1By similarity
Metal bindingi30 – 301Manganese 2By similarity
Metal bindingi62 – 621Manganese 2By similarity
Active sitei63 – 631Proton donorBy similarity
Metal bindingi111 – 1111Manganese 2By similarity
Metal bindingi186 – 1861Manganese 2By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. phosphoprotein phosphatase activity Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Manganese, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase PP1 (EC:3.1.3.16)
OrganismiBrassica napus (Rape)
Taxonomic identifieri3708 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeBrassiceaeBrassica

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – 255›255Serine/threonine-protein phosphatase PP1PRO_0000058805Add
BLAST

Proteomic databases

PRIDEiP23777.

Structurei

3D structure databases

ProteinModelPortaliP23777.
SMRiP23777. Positions 1-237.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

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: Fragment.

P23777-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
GDIHGQYQDL LRLFEYGGYP PSANFLFLGD YVDRGKQSLE TICLLLAYKI
60 70 80 90 100
RYPSKIYLLR GNHEDAKINR IYGFYDECKR RFNVRLWKIF TDCFNCLPVA
110 120 130 140 150
ALIDDKILCM HGGLSPELDN LNQIREIQRP TEIPDSGLLC DLLWSDPDQK
160 170 180 190 200
IEGWADSDRG ISCTFGADKV AEFLDKNDLD LICRGHQVVE DGYEFFAKRR
210 220 230 240 250
LVTIFSAPNY GGEFDNAGAL LSVDESLVCS FEIMKPALAS SSGHPLKKVP

KMGKS
Length:255
Mass (Da):28,850
Last modified:November 1, 1991 - v1
Checksum:i7BA2A62C12221D05
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57438 mRNA. Translation: CAA40686.1.
PIRiS12985.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57438 mRNA. Translation: CAA40686.1.
PIRiS12985.

3D structure databases

ProteinModelPortaliP23777.
SMRiP23777. Positions 1-237.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP23777.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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

  1. "Identification by molecular cloning of two cDNA sequences from the plant Brassica napus which are very similar to mammalian protein phosphatases-1 and -2A."
    Mackintosh R.W., Haycox G., Hardie D.G., Cohen P.T.W.
    FEBS Lett. 276:156-160(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiPP1_BRANA
AccessioniPrimary (citable) accession number: P23777
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: November 26, 2014
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Documents

  1. 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.