CUT12_SCHPO
ID CUT12_SCHPO Reviewed; 548 AA.
AC O59755;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=Spindle pole body-associated protein cut12;
DE AltName: Full=Cell untimely torn protein 12;
GN Name=cut12; Synonyms=stf1; ORFNames=SPBC649.05;
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 MUTAGENESIS OF GLY-71.
RC STRAIN=972 / ATCC 24843;
RX PubMed=9531532; DOI=10.1101/gad.12.7.927;
RA Bridge A.J., Morphew M., Bartlett R., Hagan I.M.;
RT "The fission yeast SPB component Cut12 links bipolar spindle formation to
RT mitotic control.";
RL Genes Dev. 12:927-942(1998).
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 FUNCTION, SELF-ASSOCIATION, AND INTERACTION WITH PLO1.
RX PubMed=12815070; DOI=10.1101/gad.256003;
RA MacIver F.H., Tanaka K., Robertson A.M., Hagan I.M.;
RT "Physical and functional interactions between polo kinase and the spindle
RT pole component Cut12 regulate mitotic commitment in S. pombe.";
RL Genes Dev. 17:1507-1523(2003).
CC -!- FUNCTION: Required for bipolar spindle formation. May act as a
CC regulator of the p34cdc2/cyclin B kinase. Required for full activation
CC of the plo1 kinase. However, in cut12.1 cells at restrictive
CC temperature the H1 kinase does rise concomitant with entry into
CC mitosis, indicating that cut12 is not required for activation of
CC p34cdc2/cyclin B. The cut12.s11 allele may promote cdc2-independent
CC phosphorylation of SPB proteins thereby overcoming the requirement for
CC cdc25 in cell cycle progression. {ECO:0000269|PubMed:12815070,
CC ECO:0000269|PubMed:9531532}.
CC -!- SUBUNIT: Self-associates. Interacts with plo1.
CC {ECO:0000269|PubMed:12815070}.
CC -!- INTERACTION:
CC O59755; P50528: plo1; NbExp=3; IntAct=EBI-1112619, EBI-1112601;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, spindle pole body {ECO:0000269|PubMed:9531532}.
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DR EMBL; Y16837; CAA76407.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA19047.1; -; Genomic_DNA.
DR PIR; T40598; T40598.
DR RefSeq; NP_595224.1; NM_001021130.2.
DR AlphaFoldDB; O59755; -.
DR SMR; O59755; -.
DR BioGRID; 277656; 18.
DR DIP; DIP-35380N; -.
DR IntAct; O59755; 5.
DR MINT; O59755; -.
DR STRING; 4896.SPBC649.05.1; -.
DR iPTMnet; O59755; -.
DR MaxQB; O59755; -.
DR PaxDb; O59755; -.
DR PRIDE; O59755; -.
DR EnsemblFungi; SPBC649.05.1; SPBC649.05.1:pep; SPBC649.05.
DR GeneID; 2541141; -.
DR KEGG; spo:SPBC649.05; -.
DR PomBase; SPBC649.05; cut12.
DR VEuPathDB; FungiDB:SPBC649.05; -.
DR HOGENOM; CLU_473405_0_0_1; -.
DR InParanoid; O59755; -.
DR OMA; PPTYAWV; -.
DR PRO; PR:O59755; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0061497; C:inner plaque of mitotic spindle pole body; IDA:PomBase.
DR GO; GO:0035974; C:meiotic spindle pole body; IDA:PomBase.
DR GO; GO:0015630; C:microtubule cytoskeleton; HDA:PomBase.
DR GO; GO:0044732; C:mitotic spindle pole body; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0030295; F:protein kinase activator activity; EXP:PomBase.
DR GO; GO:0035591; F:signaling adaptor activity; IPI:PomBase.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; EXP:PomBase.
DR GO; GO:0140480; P:mitotic spindle pole body insertion into the nuclear envelope; IMP:PomBase.
DR GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; IMP:PomBase.
DR GO; GO:0110161; P:positive regulation of mitotic spindle formation (spindle phase one); IMP:PomBase.
DR InterPro; IPR021589; Cut12.
DR Pfam; PF11500; Cut12; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Coiled coil; Cytoplasm; Cytoskeleton; Mitosis;
KW Reference proteome.
FT CHAIN 1..548
FT /note="Spindle pole body-associated protein cut12"
FT /id="PRO_0000079567"
FT REGION 122..325
FT /note="Interaction with plo1"
FT REGION 123..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 261..312
FT /evidence="ECO:0000255"
FT COILED 522..548
FT /evidence="ECO:0000255"
FT COMPBIAS 139..153
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 71
FT /note="G->V: In allele cut12.s11; causes inappropriate
FT activation of plo1 kinase in interphase."
FT /evidence="ECO:0000269|PubMed:9531532"
SQ SEQUENCE 548 AA; 61958 MW; 01FF6BC68D577A54 CRC64;
MSETLNTPPT YAWVLKAFSS KLAGTVTKPV TKMSSYIEDA ESDAELPQDA KEDLRPTETL
TPLKSKAAQN GILKTPGTLQ IKKTVNFKDI SKDAATWNRP TKNNFLFTRL DDENPLMGHE
EFKSPLLQST PKPNINNPDN ENKSKHDEFD NRYNININES YKNETKSNQR LGEDVPSKKK
YPHSMDAEIS KFKWDSNNNN DWSSLMKDCF RDVVNNNRKM KEIIKDVMID TSQAFPSESL
DEPDYTINLD APRSSSGKYW KQKFSMLDSA HSDLELELTS IRERLESLIL EKQEEINFWK
QRCRALETEK IHNHQGQQSK YKGKEFVGNR FSQMRELYTA KPSPITTKVV SRPSQSDVRE
PQEQVPSKNL HRGADMSHLA AQMLTHSSKK SHTTNLIPSE GIISSTPISA ASKVRMNLMQ
SNQTPTPAPF SIAAKKSHLP SKLSFPQDGG SLSSATTLQQ LPKARVTPNV LSSLSSNLGK
TNPTSVYQSK ANVTTSADVE KPQVKVATSS RVDYDLKSPN QRTANAKKRL EERRRRRKLK
LQELQLNS
