DEP1_SCHPO
ID DEP1_SCHPO Reviewed; 491 AA.
AC Q9P7M1; Q9UTW6; Q9UTY3;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Transcriptional regulatory protein dep1;
GN Name=dep1; ORFNames=SPBC21C3.02c;
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 166-354, 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 IDENTIFICATION IN THE RPD3C(L) COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=19040720; DOI=10.1186/gb-2008-9-11-r167;
RA Shevchenko A., Roguev A., Schaft D., Buchanan L., Habermann B., Sakalar C.,
RA Thomas H., Krogan N.J., Shevchenko A., Stewart A.F.;
RT "Chromatin Central: towards the comparative proteome by accurate mapping of
RT the yeast proteomic environment.";
RL Genome Biol. 9:R167.1-R167.22(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204 AND SER-223, AND
RP 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).
CC -!- FUNCTION: Component of the RPD3C(L) histone deacetylase complex (HDAC)
CC responsible for the deacetylation of lysine residues on the N-terminal
CC part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation
CC gives a tag for epigenetic repression and plays an important role in
CC transcriptional regulation, cell cycle progression and developmental
CC events (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the RPD3C(L) complex.
CC {ECO:0000269|PubMed:19040720}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10759889,
CC ECO:0000269|PubMed:16823372}.
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DR EMBL; CU329671; CAB76038.1; -; Genomic_DNA.
DR EMBL; AB027934; BAA87238.1; -; Genomic_DNA.
DR EMBL; AB027956; BAA87260.1; -; Genomic_DNA.
DR PIR; T50346; T50346.
DR RefSeq; NP_596582.1; NM_001022502.2.
DR AlphaFoldDB; Q9P7M1; -.
DR SMR; Q9P7M1; -.
DR BioGRID; 277121; 81.
DR STRING; 4896.SPBC21C3.02c.1; -.
DR iPTMnet; Q9P7M1; -.
DR MaxQB; Q9P7M1; -.
DR PaxDb; Q9P7M1; -.
DR PRIDE; Q9P7M1; -.
DR EnsemblFungi; SPBC21C3.02c.1; SPBC21C3.02c.1:pep; SPBC21C3.02c.
DR GeneID; 2540595; -.
DR KEGG; spo:SPBC21C3.02c; -.
DR PomBase; SPBC21C3.02c; dep1.
DR VEuPathDB; FungiDB:SPBC21C3.02c; -.
DR eggNOG; ENOG502S14R; Eukaryota.
DR HOGENOM; CLU_555700_0_0_1; -.
DR InParanoid; Q9P7M1; -.
DR OMA; THERFNA; -.
DR Reactome; R-SPO-3214815; HDACs deacetylate histones.
DR Reactome; R-SPO-5689880; Ub-specific processing proteases.
DR PRO; PR:Q9P7M1; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0033698; C:Rpd3L complex; IDA:PomBase.
DR GO; GO:0070822; C:Sin3-type complex; IBA:GO_Central.
DR GO; GO:0042826; F:histone deacetylase binding; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016575; P:histone deacetylation; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR013907; Sds3.
DR PANTHER; PTHR21964; PTHR21964; 1.
DR Pfam; PF08598; Sds3; 1.
DR SMART; SM01401; Sds3; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Nucleus; Phosphoprotein; Reference proteome;
KW Repressor; Transcription; Transcription regulation.
FT CHAIN 1..491
FT /note="Transcriptional regulatory protein dep1"
FT /id="PRO_0000116878"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 491 AA; 55628 MW; 9BAD36E96EEF9C85 CRC64;
MTENLQSESI PHEILPKEPF DLPMNNLKSS PKNKDSEKRI NNSIAESEQV VDSALSNPET
NANEDIIAPQ LPSQNSEIIE KNSPVNKLNS STSLTTHQLA SLPKLEVTDH DNVSEAETVV
LNEDEEKETS LVGSVSVTED LGDSSAIGRT ILVNNSVEPQ MENTANITIV SPSLKESDFE
SEEKATNDNN GLIETNHNSK LEESSEHEEE EDEESNIERT EDSDHQIPQR GGTLEAPRKG
GPRSGVGSRK RKRATVSRKW STNSESKIKR VALETSQEES DREIADRRSA SEQAHEADDE
KAIKRKEAFD ALLNIETEFT FLRNRLYGKK LLKLNEHEEM IQNETHERFN ACIDLITERR
DDRVRLATEN LMKQLGNIKN VMDYVTKQRK YQLLFDKRRI RQALLTKIAT KCFQLLNKQK
SVHDPTYITQ KTMSYRQSAL LQKQRIEYEA AVLCELNSFA GFPTAPIIET ASFDDIRNDL
LEMGCLSENQ D
