HSL1_YEAST
ID HSL1_YEAST Reviewed; 1518 AA.
AC P34244; A2NP40; D6VXI6;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 2.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Probable serine/threonine-protein kinase HSL1;
DE EC=2.7.11.1;
GN Name=HSL1; OrderedLocusNames=YKL101W; ORFNames=YKL453;
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=8647431; DOI=10.1101/gad.10.11.1327;
RA Ma X.-J., Lu Q., Grunstein M.;
RT "A search for proteins that interact genetically with histone H3 and H4
RT amino termini uncovers novel regulators of the Swe1 kinase in Saccharomyces
RT cerevisiae.";
RL Genes Dev. 10:1327-1340(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8256524; DOI=10.1002/yea.320091016;
RA Pallier C., Valens M., Puzos V., Fukuhara H., Cheret G., Sor F.,
RA Bolotin-Fukuhara M.;
RT "DNA sequence analysis of a 17 kb fragment of yeast chromosome XI
RT physically localizes the MRB1 gene and reveals eight new open reading
RT frames, including a homologue of the KIN1/KIN2 and SNF1 protein kinases.";
RL Yeast 9:1149-1155(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, AND SEQUENCE REVISION TO 1482.
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 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-629; SER-1220; SER-1284 AND
RP SER-1287, AND IDENTIFICATION BY 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-511; SER-1220; SER-1284 AND
RP SER-1325, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-685; SER-837; SER-866 AND
RP SER-1250, AND 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 -!- 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 -!- INTERACTION:
CC P34244; P32485: HOG1; NbExp=2; IntAct=EBI-9771, EBI-8437;
CC -!- SUBCELLULAR LOCATION: Bud neck {ECO:0000269|PubMed:14562095}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. NIM1 subfamily. {ECO:0000305}.
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DR EMBL; U65921; AAB07455.1; -; Genomic_DNA.
DR EMBL; X71133; CAA50456.1; -; Genomic_DNA.
DR EMBL; Z28101; CAA81941.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09056.2; -; Genomic_DNA.
DR PIR; S37928; S37928.
DR RefSeq; NP_012821.2; NM_001179667.2.
DR PDB; 5G04; EM; 4.00 A; S=667-872.
DR PDB; 5KHR; EM; 6.10 A; S=774-837.
DR PDB; 5L9T; EM; 6.40 A; S=818-842.
DR PDB; 5L9U; EM; 6.40 A; S=768-842.
DR PDBsum; 5G04; -.
DR PDBsum; 5KHR; -.
DR PDBsum; 5L9T; -.
DR PDBsum; 5L9U; -.
DR AlphaFoldDB; P34244; -.
DR SMR; P34244; -.
DR BioGRID; 34032; 492.
DR DIP; DIP-3022N; -.
DR ELM; P34244; -.
DR IntAct; P34244; 20.
DR MINT; P34244; -.
DR STRING; 4932.YKL101W; -.
DR iPTMnet; P34244; -.
DR MaxQB; P34244; -.
DR PaxDb; P34244; -.
DR PRIDE; P34244; -.
DR EnsemblFungi; YKL101W_mRNA; YKL101W; YKL101W.
DR GeneID; 853760; -.
DR KEGG; sce:YKL101W; -.
DR SGD; S000001584; HSL1.
DR VEuPathDB; FungiDB:YKL101W; -.
DR eggNOG; KOG0588; Eukaryota.
DR HOGENOM; CLU_003225_0_0_1; -.
DR InParanoid; P34244; -.
DR OMA; HLPFNDD; -.
DR BioCyc; YEAST:G3O-31891-MON; -.
DR PRO; PR:P34244; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P34244; protein.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0000144; C:cellular bud neck septin ring; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IDA:SGD.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IMP:SGD.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0044879; P:mitotic morphogenesis checkpoint signaling; IMP:SGD.
