ID   DIS1_SCHPO              Reviewed;         882 AA.
AC   Q09933;
DT   06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Phosphoprotein p93;
GN   Name=dis1; ORFNames=SPCC736.14;
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 [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP   PHOSPHORYLATION AT THR-279; SER-293; SER-300; SER-551; SER-556 AND SER-590.
RX   PubMed=7628693; DOI=10.1101/gad.9.13.1572;
RA   Nabeshima K., Kurooka H., Takeuchi M., Kinoshita K., Nakaseo Y.,
RA   Yanagida M.;
RT   "p93dis1, which is required for sister chromatid separation, is a novel
RT   microtubule and spindle pole body-associating protein phosphorylated at the
RT   Cdc2 target sites.";
RL   Genes Dev. 9:1572-1585(1995).
RN   [2]
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   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293; SER-551; SER-556;
RP   SER-649 AND THR-650, 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).
CC   -!- FUNCTION: Has a role in sister chromatid separation.
CC       {ECO:0000269|PubMed:7628693}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, spindle pole body {ECO:0000269|PubMed:7628693}. Cytoplasm,
CC       cytoskeleton, spindle {ECO:0000269|PubMed:7628693}. Note=Spindle pole
CC       body during metaphase and spindle microtubules during anaphase.
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DR   EMBL; D55635; BAA09505.1; -; Genomic_DNA.
DR   EMBL; CU329672; CAA19278.1; -; Genomic_DNA.
DR   PIR; T43250; T43250.
DR   RefSeq; NP_587785.1; NM_001022778.2.
DR   PDB; 5M9E; X-ray; 2.83 A; E/F/G/H=833-852.
DR   PDBsum; 5M9E; -.
DR   AlphaFoldDB; Q09933; -.
DR   SMR; Q09933; -.
DR   BioGRID; 276068; 31.
DR   STRING; 4896.SPCC736.14.1; -.
DR   iPTMnet; Q09933; -.
DR   MaxQB; Q09933; -.
DR   PaxDb; Q09933; -.
DR   PRIDE; Q09933; -.
DR   EnsemblFungi; SPCC736.14.1; SPCC736.14.1:pep; SPCC736.14.
DR   GeneID; 2539505; -.
DR   KEGG; spo:SPCC736.14; -.
DR   PomBase; SPCC736.14; dis1.
DR   VEuPathDB; FungiDB:SPCC736.14; -.
DR   eggNOG; KOG1820; Eukaryota.
DR   HOGENOM; CLU_008401_1_0_1; -.
DR   InParanoid; Q09933; -.
DR   OMA; RCLAKCM; -.
DR   PhylomeDB; Q09933; -.
DR   PRO; PR:Q09933; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR   GO; GO:0005881; C:cytoplasmic microtubule; IDA:PomBase.
DR   GO; GO:0000776; C:kinetochore; IDA:PomBase.
DR   GO; GO:0015630; C:microtubule cytoskeleton; IDA:PomBase.
DR   GO; GO:0072686; C:mitotic spindle; IDA:PomBase.
DR   GO; GO:0044732; C:mitotic spindle pole body; IDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0032991; C:protein-containing complex; NAS:PomBase.
DR   GO; GO:0000922; C:spindle pole; IBA:GO_Central.
DR   GO; GO:0005816; C:spindle pole body; IBA:GO_Central.
DR   GO; GO:0099070; C:static microtubule bundle; IDA:PomBase.
DR   GO; GO:0008017; F:microtubule binding; IDA:PomBase.
DR   GO; GO:0061863; F:microtubule plus end polymerase; EXP:PomBase.
DR   GO; GO:0051010; F:microtubule plus-end binding; IEA:InterPro.
DR   GO; GO:0051315; P:attachment of mitotic spindle microtubules to kinetochore; IMP:PomBase.
DR   GO; GO:0030951; P:establishment or maintenance of microtubule cytoskeleton polarity; IBA:GO_Central.
DR   GO; GO:1990571; P:meiotic centromere clustering; IMP:PomBase.
DR   GO; GO:0001578; P:microtubule bundle formation; IMP:PomBase.
