PSK1_SCHPO
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 03-AUG-2022, entry version 150.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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; 20.
DR STRING; 4896.SPCC4G3.08.1; -.
DR iPTMnet; Q12706; -.
DR MaxQB; Q12706; -.
DR PaxDb; Q12706; -.
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; KGSIFAM; -.
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-375165; NCAM signaling for neurite out-growth.
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:0005634; C:nucleus; 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:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
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:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:2000767; P:positive regulation of cytoplasmic translation; EXP:PomBase.
DR GO; GO:0031929; P:TOR signaling; IBA:GO_Central.
DR GO; GO:0038202; P:TORC1 signaling; IPI:PomBase.
DR CDD; cd05123; STKc_AGC; 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 Pfam; PF00069; Pkinase; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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
