ID   PSK1_SCHPO              Reviewed;         436 AA.
AC   Q12706; O00044;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 157.
DE   RecName: Full=Serine/threonine-protein kinase psk1 {ECO:0000303|PubMed:8529881};
DE            EC=2.7.11.1 {ECO:0000269|PubMed:22976295};
DE   AltName: Full=Ribosomal S6 kinase homolog psk1 {ECO:0000305|PubMed:22976295};
DE            Short=S6K homolog psk1;
GN   Name=psk1 {ECO:0000303|PubMed:8529881};
GN   ORFNames=SPCC4G3.08 {ECO:0000312|PomBase:SPCC4G3.08};
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].
RX   PubMed=8529881; DOI=10.1016/0378-1119(95)00553-1;
RA   Mukai H., Miyahara M., Takanaga H., Kitagawa M., Shibata H., Shimakawa M.,
RA   Ono Y.;
RT   "Identification of Schizosaccharomyces pombe gene psk1+, encoding a novel
RT   putative serine/threonine protein kinase, whose mutation conferred
RT   resistance to phenylarsine oxide.";
RL   Gene 166:155-159(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   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   FUNCTION, CATALYTIC ACTIVITY, AND PHOSPHORYLATION AT SER-248; THR-392 AND
RP   THR-415.
RX   PubMed=22976295; DOI=10.1242/jcs.111146;
RA   Nakashima A., Otsubo Y., Yamashita A., Sato T., Yamamoto M., Tamanoi F.;
RT   "Psk1, an AGC kinase family member in fission yeast, is directly
RT   phosphorylated and controlled by TORC1 and functions as S6 kinase.";
RL   J. Cell Sci. 125:5840-5849(2012).
CC   -!- FUNCTION: AGC kinase which plays a role in TOR complex 1 (TORC1)
CC       signaling pathway which mediates temporal control of cell growth in
CC       response to nutrients. Required for phosphorylation of ribosomal
CC       protein S6 (rps601/rps602) at 'Ser-235' and 'Ser-236'.
CC       {ECO:0000269|PubMed:22976295}.
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         Evidence={ECO:0000269|PubMed:22976295};
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; Evidence={ECO:0000269|PubMed:22976295};
CC   -!- ACTIVITY REGULATION: Phosphorylation at Tyr-102 inactivates the enzyme.
CC       {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC   -!- PTM: Phosphorylated by ksg1 and target of rapamycin complex 1 (TORC1),
CC       affecting the kinase activity of psk1 in a nutrient-dependent manner.
CC       {ECO:0000269|PubMed:22976295}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. S6 kinase subfamily. {ECO:0000305}.
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DR   EMBL; D45401; BAA08243.1; -; Genomic_DNA.
DR   EMBL; CU329672; CAB09775.1; -; Genomic_DNA.
DR   PIR; JC4516; JC4516.
DR   RefSeq; NP_587830.1; NM_001022823.2.
DR   AlphaFoldDB; Q12706; -.
DR   SMR; Q12706; -.
DR   BioGRID; 276057; 21.
DR   STRING; 284812.Q12706; -.
DR   iPTMnet; Q12706; -.
DR   MaxQB; Q12706; -.
DR   PaxDb; 4896-SPCC4G3-08-1; -.
DR   EnsemblFungi; SPCC4G3.08.1; SPCC4G3.08.1:pep; SPCC4G3.08.
DR   GeneID; 2539494; -.
DR   KEGG; spo:SPCC4G3.08; -.
DR   PomBase; SPCC4G3.08; psk1.
DR   VEuPathDB; FungiDB:SPCC4G3.08; -.
DR   eggNOG; KOG0598; Eukaryota.
DR   HOGENOM; CLU_000288_63_5_1; -.
DR   InParanoid; Q12706; -.
DR   OMA; CWTAMPP; -.
DR   PhylomeDB; Q12706; -.
DR   Reactome; R-SPO-166208; mTORC1-mediated signalling.
DR   Reactome; R-SPO-198693; AKT phosphorylates targets in the nucleus.
DR   Reactome; R-SPO-198753; ERK/MAPK targets.
DR   Reactome; R-SPO-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR   Reactome; R-SPO-375165; NCAM signaling for neurite out-growth.
DR   Reactome; R-SPO-444257; RSK activation.
DR   Reactome; R-SPO-881907; Gastrin-CREB signalling pathway via PKC and MAPK.
DR   PRO; PR:Q12706; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004711; F:ribosomal protein S6 kinase activity; IDA:PomBase.
DR   GO; GO:0035591; F:signaling adaptor activity; EXP:PomBase.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:2000767; P:positive regulation of cytoplasmic translation; EXP:PomBase.
DR   GO; GO:0038202; P:TORC1 signaling; IPI:PomBase.
DR   CDD; cd05123; STKc_AGC; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR045270; STKc_AGC.
DR   PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR   PANTHER; PTHR24351:SF243; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..436
FT                   /note="Serine/threonine-protein kinase psk1"
FT                   /id="PRO_0000086588"
FT   DOMAIN          91..350
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          351..426
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT   ACT_SITE        215
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         97..105
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         120
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         102
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         248
FT                   /note="Phosphoserine; by ksg1"
FT                   /evidence="ECO:0000269|PubMed:22976295"
FT   MOD_RES         392
FT                   /note="Phosphothreonine; by TORC1"
FT                   /evidence="ECO:0000269|PubMed:22976295"
FT   MOD_RES         415
FT                   /note="Phosphothreonine; by TORC1"
FT                   /evidence="ECO:0000269|PubMed:22976295"
SQ   SEQUENCE   436 AA;  49321 MW;  3498C4BE214530BC CRC64;
     MPVFMFDEHD NLNENYNSHL SSDDEIAEEG YDFEELEASA STITSSSDLK DGKNAKDEKG
     TVEFKVAAHG DFISSKGDNY VPSGKMRPAD FQPLTVLGRG SYGKVLLVKQ KNTGRLFAQK
     QLKKASIVLR AKGLEQTKNE RQILEEVRHP FICRLYYAFQ DHDRLYLILQ YAPGGELFSH
     LAEQRMLPED VVAFYTAELT LALIHLHKLG IVYRDLKPEN CLLDAEGHIL LTDFGLSKVA
     ENGADCRSFV GTEEYCAPEI LLEQPYDHAV DWWSMGILIF DLLTGSPPFT ANNHKRIMEK
     ITRAKPNIPF YVTSDARDII NKFLKKNPKQ RLGADGPEKG YDAIKKHRIY RRIDWNKLEK
     RMLPPPIVPC ITNPEAAENF SVEFTKLPLS TTPILHEEFG NLTIGSHSSA FQGFTYVASP
     NFLNCEFLSN NAVSNH
//