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Protein

Minor serine/threonine-protein phosphatase PP2A-1 catalytic subunit

Gene

ppa1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Essential role in cell cycle control. PP2A may be involved in controlling the entry into mitosis, possibly acting as an inhibitor.

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 bindingi57 – 571Manganese 1By similarity
Metal bindingi59 – 591Manganese 1By similarity
Metal bindingi85 – 851Manganese 1By similarity
Metal bindingi85 – 851Manganese 2By similarity
Metal bindingi117 – 1171Manganese 2By similarity
Active sitei118 – 1181Proton donorBy similarity
Metal bindingi167 – 1671Manganese 2By similarity
Metal bindingi241 – 2411Manganese 2By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. phosphoprotein phosphatase activity Source: PomBase

GO - Biological processi

  1. cell division Source: UniProtKB-KW
  2. mitotic nuclear division Source: UniProtKB-KW
  3. protein dephosphorylation Source: PomBase
  4. regulation of cytoplasmic translation Source: PomBase
  5. signal transduction Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_292227. PP2A-mediated dephosphorylation of key metabolic factors.
REACT_304275. Glycolysis.
REACT_309729. Integration of energy metabolism.
REACT_315486. ERK/MAPK targets.
REACT_328317. ERKs are inactivated.

Names & Taxonomyi

Protein namesi
Recommended name:
Minor serine/threonine-protein phosphatase PP2A-1 catalytic subunit (EC:3.1.3.16)
Gene namesi
Name:ppa1
ORF Names:SPAC823.15
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome I

Organism-specific databases

PomBaseiSPAC823.15.

Subcellular locationi

GO - Cellular componenti

  1. nucleus Source: PomBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 309309Minor serine/threonine-protein phosphatase PP2A-1 catalytic subunitPRO_0000058871Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei309 – 3091Leucine methyl esterBy similarity

Keywords - PTMi

Methylation

Proteomic databases

MaxQBiP23635.

Interactioni

Protein-protein interaction databases

BioGridi278531. 13 interactions.
MINTiMINT-4687784.
STRINGi4896.SPAC823.15-1.

Structurei

3D structure databases

ProteinModelPortaliP23635.
SMRiP23635. Positions 9-309.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PPP phosphatase family. PP-2A subfamily.Curated

Phylogenomic databases

eggNOGiCOG0639.
HOGENOMiHOG000172696.
InParanoidiP23635.
KOiK04382.
OMAiYVEIATL.
PhylomeDBiP23635.

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.

P23635-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVSGKIGEV DRWIEQLSRC EPLSEEDVIQ MCDLAKEVLS VESNVQSVRC
60 70 80 90 100
PVTVCGDIHG QFHDLMELFN IGGPSPDTNY LFMGDYVDRG YHSVETVSLL
110 120 130 140 150
IAFKIRYPQR ITILRGNHES RQITQVYGFY DECLRKYGNA NVWQYFTDLF
160 170 180 190 200
DYLPLTALIE DRIFCLHGGL SPSIDTLDHV RILDRVQEVP HEGPICDLLW
210 220 230 240 250
SDPDDRPGWG ISPRGAGYTF GPDIAEAFNH NNGLDLIARA HQLVMEGYNW
260 270 280 290 300
TTNHNVVTIF SAPNYCYRCG NQAAIMGIDD HINYAFIQYD TAPRKEELHV

TRRTPDYFL
Length:309
Mass (Da):35,291
Last modified:November 1, 1991 - v1
Checksum:i0F47604E5F740B0C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M58518 Genomic DNA. Translation: AAA63578.1.
CU329670 Genomic DNA. Translation: CAB90160.1.
PIRiA36076.
RefSeqiNP_593842.1. NM_001019271.2.

Genome annotation databases

EnsemblFungiiSPAC823.15.1; SPAC823.15.1:pep; SPAC823.15.
GeneIDi2542052.
KEGGispo:SPAC823.15.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M58518 Genomic DNA. Translation: AAA63578.1.
CU329670 Genomic DNA. Translation: CAB90160.1.
PIRiA36076.
RefSeqiNP_593842.1. NM_001019271.2.

3D structure databases

ProteinModelPortaliP23635.
SMRiP23635. Positions 9-309.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278531. 13 interactions.
MINTiMINT-4687784.
STRINGi4896.SPAC823.15-1.

Proteomic databases

MaxQBiP23635.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC823.15.1; SPAC823.15.1:pep; SPAC823.15.
GeneIDi2542052.
KEGGispo:SPAC823.15.

Organism-specific databases

PomBaseiSPAC823.15.

Phylogenomic databases

eggNOGiCOG0639.
HOGENOMiHOG000172696.
InParanoidiP23635.
KOiK04382.
OMAiYVEIATL.
PhylomeDBiP23635.

Enzyme and pathway databases

ReactomeiREACT_292227. PP2A-mediated dephosphorylation of key metabolic factors.
REACT_304275. Glycolysis.
REACT_309729. Integration of energy metabolism.
REACT_315486. ERK/MAPK targets.
REACT_328317. ERKs are inactivated.

Miscellaneous databases

NextBioi20803127.

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. "Distinct, essential roles of type 1 and 2A protein phosphatases in the control of the fission yeast cell division cycle."
    Kinoshita N., Ohkura H., Yanagida M.
    Cell 63:405-415(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 972 / HM123.
  2. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.

Entry informationi

Entry nameiPP2A1_SCHPO
AccessioniPrimary (citable) accession number: P23635
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: April 1, 2015
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: 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.