NNK1_YEAST
ID NNK1_YEAST Reviewed; 928 AA.
AC P36003; D6VX29;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Nitrogen network kinase 1;
DE EC=2.7.11.1;
GN Name=NNK1; OrderedLocusNames=YKL171W; ORFNames=YKL635;
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=8091858; DOI=10.1002/yea.320100004;
RA Vandenbol M., Bolle P.-A., Dion C., Portetelle D., Hilger F.;
RT "Sequencing and analysis of a 20.5 kb DNA segment located on the left arm
RT of yeast chromosome XI.";
RL Yeast 10:S25-S33(1994).
RN [2]
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 [3]
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 [4]
RP SUBCELLULAR LOCATION.
RX PubMed=11914276; DOI=10.1101/gad.970902;
RA Kumar A., Agarwal S., Heyman J.A., Matson S., Heidtman M., Piccirillo S.,
RA Umansky L., Drawid A., Jansen R., Liu Y., Cheung K.-H., Miller P.,
RA Gerstein M., Roeder G.S., Snyder M.;
RT "Subcellular localization of the yeast proteome.";
RL Genes Dev. 16:707-719(2002).
RN [5]
RP PREDICTION OF FUNCTION.
RX PubMed=17557329; DOI=10.1002/prot.21444;
RA Miranda-Saavedra D., Barton G.J.;
RT "Classification and functional annotation of eukaryotic protein kinases.";
RL Proteins 68:893-914(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-737 AND TYR-739, AND
RP 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178; SER-179; SER-405;
RP SER-426; SER-737 AND TYR-739, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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).
RN [8]
RP FUNCTION, AND INTERACTION WITH URE2; GDH2 AND THE TORC1 COMPLEX.
RX PubMed=20489023; DOI=10.1126/science.1176495;
RA Breitkreutz A., Choi H., Sharom J.R., Boucher L., Neduva V., Larsen B.,
RA Lin Z.Y., Breitkreutz B.J., Stark C., Liu G., Ahn J., Dewar-Darch D.,
RA Reguly T., Tang X., Almeida R., Qin Z.S., Pawson T., Gingras A.C.,
RA Nesvizhskii A.I., Tyers M.;
RT "A global protein kinase and phosphatase interaction network in yeast.";
RL Science 328:1043-1046(2010).
CC -!- FUNCTION: Serine/threonine-protein kinase involved in the
CC phosphorylation of the NAD(+)-dependent glutamate dehydrogenase GDH2.
CC When overexpressed, confers hypersensitivity to rapamycin and induces
CC rapid nuclear accumulation of GLN3 to activate the transcription of
CC nitrogen-regulated genes. {ECO:0000269|PubMed:20489023}.
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 -!- SUBUNIT: Interacts with URE2 and GDH2. Interacts also with the TORC1
CC kinase complex. {ECO:0000269|PubMed:20489023}.
CC -!- INTERACTION:
CC P36003; P33327: GDH2; NbExp=3; IntAct=EBI-9796, EBI-5815;
CC P36003; P29295: HRR25; NbExp=4; IntAct=EBI-9796, EBI-8536;
CC P36003; P35169: TOR1; NbExp=3; IntAct=EBI-9796, EBI-19374;
CC P36003; P23202: URE2; NbExp=4; IntAct=EBI-9796, EBI-20138;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11914276}.
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; Z26878; CAA81516.1; -; Genomic_DNA.
DR EMBL; Z28171; CAA82013.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA08995.1; -; Genomic_DNA.
DR PIR; S38001; S38001.
DR RefSeq; NP_012750.1; NM_001179737.1.
DR AlphaFoldDB; P36003; -.
DR BioGRID; 33967; 221.
DR DIP; DIP-2877N; -.
DR IntAct; P36003; 21.
DR MINT; P36003; -.
DR STRING; 4932.YKL171W; -.
DR iPTMnet; P36003; -.
DR MaxQB; P36003; -.
DR PaxDb; P36003; -.
DR PRIDE; P36003; -.
