STI1_YEAST
ID STI1_YEAST Reviewed; 589 AA.
AC P15705; D6W293;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 214.
DE RecName: Full=Heat shock protein STI1;
GN Name=STI1; OrderedLocusNames=YOR027W; ORFNames=OR26.17;
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=2674681; DOI=10.1128/mcb.9.9.3638-3646.1989;
RA Nicolet C.M., Craig E.A.;
RT "Isolation and characterization of STI1, a stress-inducible gene from
RT Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 9:3638-3646(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2297790; DOI=10.1016/0092-8674(90)90746-2;
RA Hirano T., Kinoshita N., Morikawa K., Yanagida M.;
RT "Snap helix with knob and hole: essential repeats in S. pombe nuclear
RT protein nuc2+.";
RL Cell 60:319-328(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
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 PROTEIN SEQUENCE OF 76-93.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7895733; DOI=10.1002/elps.11501501210;
RA Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B.,
RA Volpe T., Warner J.R., McLaughlin C.S.;
RT "Protein identifications for a Saccharomyces cerevisiae protein database.";
RL Electrophoresis 15:1466-1486(1994).
RN [6]
RP DOMAINS TPR REPEATS.
RX PubMed=1694969; DOI=10.1038/346114a0;
RA Boguski M.S., Sikorski R.S., Hieter P.A., Goebl M.;
RT "Expanding family.";
RL Nature 346:114-114(1990).
RN [7]
RP CHARACTERIZATION.
RX PubMed=8423808; DOI=10.1128/mcb.13.2.869-876.1993;
RA Smith D.F., Sullivan W.P., Marion T.N., Zaitsu K., Madden B.,
RA McCormick D.J., Toft D.O.;
RT "Identification of a 60-kilodalton stress-related protein, p60, which
RT interacts with hsp90 and hsp70.";
RL Mol. Cell. Biol. 13:869-876(1993).
RN [8]
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 [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, AND IDENTIFICATION BY
RP 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 [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS].
RX PubMed=19756047; DOI=10.1038/msb.2009.64;
RA Kung L.A., Tao S.-C., Qian J., Smith M.G., Snyder M., Zhu H.;
RT "Global analysis of the glycoproteome in Saccharomyces cerevisiae reveals
RT new roles for protein glycosylation in eukaryotes.";
RL Mol. Syst. Biol. 5:308-308(2009).
RN [12]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-99; LYS-168 AND LYS-384, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- FUNCTION: May play a role in mediating the heat shock response of some
CC HSP70 genes. It is required for optimal growth of yeast cells at both
CC low and high temperature.
CC -!- SUBUNIT: Part of a larger complex that includes HSP70, HSP90, and
CC immunophilins.
CC -!- INTERACTION:
CC P15705; P15108: HSC82; NbExp=3; IntAct=EBI-18418, EBI-8666;
CC P15705; P02829: HSP82; NbExp=18; IntAct=EBI-18418, EBI-8659;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- INDUCTION: By heat shock and canavanine.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:19756047}.
CC -!- MISCELLANEOUS: Present with 67600 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
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DR EMBL; M28486; AAA35121.1; -; Genomic_DNA.
DR EMBL; X87331; CAA60743.1; -; Genomic_DNA.
DR EMBL; Z74935; CAA99217.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10809.1; -; Genomic_DNA.
DR PIR; A32567; A32567.
DR RefSeq; NP_014670.1; NM_001183446.1.
DR PDB; 2LLV; NMR; -; A=127-197.
DR PDB; 2LLW; NMR; -; A=519-589.
DR PDB; 3UPV; X-ray; 1.60 A; A=395-518.
DR PDB; 3UQ3; X-ray; 2.60 A; A=262-515.
DR PDBsum; 2LLV; -.
DR PDBsum; 2LLW; -.
DR PDBsum; 3UPV; -.
DR PDBsum; 3UQ3; -.
DR AlphaFoldDB; P15705; -.
DR BMRB; P15705; -.
DR SMR; P15705; -.
DR BioGRID; 34430; 323.
DR DIP; DIP-2329N; -.
DR IntAct; P15705; 31.
DR MINT; P15705; -.
DR STRING; 4932.YOR027W; -.
DR iPTMnet; P15705; -.
DR SWISS-2DPAGE; P15705; -.
DR MaxQB; P15705; -.
DR PaxDb; P15705; -.
DR PRIDE; P15705; -.
DR EnsemblFungi; YOR027W_mRNA; YOR027W; YOR027W.
DR GeneID; 854192; -.
DR KEGG; sce:YOR027W; -.
DR SGD; S000005553; STI1.
DR VEuPathDB; FungiDB:YOR027W; -.
DR eggNOG; KOG0548; Eukaryota.
DR GeneTree; ENSGT00940000170181; -.
DR HOGENOM; CLU_000134_46_5_1; -.
DR InParanoid; P15705; -.
DR OMA; HYSKAWE; -.
DR BioCyc; YEAST:G3O-33574-MON; -.
DR Reactome; R-SCE-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-SCE-9696273; RND1 GTPase cycle.
DR PRO; PR:P15705; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P15705; protein.
DR GO; GO:0005737; C:cytoplasm; IPI:SGD.
DR GO; GO:0042030; F:ATPase inhibitor activity; IDA:SGD.
DR GO; GO:0030544; F:Hsp70 protein binding; IDA:SGD.
DR GO; GO:0051879; F:Hsp90 protein binding; IDA:SGD.
DR GO; GO:0003729; F:mRNA binding; IDA:SGD.
DR GO; GO:0006457; P:protein folding; IMP:SGD.
DR GO; GO:0008104; P:protein localization; IMP:SGD.
DR GO; GO:0006626; P:protein targeting to mitochondrion; IMP:SGD.