DR   GO; GO:0007019; P:microtubule depolymerization; IMP:PomBase.
DR   GO; GO:0046785; P:microtubule polymerization; IBA:GO_Central.
DR   GO; GO:0000022; P:mitotic spindle elongation; IMP:PomBase.
DR   GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central.
DR   Gene3D; 1.25.10.10; -; 2.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR034085; TOG.
DR   InterPro; IPR045110; XMAP215.
DR   PANTHER; PTHR12609; PTHR12609; 1.
DR   SMART; SM01349; TOG; 2.
DR   SUPFAM; SSF48371; SSF48371; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Cytoskeleton; Microtubule; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..882
FT                   /note="Phosphoprotein p93"
FT                   /id="PRO_0000079913"
FT   REGION          250..297
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          562..678
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          809..833
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        572..656
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        663..678
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         279
FT                   /note="Phosphothreonine; by CDC2"
FT                   /evidence="ECO:0000269|PubMed:7628693"
FT   MOD_RES         293
FT                   /note="Phosphoserine; by CDC2"
FT                   /evidence="ECO:0000269|PubMed:18257517,
FT                   ECO:0000269|PubMed:7628693"
FT   MOD_RES         300
FT                   /note="Phosphoserine; by CDC2"
FT                   /evidence="ECO:0000269|PubMed:7628693"
FT   MOD_RES         551
FT                   /note="Phosphoserine; by CDC2"
FT                   /evidence="ECO:0000269|PubMed:18257517,
FT                   ECO:0000269|PubMed:7628693"
FT   MOD_RES         556
FT                   /note="Phosphoserine; by CDC2"
FT                   /evidence="ECO:0000269|PubMed:18257517,
FT                   ECO:0000269|PubMed:7628693"
FT   MOD_RES         590
FT                   /note="Phosphoserine; by CDC2"
FT                   /evidence="ECO:0000269|PubMed:7628693"
FT   MOD_RES         649
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         650
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   882 AA;  97546 MW;  F5184C0227E9DBCF CRC64;
     MELDDFNSRI LSQIFDKSWK VRFEAYESLL HALNRALDDS DVCFQPWIHD PALWKQGLCD
     SNVPTQEHAV KSLRCFLDKS RQKGVNSAKS FVVAPLLEKC LPSPRQSIRD ASHQALLILA
     KSDALDYVLE GLFSAARVKH PKQAVASIKE LNSLLENFGI PALSPIPFYK LIPTLFAQSD
     KNIRQEASNL SITLYAWVGN AFKTHVFPQL KQIQVSDLEA SFQNVTSRTT TGGHISNSLN
     TQEVVLPSFS SNAKPKPHLS SKSSSQGNTL QRSTSSFSTP NRKVSQPSDF SASPSRSIVS
     PAKNIVGSTP VDVLSKLTPE FHTALSSPKW KDRKEALESM VPVCSNPVYQ EGDYSELLRV
     IAKSLKDANV VVVGVAALLL THIAKALRKG FLPYTGIVLP SLFDRFKERK SSLVHSLLDA
     ANAIFESCGL NDIMDETLEF LKHKNPQVKT ETLRWLNRCL QLTDVCPPRA SLETLCSLCV
     TLINDTFEPV RMATTNVLAT LVQIFSQPVL SKYIVGLDPK KLPKILELSK DITVNAHPNQ
     PSRPRLPRVA SPLKTSPVKL AVTPQAPSPL PSSNPSQASL TEESLSTRSS PTKPSTTSLR
     SQSLVNRFAS STLKAPSSSS KGVSNAASSK QSFPSSPSIS KKLETSRLST KKLPGSTMKA
     ASALKEYPQQ QSMKSGGEKQ DNLVTITMSE KVELDLLREE KAIRQVQEAE DALERERLFR
     EINDLQIQNA EMKEQVYEKE STISQKEVEI TSLRNEKDRL STRLQQVLLE LEKQHETNEE
     AMDIDLKVPE SGAIGRVTTR ATATTAMDES GNAGMVSSGI HSVSTKPSSY GTRRSLAGSM
     LQKPTQFSRP SFMFSPEARD NWRESHDLSS HLWEQIQRMK KA