ISR1_YEAST
ID ISR1_YEAST Reviewed; 443 AA.
AC Q06098; D6W4A4;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Serine/threonine-protein kinase ISR1;
DE EC=2.7.11.1;
DE AltName: Full=Inhibition of staurosporine resistance protein 1;
GN Name=ISR1; OrderedLocusNames=YPR106W;
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=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [2]
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 [3]
RP FUNCTION.
RX PubMed=9720220; DOI=10.1271/bbb.62.1376;
RA Miyahara K., Hirata D., Miyakawa T.;
RT "Functional interaction of Isr1, a predicted protein kinase, with the Pkc1
RT pathway in Saccharomyces cerevisiae.";
RL Biosci. Biotechnol. Biochem. 62:1376-1380(1998).
RN [4]
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).
CC -!- FUNCTION: Probable serine/threonine protein kinase which may function
CC redundantly with MPK1-independent branch of the PCK1 pathway that is
CC presumed to be required for the tolerance to high temperatures and
CC staurosporine. {ECO:0000269|PubMed:9720220}.
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 -!- MISCELLANEOUS: Present with 1590 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; U32445; AAB68076.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11520.1; -; Genomic_DNA.
DR PIR; S59771; S59771.
DR RefSeq; NP_015431.1; NM_001184203.1.
DR AlphaFoldDB; Q06098; -.
DR SMR; Q06098; -.
DR BioGRID; 36272; 152.
DR DIP; DIP-3818N; -.
DR IntAct; Q06098; 15.
DR MINT; Q06098; -.
DR STRING; 4932.YPR106W; -.
DR iPTMnet; Q06098; -.
DR PaxDb; Q06098; -.
DR PRIDE; Q06098; -.
DR EnsemblFungi; YPR106W_mRNA; YPR106W; YPR106W.
DR GeneID; 856221; -.
DR KEGG; sce:YPR106W; -.
DR SGD; S000006310; ISR1.
DR VEuPathDB; FungiDB:YPR106W; -.
DR eggNOG; ENOG502RW7G; Eukaryota.
DR HOGENOM; CLU_050275_0_0_1; -.
DR InParanoid; Q06098; -.
DR OMA; TSAFHIN; -.
DR BioCyc; YEAST:G3O-34246-MON; -.
DR PRO; PR:Q06098; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q06098; protein.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; ISS:SGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0106279; P:negative regulation of UDP-N-acetylglucosamine biosynthetic process; IMP:SGD.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IMP:SGD.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; 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; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..443
FT /note="Serine/threonine-protein kinase ISR1"
FT /id="PRO_0000086038"
FT DOMAIN 135..415
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 280
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 141..149
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 169
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 443 AA; 49736 MW; FBB31592EEF9349F CRC64;
MNSTPPTSPV TRVSDGSFPS ISNNSKGFAY RQPQKHKSNF AYSHLVSPVE EPTAKFSEAF
QTDYSSKAPV ATSEAHLKND LDVLFTTPRF YSPENLALMF RLSNTVSSLE FLDEFLMGIL
LAPEMDFLSN PSYSLPSNKL VGQGSYSYVY PISSSASSRC NNDSGVVLKF AKSQHKSKVI
LQEALTLAYL QYMSPSTNES HIIPFYGLTY ITKSHFRRLR SNECVPGLIL PKCEMSLYHF
NTAVSHKLSL ITKRKIWWRL MKQMIDALKS LKTNGIIHGD IKTANILITE MHVLNGGHCK
DFDFYLADFT SAFHINQTPT DLNTTVEYCA PELIDSSSDH VPTFESDLYA VGLCLLSFIS
QHEPYNELQA LVSHGSSPGI GSSSIQQSQW LINALLKKDP INLNMLRNDL FQDWKSELAL
LSRILVDRLP LENLITILDS NYI
