ELM1_YEAST
ID ELM1_YEAST Reviewed; 640 AA.
AC P32801; D6VXN9;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Serine/threonine-protein kinase ELM1;
DE EC=2.7.11.1;
GN Name=ELM1; OrderedLocusNames=YKL048C; ORFNames=YKL261;
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, AND FUNCTION.
RX PubMed=8395007; DOI=10.1128/mcb.13.9.5567-5581.1993;
RA Blacketer M.J., Koehler C.M., Coats S.G., Myers A.M., Madaule P.;
RT "Regulation of dimorphism in Saccharomyces cerevisiae: involvement of the
RT novel protein kinase homolog Elm1p and protein phosphatase 2A.";
RL Mol. Cell. Biol. 13:5567-5581(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8154189; DOI=10.1002/yea.320091212;
RA Purnelle B., Tettelin H., van Dyck L., Skala J., Goffeau A.;
RT "The sequence of a 17.5 kb DNA fragment on the left arm of yeast chromosome
RT XI identifies the protein kinase gene ELM1, the DNA primase gene PRI2, a
RT new gene encoding a putative histone and seven new open reading frames.";
RL Yeast 9:1379-1384(1993).
RN [3]
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 [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, AND MUTAGENESIS OF THR-200.
RX PubMed=12917352; DOI=10.1128/mcb.23.17.6327-6337.2003;
RA Sreenivasan A., Bishop A.C., Shokat K.M., Kellogg D.R.;
RT "Specific inhibition of Elm1 kinase activity reveals functions required for
RT early G1 events.";
RL Mol. Cell. Biol. 23:6327-6337(2003).
RN [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152 AND SER-519, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-516 AND SER-519, AND
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: Important role in G1 events required for bud emergence and
CC septin organization. Coordinates cell growth and cell division at G2/M,
CC essential for efficient cytokinesis and for regulation of SWE1.
CC {ECO:0000269|PubMed:12917352, ECO:0000269|PubMed:8395007}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- MISCELLANEOUS: Present with 149 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA02892.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M81258; AAA02892.1; ALT_FRAME; Unassigned_DNA.
DR EMBL; X71621; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z28048; CAA81883.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09109.1; -; Genomic_DNA.
DR PIR; S37869; S37869.
DR RefSeq; NP_012876.1; NM_001179614.1.
DR AlphaFoldDB; P32801; -.
DR SMR; P32801; -.
DR BioGRID; 34085; 801.
DR DIP; DIP-2731N; -.
DR IntAct; P32801; 8.
DR MINT; P32801; -.
DR STRING; 4932.YKL048C; -.
DR iPTMnet; P32801; -.
DR MaxQB; P32801; -.
DR PaxDb; P32801; -.
DR PRIDE; P32801; -.
DR EnsemblFungi; YKL048C_mRNA; YKL048C; YKL048C.
DR GeneID; 853818; -.
DR KEGG; sce:YKL048C; -.
DR SGD; S000001531; ELM1.
DR VEuPathDB; FungiDB:YKL048C; -.
DR eggNOG; KOG0585; Eukaryota.
DR HOGENOM; CLU_019325_0_0_1; -.
DR InParanoid; P32801; -.
DR BioCyc; YEAST:G3O-31849-MON; -.
DR BRENDA; 2.7.10.2; 984.
DR PRO; PR:P32801; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P32801; protein.
DR GO; GO:0005935; C:cellular bud neck; HDA:SGD.
DR GO; GO:0000144; C:cellular bud neck septin ring; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion 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:0007117; P:budding cell bud growth; IMP:SGD.
DR GO; GO:0000902; P:cell morphogenesis; IMP:SGD.
DR GO; GO:0042149; P:cellular response to glucose starvation; IMP:SGD.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:SGD.
DR GO; GO:1902935; P:protein localization to septin ring; IMP:SGD.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0007124; P:pseudohyphal growth; IMP:SGD.
DR GO; GO:0000921; P:septin ring assembly; IMP: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; Cell cycle; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..640
FT /note="Serine/threonine-protein kinase ELM1"
FT /id="PRO_0000085951"
FT DOMAIN 88..420
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 27..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 562..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..587
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 259
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 94..102
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 117
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 516
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 519
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MUTAGEN 200
FT /note="T->G: Allows selective inhibition in vivo."
FT /evidence="ECO:0000269|PubMed:12917352"
FT CONFLICT 390
FT /note="E -> Y (in Ref. 1; AAA02892)"
FT /evidence="ECO:0000305"
FT CONFLICT 484..485
FT /note="TV -> SD (in Ref. 1; AAA02892)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 640 AA; 72150 MW; 33C3A7E188DF12C4 CRC64;
MSPRQLIPTL IPEWAPLSQQ SCIREDELDS PPITPTSQTS SFGSSFSQQK PTYSTIIGEN
IHTILDEIRP YVKKITVSDQ DKKTINQYTL GVSAGSGQFG YVRKAYSSTL GKVVAVKIIP
KKPWNAQQYS VNQVMRQIQL WKSKGKITTN MSGNEAMRLM NIEKCRWEIF AASRLRNNVH
IVRLIECLDS PFSESIWIVT NWCSLGELQW KRDDDEDILP QWKKIVISNC SVSTFAKKIL
EDMTKGLEYL HSQGCIHRDI KPSNILLDEE EKVAKLSDFG SCIFTPQSLP FSDANFEDCF
QRELNKIVGT PAFIAPELCH LGNSKRDFVT DGFKLDIWSL GVTLYCLLYN ELPFFGENEF
ETYHKIIEVS LSSKINGNTL NDLVIKRLLE KDVTLRISIQ DLVKVLSRDQ PIDSRNHSQI
SSSSVNPVRN EGPVRRFFGR LLTKKGKKKT SGKGKDKVLV SATSKVTPSI HIDEEPDKEC
FSTTVLRSSP DSSDYCSSLG EEAIQVTDFL DTFCRSNESL PNLTVNNDKQ NSDMKTDRSE
SSSHSSLKIP TPIKAMIRLK SSPKENGNRT HINCSQDKPS SPLMDRTVGK RTVNNSGARK
LAHSSNILNF KAYINSEDSD IRETVEDVKT YLNFADNGQI
