DSK1_SCHPO
ID DSK1_SCHPO Reviewed; 544 AA.
AC P36616; O59749;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Protein kinase dsk1;
DE EC=2.7.11.1;
DE AltName: Full=Dis1-suppressing protein kinase;
GN Name=dsk1; ORFNames=SPBC530.14c;
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, AND SUBCELLULAR LOCATION.
RX PubMed=8485317; DOI=10.1091/mbc.4.3.247;
RA Takeuchi M., Yanagida M.;
RT "A mitotic role for a novel fission yeast protein kinase dsk1 with cell
RT cycle stage dependent phosphorylation and localization.";
RL Mol. Biol. Cell 4:247-260(1993).
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.
RX PubMed=9488736; DOI=10.1074/jbc.273.10.5963;
RA Tang Z., Yanagida M., Lin R.-J.;
RT "Fission yeast mitotic regulator Dsk1 is an SR protein-specific kinase.";
RL J. Biol. Chem. 273:5963-5969(1998).
CC -!- FUNCTION: May play an important role in mitotic control by altering
CC cellular location, degree of phosphorylation and kinase activity.
CC Abundant expression accelerates the exit when cells are in M-phase and
CC also delays the entry into mitosis when cells are in G2. Phosphorylates
CC prp2 in vitro and so may have a role in co-ordinating pre-mRNA splicing
CC with the progression of the cell division cycle.
CC {ECO:0000269|PubMed:8485317, ECO:0000269|PubMed:9488736}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8485317}. Nucleus
CC {ECO:0000269|PubMed:8485317}. Note=Enriched in the nucleus in
CC mitotically arrested mutant and wild-type mitotic cells but cytoplasmic
CC enriched in cells at other cell-cycle stages.
CC -!- PTM: Phosphorylated on Ser residue(s).
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; D13447; BAA02706.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA19180.1; -; Genomic_DNA.
DR PIR; A47726; A47726.
DR RefSeq; NP_595327.1; NM_001021234.2.
DR AlphaFoldDB; P36616; -.
DR SMR; P36616; -.
DR BioGRID; 276395; 268.
DR STRING; 4896.SPBC530.14c.1; -.
DR iPTMnet; P36616; -.
DR MaxQB; P36616; -.
DR PaxDb; P36616; -.
DR PRIDE; P36616; -.
DR EnsemblFungi; SPBC530.14c.1; SPBC530.14c.1:pep; SPBC530.14c.
DR GeneID; 2539847; -.
DR KEGG; spo:SPBC530.14c; -.
DR PomBase; SPBC530.14c; dsk1.
DR VEuPathDB; FungiDB:SPBC530.14c; -.
DR eggNOG; KOG1290; Eukaryota.
DR HOGENOM; CLU_000288_81_12_1; -.
DR InParanoid; P36616; -.
DR OMA; IEKYEWP; -.
DR PhylomeDB; P36616; -.
DR BRENDA; 2.7.11.1; 5613.
DR PRO; PR:P36616; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0032153; C:cell division site; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; IDA:PomBase.
DR GO; GO:0044732; C:mitotic spindle pole body; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; EXP:PomBase.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:PomBase.
DR GO; GO:0050265; F:RNA uridylyltransferase activity; IDA:PomBase.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IGI:CACAO.
DR GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IMP:PomBase.
DR GO; GO:0046827; P:positive regulation of protein export from nucleus; IMP:PomBase.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; IMP:PomBase.
DR GO; GO:0007088; P:regulation of mitotic nuclear division; IMP:PomBase.
DR GO; GO:0050684; P:regulation of mRNA processing; IBA:GO_Central.
DR GO; GO:0000245; P:spliceosomal complex assembly; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell cycle; Cell division; Cytoplasm; Kinase; Mitosis;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..544
FT /note="Protein kinase dsk1"
FT /id="PRO_0000085927"
FT DOMAIN 81..516
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 235..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 214
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 87..95
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 110
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 41
FT /note="A -> S (in Ref. 1; BAA02706)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 544 AA; 61056 MW; D78B9ABD82B073EE CRC64;
MGSDGSSLSP KVSQPGHTEI VDHVSEKVIT NGKNVNKKVN AEVDGKSMVE KVKTHEENAE
DYHYGGYHPV YIGEEFHHRR YVVERKLGWG HFSTVWLAYD RAAKRRVALK VVRSAEHYRE
TSIDEIRILQ KIREGDEKHL GKKHIISLLD YFVHRGPNGA HVCMVFEVLG ENLLSLIQSY
GHRGVPVGIV KQIAYQLLIA LDYLHRECGI IHTDLKPENV LICIDQDALQ HIEAPATTSS
PTSNTSSSKT RNNTGYTAKA PIIKRGQSVD NSAQERKTFA KNPTKNSKPA GQVIPSSPFT
STLSRFPSLE GAVSEISLRD SQKHNSHPNS PFSSGDNSLI LDGVNGSQEP VPKITVKIAD
LGNACWTRKH FTNDVQTRQY RSPEVILGCR WGASADCWSF ACIIFELLTG DYLFDPRNGN
SYSKEDDHIA QIIELLVNYP KQMALSGKHS RDLFNRRGEL RNIHKLKFWP LKDVLEQKYH
FSAELAQQIS DFLSPMLCFD PAKRTNAGYM SNSPWLREVA DPTFKIETTG ATGEDVPGWA
TEIR
