DNT1_SCHPO
ID DNT1_SCHPO Reviewed; 599 AA.
AC O74354;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Nucleolar protein dnt1;
GN Name=dnt1; ORFNames=SPBC25D12.02c;
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 FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=17538026; DOI=10.1091/mbc.e06-09-0853;
RA Jin Q.W., Ray S., Choi S.H., McCollum D.;
RT "The nucleolar net1/cfi1-related protein dnt1 antagonizes the septation
RT initiation network in fission yeast.";
RL Mol. Biol. Cell 18:2924-2934(2007).
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-174; SER-306 AND THR-513, 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: Negatively regulates the septation initiation network (SIN)
CC pathway, independently of the cdc14 phosphatase clp1. May also have a
CC role in silencing rDNA transcription. Required for maintaining the
CC exclusive nucleolus localization of nuc1.
CC {ECO:0000269|PubMed:17538026}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleolus. Cytoplasm,
CC cytoskeleton, spindle. Note=In late anaphase, localizes to the ends of
CC the mitotic spindle.
CC -!- PTM: Phosphorylated by clp1. {ECO:0000269|PubMed:17538026,
CC ECO:0000269|PubMed:18257517}.
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DR EMBL; CU329671; CAA20098.1; -; Genomic_DNA.
DR PIR; T39990; T39990.
DR RefSeq; NP_596544.1; NM_001022465.2.
DR AlphaFoldDB; O74354; -.
DR BioGRID; 277027; 11.
DR IntAct; O74354; 1.
DR STRING; 4896.SPBC25D12.02c.1; -.
DR iPTMnet; O74354; -.
DR MaxQB; O74354; -.
DR PaxDb; O74354; -.
DR PRIDE; O74354; -.
DR EnsemblFungi; SPBC25D12.02c.1; SPBC25D12.02c.1:pep; SPBC25D12.02c.
DR GeneID; 2540499; -.
DR KEGG; spo:SPBC25D12.02c; -.
DR PomBase; SPBC25D12.02c; dnt1.
DR VEuPathDB; FungiDB:SPBC25D12.02c; -.
DR HOGENOM; CLU_464730_0_0_1; -.
DR InParanoid; O74354; -.
DR OMA; DIPNEYC; -.
DR PRO; PR:O74354; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0072686; C:mitotic spindle; IDA:PomBase.
DR GO; GO:0005730; C:nucleolus; IDA:PomBase.
DR GO; GO:0019211; F:phosphatase activator activity; IBA:GO_Central.
DR GO; GO:0000182; F:rDNA binding; IBA:GO_Central.
DR GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR GO; GO:1902543; P:negative regulation of protein localization to mitotic spindle pole body; IMP:PomBase.
DR GO; GO:0031030; P:negative regulation of septation initiation signaling; IMP:PomBase.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IMP:PomBase.
DR GO; GO:0000183; P:rDNA heterochromatin assembly; IBA:GO_Central.
DR InterPro; IPR018844; Dnt1-like_N.
DR InterPro; IPR043185; Dnt1/Tof2/Net1.
DR PANTHER; PTHR28196; PTHR28196; 3.
DR Pfam; PF10407; Cytokin_check_N; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Mitosis; Nucleus;
KW Phosphoprotein; Reference proteome; Septation.
FT CHAIN 1..599
FT /note="Nucleolar protein dnt1"
FT /id="PRO_0000303893"
FT REGION 210..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 292..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..502
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..546
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..569
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 513
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 599 AA; 65977 MW; 6BF1F3AC1FC689E8 CRC64;
MRTTLRLHII KDGEQDNQFM ILFDPSSSIS LLKEKVQETY KSLYPFESNI NIRNIKNEES
YDIPNEYLVG EIFPTNSKVI VESFSSPLKK LDGTMINFKE KNIQHDLDGV ENDFATVQSA
SNGVHAINGK RTHPDESENP RKLPKKNFVE AIDANSPGFV YRPTSIRDRA YSISSNHDNE
STLTEGIALK EIESPDKDRK ADGIVNLSVT QEEDDNHQSF NSSLTPSQPT TYNRANFFSI
NDASSDSSSD APLRTLSSPS RLRMKDNDRK YLVEHSPAAL IKESETIDGI DDKSLRSSTR
EVSVESPNED SVNDDSSSDV SDEKETEAKH EIRAPAIIVR ETSSHPSTAV PSENDTTESE
NDTLSESSTT SISSSPSENS DTSDDLTKVD SPNKSLVNDN VSAKHDKESE NGKSKFPPPS
QTLVTTSTIS AAGNEPSDEI GSENDSDSDS DSDSSVPLSQ LQKKSQQRNS VSHEIQNRGT
KGSPKEPKAK PSTERPETHR TLSYSRLSEL SKTFSPEIRE PSLTKKTAVS MQESKEEGRS
DESSESEESG SSSDESDNSE KEDRSNPIPV EKRASTVLNT KKKRKAKRNS ALAGLAALV
