SCK1_SCHPO
ID SCK1_SCHPO Reviewed; 696 AA.
AC P50530; Q9UTF3;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Serine/threonine-protein kinase sck1;
DE EC=2.7.11.1;
GN Name=sck1; ORFNames=SPAC1B9.02c;
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=7498728; DOI=10.1093/genetics/140.2.457;
RA Jin M., Fujita M., Culley B., Apolinario E., Yamamoto M., Maundrell K.,
RA Hoffman C.;
RT "sck1, a high copy number suppressor of defects in the cAMP-dependent
RT protein kinase pathway in fission yeast, encodes a protein homologous to
RT the Saccharomyces cerevisiae SCH9 kinase.";
RL Genetics 140:457-467(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 FUNCTION.
RX PubMed=9245826; DOI=10.1099/00221287-143-7-2457;
RA Soto T., Fernandez J., Cansado J., Vicente-Soler J., Gacto M.;
RT "Protein kinase Sck1 is involved in trehalase activation by glucose and
RT nitrogen source in the fission yeast Schizosaccharomyces pombe.";
RL Microbiology 143:2457-2463(1997).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-632 AND SER-665, AND
RP 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: Protein kinase that is part of growth control pathway which
CC is at least partially redundant with the cAMP pathway. Required for
CC trehalase activation. {ECO:0000269|PubMed:9245826}.
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 -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. cAMP subfamily. {ECO:0000305}.
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DR EMBL; D38108; BAA07286.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB53053.1; -; Genomic_DNA.
DR PIR; S55694; S55694.
DR RefSeq; NP_593754.1; NM_001019184.2.
DR AlphaFoldDB; P50530; -.
DR SMR; P50530; -.
DR BioGRID; 278951; 29.
DR IntAct; P50530; 1.
DR STRING; 4896.SPAC1B9.02c.1; -.
DR iPTMnet; P50530; -.
DR MaxQB; P50530; -.
DR PaxDb; P50530; -.
DR PRIDE; P50530; -.
DR EnsemblFungi; SPAC1B9.02c.1; SPAC1B9.02c.1:pep; SPAC1B9.02c.
DR GeneID; 2542492; -.
DR KEGG; spo:SPAC1B9.02c; -.
DR PomBase; SPAC1B9.02c; sck1.
DR VEuPathDB; FungiDB:SPAC1B9.02c; -.
DR eggNOG; KOG0598; Eukaryota.
DR HOGENOM; CLU_000288_52_2_1; -.
DR InParanoid; P50530; -.
DR OMA; SYAMGTT; -.
DR PhylomeDB; P50530; -.
DR BRENDA; 2.7.11.1; 5613.
DR Reactome; R-SPO-1257604; PIP3 activates AKT signaling.
DR Reactome; R-SPO-1358803; Downregulation of ERBB2:ERBB3 signaling.
DR Reactome; R-SPO-1474151; Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
DR Reactome; R-SPO-165158; Activation of AKT2.
DR Reactome; R-SPO-165181; Inhibition of TSC complex formation by PKB.
DR Reactome; R-SPO-198323; AKT phosphorylates targets in the cytosol.
DR Reactome; R-SPO-198693; AKT phosphorylates targets in the nucleus.
DR Reactome; R-SPO-203615; eNOS activation.
DR Reactome; R-SPO-389357; CD28 dependent PI3K/Akt signaling.
DR Reactome; R-SPO-389513; CTLA4 inhibitory signaling.
DR Reactome; R-SPO-392451; G beta:gamma signalling through PI3Kgamma.
DR Reactome; R-SPO-450385; Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
DR Reactome; R-SPO-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-SPO-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-SPO-6804757; Regulation of TP53 Degradation.
DR Reactome; R-SPO-6804758; Regulation of TP53 Activity through Acetylation.
DR Reactome; R-SPO-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-SPO-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-SPO-9009391; Extra-nuclear estrogen signaling.
DR PRO; PR:P50530; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IC:PomBase.
DR GO; GO:0008289; F:lipid binding; ISM:PomBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IMP:PomBase.
DR GO; GO:0035556; P:intracellular signal transduction; IGI:PomBase.
DR GO; GO:0110034; P:negative regulation of adenylate cyclase-activating glucose-activated G protein-coupled receptor signaling pathway; IGI:PomBase.
DR GO; GO:0031138; P:negative regulation of conjugation with cellular fusion; IGI:PomBase.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:1903379; P:regulation of mitotic chromosome condensation; IGI:PomBase.
DR GO; GO:0038202; P:TORC1 signaling; IPI:PomBase.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; cAMP; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..696
FT /note="Serine/threonine-protein kinase sck1"
FT /id="PRO_0000086639"
FT DOMAIN 122..272
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 302..563
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 564..643
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 77..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 428
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 308..316
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 331
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 632
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 665
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 199
FT /note="A -> R (in Ref. 1; BAA07286)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 696 AA; 78595 MW; A7B05F5EE4D42AF7 CRC64;
MTEIFGKLHR SSNSENTNQA SPSTIQSHST QPVLSNDHST KVNDYEGKEG ASSNGYDPVF
MSDRMKMRYN EITAQLHKEQ SLKEDKESGS NSSESNGITP MGTYSEKPKL LQSRTPPSSC
YIRHDTVVPK DKNGQHAFGR LYVRLHQGRD LNVKSVNAQP YAVITFEKTQ VMVPPPFKDI
DGGIPISIPS KNRPLAGSAS GSSSGLHSEL MLADVRCPHW DFETVFDVTK MKSQMVVSVY
DKYEDDKFLG SVKITPIFLH EYVQEAWYKL EPLDLTKSLE GEIKVETIYE HIEHVRYGPE
DFTALRLIGK GTFGQVYLVR KNDTNRIYAM KKISKKLIVR KKEVTHTLGE RNILVRTSLD
ESPFIVGLKF SFQTASDLYL ITDYMSGGEL FWHLQHEGRF PEQRAKFYIA ELVLALEHLH
KHDIIYRDLK PENILLDADG HIALCDFGLS KANLSANATT NTFCGTTEYL APEVLLEDKG
YTKQVDFWSL GVLVFEMCCG WSPFYAPDVQ QMYRNIAFGK VRFPKGVLSS EGRSFVRGLL
NRNPNHRLGA VADTTELKEH PFFADINWDL LSKKKVQPPF KPNVQNDLDV SNFDKEFTNT
NVKNINIVSN VDPANASTPL SNTIQDRFRG FTFVNKSIDE QFQNLGLQEN EETDNLHACR
TTTHSSVNSI NSHGNPRTVD ANDPVADTVF GETFEA
