位置:首页 > 蛋白库 > PP2A2_SCHPO
PP2A2_SCHPO
ID   PP2A2_SCHPO             Reviewed;         322 AA.
AC   P23636;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   03-AUG-2022, entry version 162.
DE   RecName: Full=Major serine/threonine-protein phosphatase PP2A-2 catalytic subunit;
DE            EC=3.1.3.16;
GN   Name=ppa2; ORFNames=SPBC16H5.07c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=972 / HM123;
RX   PubMed=2170029; DOI=10.1016/0092-8674(90)90173-c;
RA   Kinoshita N., Ohkura H., Yanagida M.;
RT   "Distinct, essential roles of type 1 and 2A protein phosphatases in the
RT   control of the fission yeast cell division cycle.";
RL   Cell 63:405-415(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10407269;
RX   DOI=10.1002/(sici)1097-0061(199907)15:10a<893::aid-yea430>3.0.co;2-s;
RA   Xiang Z., Lyne M.H., Wood V., Rajandream M.A., Barrell B.G., Aves S.J.;
RT   "DNA sequencing and analysis of a 67.4 kb region from the right arm of
RT   Schizosaccharomyces pombe chromosome II reveals 28 open reading frames
RT   including the genes his5, pol5, ppa2, rip1, rpb8 and skb1.";
RL   Yeast 15:893-901(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
CC   -!- FUNCTION: Essential role in cell cycle control. PP2A may be involved in
CC       controlling the entry into mitosis, possibly acting as an inhibitor.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83421; EC=3.1.3.16;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:61977; EC=3.1.3.16;
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC   -!- MISCELLANEOUS: Retarded cell growth is produced by disruption of ppa2.
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-2A subfamily.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M58519; AAA63579.1; -; Genomic_DNA.
DR   EMBL; CU329671; CAA17905.1; -; Genomic_DNA.
DR   PIR; B36076; B36076.
DR   RefSeq; NP_595940.1; NM_001021848.2.
DR   AlphaFoldDB; P23636; -.
DR   SMR; P23636; -.
DR   BioGRID; 276610; 111.
DR   DIP; DIP-61477N; -.
DR   IntAct; P23636; 1.
DR   STRING; 4896.SPBC16H5.07c.1; -.
DR   MaxQB; P23636; -.
DR   PaxDb; P23636; -.
DR   EnsemblFungi; SPBC16H5.07c.1; SPBC16H5.07c.1:pep; SPBC16H5.07c.
DR   GeneID; 2540072; -.
DR   KEGG; spo:SPBC16H5.07c; -.
DR   PomBase; SPBC16H5.07c; ppa2.
DR   VEuPathDB; FungiDB:SPBC16H5.07c; -.
DR   eggNOG; KOG0371; Eukaryota.
DR   HOGENOM; CLU_004962_8_1_1; -.
DR   InParanoid; P23636; -.
DR   OMA; EGYNWGQ; -.
DR   PhylomeDB; P23636; -.
DR   Reactome; R-SPO-198753; ERK/MAPK targets.
DR   Reactome; R-SPO-202670; ERKs are inactivated.
DR   Reactome; R-SPO-389513; CTLA4 inhibitory signaling.
DR   Reactome; R-SPO-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR   Reactome; R-SPO-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR   Reactome; R-SPO-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR   PRO; PR:P23636; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0000775; C:chromosome, centromeric region; IDA:PomBase.
DR   GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0000159; C:protein phosphatase type 2A complex; IDA:PomBase.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; IMP:PomBase.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IMP:PomBase.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:1990813; P:meiotic centromeric cohesion protection; IMP:PomBase.
DR   GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR   GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; IMP:PomBase.
DR   GO; GO:0010515; P:negative regulation of induction of conjugation with cellular fusion; IMP:PomBase.
DR   GO; GO:0023052; P:signaling; NAS:PomBase.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   Pfam; PF00149; Metallophos; 1.
DR   PRINTS; PR00114; STPHPHTASE.
DR   SMART; SM00156; PP2Ac; 1.
DR   SUPFAM; SSF56300; SSF56300; 1.
DR   PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Hydrolase; Manganese; Metal-binding;
KW   Methylation; Mitosis; Protein phosphatase; Reference proteome.
FT   CHAIN           1..322
FT                   /note="Major serine/threonine-protein phosphatase PP2A-2
FT                   catalytic subunit"
FT                   /id="PRO_0000058872"
FT   ACT_SITE        131
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         70
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         72
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         98
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         98
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         130
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         180
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         254
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         322
FT                   /note="Leucine methyl ester"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   322 AA;  36489 MW;  8709C544FAFEDD85 CRC64;
     MSIDPANDSK LAPEANDATL GDVDRWIEQL KKCEPLSEAD VEMLCDKARE VLCQENNVQP
     VRNPVTVCGD IHGQFHDLME LFKIGGDVPD MNYLFMGDYV DRGYHSVETV SLLVAMKLRY
     PNRITILRGN HESRQITQVY GFYDECLRKY GSANVWKHFT NLFDYFPLTA LIEDRIFCLH
     GGLSPSIDSL DHVRTLDRVQ EVPHEGPMCD LLWSDPDDRC GWGISPRGAG YTFGQDISET
     FNHANGLSLT ARAHQLVMEG FNWAHDGDVV TIFSAPNYCY RCGNQAAILE VDDTMNQVFL
     QFDPAPREGE PVIARRTPDY FL
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024