PTK1_YEAST
ID PTK1_YEAST Reviewed; 662 AA.
AC P36002; D6VX02; P36045; Q06941;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 3.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Serine/threonine-protein kinase PTK1/STK1;
DE EC=2.7.11.1;
GN Name=PTK1; Synonyms=POT1, STK1; OrderedLocusNames=YKL198C;
GN ORFNames=YKL199C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 241-244; 300; 356-375 AND
RP 637-662.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-584, AND CHARACTERIZATION.
RX PubMed=7488221; DOI=10.1006/bbrc.1995.2717;
RA Kakinuma Y., Maruyama T., Nozaki T., Wada Y., Ohsumi Y., Igarashi K.;
RT "Cloning of the gene encoding a putative serine/threonine protein kinase
RT which enhances spermine uptake in Saccharomyces cerevisiae.";
RL Biochem. Biophys. Res. Commun. 216:985-992(1995).
RN [4]
RP CHARACTERIZATION.
RX PubMed=9154797; DOI=10.1128/mcb.17.6.2994;
RA Kaouass M., Audette M., Ramotar D., Verma S., de Montigny D., Gamache I.,
RA Torossian K., Poulin R.;
RT "The STK2 gene, which encodes a putative Ser/Thr protein kinase, is
RT required for high-affinity spermidine transport in Saccharomyces
RT cerevisiae.";
RL Mol. Cell. Biol. 17:2994-3004(1997).
CC -!- FUNCTION: Essential determinant for low-affinity spermidine transport.
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. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA09884.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA82042.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA82043.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Z28198; CAA82043.1; ALT_FRAME; Genomic_DNA.
DR EMBL; Z28198; CAA82042.1; ALT_FRAME; Genomic_DNA.
DR EMBL; D63815; BAA09884.1; ALT_FRAME; Genomic_DNA.
DR EMBL; BK006944; DAA08968.2; -; Genomic_DNA.
DR PIR; S38035; S38035.
DR PIR; S38036; S38036.
DR RefSeq; NP_012723.3; NM_001179764.2.
DR AlphaFoldDB; P36002; -.
DR SMR; P36002; -.
DR BioGRID; 33922; 102.
DR IntAct; P36002; 15.
DR MINT; P36002; -.
DR STRING; 4932.YKL198C; -.
DR iPTMnet; P36002; -.
DR MaxQB; P36002; -.
DR PaxDb; P36002; -.
DR PRIDE; P36002; -.
DR EnsemblFungi; YKL198C_mRNA; YKL198C; YKL198C.
DR GeneID; 853635; -.
DR KEGG; sce:YKL198C; -.
DR SGD; S000001681; PTK1.
DR VEuPathDB; FungiDB:YKL198C; -.
DR eggNOG; KOG0583; Eukaryota.
DR GeneTree; ENSGT00940000176810; -.
DR HOGENOM; CLU_009275_2_0_1; -.
DR InParanoid; P36002; -.
DR OMA; AYENFIR; -.
DR BioCyc; YEAST:G3O-31960-MON; -.
DR BRENDA; 2.7.11.1; 984.
DR Reactome; R-SCE-1632852; Macroautophagy.
DR Reactome; R-SCE-176187; Activation of ATR in response to replication stress.
DR Reactome; R-SCE-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
DR Reactome; R-SCE-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
DR Reactome; R-SCE-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR PRO; PR:P36002; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36002; protein.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; ISA:SGD.
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:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0000296; P:spermine transport; IGI:SGD.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..662
FT /note="Serine/threonine-protein kinase PTK1/STK1"
FT /id="PRO_0000086589"
FT DOMAIN 196..503
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 35..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 605..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 329
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 202..210
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 226
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 241..244
FT /note="KRCS -> NAAP (in Ref. 1; CAA82043)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="S -> H (in Ref. 1; CAA82043)"
FT /evidence="ECO:0000305"
FT CONFLICT 356..375
FT /note="TDPHDLSSPVKKCAGMIGSP -> HGSTRPVQPCQEVRRDDRLA (in
FT Ref. 1; CAA82043)"
FT /evidence="ECO:0000305"
FT CONFLICT 637..662
FT /note="VHHHLNIVNSLVHSSSAASSQVPAST -> GASPSEHCQQLGP (in Ref.
FT 1; CAA82042)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 662 AA; 73502 MW; 78952B1828D47048 CRC64;
MTVSHNHSTK ISQQPISSVS AFKFFGKKLL SSSHGNKLKK KASLPPDFHS TSTNDSESSS
PKLPNSLKTS RRANSFAHTT NSKRSLSSAS TKILPPAGSS TSISRGNRHS STSRNLSNSK
FSSERLVYNP YGVSTPSTSL SSVSTSMKKD PDLGFYLHDG DSKIRMLPIP IVDPNEYLPD
EMKEASIQLS DNFVFDDENK TIGWGGSCEV RKIRSKYRKK DVFALKKLNM IYNETPEKFY
KRCSKEFIIA KQLSHHVHIT NTFLLVKVPT TVYTTRGWGF VMELGLRDLF AMIQKSGWRS
VALAEKFCIF KQVACGVKFC HDQGIAHRDL KPENVLLSPD GVCKLTDFGI SDWYHTDPHD
LSSPVKKCAG MIGSPPYAPP EVMFYDSKKH YDTELQQPYD PRALDCYGLG IILMTLVNNV
IPFLESCSFD TGFRDYCDAY ENFIRLHDRA FRNRGNYRPG PGMEYHLARN FKNGHASRVA
WRLADPEAAT RYTIDDLFED PWFQGIETCV DANDKYVCKK PIIKTTTYEN PRGFHIATDV
AATTPTSNPF LKNRVPIRSM VDIAAHPSPT ATVLASSPPP PPPATHVPAE ALFTLRETPP
PQLATLTLSE EPPATPAPSA PSAPSARVRG HSPHRVVHHH LNIVNSLVHS SSAASSQVPA
ST
