PDP3_SCHPO
ID PDP3_SCHPO Reviewed; 407 AA.
AC Q09842;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=PWWP domain-containing protein 3;
GN Name=pdp3; ORFNames=SPAC23D3.01;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160; SER-162; SER-236;
RP SER-238 AND SER-242, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
RN [4]
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: Nucleus {ECO:0000269|PubMed:16823372}.
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DR EMBL; CU329670; CAA91236.1; -; Genomic_DNA.
DR PIR; S62492; S62492.
DR RefSeq; NP_594539.1; NM_001019968.2.
DR AlphaFoldDB; Q09842; -.
DR SMR; Q09842; -.
DR BioGRID; 278544; 9.
DR STRING; 4896.SPAC23D3.01.1; -.
DR iPTMnet; Q09842; -.
DR MaxQB; Q09842; -.
DR PaxDb; Q09842; -.
DR PRIDE; Q09842; -.
DR EnsemblFungi; SPAC23D3.01.1; SPAC23D3.01.1:pep; SPAC23D3.01.
DR GeneID; 2542067; -.
DR KEGG; spo:SPAC23D3.01; -.
DR PomBase; SPAC23D3.01; pdp3.
DR VEuPathDB; FungiDB:SPAC23D3.01; -.
DR HOGENOM; CLU_683630_0_0_1; -.
DR InParanoid; Q09842; -.
DR OMA; QLEHRYH; -.
DR PhylomeDB; Q09842; -.
DR PRO; PR:Q09842; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000785; C:chromatin; ISM:PomBase.
DR GO; GO:0033100; C:NuA3 histone acetyltransferase complex; ISO:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0035064; F:methylated histone binding; ISS:PomBase.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:UniProtKB-KW.
DR GO; GO:0006338; P:chromatin remodeling; ISM:PomBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR000313; PWWP_dom.
DR Pfam; PF00855; PWWP; 1.
DR SMART; SM00293; PWWP; 1.
DR PROSITE; PS50812; PWWP; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; DNA damage; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..407
FT /note="PWWP domain-containing protein 3"
FT /id="PRO_0000116417"
FT DOMAIN 63..129
FT /note="PWWP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00162"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 163..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 407 AA; 46856 MW; CBB82BD5CA78A028 CRC64;
MMVARTRSQK RKLEEINNQK KIKTKKKATG QQTSNTKNLR DVKKKGKQLA YVPRTSPRKS
YKNGEYVLAK MSSFPWWPAR VASQKSIPTE VRERLKRNFR MDNGIFVQFL PSRDYAIISS
SNVLPLTVDE SRFILDHDLS TKYIQKTVGL IIASVKRKVS FSDVEEDEFE PENTRKKLQK
PIEKPKKEKI EATPKIDGGK RLKNEKSSAE ISQTSKQRPS RRSARVRMAT DNAQKSPSPI
PSPKKTAKKR VRFAGSLEEL PKFSLEYQLA QPISTVDMYA QVHYIRFNTL LYYRYQLQEI
LLSYNHYPQE SDMSHVHQIL EMIENFSAIN SELLESTKLY SLFTLLVKLS DIPLDEKYDF
SSRFSTLLLQ FQAFVQPKTM TSNVSTAPIG KNAQVNTEAA RPSVITT
