SCK2_SCHPO
ID SCK2_SCHPO Reviewed; 646 AA.
AC Q10364;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Serine/threonine-protein kinase sck2;
DE EC=2.7.11.1;
GN Name=sck2; ORFNames=SPAC22E12.14c;
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 [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 [2]
RP FUNCTION.
RX PubMed=9560431; DOI=10.1007/s002940050333;
RA Fujita M., Yamamoto M.;
RT "S. pombe sck2+, a second homologue of S. cerevisiae SCH9 in fission yeast,
RT encodes a putative protein kinase closely related to PKA in function.";
RL Curr. Genet. 33:248-254(1998).
CC -!- FUNCTION: Protein kinase that is part of growth control pathway which
CC is at least partially redundant with the cAMP pathway.
CC {ECO:0000269|PubMed:9560431}.
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. PKC subfamily. {ECO:0000305}.
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DR EMBL; CU329670; CAA93901.1; -; Genomic_DNA.
DR PIR; T38171; T38171.
DR RefSeq; NP_594840.1; NM_001020269.2.
DR AlphaFoldDB; Q10364; -.
DR SMR; Q10364; -.
DR BioGRID; 278357; 206.
DR STRING; 4896.SPAC22E12.14c.1; -.
DR iPTMnet; Q10364; -.
DR MaxQB; Q10364; -.
DR PaxDb; Q10364; -.
DR PRIDE; Q10364; -.
DR EnsemblFungi; SPAC22E12.14c.1; SPAC22E12.14c.1:pep; SPAC22E12.14c.
DR GeneID; 2541867; -.
DR KEGG; spo:SPAC22E12.14c; -.
DR PomBase; SPAC22E12.14c; sck2.
DR VEuPathDB; FungiDB:SPAC22E12.14c; -.
DR eggNOG; KOG0598; Eukaryota.
DR HOGENOM; CLU_000288_52_3_1; -.
DR InParanoid; Q10364; -.
DR OMA; HEPSGYL; -.
DR PhylomeDB; Q10364; -.
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:Q10364; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005635; C:nuclear envelope; HDA:PomBase.
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; IMP:PomBase.
DR GO; GO:0035556; P:intracellular signal transduction; IGI:PomBase.
DR GO; GO:0031138; P:negative regulation of conjugation with cellular fusion; IGI:PomBase.
DR GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; IMP:PomBase.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0038202; P:TORC1 signaling; IPI:PomBase.
DR InterPro; IPR000961; AGC-kinase_C.
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; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 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; 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; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..646
FT /note="Serine/threonine-protein kinase sck2"
FT /id="PRO_0000086640"
FT DOMAIN 266..527
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 528..605
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 17..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..623
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 392
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 272..280
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 295
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 646 AA; 71899 MW; 4F37BF7F1D8C56FF CRC64;
MMNKWAKNWF GLSKKSVSTN SAKGSLPRSP LASIQTNQPV EEGEGGSLPS VSNLGPSSID
HPMEEFASDQ STVGNRNSND ILPEVDHEPS GYLKLQIGSL VLGGPHTDAA LAMECSRLNQ
LFVVVQFGTT EFVSPPLKWE SPGRDIGTSS RDSANVSRSS SMMSSHPIPT PAIQRTSSIP
NPLTPSYVVF DVAKPVPIDV NIYDHGNNNE FVGRTYIHPS YNYGQFEQFC NSVEVSPAYN
RMVDLRLSLN TVFQPLSQHS YGPDDFVPLK LIGKGTFGQV YLVRKKDTER VYAMKVLSKK
VIVRRKEVAH TVGERDILVQ TSAADSPFIV ALRFSFQTPK DLYLVTDYMA GGELFWHLQK
SVRFPEERAK FYIAELLLAL QALHKRGIVY RDLKPENILL DVQGHIALCD FGLSKANLSV
GTTTRTFCGT TDYLAPEVIL DEAGYDMMVD FWSLGVLLYE MTCGWSPFYA DNTQQLYKNI
VFGKVRFPRG LLSVEARDLI KLLLNRNPKH RLGAHGDVEE VMKHPFFDGI DWKKLAAKEI
SPPFKPIVEG EIDVSNFDVE FTNKAIDRDF SSTDEMSTSA PLSSTVQNGF KGFTYIDASA
MDEAFGYHNS NDSASSISSQ DDYSKDNSDM DLNRANDEVF MGQIDP
