PDP1_SCHPO
ID PDP1_SCHPO Reviewed; 359 AA.
AC O59676; Q9USE8;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=PWWP domain-containing protein 1;
DE AltName: Full=Set9-associated factor pdp1;
GN Name=pdp1; ORFNames=SPBC29A3.13;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 9-189, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [3]
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, AND IDENTIFICATION BY
RP 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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH SET9,
RP HISTONE-BINDING, FUNCTION, DOMAIN, AND MUTAGENESIS OF TRP-66 AND PHE-94.
RX PubMed=19250904; DOI=10.1016/j.molcel.2009.02.002;
RA Wang Y., Reddy B., Thompson J., Wang H., Noma K., Yates J.R. III, Jia S.;
RT "Regulation of Set9-mediated H4K20 methylation by a PWWP domain protein.";
RL Mol. Cell 33:428-437(2009).
CC -!- FUNCTION: Necessary for DNA damage checkpoint activation. Required for
CC the association of set9 with chromatin and subsequent methylation of
CC H4K20. Associates with H4K20me1 to increase the concentration of set9
CC on chromatin to perform H4K20me3. H4K20me3 is mainly enriched at
CC heterochromatin and is required for proper heterochromatin assembly.
CC {ECO:0000269|PubMed:19250904}.
CC -!- SUBUNIT: Interacts with set9 and histone H4K20me1. Associates with
CC nucleosomes. {ECO:0000269|PubMed:19250904}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10759889,
CC ECO:0000269|PubMed:16823372}.
CC -!- DOMAIN: The C-terminal region mediates association with set9, whereas
CC the N-terminal PWWP domain recognizes H4K20me1.
CC {ECO:0000269|PubMed:19250904}.
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; CU329671; CAA18390.1; -; Genomic_DNA.
DR EMBL; AB027814; BAA87118.1; -; Genomic_DNA.
DR PIR; T40084; T40084.
DR RefSeq; NP_595841.1; NM_001021745.2.
DR PDB; 2L89; NMR; -; A=45-152.
DR PDBsum; 2L89; -.
DR AlphaFoldDB; O59676; -.
DR SMR; O59676; -.
DR BioGRID; 276883; 50.
DR STRING; 4896.SPBC29A3.13.1; -.
DR iPTMnet; O59676; -.
DR MaxQB; O59676; -.
DR PaxDb; O59676; -.
DR PRIDE; O59676; -.
DR EnsemblFungi; SPBC29A3.13.1; SPBC29A3.13.1:pep; SPBC29A3.13.
DR GeneID; 2540354; -.
DR KEGG; spo:SPBC29A3.13; -.
DR PomBase; SPBC29A3.13; pdp1.
DR VEuPathDB; FungiDB:SPBC29A3.13; -.
DR HOGENOM; CLU_740005_0_0_1; -.
DR InParanoid; O59676; -.
DR OMA; YLNYEMI; -.
DR PhylomeDB; O59676; -.
DR PRO; PR:O59676; -.
DR Proteomes; UP000002485; Chromosome II.
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; IDA:PomBase.
DR GO; GO:1990889; F:H4K20me3 modified histone binding; IDA:PomBase.
DR GO; GO:0042393; F:histone binding; IDA:PomBase.
DR GO; GO:0035064; F:methylated histone binding; IPI: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; ISO:PomBase.
DR CDD; cd05840; SPBC215_ISWI_like; 1.
DR InterPro; IPR035503; IOC4-like_PWWP.
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 3D-structure; Chromatin regulator; DNA damage; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..359
FT /note="PWWP domain-containing protein 1"
FT /id="PRO_0000303950"
FT DOMAIN 52..114
FT /note="PWWP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00162"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..241
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MUTAGEN 66
FT /note="W->A: Reduces the association of set9 with
FT nucleosome and the H4K20me3 levels."
FT /evidence="ECO:0000269|PubMed:19250904"
FT MUTAGEN 94
FT /note="F->A: Reduces the association of set9 with
FT nucleosome and the H4K20me3 levels."
FT /evidence="ECO:0000269|PubMed:19250904"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:2L89"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:2L89"
FT STRAND 65..80
FT /evidence="ECO:0007829|PDB:2L89"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:2L89"
FT STRAND 86..94
FT /evidence="ECO:0007829|PDB:2L89"
FT TURN 95..98
FT /evidence="ECO:0007829|PDB:2L89"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:2L89"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:2L89"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:2L89"
FT HELIX 113..121
FT /evidence="ECO:0007829|PDB:2L89"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:2L89"
FT HELIX 128..137
FT /evidence="ECO:0007829|PDB:2L89"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:2L89"
SQ SEQUENCE 359 AA; 40923 MW; A892EE06E5F7DB2A CRC64;
MNNARTNAKR RRLSSKQGGL SISEGKESNI PSVVEESKDN LEQASADDRL NFGDRILVKA
PGYPWWPALL LRRKETKDSL NTNSSFNVLY KVLFFPDFNF AWVKRNSVKP LLDSEIAKFL
GSSKRKSKEL IEAYEASKTP PDLKEESSTD EEMDSLSAAE EKPNFLQKRK YHWETSLDES
DAESISSGSL MSITSISEMY GPTVASTSRS STQLSDQRYP LSSNFDHRGE AKGKGKQPLK
NPQERGRISP SSPLNDQTKA LMQRLLFFRH KLQKAFLSPD HLIVEEDFYN ASKYLNAISD
IPFLNYELIT STKLAKVLKR IAFLEHLEND ELYDIRQKCK NLLYSWAMFL PNEPSIKGM
