ID   PTF2_SCHPO              Reviewed;         126 AA.
AC   O60127;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Pdp3-interacting factor 2;
GN   Name=ptf2; ORFNames=SPBC16G5.13;
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 [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).
RN   [2]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MST2 COMPLEX,
RP   AND FUNCTION.
RX   PubMed=22184112; DOI=10.1074/jbc.m111.329417;
RA   Wang Y., Kallgren S.P., Reddy B.D., Kuntz K., Lopez-Maury L., Thompson J.,
RA   Watt S., Ma C., Hou H., Shi Y., Yates J.R. III, Bahler J., O'Connell M.J.,
RA   Jia S.;
RT   "Histone H3 lysine 14 acetylation is required for activation of a DNA
RT   damage checkpoint in fission yeast.";
RL   J. Biol. Chem. 287:4386-4393(2012).
CC   -!- FUNCTION: Component of the mst2 complex which is a highly specific H3
CC       lysine 14 (H3K14) acetyltransferase that functions together with gcn5
CC       to regulate global levels of H3K14 acetylation (H3K14ac), critical for
CC       DNA damage checkpoint activation. {ECO:0000269|PubMed:22184112}.
CC   -!- SUBUNIT: Component of the mst2 complex composed of at least eaf6, mst2,
CC       nto1, pdp3, ptf1, ptf2 and tfg3. {ECO:0000269|PubMed:22184112}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC       {ECO:0000269|PubMed:16823372}.
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DR   EMBL; CU329671; CAA19032.1; -; Genomic_DNA.
DR   PIR; T39605; T39605.
DR   RefSeq; NP_596762.1; NM_001023782.2.
DR   AlphaFoldDB; O60127; -.
DR   SMR; O60127; -.
DR   BioGRID; 276259; 38.
DR   STRING; 4896.SPBC16G5.13.1; -.
DR   MaxQB; O60127; -.
DR   PaxDb; O60127; -.
DR   EnsemblFungi; SPBC16G5.13.1; SPBC16G5.13.1:pep; SPBC16G5.13.
DR   GeneID; 2539706; -.
DR   KEGG; spo:SPBC16G5.13; -.
DR   PomBase; SPBC16G5.13; ptf2.
DR   VEuPathDB; FungiDB:SPBC16G5.13; -.
DR   HOGENOM; CLU_2016530_0_0_1; -.
DR   OMA; FTSHEYL; -.
DR   PRO; PR:O60127; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0036410; C:Mst2 histone acetyltransferase complex; TAS:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:UniProtKB-KW.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Chromatin regulator; Cytoplasm; DNA damage; Nucleus; Reference proteome.
FT   CHAIN           1..126
FT                   /note="Pdp3-interacting factor 2"
FT                   /id="PRO_0000116769"
SQ   SEQUENCE   126 AA;  14564 MW;  F6C760531AFB1BE2 CRC64;
     MDEIQESSCN EKLSDEDLAA EFVEFTDNIP IEIYRSLRYI RKYENFFAKE NENLNTAARL
     VCDCPISEVP SAKQKLADSL FTSHEYLRQT SAEANKLYEN VLASYKHLCE KIKYLEADNP
     LYVPAP