DR EnsemblFungi; YKL171W_mRNA; YKL171W; YKL171W.
DR GeneID; 853683; -.
DR KEGG; sce:YKL171W; -.
DR SGD; S000001654; NNK1.
DR VEuPathDB; FungiDB:YKL171W; -.
DR eggNOG; KOG0032; Eukaryota.
DR GeneTree; ENSGT00940000162886; -.
DR HOGENOM; CLU_010370_0_0_1; -.
DR InParanoid; P36003; -.
DR OMA; YAMYCLT; -.
DR BioCyc; YEAST:G3O-31938-MON; -.
DR Reactome; R-SCE-171007; p38MAPK events.
DR Reactome; R-SCE-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-SCE-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-SCE-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-SCE-450302; activated TAK1 mediates p38 MAPK activation.
DR Reactome; R-SCE-450385; Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
DR Reactome; R-SCE-450513; Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA.
DR Reactome; R-SCE-5687128; MAPK6/MAPK4 signaling.
DR PRO; PR:P36003; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36003; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0009931; F:calcium-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
DR GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IBA:GO_Central.
DR GO; GO:0004672; F:protein kinase activity; HDA:SGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0046777; P:protein autophosphorylation; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; HDA:SGD.
DR GO; GO:0006508; P:proteolysis; IMP:SGD.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR016241; Nnk1.
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 PIRSF; PIRSF000610; Ser/Thr_PK_YKL171w_prd; 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; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..928
FT /note="Nitrogen network kinase 1"
FT /id="PRO_0000086152"
FT DOMAIN 449..912
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 81..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 670..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 767..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..717
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 580
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 455..463
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 478
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 405
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 426
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 737
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 739
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
SQ SEQUENCE 928 AA; 103956 MW; 00EB03553EC5999A CRC64;
MFTSQRQLRQ NGSPMSSSRS SQHSSGTASP ISDSPASNRS YGRDLRGLMG IDIPANEPAF
NRANSSDTIY FRPKKIYKME HEHPSRSTLV QLQTRSQPDD VASSQVNPEG GTDDLELGDP
CGNQSLYTIG AEYVPDLDFT KLVNEWQKST EDLYEFRSSA TPQVQIKDSG KGNYELWSSP
DAILTQNKLR RDSFSQENSD SLSPEDSILS RNLHSKVKPI PLPRNSQQIF TPLSNLEAER
RSSYTTSSNN NSITQNNKFS FAKLKYSLPT QSSAVPASFD SNASSLNFLP TTTLSTLSEL
QISPNDMMDL IQKLPRNFLN LPYTQRKKVI IEHAPSHDYK AMMSLVKKFM LTSSRSNFSL
AGFANNASVS QATANDDNIN SRNTPNNSND TYVNTRPLQR SRHGSIASQF LSSFSPSMTS
IAKMNSNPLS GSAGGSARPD DKGMEILGHR LGKIIGFGAW GIIRECFDIE TGVGRVIKIV
KFKGHQNIKK HVLREVAIWR TLKHNRILPL LDWKLDDNYA MYCLTERIND GTLYDLVISW
DEFKRSKIPF AERCRLTIFL SLQLLSALKY MHSKTIVHGD IKLENCLLQK EGKKSDWKVF
LCDFGMSCHF DEKHVYRNDT FDENLSSGNS HRKRKSIEQT NLIKYPTTNF LPDDRTNDFD
ASENLKYQFE NRKHQPFTPK GMVSSSSHSL KHLNQPSSSS SSNLFHKPAS QPQPQHRSPF
HGRHKTTDFS NLEPEPSKYI GSLPYASPEL LRYSDARRSK SVEMHIYDSP DSSQSEISAA
SSSSSNLSSL SSSTKASAVT NSGVTTSSPS GSSTDFPCIV SPLGPASDIW ALGVMLYTML
VGKLPFNHEF EPRLRSLIKV GEFDRFSLAQ VCKFDRKKNE GTIGQGLYDT VIGCLTIDLD
KRWKLKRIEE VLQNEMNLSE AIHDNNGS
