PTK2_YEAST
ID PTK2_YEAST Reviewed; 818 AA.
AC P47116; D6VWN0; E9P962;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Serine/threonine-protein kinase PTK2/STK2;
DE EC=2.7.11.1;
GN Name=PTK2; Synonyms=STK2; OrderedLocusNames=YJR059W; ORFNames=J1725;
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 [GENOMIC DNA].
RX PubMed=8920934; DOI=10.1006/bbrc.1996.1681;
RA Nozaki T., Nishimura K., Michael A.J., Maruyama T., Kakinuma Y.,
RA Igarashi K.;
RT "A second gene encoding a putative serine/threonine protein kinase which
RT enhances spermine uptake in Saccharomyces cerevisiae.";
RL Biochem. Biophys. Res. Commun. 228:452-458(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8840504;
RX DOI=10.1002/(sici)1097-0061(199607)12:9<869::aid-yea964>3.0.co;2-1;
RA Huang M.-E., Manus V., Chuat J.-C., Galibert F.;
RT "Analysis of a 62 kb DNA sequence of chromosome X reveals 36 open reading
RT frames and a gene cluster with a counterpart on chromosome XI.";
RL Yeast 12:869-875(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [4]
RP GENOME REANNOTATION.
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP FUNCTION.
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).
RN [7]
RP FUNCTION.
RX PubMed=11003661; DOI=10.1128/mcb.20.20.7654-7661.2000;
RA Goossens A., de La Fuente N., Forment J., Serrano R., Portillo F.;
RT "Regulation of yeast H(+)-ATPase by protein kinases belonging to a family
RT dedicated to activation of plasma membrane transporters.";
RL Mol. Cell. Biol. 20:7654-7661(2000).
RN [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [9]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-56; SER-711; THR-737; SER-752
RP AND SER-755, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-623; SER-711; SER-778 AND
RP SER-781, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-56; SER-59; SER-623; SER-632;
RP SER-694; THR-700; SER-711; SER-752 AND SER-755, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Essential determinant for high-affinity spermidine transport.
CC Required for the activation of the plasma membrane proton pump PMA1 via
CC phosphorylation of 'Ser-899'. {ECO:0000269|PubMed:11003661,
CC ECO:0000269|PubMed:9154797}.
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}. Cytoplasm
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 1420 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; D87274; BAA13325.1; -; Genomic_DNA.
DR EMBL; Z49559; CAA89587.1; -; Genomic_DNA.
DR EMBL; L47993; AAB39285.1; -; Genomic_DNA.
DR EMBL; AY723837; AAU09754.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08846.1; -; Genomic_DNA.
DR PIR; S57078; S57078.
DR RefSeq; NP_012593.3; NM_001181717.3.
DR AlphaFoldDB; P47116; -.
DR SMR; P47116; -.
DR BioGRID; 33816; 717.
DR DIP; DIP-7167N; -.
DR IntAct; P47116; 11.
DR MINT; P47116; -.
DR STRING; 4932.YJR059W; -.
DR iPTMnet; P47116; -.
DR MaxQB; P47116; -.
DR PaxDb; P47116; -.
DR PRIDE; P47116; -.
DR TopDownProteomics; P47116; -.
DR EnsemblFungi; YJR059W_mRNA; YJR059W; YJR059W.
DR GeneID; 853522; -.
DR KEGG; sce:YJR059W; -.
DR SGD; S000003820; PTK2.
DR VEuPathDB; FungiDB:YJR059W; -.
DR eggNOG; KOG0583; Eukaryota.
DR GeneTree; ENSGT00940000176810; -.
DR HOGENOM; CLU_009275_1_1_1; -.
DR InParanoid; P47116; -.
DR OMA; IGSPPYT; -.
DR BioCyc; YEAST:G3O-31692-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:P47116; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47116; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA: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:0006873; P:cellular ion homeostasis; IMP:SGD.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IGI:SGD.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; HDA:SGD.
DR GO; GO:0015847; P:putrescine transport; IMP:SGD.
DR GO; GO:0008361; P:regulation of cell size; HMP:SGD.
DR GO; GO:0015848; P:spermidine transport; IMP:SGD.
DR GO; GO:0000296; P:spermine transport; IMP:SGD.
DR InterPro; IPR011009; Kinase-like_dom_sf.
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 SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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; Cytoplasm; Kinase; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..818
FT /note="Serine/threonine-protein kinase PTK2/STK2"
FT /id="PRO_0000086591"
FT DOMAIN 255..562
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 28..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 585..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..687
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..706
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 756..790
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 388
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 261..269
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 285
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 56
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 623
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 632
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 694
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 700
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 711
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 737
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 752
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 755
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 778
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 781
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CONFLICT 801
FT /note="D -> G (in Ref. 5; AAU09754)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 818 AA; 91400 MW; 55B6C882894FB4BD CRC64;
MAGNGKDKEV DKSPSVSTLK LLGKRLFNSS SHTDNSSLLL SAEQLGNGRS LRKRPTSPSI
SGSGSGGNSP SSSAGARQRS ASLHRRKNNA SVGFSNGSVS SHKSSVALQD LIKHNNNPYL
NSPSDILGTG TGIASTRDRD RAVLDREKEK ERARNKERNT HHAGLPQRSN SMASHHFPNE
NIVYNPYGIS PNHARPDTAF ADTLNTNKEN DLSFYMHDGN SKIRMLPLPI ANPNDFLPED
MKQYSVHLTD NFVFDTDNKP IGSGGSSEVR KVKSSYRQKD VYALKKLNMI YHESPEKFYK
RCSKEFIIAK HLSHNVHITN TFYLLKVPTT TYTTRGWGFI MELGVKDLFQ LMERTGWKNV
PFNEKYCLFK QVAQGIKFCH DNGIAHRDLK PENVLISKEG ICKLTDFGIS DWYHVIPHDY
TSPVKTCQGM IGSPPYTPPE VMYFDAKKHY PEKFQKPYNP LAMDSYALGI MLITMINNII
PFIDSCNTDA RFREFEVSYD NFINHQNPHF RDKGCHKPGP GSEYSLARNF KNTDATRIAW
RLADPNPATR YTMDDLFNDP FFQQIETCVE PNDDDLVRVP ELRKSTSTND FSENSLDAPH
DQEVIHTSNP FLKKETLTSK PRSMLEIAES PSLKQKSKVK DSAKTKTHDV GDEGGNESTK
PKQQDKKENL KKDEVKNGDK DKVIEEATTT NVDSILEKPT PTSTKVEDNL SEDDSTMKEL
KSMLNSTPTT PTHNGPTPLP AKAGTQLDKR MSDLSLKSET PASTKNFSAP NVSSSSNSLR
SLGSPSVSSS KKKKVIHHHL DITNSVTNMS SVSAFISR
