KNS1_YEAST
ID KNS1_YEAST Reviewed; 737 AA.
AC P32350; D6VXY4; Q12399;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2002, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Dual specificity protein kinase KNS1;
DE EC=2.7.12.1;
GN Name=KNS1; OrderedLocusNames=YLL019C;
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].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1910150; DOI=10.1007/bf00264206;
RA Padmanabha R., Gehrung S., Snyder M.;
RT "The KNS1 gene of Saccharomyces cerevisiae encodes a nonessential protein
RT kinase homologue that is distantly related to members of the CDC28/cdc2
RT gene family.";
RL Mol. Gen. Genet. 229:1-9(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9046100;
RX DOI=10.1002/(sici)1097-0061(199702)13:2<183::aid-yea65>3.0.co;2-v;
RA Purnelle B., Goffeau A.;
RT "The sequence of 32kb on the left arm of yeast chromosome XII reveals six
RT known genes, a new member of the seripauperins family and a new ABC
RT transporter homologous to the human multidrug resistance protein.";
RL Yeast 13:183-188(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
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 FUNCTION.
RX PubMed=8910305; DOI=10.1074/jbc.271.44.27299;
RA Lee K., Du C., Horn M., Rabinow L.;
RT "Activity and autophosphorylation of LAMMER protein kinases.";
RL J. Biol. Chem. 271:27299-27303(1996).
RN [6]
RP AUTOPHOSPHORYLATION.
RX PubMed=11741326; DOI=10.1006/bbrc.2001.6128;
RA Kim K.-H., Cho Y.-M., Kang W.-H., Kim J.-H., Byun K.-H., Park Y.-D.,
RA Bae K.-S., Park H.-M.;
RT "Negative regulation of filamentous growth and flocculation by Lkh1, a
RT fission yeast LAMMER kinase homolog.";
RL Biochem. Biophys. Res. Commun. 289:1237-1242(2001).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-562, AND IDENTIFICATION BY
RP 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 [8]
RP IDENTIFICATION BY MASS 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: Nonessential protein kinase. {ECO:0000269|PubMed:8910305}.
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=2.7.12.1;
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=2.7.12.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.1;
CC -!- PTM: Phosphorylated (auto-) on Ser/Thr/Tyr.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. Lammer subfamily. {ECO:0000305}.
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DR EMBL; M85200; AAA34724.1; -; Genomic_DNA.
DR EMBL; Z73125; CAA97468.1; -; Genomic_DNA.
DR EMBL; X97560; CAA66171.1; -; Genomic_DNA.
DR EMBL; Z73123; CAA97465.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09300.1; -; Genomic_DNA.
DR PIR; S64767; S64767.
DR RefSeq; NP_013081.1; NM_001181839.1.
DR AlphaFoldDB; P32350; -.
DR SMR; P32350; -.
DR BioGRID; 31233; 240.
DR DIP; DIP-1900N; -.
DR IntAct; P32350; 39.
DR MINT; P32350; -.
DR STRING; 4932.YLL019C; -.
DR iPTMnet; P32350; -.
DR PaxDb; P32350; -.
DR PRIDE; P32350; -.
DR TopDownProteomics; P32350; -.
DR EnsemblFungi; YLL019C_mRNA; YLL019C; YLL019C.
DR GeneID; 850641; -.
DR KEGG; sce:YLL019C; -.
DR SGD; S000003942; KNS1.
DR VEuPathDB; FungiDB:YLL019C; -.
DR eggNOG; KOG0671; Eukaryota.
DR GeneTree; ENSGT00960000189195; -.
DR HOGENOM; CLU_000288_5_8_1; -.
DR InParanoid; P32350; -.
DR OMA; FANRFII; -.
DR BioCyc; YEAST:G3O-32124-MON; -.
DR BRENDA; 2.7.12.1; 984.
DR PRO; PR:P32350; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P32350; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; HDA:SGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:SGD.
DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IDA:SGD.
DR GO; GO:0016480; P:negative regulation of transcription by RNA polymerase III; IDA:SGD.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0043484; P:regulation of RNA splicing; IBA:GO_Central.
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; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Tyrosine-protein kinase.
FT CHAIN 1..737
FT /note="Dual specificity protein kinase KNS1"
FT /id="PRO_0000086155"
FT DOMAIN 313..720
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 440
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 319..327
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 343
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 562
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CONFLICT 411..421
FT /note="RFPGSHIQAIA -> GSPALISGHC (in Ref. 1; AAA34724)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 737 AA; 83843 MW; F0224445BDEE8431 CRC64;
MSQNIQIGTR KRSRANMNNS TTTGPANNTS SNKTFLDNFE ETRTNKLLDE MFARQNSFLT
DNLRNSLDLN QADNPLRPRQ HQHQLFLDNE NAIELDEEPR IINTTINNSN NHNSSRVDED
ADDDIIFIKE QPIQFSSPLI LPSSSSINNN NNIVTSNNPG CGTAATSNST YITTPKKFKK
QRTISLPQLP LSKLSYQSNY FNVPDQTNAI VPRVTQTENE LLHLTGSCAK TLEGNKAVNL
TIAHSTSPFS NPPAQIASLP QSNLKKQIGS SLRKFTSNGS SESASSNKSN FKTDKDGHYV
YQENDIFGSG GRFVVKDLLG QGTFGKVLKC IDNKYEPNYV AVKVIRAVDR YREAAKTELR
ILQTILNNDP QGQFQCLLLR ECFDYKNHIC LVTDLYGRSI YDFMCSNGIA RFPGSHIQAI
ARQLIRSVCF LHDLGIIHTD LKPENILICD ETHIAQKLPL KTVQSLSKRR REASKGKRKI
LKNPEIKIID FGSAIFHYEY HPPVISTRHY RAPEIVLGLG WSFPCDIWSI ACVLVELVIG
ESLYPIHENL EHMAMMQRIN GTPFPTDIID KMFYKSKHKL GNSPSDLNST VIKHFDRKTL
SLQWPEKNKR GDTITTEKSM KRVLQSCDRL DIYISKVLKQ DYGDSLSINW NLPPEKNWSL
INSKLAWKRQ THSSSSSTTD ELDKETFLFW YWFIDLLRKM FEFDPTKRIT AKDALDHEWF
NLGILDDGIA TYNNTQG
