ID   HSP26_YEAST             Reviewed;         214 AA.
AC   P15992; D6VQ71; Q6B1V5;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 182.
DE   RecName: Full=Heat shock protein 26;
DE   AltName: Full=26 kDa heat shock protein;
GN   Name=HSP26; OrderedLocusNames=YBR072W; ORFNames=YBR0714;
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=2689876; DOI=10.1128/mcb.9.11.5265-5271.1989;
RA   Susek R.E., Lindquist S.L.;
RT   "hsp26 of Saccharomyces cerevisiae is related to the superfamily of small
RT   heat shock proteins but is without a demonstrable function.";
RL   Mol. Cell. Biol. 9:5265-5271(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CLEAVAGE OF INITIATOR METHIONINE.
RX   PubMed=2673926; DOI=10.1016/0378-1119(89)90234-5;
RA   Bossier P., Fitch I.T., Boucherie H., Tuite M.F.;
RT   "Structure and expression of a yeast gene encoding the small heat-shock
RT   protein Hsp26.";
RL   Gene 78:323-330(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7985423; DOI=10.1002/yea.320100711;
RA   van der Aart Q.J.M., Barthe C., Doignon F., Aigle M., Crouzet M.,
RA   Steensma H.Y.;
RT   "Sequence analysis of a 31 kb DNA fragment from the right arm of
RT   Saccharomyces cerevisiae chromosome II.";
RL   Yeast 10:959-964(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA   Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA   Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA   Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA   Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA   Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA   Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA   Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA   Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA   Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA   Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA   Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA   Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA   Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA   Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA   Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA   Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA   Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA   Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA   Mewes H.-W., Kleine K.;
RT   "Complete DNA sequence of yeast chromosome II.";
RL   EMBO J. 13:5795-5809(1994).
RN   [5]
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   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [7]
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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-42; SER-90 AND THR-163, 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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-208 AND SER-211, 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).
RN   [10]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [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).
CC   -!- FUNCTION: Not known. One of the major polypeptides produced on heat
CC       shock.
CC   -!- SUBUNIT: Present in large complexes.
CC   -!- INTERACTION:
CC       P15992; P15992: HSP26; NbExp=2; IntAct=EBI-8555, EBI-8555;
CC   -!- DEVELOPMENTAL STAGE: Expressed during the entry into stationary phase
CC       resulting from glucose limitation.
CC   -!- INDUCTION: By heat shock, and under other conditions of stress, such as
CC       increased salt concentration and starvation.
CC   -!- MISCELLANEOUS: Present with 19300 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00285}.
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DR   EMBL; M23871; AAA66914.1; -; Genomic_DNA.
DR   EMBL; M26942; AAA79010.1; -; Genomic_DNA.
DR   EMBL; X76294; CAA53929.1; -; Genomic_DNA.
DR   EMBL; Z35941; CAA85016.1; -; Genomic_DNA.
DR   EMBL; AY692975; AAT92994.1; -; Genomic_DNA.
DR   EMBL; BK006936; DAA07191.1; -; Genomic_DNA.
DR   PIR; S45465; S45465.
DR   RefSeq; NP_009628.1; NM_001178420.1.
DR   PDB; 7OA6; EM; 7.80 A; A/B/I/J/X=1-214.
DR   PDBsum; 7OA6; -.
DR   AlphaFoldDB; P15992; -.
DR   EMDB; EMD-12766; -.
DR   SMR; P15992; -.
DR   BioGRID; 32775; 136.
DR   DIP; DIP-3988N; -.
DR   IntAct; P15992; 143.
DR   MINT; P15992; -.
DR   STRING; 4932.YBR072W; -.
DR   CarbonylDB; P15992; -.
DR   iPTMnet; P15992; -.
DR   MaxQB; P15992; -.
DR   PaxDb; 4932-YBR072W; -.
DR   PeptideAtlas; P15992; -.
DR   TopDownProteomics; P15992; -.
DR   EnsemblFungi; YBR072W_mRNA; YBR072W; YBR072W.
DR   GeneID; 852364; -.
DR   KEGG; sce:YBR072W; -.
DR   AGR; SGD:S000000276; -.
DR   SGD; S000000276; HSP26.
DR   VEuPathDB; FungiDB:YBR072W; -.
DR   eggNOG; KOG0710; Eukaryota.
DR   HOGENOM; CLU_046737_12_0_1; -.
DR   InParanoid; P15992; -.
DR   OMA; IDIEYHQ; -.
DR   OrthoDB; 1981241at2759; -.
DR   BioCyc; YEAST:G3O-29041-MONOMER; -.
DR   BioGRID-ORCS; 852364; 4 hits in 10 CRISPR screens.
DR   PRO; PR:P15992; -.
DR   Proteomes; UP000002311; Chromosome II.
DR   RNAct; P15992; Protein.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0003729; F:mRNA binding; IDA:SGD.
DR   GO; GO:0051082; F:unfolded protein binding; IDA:SGD.
DR   GO; GO:0034605; P:cellular response to heat; IDA:SGD.
DR   GO; GO:0006457; P:protein folding; IDA:SGD.
DR   CDD; cd06464; ACD_sHsps-like; 1.
DR   Gene3D; 2.60.40.790; -; 1.
DR   InterPro; IPR002068; A-crystallin/Hsp20_dom.
DR   InterPro; IPR008978; HSP20-like_chaperone.
DR   InterPro; IPR031107; Small_HSP.
DR   PANTHER; PTHR11527:SF175; HEAT SHOCK PROTEIN 42; 1.
DR   PANTHER; PTHR11527; HEAT-SHOCK PROTEIN 20 FAMILY MEMBER; 1.
DR   Pfam; PF00011; HSP20; 1.
DR   SUPFAM; SSF49764; HSP20-like chaperones; 1.
DR   PROSITE; PS01031; SHSP; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Phosphoprotein; Reference proteome;
KW   Stress response.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:2673926,
FT                   ECO:0007744|PubMed:22814378"
FT   CHAIN           2..214
FT                   /note="Heat shock protein 26"
FT                   /id="PRO_0000126004"
FT   DOMAIN          86..207
FT                   /note="sHSP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
FT   REGION          192..214
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   MOD_RES         42
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         90
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         163
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         208
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         211
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   CONFLICT        32
FT                   /note="G -> A (in Ref. 2; AAA79010)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        207
FT                   /note="S -> C (in Ref. 2; AAA79010)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        212
FT                   /note="W -> G (in Ref. 6; AAT92994)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   214 AA;  23880 MW;  0CB8B6BD22C5308F CRC64;
     MSFNSPFFDF FDNINNEVDA FNRLLGEGGL RGYAPRRQLA NTPAKDSTGK EVARPNNYAG
     ALYDPRDETL DDWFDNDLSL FPSGFGFPRS VAVPVDILDH DNNYELKVVV PGVKSKKDID
     IEYHQNKNQI LVSGEIPSTL NEESKDKVKV KESSSGKFKR VITLPDYPGV DADNIKADYA
     NGVLTLTVPK LKPQKDGKNH VKKIEVSSQE SWGN
//