DR Gene3D; 1.25.40.10; -; 3.
DR IDEAL; IID50201; -.
DR InterPro; IPR041243; STI1.
DR InterPro; IPR045248; Sti1-like.
DR InterPro; IPR006636; STI1_HS-bd.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR22904; PTHR22904; 1.
DR Pfam; PF17830; STI1; 2.
DR Pfam; PF00515; TPR_1; 2.
DR Pfam; PF13181; TPR_8; 2.
DR SMART; SM00727; STI1; 2.
DR SMART; SM00028; TPR; 9.
DR SUPFAM; SSF48452; SSF48452; 3.
DR PROSITE; PS50005; TPR; 7.
DR PROSITE; PS50293; TPR_REGION; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Glycoprotein;
KW Isopeptide bond; Phosphoprotein; Reference proteome; Repeat;
KW Stress response; TPR repeat; Ubl conjugation.
FT CHAIN 1..589
FT /note="Heat shock protein STI1"
FT /id="PRO_0000106341"
FT REPEAT 5..38
FT /note="TPR 1"
FT REPEAT 40..73
FT /note="TPR 2"
FT REPEAT 74..107
FT /note="TPR 3"
FT DOMAIN 138..177
FT /note="STI1 1"
FT REPEAT 262..295
FT /note="TPR 4"
FT REPEAT 297..328
FT /note="TPR 5"
FT REPEAT 336..369
FT /note="TPR 6"
FT REPEAT 396..429
FT /note="TPR 7"
FT REPEAT 430..463
FT /note="TPR 8"
FT REPEAT 465..492
FT /note="TPR 9"
FT DOMAIN 537..576
FT /note="STI1 2"
FT REGION 199..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..228
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CROSSLNK 99
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 168
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 384
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT HELIX 133..137
FT /evidence="ECO:0007829|PDB:2LLV"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:2LLV"
FT HELIX 142..147
FT /evidence="ECO:0007829|PDB:2LLV"
FT HELIX 152..156
FT /evidence="ECO:0007829|PDB:2LLV"
FT HELIX 160..169
FT /evidence="ECO:0007829|PDB:2LLV"
FT HELIX 174..177
FT /evidence="ECO:0007829|PDB:2LLV"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:2LLV"
FT HELIX 182..192
FT /evidence="ECO:0007829|PDB:2LLV"
FT TURN 193..196
FT /evidence="ECO:0007829|PDB:2LLV"
FT HELIX 262..274
FT /evidence="ECO:0007829|PDB:3UQ3"
FT HELIX 278..291
FT /evidence="ECO:0007829|PDB:3UQ3"
FT HELIX 296..307
FT /evidence="ECO:0007829|PDB:3UQ3"
FT HELIX 311..327
FT /evidence="ECO:0007829|PDB:3UQ3"
FT HELIX 332..348
FT /evidence="ECO:0007829|PDB:3UQ3"
FT HELIX 352..365
FT /evidence="ECO:0007829|PDB:3UQ3"
FT HELIX 369..390
FT /evidence="ECO:0007829|PDB:3UQ3"
FT HELIX 395..408
FT /evidence="ECO:0007829|PDB:3UPV"
FT HELIX 412..425
FT /evidence="ECO:0007829|PDB:3UPV"
FT HELIX 430..442
FT /evidence="ECO:0007829|PDB:3UPV"
FT HELIX 446..459
FT /evidence="ECO:0007829|PDB:3UPV"
FT HELIX 464..476
FT /evidence="ECO:0007829|PDB:3UPV"
FT HELIX 480..498
FT /evidence="ECO:0007829|PDB:3UPV"
FT TURN 499..502
FT /evidence="ECO:0007829|PDB:3UPV"
FT HELIX 503..516
FT /evidence="ECO:0007829|PDB:3UPV"
FT HELIX 527..536
FT /evidence="ECO:0007829|PDB:2LLW"
FT HELIX 538..544
FT /evidence="ECO:0007829|PDB:2LLW"
FT HELIX 548..558
FT /evidence="ECO:0007829|PDB:2LLW"
FT HELIX 560..568
FT /evidence="ECO:0007829|PDB:2LLW"
FT HELIX 570..581
FT /evidence="ECO:0007829|PDB:2LLW"
SQ SEQUENCE 589 AA; 66265 MW; CF8A85C2BBD3C44C CRC64;
MSLTADEYKQ QGNAAFTAKD YDKAIELFTK AIEVSETPNH VLYSNRSACY TSLKKFSDAL
NDANECVKIN PSWSKGYNRL GAAHLGLGDL DEAESNYKKA LELDASNKAA KEGLDQVHRT
QQARQAQPDL GLTQLFADPN LIENLKKNPK TSEMMKDPQL VAKLIGYKQN PQAIGQDLFT
DPRLMTIMAT LMGVDLNMDD INQSNSMPKE PETSKSTEQK KDAEPQSDST TSKENSSKAP
QKEESKESEP MEVDEDDSKI EADKEKAEGN KFYKARQFDE AIEHYNKAWE LHKDITYLNN
RAAAEYEKGE YETAISTLND AVEQGREMRA DYKVISKSFA RIGNAYHKLG DLKKTIEYYQ
KSLTEHRTAD ILTKLRNAEK ELKKAEAEAY VNPEKAEEAR LEGKEYFTKS DWPNAVKAYT
EMIKRAPEDA RGYSNRAAAL AKLMSFPEAI ADCNKAIEKD PNFVRAYIRK ATAQIAVKEY
ASALETLDAA RTKDAEVNNG SSAREIDQLY YKASQQRFQP GTSNETPEET YQRAMKDPEV
AAIMQDPVMQ SILQQAQQNP AALQEHMKNP EVFKKIQTLI AAGIIRTGR
