ESL1_YEAST
ID ESL1_YEAST Reviewed; 1118 AA.
AC P40456; D6VVD6;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=EST/SMG-like protein 1 {ECO:0000303|PubMed:23893744};
GN Name=ESL1 {ECO:0000303|PubMed:23893744};
GN OrderedLocusNames=YIL151C {ECO:0000312|SGD:S000001413};
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=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(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 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170 AND SER-190, 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 [5]
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).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [7]
RP FUNCTION.
RX PubMed=23893744; DOI=10.1534/g3.113.006924;
RA Lai X., Beilharz T., Au W.C., Hammet A., Preiss T., Basrai M.A.,
RA Heierhorst J.;
RT "Yeast hEST1A/B (SMG5/6)-like proteins contribute to environment-sensing
RT adaptive gene expression responses.";
RL G3 (Bethesda) 3:1649-1659(2013).
CC -!- FUNCTION: May be involved in the regulation of gene expression
CC responses of environment-sensing pathways.
CC {ECO:0000269|PubMed:23893744}.
CC -!- MISCELLANEOUS: Present with 504 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z38059; CAA86127.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08402.1; -; Genomic_DNA.
DR PIR; S48383; S48383.
DR RefSeq; NP_012115.1; NM_001179499.1.
DR AlphaFoldDB; P40456; -.
DR SMR; P40456; -.
DR BioGRID; 34841; 78.
DR DIP; DIP-1904N; -.
DR IntAct; P40456; 6.
DR MINT; P40456; -.
DR STRING; 4932.YIL151C; -.
DR iPTMnet; P40456; -.
DR MaxQB; P40456; -.
DR PaxDb; P40456; -.
DR PRIDE; P40456; -.
DR EnsemblFungi; YIL151C_mRNA; YIL151C; YIL151C.
DR GeneID; 854655; -.
DR KEGG; sce:YIL151C; -.
DR SGD; S000001413; ESL1.
DR VEuPathDB; FungiDB:YIL151C; -.
DR eggNOG; ENOG502QQKF; Eukaryota.
DR GeneTree; ENSGT00940000176784; -.
DR HOGENOM; CLU_006407_0_0_1; -.
DR InParanoid; P40456; -.
DR OMA; YHIATVQ; -.
DR BioCyc; YEAST:G3O-31400-MON; -.
DR Reactome; R-SCE-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR PRO; PR:P40456; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40456; protein.
DR GO; GO:0005697; C:telomerase holoenzyme complex; IBA:GO_Central.
DR GO; GO:0070034; F:telomerase RNA binding; IBA:GO_Central.
DR GO; GO:0042162; F:telomeric DNA binding; IBA:GO_Central.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IBA:GO_Central.
DR InterPro; IPR045153; Est1/Ebs1-like.
DR InterPro; IPR002716; PIN_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR15696; PTHR15696; 1.
DR Pfam; PF13638; PIN_4; 1.
DR SMART; SM00670; PINc; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
PE 1: Evidence at protein level;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1118
FT /note="EST/SMG-like protein 1"
FT /id="PRO_0000202957"
FT DOMAIN 947..1087
FT /note="PINc"
FT /evidence="ECO:0000255"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 77..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 1118 AA; 128735 MW; 4F80F3A5E95C6CC3 CRC64;
MVDLMVPAND DPSNETDYSR SNNNHTHIVS DMRPTSAAFL HQKRHSSSSH NDTPESSFAK
RRVPGIVDPV GKGFIDGITN SQISAQNTPS KTDDASRRPS ISRKVMESTP QVKTSSIPTM
DVPKSPYYVN RTMLARNMKV VSRDTYEDNA NPQMRADEPL VASNGIYSNS QPQSQVTLSD
IRRAPVVAAS PPPMIRQLPS AQPNQTFIKK LQEIYKIIVV QETELQQRCL YLTTSQTTEL
KSLWAIYRLN TELIKNYINF IITALLTTQP INDLIMGQEI LDIYRIEKRL WVYGIITFLD
VLKNFSNFMD PEVCCQFIIY AFISVSNMLE DIPLKYSILW RQRLGDLSRM AISLYPSGFI
DWRLSAEYWY TESMKYIYGC GKLYYHIATV QQNSLEAFVN LGKSVFCQDP FTPSQQTLQL
LIENIYQSAF IDRSSGSANN NEIAHRNSQL IDYLKHTEVM LLPSFLENMD LQHVVLMYFK
DKFGKDFNGN DVFDTKDMFC QNPESLRYYF RHAPAFAESQ LLQLIGFGNP KNPFALLFQL
PKYLKLKKDK REKKRSEATE TSSYTDPFDV QISSESYFQN IDALNSSFND IPTNLNIWLD
SLNHINMTSI QCSIHVLTKF LHAPLVVALP HFLTWLHFIV AILKKLEMVN SKQVVAFWIH
FLRRTMPWNS IVTLGNVLVC YMLDNLHPFL KKELEKFYSL ELDDLIEYYN ENENLPEIWK
CWGTLWFDAI KKCDVMEIPG VQDHLFFDSP LDGIVFDEKD EVGEKFWMRS VRAVLLLKGI
AKKFPDLGLK VSFQASVFCR RNDIPPDYFL KNLTFKLDAY DEDNYNDNNE LDDLYDTIEI
NEEIEAVNMD PQATPNLSVV SGESIFEYTG YTRLAPDYHC FDKNGGFNSA FIYSQWSNVG
NGVTLDVSGE SIYDVANNNL SLHWEKIFFD KIAAASKGSD ENYNCTLYFV IDATSWLRHF
AHIFKLAKNN TLKFAICLTT FQELRYLRGS KDDTVVEAAT RSVITIRQLY DEKKIIPMRF
TGNIATHVEE NLEFEEQITW KTHVDEFVID AIAKLNQRFQ AERLTDENKN KGKEFAVLVT
DDDNMNQKAK DRMIKTCNTK YLFSLGSKLG INSGLCTN