DR GO; GO:0030163; P:protein catabolic process; 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:0051726; P:regulation of cell cycle; 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 3D-structure; ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1518
FT /note="Probable serine/threonine-protein kinase HSL1"
FT /id="PRO_0000086148"
FT DOMAIN 81..369
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 55..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 741..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 856..898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1005..1030
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1150..1170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1220..1243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1259..1291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..616
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..757
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..779
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..870
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 876..898
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1011..1030
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1268..1283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 239
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 87..95
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 110
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 511
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 629
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 685
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 837
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 866
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1220
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:18407956"
FT MOD_RES 1250
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1284
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:18407956"
FT MOD_RES 1287
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 1325
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CONFLICT 1482
FT /note="T -> S (in Ref. 1; AAB07455, 2; CAA50456 and 3;
FT CAA81941)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1518 AA; 169607 MW; 803F84F7574304CD CRC64;
MTGHVSKTSH VPKGRPSSLA KKAAKRAMAK VNSNPKRASG HLERVVQSVN DATKRLSQPD
STVSVATKSS KRKSRDTVGP WKLGKTLGKG SSGRVRLAKN METGQLAAIK IVPKKKAFVH
CSNNGTVPNS YSSSMVTSNV SSPSIASREH SNHSQTNPYG IEREIVIMKL ISHTNVMALF
EVWENKSELY LVLEYVDGGE LFDYLVSKGK LPEREAIHYF KQIVEGVSYC HSFNICHRDL
KPENLLLDKK NRRIKIADFG MAALELPNKL LKTSCGSPHY ASPEIVMGRP YHGGPSDVWS
CGIVLFALLT GHLPFNDDNI KKLLLKVQSG KYQMPSNLSS EARDLISKIL VIDPEKRITT
QEILKHPLIK KYDDLPVNKV LRKMRKDNMA RGKSNSDLHL LNNVSPSIVT LHSKGEIDES
ILRSLQILWH GVSRELITAK LLQKPMSEEK LFYSLLLQYK QRHSISLSSS SENKKSATES
SVNEPRIEYA SKTANNTGLR SENNDVKTLH SLEIHSEDTS TVNQNNAITG VNTEINAPVL
AQKSQFSINT LSQPESDKAE AEAVTLPPAI PIFNASSSRI FRNSYTSISS RSRRSLRLSN
SRLSLSASTS RETVHDNEMP LPQLPKSPSR YSLSRRAIHA SPSTKSIHKS LSRKNIAATV
AARRTLQNSA SKRSLYSLQS ISKRSLNLND LLVFDDPLPS KKPASENVNK SEPHSLESDS
DFEILCDQIL FGNALDRILE EEEDNEKERD TQRQRQNDTK SSADTFTISG VSTNKENEGP
EYPTKIEKNQ FNMSYKPSEN MSGLSSFPIF EKENTLSSSY LEEQKPKRAA LSDITNSFNK
MNKQEGMRIE KKIQREQLQK KNDRPSPLKP IQHQELRVNS LPNDQGKPSL SLDPRRNISQ
PVNSKVESLL QGLKFKKEPA SHWTHERGSL FMSEHVEDEK PVKASDVSIE SSYVPLTTVA
TSSRDPSVLA ESSTIQKPML SLPSSFLNTS MTFKNLSQIL ADDGDDKHLS VPQNQSRSVA
MSHPLRKQSA KISLTPRSNL NANLSVKRNQ GSPGSYLSND LDGISDMTFA MEIPTNTFTA
QAIQLMNNDT DNNKINTSPK ASSFTKEKVI KSAAYISKEK EPDNSDTNYI PDYTIPNTYD
EKAINIFEDA PSDEGSLNTS SSESDSRASV HRKAVSIDTM ATTNVLTPAT NVRVSLYWNN
NSSGIPRETT EEILSKLRLS PENPSNTHMQ KRFSSTRGSR DSNALGISQS LQSMFKDLEE
DQDGHTSQAD ILESSMSYSK RRPSEESVNP KQRVTMLFDE EEEESKKVGG GKIKEEHTKL
DNKISEESSQ LVLPVVEKKE NANNTENNYS KIPKPSTIKV TKDTAMESNT QTHTKKPILK
SVQNVEVEEA PSSDKKNWFV KLFQNFSSHN NATKASKNHV TNISFDDAHM LTLNEFNKNS
IDYQLKNLDH KFGRKVVEYD CKFVKGNFKF KIKITSTPNA STVITVKKRS KHSNTSSNKA
FEKFNDDVER VIRNAGRS
